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D-aminoacyl-tRNA deacylase (DTD) (EC 3.1.1.96) (D-tyrosyl-tRNA(Tyr) deacylase) (Gly-tRNA(Ala) deacylase) (EC 3.1.1.-)

 DTD_YEAST               Reviewed;         150 AA.
Q07648; D6VRD5;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-MAR-2018, entry version 135.
RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000250|UniProtKB:Q8IIS0};
Short=DTD {ECO:0000305};
EC=3.1.1.96 {ECO:0000305|PubMed:10766779};
AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase {ECO:0000303|PubMed:10766779};
AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000250|UniProtKB:Q8IIS0};
EC=3.1.1.- {ECO:0000250|UniProtKB:Q8IIS0};
Name=DTD1 {ECO:0000303|PubMed:10766779}; OrderedLocusNames=YDL219W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
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., 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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=DBY2057;
PubMed=10766779; DOI=10.1074/jbc.275.16.11626;
Soutourina J., Blanquet S., Plateau P.;
"D-tyrosyl-tRNA(Tyr) metabolism in Saccharomyces cerevisiae.";
J. Biol. Chem. 275:11626-11630(2000).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=DBY2057;
PubMed=10918062; DOI=10.1074/jbc.M005166200;
Soutourina J., Plateau P., Blanquet S.;
"Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces
cerevisiae cells.";
J. Biol. Chem. 275:32535-32542(2000).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
-!- FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates
mischarged D-aminoacyl-tRNAs (Probable). Hydrolyzes D-tyrosyl-
tRNA(Tyr) into D-tyrosine and free tRNA(Tyr) (PubMed:10766779).
May also deacylate mischarged D-leucyl-tRNA(Leu)
(PubMed:10918062). Also deacylates mischarged glycyl-tRNA(Ala),
protecting cells against glycine mischarging by AlaRS (By
similarity). Acts via tRNA-based rather than protein-based
catalysis; rejects L-amino acids rather than detecting D-amino
acids in the active site (By similarity). By recycling D-
aminoacyl-tRNA to D-amino acids and free tRNA molecules, this
enzyme counteracts the toxicity associated with the formation of
D-aminoacyl-tRNA entities in vivo and helps enforce protein L-
homochirality (By similarity). {ECO:0000250|UniProtKB:Q8IIS0,
ECO:0000269|PubMed:10766779, ECO:0000305|PubMed:10918062}.
-!- CATALYTIC ACTIVITY: Glycyl-tRNA(Ala) + H(2)O = glycine +
tRNA(Ala). {ECO:0000250|UniProtKB:Q8IIS0}.
-!- CATALYTIC ACTIVITY: A D-aminoacyl-tRNA + H(2)O = a D-amino acid +
tRNA. {ECO:0000305|PubMed:10766779}.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8IIS0}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10766779}.
-!- DOMAIN: A Gly-cisPro motif from one monomer fits into the active
site of the other monomer to allow specific chiral rejection of L-
amino acids. {ECO:0000250|UniProtKB:Q8IIS0}.
-!- DISRUPTION PHENOTYPE: 10-fold decrease in D-tyrosyl-tRNA(Tyr)
deacylase activity, growth becomes more sensitive to D-tyrosine
and is inhibited at 0.1 mM D-Tyr (PubMed:10766779,
PubMed:10918062). Growth is also inhibited in the presence of 0.3
mM D-leucine; wild-type cells grow well in up to 0.3 mM D-Tyr and
10 mM D-Leu (PubMed:10918062). No growth differences observed in
the presence of the other D-amino acids (PubMed:10918062).
{ECO:0000269|PubMed:10766779, ECO:0000269|PubMed:10918062}.
-!- MISCELLANEOUS: Present with 4610 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the DTD family. {ECO:0000305}.
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EMBL; Z74267; CAA98798.1; -; Genomic_DNA.
EMBL; BK006938; DAA11645.1; -; Genomic_DNA.
PIR; S67782; S67782.
RefSeq; NP_010062.1; NM_001180279.1.
ProteinModelPortal; Q07648; -.
SMR; Q07648; -.
BioGrid; 31826; 91.
DIP; DIP-5464N; -.
IntAct; Q07648; 6.
STRING; 4932.YDL219W; -.
MaxQB; Q07648; -.
PaxDb; Q07648; -.
PRIDE; Q07648; -.
EnsemblFungi; YDL219W; YDL219W; YDL219W.
GeneID; 851307; -.
KEGG; sce:YDL219W; -.
EuPathDB; FungiDB:YDL219W; -.
SGD; S000002378; DTD1.
GeneTree; ENSGT00390000008298; -.
HOGENOM; HOG000113981; -.
InParanoid; Q07648; -.
KO; K07560; -.
OMA; GVFQAHM; -.
OrthoDB; EOG092C54JK; -.
BioCyc; YEAST:G3O-29600-MONOMER; -.
BRENDA; 3.1.1.96; 984.
PRO; PR:Q07648; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central.
GO; GO:0097358; F:D-leucyl-tRNA(Leu) deacylase activity; IMP:SGD.
GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IMP:SGD.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
GO; GO:1900832; P:D-leucine catabolic process; IMP:SGD.
GO; GO:1900829; P:D-tyrosine catabolic process; IMP:SGD.
GO; GO:0006399; P:tRNA metabolic process; IMP:SGD.
CDD; cd00563; Dtyr_deacylase; 1.
Gene3D; 3.50.80.10; -; 1.
HAMAP; MF_00518; Deacylase_Dtd; 1.
InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
InterPro; IPR023509; DTD-like_sf.
PANTHER; PTHR10472; PTHR10472; 1.
Pfam; PF02580; Tyr_Deacylase; 1.
SUPFAM; SSF69500; SSF69500; 1.
TIGRFAMs; TIGR00256; TIGR00256; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Hydrolase; Reference proteome;
RNA-binding; tRNA-binding.
CHAIN 1 150 D-aminoacyl-tRNA deacylase.
/FTId=PRO_0000164634.
MOTIF 140 141 Gly-cisPro motif, important for rejection
of L-amino acids.
{ECO:0000250|UniProtKB:Q8IIS0}.
SEQUENCE 150 AA; 16746 MW; 7773D8A1FBA5E982 CRC64;
MKIVLQKVSQ ASVVVDSKVI SSIKHGYMLL VGISIDDSMA EIDKLSKKVL SLRIFEDESR
NLWKKNIKEA NGEILSVSQF TLMAKTKKGT KPDFHLAQKG HIAKELYEEF LKLLRSDLGE
EKVKDGEFGA MMSCSLTNEG PVTIILDSDQ


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