| Primary Identifier | IPR035451 | Type | Homologous_superfamily |
| Short Name | Ada-like_dom_sf |
| description | The Escherichia coli Ada protein repairs O6-methylguanine residues and methyl phosphotriesters in DNA by direct transfer of the methyl group to a cysteine residue. This domain contains four conserved cysteines that form a zinc binding site [, ]. One of these cysteines is a methyl group acceptor. The methylated domain can then specifically bind to the ada box on a DNA duplex. The zinc binding site is located in the N-terminal region and consists of four beta strands [].The methylation of the N-terminal site of Ada induces a structural change, which is independent of the transferred methyl group but enhances the promoter affinity of a remodeled surface region, trigger of the transcriptional enhancement of the ada regulon [, ].This superfamily represents the N-terminal domain of the Ada domain as well as the C-terminal domain of some ribosomal proteins (L17 from Actinobacteria and S1 from Candidatus Peregrinibacteria). |
