Description

IPR000403 is a Phosphatidylinositol 3-/4-kinase, catalytic domain.

<p>This entry represents the catalytic domain of Phosphatidylinositol 3/4-kinases (PI3/4K). This domain is also found in a number of pseudokinases, where a lack of typical motifs at the catalytic site suggest a lack of kinase activity.</p> <p>Phosphatidylinositol 3-kinase (PI3-kinase) ([ec:2.7.1.137]) [[cite:PUB00000875]] is an enzyme that phosphorylates phosphoinositides on the 3-hydroxyl group of the inositol ring. The three products of PI3-kinase - PI-3-P, PI-3,4-P(2) and PI-3,4,5-P(3) function as secondary messengers in cell signalling. Phosphatidylinositol 4-kinase (PI4-kinase) ([ec:2.7.1.67]) [[cite:PUB00001254]] is an enzyme that acts on phosphatidylinositol (PI) in the first committed step in the production of the secondary messenger inositol-1'4'5'-trisphosphate. This domain is also present in a wide range of protein kinases, involved in diverse cellular functions, such as control of cell growth, regulation of cell cycle progression, a DNA damage checkpoint, recombination, and maintenance of telomere length. Despite significant homology to lipid kinases, no lipid kinase activity has been demonstrated for any of the PIK-related kinases [[cite:PUB00014536]].</p> <p>The PI3- and PI4-kinases share a well conserved domain at their C-terminal section; this domain seems to be distantly related to the catalytic domain of protein kinases [[cite:PUB00000893], [cite:PUB00007087]]. The catalytic domain of PI3/PI4KK has the typical bilobal structure that is seen in other ATP-dependent kinases, divided into an N-lobe and a C-lobe ([pdbe:4HNE]) [[cite:PUB00090062]]. The core of this domain is the most conserved region of the PI3Ks. The N-lobe contains a five-stranded antiparallel β-sheet core flanked by a helical hairpin on one side and a helix on the other. The C-lobe contains helices, which form a helical bundle together with the N--obe helix. The helical bundle is flanked by three β-strands and a helix. Three loops are related to kinase activity, the glycine-rich G-loop, the catalytic loop and the activation loop. The G-loop has been reported to bind to the phosphate group of nucleotides [[cite:PUB00090062]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 89

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: