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B1NKT1 (VP3_ROTHP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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 Human/United States/P/1974 G3-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) [Complete proteome]
Taxonomic identifier10957 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length835 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 caution

The sequence ABB18255.1 differs from that shown. Reason: Frameshift at position 139.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 835835Protein VP3
PRO_0000368086

Regions

Compositional bias270 – 2734Poly-Tyr

Experimental info

Sequence conflict2941H → Y in ABB18255. Ref.2

Sequences

Sequence LengthMass (Da)Tools
B1NKT1 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 134FE1363B1F05ED

FASTA83597,856
        10         20         30         40         50         60 
MKVLALRHSV AQVYADTQTY LHDDSKDEYE NAFLISNLTT HNILYLNYSL KTLKILNKSG 

        70         80         90        100        110        120 
IAAVEVQSPD ELFALIRCNF TYDYENNIIY LHDYSYYTNN EIRTDQHWIT KTDIIDYLLP 

       130        140        150        160        170        180 
GWKLTYVGYN GKNTRGHYNF SFSCQNAATD DDIIIEYIYS NELDFQNFLL RKIKERMTTS 

       190        200        210        220        230        240 
LPIARLSNRV FRDKLFPSIV NIYKKVINVG PRNESMFTFL NFPTIKQFSN GAYIVKHTIK 

       250        260        270        280        290        300 
LKQEKWLGKR VSQFDIGQYK NMLNVVTTIY YYYNLYHSKP IIYMLGSAPS YWIHDIKQYS 

       310        320        330        340        350        360 
DFTFETWDPL DTPYSTIHHK ELFFDKDVNK LKDNSVLYID IRTDRKNMDW KEWRKVVEQQ 

       370        380        390        400        410        420 
TVNNLNIAYK YLSTGKAKVC CVKLTAMDLE LPITAKLLHH PTTEVRSEFY AILDAWDIIT 

       430        440        450        460        470        480 
IKRFIPKGVF YAFINNITTE NVFIQPPFKL KASPTDYIVA LYALSNDFNS RQDVINLINK 

       490        500        510        520        530        540 
QKQSLITVRM NNTFKDEPKV NFKNIYDWTF LPTDFELKDS IITSYDGCLG MFGLSISLSS 

       550        560        570        580        590        600 
KPTGNNHLFI INGTDKYYKL DQYANHMGIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL 

       610        620        630        640        650        660 
IGTNVENSVS GHVYNALIYY RYNYAFDLKR WIYLHSIGKV TVEGGRYYEH APIELIYACR 

       670        680        690        700        710        720 
SAKEFAILQD DLTVLRYANE IEGYINKVYS ITYADDPNYF IGIKFNSIPY EYDVKVPHLT 

       730        740        750        760        770        780 
LGVLFISDNM IHDVVTVLKK MKTELFKTEI STSYTYMLSD NIYVANASGV LSTYFKLYNM 

       790        800        810        820        830 
FYRNHITFGQ SRMFIPHITL SFSNKQTVRI ESTRLKINSI YLRKIKGETV FDMSE 

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References

[1]"Full genome-based classification of rotaviruses reveals a common origin between human Wa-Like and porcine rotavirus strains and human DS-1-like and bovine rotavirus strains."
Matthijnssens J., Ciarlet M., Heiman E.M., Arijs I., Delbeke T., McDonald S.M., Palombo E.A., Iturriza-Gomara M., Maes P., Patton J.T., Rahman M., Van Ranst M.
J. Virol. 82:3204-3219(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Genetic characterization of VP3 gene of group A rotaviruses."
Subodh S., Bhan M.K., Ray P.
Virus Genes 33:143-145(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 138-294.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF583039 Genomic RNA. Translation: ABU87848.1.
DQ200932 Genomic RNA. Translation: ABB18255.1. Frameshift.

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_ROTHP
AccessionPrimary (citable) accession number: B1NKT1
Secondary accession number(s): Q1ADF3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: April 16, 2014
This is version 20 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