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Conserved domains on  [gi|2217284932|ref|XP_016873883|]
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caspase-1 isoform X1 [Homo sapiens]

Protein Classification

caspase family protein( domain architecture ID 10971925)

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 ...
 197-446 1.49e-118

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: 346.15  E-value: 1.49e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932  197 YPIMDKssRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFL 276
Cdd:smart00115   1 YKMNSK--PRGLALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932  277 VFMSHGIREGICGKKHseqvpDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDS-PGVVWFKDSVGvsgnlslPTTE 355
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDElDGGVPVEDSVA-------DPES 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932  356 EFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDG----RAQMP 431
Cdd:smart00115 147 EGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFEsvnaKKQMP 226

                          250
                   ....*....|....*
gi 2217284932  432 TTERVTLTRCFYLFP 446
Cdd:smart00115 227 TIESMTLTKKLYFFP 241
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 77-131 1.69e-21

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.


The actual alignment was detected with superfamily member cd08325:

Pssm-ID: 472698  Cd Length: 83  Bit Score: 88.03  E-value: 1.69e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217284932  77 RVLNKEEMEKVKRENATVMDKTRALIDSVIPKGAQACQICITYICEEDSYLAGTL 131
Cdd:cd08325    29 NVLNEEEMEKIKEENNTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDKQLSSKL 83
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 197-446 1.49e-118

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: 346.15  E-value: 1.49e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932  197 YPIMDKssRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFL 276
Cdd:smart00115   1 YKMNSK--PRGLALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932  277 VFMSHGIREGICGKKHseqvpDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDS-PGVVWFKDSVGvsgnlslPTTE 355
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDElDGGVPVEDSVA-------DPES 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932  356 EFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDG----RAQMP 431
Cdd:smart00115 147 EGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFEsvnaKKQMP 226

                          250
                   ....*....|....*
gi 2217284932  432 TTERVTLTRCFYLFP 446
Cdd:smart00115 227 TIESMTLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 196-445 1.02e-101

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: 303.37  E-value: 1.02e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932 196 IYPIMDKssRTRLALIICNEEFDSI-PRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAhRPEHKTSDST 274
Cdd:cd00032     1 IYKMNSK--RRGLALIINNENFDKGlKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFA-SPDHSDSDSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932 275 FLVFMSHGIREGICGKKHseqvpDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDSPGVVWFKDSVGVSGNlslPTT 354
Cdd:cd00032    78 VCVILSHGEEGGIYGTDG-----DVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPP---DVE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932 355 EEFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQP----DGRAQM 430
Cdd:cd00032   150 TEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKfesvNGKKQM 229

                         250
                  ....*....|....*
gi 2217284932 431 PTTeRVTLTRCFYLF 445
Cdd:cd00032   230 PCF-RSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
206-443 3.08e-70

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 221.43  E-value: 3.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932 206 TRLALIICNEEF-DSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFLVFM---SH 281
Cdd:pfam00656   1 RGLALIIGNNNYpGTKAPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932 282 GIREGiCGKKHSEQvPDILQLNAIFNMLNTKNC-PSLKDKPKVIIIQACRGDSPGvvwfkdsvgvsgnlslptteefedd 360
Cdd:pfam00656  81 GEQVP-GGDIYGTD-EYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLED------------------------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932 361 aikKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDGRAQMPTTERVTLTR 440
Cdd:pfam00656 134 ---GGVVEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEATGKKQMPCLSSSTLTK 210


                  ...
gi 2217284932 441 CFY 443
Cdd:pfam00656 211 KFY 213
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
 77-131 1.69e-21

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: 88.03  E-value: 1.69e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217284932  77 RVLNKEEMEKVKRENATVMDKTRALIDSVIPKGAQACQICITYICEEDSYLAGTL 131
Cdd:cd08325    29 NVLNEEEMEKIKEENNTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDKQLSSKL 83
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 77-134 1.44e-15

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: 71.44  E-value: 1.44e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217284932  77 RVLNKEEMEKVKrENATVMDKTRALIDSVIPKGAQACQICITYICEEDSYLAGTLGLS 134
Cdd:pfam00619  29 NVLTEEEEEKIK-ANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLASDLEGL 85
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 78-133 6.97e-06

