The domain within your query sequence starts at position 883 and ends at position 1102; the E-value for the CYCc domain shown below is 2.02e-70.

All catalytic sites are present in this domain. Check the literature (PubMed 97222132 ) for details.



Adenylyl- / guanylyl cyclase, catalytic domain
SMART accession number:SM00044
Description: Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.
Interpro abstract (IPR001054):

Guanylate cyclases ( EC ) catalyse the formation of cyclic GMP (cGMP) from GTP. cGMP acts as an intracellular messenger, activating cGMP-dependent kinases and regulating cGMP-sensitive ion channels. The role of cGMP as a second messenger in vascular smooth muscle relaxation and retinal photo-transduction is well established. Guanylate cyclase is found both in the soluble and particulate fractions of eukaryotic cells. The soluble and plasma membrane-bound forms differ in structure, regulation and other properties [ (PUBMED:1349465) (PUBMED:1356629) (PUBMED:1680765) (PUBMED:1982420) ]. Most currently known plasma membrane-bound forms are receptors for small polypeptides. The soluble forms of guanylate cyclase are cytoplasmic heterodimers having alpha and beta subunits.

In all characterised eukaryote guanylyl- and adenylyl cyclases, cyclic nucleotide synthesis is carried out by the conserved class III cyclase domain.

GO process:cyclic nucleotide biosynthetic process (GO:0009190), intracellular signal transduction (GO:0035556)
Family alignment:
View or

There are 67904 CYCc domains in 62634 proteins in SMART's nrdb database.

Click on the following links for more information.