Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 (aka NALP1, CARD7, NAC, DEFCAP) and CARD8 (aka TUCAN, Cardinal). NLRP1 is a member of the Nod-like receptor (NLR) protein superfamily and is involved in apoptosis and inflammation. To date, it is the only NLR protein known to have a FIIND domain. The FIIND domain is also present in the CARD8 protein where, like in NLRP1, it is followed by a C-terminal CARD domain. Both proteins are described to form an "inflammasome", a macro-molecular complex able to process caspase 1 and activate pro-IL1beta. The FIIND domain is present in only a very small subset of the kingdom of life, comprising primates, rodents (mouse, rat), carnivores (dog) and a few more, such as horse. The function of this domain is yet to be determined. Publications describing the newly discovered NLRP1 protein failed to identify it as a separate domain; for example, it was taken as part of the adjacent leucine rich repeat domain (LRR). Upon discovery of CARD8 it was noted that the N-terminal region shared significant sequence identity with an undescribed region in NLRP1. Before getting its final name, FIIND, this domain was termed NALP1-associated domain (NAD).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296531359  134 FPTAGWYLWSATGLGFLVRDEVTVTIAFGSWSQHLalDLQHHEQWLVGGPLFDVTAEPEeAVAEIHLPHFISLQAGEVDV 213
Cdd:pfam13553   3 LPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFL--DLLPPQHWMVAGPLFDIKAEPG-AVTAIHLPHFICLQAGHVDT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296531359  214 SWFLVAHFKNEGMVLEHPARVEPFYAVLESPSFSLMGILLRIaSGTRLSIPITSNTLIYYHPHPEDIKFHLYLVPSDALL 293
Cdd:pfam13553  80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLRI-HATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296531359  294 TKAIDDEEDR-FHGVRLQTSPPMEPLNFGSSYIVSNSANLKVMPKELKLSYRSPGEIQHFSKFYAGQMKEPIQLEITEKR 372
Cdd:pfam13553 159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238

                         250
                  ....*....|....
gi 296531359  373 HGTLVWDTEVKPVD 386
Cdd:pfam13553 239 SETLVWEALVRPGD 252

Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 (aka NALP1, CARD7, NAC, DEFCAP) and CARD8 (aka TUCAN, Cardinal). NLRP1 is a member of the Nod-like receptor (NLR) protein superfamily and is involved in apoptosis and inflammation. To date, it is the only NLR protein known to have a FIIND domain. The FIIND domain is also present in the CARD8 protein where, like in NLRP1, it is followed by a C-terminal CARD domain. Both proteins are described to form an "inflammasome", a macro-molecular complex able to process caspase 1 and activate pro-IL1beta. The FIIND domain is present in only a very small subset of the kingdom of life, comprising primates, rodents (mouse, rat), carnivores (dog) and a few more, such as horse. The function of this domain is yet to be determined. Publications describing the newly discovered NLRP1 protein failed to identify it as a separate domain; for example, it was taken as part of the adjacent leucine rich repeat domain (LRR). Upon discovery of CARD8 it was noted that the N-terminal region shared significant sequence identity with an undescribed region in NLRP1. Before getting its final name, FIIND, this domain was termed NALP1-associated domain (NAD).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296531359  134 FPTAGWYLWSATGLGFLVRDEVTVTIAFGSWSQHLalDLQHHEQWLVGGPLFDVTAEPEeAVAEIHLPHFISLQAGEVDV 213
Cdd:pfam13553   3 LPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFL--DLLPPQHWMVAGPLFDIKAEPG-AVTAIHLPHFICLQAGHVDT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296531359  214 SWFLVAHFKNEGMVLEHPARVEPFYAVLESPSFSLMGILLRIaSGTRLSIPITSNTLIYYHPHPEDIKFHLYLVPSDALL 293
Cdd:pfam13553  80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLRI-HATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296531359  294 TKAIDDEEDR-FHGVRLQTSPPMEPLNFGSSYIVSNSANLKVMPKELKLSYRSPGEIQHFSKFYAGQMKEPIQLEITEKR 372
Cdd:pfam13553 159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238

                         250
                  ....*....|....
gi 296531359  373 HGTLVWDTEVKPVD 386
Cdd:pfam13553 239 SETLVWEALVRPGD 252

