ID R0A5G7_9FIRM Unreviewed; 683 AA. AC R0A5G7; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 02-JUN-2021, entry version 55. DE RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01228}; DE EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_01228}; DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228}; DE Short=MetRS {ECO:0000256|HAMAP-Rule:MF_01228}; GN Name=metG {ECO:0000256|HAMAP-Rule:MF_01228}; GN ORFNames=HMPREF1085_04500 {ECO:0000313|EMBL:ENZ47321.1}; OS [Clostridium] bolteae 90A9. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae; OC Enterocloster. OX NCBI_TaxID=997894 {ECO:0000313|EMBL:ENZ47321.1, ECO:0000313|Proteomes:UP000013126}; RN [1] {ECO:0000313|EMBL:ENZ47321.1, ECO:0000313|Proteomes:UP000013126} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=90A9 {ECO:0000313|EMBL:ENZ47321.1, RC ECO:0000313|Proteomes:UP000013126}; 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., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium bolteae 90A9."; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is required not only for elongation of protein synthesis but CC also for the initiation of all mRNA translation through initiator CC tRNA(fMet) aminoacylation. {ECO:0000256|ARBA:ARBA00003314, CC ECO:0000256|HAMAP-Rule:MF_01228}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L- CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, CC ChEBI:CHEBI:456215; EC=6.1.1.10; CC Evidence={ECO:0000256|ARBA:ARBA00001234, ECO:0000256|HAMAP- CC Rule:MF_01228}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01228}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01228}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_01228}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_01228}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000256|RuleBase:RU363039}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC MetG type 2A subfamily. {ECO:0000256|HAMAP-Rule:MF_01228}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01228}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ENZ47321.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AGYH01000016; ENZ47321.1; -; Genomic_DNA. DR EnsemblBacteria; ENZ47321; ENZ47321; HMPREF1085_04500. DR PATRIC; fig|997894.4.peg.4693; -. DR HOGENOM; CLU_009710_9_4_9; -. DR Proteomes; UP000013126; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd07957; Anticodon_Ia_Met; 1. DR CDD; cd00814; MetRS_core; 1. DR CDD; cd02800; tRNA_bind_EcMetRS_like; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1. DR InterPro; IPR041872; Anticodon_Met. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR004495; Met-tRNA-synth_bsu_C. DR InterPro; IPR014758; Met-tRNA_synth. DR InterPro; IPR023457; Met-tRNA_synth_2. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR033911; MetRS_core. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF09334; tRNA-synt_1g; 2. DR Pfam; PF01588; tRNA_bind; 1. DR PRINTS; PR01041; TRNASYNTHMET. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00398; metG; 1. DR TIGRFAMs; TIGR00399; metG_C_term; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_01228}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01228}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01228}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01228}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01228}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01228}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_01228}; Reference proteome {ECO:0000313|Proteomes:UP000013126}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_01228}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP- KW Rule:MF_01228}; Zinc {ECO:0000256|HAMAP-Rule:MF_01228}. FT DOMAIN 582..683 FT /note="TRNA-binding" FT /evidence="ECO:0000259|PROSITE:PS50886" FT REGION 548..569 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 411..431 FT /evidence="ECO:0000256|SAM:Coils" FT MOTIF 35..45 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228" FT MOTIF 322..326 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228" FT METAL 150 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228" FT METAL 153 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228" FT METAL 167 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228" FT METAL 170 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228" SQ SEQUENCE 683 AA; 77050 MW; 1210C70D338F9B03 CRC64; MNCSAPALCF RSEKEGINHM CQDCKKPYYI TTAIAYASGK PHIGNTYEII LADSIARYKR EQGYDVFFQT GTDEHGQKIE EKAEAAGVTP QEFVDKAAAE IKRIWDLMNT SYDKFIRTTD QDHEAQVQKI FKKLYDQGDI YKGYYEGLYC TPCESFFTES QLVDGKCPDC GREVKPAKEE AYFFRMSKYA PRLIEYINEH PEFIQPVSRK NEMMNNFLLP GLQDLCVSRT TFSWGIPVDF DPKHVTYVWL DALTNYITGI GYDCDGSSTD QFKKYWPADL HLIGKDIIRF HTIYWPIFLM ALDVPLPKQV FGHPWLLQGD GKMSKSKGNV LYADTLVDFF GVDAVRYFVL HEMPFDNDGV ISWELMVERM NSDLANILGN LVNRTISMSN KYFDGVVCDK GVCGEADEDL KKVVLEEVKK ADAKMEQLRV ADAMTEIFNI FRRCNKYIDE TTPWTLAKDE SQKDRLATVL YNLTEAIAIG ASLLYSFMPE TAEKILAQIH TDKRELSQMD AFGLYPNGQK VTDKPEILFA RMDIKEVLEK VEAMHGAEAA DQKQAGGQDG SSDNAEDSGI DLEAKPEITY DDFAKLQFQV GEIIKCEAVP KSKKLLCSQV KIGSQVRQIL SGIKAYYSPE EMVGKKVMVV TNLKPAKLAG MVSEGMILCA EDAEGSLALM TPEKSMPAGA QIC //