PROSITE documentation PDOC51437
CG-1 DNA-binding domain profile


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.

Last update:

February 2009 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

CG_1, PS51437; CG-1 DNA-binding domain profile  (MATRIX)


1AuthorsBouche N. Scharlat A. Snedden W. Bouchez D. Fromm H.
TitleA novel family of calmodulin-binding transcription activators in multicellular organisms.
SourceJ. Biol. Chem. 277:21851-21861(2002).
PubMed ID11925432

2AuthorsFinkler A. Ashery-Padan R. Fromm H.
TitleCAMTAs: calmodulin-binding transcription activators from plants to human.
SourceFEBS Lett. 581:3893-3898(2007).
PubMed ID17689537

3AuthorsGong P. Han J. Reddig K. Li H.S.
TitleA potential dimerization region of dCAMTA is critical for termination of fly visual response.
SourceJ. Biol. Chem. 282:21253-21258(2007).
PubMed ID17537720

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