We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
ProRule PRU01032
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU01032
General rule information
[?]
| Accession | PRU01032 |
| Dates | 20-AUG-2014 (Created)
26-JAN-2023 (Last updated, Version 8) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51695; SEDOLISIN |
Name | Sedolisin domain |
| Function | 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. |
| Scope(s) |
Eukaryota Bacteria Pseudomonadota |
| Example(s) | C5FHK0; |
Propagated annotation
[?]
Comments
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| case <FTGroup:2> | |
| COFACTOR | Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.; |
| end case | |
Keywords
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| case <FTGroup:1> | |
| Hydrolase | |
| Protease | |
| Serine protease | |
| end case | |
| case <FTGroup:2> | |
| Calcium | |
| Metal-binding | |
| end case | |
Gene Ontology
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| case <FTGroup:1> | |
| GO:0004252; Molecular function:serine-type endopeptidase activity | |
| end case | |
| case <FTGroup:2> | |
| GO:0046872; Molecular function:metal ion binding | |
| end case | |
Features
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| From: PS51695 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="Peptidase S53 #" | |||||||||
| ACT_SITE | 76 | 76 | /note="Charge relay system" | E | 1 | |||||||
| ACT_SITE | 80 | 80 | /note="Charge relay system" | D | 1 | |||||||
| ACT_SITE | 290 | 290 | /note="Charge relay system" | S | 1 | |||||||
| BINDING | 332 | 332 | /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" |
D | 2 | |||||||
| BINDING | 333 | 333 | /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" |
[IV] | 2 | |||||||
| BINDING | 354 | 354 | /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" |
G | 2 | |||||||
| BINDING | 356 | 356 | /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" |
D | 2 | |||||||
Additional information
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| Size range | 343-439 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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- UniProtKB/Swiss-Prot sets
Bacteria [4] Eukaryota [27] All [ 31 ]
- Retrieve set of proteins with 3D structure for this domain