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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)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glycyl-tRNA(Ala) + H2O = tRNA(Ala) + glycine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53744"},{"database":"Rhea","id":"RHEA-COMP:9657"},{"database":"Rhea","id":"RHEA-COMP:13640"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78522"}],"ecNumber":"3.1.1.96","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IIS0"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a D-aminoacyl-tRNA + H2O = a tRNA + a D-alpha-amino acid + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13953"},{"database":"Rhea","id":"RHEA-COMP:10123"},{"database":"Rhea","id":"RHEA-COMP:10124"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:59871"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:79333"}],"ecNumber":"3.1.1.96","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10766779"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:25347"},{"database":"Rhea","id":"RHEA-COMP:9707"},{"database":"Rhea","id":"RHEA-COMP:9872"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58570"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78723"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10766779"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IIS0"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10766779"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IIS0"}],"value":"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"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10766779"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10918062"}],"value":"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)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14562106"}],"value":"Present with 4610 molecules/cell in log phase SD medium"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the DTD family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"D-aminoacyl-tRNA deacylase","featureId":"PRO_0000164634"},{"type":"Motif","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"Gly-cisPro motif, important for rejection of L-amino acids","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IIS0"}]}],"keywords":[{"id":"KW-0963","category":"Cellular 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