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Conserved domains on  [gi|39995059|ref|NP_116764|]
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caspase-2 isoform 1 preproprotein [Homo sapiens]

Protein Classification

caspase family protein( domain architecture ID 10871146)

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 ...
192-447 1.83e-107

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: 318.03  E-value: 1.83e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059    192 YRLQSRPRGLALVLSNVHFTGekeLEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCI 271
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059    272 VALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGceESDAGKe 351
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPESEG--EDDAIY- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059    352 klpkmRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYApgteFHRCKE 431
Cdd:smart00115 155 -----KIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFESV----NAKKQM 225
                          250
                   ....*....|....*.
gi 39995059    432 MSEYCSTLCRHLYLFP 447
Cdd:smart00115 226 PTIESMTLTKKLYFFP 241
CARD_CASP2 cd08332
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ...
32-118 9.60e-37

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: 129.85  E-value: 9.60e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059  32 MHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQ 111
Cdd:cd08332   1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSAFCEALRETSQ 80

                ....*..
gi 39995059 112 GHLEDML 118
Cdd:cd08332  81 EHLADLL 87
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
192-447 1.83e-107

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: 318.03  E-value: 1.83e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059    192 YRLQSRPRGLALVLSNVHFTGekeLEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCI 271
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059    272 VALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGceESDAGKe 351
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPESEG--EDDAIY- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059    352 klpkmRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYApgteFHRCKE 431
Cdd:smart00115 155 -----KIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFESV----NAKKQM 225
                          250
                   ....*....|....*.
gi 39995059    432 MSEYCSTLCRHLYLFP 447
Cdd:smart00115 226 PTIESMTLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
191-446 4.23e-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: 301.83  E-value: 4.23e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059 191 AYRLQSRPRGLALVLSNVHFtgEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQlPAHRVTDSC 270
Cdd:cd00032   1 IYKMNSKRRGLALIINNENF--DKGLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059 271 IVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDgknhaGSPGCEESDAGK 350
Cdd:cd00032  78 VCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDS-----GADEPPDVETEA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059 351 EKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYapgteFHRCK 430
Cdd:cd00032 153 EDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFES-----VNGKK 227
                       250
                ....*....|....*.
gi 39995059 431 EMSEYCSTLCRHLYLF 446
Cdd:cd00032 228 QMPCFRSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
199-444 7.20e-58

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 189.46  E-value: 7.20e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059   199 RGLALVLSNVHFTGEKEleFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALL--- 275
Cdd:pfam00656   1 RGLALIIGNNNYPGTKA--PLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyys 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059   276 SHGVE---GAIYGVDGKLLQLQEVFQLFDNANC-PSLQNKPKMFFIQACRGDETDRGVdqqdgknhagspgceesdagke 351
Cdd:pfam00656  79 GHGEQvpgGDIYGTDEYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLEDGGV---------------------- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059   352 klpkmrlpTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDRegyapgtefHRCKE 431
Cdd:pfam00656 137 --------VEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEA---------TGKKQ 199
                         250
                  ....*....|....
gi 39995059   432 MSE-YCSTLCRHLY 444
Cdd:pfam00656 200 MPClSSSTLTKKFY 213
CARD_CASP2 cd08332
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ...
32-118 9.60e-37

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: 129.85  E-value: 9.60e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059  32 MHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQ 111
Cdd:cd08332   1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSAFCEALRETSQ 80

                ....*..
gi 39995059 112 GHLEDML 118
Cdd:cd08332  81 EHLADLL 87
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
32-120 1.28e-18

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: 80.46  E-value: 1.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059     32 MHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETkQ 111
Cdd:smart00114   1 MAERDKRLLRRNRVRLGEELGVDGLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQET-D 79

                   ....*....
gi 39995059    112 GHLEDMLLT 120
Cdd:smart00114  80 QKLADFLEL 88
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
37-118 1.78e-10

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: 57.18  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059    37 QETLKKNRVVLAKQLLLSELLEHL-LEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETkQGHLE 115
Cdd:pfam00619   1 RKLLKKNRVALVERLGTLDGLLDYlLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEG-DPDLA 79

                  ...
gi 39995059   116 DML 118
Cdd:pfam00619  80 SDL 82
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
192-447 1.83e-107

