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Conserved domains on  [gi|973213606|ref|XP_006642491|]
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PREDICTED: caspase-2-like isoform X2 [Lepisosteus oculatus]

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 ...
 160-387 1.36e-83

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: 260.23  E-value: 1.36e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606 160 YKMTSRPRGLALVISNVDFqpvTPDLEPRAGGEVDEETLSRLFTELGFRVTLHRNQTAQEVRASLEQFSQSSElRAVDSS 239
Cdd:cd00032    2 YKMNSKRRGLALIINNENF---DKGLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDH-SDSDSF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606 240 VVCLLSHGVEGAVYGTDGQLVELDWVLEYFDNAHCPQLQNKPKMFFIQACRGEDTDSGVDQSDGPErtssPGCEQGDAAK 319
Cdd:cd00032   78 VCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGAD----EPPDVETEAE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973213606 320 EVVKVKLPQRSDMICGFASLKGTAAMRNTRRGSWFIQEMSSVFRQRARDKHLADLLVEVNARIKQREG 387
Cdd:cd00032  154 DDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFE 221
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 7-93 8.61e-36

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: 128.70  E-value: 8.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606   7 MLPYHREALRRCSVALCKDLVIDELVQHLLSDSILTESMAESIMADKTSFQRNRALLSLLPKRGPQAFESFCTALRETEQ 86
Cdd:cd08332    1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSAFCEALRETSQ 80


                 ....*..
gi 973213606  87 QHLESML 93
Cdd:cd08332   81 EHLADLL 87
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 160-387 1.36e-83

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: 260.23  E-value: 1.36e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606 160 YKMTSRPRGLALVISNVDFqpvTPDLEPRAGGEVDEETLSRLFTELGFRVTLHRNQTAQEVRASLEQFSQSSElRAVDSS 239
Cdd:cd00032    2 YKMNSKRRGLALIINNENF---DKGLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDH-SDSDSF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606 240 VVCLLSHGVEGAVYGTDGQLVELDWVLEYFDNAHCPQLQNKPKMFFIQACRGEDTDSGVDQSDGPErtssPGCEQGDAAK 319
Cdd:cd00032   78 VCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGAD----EPPDVETEAE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973213606 320 EVVKVKLPQRSDMICGFASLKGTAAMRNTRRGSWFIQEMSSVFRQRARDKHLADLLVEVNARIKQREG 387
Cdd:cd00032  154 DDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFE 221
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 160-387 3.91e-82

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: 256.40  E-value: 3.91e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606   160 YKMTSRPRGLALVISNVDFQpvtpDLEPRAGGEVDEETLSRLFTELGFRVTLHRNQTAQEVRASLEQFSQSSELRAVDSS 239
Cdd:smart00115   1 YKMNSKPRGLALIINNENFH----SLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606   240 VVCLLSHGVEGAVYGTDGQLVELDWVLEYFDNAHCPQLQNKPKMFFIQACRGEDTDSGVDQSDGPERTSSPGceQGDAAK 319
Cdd:smart00115  77 VCVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPESEG--EDDAIY 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973213606   320 evvkvKLPQRSDMICGFASLKGTAAMRNTRRGSWFIQEMSSVFRQRARDKHLADLLVEVNARIKQREG 387
Cdd:smart00115 155 -----KIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFE 217
Peptidase_C14 pfam00656
Caspase domain;
167-389 2.26e-52

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 177.90  E-value: 2.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606  167 RGLALVISNVDFqpvtPDLE-PRAGGEVDEETLSRLFTELGFRVTLHRNQTAQEVRASLEQFSQSSELRAVDSSVVCLL- 244
Cdd:pfam00656   1 RGLALIIGNNNY----PGTKaPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLy 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606  245 --SHGVE---GAVYGTDGQLVELDWVLEYFDNAHC-PQLQNKPKMFFIQACRGEDTDSGVdqsdgpertsspgceqgdaa 318
Cdd:pfam00656  77 ysGHGEQvpgGDIYGTDEYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLEDGGV-------------------- 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973213606  319 kevvkvklpQRSDMICGFASLKGTAAMRNTRRGSWFIQEMSSVFRQRARDKHLADLLVEVNARIKQREGFA 389
Cdd:pfam00656 137 ---------VEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEATGKK 198
CARD_CASP2 cd08332
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ...
 7-93 8.61e-36

