UniProt ID: Q68EL2 |
FUNCTION: 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). {ECO:0000250|UniProtKB:Q8BHA3, ECO:0000269|PubMed:29410408}. CATALYTIC ACTIVITY: Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA- COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871, ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96; Evidence={ECO:0000269|PubMed:29410408}; CATALYTIC ACTIVITY: Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala); Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96; Evidence={ECO:0000269|PubMed:29410408}; CATALYTIC ACTIVITY: Reaction=D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr); Xref=Rhea:RHEA:25347, Rhea:RHEA-COMP:9707, Rhea:RHEA-COMP:9872, ChEBI:CHEBI:15377, ChEBI:CHEBI:58570, ChEBI:CHEBI:78442, ChEBI:CHEBI:78723; Evidence={ECO:0000250|UniProtKB:Q8BHA3}; CATALYTIC ACTIVITY: Reaction=H2O + L-alanyl-tRNA(Thr) = H(+) + L-alanine + tRNA(Thr); Xref=Rhea:RHEA:17793, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:14576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497; Evidence={ECO:0000269|PubMed:29410408}; SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8BHA3}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. DOMAIN: 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. {ECO:0000250|UniProtKB:Q8BHA3}. SIMILARITY: Belongs to the DTD family. {ECO:0000305}. |
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