P09252 (DPOL_VZVD) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 74.
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: DNA polymerase catalytic subunit EC=2.7.7.7 EC=3.1.26.4 | ||
| Gene names |
| ||
| Organism | Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3) | ||
| Taxonomic identifier | 10338 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Varicellovirus | ||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 1194 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Replicates viral genomic DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein. Additionally, the polymerase contains an intrinsic ribonuclease H (RNase H) activity that specifically degrades RNA/DNA heteroduplexes or duplex DNA substrates in the 5' to 3' direction. Therefore, it can catalyze the excision of the RNA primers that initiate the synthesis of Okazaki fragments at a replication fork during viral DNA replication By similarity. |
| Catalytic activity | Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Endonucleolytic cleavage to 5'-phosphomonoester. |
| Subunit structure | Forms a complex with the ssDNA-binding protein, the DNA polymerase processivity factor, and the alkaline exonuclease. Interacts with the helicase-primase complex composed of the primase, the helicase and the primase-associated factor; this interaction may coordinate leading and lagging strand DNA synthesis at the replication fork By similarity. |
| Subcellular location | Host nucleus By similarity. Note: the protein is present at discrete sites in nuclei, called replication compartments where viral DNA replication occurs By similarity. |
| Sequence similarities | Belongs to the DNA polymerase type-B family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA replication |
| Cellular component | Host nucleus |
| Ligand | DNA-binding |
| Molecular function | DNA-directed DNA polymerase Endonuclease Hydrolase Nuclease Nucleotidyltransferase Transferase |
| Technical term | Complete proteome Multifunctional enzyme Reference proteome |
| Gene Ontology (GO) | |
| Biological process | DNA replication Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-directed DNA polymerase activityInferred from electronic annotation. Source: UniProtKB-KW nucleotide bindingInferred from electronic annotation. Source: InterPro ribonuclease H activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 1194 | 1194 | DNA polymerase catalytic subunit | PRO_0000046525 | |||
Sequences
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References
| [1] | "The complete DNA sequence of varicella-zoster virus." Davison A.J., Scott J.E. J. Gen. Virol. 67:1759-1816(1986) [PubMed: 3018124] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X04370 Genomic DNA. Translation: CAA27911.1. |
| PIR | DJBE28. B27214. |
3D structure databases | |
| ProteinModelPortal | P09252. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| ProtClustDB | CLSP2511265. |
Family and domain databases | |
| InterPro | IPR006172. DNA-dir_DNA_pol_B. IPR017964. DNA-dir_DNA_pol_B_CS. IPR006133. DNA-dir_DNA_pol_B_exonuc. IPR006134. DNA-dir_DNA_pol_B_multi_dom. IPR023211. DNA_pol_palm_dom. IPR012337. RNaseH-like_dom. [Graphical view] |
| Gene3D | G3DSA:3.90.1600.10. DNA_pol_palm_dom. 2 hits. |
| Pfam | PF00136. DNA_pol_B. 1 hit. PF03104. DNA_pol_B_exo1. 1 hit. [Graphical view] |
| PRINTS | PR00106. DNAPOLB. |
| SMART | SM00486. POLBc. 1 hit. [Graphical view] |
| SUPFAM | SSF53098. RNaseH_fold. 1 hit. |
| PROSITE | PS00116. DNA_POLYMERASE_B. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| DrugBank | DB00787. Aciclovir. DB00426. Famciclovir. |
Entry information
| Entry name | DPOL_VZVD | ||||||||
| Accession | Primary (citable) accession number: P09252 | ||||||||
| 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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