DUTP_ASFM2
ID DUTP_ASFM2 Reviewed; 162 AA.
AC Q65243;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Mal-139; ORFNames=k1R;
OS African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10500;
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].
RX PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA Hammond J.M., Smith G.L.;
RT "Nucleotide sequence of a 55 kbp region from the right end of the genome of
RT a pathogenic African swine fever virus isolate (Malawi LIL20/1).";
RL J. Gen. Virol. 75:1655-1684(1994).
RN [2]
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 -!- 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; X71982; CAA50839.1; -; Genomic_DNA.
DR EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; Q65243; -.
DR Proteomes; UP000000860; 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..162
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000373135"
SQ SEQUENCE 162 AA; 17872 MW; FFD71331454A5737 CRC64;
MATIFFIQPI TEEAEAYYPP SMITNKRKDL GVDVYCCSNL VLQPGLNIIP LHIKVACEHM
GKKCGFKIMA RSSMCTHERL LILANGIGLI DPGYVGELML KIINLGDIPV QIWAKECLVQ
LVAQGDHVPD HINILKRNEI FPLFAPTPRG EGRFGSTGKA GL
