DUT_HHV8P
ID DUT_HHV8P Reviewed; 295 AA.
AC Q2HR78;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_04031};
DE Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_04031};
DE EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_04031};
DE AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_04031};
GN Name=DUT {ECO:0000255|HAMAP-Rule:MF_04031}; OrderedLocusNames=ORF54;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
CC -!- FUNCTION: Involved in nucleotide metabolism: produces dUMP, the
CC immediate precursor of thymidine nucleotides and decreases the
CC intracellular concentration of dUTP to avoid uracil incorporation into
CC viral DNA. {ECO:0000255|HAMAP-Rule:MF_04031}.
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:0000255|HAMAP-Rule:MF_04031};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04031};
CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_04031}.
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DR EMBL; AF148805; ABD28905.1; -; Genomic_DNA.
DR RefSeq; YP_001129407.1; NC_009333.1.
DR SMR; Q2HR78; -.
DR PRIDE; Q2HR78; -.
DR DNASU; 4961459; -.
DR GeneID; 4961459; -.
DR KEGG; vg:4961459; -.
DR Proteomes; UP000000942; Genome.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046080; P:dUTP metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07557; trimeric_dUTPase; 2.
DR Gene3D; 2.70.40.10; -; 2.
DR HAMAP; MF_04031; HSV_DUT; 1.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR InterPro; IPR034745; HSV_DUT.
DR Pfam; PF00692; dUTPase; 2.
DR SUPFAM; SSF51283; SSF51283; 2.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Reference proteome.
FT CHAIN 1..295
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000423878"
FT REGION 260..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..180
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
SQ SEQUENCE 295 AA; 33188 MW; 18A8DE282EE367AF CRC64;
MQSDSAPLPR VEYVFETSKF RMTSRANEAR LRLTNECPIL VRPHEPFIMP TGIHFTRTPS
CAFILTGETD KDVFCHTGLI DGGYRGEIQV ILLNKRKYPV TLYRGELNIC LSAFNYVLPP
LRDVSFLTPP MYANDAGFDV MVMHSMVIPP TTDQPFMIYL GVETPGPPEP HVALALGRSG
LASRGIVIDV SEWGPRGLQL KFYNYSGQPW LAQPGSRICQ IVFVERRHIL KGFKKCLRHR
KLAPGVRFRE ARVHFREDTN SVRKHTHEDN PVHEPNVATA SADIRGTKGL GSSGF