The domain within your query sequence starts at position 2 and ends at position 99; the E-value for the PP2C domain shown below is 2.9e-14.
ATIGVTRGLGDHDLKVHDSNIYIKPFLSSAPEVRVYDLSRYEHGADDVLILATDGLWDVL SNEEVAEAITQFLPNCDPDDPHRYTLAAQDLVMRARGV
PP2C |
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PFAM accession number: | PF00481 |
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Interpro abstract (IPR001932): | 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 catalyses 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 [ (PUBMED:9003755) (PUBMED:9869399) (PUBMED:22115775) (PUBMED:22668558) ]. Some proteins known to contain a PPM-type phosphatase domain are listed below:
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-sheet packs against a three-stranded beta-sheet with flanking alpha-helices [ (PUBMED:9003755) (PUBMED:22115775) ]. This entry represents a conserved region found in the N-terminal part that contains a perfectly conserved tripeptide. |
GO function: | phosphatase activity (GO:0016791) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry PP2C