Q65199 (DUTP_ASFB7) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 65.
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 | African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV) [Reference proteome] | ||||
| Taxonomic identifier | 10498 [NCBI] | ||||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Asfarviridae › Asfivirus › ![]() | ||||
| Virus host | Ornithodoros (relapsing fever ticks) [TaxID: 6937] Sus scrofa (Pig) [TaxID: 9823] |
Protein attributes
| Sequence length | 165 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | The viral dUTPase may play a role in lowering the dUTP concentration in natural infections to minimize misincorporation of deoxyuridine into the viral DNA and ensure the fidelity of genome replication. |
| Catalytic activity | dUTP + H2O = dUMP + diphosphate. |
| Cofactor | Magnesium Probable. |
| Subunit structure | Homotrimer. |
| Subcellular location | |
| Miscellaneous | Expressed early and late in the infection. |
| Sequence similarities | Belongs to the dUTPase family. |
| Biophysicochemical properties | Kinetic parameters: KM=1 µM for dUTP |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide metabolism |
| Cellular component | Host cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | dUTP metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular_component | host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 – 165 | 165 | Deoxyuridine 5'-triphosphate nucleotidohydrolase | PRO_0000373133 | |||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Analysis of the complete nucleotide sequence of African swine fever virus." Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C., Rodriguez J.F., Vinuela E. Virology 208:249-278(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "African swine fever virus dUTPase is a highly specific enzyme required for efficient replication in swine macrophages." Oliveros M., Garcia-Escudero R., Alejo A., Vinuela E., Salas M.L., Salas J. J. Virol. 73:8934-8943(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U18466 Genomic DNA. Translation: AAA65359.1. |
| RefSeq | NP_042823.1. NC_001659.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1VYQ based on UniProtKB Q8II92. |
| ProteinModelPortal | Q65199. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1488894. |
Family and domain databases | |
| InterPro | IPR008180. dUTP_pyroPase. [Graphical view] |
| Pfam | PF00692. dUTPase. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DUTP_ASFB7 | ||||||||
| Accession | Primary (citable) accession number: Q65199 | ||||||||
| 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 |

Clusters with
