Deacylates mischarged D-aminoacyl-tRNAs (By similarity). Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS (By similarity). Probably acts by rejecting L-amino acids from its binding site rather than specific recognition of D-amino acids (By similarity). Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-tRNA(Tyr) (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. In contrast to DTD1, deacylates L-Ala mischarged on tRNA(Thr)(G4.U69) by alanine-tRNA ligase AARS (PubMed:29410408). Can deacylate L-Ala due to a relaxed specificity for substrate chirality caused by the trans conformation of the Gly-Pro motif in the active site (PubMed:29410408). Also hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly) in vitro, although in vivo eef1a1a/EF-Tu may protect cognate achiral glycyl-tRNA(Gly) from DTD2-mediated deacetylation (By similarity). a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+) glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala) D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr) H2O + L-alanyl-tRNA(Thr) = H(+) + L-alanine + tRNA(Thr) Homodimer. A Gly-transPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of most L-amino acids except L-Ala. The trans conformation of the motif is maintained by Arg-143. Belongs to the DTD family.