CHASE: an extracellular sensing domain common to transmembrane receptors from prokaryotes, lower eukaryotes and plants.
A novel extracellular ligand-binding domain, termed CHASE, is described in sensory adenylyl and diguanylate cyclases, and histidine kinases, in several bacterial species, Dictyostelium and plants. The CHASE domain is predicted to sense stimuli that are specific for the developmental program of an organism.
Mougel
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School of Biology, Georgia Institute of Technology, Atlanta, GA 30332-0230, USA.
Zhulin
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IB
D000262:Adenylyl Cyclases / Q000737:chemistry / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D005057:Eukaryotic Cells; D008969:Molecular Sequence Data; D010944:Plants / Q000737:chemistry / Q000235:genetics; D011387:Prokaryotic Cells; D011494:Protein Kinases / Q000737:chemistry / Q000235:genetics; D017434:Protein Structure, Tertiary; D015800:Protozoan Proteins; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D015800:Protozoan Proteins; D011956:Receptors, Cell Surface; D011494:Protein Kinases; C101160:DhkA protein, Dictyostelium discoideum; C101765:ACG protein, Dictyostelium discoideum; D000262:Adenylyl Cyclases