SYWC_SCHPO
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 03-AUG-2022, entry version 137.
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}.
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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; 4896.SPAC2F7.13c.1; -.
DR iPTMnet; Q09692; -.
DR MaxQB; Q09692; -.
DR PaxDb; Q09692; -.
DR PRIDE; Q09692; -.
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; ISS:PomBase.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; ISS:PomBase.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; -; 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 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; 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