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: 318.03  E-value: 1.83e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059    192 YRLQSRPRGLALVLSNVHFTGekeLEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCI 271
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059    272 VALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGceESDAGKe 351
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPESEG--EDDAIY- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059    352 klpkmRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYApgteFHRCKE 431
Cdd:smart00115 155 -----KIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFESV----NAKKQM 225
                          250
                   ....*....|....*.
gi 39995059    432 MSEYCSTLCRHLYLFP 447
Cdd:smart00115 226 PTIESMTLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
191-446 4.23e-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: 301.83  E-value: 4.23e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059 191 AYRLQSRPRGLALVLSNVHFtgEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQlPAHRVTDSC 270
Cdd:cd00032   1 IYKMNSKRRGLALIINNENF--DKGLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059 271 IVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDgknhaGSPGCEESDAGK 350
Cdd:cd00032  78 VCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDS-----GADEPPDVETEA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059 351 EKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYapgteFHRCK 430
Cdd:cd00032 153 EDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFES-----VNGKK 227
                       250
                ....*....|....*.
gi 39995059 431 EMSEYCSTLCRHLYLF 446
Cdd:cd00032 228 QMPCFRSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
199-444 7.20e-58

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 189.46  E-value: 7.20e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059   199 RGLALVLSNVHFTGEKEleFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALL--- 275
Cdd:pfam00656   1 RGLALIIGNNNYPGTKA--PLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyys 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059   276 SHGVE---GAIYGVDGKLLQLQEVFQLFDNANC-PSLQNKPKMFFIQACRGDETDRGVdqqdgknhagspgceesdagke 351
Cdd:pfam00656  79 GHGEQvpgGDIYGTDEYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLEDGGV---------------------- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059   352 klpkmrlpTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDRegyapgtefHRCKE 431
Cdd:pfam00656 137 --------VEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEA---------TGKKQ 199
                         250
                  ....*....|....
gi 39995059   432 MSE-YCSTLCRHLY 444
Cdd:pfam00656 200 MPClSSSTLTKKFY 213
CARD_CASP2 cd08332
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ...
32-118 9.60e-37

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: 129.85  E-value: 9.60e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059  32 MHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQ 111
Cdd:cd08332   1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSAFCEALRETSQ 80

                ....*..
gi 39995059 112 GHLEDML 118
Cdd:cd08332  81 EHLADLL 87
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
32-120 1.28e-18

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: 80.46  E-value: 1.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059     32 MHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETkQ 111
Cdd:smart00114   1 MAERDKRLLRRNRVRLGEELGVDGLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQET-D 79

                   ....*....
gi 39995059    112 GHLEDMLLT 120
Cdd:smart00114  80 QKLADFLEL 88
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
40-118 5.48e-18

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: 78.33  E-value: 5.48e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39995059  40 LKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDML 118
Cdd:cd01671   1 LRKNRVELVEDLDVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPHLAELL 79
CARD_CASP9 cd08326
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ...
36-118 1.96e-12

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: 62.83  E-value: 1.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059  36 HQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLE 115
Cdd:cd08326   1 HRQILRRHRARLVEELQPKYLWDHLLSRGVFTPDMIEEIQAAGSRRDQARQLLIDLETRGKQAFPAFLSALRETGQTDLA 80

                ...
gi 39995059 116 DML 118
Cdd:cd08326  81 ELL 83
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
37-118 1.78e-10

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: 57.18  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995059    37 QETLKKNRVVLAKQLLLSELLEHL-LEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETkQGHLE 115
Cdd:pfam00619   1 RKLLKKNRVALVERLGTLDGLLDYlLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEG-DPDLA 79

                  ...
gi 39995059   116 DML 118
Cdd:pfam00619  80 SDL 82
CARD_RAIDD cd08327
Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a ...
32-108 1.67e-06

Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a death domain; Caspase activation and recruitment domain (CARD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal CARD, which interacts with the caspase-2 CARD, and a C-terminal Death domain (DD), which interacts with the DD of PIDD. In general, CARDs are 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: 260037  Cd Length: 94  Bit Score: 46.30  E-value: 1.67e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39995059  32 MHPHHQETLKKNRVVLAKQLLLSELLEH-LLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRE 108
Cdd:cd08327   1 MEPKHKQLLRSQRLELCAELLVDGLIVQyLYQEGILTESHVEEIQSQTTSRRKTLKLLDILPNRGPKAFHAFLDSLEE 78
CARD_BCL10 cd08810
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ...
37-110 1.48e-05

Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and recruitment domain (CARD) similar to that found in BCL10 (B-cell lymphoma 10). BCL10 and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1) are the integral components of CBM signalosomes. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells) and with CARMA1 to form L-CBM (CBM complex in lymphoid immune cells), to mediate activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. Both CARMA1 and CARD9 associate with BCL10 via a CARD-CARD interaction. 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: 260072 [Multi-domain]  Cd Length: 85  Bit Score: 43.10  E-value: 1.48e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39995059  37 QETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETK 110
Cdd:cd08810   2 KEVLEEQRHYLCDKLIADRHFDYLRSKRILTRDDCEEIQCRTTRKKRVDKLLDILAREGPDGLDALIESIRRNG 75
 
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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