<p>Synonym(s): dUTP diphosphatase, Deoxyuridine-triphosphatase. </p><p>The essential enzyme dUTP pyrophosphatase (<db_xref db="EC" dbkey="3.6.1.23"/>) 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 dUPT so that uracil cannot be incorporated into DNA [<cite idref="PUB00005269"/>].</p><p>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 <taxon tax_id="562">Escherichia coli</taxon> enzyme, despite low sequence homology between the two enzymes [<cite idref="PUB00005269"/>]. </p><p>Other enzymes like deoxycytidine triphosphate deaminase (dCTP) (<db_xref db="EC" dbkey="3.5.4.13"/>) that specifically bind uridine also belong to this group suggesting that the signature may recognise a putative uridine-binding motif.</p><p>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. </p>