ID   A0A0G0BJG3_9BACT        Unreviewed;       465 AA.
AC   A0A0G0BJG3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN   ORFNames=UR21_C0014G0002 {ECO:0000313|EMBL:KKP31172.1};
OS   Candidatus Woesebacteria bacterium GW2011_GWC2_31_9.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1618586 {ECO:0000313|EMBL:KKP31172.1, ECO:0000313|Proteomes:UP000034803};
RN   [1] {ECO:0000313|EMBL:KKP31172.1, ECO:0000313|Proteomes:UP000034803}
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:KKP31172.1}.
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DR   EMBL; LBOI01000014; KKP31172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0BJG3; -.
DR   PATRIC; fig|1618586.3.peg.722; -.
DR   Proteomes; UP000034803; 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          138..353
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
SQ   SEQUENCE   465 AA;  53732 MW;  C44102AFF3FECEA3 CRC64;
     MNKKKYYVTT AIDYTNDVIH IGHAYQKLLA DVLARYHRQV GDKTYFLTGT DEHGQKVEKS
     AKEKGIQPKE FVDKIAIENK NEWNKLNISF DRFIRTTDED HIKFAQEFYL KAKANGDIYK
     AKYEGFYCEG CESFKDESEL INKRCEFHSN KEIQEVVEEN YFFALSKYQK FLENHFKEHP
     EFVWPESKRK EILSFIKSGL KDFSVSRQNV SWGIPVPDDP THTIYVWFDA LINYLTYGIE
     ENCWPADVHV LGKDNQRFHA IYWPAMLKSA GYELPKTILV HDFISLNGQK VSKSLGNVIL
     PTELINKFGI DGTRYFFLRY GPLTNDIDIT LEKITESYNA DLANGLGNLV SRVAKLCEKI
     GFGGISKSTK FIGKVDDSIE SFRFDNALAI IWDKIKEIDV SINKVEPWKI TDEKKLTGFL
     QKTCSQIISI AYSLTPFLPD TSKKMLDIFY LDKIKSSEGL FPRLG
//