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DEATH domain superfamily
SCOP classification
InterPro annotation
| Cross references | IPR011029 SSF47986 Protein matches |
| Abstract | The death domain (DD) is a conserved region of about 80 residues found on death receptors, and which is required for death signalling, as well as a variety of non-apoptotic functions [ 11828422, 12655292]. Proteins containing this domain include the low affinity neurotrophin receptor p73, Fas, FADD (Fas-associated death domain protein), TNF-1 (tumour necrosis factor receptor-1), Pelle protein kinase, and the Tube adaptor protein [15226512].
The induction of apoptosis also relies on the presence of a second domain, called the death effector domain. The death effector domain (DED) occurs in proteins that regulate programmed cell death, including both pro- and anti-apoptotic proteins; many of these proteins are also involved in controlling cellular activation and proliferation pathways [12719729]. Proteins containing this domain include FADD (DED N-terminal, DD C-terminal), PEA-15 (phosphoproteins enriched in astrocytes 15kDa), caspases and FLIP.
The induction of apoptosis results in the activation of caspases, a family of aspartyl-specific cysteine proteases that are the main executioners of apoptosis. For example, the DED of FADD recruits two DED-containing caspases, caspase-8 and caspase-10, to form the death-inducing signal complex, which initiates apoptosis. Proteins containing the caspase recruitment domain (CARD) are involved in the recruitment and activation of caspases during apoptosis [12101092]. Other CARD proteins participate in NF-kappaB signalling pathways associated with innate or adaptive immune responses. Proteins containing CARD include Raidd, APAF-1 (apoptotic protease activating factor 1), procaspase 9 and iceberg (inhibitor of interleukin-1-beta generation).
The DD shows strong structural similarity to both DED and CARD. They all display a 6-helical closed bundle fold, with greek key topology and an internal psuedo two-fold symmetry. However, despite their overall similarity in topology, each domain forms specialised interactions, typically only with members of its own subfamily, for example DED with DED. |
InterPro database
Functional annotation
| General category | Processes_IC |
| Detailed category | Cell cycle, Apoptosis |
Function annotation of SCOP domain superfamilies
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Internal database links
The SUPERFAMILY hidden Markov model library has been used to carry
out SCOP domain assignments to all genomes at the superfamily level. Click on the 'Genome Assignments'
icon above to view the genome assignments for this superfamily.
Alignments of sequences to Alignments of sequences to 17 models
in this superfamily are available by clicking on the superfamily level 'Alignments' icon above. PDB sequences less than 40% identical
are shown by default, but any other sequences may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own.
It is possible to browse and view the proteins in the genomes which have
different combinations of domains including a DEATH domain domain. Click on the 'Domain Combinations' icon.
To view the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom click on the 'TaxViz' icon above. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.
Undirected domain occurrence networks are available for all superfamilies. Nodes in these networks represent genomes. Connections between nodes represent the presence of domain architectures, which contain the superfamily of interest, in both genomes.
There are 17 hidden Markov models representing the DEATH domain superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be viewed by clicking on the icon above.
Jump to [ Top of page · SCOP classification · InterPro annotation · Functional annotation · Internal database links ]
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