ID   A0A0G1CZJ6_9BACT        Unreviewed;       476 AA.
AC   A0A0G1CZJ6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN   ORFNames=UV66_C0001G0457 {ECO:0000313|EMBL:KKS91100.1};
OS   Candidatus Woesebacteria bacterium GW2011_GWA1_43_12.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1618557 {ECO:0000313|EMBL:KKS91100.1, ECO:0000313|Proteomes:UP000034669};
RN   [1] {ECO:0000313|EMBL:KKS91100.1, ECO:0000313|Proteomes:UP000034669}
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   -!- 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:KKS91100.1}.
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DR   EMBL; LCFI01000001; KKS91100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1CZJ6; -.
DR   PATRIC; fig|1618557.3.peg.472; -.
DR   Proteomes; UP000034669; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP 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; 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   PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363039}.
FT   DOMAIN          139..362
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
SQ   SEQUENCE   476 AA;  55215 MW;  60CDF7F944087A25 CRC64;
     MIDKKSVYIT TTLPYVNSDP HLGFALEITQ ADTVARFKRQ EGFDVFFNFG TDEHGLKIYQ
     KALEQGKETQ TYVDEYAEKF DALKKALNLS YNNFIRTTDP HHIMAARGFW ERCDKNGDIY
     KKNYKQKYCV GCELEKTDSE LIENKCPLHP NRDIEIIEEE NYFFKFSKYQ QPLLEFYKKN
     PDFVVPDGKF SEIRSFVEGG LQDFSISRIK NKMPWGIPVP NDPEHVMFVW FDALVNYVSA
     IGWPDDMKKF DKWWPVVQFA GKDNLRQQTA TWQAMLMSAG ISNSKQIFIH GFITVNGQKI
     SKSLGNTINP IDVVKKYGTD PVRYYLLSKI NPYDDSDFTF EKFEDVYNGD LANGLGNLVS
     RCAKLCENSS FDFPYDISIY HILDKKIEVS LNDYRFDEAL KIVWTKVAET DKYINENEPW
     KLEGDKLKGV LSSSVESIRH IAYNLKSFLP ETAEKIEAQF KGPKIKSDRS LFPRLP
//