ID   DUT_HHV7J               Reviewed;         379 AA.
AC   P52341;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   29-SEP-2021, entry version 79.
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=U45;
OS   Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=57278;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA   Nicholas J.;
RT   "Determination and analysis of the complete nucleotide sequence of human
RT   herpesvirus.";
RL   J. Virol. 70:5975-5989(1996).
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; U43400; AAC54707.1; -; Genomic_DNA.
DR   PIR; T41947; T41947.
DR   RefSeq; YP_073785.1; NC_001716.2.
DR   SMR; P52341; -.
DR   DNASU; 3289503; -.
DR   GeneID; 3289503; -.
DR   KEGG; vg:3289503; -.
DR   Proteomes; UP000009246; 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   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; 1.
DR   SUPFAM; SSF51283; SSF51283; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..379
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182961"
SQ   SEQUENCE   379 AA;  43877 MW;  56C61E097B67AD7C CRC64;
     MQSLPSRRSE TNKKIISEKI SETITLNKLP MSRYLHFFLF TVTDVDDIWN FSETKESSLT
     WPKIDAKQLN EYVNTELTVY QRPFSLLGIP QNGLFKSCEK IYDEFFAEHM DNEKKYLTFP
     RNRSSRFGFE NVPRVNELPI LINHFEKSRM DVILNTNKIV LVNRELIWVP CEQVRIFNLN
     VSLNIPDGLF GILTGTVNDT LCECVTELIT TENVISISLI NLSSESVMLL PGDIELVINI
     LPCYIPEPWE TYNFPSPNFI KFSLITNKDF YVESNNYTIQ NFDYMFDCPD ELKALIIANK
     EILCHGLVVE TNIWLKNTTP SVKIFNPTSQ RIFVQAGICI ATIIFTCGHF ILKLLPNRVL
     NQLAVLDKTS MLWFQYSTE