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Conserved domains on  [gi|485050375|ref|NP_001264861|]
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caspase-9 isoform 2 [Mus musculus]

Protein Classification

caspase( domain architecture ID 10169988)

caspase is a cysteine-dependent aspartate-directed protease that mediates programmed cell death; belongs to the peptidase C14 family

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 190-403 5.63e-74

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.


:

Pssm-ID: 237997  Cd Length: 243  Bit Score: 230.95  E-value: 5.63e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375 190 AYTLDSDPCGHCLIINNVNFCPssGLGTRTGSNLDRDKLEHRFRWLRFMVEVKNDLTAKKMVTALMEMAHRNHRALDCFV 269
Cdd:cd00032    1 IYKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375 270 VVILSHGCQashlqfpGAVYGTDGCSVSIEKIVNIFNGSGCPSLGGKPKLFFIQACGGEQKDHGFEVactssqgrtldsD 349
Cdd:cd00032   79 CVILSHGEE-------GGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEV------------D 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 485050375 350 SEPDAVPYQEGPrplDQLDAVSSLPTPSDILVSYSTFPGcqcCFCERDLQADSW 403
Cdd:cd00032  140 SGADEPPDVETE---AEDDAVQTIPVEADFLVAYSTVPG---YVSWRNTKKGSW 187
CARD_CASP9 cd08326
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ...
 5-90 4.92e-41

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.


:

Pssm-ID: 176740  Cd Length: 84  Bit Score: 139.87  E-value: 4.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375   5 DRQLLRRCRVRLVSELQVAELWDALLSRELFTRDMIEDIQQAGSgsRRDQARQLVTDLETRGRQALPLFISCLEDTGQGT 84
Cdd:cd08326    1 HRQILRRHRARLVEELQPKYLWDHLLSRGVFTPDMIEEIQAAGS--RRDQARQLLIDLETRGKQAFPAFLSALRETGQTD 78


                 ....*.
gi 485050375  85 LASLLQ 90
Cdd:cd08326   79 LAELLR 84
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 190-403 5.63e-74

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.


Pssm-ID: 237997  Cd Length: 243  Bit Score: 230.95  E-value: 5.63e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375 190 AYTLDSDPCGHCLIINNVNFCPssGLGTRTGSNLDRDKLEHRFRWLRFMVEVKNDLTAKKMVTALMEMAHRNHRALDCFV 269
Cdd:cd00032    1 IYKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375 270 VVILSHGCQashlqfpGAVYGTDGCSVSIEKIVNIFNGSGCPSLGGKPKLFFIQACGGEQKDHGFEVactssqgrtldsD 349
Cdd:cd00032   79 CVILSHGEE-------GGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEV------------D 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 485050375 350 SEPDAVPYQEGPrplDQLDAVSSLPTPSDILVSYSTFPGcqcCFCERDLQADSW 403
Cdd:cd00032  140 SGADEPPDVETE---AEDDAVQTIPVEADFLVAYSTVPG---YVSWRNTKKGSW 187
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 191-403 9.94e-68

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.


Pssm-ID: 214521  Cd Length: 241  Bit Score: 214.79  E-value: 9.94e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375   191 YTLDSDPCGHCLIINNVNFCpssGLGTRTGSNLDRDKLEHRFRWLRFMVEVKNDLTAKKMVTALMEMAHR-NHRALDCFV 269
Cdd:smart00115   1 YKMNSKPRGLALIINNENFH---SLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMpEHSDSDSFV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375   270 VVILSHGcqashlqFPGAVYGTDGCSVSIEKIVNIFNGSGCPSLGGKPKLFFIQACGGEQKDHGFEVactssqgrtldSD 349
Cdd:smart00115  78 CVLLSHG-------EEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPV-----------ED 139

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 485050375   350 SEPDavpyqeGPRPLDQlDAVSSLPTPSDILVSYSTFPGcqcCFCERDLQADSW 403
Cdd:smart00115 140 SVAD------PESEGED-DAIYKIPVEADFLAAYSTTPG---YVSWRNPTRGSW 183
CARD_CASP9 cd08326
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ...
 5-90 4.92e-41

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.


Pssm-ID: 176740  Cd Length: 84  Bit Score: 139.87  E-value: 4.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375   5 DRQLLRRCRVRLVSELQVAELWDALLSRELFTRDMIEDIQQAGSgsRRDQARQLVTDLETRGRQALPLFISCLEDTGQGT 84
Cdd:cd08326    1 HRQILRRHRARLVEELQPKYLWDHLLSRGVFTPDMIEEIQAAGS--RRDQARQLLIDLETRGKQAFPAFLSALRETGQTD 78


                 ....*.
gi 485050375  85 LASLLQ 90
Cdd:cd08326   79 LAELLR 84
Peptidase_C14 pfam00656
Caspase domain;
199-388 1.99e-39

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 140.15  E-value: 1.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375  199 GHCLIINNVNFCPSSGlgTRTGSNLDRDKLEHRFRWLRFMVEVKNDLTAKKMVTALMEMAHR-NHRALDCFVVVIL---S 274
Cdd:pfam00656   2 GLALIIGNNNYPGTKA--PLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARaDHSDGDSFVVVLLyysG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375  275 HGCQashlQFPGAVYGTDGCSVSIEKIVNIFNGSGC-PSLGGKPKLFFIQACGGEQKDHGfevactssqgrtldsdsepd 353
Cdd:pfam00656  80 HGEQ----VPGGDIYGTDEYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLEDGG-------------------- 135

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 485050375  354 avpyqegprpldqldavsslPTPSDILVSYSTFPG 388
Cdd:pfam00656 136 --------------------VVEADFLVAYSTAPG 150
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 1-89 1.66e-23

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.


