DAGKcDiacylglycerol kinase catalytic domain (presumed)
|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 184.108.40.206) 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)|
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