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The copyright holder for this preprint (which was not peer-reviewed) is the .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 Nsp6 of SARS-CoV-2 is equally close to Nsp6s from both Human SARS and Bat CoV, having a sequence identity of 87.24% (Figure 24D ). According to our analysis, mean PPIDs for Nsp6s are calculated to be 1.03%, 1.03%, and 1.03% for SARS-CoV-2, Human SARS CoV, and Bat CoV, respectively. Figures 24A, 24B, and 24C show the corresponding graphs of intrinsic disorder tendency of Nsp6s from SARS-CoV-2, Human SARS CoV, and Bat CoV and demonstrate that these proteins are highly ordered and show low flexibility. As it is a membrane protein, Nsp6 proteins are predicted to have only a single MoRF near the Nterminal region (residues 1-19 in SARS-CoV-2, residues 1-22 in Human SARS, and residues 1-21 in Bat CoV) by the DISOPRED3 server (Table 2, Supplementary Tables 7 and 8) . The role of these protein-binding regions for the induction of autophagy is need to be elucidated. 7 and 8 (Nsp7 and 8) . The ~10 kDa Nsp7 helps in primaseindependent de novo initiation of viral RNA replication by forming a hexadecameric ring-like structure with Nsp8 protein [142, 143] . Both non-structural proteins 7 and 8 contribute 8 molecules to the ring-structured multimeric viral RNA polymerase. Site-directed mutagenesis in Nsp8 revealed a D/ExD/E motif essential for the in vitro catalysis [142] . Figure 25D depicts the 3.1 Ã… resolution electron microscopy-based structure (PDB ID: 6NUR) of the author/funder. All rights reserved. No reuse allowed without permission.