Pssm-ID: 128424  Cd Length: 88  Bit Score: 93.56  E-value: 1.66e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375     1 MDEADRQLLRRCRVRLVSELQVAELWDALLSRELFTRDMIEDIQQAGSGSRRDqaRQLVTDLETRGRQALPLFISCLEDT 80
Cdd:smart00114   1 MAERDKRLLRRNRVRLGEELGVDGLLDYLVEKNVLTEKEIEAIKAATTKLRDK--RELVDSLQKRGSQAFDTFLDSLQET 78


                   ....*....
gi 485050375    81 gQGTLASLL 89
Cdd:smart00114  79 -DQKLADFL 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 6-92 5.51e-19

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


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 81.07  E-value: 5.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375    6 RQLLRRCRVRLVSELQ-VAELWDALLSRELFTRDMIEDIQQagSGSRRDQARQLVTDLETRGRQALPLFISCLEDtGQGT 84
Cdd:pfam00619   1 RKLLKKNRVALVERLGtLDGLLDYLLEKNVLTEEEEEKIKA--NPTRLDKARELLDLVLKKGPKACQIFLEALKE-GDPD 77


                  ....*...
gi 485050375   85 LASLLQSG 92
Cdd:pfam00619  78 LASDLEGL 85
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 190-403 5.63e-74

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.


Pssm-ID: 237997  Cd Length: 243  Bit Score: 230.95  E-value: 5.63e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375 190 AYTLDSDPCGHCLIINNVNFCPssGLGTRTGSNLDRDKLEHRFRWLRFMVEVKNDLTAKKMVTALMEMAHRNHRALDCFV 269
Cdd:cd00032    1 IYKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375 270 VVILSHGCQashlqfpGAVYGTDGCSVSIEKIVNIFNGSGCPSLGGKPKLFFIQACGGEQKDHGFEVactssqgrtldsD 349
Cdd:cd00032   79 CVILSHGEE-------GGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEV------------D 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 485050375 350 SEPDAVPYQEGPrplDQLDAVSSLPTPSDILVSYSTFPGcqcCFCERDLQADSW 403
Cdd:cd00032  140 SGADEPPDVETE---AEDDAVQTIPVEADFLVAYSTVPG---YVSWRNTKKGSW 187
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 191-403 9.94e-68

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.


Pssm-ID: 214521  Cd Length: 241  Bit Score: 214.79  E-value: 9.94e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375   191 YTLDSDPCGHCLIINNVNFCpssGLGTRTGSNLDRDKLEHRFRWLRFMVEVKNDLTAKKMVTALMEMAHR-NHRALDCFV 269
Cdd:smart00115   1 YKMNSKPRGLALIINNENFH---SLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMpEHSDSDSFV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375   270 VVILSHGcqashlqFPGAVYGTDGCSVSIEKIVNIFNGSGCPSLGGKPKLFFIQACGGEQKDHGFEVactssqgrtldSD 349
Cdd:smart00115  78 CVLLSHG-------EEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPV-----------ED 139

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 485050375   350 SEPDavpyqeGPRPLDQlDAVSSLPTPSDILVSYSTFPGcqcCFCERDLQADSW 403
Cdd:smart00115 140 SVAD------PESEGED-DAIYKIPVEADFLAAYSTTPG---YVSWRNPTRGSW 183
CARD_CASP9 cd08326
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ...
 5-90 4.92e-41

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.


Pssm-ID: 176740  Cd Length: 84  Bit Score: 139.87  E-value: 4.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375   5 DRQLLRRCRVRLVSELQVAELWDALLSRELFTRDMIEDIQQAGSgsRRDQARQLVTDLETRGRQALPLFISCLEDTGQGT 84
Cdd:cd08326    1 HRQILRRHRARLVEELQPKYLWDHLLSRGVFTPDMIEEIQAAGS--RRDQARQLLIDLETRGKQAFPAFLSALRETGQTD 78


                 ....*.
gi 485050375  85 LASLLQ 90
Cdd:cd08326   79 LAELLR 84
Peptidase_C14 pfam00656
Caspase domain;
199-388 1.99e-39

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 140.15  E-value: 1.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375  199 GHCLIINNVNFCPSSGlgTRTGSNLDRDKLEHRFRWLRFMVEVKNDLTAKKMVTALMEMAHR-NHRALDCFVVVIL---S 274
Cdd:pfam00656   2 GLALIIGNNNYPGTKA--PLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARaDHSDGDSFVVVLLyysG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375  275 HGCQashlQFPGAVYGTDGCSVSIEKIVNIFNGSGC-PSLGGKPKLFFIQACGGEQKDHGfevactssqgrtldsdsepd 353
Cdd:pfam00656  80 HGEQ----VPGGDIYGTDEYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLEDGG-------------------- 135

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 485050375  354 avpyqegprpldqldavsslPTPSDILVSYSTFPG 388
Cdd:pfam00656 136 --------------------VVEADFLVAYSTAPG 150
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 1-89 1.66e-23

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.


