id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-291950-9gtsqyfj	Rawlings, Neil D.	Introduction: The Clans and Families of Cysteine Peptidases	2012-11-09		.txt	text/plain	13752	707	53	A non-peptidase homolog is known from Trypanosoma brucei in which the catalytic Cys has been replaced by Ser. Family C10 contains streptopain (Chapter 483) and a few similar enzymes, all of which are from gram-positive bacteria. An alignment shows that residues Gln31, Cys32, His95 and Asn113 are conserved, suggesting that the N-terminal domain is a cysteine peptidase with a papain-like fold, which we include in family C51. The 'papain-like' endopeptidases of RNA viruses form a large group of cysteine peptidases that contain the catalytic dyad residues in the order Cys, His. All of the families had been included in clan CA, even though for many no tertiary structure for any member had been solved. Although no catalytic residues have been identified for any member of the family, they are predicted to occur in the order His, Glu, Gln, Cys. Family C57 contains the I7 protein from the vaccinia virus (Chapter 535), which is believed to be a polyprotein processing endopeptidase.	./cache/cord-291950-9gtsqyfj.txt	./txt/cord-291950-9gtsqyfj.txt