UniProt ID: F1QGC8
FUNCTION: D-aminoacyl-tRNA deacylase, with no observable activity on tRNAs charged with their cognate L-amino acid (By similarity). Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly) (PubMed:27224426). Deacylates mischarged D.melanogaster and E.coli glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS (PubMed:28362257). 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:27224426, ECO:0000269|PubMed:28362257}.
CATALYTIC ACTIVITY: Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + H(+) + tRNA; Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871, ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=; Evidence={ECO:0000269|PubMed:28362257};
CATALYTIC ACTIVITY: Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala); Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=; Evidence={ECO:0000269|PubMed:28362257};
SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8IIS0}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IIS0}.
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}.
SIMILARITY: Belongs to the DTD family. {ECO:0000305}.
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