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Database: UniProt
Entry: A0A0G1YZC1_9BACT
LinkDB: A0A0G1YZC1_9BACT
Original site: A0A0G1YZC1_9BACT 
ID   A0A0G1YZC1_9BACT        Unreviewed;       513 AA.
AC   A0A0G1YZC1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00018753};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN   Name=metS {ECO:0000313|EMBL:KKW20357.1};
GN   ORFNames=UY61_C0036G0004 {ECO:0000313|EMBL:KKW20357.1};
OS   Candidatus Adlerbacteria bacterium GW2011_GWC1_50_9.
OC   Bacteria; Candidatus Adlerbacteria.
OX   NCBI_TaxID=1618608 {ECO:0000313|EMBL:KKW20357.1, ECO:0000313|Proteomes:UP000034201};
RN   [1] {ECO:0000313|EMBL:KKW20357.1, ECO:0000313|Proteomes:UP000034201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363039}.
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:KKW20357.1}.
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DR   EMBL; LCQQ01000036; KKW20357.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1YZC1; -.
DR   PATRIC; fig|1618608.3.peg.545; -.
DR   Proteomes; UP000034201; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR041872; Anticodon_Met.
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; IPR032678; tRNA-synt_1_cat_dom.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   NCBIfam; TIGR00398; metG; 1.
DR   PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 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; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363039};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363039}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          18..138
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   DOMAIN          142..364
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          410..491
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
SQ   SEQUENCE   513 AA;  58955 MW;  B85E80FA15107B05 CRC64;
     MKNRMQKKFY LTTAIDYVNG APHIGHAVQK VWADIIARYH RLLGEKVWFL TGTDEHGANV
     VRTAASAGKS PKELADENSA KFRNFKEALN LSWDDFIRTS DEARHWPGVQ EFWKRLTEAG
     DIYKSDYRGL YCLGHEAFIT EKDLVDGKCK LHGREPEAIN EENYFFRLSK YSGEIKERIR
     SGELQILPES RKNEILSLLE EGLEDVSFSR PSKDISWGVP VPGDATQTVY VWAEALINYL
     SAVGYGRNDD WQGWWPADLH VFGKDNLRFH AAIWPGMLMS AKLSLPRMLL CHGFIQVGGR
     KMSKTLGNVV DPFEIVKNFG TDALRYYFSR EITIFEDGDF TEERFGETYE ANLVNGLGNY
     VRRVATMIKN DFGGQLERPA QEKIDSVPLQ KGELEYVSVP YFTDHVAWPE YHRAMENFEI
     NRAADITFNL IKELDGYVQR YEPFKLVKTD QEKARAVLWN LAYGAVSLAW MLSPFLPETS
     GKILDIFGAE GERESEWKRF VVKDRPPLFP RIP
//
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