Protein Domain : Non-structural protein NSP9 superfamily, coronavirus IPR036499

Type	Homologous_superfamily
Description	NSP9 is a single-stranded RNA-binding viral protein involved in RNA synthesis, essential for the coronavirus replication [ , , ]. The dimerisation of NSP9 is essential for binding and orienting RNA for subsequent use by the replicase machinery. NSP9 is composed of seven antiparallel β-strands and a single α-helix hat are arranged into a single compact domain and form a cone-shaped β-barrel flanked by the C-terminal α-helix () [ , ]. The NSP9 dimer interface is formed by the N-finger motifs and the parallel association of the C-terminal α-helices GXXXG motifs. The N- and C-terminal regions are more conserved than the central core one, and the GXXXG motif is strictly conserved [, ]. NSP9 binds to discrete regions on the 7SL RNA component of the signal recognition particle (SRP) and interfere with protein trafficking to the cell membrane upon infection, which interferes with essential host functions, and suppresses host immune defenses [].
Short Name	NSP9_sf_CoV