Pssm-ID: 128424  Cd Length: 88  Bit Score: 93.56  E-value: 1.66e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375     1 MDEADRQLLRRCRVRLVSELQVAELWDALLSRELFTRDMIEDIQQAGSGSRRDqaRQLVTDLETRGRQALPLFISCLEDT 80
Cdd:smart00114   1 MAERDKRLLRRNRVRLGEELGVDGLLDYLVEKNVLTEKEIEAIKAATTKLRDK--RELVDSLQKRGSQAFDTFLDSLQET 78


                   ....*....
gi 485050375    81 gQGTLASLL 89
Cdd:smart00114  79 -DQKLADFL 86
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 9-89 1.27e-19

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.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 82.56  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375   9 LRRCRVRLVSELQVAELWDALLSRELFTRDMIEDIQQAgsGSRRDQARQLVTDLETRGRQALPLFISCLEDTGQGTLASL 88
Cdd:cd01671    1 LRKNRVELVEDLDVEDILDHLIQKGVLTEEDKEEILSE--KTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPHLAEL 78


                 .
gi 485050375  89 L 89
Cdd:cd01671   79 L 79
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 6-92 5.51e-19

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


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 81.07  E-value: 5.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375    6 RQLLRRCRVRLVSELQ-VAELWDALLSRELFTRDMIEDIQQagSGSRRDQARQLVTDLETRGRQALPLFISCLEDtGQGT 84
Cdd:pfam00619   1 RKLLKKNRVALVERLGtLDGLLDYLLEKNVLTEEEEEKIKA--NPTRLDKARELLDLVLKKGPKACQIFLEALKE-GDPD 77


                  ....*...
gi 485050375   85 LASLLQSG 92
Cdd:pfam00619  78 LASDLEGL 85
DD cd08304
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 13-89 6.78e-13

Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. 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. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.


Pssm-ID: 176720  Cd Length: 69  Bit Score: 63.34  E-value: 6.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375  13 RVRLVSEL---QVAELWDALLSRelFTRDMIEDIqqagsgsrrDQARQLVTDLETRGRQALPLFISCLEDTGQGTLASLL 89
Cdd:cd08304    1 RLDLCENLtleVLQQLKTALKSR--IPPDQVEQI---------SAANELLNILESQYNHTLQLLFALFEDLGLHNLARLL 69
CARD_CASP2 cd08332
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ...
 1-89 7.73e-11

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.


Pssm-ID: 260040  Cd Length: 87  Bit Score: 58.20  E-value: 7.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375   1 MDEADRQLLRRCRVRLVSELQVAELWDALLSRELFTRDMIEDIQqaGSGSRRDQARQLVTDLETRGRQALPLFISCLEDT 80
Cdd:cd08332    1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIM--AKPTSFSQNVALLNLLPKRGPRAFSAFCEALRET 78


                 ....*....
gi 485050375  81 GQGTLASLL 89
Cdd:cd08332   79 SQEHLADLL 87
CARD_RAIDD cd08327
Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a ...
 1-79 2.12e-06

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.


Pssm-ID: 260037  Cd Length: 94  Bit Score: 45.53  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485050375   1 MDEADRQLLRRCRVRLVSELQVAEL-WDALLSRELFTRDMIEDIQQAGSGSRRdqARQLVTDLETRGRQALPLFISCLED 79
Cdd:cd08327    1 MEPKHKQLLRSQRLELCAELLVDGLiVQYLYQEGILTESHVEEIQSQTTSRRK--TLKLLDILPNRGPKAFHAFLDSLEE 78
CARD_BCL10 cd08810
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ...
 7-81 1.58e-03

Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and recruitment domain (CARD) similar to that found in BCL10 (B-cell lymphoma 10). BCL10 and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1) are the integral components of CBM signalosomes. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells) and with CARMA1 to form L-CBM (CBM complex in lymphoid immune cells), to mediate activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. Both CARMA1 and CARD9 associate with BCL10 via 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.


Pssm-ID: 260072 [Multi-domain]  Cd Length: 85  Bit Score: 37.33  E-value: 1.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485050375   7 QLLRRCRVRLVSELQVAELWDALLSRELFTRDMIEDIQQAgsGSRRDQARQLVTDLETRGRQALPLFISCLEDTG 81
Cdd:cd08810    3 EVLEEQRHYLCDKLIADRHFDYLRSKRILTRDDCEEIQCR--TTRKKRVDKLLDILAREGPDGLDALIESIRRNG 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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