DTD1
Domain
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.
Function
Possible ATPase (PubMed:15653697) involved in DNA replication, may facilitate loading of CDC45 onto pre-replication complexes (PubMed:20065034).
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.
Post-translational modifications
Preferentially phosphorylated in cells arrested early in S phase (PubMed:15653697). Phosphorylation in the C-terminus weakens the interaction with CDC45 (PubMed:20065034).
Sequence Similarities
Belongs to the DTD family.
Tissue Specificity
Expressed in many adult and fetal tissues. Highest levels in testis, ovary, spleen and in adult and fetal brain.
Cellular localization
- Nucleus
- Cytoplasm
- Associated with chromatin at some replication origins containing functional DNA-unwinding elements (PubMed:20065034).
Alternative names
C20orf88, DUEB, HARS2, DTD1, D-aminoacyl-tRNA deacylase 1, DTD, DNA-unwinding element-binding protein B, Gly-tRNA(Ala) deacylase, Histidyl-tRNA synthase-related, DUE-B