A2T3S0 (RDRP_ROTSH) Reviewed, UniProtKB/Swiss-Prot
Last modified April 16, 2014. Version 24. History...
Names and origin
|Protein names||Recommended name:|
RNA-directed RNA polymerase
|Organism||Rotavirus A (isolate Monkey/South Africa/SA11-H96/1958 G3-P5B-I2-R2-C5-M5-A5-N5-T5-E2-H5) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58)) [Reference proteome]|
|Taxonomic identifier||450149 [NCBI]|
|Taxonomic lineage||Viruses › dsRNA viruses › Reoviridae › Sedoreovirinae › Rotavirus › Rotavirus A ›|
|Virus host||Cercopithecus pygerythrus (Vervet monkey) [TaxID: 60710]|
|Sequence length||1088 AA.|
|Protein existence||Evidence at protein level|
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 dsRNA formation. To do so, the polymerase specifically recognizes and binds 4 bases 5'-UGUG-3' in the conserved 3'-sequence of plus-strand RNA templates. VP2 presumably activates the autoinhibited VP1-RNA complex to coordinate packaging and genome replication. 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. Ref.2
Virion Potential. Note: Attached inside the inner capsid as a minor component By similarity. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. Ref.2
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: InterProviral 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)
|||"Genome heterogeneity of SA11 rotavirus due to reassortment with 'O' agent."|
Small C., Barro M., Brown T.L., Patton J.T.
Virology 359:415-424(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2."|
Arnoldi F., Campagna M., Eichwald C., Desselberger U., Burrone O.R.
J. Virol. 81:2128-2137(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NSP2, INTERACTION WITH NSP5, SUBCELLULAR LOCATION.
|DQ838640 Genomic RNA. Translation: ABG75819.1.|
|RefSeq||YP_002302227.1. NC_011507.2. |
3D structure databases
Protocols and materials databases
Genome annotation 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: A2T3S0|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families