An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. 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). Upon expression in B.subtilis strain 168 confers resistance to D-Tyr and D-Asp, suggesting it acts on both of these amino acids (PubMed:25441601). glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala) a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+) Homodimer. 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. Confers the ability to grow in the presence of 20 mg/ml D-Tyr and 500 mg/ml D-Asp to B.subtilis, showing it can be used as a selective marker in bacteria that do not have a functional copy of this gene. Can also function in an E.coli MG1655 dtd deletion, although in this case it confers resistance to toxic amino acid D-Tyr but not D-Trp (D-Asp is not toxic in this experiment) (PubMed:25441601). Belongs to the DTD family.