The domain within your query sequence starts at position 26 and ends at position 106; the E-value for the Death domain shown below is 1.3e-15.



PFAM accession number:PF00531
Interpro abstract (IPR000488):

The death domain (DD) is a homotypic protein interaction module composed of a bundle of six alpha-helices. DD is related in sequence and structure to the death effector domain (DED, see IPR001875) and the caspase recruitment domain (CARD, see IPR001315), which work in similar pathways and show similar interaction properties [(PUBMED:11504623)]. DD bind each other forming oligomers. Mammals have numerous and diverse DD-containing proteins [(PUBMED:7482697)]. Within these proteins, the DD domains can be found in combination with other domains, including: CARDs, DEDs, ankyrin repeats (IPR002110), caspase-like folds, kinase domains, leucine zippers, leucine-rich repeats (LRR) (IPR001611), TIR domains (IPR000157), and ZU5 domains (IPR000906) [(PUBMED:15226512)].

Some DD-containing proteins are involved in the regulation of apoptosis and inflammation through their activation of caspases and NF-kappaB, which typically involves interactions with TNF (tumour necrosis factor) cytokine receptors [(PUBMED:14585074), (PUBMED:14601641)]. In humans, eight of the over 30 known TNF receptors contain DD in their cytoplasmic tails; several of these TNF receptors use caspase activation as a signalling mechanism. The DD mediates self-association of these receptors, thus giving the signal to downstream events that lead to apoptosis. Other DD-containing proteins, such as ankyrin, MyD88 and pelle, are probably not directly involved in cell death signalling. DD-containing proteins also have links to innate immunity, communicating with Toll family receptors through bipartite adapter proteins such as MyD88 [(PUBMED:12691620)].

GO process:signal transduction (GO:0007165)
GO function:protein binding (GO:0005515)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Death