ID   DUT_HHV11               Reviewed;         371 AA.
AC   P10234; Q09I84;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   22-SEP-2009, entry version 46.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
DE   AltName: Full=dUTP pyrophosphatase;
GN   ORFNames=UL50;
OS   Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus
OS   1).
OC   Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
OC   Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10299;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=88274327; PubMed=2839594;
RA   McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C.,
RA   McNab D., Perry L.J., Scott J.E., Taylor P.;
RT   "The complete DNA sequence of the long unique region in the genome of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 69:1531-1574(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nonneuroinvasive mutant HF10;
RX   PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA   Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT   "Determination and analysis of the DNA sequence of highly attenuated
RT   herpes simplex virus type 1 mutant HF10, a potential oncolytic
RT   virus.";
RL   Microbes Infect. 9:142-149(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17 syn+;
RA   Cunningham C., Davison A.J.;
RT   "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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
CC       into viral DNA (By similarity).
CC   -!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SIMILARITY: Belongs to the dUTPase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X14112; CAA32301.1; -; Genomic_DNA.
DR   EMBL; DQ889502; ABI63511.1; -; Genomic_DNA.
DR   EMBL; FJ593289; ACM62274.1; -; Genomic_DNA.
DR   PIR; E30089; WMBEY0.
DR   RefSeq; NP_044653.1; -.
DR   GeneID; 2703421; -.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046080; P:dUTP metabolic process; IEA:InterPro.
DR   InterPro; IPR008180; DeoxyUTP_pyroPase_dom.
DR   Pfam; PF00692; dUTPase; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide metabolism; Virus reference strain.
FT   CHAIN         1    371       Deoxyuridine 5'-triphosphate
FT                                nucleotidohydrolase.
FT                                /FTId=PRO_0000182952.
FT   COMPBIAS    152    155       Poly-Pro.
SQ   SEQUENCE   371 AA;  39128 MW;  5FFA2556AD2F7158 CRC64;
     MSQWGSGAIL VQPDSLGRGY DGDWHTAVAT RGGGVVQLNL VNRRAVAFMP KVSGDSGWAV
     GRVSLDLRMA MPADFCAIIH APALASPGHH VILGLIDSGY RGTVMAVVVA PKRTREFAPG
     TLRVDVTFLD ILATPPALTE PISLRQFPQL APPPPTGAGI REDPWLEGAL GAPSVTTALP
     ARRRGRSLVY AGELTPVQTE HGDGVREAIA FLPKREEDAG FDIVVRRPVT VPANGTTVVQ
     PSLRMLHADA GPAACYVLGR SSLNARGLLV VPTRWLPGHV CAFVVYNLTG VPVTLEAGAK
     VAQLLVAGAD ALPWIPPDNF HGTKALRNYP RGVPDSTAEP RNPPLLVFTN EFDAEAPPSE
     RGTGGFGSTG I
//