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 493798717  17 VEELQVDQLWDALLSRELFRPHMIEDIQRAGSgsRRDQARQLIIDLETRGSQALPLFISCLEDTGQDMLASFLR 90
Cdd:cd08326   13 VEELQPKYLWDHLLSRGVFTPDMIEEIQAAGS--RRDQARQLLIDLETRGKQAFPAFLSALRETGQTDLAELLR 84

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 493798717  17 VEELQVDQLWDALLSRELFRPHMIEDIQRAGSgsRRDQARQLIIDLETRGSQALPLFISCLEDTGQDMLASFLR 90
Cdd:cd08326   13 VEELQPKYLWDHLLSRGVFTPDMIEEIQAAGS--RRDQARQLLIDLETRGKQAFPAFLSALRETGQTDLAELLR 84

Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493798717   140 EQKDHGFEVASTSPEDESPGsnpepdatpfqeglrtfdQLDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDD 219
Cdd:smart00115 129 DELDGGVPVEDSVADPESEG------------------EDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQ 190

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 493798717   220 IFEQWAHSEDLQSLLLRVANAVSVKGIY----KQMPGCFNF-LRKKLFF 263
Cdd:smart00115 191 VLKEYARSLDLLDILTEVNRKVADKFESvnakKQMPTIESMtLTKKLYF 239

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        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493798717     1 MDEADRRLLRRCRLRLVEELQVDQLWDALLSRELFRPHMIEDIQRAGSGSRRDqaRQLIIDLETRGSQALPLFISCLEDT 80
Cdd:smart00114   1 MAERDKRLLRRNRVRLGEELGVDGLLDYLVEKNVLTEKEIEAIKAATTKLRDK--RELVDSLQKRGSQAFDTFLDSLQET 78

                           90
                   ....*....|.
gi 493798717    81 gQDMLASFLRT 91
Cdd:smart00114  79 -DQKLADFLEL 88

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 493798717  17 VEELQVDQLWDALLSRELFRPHMIEDIQRAGSgsRRDQARQLIIDLETRGSQALPLFISCLEDTGQDMLASFLR 90
Cdd:cd08326   13 VEELQPKYLWDHLLSRGVFTPDMIEEIQAAGS--RRDQARQLLIDLETRGKQAFPAFLSALRETGQTDLAELLR 84

Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493798717   140 EQKDHGFEVASTSPEDESPGsnpepdatpfqeglrtfdQLDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDD 219
Cdd:smart00115 129 DELDGGVPVEDSVADPESEG------------------EDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQ 190

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 493798717   220 IFEQWAHSEDLQSLLLRVANAVSVKGIY----KQMPGCFNF-LRKKLFF 263
Cdd:smart00115 191 VLKEYARSLDLLDILTEVNRKVADKFESvnakKQMPTIESMtLTKKLYF 239

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        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493798717     1 MDEADRRLLRRCRLRLVEELQVDQLWDALLSRELFRPHMIEDIQRAGSGSRRDqaRQLIIDLETRGSQALPLFISCLEDT 80
Cdd:smart00114   1 MAERDKRLLRRNRVRLGEELGVDGLLDYLVEKNVLTEKEIEAIKAATTKLRDK--RELVDSLQKRGSQAFDTFLDSLQET 78

                           90
                   ....*....|.
gi 493798717    81 gQDMLASFLRT 91
Cdd:smart00114  79 -DQKLADFLEL 88

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493798717  17 VEELQVDQLWDALLSRELFRPHMIEDIQRAGSgsRRDQARQLIIDLETRGSQALPLFISCLEDTGQDMLASFL 89
Cdd:cd01671    9 VEDLDVEDILDHLIQKGVLTEEDKEEILSEKT--RQDKARKLLDILPRRGPKAFEVFCEALRETGQPHLAELL 79