P0C9C3 (DUTP_ASFP4) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 8, 2011.
Version 9.
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 |
| ||
| Organism | African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996) (ASFV) [Complete proteome] | ||
| Taxonomic identifier | 561443 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Asfarviridae › Asfivirus › ![]() | ||
| Virus host | Ornithodoros (relapsing fever ticks) [TaxID: 6937] Phacochoerus aethiopicus (Warthog) [TaxID: 85517] Phacochoerus africanus (Warthog) [TaxID: 41426] Potamochoerus larvatus (Bushpig) [TaxID: 273792] Sus scrofa (Pig) [TaxID: 9823] |
Protein attributes
| Sequence length | 165 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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 By similarity. |
| Catalytic activity | dUTP + H2O = dUMP + diphosphate. |
| Cofactor | Magnesium By similarity. |
| Subunit structure | Homotrimer By similarity. |
| Subcellular location | Host cytoplasm By similarity. |
| Miscellaneous | Expressed early and late in the infection By similarity. |
| Sequence similarities | Belongs to the dUTPase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide metabolism |
| Cellular component | Host cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| Technical term | Complete 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_0000373134 | |||
Sequences
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References
| [1] | "African swine fever virus genomes." Kutish G.F., Rock D.L. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY261363 Genomic DNA. No translation available. |
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 | DUTP_ASFP4 | ||||||||
| Accession | Primary (citable) accession number: P0C9C3 | ||||||||
| 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
