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   16-JUN-2009, entry version 56.
DE   RecName: Full=Tryptophanyl-tRNA synthetase, cytoplasmic;
DE            EC=6.1.1.2;
DE   AltName: Full=Tryptophan--tRNA ligase;
DE            Short=TrpRS;
GN   Name=wrs1; ORFNames=SPAC2F7.13c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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   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: ATP + L-tryptophan + tRNA(Trp) = AMP +
CC       diphosphate + L-tryptophyl-tRNA(Trp).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CU329670; CAA90500.1; -; Genomic_DNA.
DR   PIR; S58157; S58157.
DR   RefSeq; NP_592983.1; -.
DR   GeneID; 2541841; -.
DR   KEGG; spo:SPAC2F7.13c; -.
DR   NMPDR; fig|4896.1.peg.2953; -.
DR   GeneDB_Spombe; SPAC2F7.13c; -.
DR   OMA; Q09692; RMERLTG.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000709-MON; -.
DR   BRENDA; 6.1.1.2; 653.
DR   ArrayExpress; Q09692; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:EC.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ib.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002306; Trp-tRNA-synth_Ib.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR10055; Trp_tRNA-synt_1b; 1.
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   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis.
FT   CHAIN         1    395       Tryptophanyl-tRNA synthetase,
FT                                cytoplasmic.
FT                                /FTId=PRO_0000136743.
FT   MOTIF        91    100       "HIGH" region.
FT   MOTIF       275    279       "KMSKS" region.
FT   MOD_RES     288    288       Phosphothreonine.
FT   MOD_RES     290    290       Phosphothreonine.
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
//