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PROSITE documentation PDOC51695 |
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 [1,2,3,E1].
The three dimensional fold of sedolisin is based on a 7-stranded, all-parallel β-sheet. The sheet is flanked on both sides by several helices (see <PDB:1GA6>) [1].
Some proteins known to contain a sedolisin domain are listed below:
The profile we developed covers the entire sedolisin domain.
Last update:November 2013 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Wlodawer A. Li M. Gustchina A. Oyama H. Dunn B.M. Oda K. |
Title | Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases. | |
Source | Acta Biochim. Pol. 50:81-102(2003). | |
PubMed ID | 12673349 |
2 | Authors | Siezen R.J. Renckens B. Boekhorst J. |
Title | Evolution of prokaryotic subtilases: genome-wide analysis reveals novel subfamilies with different catalytic residues. | |
Source | Proteins 67:681-694(2007). | |
PubMed ID | 17348030 | |
DOI | 10.1002/prot.21290 |
3 | Authors | Oda K. |
Title | New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases. | |
Source | J. Biochem. 151:13-25(2012). | |
PubMed ID | 22016395 | |
DOI | 10.1093/jb/mvr129 |
E1 | Title | https://www.ebi.ac.uk/merops/cgi-bin/famsum?family=S53 |