ID   SYW_SACS2               Reviewed;         380 AA.
AC   Q97ZX0;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 2.
DT   25-MAY-2022, entry version 96.
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=SSO0452;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK40778.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006641; AAK40778.1; ALT_INIT; Genomic_DNA.
DR   PIR; C90190; C90190.
DR   RefSeq; WP_009988707.1; NC_002754.1.
DR   AlphaFoldDB; Q97ZX0; -.
DR   SMR; Q97ZX0; -.
DR   STRING; 273057.SSO0452; -.
DR   EnsemblBacteria; AAK40778; AAK40778; SSO0452.
DR   GeneID; 44129435; -.
DR   KEGG; sso:SSO0452; -.
DR   PATRIC; fig|273057.12.peg.447; -.
DR   eggNOG; arCOG01887; Archaea.
DR   HOGENOM; CLU_032621_0_1_2; -.
DR   InParanoid; Q97ZX0; -.
DR   OMA; SIYHRFM; -.
DR   PhylomeDB; Q97ZX0; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..380
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_0000136733"
FT   MOTIF           81..89
FT                   /note="'HIGH' region"
FT   MOTIF           253..257
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   380 AA;  44691 MW;  CF8344CF63883680 CRC64;
     MPDEFTVTPW EVKGKVDYDK LIVQFGTQKI TEELKQRIKN LAGDLHVMLR RNVFFSHRDL
     DLVLNDYEKS KGFFLYTGRA PSLGMHIGHL IPFIFTKWLQ EKFNANLYIE ITDDEKYMRN
     PEFTLDQTRS WAYDNILDII AVGFNPDKTF IFQDTEYIRN MYPITVKIAK KLTFSEVRAT
     FGLDASSNIG LIFYPALQIA PTMFEKKRCL IPAGIDQDPY WRLQRDIAES LGYYKAAQIH
     SKFLPPLTGP EGKMSSSNPE TAIYLVDDPK TVERKIMKYA FSGGQPTIEL HRKYGGNPEI
     DVPFQWLYYF FEEDDNRIKE IEEEYRSGKM LTGELKQILI DKLNNFLEEH RRRREEAKEL
     VHVFKYDGKL AKQMWEKIHE