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P26190 (RDRP_ROTPC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-directed RNA polymerase

EC=2.7.7.48
Alternative name(s):
Protein VP1
OrganismRotavirus C (strain Pig/United States/Cowden/1980) (RV-C) [Complete proteome]
Taxonomic identifier10916 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
Virus hostSus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length1082 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Catalytic activity

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Cofactor

Magnesium Potential.

Subunit structure

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.

Subcellular location

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.

Sequence similarities

Belongs to the reoviridae RNA-directed RNA polymerase family.

Contains 1 RdRp catalytic domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10821082RNA-directed RNA polymerase
PRO_0000149527

Regions

Domain498 – 670173RdRp catalytic

Sequences

Sequence LengthMass (Da)Tools
P26190 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 4FE5D43379E89D96

FASTA1,082125,082
        10         20         30         40         50         60 
MDYDTLASKY LKFVYDFEDV TYQNNYFVTD EYKSDLEQYL KSIHDGEKIS QSKIDSMETA 

        70         80         90        100        110        120 
LLTKVPKEKR CLISKLVFAY GKHGNVENKL LKYGTKDALT HAIQKDVKPY ENNIITSEIF 

       130        140        150        160        170        180 
KDESEYTDTY MDPAINTSCQ SNCQAMMFTI SEMKLTDIKN ATRLEKLFTI VAATINKYGM 

       190        200        210        220        230        240 
PRHNIRYRYE WETMKDKPYH LAAWINSSIE MIACVVDHHT YMIARELIVK SFTNRTSLAK 

       250        260        270        280        290        300 
LVSSPMTVLT AMLPIRGTVI TTENLELEYS SKSVNYLISE EMAEDFMKAI EQLRDEGLEI 

       310        320        330        340        350        360 
YQDYYEKWFK SPDPLTFPNI ALIYSFSFHV GYRKQALSDA VYDQITVTYD DNVNMEMYKE 

       370        380        390        400        410        420 
YSERIENEIF TILKDKVVHE DKRLEEYELS ALLSMSSASN GVLREIDFGG QKVRSTKKNM 

       430        440        450        460        470        480 
HVIDDMYHKR YTTDIPPVDE RNPIPLGRRD VPGRRTRAIF ILPYQYFIAQ HSFAEMMLKY 

       490        500        510        520        530        540 
AKREREYSEF YSQANQVLSY GDVTRYLDSN SILCFTDVSQ WDASQHNTRV LRRSIIRAME 

       550        560        570        580        590        600 
RLKQLTHNTN IHKAIDIYIQ SQKNLENSYV LIDKKAIQYG ATASGEKQTK IMNSIANKAL 

       610        620        630        640        650        660 
IQTVLGKLMT DYTFDVKMIR VDGDDNYAIV RFPTAITEKL LSEFTSKLRS YYSEMNVKVK 

       670        680        690        700        710        720 
ALASLTGCEI AKRYIAGGML FFRAGVNILN HEKRNQDSAY DMAATLYANY IVNALRGLTM 

       730        740        750        760        770        780 
SRTFILVKIC QMTSIKITGT LRLFPMKSIL ALNSTFKVFD EVDYVINYPI SELFIQLQRK 

       790        800        810        820        830        840 
LSSIKAKSKI ADNIAKSPQF KSYVEFLNKS LTADENPIVS DGIKLTEKAK LNSYAPIALE 

       850        860        870        880        890        900 
KRRDQFNMMV SFLQNPTTFK SETVVTINDV LYFISGFIKI NSSVALPKEE NNTMPLLPVT 

       910        920        930        940        950        960 
IKRTLNYFGL RTHDYDIKGS SSTMSKIIKQ YSVYTPGIEE LYEVVNKSID SIRGYFASFN 

       970        980        990       1000       1010       1020 
VPKADVDTYI STQMYKHDRF KILQAYIYNL LSVNYGMYQL VDLNSAKFFD HVIHTPMAKT 

      1030       1040       1050       1060       1070       1080 
PTAVFMIDLA LRLKVINHCI EKGEVITVSV HANKTDYLKL WRMLWNVKTM NSPYSKNSMF 


DE 

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References

[1]"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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74216 Genomic DNA. Translation: AAB00801.1.
PIRP1XRPC. A40822.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001795. RNA-dir_pol_luteovirus.
IPR007097. RNA-dir_pol_reovirus.
IPR022071. Rotavirus_VP1.
[Graphical view]
PfamPF02123. RdRP_4. 1 hit.
PF12289. Rotavirus_VP1. 1 hit.
[Graphical view]
PROSITEPS50523. RDRP_DSRNA_REO. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRDRP_ROTPC
AccessionPrimary (citable) accession number: P26190
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families