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Q07648 (DTD_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
D-tyrosyl-tRNA(Tyr) deacylase
EC=3.1.-.-
Gene names
Name:DTD1
Ordered Locus Names:YDL219W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length150 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr). Could be a defense mechanism against a harmful effect of D-tyrosine.

Subcellular location

Cytoplasm Probable.

Miscellaneous

Present with 4610 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the DTD family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processD-amino acid catabolic process

Inferred from direct assay Ref.3. Source: SGD

cytoplasmic translation

Traceable author statement. Source: SGD

   Cellular componentcytoplasm

Inferred from direct assay. Source: SGD

   Molecular functionD-tyrosyl-tRNA(Tyr) deacylase activity

Inferred from mutant phenotype Ref.3. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 150150D-tyrosyl-tRNA(Tyr) deacylase
PRO_0000164634

Sites

Active site811Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q07648 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7773D8A1FBA5E982

FASTA15016,746
        10         20         30         40         50         60 
MKIVLQKVSQ ASVVVDSKVI SSIKHGYMLL VGISIDDSMA EIDKLSKKVL SLRIFEDESR 

        70         80         90        100        110        120 
NLWKKNIKEA NGEILSVSQF TLMAKTKKGT KPDFHLAQKG HIAKELYEEF LKLLRSDLGE 

       130        140        150 
EKVKDGEFGA MMSCSLTNEG PVTIILDSDQ

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"D-tyrosyl-tRNA(Tyr) metabolism in Saccharomyces cerevisiae."
Soutourina J., Blanquet S., Plateau P.
J. Biol. Chem. 275:11626-11630(2000) [PubMed: 10766779] [Abstract]
Cited for: CHARACTERIZATION.
Strain: DBY2057.
[4]"Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces cerevisiae cells."
Soutourina J., Plateau P., Blanquet S.
J. Biol. Chem. 275:32535-32542(2000) [PubMed: 10918062] [Abstract]
Cited for: CHARACTERIZATION.
Strain: DBY2057.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z74267 Genomic DNA. Translation: CAA98798.1.
BK006938 Genomic DNA. Translation: DAA11645.1.
PIRS67782.
RefSeqNP_010062.1. NM_001180279.1.

3D structure databases

ProteinModelPortalQ07648.
SMRQ07648. Positions 1-149.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5464N.
IntActQ07648. 8 interactions.
MINTMINT-499872.
STRINGQ07648.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL219W; YDL219W; YDL219W.
GeneID851307.
KEGGsce:YDL219W.
NMPDRfig|4932.3.peg.795.

Organism-specific databases

CYGDYDL219w.
SGDS000002378. DTD1.

Phylogenomic databases

eggNOGfuNOG09961.
GeneTreeEFGT00050000006799.
HOGENOMHBG286048.
OMAMKAVIQR.
OrthoDBEOG4F4WMN.

Gene expression databases

ArrayExpressQ07648.
GenevestigatorQ07648.
GermOnlineYDL219W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR023509. DTD-like_dom.
IPR003732. DTyrtRNA_deacyls.
[Graphical view]
Gene3DG3DSA:3.50.80.10. DTyrtRNA_deacyls. 1 hit.
KOK07560.
PANTHERPTHR10472. DTyrtRNA_deacyls. 1 hit.
PfamPF02580. Tyr_Deacylase. 1 hit.
[Graphical view]
SUPFAMSSF69500. DTyrtRNA_deacyls. 1 hit.
TIGRFAMsTIGR00256. TIGR00256. 1 hit.
ProtoNetSearch...

Other

NextBio968322.

Entry information

Entry nameDTD_YEAST
AccessionPrimary (citable) accession number: Q07648
Secondary accession number(s): D6VRD5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents