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The copyright holder for this preprint (which was not peer-reviewed) is the .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 and a C-terminal domain (192-345 residues) consisting of two anti-parallel three -strand sheets on each side of a central α-helical core [156] . The Nsp15 is found to be quite conserved across human SARS and bat CoVs. SARS-CoV-2 Nsp15 shares an 88.73% sequence identity with Nsp15 of Human SARS and 88.15% with Nsp15 of Bat CoV (Supplementary Figure S2H) . Calculated mean PPIDs of Nsp15s from SARS-CoV-2, Human SARS, and Bat CoV are 1.73%, 2.60%, and 2.60%, respectively. Similar to many other non-structural proteins of coronaviruses, Nsp15s from SARS-CoV-2, Human SARS, and Bat CoV are predicted to possess multiple flexible regions but contain virtually no IDPRs (see Figures 32A, 32B, and 32C) . Similarly, no significant disorderbinding regions are predicted in Nsp15 proteins ( Table 2) . SARS-CoV-2 contain one MoRF (residues 9-13) predicted by MoRFPred server. Human SARS do not have a single MoRF while Bat CoV possesses two very short binding regions (Supplementary Table 7 and 8). Supplementary Table 9 , 10, and 11 depicts the presence of many RNA binding residues and few DNA binding residues in Nsp15 of all three viruses. author/funder. All rights reserved. No reuse allowed without permission.