ID   DUT_ICHVA               Reviewed;         188 AA.
AC   P28893;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
DE   AltName: Full=dUTP pyrophosphatase;
GN   Name=49;
OS   Ictalurid herpesvirus 1 (strain Auburn) (IcHV-1) (Channel catfish
OS   herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Alloherpesviridae; Ictalurivirus.
OX   NCBI_TaxID=766178;
OH   NCBI_TaxID=7996; Ictaluridae (bullhead catfishes).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1727613; DOI=10.1016/0042-6822(92)90056-u;
RA   Davison A.J.;
RT   "Channel catfish virus: a new type of herpesvirus.";
RL   Virology 186:9-14(1992).
CC   -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it produces
CC       dUMP, the immediate precursor of thymidine nucleotides and it decreases
CC       the intracellular concentration of dUTP so that uracil cannot be
CC       incorporated into DNA.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR   EMBL; M75136; AAA88152.1; -; Genomic_DNA.
DR   PIR; E36791; WZBEI1.
DR   RefSeq; NP_041140.1; NC_001493.2.
DR   SMR; P28893; -.
DR   GeneID; 1488441; -.
DR   KEGG; vg:1488441; -.
DR   Proteomes; UP000007643; Genome.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:InterPro.
DR   GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   InterPro; IPR008181; dUTPase.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   PANTHER; PTHR11241; PTHR11241; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
DR   TIGRFAMs; TIGR00576; dut; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..188
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182955"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   188 AA;  20129 MW;  F9E924FA21366EF2 CRC64;
     MGEMTSGVDG HGSTKRTTSE AQKMDFNTDR GSAIPTGDDR GYQCGVIGDS VRFSVFTGYD
     AADVSIPKIS SPGSAGFDLS VLEDREFIRG CHYRLPTGLA IAVPRGYVGI ITPRSSQAKN
     FVSTGIIDSD FRGHIHIMVS AIADFSVKKN QRIAQLVVTP CLTQSEVVPY ETLERTRRGT
     GGFGSSGQ