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Conserved domains on  [gi|1826689208|ref|NP_001366248|]
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caspase-4 isoform 3 [Mus musculus]

Protein Classification

caspase family protein( domain architecture ID 11254530)

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

CATH:  3.40.50.1460
EC:  3.4.22.-
Gene Ontology:  GO:0008234
MEROPS:  C14
PubMed:  9357314
SCOP:  4003593

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 ...
5-254 2.52e-114

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: 327.66  E-value: 2.52e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208    5 YPIKEANGRTrkALIICNTEFKHLSLRYGANFDIIGMKGLLEDLGYDVVVKEELTAEGMESEMKDFAALSEHQTSDSTFL 84
Cdd:smart00115   1 YKMNSKPRGL--ALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208   85 VLMSHGTLHGICGTMHsektpDVLQYDTIYQIFNNCHCPGLRDKPKVIIVQACRGG-NSGEMWIRESSkpqlcrgVDLPR 163
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDeLDGGVPVEDSV-------ADPES 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208  164 NMEADAVKLSHVEKDFIAFYSTTPHHLSYRDKTGGSYFITRLISCFRKHACSCHLFDIFLKVQQS----FEKASIHSQMP 239
Cdd:smart00115 147 EGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKvadkFESVNAKKQMP 226
                          250
                   ....*....|....*
gi 1826689208  240 TIDRATLTRYFYLFP 254
Cdd:smart00115 227 TIESMTLTKKLYFFP 241
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
5-254 2.52e-114

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: 327.66  E-value: 2.52e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208    5 YPIKEANGRTrkALIICNTEFKHLSLRYGANFDIIGMKGLLEDLGYDVVVKEELTAEGMESEMKDFAALSEHQTSDSTFL 84
Cdd:smart00115   1 YKMNSKPRGL--ALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208   85 VLMSHGTLHGICGTMHsektpDVLQYDTIYQIFNNCHCPGLRDKPKVIIVQACRGG-NSGEMWIRESSkpqlcrgVDLPR 163
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDeLDGGVPVEDSV-------ADPES 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208  164 NMEADAVKLSHVEKDFIAFYSTTPHHLSYRDKTGGSYFITRLISCFRKHACSCHLFDIFLKVQQS----FEKASIHSQMP 239
Cdd:smart00115 147 EGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKvadkFESVNAKKQMP 226
                          250
                   ....*....|....*
gi 1826689208  240 TIDRATLTRYFYLFP 254
Cdd:smart00115 227 TIESMTLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
4-253 6.95e-96

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: 281.03  E-value: 6.95e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208   4 IYPIKEanGRTRKALIICNTEFKH-LSLRYGANFDIIGMKGLLEDLGYDVVVKEELTAEGMESEMKDFAAlSEHQTSDST 82
Cdd:cd00032     1 IYKMNS--KRRGLALIINNENFDKgLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208  83 FLVLMSHGTLHGICGTMHsektpDVLQYDTIYQIFNNCHCPGLRDKPKVIIVQACRGGNSGEMWIRESSKPQlcrGVDLP 162
Cdd:cd00032    78 VCVILSHGEEGGIYGTDG-----DVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADE---PPDVE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208 163 RNMEADAVKLSHVEKDFIAFYSTTPHHLSYRDKTGGSYFITRLISCFRKHACSCHLFDIFLKVQQSF----EKASIHSQM 238
Cdd:cd00032   150 TEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVaekfESVNGKKQM 229
                         250
                  ....*....|....*
gi 1826689208 239 PTIdRATLTRYFYLF 253
Cdd:cd00032   230 PCF-RSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
14-251 3.97e-66

