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Description

Nucleoprotein (UniProt: P0DTC9, also known as Nucleocapsid protein, NC, Protein N) is encoded by the N gene (Gene ID: 1489678) in Human SARS-2 coronavirus. The SARS-CoV-2 (COVID-19 causing virus) is a positive-strand RNA virus that causes severe respiratory syndrome in human. The mature SARS-CoV-2 contains 4 structural proteins: Envelope (E), Membrane (M), Nucleocapsid (N), and the Spike protein (S). Nucleoprotein of SARS-CoV-2 is an homooligomeric protein that packages the positive strand viral genome RNA into helical ribonucleocapsid and plays a role in virion assembly through its interactions with the viral genome and membrane protein M. It plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Nucleocapsid protein can be divided into five domains: an intrinsically disordered N-terminal domain (NTD), an RNA-binding domain (RBD), a predicted disordered central linker (LINK), a dimerization domain, and a disordered C-terminal domain. The NTD is thought to mediate a specific interaction with the viral genome s packaging signal, and the CTD forms a compact dimer that has been proposed to aid vRNP assembly. The RNA binding region of SARS-CoV-2 is localized to amino acids 41-186 and the dimerization domain resides in amino acids 258-361. The complete N protein of SARS- COV-2 is a highly basic with positive net charges and high pI (10.11). Its N-terminal region is more basic with positive charge, while the C-terminal region is acidic with negative charge. The middle region of nucleoprotein displays relatively higher hydrophobicity and the two termini display greater hydrophilicity. Nucleoprotein can undergo phosphorylation at multiple serines by GSK-3, CKII, Akt, CDKs, and Polo-like kinases. Some of these phosphorylation events are essential for RNA binding, oligomerization and localization to nucleoli. Phosphorylation is also required for recruitment of host RNA helicase DDX1 (DEAD-Box Helicase 1) that facilitates template readthrough and enables longer subgenomic mRNA synthesis. (Ref.: Cubuk, J., et al. (2021). Nat. Commun. 12, Article number: 1936, Lu, S., et al. (2021). Nat. Commun . 12, Article number 502, Miranda, J., et al. (2021). Mol. Med. 27, Article 161).