Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.

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gi 1616013163 802 WDNLLHWLAEELAEEGAeVLAASLPLRRSTVQLIKLKHPDDPTEQIHELLCFWKRSLPTSTDKIRLLARHLRKMGRGDLT 881
Cdd:cd08779     1 TDSNLLSLAKELGEDWQ-KLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLA 79

                  ....*..
gi 1616013163 882 EELKFKW 888
Cdd:cd08779    80 EELRDKL 86

Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616013163 802 WDNLLHWLAEELAEEGAeVLAASLPLRRSTVQLIKLKHPDDPTEQIHELLCFWKRSLPTSTDKIRLLARHLRKMGRGDLT 881
Cdd:cd08779     1 TDSNLLSLAKELGEDWQ-KLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLA 79

                  ....*..
gi 1616013163 882 EELKFKW 888
Cdd:cd08779    80 EELRDKL 86

Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616013163 802 WDNLLHWLAEELAEEGAeVLAASLPLRRSTVQLIKLKHPDDPTEQIHELLCFWKRSLPTSTDKIRLLARHLRKMGRGDLT 881
Cdd:cd08779     1 TDSNLLSLAKELGEDWQ-KLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLA 79

                  ....*..
gi 1616013163 882 EELKFKW 888
Cdd:cd08779    80 EELRDKL 86

Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.

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gi 1616013163 821 LAASLPLRRSTVQLIKLKHPDDPTEQIHELLCFWKRSLPTSTDKIRLLaRHLRKMGRGDLTEELK 885
Cdd:cd01670    16 LARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLI-QALREIGRRDLAEKLE 79