Protein Domain : IPR002374

Type:  Family Name:  cGMP-dependent kinase
Description:  Guanosine cyclase 3',5'-dependent protein kinases are known to play a role in smooth muscle relaxation, ion fluxes in kidneys and intestines, and neuronal function. The predominant form of cGMP-dependent protein kinase is a dimer of identical 75 kDa subunits, although larger subunits of 86 and 130 kDa have been found []. The enzyme is kept in an inactive form by the interaction of the catalytic domain of one subunit with the region on the other subunit that precedes the cGMP binding domain. Each subunit contains two cGMP-binding regions, found together in the sequence: binding of two molecules of cGMP precipitates a conformational change in the active site that allows the substrate to bind.Although cGMP- and cAMP-dependent protein kinases are similar both in structure and sequence around the nucleotide binding site, and in the method of activation and inactivation, there are some basic contrasts. The major difference is that all of the functional domains of the cGMP- dependent enzymes are found on a single polypeptide chain, whereas cAMP- dependent protein kinases have separate regulatory (cAMP binding) and catalytic chains. Short Name:  cGMP_dep_kinase

0 Child Features

10 Contains

DB identifier Type Name
IPR000719 Domain Protein kinase domain
IPR011009 Domain Protein kinase-like domain
IPR002290 Domain Serine/threonine/dual specificity protein kinase, catalytic domain
IPR018490 Domain Cyclic nucleotide-binding-like
IPR000595 Domain Cyclic nucleotide-binding domain
IPR014710 Domain RmlC-like jelly roll fold
IPR000961 Domain AGC-kinase, C-terminal
IPR017441 Binding_site Protein kinase, ATP binding site
IPR008271 Active_site Serine/threonine-protein kinase, active site
IPR018488 Conserved_site Cyclic nucleotide-binding, conserved site

2 Cross Referencess


0 Found In

2 GO Annotations

GO Term Gene Name Organism
GO:0004692 IPR002374
GO:0005524 IPR002374

0 Parent Features

0 Proteins

1 Publications

First Author Title Year Journal Volume Pages PubMed ID