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DUT_HCMVA
ID   DUT_HCMVA               Reviewed;         388 AA.
AC   P16824; Q7M6M0;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   29-SEP-2021, entry version 87.
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   Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=10360;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA   Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA   Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA   Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT   "Analysis of the protein-coding content of the sequence of human
RT   cytomegalovirus strain AD169.";
RL   Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN   [2]
RP   GENOME REANNOTATION.
RX   PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA   Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA   McGeoch D.J., Hayward G.S.;
RT   "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT   cytomegalovirus genome.";
RL   J. Gen. Virol. 84:17-28(2003).
RN   [3]
RP   ERRATUM OF PUBMED:12533697.
RA   Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA   McGeoch D.J., Hayward G.S.;
RL   J. Gen. Virol. 84:1053-1053(2003).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004;
RA   Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA   Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA   Shenk T., Smith R.D., Nelson J.A.;
RT   "Identification of proteins in human cytomegalovirus (HCMV) particles: the
RT   HCMV proteome.";
RL   J. Virol. 78:10960-10966(2004).
RN   [5]
RP   ERRATUM OF PUBMED:15452216.
RA   Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA   Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA   Shenk T., Smith R.D., Nelson J.A.;
RL   J. Virol. 78:13395-13395(2004).
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   -!- SUBCELLULAR LOCATION: Virion.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_04031}.
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DR   EMBL; X17403; CAA35387.1; -; Genomic_DNA.
DR   EMBL; BK000394; DAA00168.1; -; Genomic_DNA.
DR   PIR; S09835; S09835.
DR   SMR; P16824; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000008991; Genome.
DR   Proteomes; UP000008992; 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   HAMAP; MF_04031; HSV_DUT; 1.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR006882; Herpes_Orf11.
DR   InterPro; IPR034745; HSV_DUT.
DR   Pfam; PF04797; Herpes_ORF11; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome; Virion.
FT   CHAIN           1..388
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182965"
FT   REGION          77..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   388 AA;  43575 MW;  A747D7D4C1E80DA6 CRC64;
     MLTMLTDRID SQLVLSRLPR SRFQRFWETP TLIMKEESAS SSGSIILAEK SVNMRYCVRF
     ASDSDFQTTF TLPQSTEEKY DKEQHPGEDE ASSPLPSPLK VPYKWMPSSF IVKQCHTQLA
     FYNKHIIWLS RERKVPTSLG VSLYIPEGFF GITFYKCLDA QFVCMPELLE SRLQVPQLDV
     VNLNDTFQSI FPGTIEGDIG VFPCFVPEPW QLMNLPPPNE HRFFSLRTRQ TLVIGPGHTQ
     TVYFDAAYVH APGICALIVG VRQFSQSDLI IRPTIWLPGT AAGVTVVNTS HTTVCISPHT
     TVAKAVFTTH RFTYLPVGSH PLGQMIVPPT PDIGFTHTPE HALLQRTPSP VDDDVDETEE
     DEKSSDAESP VNTNDVIFDV GPKPPRHP
 
 
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