Binding Site

PPM-type phosphatase, divalent cation binding (IPR000222)

Short name: PP2C_BS


Protein phosphatases remove phosphate groups from various proteins that are the key components of a number of signalling pathways in eukaryotes and prokaryotes. Protein phosphatases that dephosphorylate Ser and Thr residues are classified into the phosphoprotein (PPP) and the protein phosphatase Mg(2+)- or Mn(2+)-dependent (PPM) families. The core structure of PPMs is the 300-residue PPM-type phosphatase domain that catalyzes the dephosphorylation of phosphoserine- and phosphothreonine-containing protein. The PPM-type phosphatase domain is found as a module in diverse structural contexts and is modulated by targeting and regulatory subunits [PMID: 9003755, PMID: 9869399, PMID: 22115775, PMID: 22668558].

The PP2C-type phosphatase domain consists of 10 segments of beta-strands and 5 segments of alpha-helix and comprises a pair of detached subdomains. The first is a small beta-sandwich with strand beta1 packed against strands beta2 and beta3; the second is a larger beta-sandwich in which a four-stranded beta- heet packs against a three-stranded beta-sheet with flanking alpha-helices [PMID: 9003755, PMID: 22115775].

This entry represents a conserved aspartate residue involved in divalent cation binding [PMID: 9003755].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0043169 cation binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns