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

Nsp10 performs several functions for SARS-CoV. It forms a complex with Nsp14 for dsRNA hydrolysis in 3′ to 5′ direction and activates its exonuclease activity [148] . It also stimulates the methyltransferase (MTase) activity of Nsp14 required during RNA-cap formation after replication [149] . Figure 28D represents the X-ray crystal structure of the Nsp10/Nsp14 complex (PDB ID: 5C8T) [150] . In agreement with the results of previous biochemical experimental studies, the structure identified important interactions with the ExoN (exonuclease domain) of Nsp14 without affecting its N7-MTase activity [148, 149] . SARS-CoV-2 Nsp10 protein is quite conserved having a 97.12% sequence identity with Nsp10 of Human SARS and 97.84% with Nsp10 of Bat CoV (Figure 28E) . Mean PPIDs of all three studied Nsp10 proteins are found to be 5.04%. Figures 28A, 28B , and 28C represent disorder profiles of Nsp10s and signify the lack of long IDPRs but presence flexible regions in these proteins. Furthermore, 25-32, 91-99, and 133-138) was identified by MoRFchibi_web server and one MoRF (residues [11] [12] [13] [14] [15] [16] [17] [18] author/funder. All rights reserved. No reuse allowed without permission.