DUTP_ASFK5
ID DUTP_ASFK5 Reviewed; 165 AA.
AC P0C9C5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 23-FEB-2022, entry version 39.
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=Ken-143;
OS African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561445;
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 [LARGE SCALE 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 Evidence={ECO:0000250|UniProtKB:Q65199};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C9C5; -.
DR Proteomes; UP000000861; 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 Host cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Virion.
FT CHAIN 1..165
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000373137"
SQ SEQUENCE 165 AA; 18348 MW; 415166F0DDB5FD22 CRC64;
MATNFFIQPI TEEAETYYPP SVITNKRQDL GVDVYCCSDL VLQPGLNIVR LHIKVACEHR
GKKCGFKIMA RSSMCTHERL LILANSIGLI DPGYVGELML KIINLGDTPV QIWAKECLVQ
LVAQGDHVPD HINILKRNQI FPLFAPTPRG EGRFGSTGEA GIMRT