Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent aspartate-directed proteases that mediate programmed cell death (apoptosis). Caspases are synthesized as inactive 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 homologs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919732  159 YKLISEPRGLALILSNVHFSSekdLEYRAGGDVDCTSLEMLFKHLGYQVTVFHDQTAQEMQNALERFSKMPGHRDVDSCI 238
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1728919732  239 VALLSHGVEGGVYGSDGKLLQLQEAFRLFDNANCPNLQNKPKMFFIQACRGG 290
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGD 129

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 1728919732  159 YKLISEPRGLALILSNVHFSSekdLEYRAGGDVDCTSLEMLFKHLGYQVTVFHDQTAQEMQNALERFSKMPGHRDVDSCI 238
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1728919732  239 VALLSHGVEGGVYGSDGKLLQLQEAFRLFDNANCPNLQNKPKMFFIQACRGG 290
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGD 129

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919732   1 MQRCHQEALKKNRVMLAKQLLLKELMEHMIEKDIFTTEMVEMIQAKSGSFSQNVEFLNLLPKRGPNAFSAFCEALRETKQ 80
Cdd:cd08332     1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSAFCEALRETSQ 80

                  ....*..
gi 1728919732  81 QHLEAVI 87
Cdd:cd08332    81 EHLADLL 87

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 1728919732    1 MQRCHQEALKKNRVMLAKQLLLKELMEHMIEKDIFTTEMVEMIQAKSGSFSQNVEFLNLLPKRGPNAFSAFCEALRETkQ 80
Cdd:smart00114   1 MAERDKRLLRRNRVRLGEELGVDGLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQET-D 79

                   ....
gi 1728919732   81 QHLE 84
Cdd:smart00114  80 QKLA 83

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 1728919732  159 YKLISEPRGLALILSNVHFSSekdLEYRAGGDVDCTSLEMLFKHLGYQVTVFHDQTAQEMQNALERFSKMPGHRDVDSCI 238
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1728919732  239 VALLSHGVEGGVYGSDGKLLQLQEAFRLFDNANCPNLQNKPKMFFIQACRGG 290
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGD 129

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919732   1 MQRCHQEALKKNRVMLAKQLLLKELMEHMIEKDIFTTEMVEMIQAKSGSFSQNVEFLNLLPKRGPNAFSAFCEALRETKQ 80
Cdd:cd08332     1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSAFCEALRETSQ 80

                  ....*..
gi 1728919732  81 QHLEAVI 87
Cdd:cd08332    81 EHLADLL 87

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 1728919732   9 LKKNRVMLAKQLLLKELMEHMIEKDIFTTEMVEMIQAKSGSFSQNVEFLNLLPKRGPNAFSAFCEALRETKQQHL 83
Cdd:cd01671     1 LRKNRVELVEDLDVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPHL 75

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 1728919732   6 QEALKKNRVMLAKQLL-LKELMEHMIEKDIFTTEMVEMIQAKSGSFSQNVEFLNLLPKRGPNAFSAFCEALRETkQQHL 83
Cdd:pfam00619   1 RKLLKKNRVALVERLGtLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEG-DPDL 78

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728919732   1 MQRCHQEALKKNRVMLAKQLLLKELM-EHMIEKDIFTTEMVEMIQAKSGSFSQNVEFLNLLPKRGPNAFSAFCEALRE 77
Cdd:cd08327     1 MEPKHKQLLRSQRLELCAELLVDGLIvQYLYQEGILTESHVEEIQSQTTSRRKTLKLLDILPNRGPKAFHAFLDSLEE 78

Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain is found near the N-terminus and interacts with the C-terminal domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919732   5 HQEALKKNRVMLAKQLLLKELMEHMieKDIFTTEMVEMIQAK---SGSFSQNVEFLN-LLPKRGPNAFSAFCEALRETKQ 80
Cdd:pfam16739   5 YRRLLRLFRPRLKDTIKPTEILPHL--PECLTEDDKERIRAEtnnKGNTAAAELLLDrLVRSDREGWFRAFLDALRKTGH 82

                  ...
gi 1728919732  81 QHL 83
Cdd:pfam16739  83 DGL 85

Caspase activation and recruitment domain found in MDA5, second repeat; Caspase activation and recruitment domain (CARD) found in MDA5 (melanoma-differentiation-associated gene 5), second repeat. MDA5, also known as IFIH1, contains two N-terminal CARD domains and a C-terminal RNA helicase domain. MDA5 is a cytoplasmic DEAD box RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. Although very similar in sequence, MDA5 recognizes different sets of viruses compared to RIG-I, a related RNA helicase. MDA5 associates with IPS-1 through a CARD-CARD interaction. 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 1728919732  20 LLLKELMEHMIEKDIFTTEMVEMIQAKS---GSFSQNVEFLNLLPKRGPNAFSAFCEALRETKQQHL 83
Cdd:cd08819    18 MKTTDVCDKCLEKGLLTAEDRERILAATenhGNRSGARELLSRIVRQKEGWFSKFLQALRETEHNNL 84