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Conserved domains on  [gi|15431328|ref|NP_150634|]
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caspase-1 isoform alpha precursor [Homo sapiens]

Protein Classification

caspase family protein( domain architecture ID 10871135)

caspase family protein similar to caspases which are cysteine class enzymes that drive the terminal stages of apoptosis as well as other cellular remodeling and inflammatory events

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
153-402 2.28e-119

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: 346.53  E-value: 2.28e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328    153 YPIMDKssRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFL 232
Cdd:smart00115   1 YKMNSK--PRGLALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328    233 VFMSHGIREGICGKKHseqvpDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDS-PGVVWFKDSVGvsgnlslPTTE 311
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDElDGGVPVEDSVA-------DPES 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328    312 EFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDG----RAQMP 387
Cdd:smart00115 147 EGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFEsvnaKKQMP 226
                          250
                   ....*....|....*
gi 15431328    388 TTERVTLTRCFYLFP 402
Cdd:smart00115 227 TIESMTLTKKLYFFP 241
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
5-87 3.54e-34

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.


:

Pssm-ID: 260036  Cd Length: 83  Bit Score: 121.93  E-value: 3.54e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328   5 VLKEKRKLFIRSMGEGTINGLLDELLQTRVLNKEEMEKVKRENATVMDKTRALIDSVIPKGAQACQICITYICEEDSYLA 84
Cdd:cd08325   1 RLKEKRVKFVESVGKGVINGLLDDLLEKNVLNEEEMEKIKEENNTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDKQLS 80

                ...
gi 15431328  85 GTL 87
Cdd:cd08325  81 SKL 83
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
153-402 2.28e-119

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: 346.53  E-value: 2.28e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328    153 YPIMDKssRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFL 232
Cdd:smart00115   1 YKMNSK--PRGLALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328    233 VFMSHGIREGICGKKHseqvpDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDS-PGVVWFKDSVGvsgnlslPTTE 311
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDElDGGVPVEDSVA-------DPES 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328    312 EFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDG----RAQMP 387
Cdd:smart00115 147 EGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFEsvnaKKQMP 226
                          250
                   ....*....|....*
gi 15431328    388 TTERVTLTRCFYLFP 402
Cdd:smart00115 227 TIESMTLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
152-401 4.96e-102

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: 302.60  E-value: 4.96e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328 152 IYPIMDKssRTRLALIICNEEFDSI-PRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAhRPEHKTSDST 230
Cdd:cd00032   1 IYKMNSK--RRGLALIINNENFDKGlKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFA-SPDHSDSDSF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328 231 FLVFMSHGIREGICGKKHseqvpDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDSPGVVWFKDSVGVSGNlslPTT 310
Cdd:cd00032  78 VCVILSHGEEGGIYGTDG-----DVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPP---DVE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328 311 EEFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQP----DGRAQM 386
Cdd:cd00032 150 TEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKfesvNGKKQM 229
                       250
                ....*....|....*
gi 15431328 387 PTTeRVTLTRCFYLF 401
Cdd:cd00032 230 PCF-RSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
162-399 8.85e-71

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 221.43  E-value: 8.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328   162 TRLALIICNEEF-DSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFLVFM---SH 237
Cdd:pfam00656   1 RGLALIIGNNNYpGTKAPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328   238 GIREGiCGKKHSEQvPDILQLNAIFNMLNTKNC-PSLKDKPKVIIIQACRGDSPGvvwfkdsvgvsgnlslptteefedd 316
Cdd:pfam00656  81 GEQVP-GGDIYGTD-EYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLED------------------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328   317 aikKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDGRAQMPTTERVTLTR 396
Cdd:pfam00656 134 ---GGVVEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEATGKKQMPCLSSSTLTK 210

                  ...
gi 15431328   397 CFY 399
Cdd:pfam00656 211 KFY 213
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
5-87 3.54e-34

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.


Pssm-ID: 260036  Cd Length: 83  Bit Score: 121.93  E-value: 3.54e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328   5 VLKEKRKLFIRSMGEGTINGLLDELLQTRVLNKEEMEKVKRENATVMDKTRALIDSVIPKGAQACQICITYICEEDSYLA 84
Cdd:cd08325   1 RLKEKRVKFVESVGKGVINGLLDDLLEKNVLNEEEMEKIKEENNTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDKQLS 80

                ...
gi 15431328  85 GTL 87
Cdd:cd08325  81 SKL 83
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
3-90 3.07e-25

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: 98.02  E-value: 3.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328     3 DKVLKEKRKLFIRSMGegTINGLLDELLQTRVLNKEEMEKVKrENATVMDKTRALIDSVIPKGAQACQICITYICEEDSY 82
Cdd:pfam00619   1 RKLLKKNRVALVERLG--TLDGLLDYLLEKNVLTEEEEEKIK-ANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77

                  ....*...
gi 15431328    83 LAGTLGLS 90
Cdd:pfam00619  78 LASDLEGL 85
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
8-89 1.57e-09

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: 54.27  E-value: 1.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328      8 EKRKLFIRSMGEGTING---LLDELLQTRVLNKEEMEKVKRENATVMDKtRALIDSVIPKGAQACQICITYICEEDSYLA 84
Cdd:smart00114   5 DKRLLRRNRVRLGEELGvdgLLDYLVEKNVLTEKEIEAIKAATTKLRDK-RELVDSLQKRGSQAFDTFLDSLQETDQKLA 83

                   ....*
gi 15431328     85 GTLGL 89
Cdd:smart00114  84 DFLEL 88
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
153-402 2.28e-119

