D-aminoacyl-tRNA deacylase, with no observable activity on tRNAs charged with their cognate L-amino acid (PubMed:20007323, PubMed:24302572, PubMed:27224426). Probably acts by rejecting L-amino acids from its binding site rather than specific recognition of D-amino acids (PubMed:27224426). Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-tRNA(Tyr) (PubMed:20007323, PubMed:24302572, PubMed:27224426). Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly) (PubMed:27224426). Deacylates mischarged D.melanogaster and E.coli glycyl-tRNA(Ala) (PubMed:28362257). Probably acts via tRNA-based rather than protein-based catalysis (PubMed:24302572, PubMed:27224426). Acts on tRNAs only when the D-amino acid is either attached to the ribose 3'-OH or transferred to the 3'-OH from the 2'-OH through rapid transesterification (PubMed:24302572). Binds a number of other D-amino acids (D-Arg, D-Glu, D-His, D-Lys, D-Ser), suggesting it may also deacylate other mischarged tRNAs (PubMed:20007323). glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala) a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+) D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr) Homodimer (PubMed:20007323, PubMed:24302572). 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 (PubMed:24302572, PubMed:27224426). In the crystal structures with bound ADP (PDB 3KO4, 3KO5), the adenosine moiety is thought to represent the authentic C-terminal adenosine of charged tRNA and is annotated as such in this entry (PubMed:20007323). Belongs to the DTD family. Initially the conserved reside Thr-90 was thought to be a nucleophile; mutagenesis in this organism and E.coli indicates it is not.