PF00781

Diacylglycerol kinase catalytic domain

Pfam entry
Member databasePfam
Pfam typefamily
Short nameDAGK_cat
ClanPFK
AuthorSMART; Coggill P;0000-0001-5731-1588
Sequence Ontology0100021

Description

Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologues. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family
[1]
.

References

1.Crystal structure of YegS, a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site. Bakali HM, Herman MD, Johnson KA, Kelly AA, Wieslander A, Hallberg BM, Nordlund P. J. Biol. Chem. 282, 19644-52, (2007). View articlePMID: 17351295

Further reading

2. Diacylglycerol kinase: a key modulator of signal transduction? Kanoh H, Yamada K, Sakane F. Trends Biochem. Sci. 15, 47-50, (1990). View articlePMID: 2159661

3. Porcine diacylglycerol kinase sequence has zinc finger and E-F hand motifs. Sakane F, Yamada K, Kanoh H, Yokoyama C, Tanabe T. Nature 344, 345-8, (1990). View articlePMID: 2156169

4. 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. Sakane F, Imai S, Kai M, Wada I, Kanoh H. J. Biol. Chem. 271, 8394-401, (1996). View articlePMID: 8626538

5. Purification, cDNA-cloning and expression of human diacylglycerol kinase. Schaap D, de Widt J, van der Wal J, Vandekerckhove J, van Damme J, Gussow D, Ploegh HL, van Blitterswijk WJ, van der Bend RL. FEBS Lett. 275, 151-8, (1990). View articlePMID: 2175712

Wikipedia

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