ID   DUT_SHV21               Reviewed;         287 AA.
AC   Q01034;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_04031};
DE            Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_04031};
DE            EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_04031};
DE   AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_04031};
GN   Name=DUT {ECO:0000255|HAMAP-Rule:MF_04031}; OrderedLocusNames=54, EDRF3;
OS   Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=10383;
OH   NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA   Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA   Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA   Honess R.W.;
RT   "Primary structure of the herpesvirus saimiri genome.";
RL   J. Virol. 66:5047-5058(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1314457; DOI=10.1016/0042-6822(92)90759-i;
RA   Nicholas J., Cameron K.R., Coleman H., Newman C., Honess R.W.;
RT   "Analysis of nucleotide sequence of the rightmost 43 kbp of herpesvirus
RT   saimiri (HVS) L-DNA: general conservation of genetic organization between
RT   HVS and Epstein-Barr virus.";
RL   Virology 188:296-310(1992).
CC   -!- FUNCTION: Involved in nucleotide metabolism: produces dUMP, the
CC       immediate precursor of thymidine nucleotides and decreases the
CC       intracellular concentration of dUTP to avoid uracil incorporation into
CC       viral DNA. {ECO:0000255|HAMAP-Rule:MF_04031}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04031};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04031};
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_04031}.
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DR   EMBL; X64346; CAA45677.1; -; Genomic_DNA.
DR   EMBL; M86409; AAA46131.1; -; Genomic_DNA.
DR   RefSeq; NP_040256.1; NC_001350.1.
DR   SMR; Q01034; -.
DR   PRIDE; Q01034; -.
DR   GeneID; 1682515; -.
DR   KEGG; vg:1682515; -.
DR   Proteomes; UP000000587; Genome.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046080; P:dUTP metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.70.40.10; -; 2.
DR   HAMAP; MF_04031; HSV_DUT; 1.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR034745; HSV_DUT.
DR   Pfam; PF00692; dUTPase; 2.
DR   SUPFAM; SSF51283; SSF51283; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..287
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182957"
FT   REGION          264..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         173..175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
SQ   SEQUENCE   287 AA;  32508 MW;  598D495D74274A11 CRC64;
     MPYKVPEIYY RFEPQTFYIT SPARASNLQL INHNNILVKA GQVTIVSTGI IFPKETSFAF
     ILYGKSAKSI FCHTGLIDPG FQGELKLIVL NKTEDDITLF ENDLRVSVTA FVYGVPKLHD
     YSDLCPPRYS KDAGFDLYLP TDVTVKPRVP NRYSVNICCP AQLKSYKPVL FGRSGLAAKG
     LTIKVSRWQN QLQIIFYNYT KSQITYTART RIAQVVFMHK KHLPTTLTRL KPTMHLSENI
     KYSWARVSFQ DIKTFPVQDE KLYSSSKDTS DSQMSRGDAG LGSSGLM