Reviewed,
UniProtKB/Swiss-Prot P04293 (DPOL_HHV11)
Last modified
November 3, 2009.
Version 67.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: DNA polymerase catalytic subunit EC=2.7.7.7 EC=3.1.26.4 | ||
| Gene names |
| ||
| Organism | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) | ||
| Taxonomic identifier | 10299 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus | ||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 1235 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
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. Ref.5 |
| 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 UL29, the DNA polymerase processivity factor, and the alkaline exonuclease. Interacts with the putative helicase-primase complex subunit UL8; this interaction may coordinate leading and lagging strand DNA synthesis at the replication fork By similarity. |
| Subcellular location | Host nucleus Potential. 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. |
| Sequence caution | The sequence CAA26941.1 differs from that shown. Reason: Frameshift at position 114. |
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 Virus reference strain |
| 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 nucleusInferred from electronic annotation. Source: UniProtKB-KW |
| 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 |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1235 | 1235 | DNA polymerase catalytic subunit | PRO_0000046511 | |||||
Regions | |||||||||
| Compositional bias | 4 – 7 | 4 | Poly-Gly | ||||||
| Compositional bias | 659 – 688 | 30 | Glu-rich | ||||||
| Compositional bias | 986 – 991 | 6 | Poly-Ala | ||||||
| Compositional bias | 1101 – 1128 | 28 | Pro-rich | ||||||
Natural variations | |||||||||
| Natural variant | 33 | 1 | S → G in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 102 | 1 | A → T in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 330 | 1 | A → R in strain: Nonneuroinvasive mutant HF10 and 17 syn+. | ||||||
| Natural variant | 646 | 1 | A → T in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 802 | 1 | L → F in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 905 | 1 | V → M in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 1203 | 1 | A → T in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 1208 – 1209 | 2 | TA → AT in strain: Nonneuroinvasive mutant HF10. | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1." McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P. J. Gen. Virol. 69:1531-1574(1988) [PubMed: 2839594] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "DNA sequence of the region in the genome of herpes simplex virus type 1 containing the genes for DNA polymerase and the major DNA binding protein." Quinn J.P., McGeoch D.J. Nucleic Acids Res. 13:8143-8163(1985) [PubMed: 2999714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Determination and analysis of the DNA sequence of highly attenuated herpes simplex virus type 1 mutant HF10, a potential oncolytic virus." Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y. Microbes Infect. 9:142-149(2007) [PubMed: 17218138] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nonneuroinvasive mutant HF10. |
| [4] | "Herpes simplex virus type 1 bacterial artificial chromosome." Cunningham C., Davison A.J. Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 17 syn+. |
| [5] | "Herpes simplex-1 DNA polymerase. Identification of an intrinsic 5'----3' exonuclease with ribonuclease H activity." Crute J.J., Lehman I.R. J. Biol. Chem. 264:19266-19270(1989) [PubMed: 2553735] [Abstract] Cited for: FUNCTION. |
| [6] | "The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex." Marsden H.S., McLean G.W., Barnard E.C., Francis G.J., MacEachran K., Murphy M., McVey G., Cross A., Abbotts A.P., Stow N.D. J. Virol. 71:6390-6397(1997) [PubMed: 9261356] [Abstract] Cited for: INTERACTION WITH UL8. |
Cross-references
Sequence databases | |
|---|---|
| X14112 Genomic DNA. Translation: CAA32323.1. X03181 Genomic DNA. Translation: CAA26941.1. Frameshift. DQ889502 Genomic DNA. Translation: ABI63492.1. FJ593289 Genomic DNA. Translation: ACM62253.1. | |
| PIR | DJBEV1. A00715. DJBEH7. C30085. |
| RefSeq | NP_044632.1. |
3D structure databases | |
| SMR | P04293. Positions 60-640, 700-1110. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2703462. |
Family and domain databases | |
| InterPro | IPR006172. DNA-dir_DNA_pol_B. IPR006134. DNA-dir_DNA_pol_B_cons-reg. IPR017966. DNA-dir_DNA_pol_B_cons_reg2. IPR017964. DNA-dir_DNA_pol_B_CS. IPR006133. DNA-dir_DNA_pol_B_exonuc. [Graphical view] |
| PANTHER | PTHR10322. DNA_pol_B. 1 hit. |
| Pfam | PF00136. DNA_pol_B. 1 hit. PF03104. DNA_pol_B_exo. 1 hit. [Graphical view] |
| PRINTS | PR00106. DNAPOLB. |
| SMART | SM00486. POLBc. 1 hit. [Graphical view] |
| PROSITE | PS00116. DNA_POLYMERASE_B. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| DrugBank | DB00787. Aciclovir. DB00426. Famciclovir. DB00529. Foscarnet. DB01004. Ganciclovir. DB00249. Idoxuridine. DB00299. Penciclovir. DB00432. Trifluridine. DB00577. Valaciclovir. DB01610. Valganciclovir. |
Entry information
| Entry name | DPOL_HHV11 | ||||||||
| Accession | Primary (citable) accession number: P04293 Secondary accession number(s): B9VQF8, Q09IA3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||

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