The domain within your query sequence starts at position 141 and ends at position 544; the E-value for the PP2Ac domain shown below is 1.97e-118.

All catalytic sites are present in this domain. Check the literature (PubMed 7500362 ) for details.

LHARYVLNLLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPE
RAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKY
KIHGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDKTDLELLAKLDRHKIVSTMRCKT
RKESENREEQKRKDNQTSSGQKPTPWFLPQSRSLPSSPFHLGSGFKAYKAGRSCSIPCGS
PNSKELSRRGQVRRSVDLELEQCRQQAGFLGIREKGESLPLAPDADCVADGGGVLEPTPE
EWKQVVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYE
FCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIVQYQANK

PP2Ac

Protein phosphatase 2A homologues, catalytic domain.
PP2Ac
SMART accession number:SM00156
Description: Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.
Interpro abstract (IPR006186):

Protein phosphorylation plays a central role in the regulation of cell functions [ (PUBMED:2827745) ], causing the activation or inhibition of many enzymes involved in various biochemical pathways [ (PUBMED:2176161) ]. Kinases and phosphatases are the enzymes responsible for this, and may themselves be subject to control through the action of hormones and growth factors [ (PUBMED:2827745) ]. Serine/threonine (S/T) phosphatases ( EC 3.1.3.16 ) catalyse the dephosphorylation of phosphoserine and phosphothreonine residues. In mammalian tissues four different types of PP have been identified and are known as PP1, PP2A, PP2B and PP2C. Except for PP2C, these enzymes are evolutionary related. The catalytic regions of the proteins are well conserved and have a slow mutation rate, suggesting that major changes in these regions are highly detrimental [ (PUBMED:2827745) ].

Protein phosphatase-1 (PP1) and protein phosphatase-2A (PP2A) have a broad specificity and there are two closely related isoforms of each, alpha and beta. PP2A is a trimeric enzyme that consists of a core composed of a catalytic subunit associated with a 65kDa regulatory subunit and a third variable subunit. Protein phosphatase-2B (PP2B or calcineurin), a calcium-dependent enzyme whose activity is stimulated by calmodulin, is composed of two subunits the catalytic A-subunit and the calcium-binding B-subunit. The specificity of PP2B is restricted. Other serine/threonine specific protein phosphatases that have been characterised include mammalian phosphatase-X (PP-X), and Drosophila phosphatase-V (PP-V), which are closely related but yet distinct from PP2A; yeast phosphatase PPH3, which is similar to PP2A, but with different enzymatic properties; and Drosophila phosphatase-Y (PP-Y), and yeast phosphatases Z1 and Z2 which are closely related but yet distinct from PP1.

GO function:hydrolase activity (GO:0016787)
Family alignment:
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There are 25154 PP2Ac domains in 25130 proteins in SMART's nrdb database.

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