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: 128.70  E-value: 8.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606   7 MLPYHREALRRCSVALCKDLVIDELVQHLLSDSILTESMAESIMADKTSFQRNRALLSLLPKRGPQAFESFCTALRETEQ 86
Cdd:cd08332    1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSAFCEALRETSQ 80


                 ....*..
gi 973213606  87 QHLESML 93
Cdd:cd08332   81 EHLADLL 87
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 7-95 1.17e-19

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: 83.54  E-value: 1.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606     7 MLPYHREALRRCSVALCKDLVIDELVQHLLSDSILTESMAESIMADKTSFQRNRALLSLLPKRGPQAFESFCTALRETeQ 86
Cdd:smart00114   1 MAERDKRLLRRNRVRLGEELGVDGLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQET-D 79


                   ....*....
gi 973213606    87 QHLESMLRD 95
Cdd:smart00114  80 QKLADFLEL 88
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 12-95 1.46e-16

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: 74.52  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606   12 REALRRCSVALCKDL-VIDELVQHLLSDSILTESMAESIMADKTSFQRNRALLSLLPKRGPQAFESFCTALREtEQQHLE 90
Cdd:pfam00619   1 RKLLKKNRVALVERLgTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKE-GDPDLA 79


                  ....*
gi 973213606   91 SMLRD 95
Cdd:pfam00619  80 SDLEG 84
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 160-387 1.36e-83

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: 260.23  E-value: 1.36e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606 160 YKMTSRPRGLALVISNVDFqpvTPDLEPRAGGEVDEETLSRLFTELGFRVTLHRNQTAQEVRASLEQFSQSSElRAVDSS 239
Cdd:cd00032    2 YKMNSKRRGLALIINNENF---DKGLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDH-SDSDSF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606 240 VVCLLSHGVEGAVYGTDGQLVELDWVLEYFDNAHCPQLQNKPKMFFIQACRGEDTDSGVDQSDGPErtssPGCEQGDAAK 319
Cdd:cd00032   78 VCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGAD----EPPDVETEAE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973213606 320 EVVKVKLPQRSDMICGFASLKGTAAMRNTRRGSWFIQEMSSVFRQRARDKHLADLLVEVNARIKQREG 387
Cdd:cd00032  154 DDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFE 221
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 160-387 3.91e-82

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: 256.40  E-value: 3.91e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606   160 YKMTSRPRGLALVISNVDFQpvtpDLEPRAGGEVDEETLSRLFTELGFRVTLHRNQTAQEVRASLEQFSQSSELRAVDSS 239
Cdd:smart00115   1 YKMNSKPRGLALIINNENFH----SLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606   240 VVCLLSHGVEGAVYGTDGQLVELDWVLEYFDNAHCPQLQNKPKMFFIQACRGEDTDSGVDQSDGPERTSSPGceQGDAAK 319
Cdd:smart00115  77 VCVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPESEG--EDDAIY 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973213606   320 evvkvKLPQRSDMICGFASLKGTAAMRNTRRGSWFIQEMSSVFRQRARDKHLADLLVEVNARIKQREG 387
Cdd:smart00115 155 -----KIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFE 217
Peptidase_C14 pfam00656
Caspase domain;
167-389 2.26e-52

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 177.90  E-value: 2.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606  167 RGLALVISNVDFqpvtPDLE-PRAGGEVDEETLSRLFTELGFRVTLHRNQTAQEVRASLEQFSQSSELRAVDSSVVCLL- 244
Cdd:pfam00656   1 RGLALIIGNNNY----PGTKaPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLy 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606  245 --SHGVE---GAVYGTDGQLVELDWVLEYFDNAHC-PQLQNKPKMFFIQACRGEDTDSGVdqsdgpertsspgceqgdaa 318
Cdd:pfam00656  77 ysGHGEQvpgGDIYGTDEYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLEDGGV-------------------- 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973213606  319 kevvkvklpQRSDMICGFASLKGTAAMRNTRRGSWFIQEMSSVFRQRARDKHLADLLVEVNARIKQREGFA 389
Cdd:pfam00656 137 ---------VEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEATGKK 198
CARD_CASP2 cd08332
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ...
 7-93 8.61e-36

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: 128.70  E-value: 8.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606   7 MLPYHREALRRCSVALCKDLVIDELVQHLLSDSILTESMAESIMADKTSFQRNRALLSLLPKRGPQAFESFCTALRETEQ 86
Cdd:cd08332    1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSAFCEALRETSQ 80


                 ....*..
gi 973213606  87 QHLESML 93
Cdd:cd08332   81 EHLADLL 87
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 15-93 8.71e-26

