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. It is found at the N-terminal in extracellular … expand

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. It is found at the N-terminal 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 as PAS ( IPR000014 ), GAF ( IPR003018 ), phosphohistidine, and response regulatory domains. This domain is predicted to bind diverse low molecular weight ligands, such as cytokinin-like adenine derivatives or peptides, and mediate signal transduction through the respective receptors [ PUBMED:11590001 PUBMED:11590000 ]. It has a predicted α+β fold, with two extended α helices on both boundaries and two central α helices separated by β sheets. The N-terminal and C-terminal regions are less conserved compared with the central part of the domain, which shows strongly conserved motifs.