Active Site

Uracil-DNA glycosylase, active site (IPR018085)

Short name: Ura-DNA_Glyclase_AS

Description

Uracil-DNA glycosylase EC:3.2.2 (UNG) [PMID: 3052275] is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved [PMID: 2555154] in bacteria and eukaryotes as well as in herpes viruses. More distantly related uracil-DNA glycosylases are also found in poxviruses [PMID: 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 [PMID: 8332455]. The N-terminal 77 amino acids of UNG1 seem to be required for mitochondrial localisation [PMID: 8332455], 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 [PMID: 7845459, PMID: 7697717] to act as a general base in the catalytic mechanism.

This signature pattern covers the most N-terminal conserved region, which contains an aspartic acid residue that has been proposed, based on X-ray structures [PMID: 7845459, PMID: 7697717] to act as a general base in the catalytic mechanism.

GO terms

Biological Process

GO:0006281 DNA repair

Molecular Function

GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns