ID A0A225CMT9_9MICO Unreviewed; 525 AA. AC A0A225CMT9; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 22-NOV-2017, entry version 2. 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=B5P24_08690 {ECO:0000313|EMBL:OQJ63062.1}; OS Clavibacter michiganensis subsp. tessellarius. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Clavibacter. OX NCBI_TaxID=31965 {ECO:0000313|EMBL:OQJ63062.1, ECO:0000313|Proteomes:UP000215316}; RN [1] {ECO:0000313|EMBL:OQJ63062.1, ECO:0000313|Proteomes:UP000215316} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33566 {ECO:0000313|EMBL:OQJ63062.1, RC ECO:0000313|Proteomes:UP000215316}; 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. RN [2] {ECO:0000313|EMBL:OQJ63062.1, ECO:0000313|Proteomes:UP000215316} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33566 {ECO:0000313|EMBL:OQJ63062.1, RC ECO:0000313|Proteomes:UP000215316}; RA Yuan X.-K., Li X.-S., Nie J., De Boer S.H.; RT "Genomes of multiple Clavibacter strains from different subspecies."; RL Submitted (AUG-2017) 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}. 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:SAAS00725727}. 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: Monomer. {ECO:0000256|HAMAP-Rule:MF_01228}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228}. 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:OQJ63062.1}. 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; MZMQ01000001; OQJ63062.1; -; Genomic_DNA. DR Proteomes; UP000215316; Unassembled WGS sequence. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR CDD; cd00814; MetRS_core; 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; 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; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR PRINTS; PR01041; TRNASYNTHMET. DR SUPFAM; SSF47323; SSF47323; 1. DR TIGRFAMs; TIGR00398; metG; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00725705}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01228, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00725715}; KW Complete proteome {ECO:0000313|Proteomes:UP000215316}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01228, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00725673, KW ECO:0000313|EMBL:OQJ63062.1}; 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:SAAS00725669}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01228, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00725723}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01228}. FT DOMAIN 7 368 tRNA-synt_1g. {ECO:0000259|Pfam:PF09334}. FT DOMAIN 391 490 Anticodon_1. {ECO:0000259|Pfam:PF08264}. FT MOTIF 14 24 "HIGH" region. {ECO:0000256|HAMAP-Rule: FT MF_01228}. FT MOTIF 305 309 "KMSKS" region. {ECO:0000256|HAMAP-Rule: FT MF_01228}. FT METAL 130 130 Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}. FT METAL 133 133 Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}. FT METAL 155 155 Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}. FT METAL 158 158 Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}. SQ SEQUENCE 525 AA; 58890 MW; 690B1421CEB5BAD5 CRC64; MSRGEPFYIT TPIFYVNDVP HIGHAYTEVA ADVLARWHRQ RGDDTWFLTG TDEHGQKILR TATANDTTPQ AWADRLVTES WQPLLAAVDI SNDDFIRTTD ARHEESVKVF LQRLHDAGYI YTGEYKGYYC VGCEEYKQPS DLLEGTGPFE GQLVCAIHSK PVELLEEKNY FFRMSDFGER LLAFYEERPD FIQPESARNE ILSFVRRGLE DLSISRSSFD WGIPIPWDES HVVYVWFEAL MNYVTAIGYG VDDEEFRRRW PATHLVGKDI LRFHAVIWPA MLMALGEEPP RRVFGHGWLL VGGEKMSKSK LTGIVPQTIT DTFGIDAFRY HFMRAFAFGQ DGSFSWEDLS ARYQAELANG FGNLSSRVIA MVGRYFDGRI PEANALTEAD ERVLSVARSA AETADEAIER LAIHEALAAV WTLVDELNGY ITSQEPWALA KKEDGRARLE TVLHTAVRGL GTLAVLLAPV LPGATAKLWT ALGGTGTVGQ QRIDLADEWT GSGTVTPLEA PLFPRIEQEP ATPAA //