v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | The unique coronavirus transcription/replication machinery comprised of multiple virus-encoded non structural proteins (NSP) plays a vital role during initial and intermediate phases of the viral life cycle. NSP15 forms a hexamer made of dimers of trimers which is suggested to be a functional unit, responsible for the endoribonuclease activity. The NSP15 monomer consists of three domains: N-terminal, middle and C-terminal [ , ]. The catalytic function of NSP15 resides in the C-terminal NendoU domain. The active site carries six key residues conserved among SARS-CoV-2, SARS-CoV and MERS-CoV, suggesting that its activity is important for sustained replication in the host [, ].This entry represents the N-terminal oligomerization domain of the NSP15, which stabilises the hexamer and is critical for its formation [ ]. This domain is composed of three-stranded antiparallel β-sheet and two α-helices [, , , ].This entry represents the N-terminal oligomerisation domain of the NSP15 from alpha and beta coronaviruses. |
| Short Name | NSP15_alpha_betaCoV_N |