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The copyright holder for this preprint (which was not peer-reviewed) is the .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 intrinsic disorder content of 9.28%, comparatively lower than that of the Human SARS ORF9b protein. MoRFs lies in the N-terminal region of ORF9b proteins ( Table 2, Supplementary Table 7 and 8). In the absence of other viral proteins, its first 41 residues have been demonstrated to induce membranous structures similar to DMVs [106] . The available crystal structure also has the missing electron density in the N-terminal region suggests that these flexible amino acids are likely to interact with host lipids. The first 3-29 residues of SARS-CoV2 are identified as disorder-based protein binding region that may have role in its interaction with host lipids and formation of DMVs. Supplementary Tables 9, 10, and 11 represents nucleotide-binding residues for ORF9b of SARS-CoV-2, Human SARS, and Bat CoV.