The domain within your query sequence starts at position 69 and ends at position 198; the E-value for the dUTPase domain shown below is 1.6e-52.



PFAM accession number:PF00692
Interpro abstract (IPR029054):

This entry represents a distorted barrel domain found in deoxyuridine triphosphate nucleotidohydrolases and CTP deaminases.

Deoxyuridine triphosphate nucleotidohydrolase (dUTPase) cleaves dUTP into pyrophosphate and dUMP. Three different subunit organisations of dUTPases have been found: they are either monomers, dimers or trimers [ (PUBMED:11375495) ]. dUTPases from E. coli [ (PUBMED:8646539) ], human [ (PUBMED:8805593) ], and some virus [ (PUBMED:9878436) ] all share a common distorted barrel fold and form trimers [ (PUBMED:15276840) ]. In the homotrimer, each subunit folds into a twisted antiparallel beta-barrel with the N and C-terminal portions interacting with adjacent subunits [ (PUBMED:9878436) ].

CTP deaminase is a member of the family of the structurally related trimeric dUTPases and the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii [ (PUBMED:15539408) ].

The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases. It consists of three domain, domains I and II having a dUTPase fold [ (PUBMED:16154087) ].

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