3.4.21.90	additional information	the active site of the protease releases the core protein from the growing polyprotein containing all structural proteins during translation. A short linker sequence connects the basic domain to the protease domain. In the Sindbis virus core protein, the basic domain, the linker sequence and the protease domain comprise amino acid residues M(1) to Q(94), P(95) to D(113), and R(114) to W(264), respectively. Core protein domain beginning at M(106) does not bind to the 60S ribosomal subunit, whereas core protein domain beginning at Q(94) binds to the 60S ribosomal subunit and inhibits the disassembly of cores in vitro	Sindbis virus	89	
3.4.21.90	additional information	the active site of the protease releases the core protein from the growing polyprotein containing all structural proteins during translation. Core protein is associated to the large 60S ribosomal subunit during in vitro protein synthesis and in the infected cell	Semliki forest virus	89	
3.4.21.90	additional information	the region that is responsible for nucleocapsid core accumulation has considerable overlap with the region that controls encapsidation specificity. Amino acids 96 to 113 are responsible for the specific encapsidation of genomic RNA. Amino acids 99 and 105 may interact directly with the encapsidation signal. Amino acids 106 to 113 are responsible for nucleocapsid core accumulation	Sindbis virus	89	
3.4.21.90	Sindbis virus core protein + H2O	-	Sindbis virus	15809	
3.4.21.90	Sindbis virus core protein + H2O	autocatalytic cleavage at Trp264	Sindbis virus	15809	
3.4.21.90	Sindbis virus core protein + H2O	autocatalytic cleavage at Trp264,  . Besides its catalytic activity it also plays important roles in the formation of the viral core, the recognition of the spike proteins during the budding process, the recognition and packaging of the viral RNA, and possibly the inhibition of the host cell protein synthesis	Sindbis virus	369541