{PDOC50816}
{PS50816; NAF}
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* NAF domain profile *
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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
[1].

The profile we developed covers the entire NAF domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: The  NAF  domain has also been named FISL motif for its conserved amino
 acid residues [2].

-Last update: November 2003 / First entry.

[ 1] Albrecht V., Ritz O., Linder S., Harter K., Kudla J.
     "The NAF domain defines a novel protein-protein interaction module
     conserved in Ca2+-regulated kinases."
     EMBO J. 20:1051-1063(2001).
     PubMed=11230129; DOI=10.1093/emboj/20.5.1051
[ 2] Guo Y., Halfter U., Ishitani M., Zhu J.-K.
     "Molecular characterization of functional domains in the protein
     kinase SOS2 that is required for plant salt tolerance."
     Plant Cell 13:1383-1400(2001).
     PubMed=11402167

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