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S8 family serine peptidase
The founding member of this family is the N-terminal prodomain of fervidolysin, an extracellular subtilisin-like serine protease. This domain folds into a globular alpha/beta structure consisting of four-stranded antiparallel beta-sheet and two alpha-helices packed on one side of it [1]. The prodomain is proteolytically cleaved and removed from the proenzyme. Paper describing PDB structure 1r6v. [1]. 14687574. Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin. Kim JS, Kluskens LD, de Vos WM, Huber R, van der Oost J;. J Mol Biol. 2004;335:787-797. (from Pfam)
Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see Pfam:PF00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567. (from Pfam)
S8 family peptidase
S8 family peptidase is a subtilisin-like serine protease containing an Asp/His/Ser catalytic triad that is not homologous to trypsin; similar to Bacillus sp. thermophilic serine proteinase
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