Sequence-based predictions for the characteristics of the proteins that compose the SARS-CoV-2 virus, which causes COVID-19
Homooligomer. Both monomeric and oligomeric forms interact with RNA. Interacts with protein M. Interacts with NSP3; this interaction serves to tether the genome to the newly translated replicase-transcriptase complex at a very early stage of infection.
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The above plot shows the following predictions for the YP_009724397 SARS-CoV-2 protein:
|DynaMine backbone dynamics||Values above 0.8 indicate rigid conformations, values above 1.0 membrane spanning regions, values below 0.69 flexible regions. Values between 0.80-0.69 are 'context' dependent and capable of being either rigid or flexible.|
|DynaMine sidechain dynamics||Higher values mean more likely rigid. These values are highly dependent on the amino acid type (i.e. a Trp will be rigid, an Asp flexible).|
|DynaMine conformational propensities (sheet, helix, coil)||Higher values indicate higher propensities.|
|EFoldMine earlyFolding propensity||Values above 0.169 indicate residues that are likely to start the protein folding process, based on only local interactions with other amino acids.|
|Disomine disorder||Values above 0.5 indicate that this is likely a disordered residue.|
|Agmata aggregation propensity||These values are divided by a factor of 20 from the original. Peaks indicate residues likely to be involved in beta-sheet aggregation.|
|SeRenDIP protein-protein interactions (PPI)||Values above 0.5 indicate that this residue likely participates in protein-protein interactions.|
|SeRenDIP epitopes (epitope)||Values above 0.5 indicate that this residue is predicted to be recognised as an epitope.|
The above plot shows the range of the predictions for YP_009724397. This is based on an analysis of a multiple sequence alignment for this protein, and shows it 'evolutionary allowed' range. The red line corresponds to the prediction in the top graph, the other lines show the quartile and outlier range of the distribution.
Values of the red line outside of the quartile range therefore indicate rather unusual behavior for this particular protein compared to its homologues.