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Q9YYS0 (DUT_ADEG8) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 54. 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
OrganismAvian adenovirus 8 (strain ATCC A-2A) (FAdV-8) (Fowl adenovirus 8)
Taxonomic identifier66295 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageAdenoviridaeAviadenovirusFowl adenovirus E
Virus hostGalliformes [TaxID: 8976]

Protein attributes

Sequence length163 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA By similarity.

Catalytic activity

dUTP + H2O = dUMP + diphosphate.

Cofactor

Magnesium By similarity.

Pathway

Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.

Sequence similarities

Belongs to the dUTPase family.

Ontologies

Keywords
   Biological processNucleotide metabolism
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological_processdUMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

dUTP 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 – 163163Deoxyuridine 5'-triphosphate nucleotidohydrolase
PRO_0000182968

Sequences

Sequence LengthMass (Da)Tools
Q9YYS0 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 08DDE78EF8D89419

FASTA16317,426
        10         20         30         40         50         60 
MSFDSGCPPT PPVKLLFKKH SPFAVTPQRA TSGAAGYDLC SSADVVVPPK SRSLIPTDLS 

        70         80         90        100        110        120 
FQFPRGVYGR IAPRSGLAVK FFIDVGAGVI DSDYRGIVSV LLFNFSDHNF NVRRGDRIAQ 

       130        140        150        160 
LILERHLTPD LEERSGLDET ARGAAGFGST GGFDTGVCPS SFS 

« Hide

References

[1]"Sequence and transcriptional analysis of terminal regions of the fowl adenovirus type 8 genome."
Cao J.X., Krell P.J., Nagy E.
J. Gen. Virol. 79:2507-2516(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF021253 Genomic DNA. Translation: AAC71662.1.

3D structure databases

ProteinModelPortalQ9YYS0.
SMRQ9YYS0. Positions 18-139.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9YYS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00610; UER00666.

Family and domain databases

InterProIPR008180. dUTP_pyroPase.
IPR008181. dUTP_pyroPase_sf.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00576. dut. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDUT_ADEG8
AccessionPrimary (citable) accession number: Q9YYS0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: October 16, 2013
This is version 54 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

PATHWAY comments

Index of metabolic and biosynthesis pathways