ID   SYWC_SCHPO              Reviewed;         395 AA.
AC   Q09692;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Tryptophan--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.2;
DE   AltName: Full=Tryptophanyl-tRNA synthetase;
DE            Short=TrpRS;
GN   Name=wrs1; ORFNames=SPAC2F7.13c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-288 AND THR-290, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329670; CAA90500.1; -; Genomic_DNA.
DR   PIR; S58157; S58157.
DR   RefSeq; NP_592983.1; NM_001018383.2.
DR   AlphaFoldDB; Q09692; -.
DR   SMR; Q09692; -.
DR   BioGRID; 278332; 1.
DR   STRING; 284812.Q09692; -.
DR   iPTMnet; Q09692; -.
DR   MaxQB; Q09692; -.
DR   PaxDb; 4896-SPAC2F7-13c-1; -.
DR   EnsemblFungi; SPAC2F7.13c.1; SPAC2F7.13c.1:pep; SPAC2F7.13c.
DR   GeneID; 2541841; -.
DR   KEGG; spo:SPAC2F7.13c; -.
DR   PomBase; SPAC2F7.13c; wrs1.
DR   VEuPathDB; FungiDB:SPAC2F7.13c; -.
DR   eggNOG; KOG2145; Eukaryota.
DR   HOGENOM; CLU_032621_0_1_1; -.
DR   InParanoid; Q09692; -.
DR   OMA; SIYHRFM; -.
DR   PhylomeDB; Q09692; -.
DR   PRO; PR:Q09692; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
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; PTHR10055:SF1; TRYPTOPHAN--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10055; TRYPTOPHANYL-TRNA SYNTHETASE; 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   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..395
FT                   /note="Tryptophan--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000136743"
FT   MOTIF           91..100
FT                   /note="'HIGH' region"
FT   MOTIF           275..279
FT                   /note="'KMSKS' region"
FT   MOD_RES         288
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         290
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   395 AA;  44910 MW;  E656AE8B76C5FDF9 CRC64;
     MSVEEQIVTP WDVKGSIVDG EEKGIDYERL IVQFGTRKIT PEQLERFEKL TGKKPHLLLR
     RGAFFSHRDF DMILDRYEQK KPFYLYTGRG PSSDSMHLGH MIPFMFCKWL QDVFQVPLVI
     QLTDDEKFLF KQGVSLEDCQ RFARENAKDI IAVGFDPKKT FIFMNSTYVG GAFYQNVVRI
     AKCITANQSK ACFGFTDSDS IGKIHFASIQ AAPSFSSSFP HIFNGAKDIP CLIPCAIDQD
     PYFRLTRDVS GRLKFKKPAL LHSRFFPALQ GPQSKMSASK DSSAIFMTDT PNKIKNKINR
     HAFSGGGATI EIHREKGGNP DVDVAYQYLS FFLDDDEKLK QLYNTYKAGT LSTGEMKGEC
     IKLLQQFVSD FQAARSKVDE ATLDMFMDGS RKLEW
//