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 204.48  E-value: 3.97e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208  14 TRKALIICNTEFKHLSL-RYGANFDIIGMKGLLEDLGYDVVVKEELTAEGMESEMKDFAALSEHQTSDSTFLVLM---SH 89
Cdd:pfam00656   1 RGLALIIGNNNYPGTKApLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208  90 GTLHGIcGTMHSEKtPDVLQYDTIYQIFNNCHC-PGLRDKPKVIIVQACRGgnsgemwiresskpqlcrgvdlprNMEAD 168
Cdd:pfam00656  81 GEQVPG-GDIYGTD-EYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRG------------------------NLEDG 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208 169 AVklshVEKDFIAFYSTTPHHLSYRDKTGGSYFITRLISCFRKHACSCHLFDIFLKVQQSFEKASIHSQMPTIDRATLTR 248
Cdd:pfam00656 135 GV----VEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEATGKKQMPCLSSSTLTK 210

                  ...
gi 1826689208 249 YFY 251
Cdd:pfam00656 211 KFY 213
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
5-254 2.52e-114

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: 327.66  E-value: 2.52e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208    5 YPIKEANGRTrkALIICNTEFKHLSLRYGANFDIIGMKGLLEDLGYDVVVKEELTAEGMESEMKDFAALSEHQTSDSTFL 84
Cdd:smart00115   1 YKMNSKPRGL--ALIINNENFHSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208   85 VLMSHGTLHGICGTMHsektpDVLQYDTIYQIFNNCHCPGLRDKPKVIIVQACRGG-NSGEMWIRESSkpqlcrgVDLPR 163
Cdd:smart00115  79 VLLSHGEEGGIYGTDG-----DPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDeLDGGVPVEDSV-------ADPES 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208  164 NMEADAVKLSHVEKDFIAFYSTTPHHLSYRDKTGGSYFITRLISCFRKHACSCHLFDIFLKVQQS----FEKASIHSQMP 239
Cdd:smart00115 147 EGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKvadkFESVNAKKQMP 226
                          250
                   ....*....|....*
gi 1826689208  240 TIDRATLTRYFYLFP 254
Cdd:smart00115 227 TIESMTLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
4-253 6.95e-96

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: 281.03  E-value: 6.95e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208   4 IYPIKEanGRTRKALIICNTEFKH-LSLRYGANFDIIGMKGLLEDLGYDVVVKEELTAEGMESEMKDFAAlSEHQTSDST 82
Cdd:cd00032     1 IYKMNS--KRRGLALIINNENFDKgLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208  83 FLVLMSHGTLHGICGTMHsektpDVLQYDTIYQIFNNCHCPGLRDKPKVIIVQACRGGNSGEMWIRESSKPQlcrGVDLP 162
Cdd:cd00032    78 VCVILSHGEEGGIYGTDG-----DVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADE---PPDVE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208 163 RNMEADAVKLSHVEKDFIAFYSTTPHHLSYRDKTGGSYFITRLISCFRKHACSCHLFDIFLKVQQSF----EKASIHSQM 238
Cdd:cd00032   150 TEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVaekfESVNGKKQM 229
                         250
                  ....*....|....*
gi 1826689208 239 PTIdRATLTRYFYLF 253
Cdd:cd00032   230 PCF-RSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
14-251 3.97e-66

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 204.48  E-value: 3.97e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208  14 TRKALIICNTEFKHLSL-RYGANFDIIGMKGLLEDLGYDVVVKEELTAEGMESEMKDFAALSEHQTSDSTFLVLM---SH 89
Cdd:pfam00656   1 RGLALIIGNNNYPGTKApLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208  90 GTLHGIcGTMHSEKtPDVLQYDTIYQIFNNCHC-PGLRDKPKVIIVQACRGgnsgemwiresskpqlcrgvdlprNMEAD 168
Cdd:pfam00656  81 GEQVPG-GDIYGTD-EYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRG------------------------NLEDG 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826689208 169 AVklshVEKDFIAFYSTTPHHLSYRDKTGGSYFITRLISCFRKHACSCHLFDIFLKVQQSFEKASIHSQMPTIDRATLTR 248
Cdd:pfam00656 135 GV----VEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEATGKKQMPCLSSSTLTK 210

                  ...
gi 1826689208 249 YFY 251
Cdd:pfam00656 211 KFY 213
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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