Encapsidates the genome in a ratio of one protein N per nine ribonucleotides, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity). Homomultimerizes to form the nucleocapsid. Binds to viral genomic RNA. In nucleocapsid, binds protein P and thereby positions the polymerase on the template. Protein P acts as a chaperone on free protein N to prevent it from aggregation before encapsidating genomic RNA (By similarity). Phosphorylated by host CK2. Unphosphorylated protein N seems to have a better affinity for leader viral promoter encapsidation. Phosphorylation of protein N in ribonucleocapsid may stabilize the interaction with protein P, thereby playing an important role in viral transcription/replication (By similarity). Displays a superantigen activity in human and mouse, activating mostly V-beta-8 subtypes of T-cell receptor. Belongs to the lyssavirus nucleocapsid protein family.