MutY, C-terminal (IPR029119)

Short name: MutY_C

Overlapping homologous superfamilies

Domain relationships



Adenine DNA glycosylase (called MutY in bacteria and hMYH in humans) initiates repair of A-oxoG to C-G by removing the inappropriately paired adenine base from the DNA backbone. MutY belongs to a structural superfamily of proteins (the NUDIX hydrolase superfamily) that hydrolyse a wide range of organic pyrophosphates [PMID: 16378245].

Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. They are also recognized by a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V). However, DNA glycosylase does not seem to contain this signature motif. DNA glycosylase consists of 2 domains: the N-terminal domain contains the catalytic properties of the enzyme and the C-terminal domain affects substrate (oxoG) binding and enzymatic turnover. The C-terminal domain is highly similar to MutT, based on secondary structure and topology, despite low sequence identity. MutT sanitizes the nucleotide precursor pool by hydrolyzing oxo-dGTP to oxo-dGMO and inorganic pyrophosphate. The similarity strongly suggests that the two proteins share a common evolutionary origin [PMID: 11554314, PMID: 15465463, PMID: 15102448, PMID: 14618256, PMID: 10858279, PMID: 10350454, PMID: 15056851].

This entry represents the C-terminal domain of MutY. Its structure is similar to the NUDIX fold, which is an alpha/beta/alpha sandwich [PMID: 10858279, PMID: 16378245].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.