ID A0A0P6WPA3_9CHLR Unreviewed; 594 AA. AC A0A0P6WPA3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 22-NOV-2017, entry version 15. 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; Chloroflexi; 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 CC but also for the initiation of all mRNA translation through CC initiator tRNA(fMet) aminoacylation. {ECO:0000256|HAMAP- CC Rule:MF_00098}. CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP + CC diphosphate + L-methionyl-tRNA(Met). {ECO:0000256|HAMAP- CC Rule:MF_00098, ECO:0000256|SAAS:SAAS00720840}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00098}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00098}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00098}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00098, CC ECO:0000256|SAAS:SAAS00629344}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. MetG type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00098}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00098}. 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: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 EnsemblBacteria; KPL70588; KPL70588; ADM99_15870. DR PATRIC; fig|229920.5.peg.550; -. 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; cd00814; MetRS_core; 1. DR Gene3D; 2.20.28.20; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. 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 Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR PRINTS; PR01041; TRNASYNTHMET. DR SUPFAM; SSF47323; SSF47323; 2. DR SUPFAM; SSF57770; SSF57770; 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|HAMAP-Rule:MF_00098, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00720757}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00098, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00720806}; KW Complete proteome {ECO:0000313|Proteomes:UP000050430}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00098, KW ECO:0000256|SAAS:SAAS00629349}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00098, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00720833, KW ECO:0000313|EMBL:KPL70588.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00098}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00098, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00720633}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00098, KW ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00720831}; KW Reference proteome {ECO:0000313|Proteomes:UP000050430}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00098}. FT DOMAIN 5 412 tRNA-synt_1g. {ECO:0000259|Pfam:PF09334}. FT DOMAIN 433 526 Anticodon_1. {ECO:0000259|Pfam:PF08264}. FT MOTIF 12 22 "HIGH" region. {ECO:0000256|HAMAP-Rule: FT MF_00098}. FT METAL 144 144 Zinc. {ECO:0000256|HAMAP-Rule:MF_00098}. FT METAL 147 147 Zinc. {ECO:0000256|HAMAP-Rule:MF_00098}. FT METAL 157 157 Zinc. {ECO:0000256|HAMAP-Rule:MF_00098}. FT METAL 160 160 Zinc. {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 //