Q3KST7 (DUT_EBVG) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 8, 2011.
Version 29.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Deoxyuridine 5'-triphosphate nucleotidohydrolase Short name=dUTPase EC=3.6.1.23 Alternative name(s): dUTP pyrophosphatase | ||||
| Gene names |
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| Organism | Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4) [Complete proteome] | ||||
| Taxonomic identifier | 10376 [NCBI] | ||||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Lymphocryptovirus | ||||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 278 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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 process | Nucleotide metabolism |
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | dUTP metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular_function | dUTP diphosphatase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 278 | 278 | Deoxyuridine 5'-triphosphate nucleotidohydrolase | PRO_0000375927 | |||||||
Regions | |||||||||||
| Region | 171 – 173 | 3 | Substrate binding By similarity | ||||||||
Sites | |||||||||||
| Binding site | 76 | 1 | Substrate; via amide nitrogen By similarity | ||||||||
| Binding site | 84 | 1 | Substrate; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 4 ↔ 246 | By similarity | |||||||||
Sequences
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References
| [1] | "Genomic sequence analysis of Epstein-Barr virus strain GD1 from a nasopharyngeal carcinoma patient." Zeng M.-S., Li D.-J., Liu Q.-L., Song L.-B., Li M.-Z., Zhang R.-H., Yu X.-J., Wang H.-M., Ernberg I., Zeng Y.-X. J. Virol. 79:15323-15330(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY961628 Genomic DNA. Translation: AAY41113.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR008180. dUTP_pyroPase. [Graphical view] |
| Pfam | PF00692. dUTPase. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DUT_EBVG | ||||||||
| Accession | Primary (citable) accession number: Q3KST7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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