ID   DUT_HHV6G               Reviewed;         376 AA.
AC   P30007;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   02-JUN-2021, entry version 63.
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 GS) (HHV-6 variant A) (Human B lymphotropic
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=10369;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1654455; DOI=10.1128/jvi.65.10.5597-5604.1991;
RA   Josephs S.F., Ablashi D.V., Salahuddin S.Z., Jagodzinski L.L.,
RA   Wong-Staal F., Gallo R.C.;
RT   "Identification of the human herpesvirus 6 glycoprotein H and putative
RT   large tegument protein genes.";
RL   J. Virol. 65:5597-5604(1991).
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; S57509; AAB19782.1; -; Genomic_DNA.
DR   PIR; D40511; D40511.
DR   SMR; P30007; -.
DR   BRENDA; 3.6.1.23; 14280.
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; SSF51283; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism.
FT   CHAIN           1..376
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182958"
SQ   SEQUENCE   376 AA;  43408 MW;  B967E545601E1683 CRC64;
     MYSAISEKIS ETITLQRQTS SRYIEFFVFR NVDINELWTT DISEDKTHDV WPAVNKKSFK
     KFLENELTSY QRPIPLLGIP QNGTVSKTCK KEKQRETDCV NYERKHGNPV 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 ATSNNA