Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a death domain; Caspase activation and recruitment domain (CARD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal CARD, which interacts with the caspase-2 CARD, and a C-terminal Death domain (DD), which interacts with the DD of PIDD. In general, CARDs are DDs associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360289   1 MEARDKQVLRSLRLELGAEVLVEGLVLQYLYQEGILTENHIQEIKAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQEFP 80
Cdd:cd08327     1 MEPKHKQLLRSQRLELCAELLVDGLIVQYLYQEGILTESHVEEIQSQTTSRRKTLKLLDILPNRGPKAFHAFLDSLEEFP 80

                          90
                  ....*....|....
gi 1720360289  81 WVREKLEKAREEVT 94
Cdd:cd08327    81 WVRDKLLLLREEGE 94

Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a death domain; Caspase activation and recruitment domain (CARD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal CARD, which interacts with the caspase-2 CARD, and a C-terminal Death domain (DD), which interacts with the DD of PIDD. In general, CARDs are DDs associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360289   1 MEARDKQVLRSLRLELGAEVLVEGLVLQYLYQEGILTENHIQEIKAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQEFP 80
Cdd:cd08327     1 MEPKHKQLLRSQRLELCAELLVDGLIVQYLYQEGILTESHVEEIQSQTTSRRKTLKLLDILPNRGPKAFHAFLDSLEEFP 80

                          90
                  ....*....|....
gi 1720360289  81 WVREKLEKAREEVT 94
Cdd:cd08327    81 WVRDKLLLLREEGE 94

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360289   6 KQVLRSLRLELGAEVLVEGLVLQYLYQEGILTENHIQEIKAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQE-FPWVRE 84
Cdd:pfam00619   1 RKLLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEgDPDLAS 80

                  ...
gi 1720360289  85 KLE 87
Cdd:pfam00619  81 DLE 83

Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a death domain; Caspase activation and recruitment domain (CARD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal CARD, which interacts with the caspase-2 CARD, and a C-terminal Death domain (DD), which interacts with the DD of PIDD. In general, CARDs are DDs associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360289   1 MEARDKQVLRSLRLELGAEVLVEGLVLQYLYQEGILTENHIQEIKAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQEFP 80
Cdd:cd08327     1 MEPKHKQLLRSQRLELCAELLVDGLIVQYLYQEGILTESHVEEIQSQTTSRRKTLKLLDILPNRGPKAFHAFLDSLEEFP 80

                          90
                  ....*....|....
gi 1720360289  81 WVREKLEKAREEVT 94
Cdd:cd08327    81 WVRDKLLLLREEGE 94

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360289   9 LRSLRLELGAEVLVEgLVLQYLYQEGILTENHIQEIKAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQE--FPWVREKL 86
Cdd:cd01671     1 LRKNRVELVEDLDVE-DILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALREtgQPHLAELL 79

Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment domain (CARD) similar to that found in caspase-2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Caspase-2 (also known as ICH1, NEDD2, or CASP2) is one of the most evolutionarily conserved caspases, and plays a role in apoptosis, DNA damage response, cell cycle regulation, and tumor suppression. It is localized in the nucleus and exhibits properties of both an initiator and an effector caspase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360289   1 MEARDKQVLRSLRLELGAEVLVEGLvLQYLYQEGILTENHIQEIKAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQE 78
Cdd:cd08332     1 MQKRHREALKKNRVKLAKELVLDEL-LIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSAFCEALRE 77

Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment domain (CARD) similar to that found in caspase-9 (CASP9, MCH6, APAF3), which interacts with the CARD of apoptotic protease-activating factor 1 (APAF-1). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-9 is the initiator caspase associated with the intrinsic or mitochondrial pathway of apoptosis, induced by many pro-apoptotic signals. Together with APAF-1, it forms the heptameric 'apoptosome' in response to the release of cytochrome c from mitochondria. Activated caspase-9 cleaves and activates downstream effector caspases, like caspase-3, caspase-6, and caspase-7, resulting in apoptosis. In general, CARDs are death domains (DDs) associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720360289   5 DKQVLRSLRLELGAEVLVEGLvLQYLYQEGILTENHIQEIKAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQE 78
Cdd:cd08326     1 HRQILRRHRARLVEELQPKYL-WDHLLSRGVFTPDMIEEIQAAGSRRDQARQLLIDLETRGKQAFPAFLSALRE 73