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Conserved domains on  [gi|15718700|ref|NP_203125|]
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caspase-7 isoform alpha precursor [Homo sapiens]

Protein Classification

caspase( domain architecture ID 10034008)

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 ...
60-301 3.73e-117

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: 336.88  E-value: 3.73e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700  60 YNMNFEKLGKCIIINNKNFDKvtGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFAC 139
Cdd:cd00032   2 YKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFVC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700 140 ILLSHGEENVIYGKDG-VTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPIN------DTDANPRYK 212
Cdd:cd00032  80 VILSHGEEGGIYGTDGdVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEppdvetEAEDDAVQT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700 213 IPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESQsddphfHEKKQIPCVV 292
Cdd:cd00032 160 IPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFESV------NGKKQMPCFR 233

                ....*....
gi 15718700 293 SMLTKELYF 301
Cdd:cd00032 234 STLTKKLYF 242
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
60-301 3.73e-117

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: 336.88  E-value: 3.73e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700  60 YNMNFEKLGKCIIINNKNFDKvtGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFAC 139
Cdd:cd00032   2 YKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFVC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700 140 ILLSHGEENVIYGKDG-VTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPIN------DTDANPRYK 212
Cdd:cd00032  80 VILSHGEEGGIYGTDGdVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEppdvetEAEDDAVQT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700 213 IPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESQsddphfHEKKQIPCVV 292
Cdd:cd00032 160 IPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFESV------NGKKQMPCFR 233

                ....*....
gi 15718700 293 SMLTKELYF 301
Cdd:cd00032 234 STLTKKLYF 242
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
60-302 9.71e-116

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: 333.44  E-value: 9.71e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700     60 YNMNFEKLGKCIIINNKNFDKvtgMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKK-ASEEDHTNAACFA 138
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEfAAMPEHSDSDSFV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700    139 CILLSHGEENVIYGKDG-VTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPINDT---DANPRYKIP 214
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGdPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPEsegEDDAIYKIP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700    215 VEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESqsddphFHEKKQIPCVVSM 294
Cdd:smart00115 158 VEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFES------VNAKKQMPTIESM 231

                   ....*....
gi 15718700    295 -LTKELYFS 302
Cdd:smart00115 232 tLTKKLYFF 240
Peptidase_C14 pfam00656
Caspase domain;
68-300 1.06e-79

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 240.69  E-value: 1.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700    68 GKCIIINNKNFDKVTGmgVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKK-ASEEDHTNAACFACILL---S 143
Cdd:pfam00656   2 GLALIIGNNNYPGTKA--PLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDfAARADHSDGDSFVVVLLyysG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700   144 HGEE---NVIYGKDG-VTPIKDLTAHFRGDRC-KTLLEKPKLFFIQACRGTELDDGiqadsgpindtdanprykiPVEAD 218
Cdd:pfam00656  80 HGEQvpgGDIYGTDEyLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLEDGG-------------------VVEAD 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700   219 FLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHfesqsddphfHEKKQIPCVVS-MLTK 297
Cdd:pfam00656 141 FLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEA----------TGKKQMPCLSSsTLTK 210

                  ...
gi 15718700   298 ELY 300
Cdd:pfam00656 211 KFY 213
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
60-301 3.73e-117

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: 336.88  E-value: 3.73e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700  60 YNMNFEKLGKCIIINNKNFDKvtGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFAC 139
Cdd:cd00032   2 YKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFVC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700 140 ILLSHGEENVIYGKDG-VTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPIN------DTDANPRYK 212
Cdd:cd00032  80 VILSHGEEGGIYGTDGdVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEppdvetEAEDDAVQT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700 213 IPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESQsddphfHEKKQIPCVV 292
Cdd:cd00032 160 IPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFESV------NGKKQMPCFR 233

                ....*....
gi 15718700 293 SMLTKELYF 301
Cdd:cd00032 234 STLTKKLYF 242
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
60-302 9.71e-116

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: 333.44  E-value: 9.71e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700     60 YNMNFEKLGKCIIINNKNFDKvtgMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKK-ASEEDHTNAACFA 138
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEfAAMPEHSDSDSFV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700    139 CILLSHGEENVIYGKDG-VTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPINDT---DANPRYKIP 214
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGdPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPEsegEDDAIYKIP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700    215 VEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESqsddphFHEKKQIPCVVSM 294
Cdd:smart00115 158 VEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFES------VNAKKQMPTIESM 231

                   ....*....
gi 15718700    295 -LTKELYFS 302
Cdd:smart00115 232 tLTKKLYFF 240
Peptidase_C14 pfam00656
Caspase domain;
68-300 1.06e-79

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 240.69  E-value: 1.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700    68 GKCIIINNKNFDKVTGmgVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKK-ASEEDHTNAACFACILL---S 143
Cdd:pfam00656   2 GLALIIGNNNYPGTKA--PLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDfAARADHSDGDSFVVVLLyysG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700   144 HGEE---NVIYGKDG-VTPIKDLTAHFRGDRC-KTLLEKPKLFFIQACRGTELDDGiqadsgpindtdanprykiPVEAD 218
Cdd:pfam00656  80 HGEQvpgGDIYGTDEyLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLEDGG-------------------VVEAD 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718700   219 FLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHfesqsddphfHEKKQIPCVVS-MLTK 297
Cdd:pfam00656 141 FLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEA----------TGKKQMPCLSSsTLTK 210

                  ...
gi 15718700   298 ELY 300
Cdd:pfam00656 211 KFY 213
 
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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