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 PRU01379
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU01379
General rule information
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| Accession | PRU01379 |
| Dates | 11-AUG-2023 (Created)
29-AUG-2023 (Last updated, Version 3) |
| Data class | Domain; |
| Predictors |
PROSITE; PS52035; PEPTIDASE_M14 |
Name | Peptidase family M14 domain |
| Function | M14 metallocarboxypeptidases are a diverse and important class of peptidases that catalyze the removal of the C-terminal residue from polypeptides by means of a coordinated Zn(2+) cofactor. |
| Scope(s) |
Eukaryota Bacteria |
| Example(s) | Q09M02; |
Propagated annotation
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Comments
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| case <FTGroup:1> | |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; |
| end case | |
| SIMILARITY | Belongs to the peptidase M14 family. |
Keywords
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| Carboxypeptidase | |
| Hydrolase | |
| Metalloprotease | |
| Protease | |
| end case | |
| case <FTGroup:1> | |
| Metal-binding | |
| Zinc | |
| end case | |
Gene Ontology
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| case <FTGroup:1> | |
| GO:0008270; Molecular function:zinc ion binding | |
| end case | |
| case <FTTag:act_site> and <FTGroup:1> | |
| GO:0004181; Molecular function:metallocarboxypeptidase activity | |
| GO:0006508; Biological process:proteolysis | |
Features
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| From: PS52035 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="Peptidase M14 #" | |||||||||
| ACT_SITE | 256 | 256 | /note="Proton donor/acceptor" | act_site | E | |||||||
| BINDING | 62 | 62 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic" |
H | 1 | |||||||
| BINDING | 65 | 65 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic" |
E | 1 | |||||||
| BINDING | 182 | 182 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic" |
H | 1 | |||||||
Additional information
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| Size range | 234-454 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1-3 |
| 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 [10] Eukaryota [147] All [ 157 ]
- Retrieve set of proteins with 3D structure for this domain