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Q9YYS0

- DUT_ADEG8

UniProt

Q9YYS0 - DUT_ADEG8

Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene
N/A
Organism
Avian adenovirus 8 (strain ATCC A-2A) (FAdV-8) (Fowl adenovirus 8)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    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 activityi

    dUTP + H2O = dUMP + diphosphate.

    Cofactori

    Magnesium.By similarity

    Pathwayi

    GO - Molecular functioni

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

    GO - Biological processi

    1. dUMP biosynthetic process Source: UniProtKB-UniPathway
    2. dUTP metabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00610; UER00666.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyuridine 5'-triphosphate nucleotidohydrolase (EC:3.6.1.23)
    Short name:
    dUTPase
    Alternative name(s):
    dUTP pyrophosphatase
    OrganismiAvian adenovirus 8 (strain ATCC A-2A) (FAdV-8) (Fowl adenovirus 8)
    Taxonomic identifieri66295 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeAviadenovirusFowl aviadenovirus E
    Virus hostiGalliformes [TaxID: 8976]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 163163Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_0000182968Add
    BLAST

    Proteomic databases

    PRIDEiQ9YYS0.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9YYS0.
    SMRiQ9YYS0. Positions 18-139.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the dUTPase family.Curated

    Family and domain databases

    Gene3Di2.70.40.10. 1 hit.
    InterProiIPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    IPR008181. dUTPase_1.
    [Graphical view]
    PfamiPF00692. dUTPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51283. SSF51283. 1 hit.
    TIGRFAMsiTIGR00576. dut. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9YYS0-1 [UniParc]FASTAAdd to Basket

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    MSFDSGCPPT PPVKLLFKKH SPFAVTPQRA TSGAAGYDLC SSADVVVPPK    50
    SRSLIPTDLS FQFPRGVYGR IAPRSGLAVK FFIDVGAGVI DSDYRGIVSV 100
    LLFNFSDHNF NVRRGDRIAQ LILERHLTPD LEERSGLDET ARGAAGFGST 150
    GGFDTGVCPS SFS 163
    Length:163
    Mass (Da):17,426
    Last modified:May 1, 1999 - v1
    Checksum:i08DDE78EF8D89419
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF021253 Genomic DNA. Translation: AAC71662.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF021253 Genomic DNA. Translation: AAC71662.1 .

    3D structure databases

    ProteinModelPortali Q9YYS0.
    SMRi Q9YYS0. Positions 18-139.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q9YYS0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00610 ; UER00666 .

    Family and domain databases

    Gene3Di 2.70.40.10. 1 hit.
    InterProi IPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    IPR008181. dUTPase_1.
    [Graphical view ]
    Pfami PF00692. dUTPase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51283. SSF51283. 1 hit.
    TIGRFAMsi TIGR00576. dut. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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].

    Entry informationi

    Entry nameiDUT_ADEG8
    AccessioniPrimary (citable) accession number: Q9YYS0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3