Deoxyuridine triphosphate nucleotidohydrolase, archaeal (IPR023537)

Short name: dUTPase_archaeal

Overlapping homologous superfamilies

Family relationships



The essential enzyme deoxyuridine triphosphate nucleotidohydrolase (dUTPase) (EC: is specific for dUTP and is critical for the fidelity of DNA replication and repair. dUTPase hydrolyzes dUTP to dUMP and pyrophosphate, simultaneously reducing dUTP levels and providing the dUMP for dTTP biosynthesis. dUTPase decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA [PMID: 8805593].

The crystal structure of human dUTPase reveals that each subunit of the dUTPase trimer folds into an eight-stranded jelly-roll beta barrel, with the C-terminal beta strands interchanged among the subunits. The structure is similar to that of the Escherichia coli enzyme, despite low sequence homology between the two enzymes [PMID: 8805593].

Other enzymes like deoxycytidine triphosphate (dCTP) deaminase (EC: that specifically bind uridine also belong to this group suggesting that the signature may recognise a putative uridine-binding motif.

Some retroviruses encode dUTPases. Retroviral dUTPase is synthesised as part of POL polyprotein that contains; an aspartyl protease, a reverse transcriptase, dUTPase and RNase H.

This entry represents archaeal dUTPases.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0004170 dUTP diphosphatase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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