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Conserved domains on  [gi|4502577|ref|NP_001216|]
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caspase-4 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 ...
 126-375 6.95e-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: 344.22  E-value: 6.95e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577     126 YPIKERNnrTRLALIICNTEFDHLPPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATRPEHKSSDSTFL 205
Cdd:smart00115   1 YKMNSKP--RGLALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577     206 VLMSHGILEGICGTVHdekkpDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRG-ANRGELWVRDSPASLEvassqssE 284
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGdELDGGVPVEDSVADPE-------S 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577     285 NLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPR----AKAQMP 360
Cdd:smart00115 147 EGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFesvnAKKQMP 226

                          250
                   ....*....|....*
gi 4502577     361 TIERLSMTRYFYLFP 375
Cdd:smart00115 227 TIESMTLTKKLYFFP 241
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
 5-81 2.03e-28

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: 106.14  E-value: 2.03e-28
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4502577    5 NHRKKPLKVLESLGKDFLTGVLDNLVEQNVLNWKEEEKKKYYDAKTEDKVRVMADSMQEKQRMAGQMLLQTFFNIDQ 81
Cdd:cd08325   1 RLKEKRVKFVESVGKGVINGLLDDLLEKNVLNEEEMEKIKEENNTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDK 77
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 126-375 6.95e-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: 344.22  E-value: 6.95e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577     126 YPIKERNnrTRLALIICNTEFDHLPPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATRPEHKSSDSTFL 205
Cdd:smart00115   1 YKMNSKP--RGLALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577     206 VLMSHGILEGICGTVHdekkpDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRG-ANRGELWVRDSPASLEvassqssE 284
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGdELDGGVPVEDSVADPE-------S 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577     285 NLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPR----AKAQMP 360
Cdd:smart00115 147 EGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFesvnAKKQMP 226

                          250
                   ....*....|....*
gi 4502577     361 TIERLSMTRYFYLFP 375
Cdd:smart00115 227 TIESMTLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 125-374 1.07e-96

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: 287.96  E-value: 1.07e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577  125 IYPIKERnnRTRLALIICNTEFDH-LPPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATrPEHKSSDST 203
Cdd:cd00032   1 IYKMNSK--RRGLALIINNENFDKgLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577  204 FLVLMSHGILEGICGTVHDekkpdVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGANRGELWVRDSPASLEVASSqss 283
Cdd:cd00032  78 VCVILSHGEEGGIYGTDGD-----VVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPDVE--- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577  284 ENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPR----AKAQM 359
Cdd:cd00032 150 TEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFesvnGKKQM 229

                       250
                ....*....|....*
gi 4502577  360 PTIeRLSMTRYFYLF 374
Cdd:cd00032 230 PCF-RSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
135-372 3.45e-69

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 216.42  E-value: 3.45e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577    135 TRLALIICNTEFDHL-PPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATRPEHKSSDSTFLVLM---SH 210
Cdd:pfam00656   1 RGLALIIGNNNYPGTkAPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577    211 GIlEGICGTVHDeKKPDVLLYDTIFQIFNNRNCL-SLKDKPKVIIVQACRGanrgelwvrdspaslevassqsseNLEED 289
Cdd:pfam00656  81 GE-QVPGGDIYG-TDEYLVPVDALTNLFTGDDCLpSLVGKPKLFIIDACRG------------------------NLEDG 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577    290 AVykthVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPRAKAQMPTIERLSMTR 369
Cdd:pfam00656 135 GV----VEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEATGKKQMPCLSSSTLTK 210


                  ...
gi 4502577    370 YFY 372
Cdd:pfam00656 211 KFY 213
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
 5-81 2.03e-28

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: 106.14  E-value: 2.03e-28
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4502577    5 NHRKKPLKVLESLGKDFLTGVLDNLVEQNVLNWKEEEKKKYYDAKTEDKVRVMADSMQEKQRMAGQMLLQTFFNIDQ 81
Cdd:cd08325   1 RLKEKRVKFVESVGKGVINGLLDDLLEKNVLNEEEMEKIKEENNTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDK 77
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 1-89 1.75e-22

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: 90.47  E-value: 1.75e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577       1 MAE---GNHRKKPLKVLESLGKDfltGVLDNLVEQNVLNWKEEEKKKYYDAKTEDKvRVMADSMQEKQRMAGQMLLQTFF 77
Cdd:smart00114   1 MAErdkRLLRRNRVRLGEELGVD---GLLDYLVEKNVLTEKEIEAIKAATTKLRDK-RELVDSLQKRGSQAFDTFLDSLQ 76

