ID   A0A0G0U2V2_9BACT        Unreviewed;       463 AA.
AC   A0A0G0U2V2;
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=UU29_C0005G0005 {ECO:0000313|EMBL:KKR83424.1};
OS   Candidatus Daviesbacteria bacterium GW2011_GWA2_40_9.
OC   Bacteria; Candidatus Daviesbacteria.
OX   NCBI_TaxID=1618424 {ECO:0000313|EMBL:KKR83424.1, ECO:0000313|Proteomes:UP000034601};
RN   [1] {ECO:0000313|EMBL:KKR83424.1, ECO:0000313|Proteomes:UP000034601}
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:KKR83424.1}.
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DR   EMBL; LCAB01000005; KKR83424.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0U2V2; -.
DR   PATRIC; fig|1618424.3.peg.293; -.
DR   Proteomes; UP000034601; 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; 2.
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          5..149
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          152..352
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
SQ   SEQUENCE   463 AA;  53148 MW;  7950DCF0D0C50402 CRC64;
     MNKFFATTPI YYVNDVPHIG HTYTTIAADV LTRYHHQKGK EAQLLTGTDE HGAKIAEAAK
     KHGEKPKEYA DKISQEFKKT WDKLNINYVR FIRTTDEDHI KIVQEFLLKM YKNGAVEEKP
     RLYKGLYCVP HEKFMSKDEL VNGLCPDHKT APIDYAEENY YFRLSDYQQK LEQLISEDKI
     KVRPLTRKNE VLGKIRQGLE DISISRANLE WGIPLPFDTS HTTYVWIDAL INYYTYGSAN
     DLWPADLHLV GKDILWFHSV IWPAMLLSIG EEPPKEVFAH GFFTINGEKM SKTIGNVIKP
     EELINKYGVD GTRYVLLAAF PFGEDGNFSW ELFDRLYNAD LANGLGNLVA RVARLSEKSG
     LSINQDMGEH ETKDFEEKIE SLDFSGALVV ANHYLKNIDE KISQEKPWEI KDKDKLQKLL
     TSYISEIVKT VKLFQPFLPQ TAENILSQFS GSIKSAPPLF PRV
//