ID   DUT_HHV6Z               Reviewed;         376 AA.
AC   P52541;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, 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=U45;
OS   Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Betaherpesvirinae; Roseolovirus;
OC   Roseolovirus humanbeta6b; Human herpesvirus 6B.
OX   NCBI_TaxID=36351;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7983761; DOI=10.1128/jvi.69.1.589-596.1995;
RA   Stamey F.R., Dominguez G., Black J.B., Dambaugh T.R., Pellett P.E.;
RT   "Intragenomic linear amplification of human herpesvirus 6B oriLyt suggests
RT   acquisition of oriLyt by transposition.";
RL   J. Virol. 69:589-596(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA   Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA   Pellett P.E.;
RT   "Human herpesvirus 6B genome sequence: coding content and comparison with
RT   human herpesvirus 6A.";
RL   J. Virol. 73:8040-8052(1999).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_04031};
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_04031}.
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DR   EMBL; AF157706; AAB06343.1; -; Genomic_DNA.
DR   PIR; T44005; T44005.
DR   RefSeq; NP_050226.1; NC_000898.1.
DR   SMR; P52541; -.
DR   DNASU; 1497047; -.
DR   GeneID; 1497047; -.
DR   KEGG; vg:1497047; -.
DR   Proteomes; UP000006930; Segment.
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; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..376
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182960"
SQ   SEQUENCE   376 AA;  43407 MW;  7CF7104EFBC92F0B CRC64;
     MYSVISEKIS ETITLQRQTS SRYIEFFVFR NVDINELWTT DISEDKTHDV WPAINEKSFK
     KFLENELTSY QRPISLLGIP QNGTVSKTCK REKQRETDCV NYVRKHGNPV TFYPRHRAKR
     NANTDTCISE EPSILVSHHR NSKMDVFMDA NKITLVNREL IWVPHDQVRI VKLDISLCIP
     DGFFGVIIGH SNDVFCECIT EIITDETDIS VFLMNLSEHS LMLLPGDVEF SINFLPCYIP
     EPWEMINLSP PESAVFHLKT CREFIIKPNS YTIQCFDAMY VCADELKALM IPSKEIIKLG
     LLIETYIWNK DTIPSIKIFN STRKTIYIPT GICIARIIFT CGHFCLSLMP ERAINRLQVL
     DASSFFLFHY AAFSNA
//