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Conserved domains on  [gi|2493534|sp|O08736|]
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RecName: Full=Caspase-12; Short=CASP-12; Flags: Precursor

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 ...
 166-417 1.92e-110

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: 324.19  E-value: 1.92e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534     166 YPVMEKEGRtrLALIICNKKFDYLFDRDNADTDILNMQELLENLGYSVVLKENLTAQEMETELMQFAGRPEHQSSDSTFL 245
Cdd:smart00115   1 YKMNSKPRG--LALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534     246 VFMSHGILEGICGVKHrnkkpDVLHDDTIFKIFNNSNCRSLRNKPKILIMQACRG-RYNGTIWVSTNKGIATADTDEerv 324
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGdELDGGVPVEDSVADPESEGED--- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534     325 lsckwnNSITKAHVETDFIAFKSSTPHNISWKVGKTGSLFISKLIDCFKKYCWCYHLEEIFRKVQHSFEVPGE----LTQ 400
Cdd:smart00115 151 ------DAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFEsvnaKKQ 224

                          250
                   ....*....|....*..
gi 2493534     401 MPTIERVSMTRYFYLFP 417
Cdd:smart00115 225 MPTIESMTLTKKLYFFP 241
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
 6-88 4.11e-26

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: 100.36  E-value: 4.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534    6 THERDPIYKIKGLAKDMLDGVFDDLVEKNVLNGDELLKIGESASFILNKAENLVENFLEKTDMAGKIFAGHIANSQEQLS 85
Cdd:cd08325   1 RLKEKRVKFVESVGKGVINGLLDDLLEKNVLNEEEMEKIKEENNTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDKQLS 80


                ...
gi 2493534   86 LQF 88
Cdd:cd08325  81 SKL 83
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 166-417 1.92e-110

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: 324.19  E-value: 1.92e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534     166 YPVMEKEGRtrLALIICNKKFDYLFDRDNADTDILNMQELLENLGYSVVLKENLTAQEMETELMQFAGRPEHQSSDSTFL 245
Cdd:smart00115   1 YKMNSKPRG--LALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534     246 VFMSHGILEGICGVKHrnkkpDVLHDDTIFKIFNNSNCRSLRNKPKILIMQACRG-RYNGTIWVSTNKGIATADTDEerv 324
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGdELDGGVPVEDSVADPESEGED--- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534     325 lsckwnNSITKAHVETDFIAFKSSTPHNISWKVGKTGSLFISKLIDCFKKYCWCYHLEEIFRKVQHSFEVPGE----LTQ 400
Cdd:smart00115 151 ------DAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFEsvnaKKQ 224

                          250
                   ....*....|....*..
gi 2493534     401 MPTIERVSMTRYFYLFP 417
Cdd:smart00115 225 MPTIESMTLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 165-416 1.19e-90

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: 274.09  E-value: 1.19e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534  165 IYPVMEKegRTRLALIICNKKFDY-LFDRDNADTDILNMQELLENLGYSVVLKENLTAQEMETELMQFAgRPEHQSSDST 243
Cdd:cd00032   1 IYKMNSK--RRGLALIINNENFDKgLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFA-SPDHSDSDSF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534  244 FLVFMSHGILEGICGVKHrnkkpDVLHDDTIFKIFNNSNCRSLRNKPKILIMQACRGRYNGTIWVSTNKGIATADTDEEr 323
Cdd:cd00032  78 VCVILSHGEEGGIYGTDG-----DVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPDVETE- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534  324 vlscKWNNSITKAHVETDFIAFKSSTPHNISWKVGKTGSLFISKLIDCFKKYCWCYHLEEIFRKVQHSFEVPGE----LT 399
Cdd:cd00032 152 ----AEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFEsvngKK 227

                       250
                ....*....|....*..
gi 2493534  400 QMPTIeRVSMTRYFYLF 416
Cdd:cd00032 228 QMPCF-RSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
175-414 2.85e-62

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 200.24  E-value: 2.85e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534    175 TRLALIICNKKFDYLF-DRDNADTDILNMQELLENLGYSVVLKENLTAQEMETELMQFAGRPEHQSSDSTFLVFM---SH 250
Cdd:pfam00656   1 RGLALIIGNNNYPGTKaPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534    251 GILEGicGVKHRNKKPDVLHDDTIFKIFNNSNC-RSLRNKPKILIMQACRGryngtiwvstnkgiatadtdeervlsckw 329
Cdd:pfam00656  81 GEQVP--GGDIYGTDEYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRG----------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534    330 nNSITKAHVETDFIAFKSSTPHNISWKVGKTGSLFISKLIDCFKKYCWCYHLEEIFRKVQHSFEVPGELTQMPTIERVSM 409
Cdd:pfam00656 130 -NLEDGGVVEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEATGKKQMPCLSSSTL 208


                  ....*
gi 2493534    410 TRYFY 414
Cdd:pfam00656 209 TKKFY 213
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
 6-88 4.11e-26

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: 100.36  E-value: 4.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534    6 THERDPIYKIKGLAKDMLDGVFDDLVEKNVLNGDELLKIGESASFILNKAENLVENFLEKTDMAGKIFAGHIANSQEQLS 85
Cdd:cd08325   1 RLKEKRVKFVESVGKGVINGLLDDLLEKNVLNEEEMEKIKEENNTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDKQLS 80


                ...
gi 2493534   86 LQF 88
Cdd:cd08325  81 SKL 83
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 4-91 1.62e-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: 62.96  E-value: 1.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534      4 RRTHERDPIYKIKGLAkdMLDGVFDDLVEKNVLNGDELLKIGESAsFILNKAENLVENFLEKTDMAGKIFAGHIANSQEQ 83
Cdd:pfam00619   1 RKLLKKNRVALVERLG--TLDGLLDYLLEKNVLTEEEEEKIKANP-TRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77