                           90
                   ....*....|..
gi 4502577      78 NIDQISPNKKAH 89
Cdd:smart00114  77 ETDQKLADFLEL 88
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 6-81 1.47e-12

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: 62.58  E-value: 1.47e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4502577      6 HRKKPLKVLESLGkdFLTGVLDNLVEQNVLNWKEEEKKKYyDAKTEDKVRVMADSMQEKQRMAGQMLLQTFFNIDQ 81
Cdd:pfam00619   4 LKKNRVALVERLG--TLDGLLDYLLEKNVLTEEEEEKIKA-NPTRLDKARELLDLVLKKGPKACQIFLEALKEGDP 76
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 126-375 6.95e-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: 344.22  E-value: 6.95e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577     126 YPIKERNnrTRLALIICNTEFDHLPPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATRPEHKSSDSTFL 205
Cdd:smart00115   1 YKMNSKP--RGLALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577     206 VLMSHGILEGICGTVHdekkpDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRG-ANRGELWVRDSPASLEvassqssE 284
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGdELDGGVPVEDSVADPE-------S 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577     285 NLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPR----AKAQMP 360
Cdd:smart00115 147 EGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFesvnAKKQMP 226

                          250
                   ....*....|....*
gi 4502577     361 TIERLSMTRYFYLFP 375
Cdd:smart00115 227 TIESMTLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 125-374 1.07e-96

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: 287.96  E-value: 1.07e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577  125 IYPIKERnnRTRLALIICNTEFDH-LPPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATrPEHKSSDST 203
Cdd:cd00032   1 IYKMNSK--RRGLALIINNENFDKgLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577  204 FLVLMSHGILEGICGTVHDekkpdVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGANRGELWVRDSPASLEVASSqss 283
Cdd:cd00032  78 VCVILSHGEEGGIYGTDGD-----VVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPDVE--- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577  284 ENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPR----AKAQM 359
Cdd:cd00032 150 TEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFesvnGKKQM 229

                       250
                ....*....|....*
gi 4502577  360 PTIeRLSMTRYFYLF 374
Cdd:cd00032 230 PCF-RSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
135-372 3.45e-69

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 216.42  E-value: 3.45e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577    135 TRLALIICNTEFDHL-PPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATRPEHKSSDSTFLVLM---SH 210
Cdd:pfam00656   1 RGLALIIGNNNYPGTkAPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577    211 GIlEGICGTVHDeKKPDVLLYDTIFQIFNNRNCL-SLKDKPKVIIVQACRGanrgelwvrdspaslevassqsseNLEED 289
Cdd:pfam00656  81 GE-QVPGGDIYG-TDEYLVPVDALTNLFTGDDCLpSLVGKPKLFIIDACRG------------------------NLEDG 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577    290 AVykthVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPRAKAQMPTIERLSMTR 369
Cdd:pfam00656 135 GV----VEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEATGKKQMPCLSSSTLTK 210


                  ...
gi 4502577    370 YFY 372
Cdd:pfam00656 211 KFY 213
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
 5-81 2.03e-28

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: 106.14  E-value: 2.03e-28
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4502577    5 NHRKKPLKVLESLGKDFLTGVLDNLVEQNVLNWKEEEKKKYYDAKTEDKVRVMADSMQEKQRMAGQMLLQTFFNIDQ 81
Cdd:cd08325   1 RLKEKRVKFVESVGKGVINGLLDDLLEKNVLNEEEMEKIKEENNTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDK 77
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 1-89 1.75e-22

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: 90.47  E-value: 1.75e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502577       1 MAE---GNHRKKPLKVLESLGKDfltGVLDNLVEQNVLNWKEEEKKKYYDAKTEDKvRVMADSMQEKQRMAGQMLLQTFF 77
Cdd:smart00114   1 MAErdkRLLRRNRVRLGEELGVD---GLLDYLVEKNVLTEKEIEAIKAATTKLRDK-RELVDSLQKRGSQAFDTFLDSLQ 76

                           90
                   ....*....|..
gi 4502577      78 NIDQISPNKKAH 89
Cdd:smart00114  77 ETDQKLADFLEL 88
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 6-81 1.47e-12

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: 62.58  E-value: 1.47e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4502577      6 HRKKPLKVLESLGkdFLTGVLDNLVEQNVLNWKEEEKKKYyDAKTEDKVRVMADSMQEKQRMAGQMLLQTFFNIDQ 81
Cdd:pfam00619   4 LKKNRVALVERLG--TLDGLLDYLLEKNVLTEEEEEKIKA-NPTRLDKARELLDLVLKKGPKACQIFLEALKEGDP 76
 
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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