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Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

DUT

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

Mg2+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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.6.1.23. 2112.

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 Componenti: 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 – 115Combined sources
Beta strandi16 – 227Combined sources
Beta strandi25 – 328Combined sources
Beta strandi34 – 363Combined sources
Beta strandi40 – 5112Combined sources
Beta strandi56 – 638Combined sources
Beta strandi65 – 706Combined sources
Beta strandi73 – 753Combined sources
Beta strandi83 – 9311Combined sources
Beta strandi95 – 973Combined sources
Beta strandi103 – 11210Combined sources
Beta strandi127 – 1304Combined sources
Beta strandi134 – 1374Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi149 – 1546Combined sources
Beta strandi164 – 1696Combined sources
Helixi172 – 1765Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi190 – 1978Combined sources
Beta strandi199 – 2013Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi210 – 2189Combined sources
Helixi219 – 2213Combined sources
Beta strandi222 – 2243Combined sources
Turni232 – 2354Combined sources
Beta strandi237 – 2426Combined sources
Beta strandi248 – 2503Combined sources
Helixi252 – 2543Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MEACPHIRYA FQNDKLLLQQ ASVGRLTLVN KTTILLRPMK TTTVDLGLYA
60 70 80 90 100
RPPEGHGLML WGSTSRPVTS HVGIIDPGYT GELRLILQNQ RRYNSTLRPS
110 120 130 140 150
ELKIHLAAFR YATPQMEEDK GPINHPQYPG DVGLDVSLPK DLALFPHQTV
160 170 180 190 200
SVTLTVPPPS IPHHRPTIFG RSGLAMQGIL VKPCRWRRGG VDVSLTNFSD
210 220 230 240 250
QTVFLNKYRR FCQLVYLHKH HLTSFYSPHS DAGVLGPRSL FRWASCTFEE
260 270
VPSLAMGDSG LSEALEGRQG RGFGSSGQ
Length:278
Mass (Da):30,953
Last modified:July 21, 1986 - v1
Checksum:i73C90EFF4B863525
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
KEGGivg:3783715.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24850.1.
AJ507799 Genomic DNA. Translation: CAD53414.1.
PIRiA03758. QQBE17.
RefSeqiYP_401664.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

IntActiP03195. 3 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783715.
KEGGivg:3783715.

Enzyme and pathway databases

BRENDAi3.6.1.23. 2112.

Miscellaneous databases

EvolutionaryTraceiP03195.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 1, 2015
This is version 73 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.