PROSITE documentation PDOC50839

CHASE domain profile

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 signaling domains such as histidine kinase (see <PDOC50109>), adenyl cyclase, GGDEF-type nucleotide cyclase and EAL-type phosphodiesterase domains, as well as non-enzymatic domains such PAS (see <PDOC50112>), GAF, phosphohistidine and response regulatory domains (see <PDOC50110>). 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 [1,2].

Some proteins known to contain a CHASE domain are listed below:

• Arabidopsis thaliana cytokinin receptor (Cre1), which transduces the signal for cell division and differentiation downstream of cytokinins (plant hormones).
• Dictyostelium discoideum spore differentiation factor receptor dhkA.
• Dictyostelium discoideum receptor-adenylyl cyclase ACG.
• Leishmania major hypothetical protein L4768.01.
• Synechocystis sp. PCC 7603 hypothetical protein sll0267.

The profile we developed covers the entire CHASE domain.