{PDOC50839} {PS50839; CHASE} {BEGIN} ************************ * 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 ), adenyl cyclase, GGDEF-type nucleotide cyclase and EAL-type phosphodiesterase domains, as well as non-enzymatic domains such PAS (see ), GAF, phosphohistidine and response regulatory domains (see ). 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 alpha+beta fold, with two extended alpha helices on both boundaries and two central alpha helices separated by beta 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. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: June 2003 / First entry. [ 1] Anantharaman V., Aravind L. "The CHASE domain: a predicted ligand-binding module in plant cytokinin receptors and other eukaryotic and bacterial receptors." Trends Biochem. Sci. 26:579-582(2001). PubMed=11590000 [ 2] Mougel C., Zhulin I.B. "CHASE: an extracellular sensing domain common to transmembrane receptors from prokaryotes, lower eukaryotes and plants." Trends Biochem. Sci. 26:582-584(2001). PubMed=11590001 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}