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annotation rule: PRU01082

General rule information [?]

Accession PRU01082
Dates 4-FEB-2015 (Created)
27-OCT-2018 (Last updated, Version 3)
Data class Domain
Predictors PROSITE; PS51746; PPM_2
Name PPM-type phosphatase domain
Function The 300-residue protein phosphatase Mg(2+)- or Mn(2+)-dependent (PPM)-type phosphatase domain that catalyzes the dephosphorylation of phosphoserine- and phosphothreonine-containing protein.

Propagated annotation [?]


Description [?]

+ RecName: EC=3.1.3.16;

Comments [?]

Catalytic activity Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16;.
Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl- [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA- COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;.
Cofactor Mg(2+)
Mn(2+)
Note: Binds 2 magnesium or manganese ions per subunit

Cross-references [?]

PROSITE PS01032; PPM_1; 1;

Gene Ontology [?]

GO:0046872; Molecular function: metal ion binding.

Keywords [?]


Features [?]

From: PS51746
Key     From     To       Description   Tag   Condition   FTGroup
DOMAIN     from     to       PPM-type phosphatase #        

Additional information [?]

Size range 96-574 amino acids
Related rules None
Repeats 1
Topology Undefined
Example Q7XR06 (P2C45_ORYSJ)
Scope
Eukaryota
Bacteria
Viruses; Mimivirus
Comments None

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.



UniProtKB rule member sequences [?]