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Conserved domains on  [gi|1728919727|ref|XP_030327700|]
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caspase-2 isoform X3 [Strigops habroptila]

Protein Classification

caspase( domain architecture ID 10327176)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 102-357 1.50e-94

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: 281.80  E-value: 1.50e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 102 AYKLISEPRGLALILSNVHFssEKDLEYRAGGDVDCTSLEMLFKHLGYQVTVFHDQTAQEMQNALERFSKmPGHRDVDSC 181
Cdd:cd00032     1 IYKMNSKRRGLALIINNENF--DKGLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 182 IVALLSHGVEGGVYGSDGKLLQLQEAFRLFDNANCPNLQNKPKMFFIQACRGDETDRGVDQRDgkewsDSPGCEESDANK 261
Cdd:cd00032    78 VCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDS-----GADEPPDVETEA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 262 EENLKLRLPTCSDMICGYACLKGTAAMRNTKRGSWYVEALTSVFAEDSRDTHVADMLVKVNRHIKQREGYapgteFHRCK 341
Cdd:cd00032   153 EDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFES-----VNGKK 227

                         250
                  ....*....|....*.
gi 1728919727 342 EMSEYCSTLCRDLYLF 357
Cdd:cd00032   228 QMPCFRSTLTKKLYFF 243
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 1-44 6.17e-16

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 cd08332:

Pssm-ID: 472698  Cd Length: 87  Bit Score: 72.07  E-value: 6.17e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1728919727   1 MQRCHQEALKKNRVMLAKQLLLKELMEHMIEKDIFTTEMVEMIQ 44
Cdd:cd08332     1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIM 44
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 102-357 1.50e-94

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: 281.80  E-value: 1.50e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 102 AYKLISEPRGLALILSNVHFssEKDLEYRAGGDVDCTSLEMLFKHLGYQVTVFHDQTAQEMQNALERFSKmPGHRDVDSC 181
Cdd:cd00032     1 IYKMNSKRRGLALIINNENF--DKGLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 182 IVALLSHGVEGGVYGSDGKLLQLQEAFRLFDNANCPNLQNKPKMFFIQACRGDETDRGVDQRDgkewsDSPGCEESDANK 261
Cdd:cd00032    78 VCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDS-----GADEPPDVETEA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 262 EENLKLRLPTCSDMICGYACLKGTAAMRNTKRGSWYVEALTSVFAEDSRDTHVADMLVKVNRHIKQREGYapgteFHRCK 341
Cdd:cd00032   153 EDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFES-----VNGKK 227

                         250
                  ....*....|....*.
gi 1728919727 342 EMSEYCSTLCRDLYLF 357
Cdd:cd00032   228 QMPCFRSTLTKKLYFF 243
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 103-358 1.22e-92

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: 276.81  E-value: 1.22e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727  103 YKLISEPRGLALILSNVHFSSekdLEYRAGGDVDCTSLEMLFKHLGYQVTVFHDQTAQEMQNALERFSKMPGHRDVDSCI 182
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727  183 VALLSHGVEGGVYGSDGKLLQLQEAFRLFDNANCPNLQNKPKMFFIQACRGDETDRGVDQRDGKEWSDSPGceESDANKe 262
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPESEG--EDDAIY- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727  263 enlklRLPTCSDMICGYACLKGTAAMRNTKRGSWYVEALTSVFAEDSRDTHVADMLVKVNRHIKQREGYApgteFHRCKE 342
Cdd:smart00115 155 -----KIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFESV----NAKKQM 225

                          250
                   ....*....|....*.
gi 1728919727  343 MSEYCSTLCRDLYLFP 358
Cdd:smart00115 226 PTIESMTLTKKLYFFP 241
Peptidase_C14 pfam00656
Caspase domain;
110-355 1.20e-59

