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P03195

- DUT_EBVB9

UniProt

P03195 - DUT_EBVB9

Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

DUT

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Involved in nucleotide metabolism: produces dUMP, the immediate precursor of thymidine nucleotides and decreases the intracellular concentration of dUTP to avoid uracil incorporation into DNA. Induces immune dysregulation that contributes to the pathophysiology of the virus infection.

    Catalytic activityi

    dUTP + H2O = dUMP + diphosphate.

    Cofactori

    Magnesium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei76 – 761Substrate; via amide nitrogen
    Binding sitei84 – 841Substrate; via amide nitrogen and carbonyl oxygen

    GO - Molecular functioni

    1. dUTP diphosphatase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. dUTP metabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyuridine 5'-triphosphate nucleotidohydrolase (EC:3.6.1.23)
    Short name:
    dUTPase
    Alternative name(s):
    dUTP pyrophosphatase
    Gene namesi
    Name:DUT
    ORF Names:BLLF3
    OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
    Taxonomic identifieri10377 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007640: Genome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 278278Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_0000182962Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi4 ↔ 246

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    IntActiP03195. 3 interactions.

    Structurei

    Secondary structure

    1
    278
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 115
    Beta strandi16 – 227
    Beta strandi25 – 328
    Beta strandi34 – 363
    Beta strandi40 – 5112
    Beta strandi56 – 638
    Beta strandi65 – 706
    Beta strandi73 – 753
    Beta strandi83 – 9311
    Beta strandi95 – 973
    Beta strandi103 – 11210
    Beta strandi127 – 1304
    Beta strandi134 – 1374
    Beta strandi142 – 1443
    Beta strandi149 – 1546
    Beta strandi164 – 1696
    Helixi172 – 1765
    Beta strandi179 – 1813
    Beta strandi190 – 1978
    Beta strandi199 – 2013
    Beta strandi203 – 2053
    Beta strandi210 – 2189
    Helixi219 – 2213
    Beta strandi222 – 2243
    Turni232 – 2354
    Beta strandi237 – 2426
    Beta strandi248 – 2503
    Helixi252 – 2543

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BSYX-ray1.50A1-278[»]
    2BT1X-ray2.70A1-278[»]
    2WE0X-ray2.01A1-278[»]
    2WE1X-ray1.80A1-278[»]
    2WE2X-ray1.50A1-278[»]
    2WE3X-ray2.00A1-256[»]
    ProteinModelPortaliP03195.
    SMRiP03195. Positions 3-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03195.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni171 – 1733Substrate binding

    Sequence similaritiesi

    Belongs to the dUTPase family.Curated

    Family and domain databases

    Gene3Di2.70.40.10. 3 hits.
    InterProiIPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    [Graphical view]
    PfamiPF00692. dUTPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51283. SSF51283. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    P03195-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEACPHIRYA FQNDKLLLQQ ASVGRLTLVN KTTILLRPMK TTTVDLGLYA    50
    RPPEGHGLML WGSTSRPVTS HVGIIDPGYT GELRLILQNQ RRYNSTLRPS 100
    ELKIHLAAFR YATPQMEEDK GPINHPQYPG DVGLDVSLPK DLALFPHQTV 150
    SVTLTVPPPS IPHHRPTIFG RSGLAMQGIL VKPCRWRRGG VDVSLTNFSD 200
    QTVFLNKYRR FCQLVYLHKH HLTSFYSPHS DAGVLGPRSL FRWASCTFEE 250
    VPSLAMGDSG LSEALEGRQG RGFGSSGQ 278
    Length:278
    Mass (Da):30,953
    Last modified:July 21, 1986 - v1
    Checksum:i73C90EFF4B863525
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01555 Genomic DNA. Translation: CAA24850.1.
    AJ507799 Genomic DNA. Translation: CAD53414.1.
    PIRiA03758. QQBE17.
    RefSeqiYP_401664.1. NC_007605.1.

    Genome annotation databases

    GeneIDi3783715.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01555 Genomic DNA. Translation: CAA24850.1 .
    AJ507799 Genomic DNA. Translation: CAD53414.1 .
    PIRi A03758. QQBE17.
    RefSeqi YP_401664.1. NC_007605.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BSY X-ray 1.50 A 1-278 [» ]
    2BT1 X-ray 2.70 A 1-278 [» ]
    2WE0 X-ray 2.01 A 1-278 [» ]
    2WE1 X-ray 1.80 A 1-278 [» ]
    2WE2 X-ray 1.50 A 1-278 [» ]
    2WE3 X-ray 2.00 A 1-256 [» ]
    ProteinModelPortali P03195.
    SMRi P03195. Positions 3-256.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P03195. 3 interactions.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3783715.

    Miscellaneous databases

    EvolutionaryTracei P03195.

    Family and domain databases

    Gene3Di 2.70.40.10. 3 hits.
    InterProi IPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    [Graphical view ]
    Pfami PF00692. dUTPase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51283. SSF51283. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases."
      Tarbouriech N., Buisson M., Seigneurin J.M., Cusack S., Burmeister W.P.
      Structure 13:1299-1310(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 4-116 AND 121-256, SUBUNIT.

    Entry informationi

    Entry nameiDUT_EBVB9
    AccessioniPrimary (citable) accession number: P03195
    Secondary accession number(s): Q777F3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Caution

    BLLF3 is known as BLLF2 in PubMed:6087149.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3