CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria. Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognised by CHASE2 domains are not known at this time (PUBMED:12486065).
CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are upstream of signal transduction pathways in bacteria. Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. The environmental factors that are recognised by CHASE2 domains are not currently known [ (PUBMED:12486065) ].
Family alignment:
There are 9290 CHASE2 domains in 9289 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing CHASE2 domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with CHASE2 domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing CHASE2 domain in the selected taxonomic class.
Common extracellular sensory domains in transmembrane receptors fordiverse signal transduction pathways in bacteria and archaea.
J Bacteriol. 2003; 185: 285-94
Display abstract
Transmembrane receptors in microorganisms, such as sensory histidinekinases and methyl-accepting chemotaxis proteins, are molecular devicesfor monitoring environmental changes. We report here that sensory domainsharing is widespread among different classes of transmembrane receptors.We have identified two novel conserved extracellular sensory domains,named CHASE2 and CHASE3, that are found in at least four classes oftransmembrane receptors: histidine kinases, adenylate cyclases, predicteddiguanylate cyclases, and either serine/threonine protein kinases (CHASE2)or methyl-accepting chemotaxis proteins (CHASE3). Three otherextracellular sensory domains were shared by at least two differentclasses of transmembrane receptors: histidine kinases and eitherdiguanylate cyclases, adenylate cyclases, or phosphodiesterases. Theseobservations suggest that microorganisms use similar conserved domains tosense similar environmental signals and transmit this information viadifferent signal transduction pathways to different regulatory circuits:transcriptional regulation (histidine kinases), chemotaxis(methyl-accepting proteins), catabolite repression (adenylate cyclases),and modulation of enzyme activity (diguanylate cyclases andphosphodiesterases). The variety of signaling pathways using theCHASE-type domains indicates that these domains sense some criticallyimportant extracellular signals.
Links (links to other resources describing this domain)
