Protein Domain : D-aminoacyl-tRNA deacylase-like superfamily IPR023509

Type	Homologous_superfamily
Description	D-tyrosyl-tRNA(Tyr) deacylase (DTD), also known as D-aminoacyl-tRNA deacylase, is an editing enzyme that removes D-amino acids from mischarged tRNAs. Structural studies have shown various different modes of D-amino acid recognition by DTDs, suggesting an inherent plasticity that can accommodate all d-amino acids. DTDs are essentially inactive toward L-aa-tRNAs [ , ].This superfamily represents a DTD fold, consisting of a β-barrel closed on one side by a β-sheet lid [ ]. The DTD fold is present across the domains of life in twodifferent functional contexts: as an N-terminal editing domain of archaeal ThrRS (Threonyl-tRNA synthetase), which specifically removes noncognate L-serine mischarged on tRNAThr, and as a freestanding'chiral proofreading' enzyme, which removes D-amino acids from tRNAs in bacteria and eukaryotes [].
Short Name	DTD-like_sf