The domain within your query sequence starts at position 475 and ends at position 606; the E-value for the DBC1 domain shown below is 4.46e-90.

FQHPARLVKFLVGMKGKDEAMAIGGHWSPSLDGPNPEKDPSVLIKTAIRCCKALTGIDLS
VCTQWYRFAEIRYHRPEETHKGRTVPAHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQL
VEKLQGERKKAD

DBC1

DBC1
SMART accession number:SM01122
Description: DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the Nudix hydrolase (MutT) domain ((PUBMED:18418069)). DBC1 is predicted to bind NAD metabolites and regulate the activity of SIRT1 or related deacetylases by sensing the soluble products or substrates of the NAD-dependent deacetylation reaction ((PUBMED:18418069)).
Interpro abstract (IPR025954): Deleted in breast cancer 1 (DBC1), also known as cell division cycle and apoptosis regulator protein 2 (CCAR2), and its paralogous cell division cycle and apoptosis regulator protein 1 (CCAR1) are large multi-domain proteins, with a nuclear or perinuclear localisation, and a role in promoting apoptosis upon processing by caspases [(PUBMED:18418069)]. This entry represents the central conserved globular domain present in DBC1 and homologues, and is a catalytically inactive version of the Nudix hydrolase (MutT) domain [(PUBMED:18418069)]. It may have a role in binding NAD metabolites, such as ADP-ribose.
Family alignment:
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There are 1043 DBC1 domains in 1041 proteins in SMART's nrdb database.

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