title: CHASE: an extracellular sensing domain common to transmembrane receptors from prokaryotes, lower eukaryotes and plants.
abstract: 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.
authors.affiliation: School of Biology, Georgia Institute of Technology, Atlanta, GA 30332-0230, USA.
authors.forename: C
authors.initials: C
authors.lastname: Mougel
authors.forename: I B
authors.initials: IB
authors.lastname: Zhulin
mesh_terms: 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
chemical_list: D015800:Protozoan Proteins; D011956:Receptors, Cell Surface; D011494:Protein Kinases; C101160:DhkA protein, Dictyostelium discoideum; C101765:ACG protein, Dictyostelium discoideum; D000262:Adenylyl Cyclases