IPR006189
CHASE domain
InterPro entry
Short name | CHASE_dom |
Overlapping homologous superfamilies |
Description
The CHASE domain is an extracellular domain of 200-230 amino acids, which is found in transmembrane receptors from bacteria, lower eukaryotes and plants. It has been named CHASE (Cyclases/Histidine kinases Associated Sensory Extracellular) because of its presence in diverse receptor-like proteins with histidine kinase and nucleotide cyclase domains. The CHASE domain always occurs N-terminally in extracellular or periplasmic locations, followed by an intracellular tail housing diverse enzymatic signalling domains such as histidine kinase (
IPR005467), adenyl cyclase, GGDEF-type nucleotide cyclase and EAL-type phosphodiesterase domains, as well as non-enzymatic domains such PAS (
IPR000014), GAF (
IPR003018), phosphohistidine and response regulatory domains. The CHASE domain is predicted to bind diverse low molecular weight ligands, such as the cytokinin-like adenine derivatives or peptides, and mediate signal transduction through the respective receptors
[1, 2].
The CHASE domain has a predicted α+β fold, with two extended α helices on both boundaries and two central α helices separated by β sheets. The termini are less conserved compared with the central part of the domain, which shows strongly conserved motifs.
References
1.CHASE: an extracellular sensing domain common to transmembrane receptors from prokaryotes, lower eukaryotes and plants. Mougel C, Zhulin IB. Trends Biochem. Sci. 26, 582-4, (2001). View articlePMID: 11590001
2.The CHASE domain: a predicted ligand-binding module in plant cytokinin receptors and other eukaryotic and bacterial receptors. Anantharaman V, Aravind L. Trends Biochem. Sci. 26, 579-82, (2001). View articlePMID: 11590000
Cross References
Representative structure
3t4l: Arabidopsis histidine kinase 4 sensor domain in complex with trans-zeatin