                  ....*...
gi 2493534     84 LSLQFSND 91
Cdd:pfam00619  78 LASDLEGL 85
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 2-84 7.55e-03

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: 35.39  E-value: 7.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534       2 AARRTHERDPIykiKGLAKDMLDGVFDDLVEKNVLNGDELLKIGESAsfilNKAENLVENFL---EKTDMAGKIFAGHIA 78
Cdd:smart00114   4 RDKRLLRRNRV---RLGEELGVDGLLDYLVEKNVLTEKEIEAIKAAT----TKLRDKRELVDslqKRGSQAFDTFLDSLQ 76


                   ....*.
gi 2493534      79 NSQEQL 84
Cdd:smart00114  77 ETDQKL 82
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 166-417 1.92e-110

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: 324.19  E-value: 1.92e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534     166 YPVMEKEGRtrLALIICNKKFDYLFDRDNADTDILNMQELLENLGYSVVLKENLTAQEMETELMQFAGRPEHQSSDSTFL 245
Cdd:smart00115   1 YKMNSKPRG--LALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534     246 VFMSHGILEGICGVKHrnkkpDVLHDDTIFKIFNNSNCRSLRNKPKILIMQACRG-RYNGTIWVSTNKGIATADTDEerv 324
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGdELDGGVPVEDSVADPESEGED--- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534     325 lsckwnNSITKAHVETDFIAFKSSTPHNISWKVGKTGSLFISKLIDCFKKYCWCYHLEEIFRKVQHSFEVPGE----LTQ 400
Cdd:smart00115 151 ------DAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFEsvnaKKQ 224

                          250
                   ....*....|....*..
gi 2493534     401 MPTIERVSMTRYFYLFP 417
Cdd:smart00115 225 MPTIESMTLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 165-416 1.19e-90

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: 274.09  E-value: 1.19e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534  165 IYPVMEKegRTRLALIICNKKFDY-LFDRDNADTDILNMQELLENLGYSVVLKENLTAQEMETELMQFAgRPEHQSSDST 243
Cdd:cd00032   1 IYKMNSK--RRGLALIINNENFDKgLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFA-SPDHSDSDSF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534  244 FLVFMSHGILEGICGVKHrnkkpDVLHDDTIFKIFNNSNCRSLRNKPKILIMQACRGRYNGTIWVSTNKGIATADTDEEr 323
Cdd:cd00032  78 VCVILSHGEEGGIYGTDG-----DVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPDVETE- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534  324 vlscKWNNSITKAHVETDFIAFKSSTPHNISWKVGKTGSLFISKLIDCFKKYCWCYHLEEIFRKVQHSFEVPGE----LT 399
Cdd:cd00032 152 ----AEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFEsvngKK 227

                       250
                ....*....|....*..
gi 2493534  400 QMPTIeRVSMTRYFYLF 416
Cdd:cd00032 228 QMPCF-RSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
175-414 2.85e-62

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 200.24  E-value: 2.85e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534    175 TRLALIICNKKFDYLF-DRDNADTDILNMQELLENLGYSVVLKENLTAQEMETELMQFAGRPEHQSSDSTFLVFM---SH 250
Cdd:pfam00656   1 RGLALIIGNNNYPGTKaPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534    251 GILEGicGVKHRNKKPDVLHDDTIFKIFNNSNC-RSLRNKPKILIMQACRGryngtiwvstnkgiatadtdeervlsckw 329
Cdd:pfam00656  81 GEQVP--GGDIYGTDEYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRG----------------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534    330 nNSITKAHVETDFIAFKSSTPHNISWKVGKTGSLFISKLIDCFKKYCWCYHLEEIFRKVQHSFEVPGELTQMPTIERVSM 409
Cdd:pfam00656 130 -NLEDGGVVEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEATGKKQMPCLSSSTL 208


                  ....*
gi 2493534    410 TRYFY 414
Cdd:pfam00656 209 TKKFY 213
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
 6-88 4.11e-26

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: 100.36  E-value: 4.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534    6 THERDPIYKIKGLAKDMLDGVFDDLVEKNVLNGDELLKIGESASFILNKAENLVENFLEKTDMAGKIFAGHIANSQEQLS 85
Cdd:cd08325   1 RLKEKRVKFVESVGKGVINGLLDDLLEKNVLNEEEMEKIKEENNTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDKQLS 80


                ...
gi 2493534   86 LQF 88
Cdd:cd08325  81 SKL 83
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 4-91 1.62e-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: 62.96  E-value: 1.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534      4 RRTHERDPIYKIKGLAkdMLDGVFDDLVEKNVLNGDELLKIGESAsFILNKAENLVENFLEKTDMAGKIFAGHIANSQEQ 83
Cdd:pfam00619   1 RKLLKKNRVALVERLG--TLDGLLDYLLEKNVLTEEEEEKIKANP-TRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77


                  ....*...
gi 2493534     84 LSLQFSND 91
Cdd:pfam00619  78 LASDLEGL 85
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 2-84 7.55e-03

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: 35.39  E-value: 7.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493534       2 AARRTHERDPIykiKGLAKDMLDGVFDDLVEKNVLNGDELLKIGESAsfilNKAENLVENFL---EKTDMAGKIFAGHIA 78
Cdd:smart00114   4 RDKRLLRRNRV---RLGEELGVDGLLDYLVEKNVLTEKEIEAIKAAT----TKLRDKRELVDslqKRGSQAFDTFLDSLQ 76


                   ....*.
gi 2493534      79 NSQEQL 84
Cdd:smart00114  77 ETDQKL 82
 
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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