ID   DUT_HCMVM               Reviewed;         388 AA.
AC   Q6SW70; D2K3M9;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   23-FEB-2022, entry version 75.
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=UL72;
OS   Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=295027;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA   Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA   Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA   Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT   "Genetic content of wild-type human cytomegalovirus.";
RL   J. Gen. Virol. 85:1301-1312(2004).
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   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 2/2.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_04031}.
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DR   EMBL; AY446894; AAR31625.1; -; Genomic_DNA.
DR   RefSeq; YP_081520.1; NC_006273.2.
DR   SMR; Q6SW70; -.
DR   PRIDE; Q6SW70; -.
DR   DNASU; 3077454; -.
DR   GeneID; 3077454; -.
DR   KEGG; vg:3077454; -.
DR   Reactome; R-HSA-9609690; HCMV Early Events.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000000938; 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:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046080; P:dUTP metabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04031; HSV_DUT; 1.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR006882; Herpes_Orf11.
DR   InterPro; IPR034745; HSV_DUT.
DR   Pfam; PF04797; Herpes_ORF11; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..388
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000416708"
FT   REGION          77..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   388 AA;  43459 MW;  4B04A9E1909D9882 CRC64;
     MLTMLTDRID SQLVLSRLPR SRFQRFWETP TLIMKEESAP SSGSIILAEK SVNMRYCVRF
     ASDSDFQTTF TLPQSTEEKY DKEQHPGEDE ASSPLPSPLK VPYKWMPSSF IVKQCHTQLA
     FYNKHIIWLS RERKVPTSLG VSLYIPEGFF GITFYKCLDA QFVCMPELLE SGLQVPQLDV
     VNLNDTFQSI FPGTIEGDIG VFPCFVPEPW QLMNLPPPNE HRFFSLRTRQ TLVIGPGHTQ
     TVYFDAAYVH APGICALIVG VRQFSQSDLI IRPTIWLPGT AAGVTVVNTS HTTVCISPHT
     TVAKAVFTTH RFTYLPVGSH PLGQMIVPPT PDIGFTHTPE HALLQRTPSP VDDDVDETEE
     DEKSSDAESP VNTSDVIFDV GPKPPRHP