| Type: | Domain | Name: | KEN domain |
| Description: | The proteins listed below share a common architecture with a protein kinase homology domain (see ) followed by an ~135-residue globular kinase-extension nuclease (KEN) domain made of eight helices []: - Mammalian 2-5A-dependent RNase or RNase L (EC 3.1.26.-), an interferon- induced enzyme implicated in both the molecular mechanisms of interferonaction and the fundamental control of RNA stability. 2-5A-dependent RNase is a unique enzyme in that it requires 2-5A, unusual oligoadenylates with2',5'-phosphodiester linkages. RNase L is catalytically active only after binding to an unusual activator molecule containing a 5'-phosphorylated 2',5'-linked oligoadenylate (2-5A), in the N-terminal half. RNase L consists of three domains, namely the N-terminal ankyrin repeat domain (see), the protein kinase homology domain, and the C-terminal KEN domain [, , ].- Eukaryotic Ire1/Ern1, an ancient transmembrane sensor of endoplasmic reticulum (ER) stress with dual protein kinase and ribonuclease activities.In response to ER stress Ire1/Ern1 catalyzes the splicing of target mRNAs in a spliceosome-independent manner. Ire1/Ern1 is a type 1 transmembranereceptor consisting of an N-terminal ER luminal domain, a transmembrane segment and a cytoplasmic region. The cytoplasmic region encompasses aprotein kinase domain followed by a C-terminal KEN domain [, ]. The dimerisation of the kinase domain activates the ribonuclease function of the KEN domain []. | Short Name: | KEN_dom |
