SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q65526

- VP3_ROTBS

UniProt

Q65526 - VP3_ROTBS

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Protein VP3
Gene
N/A
Organism
Rotavirus C (isolate Cow/Japan/Shintoku/1991) (RV-C)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

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.

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. RNA binding Source: UniProtKB-KW
  3. mRNA (guanine-N7-)-methyltransferase activity Source: UniProtKB-EC
  4. mRNA guanylyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. viral process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

mRNA capping, mRNA processing

Keywords - Ligandi

GTP-binding, Nucleotide-binding, RNA-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Protein VP3
Including the following 2 domains:
mRNA guanylyltransferase (EC:2.7.7.50)
mRNA (guanine-N(7)-)-methyltransferase (EC:2.1.1.56)
OrganismiRotavirus C (isolate Cow/Japan/Shintoku/1991) (RV-C)
Taxonomic identifieri33723 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]

Subcellular locationi

Virion Reviewed prediction
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 Reviewed prediction.

GO - Cellular componenti

  1. viral nucleocapsid Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 695695Protein VP3
PRO_0000369871Add
BLAST

Interactioni

Subunit structurei

Interacts with VP1 Reviewed prediction. Interacts with VP2.

Family & Domainsi

Sequence similaritiesi

Belongs to the rotavirus VP3 family.

Family and domain databases

InterProiIPR011181. VP3_Rotav.
[Graphical view]
PfamiPF06929. Rotavirus_VP3. 1 hit.
[Graphical view]
PIRSFiPIRSF004015. LigT_rotavirus. 1 hit.
PROSITEiPS51589. SAM_MT56_VP3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q65526-1 [UniParc]FASTAAdd to Basket

« Hide

MRVLGLFERG NNLNFADTYV YTWNKQYSFH ENAFLISNQV ATTIIIYLDK    50
EIVNQVNEAF NLLNSNGIPA LIIKSDHIGI FTSSNFTYDW QNKIIYFHEY 100
TYYKNNEFIV SDEFWLNTSI QDLLPYKVLF FERGLRKLYE GEEYILYNTA 150
TDDDIIYKYI YEKDVIMSGN DYSKLYDTKS FKNFVHFMRL LRMRFAVPFD 200
QLSNRVTRSR AFAKSKIHIG LRNESIPQAL DNIHHYWINY SANGMRVSEL 250
KGSGSYSEKK ISEFDIGQFK NYMNFLTLMF YIKNMKKKPS CTIIGAAPGY 300
WIPSMKKYFN IVTYDDKHVD STEHYNRYFT DDDIASVKTN GVYIDVRSDF 350
KNYDWKKRRQ LVEEETMRWL SITYKLLENR YVEAVLLKMT AMDIEIPDGY 400
FVHFPTTYRK SEYYLLVDKQ TVKRPKIKIT KSLAYGAINT IFSDNVFISG 450
KYSLKGKTEG VLALYCLSNT INPKEKVVQY ANSFSGTCMT VRLNNTYILN 500
KIIDFKTNAD YTFLPSDFQC SIKTVLTSYR GYAGVFGYAI TKDLKSDGNN 550
HIYIIPNARD DDNFDTFASH LGLSRYSHSK RFSESATTMS GYLFRDMVSG 600
KENMEDTDTE NLASGHVFNA IAHYRFDYTY DIVGWLKLHK MRKFRVKSNI 650
YGEHTDDEIR NAIEAAYVYY LLDGDEVGKE YAKRIMEIWD VQTWG 695
Length:695
Mass (Da):81,517
Last modified:November 1, 1996 - v1
Checksum:i1EF9F1ECFFAD3328
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U26552 Genomic DNA. Translation: AAB01673.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U26552 Genomic DNA. Translation: AAB01673.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR011181. VP3_Rotav.
[Graphical view ]
Pfami PF06929. Rotavirus_VP3. 1 hit.
[Graphical view ]
PIRSFi PIRSF004015. LigT_rotavirus. 1 hit.
PROSITEi PS51589. SAM_MT56_VP3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequence analysis of VP3 and VP4 genes of a bovine group C rotavirus: molecular evidence for a new P type."
    Jiang B., Gentsch J.R., Tsunemitsu H., Saif L.J., Glass R.I.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiVP3_ROTBS
AccessioniPrimary (citable) accession number: Q65526
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi