The domain within your query sequence starts at position 72 and ends at position 262; the E-value for the UDG domain shown below is 4.98e0.

TRYCQGPKEVLFLGMNPGPFGMAQTGVPFGEVNVVRDWLGVGGPVLTPPQEHPKRPVLGL
ECPQSEVSGARFWGFFRTLCGQPQVFFRHCFVHNLCPLLFLAPSGRNLTPAELPAKQREQ
LLSICDAALCRQVQLLGVRLVVGVGRLAEQRARRALAGLTPEVQVEGLLHPSPRSAQANK
GWEAAARERLQ

UDG

Uracil DNA glycosylase superfamily
UDG
SMART accession number:SM00986
Description: -
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) ].

Family alignment:
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There are 48770 UDG domains in 48764 proteins in SMART's nrdb database.

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