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 191.77  E-value: 1.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 110 RGLALILSNVHFSSEKdlEYRAGGDVDCTSLEMLFKHLGYQVTVFHDQTAQEMQNALERFSKMPGHRDVDSCIVALL--- 186
Cdd:pfam00656   1 RGLALIIGNNNYPGTK--APLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyys 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 187 SHGVE---GGVYGSDGKLLQLQEAFRLFDNANC-PNLQNKPKMFFIQACRGDETDRGVdqrdgkewsdspgceesdanke 262
Cdd:pfam00656  79 GHGEQvpgGDIYGTDEYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLEDGGV---------------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 263 enlklrlpTCSDMICGYACLKGTAAMRNTKRGSWYVEALTSVFAEDSRDTHVADMLVKVNRHIKQRegyapgtefHRCKE 342
Cdd:pfam00656 137 --------VEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEA---------TGKKQ 199

                         250
                  ....*....|....
gi 1728919727 343 MSE-YCSTLCRDLY 355
Cdd:pfam00656 200 MPClSSSTLTKKFY 213
CARD_CASP2 cd08332
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ...
 1-44 6.17e-16

Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment domain (CARD) similar to that found in caspase-2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Caspase-2 (also known as ICH1, NEDD2, or CASP2) is one of the most evolutionarily conserved caspases, and plays a role in apoptosis, DNA damage response, cell cycle regulation, and tumor suppression. It is localized in the nucleus and exhibits properties of both an initiator and an effector caspase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260040  Cd Length: 87  Bit Score: 72.07  E-value: 6.17e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1728919727   1 MQRCHQEALKKNRVMLAKQLLLKELMEHMIEKDIFTTEMVEMIQ 44
Cdd:cd08332     1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIM 44
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 1-44 4.37e-07

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: 47.33  E-value: 4.37e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1728919727    1 MQRCHQEALKKNRVMLAKQLLLKELMEHMIEKDIFTTEMVEMIQ 44
Cdd:smart00114   1 MAERDKRLLRRNRVRLGEELGVDGLLDYLVEKNVLTEKEIEAIK 44
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 6-46 1.80e-05

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: 42.55  E-value: 1.80e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1728919727   6 QEALKKNRVMLAKQLL-LKELMEHMIEKDIFTTEMVEMIQLE 46
Cdd:pfam00619   1 RKLLKKNRVALVERLGtLDGLLDYLLEKNVLTEEEEEKIKAN 42
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 102-357 1.50e-94

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: 281.80  E-value: 1.50e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 102 AYKLISEPRGLALILSNVHFssEKDLEYRAGGDVDCTSLEMLFKHLGYQVTVFHDQTAQEMQNALERFSKmPGHRDVDSC 181
Cdd:cd00032     1 IYKMNSKRRGLALIINNENF--DKGLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 182 IVALLSHGVEGGVYGSDGKLLQLQEAFRLFDNANCPNLQNKPKMFFIQACRGDETDRGVDQRDgkewsDSPGCEESDANK 261
Cdd:cd00032    78 VCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDS-----GADEPPDVETEA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 262 EENLKLRLPTCSDMICGYACLKGTAAMRNTKRGSWYVEALTSVFAEDSRDTHVADMLVKVNRHIKQREGYapgteFHRCK 341
Cdd:cd00032   153 EDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFES-----VNGKK 227

                         250
                  ....*....|....*.
gi 1728919727 342 EMSEYCSTLCRDLYLF 357
Cdd:cd00032   228 QMPCFRSTLTKKLYFF 243
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 103-358 1.22e-92

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: 276.81  E-value: 1.22e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727  103 YKLISEPRGLALILSNVHFSSekdLEYRAGGDVDCTSLEMLFKHLGYQVTVFHDQTAQEMQNALERFSKMPGHRDVDSCI 182
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727  183 VALLSHGVEGGVYGSDGKLLQLQEAFRLFDNANCPNLQNKPKMFFIQACRGDETDRGVDQRDGKEWSDSPGceESDANKe 262
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPESEG--EDDAIY- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727  263 enlklRLPTCSDMICGYACLKGTAAMRNTKRGSWYVEALTSVFAEDSRDTHVADMLVKVNRHIKQREGYApgteFHRCKE 342
Cdd:smart00115 155 -----KIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFESV----NAKKQM 225

