ID R0A5G7_9FIRM Unreviewed; 683 AA. AC R0A5G7; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 13-APR-2016, entry version 24. DE RecName: Full=Methionine--tRNA ligase {ECO:0000256|SAAS:SAAS00252424}; DE EC=6.1.1.10 {ECO:0000256|SAAS:SAAS00252424}; 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. CC {ECO:0000256|SAAS:SAAS00044467}. CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP + CC diphosphate + L-methionyl-tRNA(Met). CC {ECO:0000256|SAAS:SAAS00252038}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|SAAS:SAAS00226982}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00089728}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000256|RuleBase:RU363039}. CC -!- SIMILARITY: Contains tRNA-binding domain. CC {ECO:0000256|SAAS:SAAS00514390}. CC -!- CAUTION: The 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 Proteomes; UP000013126; 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:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.620; -; 2. 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; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR009080; tRNAsynth_1a_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|RuleBase:RU363039, KW ECO:0000256|SAAS:SAAS00514506}; KW ATP-binding {ECO:0000256|RuleBase:RU363039, KW ECO:0000256|SAAS:SAAS00514403}; KW Complete proteome {ECO:0000313|Proteomes:UP000013126}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00514420}; KW Ligase {ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00514489, KW ECO:0000313|EMBL:ENZ47321.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363039, KW ECO:0000256|SAAS:SAAS00514464}; KW Protein biosynthesis {ECO:0000256|RuleBase:RU363039, KW ECO:0000256|SAAS:SAAS00514398}; KW RNA-binding {ECO:0000256|SAAS:SAAS00514389}; KW tRNA-binding {ECO:0000256|SAAS:SAAS00514462}. FT DOMAIN 582 683 TRNA-binding. {ECO:0000259|PROSITE: FT PS50886}. 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 //