ID   DUTP_ASFP4              Reviewed;         165 AA.
AC   P0C9C3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase {ECO:0000250|UniProtKB:Q65199};
DE            EC=3.6.1.23 {ECO:0000250|UniProtKB:Q65199};
DE   AltName: Full=dUTP pyrophosphatase;
GN   OrderedLocusNames=Pret-143;
OS   African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561443;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH   NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH   NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kutish G.F., Rock D.L.;
RT   "African swine fever virus genomes.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The viral dUTPase may play a role in lowering the dUTP
CC       concentration in natural infections to minimize misincorporation of
CC       deoxyuridine into the viral DNA and ensure the fidelity of genome
CC       replication. {ECO:0000250|UniProtKB:Q65199}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q65199};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q65199}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:Q65199}.
CC       Virion {ECO:0000250|UniProtKB:Q65199}. Note=Found in association with
CC       viral nucleoid. {ECO:0000250|UniProtKB:Q65199}.
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR   EMBL; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0C9C3; -.
DR   Proteomes; UP000000859; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
PE   3: Inferred from homology;
KW   Early protein; Host cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide metabolism; Virion.
FT   CHAIN           1..165
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000373134"
SQ   SEQUENCE   165 AA;  18289 MW;  7BAAB5C34D8D26F0 CRC64;
     MATNFFIQPI TEEAEAYYPP SVITNKRKDL GVDVYCCSDL VLQPGLNIVR LHIKVACEHM
     GKKCGFKIMA RSSMCTYERL LILANGIGLI DPGYVGELML KIINLGDTPV QIWAKECLVQ
     LVAQGDHVPD HINILKRNQI FPLFAPTPRG EGRFGSTGEA GIMRT