|PROSITE documentation PDOC50816 [for PROSITE entry PS50816]|
The NAF domain is a 25 amino acid domain that is found in a plant-specific subgroup of serine-threonine protein kinases (CIPKs), that interact with calcineurin B-like calcium sensor proteins (CBLs). Whereas the N-terminal part of CIPKs comprises a conserved catalytic domain typical of Ser-Thr kinases, the much less conserved C-terminal domain appears to be unique to this subgroup of kinases. The only exception is the NAF domain that forms an 'island of conservation' in this otherwise variable region. The NAF domain has been named after the prominent conserved amino acids Asn-Ala-Phe. It represents a minimum protein interaction module that is both necessary and sufficient to mediate the interaction with the CBL calcium sensor proteins [1,2].
The secondary structure of the NAF domain is currently not known, but secondary structure computation of the C-terminal region of Arabidopsis thaliana CBL-interacting protein kinase 1 revealed a long helical structure .
The profile we developed covers the entire NAF domain.Note:
The NAF domain has also been named FISL motif for its conserved amino acid residues .Last update:
November 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Albrecht V., Ritz O., Linder S., Harter K., Kudla J.|
|Title||The NAF domain defines a novel protein-protein interaction module conserved in Ca2+-regulated kinases.|
|Source||EMBO J. 20:1051-1063(2001).|
|2||Authors||Guo Y., Halfter U., Ishitani M., Zhu J.-K.|
|Title||Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance.|
|Source||Plant Cell 13:1383-1400(2001).|