ID A0A1F7WK87_9BACT Unreviewed; 317 AA.
AC A0A1F7WK87;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN ORFNames=A2115_02655 {ECO:0000313|EMBL:OGM03234.1};
OS Candidatus Woesebacteria bacterium GWA1_41_8.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1802471 {ECO:0000313|EMBL:OGM03234.1, ECO:0000313|Proteomes:UP000176198};
RN [1] {ECO:0000313|EMBL:OGM03234.1, ECO:0000313|Proteomes:UP000176198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGM03234.1}.
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DR EMBL; MGFJ01000001; OGM03234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7WK87; -.
DR STRING; 1802471.A2115_02655; -.
DR Proteomes; UP000176198; 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; 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.
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 317 AA; 36008 MW; 676A79E123352B4D CRC64;
MSEKKILVSG VKPTGRSHIG NYFGALRQFV ALQDEYKSHI FVADLHALTT VQNRAEMEEN
ILGVVLDFLA VGLDPKKTVL YKQSDVPQVA ELAWIFDCLT TVPYLMRAHA FKDAEARNKE
INVGVFNYPM LMAADILIQD ADAVPVGQDQ RQHIEISRDT AEKFNRIFGE TFKVPVSYIL
ENVATVPGTD GQKMSKGYNN TIPLFATNEE IEKAVLSIVT DSGIGKPENV YAIHTLFREK
KELDELYSEK QGKYKELKEA LIEDMKTFVR PLREKRAEFE KDKGRVLEII KQGGEVARQR
AEKKMEEVRE KVGFKLH
//
