C14orf126 (Vector pENTR223.1, Accession No. BC010618)

Length: 507 Sequence: atggctgagg gtagccggat tcctcaggcc cgggcgctcc tacagcagtg cctgcacgcc cggctgcaaa ttcgcccagc cgatggggac gtcgcggccc agtgggtgga ggtccaaaga ggactggtga tctacgtgtg ctttttcaag ggagctgata aagaacttct tcccaaaatg gttaatacac tgttaaatgt gaaattaagt gagacagaaa atggcaagca tgtctctata ttggatctac ctggcaacat tcttattatc cctcaagcta cccttggagg aagactaaaa ggaagaaaca tgcaatatca ctctaactct ggaaaagaag aagggtttga actttactct caatttgtga ctctatgtga aaaagaagta gctgctaata gcaagtgtgc tgaagctagg gttgtagtgg aacatggcac ttatgggaac aggcaggtgt taaagctgga caccaacgga ccattcacac acttaattga Protein function: Deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Probably acts by rejecting L-amino acids from its binding site rather than specific recognition of D-amino acids. Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl- tRNA(Tyr). 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. [The UniProt Consortium]