{PDOC51437}
{PS51437; CG_1}
{BEGIN}
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* CG-1 DNA-binding domain profile *
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Calmodulin-binding transcription  activators  (CAMTAs)  comprise  a  conserved
family of   transcription   activators   in  a  wide  range  of  multicellular
eukaryotes, which  possibly  respond to calcium signaling by direct binding of
calmodulin. The  CAMTA  proteins  consist  of  multiple  predicted  functional
domains, evolutionarily  conserved in amino acid sequences, and organized in a
conserved order.   The   functional   domains  include:  a  bipartite  nuclear
localization signal  (NLS)  (see  <PDOC00015>)  in  the N-terminal part of all
CAMTA proteins;  a  CG-1 domain, containing the predicted bipartite NLS; a TIG
domain reported  to  be  implicated  in  nonspecific  DNA  contacts in various
transcription factors  (TFs),  and  involved  in protein dimerization; ankyrin
(ANK) repeats  (see <PDOC50088>), known to be involved in nonspecific protein-
protein interactions  and  present  in  a large number of functionally diverse
proteins; and  a  variable  number  of  IQ  motifs (see <PDOC50096>), known as
calmodulin-binding sites, localized in the C-terminal part of CAMTAs. Although
spacing is  highly  variable,  overall domain organization is conserved in all
proteins. It  is  likely  that CAMTAs are present exclusively in multicellular
organisms. This  may suggest their involvement in cell-cell communication and/
or developmental processes that are unique to multicellular organisms [1,2].

The CG-1 domain of about 130 amino acid residues is named after a partial cDNA
clone isolated  from  parsley  (Petroselinum  crispum)  encoding  a  sequence-
specific DNA-binding  protein.  The  CG-1  domain of CAMTA recognizes specific
CGCG box-containing   DNA   sequences,  and  a  nearby  region  activates  the
transcription [1,3].

The profile we developed covers the entire CG-1 DNA-binding domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: February 2009 / First entry.

[ 1] Bouche N., Scharlat A., Snedden W., Bouchez D., Fromm H.
     "A novel family of calmodulin-binding transcription activators in
     multicellular organisms."
     J. Biol. Chem. 277:21851-21861(2002).
     PubMed=11925432; DOI=10.1074/jbc.M200268200
[ 2] Finkler A., Ashery-Padan R., Fromm H.
     "CAMTAs: calmodulin-binding transcription activators from plants to
     human."
     FEBS Lett. 581:3893-3898(2007).
     PubMed=17689537; DOI=10.1016/j.febslet.2007.07.051
[ 3] Gong P., Han J., Reddig K., Li H.S.
     "A potential dimerization region of dCAMTA is critical for termination
     of fly visual response."
     J. Biol. Chem. 282:21253-21258(2007).
     PubMed=17537720; DOI=10.1074/jbc.M701223200

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