DUTP_ASFB7
ID DUTP_ASFB7 Reviewed; 165 AA.
AC Q65199;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE Short=dUTPase {ECO:0000303|PubMed:10515998};
DE EC=3.6.1.23 {ECO:0000269|PubMed:10515998};
DE AltName: Full=dUTP pyrophosphatase;
GN OrderedLocusNames=Ba71V-131; ORFNames=E165R;
OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10498;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA Rodriguez J.F., Vinuela E.;
RT "Analysis of the complete nucleotide sequence of African swine fever
RT virus.";
RL Virology 208:249-278(1995).
RN [2]
RP SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION,
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=10515998; DOI=10.1128/jvi.73.11.8934-8943.1999;
RA Oliveros M., Garcia-Escudero R., Alejo A., Vinuela E., Salas M.L.,
RA Salas J.;
RT "African swine fever virus dUTPase is a highly specific enzyme required for
RT efficient replication in swine macrophages.";
RL J. Virol. 73:8934-8943(1999).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA Alejo A., Matamoros T., Guerra M., Andres G.;
RT "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL J. Virol. 92:0-0(2018).
RN [4]
RP INDUCTION.
RX PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA Dixon L., Werner F.;
RT "The African Swine Fever Virus Transcriptome.";
RL J. Virol. 94:0-0(2020).
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:0000269|PubMed:10515998}.
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:0000269|PubMed:10515998};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for dUTP {ECO:0000269|PubMed:10515998};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10515998}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:10515998}.
CC Virion {ECO:0000269|PubMed:30185597}. Note=Found in association with
CC viral nucleoid. {ECO:0000269|PubMed:30185597}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:10515998, ECO:0000269|PubMed:32075923}.
CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR EMBL; U18466; AAA65359.1; -; Genomic_DNA.
DR RefSeq; NP_042823.1; NC_001659.2.
DR PDB; 6LIS; X-ray; 2.00 A; A/B/C/D/E/F=1-165.
DR PDB; 6LJ3; X-ray; 2.00 A; A/B/C=1-165.
DR PDB; 6LJO; X-ray; 2.28 A; A=1-165.
DR PDBsum; 6LIS; -.
DR PDBsum; 6LJ3; -.
DR PDBsum; 6LJO; -.
DR SMR; Q65199; -.
DR GeneID; 22220359; -.
DR KEGG; vg:22220359; -.
DR Proteomes; UP000000624; 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 1: Evidence at protein level;
KW 3D-structure; Early protein; Host cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Nucleotide metabolism; Reference proteome; Virion.
FT CHAIN 1..165
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000373133"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:6LIS"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:6LIS"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:6LIS"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6LIS"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6LJ3"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:6LJ3"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:6LJ3"
FT TURN 159..163
FT /evidence="ECO:0007829|PDB:6LJ3"
SQ SEQUENCE 165 AA; 18262 MW; 06633952CDC927E5 CRC64;
MATNFFIQPI TQEAEAYYPP SVITNKRKDL GVDVYCCSDL VLQPGLNIVR LHIKVACEHM
GKKCGFKIMA RSSMCTHERL LILANGIGLI DPGYVGELML KIINLGDTPV QIWAKECLVQ
LVAQGDHVPD HINILKRNQI FPLFAPTPRG EGRFGSTGEA GIMRT
