Table 2.
Structural and functional details of NSPs of SARS-CoV-2.
| Name | Function | Nucleotide Location | Amino Acids |
|---|---|---|---|
| NSP1 | Host mRNA degradation and translation inhibition |
266–805 | 180 |
| NSP2 | Unknown | 806–2719 | 638 |
| NSP3 | Polyprotein processing, de-ADP ribosylation, Deubiquitinating, Interferon antagonist, DMV (double-membrane vesicle) formation |
2720–8554 | 1945 |
| NSP4 | DMV formation | 8555–10,054 | 500 |
| NSP5 | Polyprotein processing, Inhibition of interferon signaling |
10,055–10,972 | 306 |
| NSP6 | DMV formation | 10,973–11,842 | 290 |
| NSP7 | Cofactor for RNA-dependent RNA polymerase | 11,843–12,091 | 83 |
| NSP8 | primase or 3′-terminal adenylyl transferase, cofactor for RNA-dependent RNA polymerase |
12,092–12,685 | 198 |
| NSP9 | Binding of single-stranded RNA | 12,686–13,024 | 113 |
| NSP10 | Cofactor for nsp14 and 16 | 13,025–13,441 | 139 |
| NSP11 | Unknown | 13,442–13,480 | 13 |
| NSP12 | RNA-dependent RNA polymerase, Nucleotidyl transferase |
13,442–16,236 | 932 |
| NSP13 | Helicase, RNA 5′ triphosphatase |
16,237–18,039 | 601 |
| NSP14 | 3′ to 5′ exoribonuclease, Proofreading, RNA cap formation, Guanosine N7-methyltransferase |
18,040–19,620 | 527 |
| NSP15 | Endoribonuclease, evasion of immune response | 19,621–20,658 | 346 |
| NSP16 | RNA cap formation, Ribose 2′ O-methyltransferase |
20,659–21,552 | 298 |