To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https
annotation rule: PRU01082

General rule information [?]

Accession PRU01082
Dates 4-FEB-2015 (Created)
16-DEC-2016 (Last updated, Version 2)
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 [a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate.
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 copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to license@isb-sib.ch or see: prosite_license.html.



UniProtKB rule member sequences [?]