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: 44.25  E-value: 6.97e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217284932   78 VLNKEEMEKVKRENATVMDKtRALIDSVIPKGAQACQICITYICEEDSYLAGTLGL 133
Cdd:smart00114  34 VLTEKEIEAIKAATTKLRDK-RELVDSLQKRGSQAFDTFLDSLQETDQKLADFLEL 88
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 197-446 1.49e-118

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: 346.15  E-value: 1.49e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932  197 YPIMDKssRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFL 276
Cdd:smart00115   1 YKMNSK--PRGLALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932  277 VFMSHGIREGICGKKHseqvpDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDS-PGVVWFKDSVGvsgnlslPTTE 355
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDElDGGVPVEDSVA-------DPES 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932  356 EFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDG----RAQMP 431
Cdd:smart00115 147 EGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFEsvnaKKQMP 226

                          250
                   ....*....|....*
gi 2217284932  432 TTERVTLTRCFYLFP 446
Cdd:smart00115 227 TIESMTLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 196-445 1.02e-101

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: 303.37  E-value: 1.02e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932 196 IYPIMDKssRTRLALIICNEEFDSI-PRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAhRPEHKTSDST 274
Cdd:cd00032     1 IYKMNSK--RRGLALIINNENFDKGlKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFA-SPDHSDSDSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932 275 FLVFMSHGIREGICGKKHseqvpDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDSPGVVWFKDSVGVSGNlslPTT 354
Cdd:cd00032    78 VCVILSHGEEGGIYGTDG-----DVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPP---DVE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932 355 EEFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQP----DGRAQM 430
Cdd:cd00032   150 TEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKfesvNGKKQM 229

                         250
                  ....*....|....*
gi 2217284932 431 PTTeRVTLTRCFYLF 445
Cdd:cd00032   230 PCF-RSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
206-443 3.08e-70

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 221.43  E-value: 3.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932 206 TRLALIICNEEF-DSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFLVFM---SH 281
Cdd:pfam00656   1 RGLALIIGNNNYpGTKAPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932 282 GIREGiCGKKHSEQvPDILQLNAIFNMLNTKNC-PSLKDKPKVIIIQACRGDSPGvvwfkdsvgvsgnlslptteefedd 360
Cdd:pfam00656  81 GEQVP-GGDIYGTD-EYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLED------------------------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284932 361 aikKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDGRAQMPTTERVTLTR 440
Cdd:pfam00656 134 ---GGVVEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEATGKKQMPCLSSSTLTK 210


                  ...
gi 2217284932 441 CFY 443
Cdd:pfam00656 211 KFY 213
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
 77-131 1.69e-21

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: 88.03  E-value: 1.69e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217284932  77 RVLNKEEMEKVKRENATVMDKTRALIDSVIPKGAQACQICITYICEEDSYLAGTL 131
Cdd:cd08325    29 NVLNEEEMEKIKEENNTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDKQLSSKL 83
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 77-134 1.44e-15

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: 71.44  E-value: 1.44e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217284932  77 RVLNKEEMEKVKrENATVMDKTRALIDSVIPKGAQACQICITYICEEDSYLAGTLGLS 134
Cdd:pfam00619  29 NVLTEEEEEKIK-ANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLASDLEGL 85
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 78-133 6.97e-06

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: 44.25  E-value: 6.97e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217284932   78 VLNKEEMEKVKRENATVMDKtRALIDSVIPKGAQACQICITYICEEDSYLAGTLGL 133
Cdd:smart00114  34 VLTEKEIEAIKAATTKLRDK-RELVDSLQKRGSQAFDTFLDSLQETDQKLADFLEL 88
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 77-131 5.44e-03

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: 35.57  E-value: 5.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217284932  77 RVLNKEEMEKVKRENaTVMDKTRALIDSVIPKGAQACQICITyICEED--SYLAGTL 131
Cdd:cd01671    25 GVLTEEDKEEILSEK-TRQDKARKLLDILPRRGPKAFEVFCE-ALRETgqPHLAELL 79
 
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.
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