This short domain is rich in cysteines and histidines. The pattern of conservation is similar to that found in IPR002219. C1 domains are protein kinase C-like zinc finger structures. Diacylglycerol (DAG) kinases (DGKs) have a two or three commonly conserved cysteine-rich C1 domains [1]. DGKs modulate the balance between the two signaling lipids, DAG and phosphatidic acid (PA), by phosphorylating DAG to yield PA [2].

The PKD (protein kinase D) family are novel DAG receptors. They have twin C1 domains, designated C1a and C1b, which bind DAG or phorbol esters. Individual C1 domains differ in ligand-binding activity and selectivity [3].

1. Diacylglycerol kinases as emerging potential drug targets for a variety of diseases. Biochim. Biophys. Acta 9, 626-40
2. Diacylglycerol kinases: why so many of them? Biochem. J. 1771, 793-806
3. Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family. null 411, 333-42

This short domain is rich in cysteines and histidines. The pattern of conservation is similar to
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