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: 100.67  E-value: 8.71e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 973213606  15 LRRCSVALCKDLVIDELVQHLLSDSILTESMAESIMADKTSFQRNRALLSLLPKRGPQAFESFCTALRETEQQHLESML 93
Cdd:cd01671    1 LRKNRVELVEDLDVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPHLAELL 79
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 7-95 1.17e-19

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: 83.54  E-value: 1.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606     7 MLPYHREALRRCSVALCKDLVIDELVQHLLSDSILTESMAESIMADKTSFQRNRALLSLLPKRGPQAFESFCTALRETeQ 86
Cdd:smart00114   1 MAERDKRLLRRNRVRLGEELGVDGLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQET-D 79


                   ....*....
gi 973213606    87 QHLESMLRD 95
Cdd:smart00114  80 QKLADFLEL 88
CARD_CASP9 cd08326
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ...
 11-94 1.76e-18

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: 80.16  E-value: 1.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606  11 HREALRRCSVALCKDLVIDELVQHLLSDSILTESMAESIMADKTSFQRNRALLSLLPKRGPQAFESFCTALRETEQQHLE 90
Cdd:cd08326    1 HRQILRRHRARLVEELQPKYLWDHLLSRGVFTPDMIEEIQAAGSRRDQARQLLIDLETRGKQAFPAFLSALRETGQTDLA 80


                 ....
gi 973213606  91 SMLR 94
Cdd:cd08326   81 ELLR 84
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 12-95 1.46e-16

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: 74.52  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606   12 REALRRCSVALCKDL-VIDELVQHLLSDSILTESMAESIMADKTSFQRNRALLSLLPKRGPQAFESFCTALREtEQQHLE 90
Cdd:pfam00619   1 RKLLKKNRVALVERLgTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKE-GDPDLA 79


                  ....*
gi 973213606   91 SMLRD 95
Cdd:pfam00619  80 SDLEG 84
CARD_RAIDD cd08327
Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a ...
 7-83 5.61e-16

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: 73.27  E-value: 5.61e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973213606   7 MLPYHREALRRCSVALCKDLVIDELV-QHLLSDSILTESMAESIMADKTSFQRNRALLSLLPKRGPQAFESFCTALRE 83
Cdd:cd08327    1 MEPKHKQLLRSQRLELCAELLVDGLIvQYLYQEGILTESHVEEIQSQTTSRRKTLKLLDILPNRGPKAFHAFLDSLEE 78
CARD_BCL10 cd08810
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ...
 13-87 2.26e-07

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: 48.50  E-value: 2.26e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973213606  13 EALRRCSVALCKDLVIDELVQHLLSDSILTESMAESIMADKTSFQRNRALLSLLPKRGPQAFESFCTALRETEQQ 87
Cdd:cd08810    3 EVLEEQRHYLCDKLIADRHFDYLRSKRILTRDDCEEIQCRTTRKKRVDKLLDILAREGPDGLDALIESIRRNGTQ 77
CARD_APAF1 cd08323
Caspase activation and recruitment domain similar to that found in Apoptotic ...
 11-95 1.83e-06

Caspase activation and recruitment domain similar to that found in Apoptotic Protease-Activating Factor 1; Caspase activation and recruitment domain (CARD) similar to that found in apoptotic protease-activating factor 1 (APAF-1), which is an activator of caspase-9. APAF-1 contains WD-40 repeats, a CARD, and an ATPase domain. Upon stimulation, APAF-1, together with caspase-9, forms the heptameric 'apoptosome', which leads to the processing and activation of caspase-9, starting a caspase cascade which leads to 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: 260034  Cd Length: 86  Bit Score: 45.96  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973213606  11 HREALRRcsvalckDLVIDELVQHLLSDSILTESMAESIMADKTSFQRNRALLSLLPKRGPQAFESFCTALRETEQQHLE 90
Cdd:cd08323    6 HRAALER-------DIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLA 78


                 ....*
gi 973213606  91 SMLRD 95
Cdd:cd08323   79 ALLHD 83
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 11-85 9.56e-06

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. 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: 260039  Cd Length: 81  Bit Score: 43.74  E-value: 9.56e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973213606  11 HREAL--RRCSValckDLVIDELVQHllsdsILTESMAESIMADKTSFQRNRALLSLLPKRGPQAFESFCTALRETE 85
Cdd:cd08330    6 HREALiqRVTNV----DPILDELRGK-----VLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETN 73
 
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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