P26190 (RDRP_ROTPC) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 62. History...
Names and origin
|Protein names||Recommended name:|
RNA-directed RNA polymerase
|Organism||Rotavirus C (strain Pig/United States/Cowden/1980) (RV-C) [Complete proteome]|
|Taxonomic identifier||10916 [NCBI]|
|Taxonomic lineage||Viruses › dsRNA viruses › Reoviridae › Sedoreovirinae › Rotavirus ›|
|Virus host||Sus scrofa (Pig) [TaxID: 9823]|
|Sequence length||1082 AA.|
|Protein existence||Inferred from homology|
General annotation (Comments)
RNA-directed RNA polymerase that is involved in both transcription and genome replication. Together with VP3 capping enzyme, forms an enzyme complex positioned near the channels situated at each of the five-fold vertices of the core. Following infection, the outermost layer of the virus is lost, leaving a double-layered particle (DLP) made up of the core and VP6 shell. VP1 then catalyzes the transcription of fully conservative plus-strand genomic RNAs that are extruded through the DLP's channels into the cytoplasm where they function as mRNAs for translation of viral proteins. One copy of each of the viral (+)RNAs is also recruited during core assembly, together with newly synthesized polymerase complexes and VP2. The polymerase of these novo-formed particles catalyzes the synthesis of complementary minus-strands leading to dsDNA formation. To do so, the polymerase specifically recognizes conserved 3' sequence(s) in plus-strand RNA templates. Once dsRNA synthesis is complete, the polymerase switches to the transcriptional mode, thus providing secondary transcription By similarity.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Interacts with VP3 Potential. Interacts with VP2; this interaction activates VP1. Interacts with NSP5; this interaction is probably necessary for the formation of functional virus factories. Interacts with NSP2; this interaction is weak By similarity.
Virion Potential. Note: Attached inside the inner capsid as a minor component. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging By similarity.
Belongs to the reoviridae RNA-directed RNA polymerase family.
Contains 1 RdRp catalytic domain.
|Biological process||Viral RNA replication|
RNA-directed RNA polymerase
|Technical term||Complete proteome|
|Gene Ontology (GO)|
Inferred from electronic annotation. Source: InterProtranscription, RNA-templated
Inferred from electronic annotation. Source: GOCviral genome replication
Inferred from electronic annotation. Source: InterPro
Inferred from electronic annotation. Source: UniProtKB-SubCell
Inferred from electronic annotation. Source: UniProtKB-KWRNA-directed RNA polymerase activity
Inferred from electronic annotation. Source: UniProtKB-KWnucleotide binding
Inferred from electronic annotation. Source: UniProtKB-KW
|Complete GO annotation...|
Sequence annotation (Features)
|||"Sequences of the four larger proteins of a porcine group C rotavirus and comparison with the equivalent group A rotavirus proteins."|
Bremont M., Juste-Lesage P., Chabanne-Vautherot D., Charpilienne A., Cohen J.
Virology 186:684-692(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
|M74216 Genomic DNA. Translation: AAB00801.1.|
|PIR||P1XRPC. A40822. |
3D structure databases
Protocols and materials databases
Family and domain databases
|InterPro||IPR001795. RNA-dir_pol_luteovirus. |
|Pfam||PF02123. RdRP_4. 1 hit. |
PF12289. Rotavirus_VP1. 1 hit.
|PROSITE||PS50523. RDRP_DSRNA_REO. 1 hit. |
|Accession||Primary (citable) accession number: P26190|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families