| Type: | Family | Name: | A/G-specific adenine glycosylase MutY |
| Description: | The DNA repair enzyme MutY plays an important role in the prevention of DNA mutations resulting from the presence of the oxidatively damaged lesion 7,8-dihydro-8-oxo-2'-deoxyguanosine (8-OxoG). 8-OxoG can mispair with 2'-deoxycytidine 5'-triphosphate or with 2'-deoxyadenosine triphosphate during DNA replication, forming C*8-oxoG and A*8-oxoG mispairs. If unrepaired, the A=8-oxoG mispairs can result in deleterious C:G to A:T transversions. MutY, with its DNA glycosylase activity, excises adenine paired with guanine or 8-oxoG [].Multiple forms of the mammalian homologue of MutY are formed by alternative splicing and locate to the nucleus or mitochondrion, where they have been shown to interact with several other proteins involved in the repair of DNA damage [, ]. The HhH-GPD domain within the protein binds the phosphate backbone of the substrate. | Short Name: | A/G_AdeGlyc_MutY |
| DB identifier | Type | Name |
|---|---|---|
| IPR003651 | Conserved_site | Endonuclease III-like, iron-sulphur cluster loop motif |
| IPR003265 | Domain | HhH-GPD domain |
| IPR000445 | Conserved_site | Helix-hairpin-helix motif |
| IPR003583 | Domain | Helix-hairpin-helix DNA-binding motif, class 1 |
| IPR004035 | Binding_site | Endonuclease III, iron-sulphur binding site |
