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Conserved domains on  [gi|312596929|ref|NP_127463|]
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caspase-9 isoform 3 [Homo sapiens]

Protein Classification

CASc domain-containing protein (domain architecture ID 10034008)

CASc domain-containing protein

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 ...
69-331 8.66e-109

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: 316.85  E-value: 8.66e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929  69 AYILSMEPCGHCLIINNVNFCResGLRTRTGSNIDCEKLRRRFSSLHFMVEVKGDLTAKKMVLALLELAQQDHGALDCCV 148
Cdd:cd00032    1 IYKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929 149 VVILSHGCQashlqfpGAVYGTDGCPVSVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGSN 228
Cdd:cd00032   79 CVILSHGEE-------GGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPDVETE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929 229 PEPdatpfqeglrtfdqlDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSEDLQSLLLRVANAV 308
Cdd:cd00032  152 AED---------------DAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKV 216
                        250       260
                 ....*....|....*....|....*..
gi 312596929 309 SVK----GIYKQMPGCFNFLRKKLFFK 331
Cdd:cd00032  217 AEKfesvNGKKQMPCFRSTLTKKLYFF 243
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
69-331 8.66e-109

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: 316.85  E-value: 8.66e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929  69 AYILSMEPCGHCLIINNVNFCResGLRTRTGSNIDCEKLRRRFSSLHFMVEVKGDLTAKKMVLALLELAQQDHGALDCCV 148
Cdd:cd00032    1 IYKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929 149 VVILSHGCQashlqfpGAVYGTDGCPVSVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGSN 228
Cdd:cd00032   79 CVILSHGEE-------GGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPDVETE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929 229 PEPdatpfqeglrtfdqlDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSEDLQSLLLRVANAV 308
Cdd:cd00032  152 AED---------------DAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKV 216
                        250       260
                 ....*....|....*....|....*..
gi 312596929 309 SVK----GIYKQMPGCFNFLRKKLFFK 331
Cdd:cd00032  217 AEKfesvNGKKQMPCFRSTLTKKLYFF 243
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
70-330 8.15e-104

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: 304.16  E-value: 8.15e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929    70 YILSMEPCGHCLIINNVNFCResgLRTRTGSNIDCEKLRRRFSSLHFMVEVKGDLTAKKMVLALLELAQ-QDHGALDCCV 148
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAmPEHSDSDSFV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929   149 VVILSHGcqashlqFPGAVYGTDGCPVSVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGsn 228
Cdd:smart00115  78 CVLLSHG-------EEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPESEG-- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929   229 pepdatpfqeglrtfdQLDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSEDLQSLLLRVANAV 308
Cdd:smart00115 149 ----------------EDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKV 212
                          250       260
                   ....*....|....*....|....*..
gi 312596929   309 SVKGIY----KQMPGCFNF-LRKKLFF 330
Cdd:smart00115 213 ADKFESvnakKQMPTIESMtLTKKLYF 239
Peptidase_C14 pfam00656
Caspase domain;
78-330 2.84e-83

Caspase domain;


Pssm-ID: 334197  Cd Length: 230  Bit Score: 251.47  E-value: 2.84e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929   78 GHCLIINNVNFCresGLRTRTGSNIDCEKLRRRFSSLHFMVEVKGDLTAKKMVLALLELAQ-QDHGALDCCVVVILSHGC 156
Cdd:pfam00656   1 GLALIIGNNNYP---GLSPLRGCDNDAEALAELLKRLGFEVEVFDDLTAEEIRRALRDLAKrADHSDGDSLVVVYSGHGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929  157 QashlqfpGAVYGTDGC-PVSVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGSNPEPDATp 235
Cdd:pfam00656  78 Q-------GYIYPVDGGgVIDDDEIFDLFNGDNCPSLAGKPKLFIIQACRGGPLDEGVELDSGGDEGEEVESKPEKDGL- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929  236 fqeglrtfdqldaiSSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSEDLQSLLLRVANAVSVKGiYK 315
Cdd:pfam00656 150 --------------SKIPVEADFLVAYSTAPGQVSWRGTGNGSWFIQALCQVLREPGKDLDLLDLLTKVRRRVESTK-GK 214
                         250
                  ....*....|....*.
gi 312596929  316 QMPGC-FNFLRKKLFF 330
Cdd:pfam00656 215 QIPCLsSSTLTKKFYF 230
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
69-331 8.66e-109

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: 316.85  E-value: 8.66e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929  69 AYILSMEPCGHCLIINNVNFCResGLRTRTGSNIDCEKLRRRFSSLHFMVEVKGDLTAKKMVLALLELAQQDHGALDCCV 148
Cdd:cd00032    1 IYKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929 149 VVILSHGCQashlqfpGAVYGTDGCPVSVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGSN 228
Cdd:cd00032   79 CVILSHGEE-------GGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPDVETE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929 229 PEPdatpfqeglrtfdqlDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSEDLQSLLLRVANAV 308
Cdd:cd00032  152 AED---------------DAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKV 216
                        250       260
                 ....*....|....*....|....*..
gi 312596929 309 SVK----GIYKQMPGCFNFLRKKLFFK 331
Cdd:cd00032  217 AEKfesvNGKKQMPCFRSTLTKKLYFF 243
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
70-330 8.15e-104

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: 304.16  E-value: 8.15e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929    70 YILSMEPCGHCLIINNVNFCResgLRTRTGSNIDCEKLRRRFSSLHFMVEVKGDLTAKKMVLALLELAQ-QDHGALDCCV 148
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAmPEHSDSDSFV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929   149 VVILSHGcqashlqFPGAVYGTDGCPVSVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGsn 228
Cdd:smart00115  78 CVLLSHG-------EEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPESEG-- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929   229 pepdatpfqeglrtfdQLDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSEDLQSLLLRVANAV 308
Cdd:smart00115 149 ----------------EDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKV 212
                          250       260
                   ....*....|....*....|....*..
gi 312596929   309 SVKGIY----KQMPGCFNF-LRKKLFF 330
Cdd:smart00115 213 ADKFESvnakKQMPTIESMtLTKKLYF 239
Peptidase_C14 pfam00656
Caspase domain;
78-330 2.84e-83

Caspase domain;


Pssm-ID: 334197  Cd Length: 230  Bit Score: 251.47  E-value: 2.84e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929   78 GHCLIINNVNFCresGLRTRTGSNIDCEKLRRRFSSLHFMVEVKGDLTAKKMVLALLELAQ-QDHGALDCCVVVILSHGC 156
Cdd:pfam00656   1 GLALIIGNNNYP---GLSPLRGCDNDAEALAELLKRLGFEVEVFDDLTAEEIRRALRDLAKrADHSDGDSLVVVYSGHGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929  157 QashlqfpGAVYGTDGC-PVSVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGSNPEPDATp 235
Cdd:pfam00656  78 Q-------GYIYPVDGGgVIDDDEIFDLFNGDNCPSLAGKPKLFIIQACRGGPLDEGVELDSGGDEGEEVESKPEKDGL- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312596929  236 fqeglrtfdqldaiSSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSEDLQSLLLRVANAVSVKGiYK 315
Cdd:pfam00656 150 --------------SKIPVEADFLVAYSTAPGQVSWRGTGNGSWFIQALCQVLREPGKDLDLLDLLTKVRRRVESTK-GK 214
                         250
                  ....*....|....*.
gi 312596929  316 QMPGC-FNFLRKKLFF 330
Cdd:pfam00656 215 QIPCLsSSTLTKKFYF 230
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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