ID R0A5G7_9FIRM Unreviewed; 683 AA. AC R0A5G7; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 33. 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; Clostridiales; Lachnospiraceae. 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., RA Wortman J., 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 CC but also for the initiation of all mRNA translation through CC initiator tRNA(fMet) aminoacylation. {ECO:0000256|HAMAP- CC Rule:MF_01228, ECO:0000256|SAAS:SAAS00629317}. CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP + CC diphosphate + L-methionyl-tRNA(Met). {ECO:0000256|HAMAP- CC Rule:MF_01228, ECO:0000256|SAAS:SAAS00654290}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01228}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01228}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01228, CC ECO:0000256|SAAS:SAAS00629338}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228, CC ECO:0000256|SAAS:SAAS00654270}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. MetG type 2A subfamily. {ECO:0000256|HAMAP-Rule:MF_01228}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01228}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 Proteomes; UP000013126; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR CDD; cd00814; MetRS_core; 1. DR CDD; cd02800; tRNA_bind_EcMetRS_like; 1. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1. 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; 1. 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|HAMAP-Rule:MF_01228, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00654294}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01228, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00654376}; KW Complete proteome {ECO:0000313|Proteomes:UP000013126}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228, KW ECO:0000256|SAAS:SAAS00654286}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01228, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00654316, KW ECO:0000313|EMBL:ENZ47321.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01228}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01228, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00654333}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01228, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00654288}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01228, ECO:0000256|PROSITE- KW ProRule:PRU00209, ECO:0000256|SAAS:SAAS00514389}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01228, ECO:0000256|PROSITE- KW ProRule:PRU00209, ECO:0000256|SAAS:SAAS00514462}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01228}. FT DOMAIN 582 683 TRNA-binding. {ECO:0000259|PROSITE: FT PS50886}. FT MOTIF 35 45 "HIGH" region. {ECO:0000256|HAMAP-Rule: FT MF_01228}. FT MOTIF 322 326 "KMSKS" region. {ECO:0000256|HAMAP-Rule: FT MF_01228}. FT METAL 150 150 Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}. FT METAL 153 153 Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}. FT METAL 167 167 Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}. FT METAL 170 170 Zinc. {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 //