Type: | Domain | Name: | Uracil-DNA glycosylase-like |
Description: | This entry represents various uracil-DNA glycosylases and related DNA glycosylases (), such as uracil-DNA glycosylase [], thermophilic uracil-DNA glycosylase [], G:T/U mismatch-specific DNA glycosylase (Mug) [], and single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) []. These proteins have a 3-layer alpha/beta/alpha structure.Uracil-DNA glycosylases are DNA repair enzymes that excise uracil residues from DNA by cleaving the N-glycosylic bond, initiating the base excision repair pathway. Uracil in DNA can arise either through the deamination of cytosine to form mutagenic U:G mispairs, or through the incorporation of dUMP by DNA polymerase to form U:A pairs []. These aberrant uracil residues are genotoxic []. The sequence of uracil-DNA glycosylase is extremely well conserved [] in bacteria and eukaryotes as well as in herpes viruses. More distantly related uracil-DNA glycosylases are also found in poxviruses []. | Short Name: | Uracil-DNA_glycosylase-like |