Protein Domain : Alkylbase DNA glycosidase, conserved site IPR000035

Type  Conserved_site
Description  Alkylbase DNA glycosidases [ ] are DNA repair enzymes that hydrolyse the deoxyribose N-glycosidic bond to excise various alkylated bases from a damaged DNA polymer. In Escherichia coli there are two alkylbase DNA glycosidases: one (gene tag) which is constitutively expressed and which is specific for the removal of 3-methyladenine (), and one (gene alkA) which is induced during adaptation to alkylation and which can remove a variety of alkylation products ( ). Tag and alkA do not share any region of sequence similarity. In yeast there is an alkylbase DNA glycosidase (gene MAG1) [ , ], which can remove 3-methyladenine or 7-methyladenine and which is structurally related to alkA. MAG and alkA are both proteins of about 300 amino acid residues. While the C- and N-terminal ends appear to be unrelated, there is a central region of about 130 residues which is well conserved.
Short Name  Alkylbase_DNA_glycsylse_CS

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