InterPro domain: IPR005122

This entry represents various uracil-DNA glycosylases and related DNA glycosylases ( 3.2.2 ), such as uracil-DNA glycosylase [ 1 ], thermophilic uracil-DNA glycosylase [ 2 ], G:T/U mismatch-specific DNA glycosylase (Mug) [ 3 ], and single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) [ 4 ]. 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 [ 5 ]. These aberrant uracil residues are genotoxic [ 6 ]. The sequence of uracil-DNA glycosylase is extremely well conserved [ 7 ] in bacteria and eukaryotes as well as in herpes viruses. More distantly related uracil-DNA glycosylases are also found in poxviruses [ 8 ].

1. Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. Cell 80, 869-78
2. Thermostable uracil-DNA glycosylase from Thermotoga maritima a member of a novel class of DNA repair enzymes. Curr. Biol. 9, 531-4
3. Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell 92, 117-29
4. The cap-binding protein complex in uninfected and poliovirus-infected HeLa cells. J. Biol. Chem. 262, 13599-606
5. Uracil in DNA--general mutagen, but normal intermediate in acquired immunity. DNA Repair (Amst.) 6, 505-16
6. Genomic uracil and human disease. Exp. Cell Res. 312, 2666-72
7. Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme. EMBO J. 8, 3121-5
8. Identification of a poxvirus gene encoding a uracil DNA glycosylase. Proc. Natl. Acad. Sci. U.S.A. 90, 4518-22