|PROSITE documentation PDOC50146 [for PROSITE entry PS50146]|
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 [1,2]. Eukaryotic DAG-kinase (EC 188.8.131.52) catalyzes 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 characterized by different functional domains, such as the calcium-binding EF hand (see <PDOC00018>), PH (see <PDOC50003>), SAM (see <PDOC50105>), DAG/PE-binding C1 domain (see <PDOC00379>) and ankyrin repeats (see <PDOC50088>) .
In bacteria, an integral membrane DAG kinase forms a homotrimeric protein that lacks the DAGKc domain (see <PDOC00820>). 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 α/β fold (see <PDB: 2BON; A>) . The tertiary structure resembles that of NAD kinases and contains a metal-binding site in the C-terminal region [2,4].
Some proteins known to contain a DAGKc domain are listed below:
The profile we developed covers the entire DAGKc domain.Last update:
June 2009 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Sakane F., Imai S., Kai M., Wada I., Kanoh H.|
|Title||Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases.|
|Source||J. Biol. Chem. 271:8394-8401(1996).|
|2||Authors||Bakali H.M., Herman M.D., Johnson K.A., Kelly A.A., Wieslander A., Hallberg B.M., Nordlund P.|
|Title||Crystal structure of YegS, a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site.|
|Source||J. Biol. Chem. 282:19644-19652(2007).|
|3||Authors||Sakane F., Imai S., Kai M., Yasuda S., Kanoh H.|
|Title||Diacylglycerol kinases: why so many of them?|
|Source||Biochim. Biophys. Acta 1771:793-806(2007).|
|4||Authors||Jerga A., Miller D.J., White S.W., Rock C.O.|
|Title||Molecular determinants for interfacial binding and conformational change in a soluble diacylglycerol kinase.|
|Source||J. Biol. Chem. 284:7246-7254(2009).|