UDGUracil DNA glycosylase superfamily
|SMART accession number:||SM00986|
|Interpro abstract (IPR005122):|
This entry represents various uracil-DNA glycosylases and related DNA glycosylases (EC 3.2.2), such as uracil-DNA glycosylase [(PUBMED:7697717)], thermophilic uracil-DNA glycosylase [(PUBMED:10339434)], G:T/U mismatch-specific DNA glycosylase (Mug) [(PUBMED:9489705)], and single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) [(PUBMED:2820976)]. 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 [(PUBMED:17116429)]. These aberrant uracil residues are genotoxic [(PUBMED:16860315)]. The sequence of uracil-DNA glycosylase is extremely well conserved [(PUBMED:2555154)] in bacteria and eukaryotes as well as in herpes viruses. More distantly related uracil-DNA glycosylases are also found in poxviruses [(PUBMED:8389453)]. In eukaryotic cells, UNG activity is found in both the nucleus and the mitochondria. Human UNG1 protein is transported to both the mitochondria and the nucleus [(PUBMED:8332455)]. The N-terminal 77 amino acids of UNG1 seem to be required for mitochondrial localization, but the presence of a mitochondrial transit peptide has not been directly demonstrated. The most N-terminal conserved region contains an aspartic acid residue which has been proposed, based on X-ray structures [(PUBMED:7845459)] to act as a general base in the catalytic mechanism.
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