DUT_MUHVS
ID DUT_MUHVS Reviewed; 382 AA.
AC Q69151;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 68.
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=UL72;
OS Murid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Muromegalovirus.
OX NCBI_TaxID=10367;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7483291; DOI=10.1007/bf01724298;
RA Messerle M., Rapp M., Lucin P., Koszinowski U.H.;
RT "Characterization of a conserved gene block in the murine cytomegalovirus
RT genome.";
RL Virus Genes 10:73-80(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8971012; DOI=10.1128/jvi.70.12.8833-8849.1996;
RA Rawlinson W.D., Farrell H.E., Barrell B.G.;
RT "Analysis of the complete DNA sequence of murine cytomegalovirus.";
RL J. Virol. 70:8833-8849(1996).
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 -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC route): step 2/2.
CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_04031}.
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DR EMBL; L07319; AAA96663.1; -; Genomic_DNA.
DR EMBL; U68299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; Q69151; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000008774; 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:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046080; P:dUTP metabolic process; IEA:UniProtKB-UniRule.
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; IPR034745; HSV_DUT.
DR Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Reference proteome.
FT CHAIN 1..382
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000182966"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 42885 MW; 0280F70C9B46048D CRC64;
MIKPNIPAPV RPNLPLSSPD SVLPQAMKDP FNIFDDDEPS EDTSSSEQSS RPPPREMMIS
SSCALREQTN SSFLNRFFPE DDESSENGAA LAEINQLLRD GPEAPPREPT PKEARRPEKM
QKIFFQTYGN DFKVEAHGDR LLAQNQRVVR LFERGRILGL GVKMNIPMGY CAVTNCFHPP
GCVCVMDMAG YGPSDIRAQI VNISSGPLEL PPNMLQIHIH MLPMLLPEPW QTINLMAPHQ
GDTYFDLRLR RPLSLPPRAS KNLKFEAGHL CEEDARRCLV IPCRHLATKR VLLDPTVWRP
NSLAVLRVLN ASDEHVDLEA GMAMAKIIFT TPGITPFKPS LTSVMMSFDV PRSDLKLVKG
GRRDYYRAEE RMRSGRDSSN EG