The domain within your query sequence starts at position 109 and ends at position 304; the E-value for the Pur_DNA_glyco domain shown below is 1.2e-61.

EFFDQPAVTLARAFLGQVLVRRLADGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRG
MFMKPGTLYVYLIYGMYFCLNVSSQGAGACVLLRALEPLEGLETMRQLRNSLRKSTVGRS
LKDRELCSGPSKLCQALAIDKSFDQRDLAQDDAVWLEHGPLESSSPAVVVAAARIGIGHA
GEWTQKPLRFYVQGSP

Pur_DNA_glyco

Pur_DNA_glyco
PFAM accession number:PF02245
Interpro abstract (IPR003180):

Methylpurine-DNA glycosylase (MPG, or alkyladenine DNA glycosylase (AAG)) is a base excision-repair protein, catalyzing the first step in base excision repair by cleaving damaged DNA bases within double-stranded DNA to produce an abasic site. MPG bends DNA by intercalating between the base pairs, causing the damaged base to flip out of the double helix and into the enzyme active site for cleavage. It is responsible for the hydrolysis of the deoxyribose N-glycosidic bond, excising 3-methyladenine and 3-methylguanine from damaged DNA [(PUBMED:18191412), (PUBMED:10440863), (PUBMED:11554308), (PUBMED:9790531), (PUBMED:11106395), (PUBMED:14567703), (PUBMED:14688248), (PUBMED:15990363), (PUBMED:12077143), (PUBMED:14555760), (PUBMED:12323378)]. Its action is induced by alkylating chemotherapeutics, as well as deaminated and lipid peroxidation-induced purine adducts [(PUBMED:17768096)]. MPG without an N-terminal extension excises hypoxanthine with one-third of the efficiency of full-length MPG under similar conditions, suggesting that is function may largely be attributable to the N-terminal extension [(PUBMED:17716976)].

Although AAG represents one of six DNA glycosylase classes, it lacks the helix-hairpin-helix active site motif associated with other base excision repair glycosylases and is structurally distinct from them.

GO process:base-excision repair (GO:0006284)
GO function:alkylbase DNA N-glycosylase activity (GO:0003905), DNA binding (GO:0003677)

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