ID   SYW_PYRAB               Reviewed;         385 AA.
AC   Q9UY11; G8ZK60;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Tryptophan--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00140};
DE            EC=6.1.1.2 {ECO:0000255|HAMAP-Rule:MF_00140};
DE   AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00140};
DE            Short=TrpRS {ECO:0000255|HAMAP-Rule:MF_00140};
GN   Name=trpS {ECO:0000255|HAMAP-Rule:MF_00140}; OrderedLocusNames=PYRAB16970;
GN   ORFNames=PAB1111;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC         tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC         Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00140};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00140}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00140}.
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DR   EMBL; AJ248288; CAB50601.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE71167.1; -; Genomic_DNA.
DR   PIR; C75020; C75020.
DR   RefSeq; WP_010868815.1; NC_000868.1.
DR   AlphaFoldDB; Q9UY11; -.
DR   SMR; Q9UY11; -.
DR   STRING; 272844.PAB1111; -.
DR   PRIDE; Q9UY11; -.
DR   EnsemblBacteria; CAB50601; CAB50601; PAB1111.
DR   GeneID; 1495996; -.
DR   KEGG; pab:PAB1111; -.
DR   PATRIC; fig|272844.11.peg.1813; -.
DR   eggNOG; arCOG01887; Archaea.
DR   HOGENOM; CLU_032621_0_1_2; -.
DR   OMA; SIYHRFM; -.
DR   OrthoDB; 33997at2157; -.
DR   PhylomeDB; Q9UY11; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00806; TrpRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00140_A; Trp_tRNA_synth_A; 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   InterPro; IPR020653; Tryptophan-tRNA-ligase_arc.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   TIGRFAMs; TIGR00233; trpS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..385
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_0000136727"
FT   MOTIF           82..90
FT                   /note="'HIGH' region"
FT   MOTIF           253..257
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   385 AA;  45100 MW;  4C29D01414976B12 CRC64;
     MVEDFKVTPW EVEGVVDYNK LIEHFGTSPL TEELLEKTAE LTKSELPLFF RRKFFFSHRD
     YDKVLQDYEE GRGFFLYTGR GPSGPMHIGH IIPFFATKWL QEKFGVNLYI QITDDEKFLF
     KENLTFEDTK HWAYENILDI IAVGFDPDKT FIFQNSEFTK IYEMAIPIAK KINFSMAKAV
     FGFTEQSKIG MIFFPAIQIA PTFFEKRRCL IPAAIDQDPY WRLQRDFAES LGYYKTAAIH
     SKFVPSLTSL SGKMSASKPE TAIYLTDSPE DVEKKVWKFA LTGGRPTLKE QREKGGEPEK
     CVVFKWLEIF FEEDDKKLKE RYYACKNGEL TCGECKRYLI SKIQEFLKEH QKRRKKAEKQ
     IEKFKYTGKL AQEMWDKAIP EPLKG