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: 346.53  E-value: 2.28e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328    153 YPIMDKssRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFL 232
Cdd:smart00115   1 YKMNSK--PRGLALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328    233 VFMSHGIREGICGKKHseqvpDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDS-PGVVWFKDSVGvsgnlslPTTE 311
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDElDGGVPVEDSVA-------DPES 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328    312 EFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDG----RAQMP 387
Cdd:smart00115 147 EGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFEsvnaKKQMP 226
                          250
                   ....*....|....*
gi 15431328    388 TTERVTLTRCFYLFP 402
Cdd:smart00115 227 TIESMTLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
152-401 4.96e-102

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: 302.60  E-value: 4.96e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328 152 IYPIMDKssRTRLALIICNEEFDSI-PRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAhRPEHKTSDST 230
Cdd:cd00032   1 IYKMNSK--RRGLALIINNENFDKGlKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFA-SPDHSDSDSF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328 231 FLVFMSHGIREGICGKKHseqvpDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDSPGVVWFKDSVGVSGNlslPTT 310
Cdd:cd00032  78 VCVILSHGEEGGIYGTDG-----DVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPP---DVE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328 311 EEFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQP----DGRAQM 386
Cdd:cd00032 150 TEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKfesvNGKKQM 229
                       250
                ....*....|....*
gi 15431328 387 PTTeRVTLTRCFYLF 401
Cdd:cd00032 230 PCF-RSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
162-399 8.85e-71

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 221.43  E-value: 8.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328   162 TRLALIICNEEF-DSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFLVFM---SH 237
Cdd:pfam00656   1 RGLALIIGNNNYpGTKAPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328   238 GIREGiCGKKHSEQvPDILQLNAIFNMLNTKNC-PSLKDKPKVIIIQACRGDSPGvvwfkdsvgvsgnlslptteefedd 316
Cdd:pfam00656  81 GEQVP-GGDIYGTD-EYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLED------------------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328   317 aikKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDGRAQMPTTERVTLTR 396
Cdd:pfam00656 134 ---GGVVEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEATGKKQMPCLSSSTLTK 210

                  ...
gi 15431328   397 CFY 399
Cdd:pfam00656 211 KFY 213
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
5-87 3.54e-34

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.


Pssm-ID: 260036  Cd Length: 83  Bit Score: 121.93  E-value: 3.54e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328   5 VLKEKRKLFIRSMGEGTINGLLDELLQTRVLNKEEMEKVKRENATVMDKTRALIDSVIPKGAQACQICITYICEEDSYLA 84
Cdd:cd08325   1 RLKEKRVKFVESVGKGVINGLLDDLLEKNVLNEEEMEKIKEENNTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDKQLS 80

                ...
gi 15431328  85 GTL 87
Cdd:cd08325  81 SKL 83
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
3-90 3.07e-25

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: 98.02  E-value: 3.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328     3 DKVLKEKRKLFIRSMGegTINGLLDELLQTRVLNKEEMEKVKrENATVMDKTRALIDSVIPKGAQACQICITYICEEDSY 82
Cdd:pfam00619   1 RKLLKKNRVALVERLG--TLDGLLDYLLEKNVLTEEEEEKIK-ANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77

                  ....*...
gi 15431328    83 LAGTLGLS 90
Cdd:pfam00619  78 LASDLEGL 85
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
8-89 1.57e-09

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: 54.27  E-value: 1.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431328      8 EKRKLFIRSMGEGTING---LLDELLQTRVLNKEEMEKVKRENATVMDKtRALIDSVIPKGAQACQICITYICEEDSYLA 84
Cdd:smart00114   5 DKRLLRRNRVRLGEELGvdgLLDYLVEKNVLTEKEIEAIKAATTKLRDK-RELVDSLQKRGSQAFDTFLDSLQETDQKLA 83

                   ....*
gi 15431328     85 GTLGL 89
Cdd:smart00114  84 DFLEL 88
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
6-73 1.46e-07

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: 48.67  E-value: 1.46e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15431328   6 LKEKRKLFIRSMgegTINGLLDELLQTRVLNKEEMEKVKRENaTVMDKTRALIDSVIPKGAQACQICI 73
Cdd:cd01671   1 LRKNRVELVEDL---DVEDILDHLIQKGVLTEEDKEEILSEK-TRQDKARKLLDILPRRGPKAFEVFC 64
CARD_RIP2_CARD3 cd08786
Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase ...
4-74 9.02e-06

Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase activation and recruitment domain (CARD) of Receptor Interacting Protein 2 (RIP2/RIPK2/RICK/CARDIAK/CARD3). RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP2 harbors a C-terminal CARD domain and functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR)-family, NOD1 and NOD2, which recognizes bacterial peptidoglycans released upon infection. This cascade is implicated in inflammatory immune responses and the clearance of intracellular pathogens. RIP2 associates with NOD1 and NOD2 via CARD-CARD interactions. 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: 176764  Cd Length: 87  Bit Score: 43.76  E-value: 9.02e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15431328   4 KVLKEKRKLFIRSMGEGTINGLLDELLQTRVLNKEEMEKVKREnATVMDKTRALIDSVIPKGAQACQICIT 74
Cdd:cd08786   1 QWIASKREEIVSQMTEACLNQSLDALLSRQLLMREDYELISTK-PTRTSKVRQLLDTCDCQGEEFARVVVQ 70
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
25-83 1.07e-04

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.


Pssm-ID: 260038  Cd Length: 94  Bit Score: 40.89  E-value: 1.07e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15431328  25 LLDELLQTRVLNKEEMEKVKRENATVMdKTRALIDSVIPKGAQACQICITYICEEDSYL 83
Cdd:cd08329  28 ILDHLLSANVITEQEYDVIKQKTQTPL-QARELIDTILVKGNAAAEVFRNCLKEIDVVL 85
 
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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