The domain within your query sequence starts at position 589 and ends at position 651; the E-value for the Ribonuc_2-5A domain shown below is 2.9e-12.



PFAM accession number:PF06479
Interpro abstract (IPR010513):

The proteins listed below share a common architecture with a protein kinase homology domain followed by an ~135-residue globular kinase-extension nuclease (KEN) domain made of eight helices [ (PUBMED:18191223) ]:

  • Mammalian 2-5A-dependent RNase or RNase L (EC 3.1.26.-), an interferon-induced enzyme implicated in both the molecular mechanisms of interferon action and the fundamental control of RNA stability. 2-5A-dependent RNase is a unique enzyme in that it requires 2-5A, unusual oligoadenylates with 2',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 the protein kinase homology domain, and the C-terminal KEN domain [ (PUBMED:7680958) (PUBMED:15385955) (PUBMED:18426919) ].
  • 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 transmembrane receptor consisting of an N-terminal ER luminal domain, a transmembrane segment and a cytoplasmic region. The cytoplasmic region encompasses a protein kinase domain followed by a C-terminal KEN domain [ (PUBMED:18191223) (PUBMED:9637683) ].

The dimerisation of the kinase domain activates the ribonuclease function of the KEN domain [ (PUBMED:18191223) ].

GO process:mRNA processing (GO:0006397)
GO function:ribonuclease activity (GO:0004540)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Ribonuc_2-5A