                          250
                   ....*....|....*.
gi 1728919727  343 MSEYCSTLCRDLYLFP 358
Cdd:smart00115 226 PTIESMTLTKKLYFFP 241
Peptidase_C14 pfam00656
Caspase domain;
110-355 1.20e-59

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 191.77  E-value: 1.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 110 RGLALILSNVHFSSEKdlEYRAGGDVDCTSLEMLFKHLGYQVTVFHDQTAQEMQNALERFSKMPGHRDVDSCIVALL--- 186
Cdd:pfam00656   1 RGLALIIGNNNYPGTK--APLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyys 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 187 SHGVE---GGVYGSDGKLLQLQEAFRLFDNANC-PNLQNKPKMFFIQACRGDETDRGVdqrdgkewsdspgceesdanke 262
Cdd:pfam00656  79 GHGEQvpgGDIYGTDEYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLEDGGV---------------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728919727 263 enlklrlpTCSDMICGYACLKGTAAMRNTKRGSWYVEALTSVFAEDSRDTHVADMLVKVNRHIKQRegyapgtefHRCKE 342
Cdd:pfam00656 137 --------VEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEA---------TGKKQ 199

                         250
                  ....*....|....
gi 1728919727 343 MSE-YCSTLCRDLY 355
Cdd:pfam00656 200 MPClSSSTLTKKFY 213
CARD_CASP2 cd08332
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ...
 1-44 6.17e-16

Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment domain (CARD) similar to that found in caspase-2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Caspase-2 (also known as ICH1, NEDD2, or CASP2) is one of the most evolutionarily conserved caspases, and plays a role in apoptosis, DNA damage response, cell cycle regulation, and tumor suppression. It is localized in the nucleus and exhibits properties of both an initiator and an effector caspase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260040  Cd Length: 87  Bit Score: 72.07  E-value: 6.17e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1728919727   1 MQRCHQEALKKNRVMLAKQLLLKELMEHMIEKDIFTTEMVEMIQ 44
Cdd:cd08332     1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIM 44
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 1-44 4.37e-07

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: 47.33  E-value: 4.37e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1728919727    1 MQRCHQEALKKNRVMLAKQLLLKELMEHMIEKDIFTTEMVEMIQ 44
Cdd:smart00114   1 MAERDKRLLRRNRVRLGEELGVDGLLDYLVEKNVLTEKEIEAIK 44
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 9-46 1.17e-06

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: 45.97  E-value: 1.17e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1728919727   9 LKKNRVMLAKQLLLKELMEHMIEKDIFTTEMVEMIQLE 46
Cdd:cd01671     1 LRKNRVELVEDLDVEDILDHLIQKGVLTEEDKEEILSE 38
CARD_CASP9 cd08326
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ...
 5-44 5.39e-06

Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment domain (CARD) similar to that found in caspase-9 (CASP9, MCH6, APAF3), which interacts with the CARD of apoptotic protease-activating factor 1 (APAF-1). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-9 is the initiator caspase associated with the intrinsic or mitochondrial pathway of apoptosis, induced by many pro-apoptotic signals. Together with APAF-1, it forms the heptameric 'apoptosome' in response to the release of cytochrome c from mitochondria. Activated caspase-9 cleaves and activates downstream effector caspases, like caspase-3, caspase-6, and caspase-7, resulting in apoptosis. In general, CARDs are death domains (DDs) associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176740  Cd Length: 84  Bit Score: 43.95  E-value: 5.39e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1728919727   5 HQEALKKNRVMLAKQLLLKELMEHMIEKDIFTTEMVEMIQ 44
Cdd:cd08326     1 HRQILRRHRARLVEELQPKYLWDHLLSRGVFTPDMIEEIQ 40
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 6-46 1.80e-05

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: 42.55  E-value: 1.80e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1728919727   6 QEALKKNRVMLAKQLL-LKELMEHMIEKDIFTTEMVEMIQLE 46
Cdd:pfam00619   1 RKLLKKNRVALVERLGtLDGLLDYLLEKNVLTEEEEEKIKAN 42
 
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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