DAGKc

Diacylglycerol kinase catalytic domain (presumed)
DAGKc
SMART accession number:SM00046
Description: Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.
Interpro abstract (IPR001206):

The DAG-kinase catalytic domain or DAGKc domain is present in mammalian lipid kinases, such as diacylglycerol (DAG), ceramide and sphingosine kinases, as well as in related bacterial proteins [ (PUBMED:8626538) (PUBMED:17351295) ]. Eukaryotic DAG-kinase ( EC 2.7.1.107 ) catalyses the phosphorylation of DAG to phosphatidic acid, thus modulating the balance between the two signaling lipids. At least ten different isoforms have been identified in mammals, which form 5 groups characterised by different functional domains, such as the calcium-binding EF hand PH SAM DAG/PE-binding C1 domain and ankyrin repeats [ (PUBMED:17512245) ].

In bacteria, an integral membrane DAG kinase forms a homotrimeric protein that lacks the DAGKc domain. In contrast, the bacterial yegS protein is a soluble cytosolic protein that contains the DAGKc domain in the N-terminal part. YegS is a lipid kinase with two structural domains, wherein the active site is located in the interdomain cleft, C-terminal to the DAGKc domain which forms an alpha/beta fold [ (PUBMED:17351295) ]. The tertiary structure resembles that of NAD kinases and contains a metal-binding site in the C-terminal region [ (PUBMED:17351295) (PUBMED:19112175) ].

This domain is usually associated with an accessory domain (see IPR000756 ).

GO function:kinase activity (GO:0016301)
Family alignment:
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There are 30346 DAGKc domains in 30334 proteins in SMART's nrdb database.

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