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P26192 (VP3_ROTPC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. 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 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 length692 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. 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.

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 – 692692Protein VP3
PRO_0000149536

Sequences

Sequence LengthMass (Da)Tools
P26192 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: D679352CF22FE7DE

FASTA69281,378
        10         20         30         40         50         60 
MRVLGLFERG NNLNFADTYI YTWNKQYSYH ENAFLISNQV ATTIIIYLSD TIVNEVDKAF 

        70         80         90        100        110        120 
TLLNSNGIPA LVIRKDHIGI FTSSNFTYDW QHKIVYFHEY TYYKNNEFIV SDEFWLHTNI 

       130        140        150        160        170        180 
HELLPYKLLY YERGMRKLYD GEEYTLYNTA TDDDILYKYI YEKDAIMSGD DYSELYDDKN 

       190        200        210        220        230        240 
FRNFVHFMRL LRMRFAVPFD QLSNRVTRSR AFFKSKIHIG LRNESIPQAL DNINSQWINY 

       250        260        270        280        290        300 
SANGIMISEL KGSGSYSEKR ISEFDIGQFK NYMNFLTLMF YIKNMKKRPS CTIIGAAPGY 

       310        320        330        340        350        360 
WIPSMKRYFT IITYDDKIVD STEHHNRYFS EEDITKVRTN GVYIDVRSDF DKSDWKKRRQ 

       370        380        390        400        410        420 
LVEEETKRWL EISYRLLEGK YVEAVLLKMT AMDIEIPDGY FVHFPTTYRK SEYYLLIDKQ 

       430        440        450        460        470        480 
IIKKQKVKVT KSLMYNAINT IYSDNVFISG KYTLRGKTEG VVALYCLSNT INQKDKVIQY 

       490        500        510        520        530        540 
ANSFSGTCMT VRLNNTYEVN KVINLNNADY TFLPSDFVCP VNTVLTSYRG YAGVFGYAIT 

       550        560        570        580        590        600 
KDLKSDGNNH IYIIPNARDE NNFDTFASHL GLSRYSHSKR FSESATTMSG YLFRDMVSGK 

       610        620        630        640        650        660 
EDMGDTDKAN YASGHVFNAI AHYRFDYTYD IVGWLRLHKN KQFRVKSDIY EEHTSDEVRN 

       670        680        690 
AIEAAYTYYL LDGDRVGKEY AKKIMEIWEA QV 

« Hide

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
M74219 Genomic DNA. Translation: AAA99239.1.
PIRP3XRPC. C40822.

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_ROTPC
AccessionPrimary (citable) accession number: P26192
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 46 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