A0A024CFU0 · A0A024CFU0_9REOV

  • Protein
    Protein VP3
  • Gene
    VP3
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Organism
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Counteracts the host innate immune response thanks to its phosphodiesterase that degrades the 5'-triphosphorylated, 2'-5' linked adenylate oligomers produced by the host cell IFN-inducible 2',5'-oligoadenylate synthetase (OAS). The host RNaseL is therefore not activated.
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 a VP1-VP3 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 do not.

Catalytic activity

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site718For 2'-5'-phosphodiesterase activity
Active site720For 2'-5'-phosphodiesterase activity
Active site797For 2'-5'-phosphodiesterase activity
Active site799For 2'-5'-phosphodiesterase activity

GO annotations

AspectTerm
Cellular Componentviral nucleocapsid
Molecular FunctionGTP binding
Molecular Functionhydrolase activity
Molecular FunctionmRNA 5'-cap (guanine-N7-)-methyltransferase activity
Molecular FunctionmRNA guanylyltransferase activity
Molecular FunctionRNA binding
Biological Processsymbiont-mediated suppression of host innate immune response
Biological Processvirus-mediated perturbation of host defense response

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Protein VP3

Including 3 domains:

  • Recommended name
    2',5'-phosphodiesterase
  • EC number
  • Recommended name
    mRNA guanylyltransferase
  • EC number
  • Recommended name
    mRNA (guanine-N(7))-methyltransferase
  • EC number

Gene names

    • Name
      VP3
    • ORF names
      L312_46672gpVP3
      , L312_46673gpVP3

Organism names

  • Taxonomic identifier
  • Organism
    Rotavirus A
  • Strains
    • RVA/Human-wt/ZAF/MRC-DPRU82/2012/G2P[4]
    • RVA/Pig-wt/ZAF/MRC-DPRU1533/2007/G2P[4]
    • RVA/Human-wt/MWI/BID115/2012/G2P[4]
    • RVA/Human-wt/MWI/BID11D/2012/G2P[4]
    • RVA/Human-wt/MWI/BID11V/2012/G2P[4]
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Duplornaviricota > Resentoviricetes > Reovirales > Sedoreoviridae > Rotavirus

Accessions

  • Primary accession
    A0A024CFU0

Proteomes

Subcellular Location

Virion
Note: Attached inside the inner capsid as a minor component. There are about 11 to 12 copies per virion.

Keywords

  • Cellular component

Interaction

Subunit

Interacts with VP1. Interacts with VP2.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region171-245N7-methyltransferase activity
Region246-4282'-O-methyltransferase activity
Region429-555N7-methyltransferase activity
Region556-692GTase/RTPase activity
Region693-8352'-5'-phosphodiesterase activity

Domain

Contains a bipartite N7-methyltransferase domain, a 2'-O-methyltransferase domain and a GTase/RTPase domain. The C-terminus contains a phosphodiesterase domain that degrades the 5'-triphosphorylated, 2'-5' linked adenylate oligomers produced by the host cell in response to IFN stimulation.

Sequence similarities

Belongs to the rotavirus VP3 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    835
  • Mass (Da)
    97,948
  • Last updated
    2014-07-09 v1
  • Checksum
    6F4FBBBE438C9614
MKVLALRHSVAQVYADTQVYTHDDSKDEYENAFLISNLTTHNILYLNYNVKTLQILNKSGIAAIEIQKIDELFTLIRCNFTYDYIDNVVYLHDYSYYTNNEIRTDQHWITKTNIEDYLLPGWKLTYVGYNGSNTRGHYNFSFRCQNAATDDDAIIEYIYSDELDFQNFILKKIKERMTTSLPIARLSNRVFRDKLFKTLSVNHDKVVNIGPRNESMFTFLDYPSVKQFSNGPYLVKDTIKLKQERWLGKRLSQFDIGQYKNMLNVLTTLYQYYDIYHEKPIVYMVGSAPSHWIYDVKQYSNLKFETWDPLDTPYSNLHHKELFYINDVQKLKDNSILYIDIRTDRGTVDWKEWRKIVERQTIDNLHIAYKYLSIGKAKVCCVKMTAMDLELPISAKLLHHPTTEIRSEFYLVMDIWDSKNIKRFIPKGVLYSYINNTITENVFIQQPFKLKTLKNEYIIALYALSNDLNNREDVVKLINNQKKALMTVRINNTFKDEPKVGFKNIYDWTFLPTDFETNGSIITSYDGCLGIFGLSISLASKPTGNNHLFILSGTDKYFKLDQFANHMSISRRSHQIRFSESATSYSGYIFRDLSNNNFNLIGTNVENSVSGHVYNALIYYRYNYSFDLKRWIYLHSTGKASIEGGKYYEHAPIELIYACRSAREFAKLQDDLTVLRYSNEIENYINKVYSITYADDPNYFIGVKFKNIPYKYNVKVPHLTFGVLNISEQMLPDVITILKRFKNELFGMEITTSYTYMLSDEVYVANISGVLSTYFKIYNAFYKEQITFGQSRMFIPHVTLSFSNEKAVRIDTTRLYIDSIYLRKIKGDTVFDMTG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KJ752207
EMBL· GenBank· DDBJ
AHZ33011.1
EMBL· GenBank· DDBJ
Genomic RNA
KJ752374
EMBL· GenBank· DDBJ
AHZ33193.1
EMBL· GenBank· DDBJ
Genomic RNA
MG181779
EMBL· GenBank· DDBJ
AUF73906.1
EMBL· GenBank· DDBJ
Genomic RNA
MG181790
EMBL· GenBank· DDBJ
AUF73907.1
EMBL· GenBank· DDBJ
Genomic RNA
MG181801
EMBL· GenBank· DDBJ
AUF73908.1
EMBL· GenBank· DDBJ
Genomic RNA
MG181812
EMBL· GenBank· DDBJ
AUF73909.1
EMBL· GenBank· DDBJ
Genomic RNA
MG181900
EMBL· GenBank· DDBJ
AUF73917.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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