SMART: Pfam domain UDG

The domain within your query sequence starts at position 112 and ends at position 186; the E-value for the UDG domain shown below is 9.6e-10.

PDILTFNLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGK
YGIGFTNMVERTTPG

UDG

PFAM accession number:	PF03167
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) ].

PFAM accession number:

PF03167

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) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry UDG