| Type: | Domain | Name: | Sedolisin domain |
| Description: | 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 themature 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 ortripeptidyl peptidases. They are widely distributed among archea, bacteria, fungi, slime mold, amoeba and animal kingdom including amphibians, fish andmammals. Sedolisins form peptidase family S53 of the subtilisin-like (SB) clan [, , ].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 [].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-1results in infantile neuronal ceroid lipofuscinosis (Batten disease), a rare but fatal neurodegenerative disorder. | Short Name: | Sedolisin_dom |
| DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
|---|---|---|---|---|
| 58196 | I0YNJ1 | PAC:27394573 | Coccomyxa subellipsoidea C-169 |
392
 |
| 100010 | C1E3R6 | PAC:27400571 | Micromonas sp RCC299 |
1386
|
