Dark Proteome of Newly Emerged SARS-CoV-2 in Comparison with Human and Bat Coronaviruses

Rajanish Giri; Taniya Bhardwaj; Meenakshi Shegane; Bhuvaneshwari R. Gehi; Prateek Kumar; Kundlik Gadhave

The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.13.990598 doi: bioRxiv preprint serves as protein-binding region. We found that the residues from 45-75 is a long MoRF in E proteins of all three viruses as predicted by MoRFchibi_web ( Table 2, Supplementary Table 7 and 8). As aforementioned, these randomly-coiled binding-residues at C-terminus may gain structure while assisting the protein-protein interaction mediated by E protein. One more MoRF region (residues [26] [27] [28] [29] [30] in the transmembrane domain was observed by DISOPRED3 in the E protein of all three viruses. Since these residues are the part of ion channel, we speculate that these residues do specific interactions and may be guiding the specifi functions of ion channel activity. Few RNA binding residues by PPRint and DisoRDPbind and several DNA binding residues by DRNApred are predicted for E protein in all three viruses.