The domain within your query sequence starts at position 85 and ends at position 401; the E-value for the PI3_PI4_kinase domain shown below is 7.4e-61.

PELCPFYSRSLCYKTTTALGYYNIIGVFKPKSEEPYGQLNPKWTKYVHKVCCPCCFGRGC
LLPNQGYLSEAGAYLVDVKLNLGIVPKTKVVWLVSETFNYSAIDRAKSRGKKYALEKVPK
VGRKFHRIGLPPKVGSFQLFVKDYKEAEYWLRRFEAEPLPENIRKQFQSQFEKLVILDYI
IRNTDRGNDNWLVKYDEMKYAKKIESEESNWIDNKQLLIKIAAIDNGLAFPFKHPDEWRA
YPFHWAWLPQAKVPFSEETRNLILPYISDMNFVQDLCEDLYELFKTDKGFDRAAFENQMS
VMRGQILNLTQALRDGK

PI3_PI4_kinase

PI3_PI4_kinase
PFAM accession number:PF00454
Interpro abstract (IPR000403):

Phosphatidylinositol 3-kinase (PI3-kinase) (EC 2.7.1.137) [(PUBMED:1322797)] 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) [(PUBMED:8194527)] 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 [(PUBMED:12456783)].

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 [(PUBMED:8387896), (PUBMED:12151228)]. The catalytic domain of PI3K has the typical bilobal structure that is seen in other ATP-dependent kinases, with a small N-terminal lobe and a large C-terminal lobe. The core of this 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 protein kinases, the PI3K loop which interacts with the phosphates of the ATP and is 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.

This domain is also found in a number of pseudokinases, where a lack of typical motifs at the calatytic site suggest a lack of kinase activity.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PI3_PI4_kinase