Q80874 · VSR_BSMV

Function

function

Suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs (PubMed:12438624).
Promotes viral cell-to-cell long distance movement by enhancing the ATPase activity of TGB1 (PubMed:12438624, PubMed:32730331).
Enhances RNA helicase activity of replication protein alpha-A (PubMed:28388677).
Suppresses autophagy induced by the host as a defense mechanism against viral infection (PubMed:29848767).

Miscellaneous

The genome of this virus consists of three linear, positive, single-stranded RNAs encapsidated in separate virions designated RNA-alpha, RNA-beta and RNA-gamma. Three proteins (alpha-A, beta-A and gamma-A) are translated directly from these genomic RNAs and the remaining proteins encoded on RNA-beta (beta-B, beta-C and beta-D) and RNA-gamma (gamma-B) are expressed via three subgenomic messenger RNAs.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componenthost cell endoplasmic reticulum
Cellular Componenthost cell plasmodesma
Molecular Functionmetal ion binding
Biological Processsuppression by virus of host autophagy
Biological Processsymbiont-mediated suppression of host RNAi-mediated antiviral immune response
Biological Processvirus-mediated perturbation of host defense response

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Suppressor of RNA silencing
  • Alternative names
    • Gamma-B protein
    • Gammab protein

Organism names

Accessions

  • Primary accession
    Q80874
  • Secondary accessions
    • Q07118

Proteomes

Subcellular Location

Note: Recruited by the replication protein alpha-A to viral replication sites at the host chloroplast membrane.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis7Complete loss of C1 zinc-binding activity; when associated with S-9; S-10; S-19 and S-23.
Mutagenesis9Complete loss of C1 zinc-binding activity; when associated with S-7; S-10; S-19 and S-23.
Mutagenesis10Complete loss of C1 zinc-binding activity; when associated with S-7; S-9; S-19 and S-23.
Mutagenesis19Complete loss of C1 zinc-binding activity; when associated with S-7; S-9; S-10 and S-23.
Mutagenesis23Complete loss of C1 zinc-binding activity; when associated with S-7; S-9; S-10 and S-19.
Mutagenesis25Complete loss of BM zinc-binding activity; when associated with K-26; E-33; K-35 and E-36.
Mutagenesis26Complete loss of BM zinc-binding activity; when associated with E-25; E-33; K-35 and E-36.
Mutagenesis33Complete loss of BM zinc-binding activity; when associated with E-25; K-26; K-35 and E-36.
Mutagenesis35Complete loss of BM zinc-binding activity; when associated with E-25; K-26; E-33 and E-36.
Mutagenesis36Complete loss of BM zinc-binding activity; when associated with E-25; K-26; E-33 and K-35.
Mutagenesis60Complete loss of C2 zinc-binding activity; when associated with S-64; S-71; S-81 and S-85.
Mutagenesis64Complete loss of C2 zinc-binding activity; when associated with S-60; S-71; S-81 and S-85.
Mutagenesis71Complete loss of C2 zinc-binding activity; when associated with S-60; S-64; S-81 and S-85.
Mutagenesis81Complete loss of C2 zinc-binding activity; when associated with S-60; S-64; S-71 and S-85.
Mutagenesis85Complete loss of C2 zinc-binding activity; when associated with S-60; S-64; S-71 and S-81.
Mutagenesis96Reduced viral accumulation.
Mutagenesis96No effect on viral accumulation.

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00002224941-153Suppressor of RNA silencing
Modified residue96Phosphoserine

Post-translational modification

Phosphorylated at Ser-96 by a host PKA-like kinase; the phosphorylation at this site seems to suppress host cell death.
Serine-phosphorylated by host STY46 kinase.

Keywords

PTM databases

Interaction

Subunit

Homooligomer (PubMed:29453938).
Interacts (via C-terminus) with replication protein alpha-A (PubMed:28388677).
Interacts (via N-terminus) with the movement protein TGB1; this interaction targets gammab-TGB1 at the periphery of chloroplasts and plasmodesmata (PubMed:32730331).
Interacts with host autophagy protein ATG7; this interaction disrupts the host ATG7-ATG8 interaction to promote viral infection (PubMed:29848767).
Interacts (via BM region) with host STY46; this interaction inhibits the viral infection (PubMed:33576790).

Family & Domains

Features

Showing features for region, coiled coil.

Type
IDPosition(s)Description
Region1-23C-1
Region1-85Interaction with TGB1
Region19-47Basic motif (BM)
Region60-85C-2
Region86-127Interaction with replication protein alpha-A
Coiled coil92-132

Domain

The three domains C1, BM and C2 are involved in zinc-binding. Zinc-binding of each of the motifs is critical for the biological activity.
The coiled coil domain is probably involved in homooligomerization.

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    153
  • Mass (Da)
    17,160
  • Last updated
    1996-11-01 v1
  • Checksum
    979B4CC3F451EA97
MMATFSCVCCGTSTTSTYCGKRCERKHVYSETRNKRLELYKKYLLEPQKCALNGIVGHSCGMPCSIAEEACDQLPIVSRFCGQKHADLYDSLLKRSEQELLLEFLQKKMQELKLSHIVKMAKLESEVNAIRKSVASSFEDSVGCDDSSSVSKL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict54in Ref. 2; CAA36984
Sequence conflict63in Ref. 2; CAA36984

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M16576
EMBL· GenBank· DDBJ
AAA66601.1
EMBL· GenBank· DDBJ
Genomic RNA
X52774
EMBL· GenBank· DDBJ
CAA36984.1
EMBL· GenBank· DDBJ
Genomic RNA

Genome annotation databases

Similar Proteins

Disclaimer

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