Description

IPR015433 is a Phosphatidylinositol kinase.

<p>This group of proteins is comprised entirely of phosphatidylinositol 3- and phosphatidylinositol 4-kinases. Phosphatidylinositol 3-kinase (PI3-kinase) [[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) [[cite:PUB00001254]] acts on phosphatidylinositol (PI) in the first committed step of the production of the secondary messenger inositol-1,4,5-trisphosphate. The PI3- and PI4-kinases share a well-conserved domain at their C-terminal section, which is distantly related to the catalytic domain of protein kinases [[cite:PUB00000893], [cite:PUB00007087]]. The catalytic domain of PI3K has a bilobal structure with a small N-terminal lobe and a large C-terminal lobe; this structure is often found in other ATP-dependent kinases. The core of this catalytic domain is the most conserved region of the PI3Ks. The ATP cofactor binds in the crevice formed by the N-and C-terminal lobes, a loop between two strands provides a hydrophobic pocket for binding of the adenine moiety, and a lysine residue interacts with the alpha-phosphate. In contrast to other protein kinases, the PI3K loop interacts with the phosphates of the ATP, known as the glycine-rich or P-loop, contains no glycine residues. Instead, contact with the ATP -phosphate is maintained through the side chain of a conserved serine residue.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 31

Co-occuring domains 1

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