Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P03195 (DUT_EBVB9) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxyuridine 5'-triphosphate nucleotidohydrolase

Short name=dUTPase
EC=3.6.1.23
Alternative name(s):
dUTP pyrophosphatase
Gene names
Name:DUT
ORF Names:BLLF3
OrganismEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) [Reference proteome]
Taxonomic identifier10377 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length278 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

dUTP + H2O = dUMP + diphosphate.

Cofactor

Magnesium By similarity.

Subunit structure

Monomer. Ref.2

Sequence similarities

Belongs to the dUTPase family.

Caution

BLLF3 is known as BLLF2 in Ref.1.

Ontologies

Keywords
   Biological processNucleotide metabolism
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdUTP metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functiondUTP diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 278278Deoxyuridine 5'-triphosphate nucleotidohydrolase
PRO_0000182962

Regions

Region171 – 1733Substrate binding

Sites

Binding site761Substrate; via amide nitrogen
Binding site841Substrate; via amide nitrogen and carbonyl oxygen

Amino acid modifications

Disulfide bond4 ↔ 246

Secondary structure

....................................................... 278
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03195 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 73C90EFF4B863525

FASTA27830,953
        10         20         30         40         50         60 
MEACPHIRYA FQNDKLLLQQ ASVGRLTLVN KTTILLRPMK TTTVDLGLYA RPPEGHGLML 

        70         80         90        100        110        120 
WGSTSRPVTS HVGIIDPGYT GELRLILQNQ RRYNSTLRPS ELKIHLAAFR YATPQMEEDK 

       130        140        150        160        170        180 
GPINHPQYPG DVGLDVSLPK DLALFPHQTV SVTLTVPPPS IPHHRPTIFG RSGLAMQGIL 

       190        200        210        220        230        240 
VKPCRWRRGG VDVSLTNFSD QTVFLNKYRR FCQLVYLHKH HLTSFYSPHS DAGVLGPRSL 

       250        260        270 
FRWASCTFEE VPSLAMGDSG LSEALEGRQG RGFGSSGQ 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence and expression of the B95-8 Epstein-Barr virus genome."
Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J., Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C., Tuffnell P.S., Barrell B.G.
Nature 310:207-211(1984) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01555 Genomic DNA. Translation: CAA24850.1.
AJ507799 Genomic DNA. Translation: CAD53414.1.
PIRQQBE17. A03758.
RefSeqYP_401664.1. NC_007605.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP03195.
SMRP03195. Positions 3-256.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3783715.

Phylogenomic databases

ProtClustDBPHA3131.

Family and domain databases

InterProIPR008180. dUTP_pyroPase.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03195.

Entry information

Entry nameDUT_EBVB9
AccessionPrimary (citable) accession number: P03195
Secondary accession number(s): Q777F3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 16, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references