Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6WNV6 (VP3_ROTCC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 25. 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:
Protein VP3

Including the following 2 domains:

  1. mRNA guanylyltransferase
    EC=2.7.7.50
  2. mRNA (guanine-N(7)-)-methyltransferase
    EC=2.1.1.56
OrganismRotavirus A (strain Chicken/Ireland/Ch2/1979 G7-Px[x]-Ix-Rx-Cx-M4-Ax-Nx-Tx-Ex-Hx) (RV-A) (Rotavirus A (strain Ch-2))
Taxonomic identifier31589 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostGallus gallus (Chicken) [TaxID: 9031]

Protein attributes

Sequence length829 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Multifunctional enzyme involved in mRNA capping. Catalyzes the formation of the 5' cap structure on the viral plus-strand transcripts. Specifically binds to GTP and displays guanylyltransferase and methyltransferase activities. Has affinity for ssRNA but not for dsRNA. Capping activity is non-specific and caps RNAs that initiate with either a G or an A residue. Together with VP1 polymerase, 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 capped by VP3 and extruded through the DLP's channels into the cytoplasm where they function as mRNAs for translation of viral proteins. DLPs probably have an RNA triphosphatase activity as well, whereas open cores don't By similarity.

Catalytic activity

GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.

S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.

Subunit structure

Interacts with VP1 Potential. Interacts with VP2 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 Potential.

Sequence similarities

Belongs to the rotavirus VP3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 829829Protein VP3
PRO_0000368072

Regions

Compositional bias267 – 2704Poly-Tyr

Sequences

Sequence LengthMass (Da)Tools
Q6WNV6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: A45EE6B3F66379E1

FASTA82997,789
        10         20         30         40         50         60 
MKVIALRRDL VSSYADTQVY EHDVDKDYYE NAYLISNITA HNVLYVDYSI QVIEILNKSG 

        70         80         90        100        110        120 
IASLIAINKD KLEILIKSNY TYDYYKNIVY LHDYSYYNLN ELRTDQYWLT TTNIEEYILP 

       130        140        150        160        170        180 
GWKLTYVGQL GIKTRGHYTY SFICQNTATD DDIIYDYIYS NEVDFLPFLL QALNKRLTTA 

       190        200        210        220        230        240 
VNFHRLSNRI FREYLYSKVP KDTINIGPRN ESMFTLLRYP YITNYAANEF KVSDLIRLTQ 

       250        260        270        280        290        300 
EKWIGAENSQ FDIGQFKNMC NVLSTIYYYY NKYHAYPRIY MLGSAPSYWL YDLLQVYNFD 

       310        320        330        340        350        360 
IETWDPLDTP FSKRHHKAMF AISDTEKLSD NSILYIDIRS DRNGADWREW RQRVEDETKI 

       370        380        390        400        410        420 
NLEIMRKYLQ RGKTRICCCK ITAMDIELPA TSILLHFPTT KIQSECYVIC TQEMLQDKKR 

       430        440        450        460        470        480 
FVPKGAFYSF INNTKTDNVF VSPVYKVKPT NKFVVALYSL SNENNDRDKV IDFTQKQKRG 

       490        500        510        520        530        540 
IITLRMNNTF NYEYRLQFKS TYDYLYLPSE VSREGTIVTS YDGYIAMHNL SLSLESKATG 

       550        560        570        580        590        600 
NNHLFISFSD ANYGQIDSYC THMGISRRSH SVRFSEAATT LSGYMFRDIT NGKFNLINTN 

       610        620        630        640        650        660 
VENAVSGHVY NALVYFRYNY RFDLLRWINL HAKDEVMIQG GRYYEHAPPE LLYACQSALV 

       670        680        690        700        710        720 
FAKLQNDLTL IEYVNSVNRY ILNKYNLKYA DDPNYYIHID FVDLPFKYTV PDPHLTGGLL 

       730        740        750        760        770        780 
FLNDFDIQNT ITILRSVKED LIALNLLTQY TYMLTDSIYV ANVDGYLQFY YKLYMKFYRK 

       790        800        810        820 
QIVFGQSRMF LPHITLSKEK KKPVRIDATK LVIKSIKLRK IKSDVEYCI 

« Hide

References

[1]"Sequence analysis of the guanylyltransferase (VP3) of group A rotaviruses."
Cook J.P., McCrae M.A.
J. Gen. Virol. 85:929-932(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY277923 Genomic RNA. Translation: AAQ21050.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR011181. VP3_Rotav.
[Graphical view]
PfamPF06929. Rotavirus_VP3. 1 hit.
[Graphical view]
PIRSFPIRSF004015. LigT_rotavirus. 1 hit.
PROSITEPS51589. SAM_MT56_VP3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVP3_ROTCC
AccessionPrimary (citable) accession number: Q6WNV6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 25 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