ID A0A0P6WPA3_9CHLR Unreviewed; 594 AA. AC A0A0P6WPA3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 28-JUN-2023, entry version 34. DE RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00098}; DE EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_00098}; DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00098}; DE Short=MetRS {ECO:0000256|HAMAP-Rule:MF_00098}; GN Name=metG {ECO:0000256|HAMAP-Rule:MF_00098}; GN ORFNames=ADM99_15870 {ECO:0000313|EMBL:KPL70588.1}; OS Leptolinea tardivitalis. OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Leptolinea. OX NCBI_TaxID=229920 {ECO:0000313|EMBL:KPL70588.1, ECO:0000313|Proteomes:UP000050430}; RN [1] {ECO:0000313|EMBL:KPL70588.1, ECO:0000313|Proteomes:UP000050430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YMTK-2 {ECO:0000313|EMBL:KPL70588.1, RC ECO:0000313|Proteomes:UP000050430}; RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.; RT "Genome sequence of Leptolinea tardivitalis DSM 16556."; RL Submitted (JUL-2015) 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_00098}. 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_00098}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00098}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00098}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00098}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00098}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC MetG type 1 subfamily. {ECO:0000256|ARBA:ARBA00008258, CC ECO:0000256|HAMAP-Rule:MF_00098}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00098}. 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:KPL70588.1}. 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; LGCK01000014; KPL70588.1; -; Genomic_DNA. DR RefSeq; WP_062422492.1; NZ_LGCK01000014.1. DR AlphaFoldDB; A0A0P6WPA3; -. DR STRING; 229920.ADM99_15870; -. DR EnsemblBacteria; KPL70588; KPL70588; ADM99_15870. DR PATRIC; fig|229920.5.peg.550; -. DR OrthoDB; 9810191at2; -. DR Proteomes; UP000050430; 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; HUPs; 1. DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1. DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR041872; Anticodon_Met. DR InterPro; IPR023458; Met-tRNA_ligase_1. DR InterPro; IPR014758; Met-tRNA_synth. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR033911; MetRS_core. DR InterPro; IPR029038; MetRS_Zn. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1. DR PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1. DR Pfam; PF19303; Anticodon_3; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR PRINTS; PR01041; TRNASYNTHMET. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR TIGRFAMs; TIGR00398; metG; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00098}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00098}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00098}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00098}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00098}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00098}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00098}; Reference proteome {ECO:0000313|Proteomes:UP000050430}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00098}. FT DOMAIN 5..412 FT /note="Methionyl/Leucyl tRNA synthetase" FT /evidence="ECO:0000259|Pfam:PF09334" FT DOMAIN 423..528 FT /note="Methionyl-tRNA synthetase anticodon-binding" FT /evidence="ECO:0000259|Pfam:PF19303" FT MOTIF 12..22 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098" FT BINDING 144 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098" FT BINDING 147 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098" FT BINDING 157 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098" FT BINDING 160 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098" SQ SEQUENCE 594 AA; 67657 MW; D483A59FE6C8D617 CRC64; MIENVLVSVA WPYANAEIHV GNITGAYLPA DIFARYQRLR GRKVLMVSGS DSHGTPITVR ADAEKTTPLE VYQRYHNSFL DLFKELGLTY DLFTSTHTSN HFDVSQKIFL SLQKNGYLYT DRELQWYAPS QKRFLPDRYV EGTCYICGFE NARSDQCDKC GNLLDPAQLI NPRSKVDGST PELRETEHTY LDLGKLQPAV VEFLKQRESY WRPNVLRQSL GQILADNLHG RAITRDLDWG IPVPLEGWDG KCLYVWFEAV IGYLSASIEW SKLIGKPDAW TEWWHGPQSQ AYYFIGKDNI PFHAVIWPAQ LTGSGKAFDE LMGLPNPAPL NLPYDVPANE FMNLENQKIS GSRNWAVWGR DFLTRYDPDP LRYYLTVNMP ESKDTDWDWE DFFHRNNDEL VATWGNLANR VLSFTCKHWE NKVPDPGELT DMDKDLLAQV EKGFETVAAE MDAVHLRAAL AEGMRLATEV NKYLDQTAPW SAIKTDKAAA ARSVYTALKA IDSLKILLAP FLPFTSERLN GFFGNDRPLF GKQYIDTISD DLGTHAALRY DPDGASGKWE PSKLEPGKEL VNPQPLFKKL DASIIEEERK RLGH //