SMART: Pfam domain NUDIX

The domain within your query sequence starts at position 353 and ends at position 463; the E-value for the NUDIX_4 domain shown below is 2.3e-23.

GPLVLLVQRPDSGLLAGLWEFPSVTLEPSEQHQHKALLQELQRWCGPLPAIRLQHLGEVI
HIFSHIKLTYQVYSLALDQAPASTAPPGARWLTWEEFCNAAVSTAMKKVFR

NUDIX_4

PFAM accession number:	PF14815
Interpro abstract (IPR029119):	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 [ (PUBMED: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 [ (PUBMED:11554314) (PUBMED:15465463) (PUBMED:15102448) (PUBMED:14618256) (PUBMED:10858279) (PUBMED:10350454) (PUBMED: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 [ (PUBMED:10858279) (PUBMED:16378245) ].

PFAM accession number:

PF14815

Interpro abstract (IPR029119):

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 [ (PUBMED: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 [ (PUBMED:11554314) (PUBMED:15465463) (PUBMED:15102448) (PUBMED:14618256) (PUBMED:10858279) (PUBMED:10350454) (PUBMED: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 [ (PUBMED:10858279) (PUBMED:16378245) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry NUDIX_4