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 296531359 405 KENHRQLQARMgDLKGVLDDLQDNEVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERD-PYLVSYL 482
Cdd:cd01671    2 RKNRVELVEDL-DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGqPHLAELL 79

Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 (aka NALP1, CARD7, NAC, DEFCAP) and CARD8 (aka TUCAN, Cardinal). NLRP1 is a member of the Nod-like receptor (NLR) protein superfamily and is involved in apoptosis and inflammation. To date, it is the only NLR protein known to have a FIIND domain. The FIIND domain is also present in the CARD8 protein where, like in NLRP1, it is followed by a C-terminal CARD domain. Both proteins are described to form an "inflammasome", a macro-molecular complex able to process caspase 1 and activate pro-IL1beta. The FIIND domain is present in only a very small subset of the kingdom of life, comprising primates, rodents (mouse, rat), carnivores (dog) and a few more, such as horse. The function of this domain is yet to be determined. Publications describing the newly discovered NLRP1 protein failed to identify it as a separate domain; for example, it was taken as part of the adjacent leucine rich repeat domain (LRR). Upon discovery of CARD8 it was noted that the N-terminal region shared significant sequence identity with an undescribed region in NLRP1. Before getting its final name, FIIND, this domain was termed NALP1-associated domain (NAD).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296531359  134 FPTAGWYLWSATGLGFLVRDEVTVTIAFGSWSQHLalDLQHHEQWLVGGPLFDVTAEPEeAVAEIHLPHFISLQAGEVDV 213
Cdd:pfam13553   3 LPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFL--DLLPPQHWMVAGPLFDIKAEPG-AVTAIHLPHFICLQAGHVDT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296531359  214 SWFLVAHFKNEGMVLEHPARVEPFYAVLESPSFSLMGILLRIaSGTRLSIPITSNTLIYYHPHPEDIKFHLYLVPSDALL 293
Cdd:pfam13553  80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLRI-HATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296531359  294 TKAIDDEEDR-FHGVRLQTSPPMEPLNFGSSYIVSNSANLKVMPKELKLSYRSPGEIQHFSKFYAGQMKEPIQLEITEKR 372
Cdd:pfam13553 159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238

                         250
                  ....*....|....
gi 296531359  373 HGTLVWDTEVKPVD 386
Cdd:pfam13553 239 SETLVWEALVRPGD 252

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 296531359 405 KENHRQLQARMgDLKGVLDDLQDNEVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERD-PYLVSYL 482
Cdd:cd01671    2 RKNRVELVEDL-DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGqPHLAELL 79

Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase activation and recruitment domain (CARD) similar to those found in Caspase-1 (CASP1, ICE) and related proteins, including CARD-only proteins such as ICEBERG or CARD18, INCA (CARD17), CARD16 (COP1, PSEUDO-ICE), CARD8 (DACAR, NDPP1, TUCAN), and CARD12 (NLRC4), as well as ICE-like caspases such as CASP12, CASP5 (ICH-3) and CASP4 (TX, ICH-2). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. CASP1 plays a central role in the cellular response to a wide variety of microbial and non-microbial stimuli, being activated by the inflammasome or the pyroptosome. CARD8 binds itself and the initiator caspase-9, interfering with the binding of APAF-1 and suppressing caspase-9 activation. CARD12 is a Nod-like receptor (NLR) that plays an important role in the innate immune response to Gram-negative bacteria. Caspase-4 (CASP4), -5 (CASP5), and -12 (CASP12) are inflammatory caspases implicated in inflammation and endoplasmic reticulum stress-induced apoptosis. 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 296531359 418 LKGVLDDLQDNEVLTENEKELVEQEK-TRQSKNEALLSMVEKKGDLALDVLFRSISERDPYL 478
Cdd:cd08325   18 INGLLDDLLEKNVLNEEEMEKIKEENnTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDKQL 79

Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. 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 296531359 400 GAAFVKENHRQLQARMGDLKGVLDDLQDNEVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERDPYLV 479
Cdd:cd08329    7 DLSLIRKNRMALFQHLTCVLPILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCLKEIDVVLY 86

                 ....*.
gi 296531359 480 SYLRQQ 485
Cdd:cd08329   87 RDLFVQ 92