Diacylglycerol kinase, catalytic domain (IPR001206)

Short name: Diacylglycerol_kinase_cat_dom

Overlapping homologous superfamilies

Domain relationships



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 [PMID: 8626538, PMID: 17351295]. Eukaryotic DAG-kinase (EC: 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 (see PDOC00018), PH (see PDOC50003), SAM (see PDOC50105) , DAG/PE-binding C1 domain (see PDOC00379) and ankyrin repeats (see PDOC50088) [PMID: 17512245].

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 alpha/beta fold [PMID: 17351295]. The tertiary structure resembles that of NAD kinases and contains a metal-binding site in the C-terminal region [PMID: 17351295, PMID: 19112175].

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

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016301 kinase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles