P0C8K5 (RPB2_ASFWA) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 8, 2011.
Version 14.
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-directed RNA polymerase subunit 2 EC=2.7.7.6 | ||
| Gene names |
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| Organism | African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV) [Complete proteome] | ||
| Taxonomic identifier | 561444 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Asfarviridae › Asfivirus | ||
| Virus host | Ornithodoros (relapsing fever ticks) [TaxID: 6937] Sus scrofa (Pig) [TaxID: 9823] Phacochoerus africanus (Warthog) [TaxID: 41426] Phacochoerus aethiopicus (Warthog) [TaxID: 85517] Potamochoerus larvatus (Bushpig) [TaxID: 273792] |
Protein attributes
| Sequence length | 1242 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Component of the DNA-dependent RNA polymerase that catalyzes the transcription in the cytoplasm of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Subunit 2 is the second largest component of RNA polymerase. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. DNA-dependent RNA polymerase is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template By similarity. |
| Catalytic activity | Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). |
| Subunit structure | Component of the RNA polymerase that consists of at least 6 subunits Probable. |
| Subcellular location | Host cytoplasm Potential. |
| Miscellaneous | The binding of ribonucleoside triphosphate to the RNA polymerase transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion coordinated by three conserved aspartate residues of the two largest RNA Pol subunits By similarity. |
| Sequence similarities | Belongs to the RNA polymerase beta chain family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription |
| Cellular component | DNA-directed RNA polymerase Host cytoplasm |
| Domain | Zinc-finger |
| Ligand | Metal-binding Zinc |
| Molecular function | Nucleotidyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Cellular component | host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activityInferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW ribonucleoside 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 – 1242 | 1242 | DNA-directed RNA polymerase subunit 2 | PRO_0000355628 | |||||
Regions | |||||||||
| Zinc finger | 1180 – 1201 | 22 | C4-type | ||||||
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 [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY261366 Genomic DNA. No translation available. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR015712. DNA-dir_RNA_pol_su2. IPR007120. DNA-dir_RNA_pol_su2_6. IPR007121. RNA_pol_bsu_CS. IPR007644. RNA_pol_bsu_protrusion. IPR007642. RNA_pol_Rpb2_2. IPR007645. RNA_pol_Rpb2_3. IPR007646. RNA_pol_Rpb2_4. IPR007647. RNA_pol_Rpb2_5. IPR007641. RNA_pol_Rpb2_7. IPR014724. RNA_pol_RPB2_OB-fold. [Graphical view] |
| Gene3D | G3DSA:2.40.270.10. G3DSA:2.40.270.10. 2 hits. G3DSA:2.40.50.150. Ribosomal_L2. 1 hit. |
| PANTHER | PTHR20856. RNA_pol_I_sub2. 1 hit. |
| Pfam | PF04563. RNA_pol_Rpb2_1. 1 hit. PF04561. RNA_pol_Rpb2_2. 1 hit. PF04565. RNA_pol_Rpb2_3. 1 hit. PF04566. RNA_pol_Rpb2_4. 1 hit. PF04567. RNA_pol_Rpb2_5. 1 hit. PF00562. RNA_pol_Rpb2_6. 1 hit. PF04560. RNA_pol_Rpb2_7. 1 hit. [Graphical view] |
| PROSITE | PS01166. RNA_POL_BETA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RPB2_ASFWA | ||||||||
| Accession | Primary (citable) accession number: P0C8K5 | ||||||||
| 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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