D-aminoacyl-tRNA deacylase 2 (EC 3.1.1.96) (Animalia-specific tRNA deacylase) (ATD) (D-tyrosyl-tRNA(Tyr) deacylase 2) (L-alanyl-tRNA deacylase)
1_MAEGS 6_ RIPQA 11_ RALLQ 16_ QCLHA 21_ RLQIR 26_ PADGD 31_ VAAQW 36_ VEVQR 41_ GLVIY 46_ VCFFK 51_ GADKE 56_ LLPKM 61_ VNTLL 66_ NVKLS 71_ ETENG 76_ KHVSI 81_ LDLPG 86_ NILII 91_ PQATL 96_ GGRLK 101_ GRNMQ 106_ YHSNS 111_ GKEEG 116_ FELYS 121_ QFVTL 126_ CEKEV 131_ AANSK 136_ CAEAR 141_ VVVEH 146_ GTYGN 151_ RQVLK 156_ LDTNG 161_PFTHL
1: 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 EEF1A1/EF-Tu may protect cognate achiral glycyl-tRNA(Gly) from DTD2-mediated deacetylation (By similarity)