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Q07275 (DUT_EBVA8) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 AG876) (HHV-4) (Human herpesvirus 4) [Reference proteome]
Taxonomic identifier82830 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length278 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Catalytic activity

dUTP + H2O = dUMP + diphosphate.

Cofactor

Magnesium By similarity.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the dUTPase family.

Ontologies

Keywords
   Biological processNucleotide metabolism
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical termComplete 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_0000182963

Regions

Region171 – 1733Substrate binding By similarity

Sites

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

Amino acid modifications

Disulfide bond4 ↔ 246 By similarity

Experimental info

Sequence conflict2451S → T in AAA02786. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q07275 [UniParc].

Last modified May 26, 2009. Version 2.
Checksum: 05073FAB4B863531

FASTA27830,892
        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 
FRWASCAFEE VPGLAMGDSG LSEALEGRQG RGFGSSGQ 

« Hide

References

« Hide 'large scale' references
[1]"The Epstein-Barr virus candidate vaccine antigen gp340/220 is highly conserved between virus types A and B."
Lees J.F., Arrand J.E., Pepper S.V., Stewart J.P., Mackett M., Arrand J.R.
Virology 195:578-586(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome of Epstein-Barr virus type 2 strain AG876."
Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.
Virology 350:164-170(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07923 Genomic DNA. Translation: AAA02786.1. Sequence problems.
DQ279927 Genomic DNA. Translation: ABB89239.1.
RefSeqYP_001129459.1. NC_009334.1.

3D structure databases

ProteinModelPortalQ07275.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5176172.

Family and domain databases

Gene3D2.70.40.10. 3 hits.
InterProIPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMSSF51283. SSF51283. 2 hits.
ProtoNetSearch...

Entry information

Entry nameDUT_EBVA8
AccessionPrimary (citable) accession number: Q07275
Secondary accession number(s): Q1HVG9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 26, 2009
Last modified: June 11, 2014
This is version 49 of the entry and version 2 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