ID   DUT_HHV6U               Reviewed;         376 AA.
AC   Q06095;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   24-JAN-2024, entry version 87.
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 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS   lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Betaherpesvirinae; Roseolovirus;
OC   Roseolovirus humanbeta6a; Human betaherpesvirus 6A.
OX   NCBI_TaxID=10370;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1333836; DOI=10.3109/10425179209039693;
RA   Gompels U.A., Carss A.L., Sun N., Arrand J.R.;
RT   "Infectivity determinants encoded in a conserved gene block of human
RT   herpesvirus-6.";
RL   DNA Seq. 3:25-39(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA   Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA   Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT   "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT   genome evolution.";
RL   Virology 209:29-51(1995).
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; X64320; CAA45600.1; -; Genomic_DNA.
DR   EMBL; X83413; CAA58379.1; -; Genomic_DNA.
DR   EMBL; X92436; CAA63171.1; -; Genomic_DNA.
DR   PIR; A56653; A56653.
DR   RefSeq; NP_042938.1; NC_001664.2.
DR   SMR; Q06095; -.
DR   DNASU; 1487924; -.
DR   GeneID; 1487924; -.
DR   KEGG; vg:1487924; -.
DR   Proteomes; UP000009295; 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_0000182959"
SQ   SEQUENCE   376 AA;  43398 MW;  81B3CE9C817D27D5 CRC64;
     MYSAISEKIS ETITLQRQTS SRYIEFFVFR NVDINELWTT DISEDKTHDV WPAVNEKSFK
     KFLENELTSY QRPIPLLGIP QNGTVSKTCK KEKQRETDCV NYERKRGNPV TFYPRHRAKR
     NANTDTCISE EPSILVSHHR NSKMDVFMDT NKITLVNREL IWVPHDQVRI VKLDISLYIP
     DGFFGVITGH SNDVFCECVT EIITDETDIS VFLMNLSEHS LMLLPGDVEF SINFLPCYIP
     EPWEMINLSP PEFAIFHLKA SREFIAKPNS YTIQYFDAMY VCADELKALM IPSKEIAKLG
     LLIETYIWNK DTIPSIKIFN STRKTIYIPT GICIARIIFT CGHFCLSLMP ERAINRLQVL
     DANSSFLFHY AASNNA
//