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ProRule PRU01379


General rule information [?]

Accession PRU01379
Dates 11-AUG-2023 (Created)
29-AUG-2023 (Last updated, Version 2)
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 (CBPC5_MOUSE);

Propagated annotation [?]

Comments [?]

case <FTGroup:1>
COFACTORName=Zn(2+); Xref=ChEBI:CHEBI:29105;
end case
SIMILARITYBelongs to the peptidase M14 family.

Keywords [?]

Carboxypeptidase
Hydrolase
Metalloprotease
Protease
end case
case <FTGroup:1>
Metal-binding
Zinc
end case

Gene Ontology [?]

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 [?]

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 [?]

Size range 234-454 amino acids
Related rules None
Fusion None
Repeats 1-3
Topology Undefined

Copyright

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.



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UniProtKB rule member sequences [?]