Seroatlas · Protein domains

Serine proteases, trypsin family, histidine active site

IPR018114

Definition

This entry represents the histidine active site of serine proteases belonging to the MEROPS peptidase family S1 (chymotrypsin family, clan PA(S)). The catalytic activity of the serine proteases from the chymotrypsin family is provided by a charge relay system involving an aspartic acid residue hydrogen-bonded to a histidine, which itself is hydrogen-bonded to a serine. The sequences in the vicinity of the active site histidine residues are well conserved in this family of proteases PMID:3136396. 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 PMID: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 PMID:7845208.

102 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (102 proteins: gene, accession, name)

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