##gff-version 3
P53397	UniProtKB	Chain	1	376	.	.	.	ID=PRO_0000058595;Note=N-glycosylase/DNA lyase	
P53397	UniProtKB	Active site	241	241	.	.	.	Note=Schiff-base intermediate with DNA	
P53397	UniProtKB	Binding site	134	134	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P53397	UniProtKB	Binding site	139	139	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P53397	UniProtKB	Binding site	189	189	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P53397	UniProtKB	Binding site	258	258	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P53397	UniProtKB	Binding site	260	260	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P53397	UniProtKB	Binding site	262	262	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P53397	UniProtKB	Binding site	320	320	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P53397	UniProtKB	Binding site	324	324	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P53397	UniProtKB	Mutagenesis	241	241	.	.	.	Note=Abolishes both DNA glycosylase and AP lyase activity. K->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677220,ECO:0000269|PubMed:9241232;Dbxref=PMID:10677220,PMID:9241232	
P53397	UniProtKB	Mutagenesis	241	241	.	.	.	Note=Diminishes both DNA glycosylase and AP lyase activity. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677220,ECO:0000269|PubMed:9241232;Dbxref=PMID:10677220,PMID:9241232