ID A0A225CMT9_9MICO Unreviewed; 525 AA. AC A0A225CMT9; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 12-AUG-2020, entry version 13. 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; 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 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: 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 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: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: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:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd07957; Anticodon_Ia_Met; 1. DR CDD; cd00814; MetRS_core; 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; 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; 2. 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|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_01228, ECO:0000256|RuleBase:RU363039}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01228, ECO:0000256|RuleBase:RU363039}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01228, KW ECO:0000256|RuleBase:RU363039, ECO:0000313|EMBL:OQJ63062.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01228}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01228, ECO:0000256|RuleBase:RU363039}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_01228, ECO:0000256|RuleBase:RU363039}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01228}. FT DOMAIN 8..148 FT /note="tRNA-synt_1g" FT /evidence="ECO:0000259|Pfam:PF09334" FT DOMAIN 154..368 FT /note="tRNA-synt_1g" FT /evidence="ECO:0000259|Pfam:PF09334" FT DOMAIN 391..490 FT /note="Anticodon_1" FT /evidence="ECO:0000259|Pfam:PF08264" FT MOTIF 14..24 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228" FT MOTIF 305..309 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228" FT METAL 130 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228" FT METAL 133 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228" FT METAL 155 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228" FT METAL 158 FT /note="Zinc" FT /evidence="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 //