Pathways & interactions
dUTPase-like superfamily (IPR036157)
Short name: dUTPase-like_sf
- Deoxyuridine triphosphate nucleotidohydrolase (IPR008181)
- Deoxycytidine triphosphate deaminase, bacterial (IPR010550)
- dCTP deaminase (IPR011962)
- Deoxyuridine triphosphate nucleotidohydrolase, archaeal (IPR023537)
- dUTPase-like (IPR029054)
- dUTPase, trimeric (IPR033704)
- Deoxyuridine 5-triphosphate nucleotidohydrolase (IPR034745)
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 [PMID: 11375495]. dUTPases from E. coli [PMID: 8646539], human [PMID: 8805593], and some virus [PMID: 9878436] all share a common distorted barrel fold and form trimers [PMID: 15276840]. In the homotrimer, each subunit folds into a twisted antiparallel beta-barrel with the N and C-terminal portions interacting with adjacent subunits [PMID: 9878436].
CTP deaminase is a member of the family of the structurally related trimeric dUTPases and the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii [PMID: 15539408].
The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases. It consists of three domain, domains I and II having a dUTPase fold [PMID: 16154087].