DTD_YEAST
ID DTD_YEAST Reviewed; 150 AA.
AC Q07648; D6VRD5;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000250|UniProtKB:Q8IIS0};
DE Short=DTD {ECO:0000305};
DE EC=3.1.1.96 {ECO:0000305|PubMed:10766779};
DE AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase {ECO:0000303|PubMed:10766779};
DE AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000250|UniProtKB:Q8IIS0};
GN Name=DTD1 {ECO:0000303|PubMed:10766779}; OrderedLocusNames=YDL219W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=DBY2057;
RX PubMed=10766779; DOI=10.1074/jbc.275.16.11626;
RA Soutourina J., Blanquet S., Plateau P.;
RT "D-tyrosyl-tRNA(Tyr) metabolism in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:11626-11630(2000).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DBY2057;
RX PubMed=10918062; DOI=10.1074/jbc.m005166200;
RA Soutourina J., Plateau P., Blanquet S.;
RT "Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces
RT cerevisiae cells.";
RL J. Biol. Chem. 275:32535-32542(2000).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged
CC D-aminoacyl-tRNAs (Probable). Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-
CC tyrosine and free tRNA(Tyr) (PubMed:10766779). May also deacylate
CC mischarged D-leucyl-tRNA(Leu) (PubMed:10918062). Also deacylates
CC mischarged glycyl-tRNA(Ala), protecting cells against glycine
CC mischarging by AlaRS (By similarity). Acts via tRNA-based rather than
CC protein-based catalysis; rejects L-amino acids rather than detecting D-
CC amino acids in the active site (By similarity). By recycling D-
CC aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme
CC counteracts the toxicity associated with the formation of D-aminoacyl-
CC tRNA entities in vivo and helps enforce protein L-homochirality (By
CC similarity). {ECO:0000250|UniProtKB:Q8IIS0,
CC ECO:0000269|PubMed:10766779, ECO:0000305|PubMed:10918062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96;
CC Evidence={ECO:0000250|UniProtKB:Q8IIS0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96;
CC Evidence={ECO:0000305|PubMed:10766779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr);
CC Xref=Rhea:RHEA:25347, Rhea:RHEA-COMP:9707, Rhea:RHEA-COMP:9872,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58570, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78723; Evidence={ECO:0000269|PubMed:10766779};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8IIS0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10766779}.
CC -!- DOMAIN: A Gly-cisPro motif from one monomer fits into the active site
CC of the other monomer to allow specific chiral rejection of L-amino
CC acids. {ECO:0000250|UniProtKB:Q8IIS0}.
CC -!- DISRUPTION PHENOTYPE: 10-fold decrease in D-tyrosyl-tRNA(Tyr) deacylase
CC activity, growth becomes more sensitive to D-tyrosine and is inhibited
CC at 0.1 mM D-Tyr (PubMed:10766779, PubMed:10918062). Growth is also
CC inhibited in the presence of 0.3 mM D-leucine; wild-type cells grow
CC well in up to 0.3 mM D-Tyr and 10 mM D-Leu (PubMed:10918062). No growth
CC differences observed in the presence of the other D-amino acids
CC (PubMed:10918062). {ECO:0000269|PubMed:10766779,
CC ECO:0000269|PubMed:10918062}.
CC -!- MISCELLANEOUS: Present with 4610 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000305}.
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DR EMBL; Z74267; CAA98798.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11645.1; -; Genomic_DNA.
DR PIR; S67782; S67782.
DR RefSeq; NP_010062.1; NM_001180279.1.
DR AlphaFoldDB; Q07648; -.
DR SMR; Q07648; -.
DR BioGRID; 31826; 96.
DR DIP; DIP-5464N; -.
DR IntAct; Q07648; 6.
DR STRING; 4932.YDL219W; -.
DR MaxQB; Q07648; -.
DR PaxDb; Q07648; -.
DR PRIDE; Q07648; -.
DR EnsemblFungi; YDL219W_mRNA; YDL219W; YDL219W.
DR GeneID; 851307; -.
DR KEGG; sce:YDL219W; -.
DR SGD; S000002378; DTD1.
DR VEuPathDB; FungiDB:YDL219W; -.
DR eggNOG; KOG3323; Eukaryota.
DR GeneTree; ENSGT00940000153431; -.
DR HOGENOM; CLU_076901_0_4_1; -.
DR InParanoid; Q07648; -.
DR OMA; GVFQAHM; -.
DR BioCyc; YEAST:G3O-29600-MON; -.
DR BRENDA; 3.1.1.96; 984.
DR PRO; PR:Q07648; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07648; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0097358; F:D-leucyl-tRNA(Leu) deacylase activity; IMP:SGD.
DR GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IMP:SGD.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:1900832; P:D-leucine catabolic process; IMP:SGD.
DR GO; GO:1900829; P:D-tyrosine catabolic process; IMP:SGD.
DR GO; GO:0006399; P:tRNA metabolic process; IMP:SGD.
DR CDD; cd00563; Dtyr_deacylase; 1.
DR Gene3D; 3.50.80.10; -; 1.
DR HAMAP; MF_00518; Deacylase_Dtd; 1.
DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR InterPro; IPR023509; DTD-like_sf.
DR PANTHER; PTHR10472; PTHR10472; 1.
DR Pfam; PF02580; Tyr_Deacylase; 1.
DR SUPFAM; SSF69500; SSF69500; 1.
DR TIGRFAMs; TIGR00256; TIGR00256; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..150
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_0000164634"
FT MOTIF 140..141
FT /note="Gly-cisPro motif, important for rejection of L-amino
FT acids"
FT /evidence="ECO:0000250|UniProtKB:Q8IIS0"
SQ SEQUENCE 150 AA; 16746 MW; 7773D8A1FBA5E982 CRC64;
MKIVLQKVSQ ASVVVDSKVI SSIKHGYMLL VGISIDDSMA EIDKLSKKVL SLRIFEDESR
NLWKKNIKEA NGEILSVSQF TLMAKTKKGT KPDFHLAQKG HIAKELYEEF LKLLRSDLGE
EKVKDGEFGA MMSCSLTNEG PVTIILDSDQ
