ID   A0A0G1VIY4_9BACT        Unreviewed;       318 AA.
AC   A0A0G1VIY4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE            EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN   ORFNames=UY03_C0002G0024 {ECO:0000313|EMBL:KKU78198.1};
OS   Parcubacteria group bacterium GW2011_GWA2_47_64.
OC   Bacteria.
OX   NCBI_TaxID=1618845 {ECO:0000313|EMBL:KKU78198.1, ECO:0000313|Proteomes:UP000034132};
RN   [1] {ECO:0000313|EMBL:KKU78198.1, ECO:0000313|Proteomes:UP000034132}
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|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363036}.
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:KKU78198.1}.
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DR   EMBL; LCOL01000002; KKU78198.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1VIY4; -.
DR   PATRIC; fig|1618845.3.peg.94; -.
DR   Proteomes; UP000034132; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00806; TrpRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002306; Trp-tRNA-ligase.
DR   NCBIfam; TIGR00233; trpS; 1.
DR   PANTHER; PTHR43766; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43766:SF1; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363036};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363036};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363036};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363036};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363036}.
SQ   SEQUENCE   318 AA;  35684 MW;  D2E8D016BF1E292C CRC64;
     MAQGKKILLS GIQPSGRPHI GNYFGAMKQF VEMQRDHDCF FMIADYHALN TIQDAGALQK
     GIIDLAIDYL AVGLDPKKSV IFKQSDVSEH TELAWIFDAI TTMPFLARAH AFKDAEAKNK
     EISVGLFNYP MLMAADILLY DTDIVPVGAD QKQHVEITRD TAEKFNRIFG KTFNLPEAKI
     LPTVAVVPGI DGRKMSKSYG NTVPLFAEDE EIEKLVMSIV TDSSGGIPKN VYEIHKLFRS
     EDDLASLYQS KEGKYKELKE KLTHDIKAFI RPLRERRKAI ANDTDAVRNI LKDGGTRAKE
     KASAKMEEVR EKVGVKLY
//