Sedolisin domain (IPR030400)

Short name: Sedolisin_dom

Overlapping homologous superfamilies

Domain relationships


This entry represents the sedolisin domain.

Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold ressembles that of subtilisin; however they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The defining features of these enzymes are a unique catalytic triad, Ser-Glu-Asp (SED in single-letter notation), as well as the presence of an aspartic acid residue in the oxyanion hole. Sedolisins are acid-acting endopeptidases or tripeptidyl peptidases. They are widely distributed among archea, bacteria, fungi, slime mold, amoeba and animal kingdom including amphibians, fish and mammals. Sedolisins form peptidase family S53 of the subtilisin-like (SB) clan [PMID: 12673349, PMID: 17348030, PMID: 22016395].

The three dimensional fold of sedolisin is based on a 7-stranded, all-parallel beta-sheet. The sheet is flanked on both sides by several helices [PMID: 12673349].

Some proteins known to contain a sedolisin domain are listed below:

  • Pseudomonas sedolisin.
  • Xanthomonas sp. Xanthomonalisin.
  • Bacterial kumamolisin.
  • Aspergillus oryzae aorsin.
  • Fungal sedolisin-B, a secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence.
  • Mammalian lysosomal tripeptidyl-peptidase 1 (TPP-1) or CLN2, involved in hydrolysis of hydrophobic proteins. A hereditary deficiency of human TPP-1 results in infantile neuronal ceroid lipofuscinosis (Batten disease), a rare but fatal neurodegenerative disorder.

GO terms

Biological Process

GO:0006508 proteolysis

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles