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Reviewed, UniProtKB/Swiss-Prot Q09692 (SYWC_SCHPO)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tryptophanyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.2
Alternative name(s):
    Tryptophan--tRNA ligase
      Short name=TrpRS
Gene names
Name: wrs1
ORF Names: SPAC2F7.13c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp).

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtryptophanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

tryptophan-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 395395Tryptophanyl-tRNA synthetase, cytoplasmic
PRO_0000136743

Regions

Motif91 – 10010"HIGH" region
Motif275 – 2795"KMSKS" region

Amino acid modifications

Modified residue2881Phosphothreonine Ref.2
Modified residue2901Phosphothreonine Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q09692-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: E656AE8B76C5FDF9

FASTA39544,910
        10         20         30         40         50         60 
MSVEEQIVTP WDVKGSIVDG EEKGIDYERL IVQFGTRKIT PEQLERFEKL TGKKPHLLLR 

        70         80         90        100        110        120 
RGAFFSHRDF DMILDRYEQK KPFYLYTGRG PSSDSMHLGH MIPFMFCKWL QDVFQVPLVI 

       130        140        150        160        170        180 
QLTDDEKFLF KQGVSLEDCQ RFARENAKDI IAVGFDPKKT FIFMNSTYVG GAFYQNVVRI 

       190        200        210        220        230        240 
AKCITANQSK ACFGFTDSDS IGKIHFASIQ AAPSFSSSFP HIFNGAKDIP CLIPCAIDQD 

       250        260        270        280        290        300 
PYFRLTRDVS GRLKFKKPAL LHSRFFPALQ GPQSKMSASK DSSAIFMTDT PNKIKNKINR 

       310        320        330        340        350        360 
HAFSGGGATI EIHREKGGNP DVDVAYQYLS FFLDDDEKLK QLYNTYKAGT LSTGEMKGEC 

       370        380        390 
IKLLQQFVSD FQAARSKVDE ATLDMFMDGS RKLEW 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-288 AND THR-290, MASS SPECTROMETRY.

Cross-references

Sequence databases

CU329670 Genomic DNA. Translation: CAA90500.1.
PIRS58157.
RefSeqNP_592983.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2541841.
KEGGspo:SPAC2F7.13c.
NMPDRfig|4896.1.peg.2953.

Organism-specific databases

GeneDB_SpombeSPAC2F7.13c.

Phylogenomic databases

OMAQ09692. RMERLTG.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-000709-MON.
BRENDA6.1.1.2. 653.

Gene expression databases

ArrayExpressQ09692.

Family and domain databases

InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ib.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002306. Trp-tRNA-synth_Ib.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR10055. Trp_tRNA-synt_1b. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01039. TRNASYNTHTRP.
TIGRFAMsTIGR00233. trpS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYWC_SCHPO
AccessionPrimary (citable) accession number: Q09692
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents