Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). Inhibits the IFN signaling response directed by the dsRNA sensor DDX58/RIG-I (PubMed:33478127). Homotrimer (PubMed:15564476, PubMed:16940519). Homomultimer (PubMed:14512541, PubMed:18753226, PubMed:15564476). Homomultimerizes and binds to viral genomic RNA to form the nucleocapsid (By similarity). Interacts with host MAP1LC3B; this interaction participates to the protection of Gn from virus-triggered autophagy (By similarity). Interacts with host SNAP29; this interaction participates to the protection of glycoprotein N from virus-triggered autophagy (By similarity). Interacts (via N-terminus) with host RPS19; this interaction probably mediates the loading of the 40S ribosomal subunit on viral capped mRNA during N-mediated translation initiation (By similarity). Interacts with the viral RdRp (By similarity). Interacts with host SUMO1 (via N-terminus) (PubMed:12606074). Interacts with host DAXX (By similarity). Interacts with the viral glycoprotein N (via C-terminus) (PubMed:20566401). Interacts with the viral glycoprotein C (via C-terminus) (By similarity). Internal protein of virus particle. The N-terminus is required for chaperone activity and, in trimeric form, this region likely serves in high affinity vRNA panhandle recognition (By similarity). The N-terminus also contains a coiled coil region, which probably participates in but is insufficient to initiate N trimerization (PubMed:18753226, PubMed:16940519). The YxxL motif is indispensable for the interaction with host MAP1LC3B (By similarity). The central region is involved in specific RNA-binding (By similarity). Has distinct cap- and RNA-binding sites so it can bind simultaneously both the vRNA and mRNA cap (By similarity). Belongs to the hantavirus nucleocapsid protein family.