Trypsin-like serine protease
SMART accession number:SM00020
Description: Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Interpro abstract (IPR001254):

This group of serine proteases belong to the MEROPS peptidase family S1 (chymotrypsin family, clan PA(S)).

The chymotrypsin family is almost totally confined to animals, although trypsin-like enzymes are found in actinomycetes of the genera Streptomyces and Saccharopolyspora, and in the fungus Fusarium oxysporum [(PUBMED:7845208)]. The enzymes are inherently secreted, being synthesised with a signal peptide that targets them to the secretory pathway. Animal enzymes are either secreted directly, packaged into vesicles for regulated secretion, or are retained in leukocyte granules [(PUBMED:7845208)].

GO process:proteolysis (GO:0006508)
GO function:serine-type endopeptidase activity (GO:0004252)
Family alignment:
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There are 31415 Tryp_SPc domains in 30256 proteins in SMART's nrdb database.

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