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 2128267006   1 MDARDKQLLRSLRLELCTEVLVDGLVIQYLYQEGILTDSHVQEIKSQTTSQRKTMMLLDILPTRGPKAFDAFLDSLQEFP 80
Cdd:cd08327     1 MEPKHKQLLRSQRLELCAELLVDGLIVQYLYQEGILTESHVEEIQSQTTSRRKTLKLLDILPNRGPKAFHAFLDSLEEFP 80

                          90
                  ....*....|....
gi 2128267006  81 WVKDKLKVKRKEMT 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 2128267006   1 MDARDKQLLRSLRLELCTEVLVDGLVIQYLYQEGILTDSHVQEIKSQTTSQRKTMMLLDILPTRGPKAFDAFLDSLQEFP 80
Cdd:cd08327     1 MEPKHKQLLRSQRLELCAELLVDGLIVQYLYQEGILTESHVEEIQSQTTSRRKTLKLLDILPNRGPKAFHAFLDSLEEFP 80

                          90
                  ....*....|....
gi 2128267006  81 WVKDKLKVKRKEMT 94
Cdd:cd08327    81 WVRDKLLLLREEGE 94

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2128267006    1 MDARDKQLLRSLRLELCTEVLVDGLvIQYLYQEGILTDSHVQEIKSQTTSQRKTMMLLDILPTRGPKAFDAFLDSLQEF 79
Cdd:smart00114   1 MAERDKRLLRRNRVRLGEELGVDGL-LDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQET 78

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2128267006  111 SSPTDQQMNKLA-RRLGPEWEHIVLCLGLSHTDIYRCKVNHPHNVQSQIVAAFVLWRQRFGKSATIQSL 178
Cdd:smart00005   1 PELTRQKLAKLLdHPLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTL 69

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 2128267006   1 MDARDKQLLRSLRLELCTEVLVDGLVIQYLYQEGILTDSHVQEIKSQTTSQRKTMMLLDILPTRGPKAFDAFLDSLQEFP 80
Cdd:cd08327     1 MEPKHKQLLRSQRLELCAELLVDGLIVQYLYQEGILTESHVEEIQSQTTSRRKTLKLLDILPNRGPKAFHAFLDSLEEFP 80

                          90
                  ....*....|....
gi 2128267006  81 WVKDKLKVKRKEMT 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 2128267006   9 LRSLRLELCTEVLVDgLVIQYLYQEGILTDSHVQEIKSQTTSQRKTMMLLDILPTRGPKAFDAFLDSLQE--FPWVKDKL 86
Cdd:cd01671     1 LRKNRVELVEDLDVE-DILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALREtgQPHLAELL 79

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2128267006   6 KQLLRSLRLELCTEVLVDGLVIQYLYQEGILTDSHVQEIKSQTTSQRKTMMLLDILPTRGPKAFDAFLDSLQE 78
Cdd:pfam00619   1 RKLLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKE 73

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2128267006 117 QMNKLARRLGPEWEHIVLCLGLSHTDIYRCKVNHPHNVQSQIVAAFVLWRQRFGKSATIQSLQASL 182
Cdd:cd01670     1 YFDLVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQAL 66

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2128267006  111 SSPTDQQMNKLA-RRLGPEWEHIVLCLGLSHTDIYRCKVNHPHNVQSQIVAAFVLWRQRFGKSATIQSL 178
Cdd:smart00005   1 PELTRQKLAKLLdHPLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTL 69

Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation and recruitment domain (CARD) found in CARD9, CARD14 (CARMA2), CARD10 (CARMA3), CARD11 (CARMA1) and BCL10. BCL10 (B-cell lymphoma 10), together with Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), are integral components of the CBM signalosome. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells), and with CARD11 to form L-CBM (CBM complex in lymphoid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. BCL10/Malt1 also associates with CARD10, which is more widely expressed and is not restricted to hematopoietic cells, to play a role in GPCR-induced NF-kB activation. CARD14 has also been shown to associate with BCL10. 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128267006  29 YLYQEGILTDSHVQEIKSQTTSQR-KTMMLLDILPTRGPKAFDAFLDSLQ-EFPWVKDKL 86
Cdd:cd08785    24 YLRQKKVLSEDDEEEILSKPSLPRnRAGYLLDILKTRGKNGYDAFLESLEfYYPELFTKV 83

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 2128267006   5 DKQLLRSLRLELCTEVLVDGLViQYLYQEGILTDSHVQEIKSQTTSQRKTMMLLDILPTRGPKAFDAFLDSLQE 78
Cdd:cd08326     1 HRQILRRHRARLVEELQPKYLW-DHLLSRGVFTPDMIEEIQAAGSRRDQARQLLIDLETRGKQAFPAFLSALRE 73

Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in FAS-associated via death domain (FADD). FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor, FAS, and its DED recruits the initiator caspases, caspase-8 and -10, to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. 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. They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2128267006 125 LGPEWEHIVLCLGLSHTDIYRCKVNHPHNVQSQIVAAFVLWRQRFGKSATIQSLQASL 182
Cdd:cd08306    12 LGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKAL 69

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. 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
                  ....*....|....*....|....*....|....*....|....*....
gi 2128267006  30 LYQeGILTDSHVQEIKSQTTSQRKTMMLLDILPTRGPKAFDAFLDSLQE 78
Cdd:cd08330    24 LRG-KVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKE 71