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Conserved domains on  [gi|1720426298|ref|XP_030099126|]
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caspase-3 isoform X1 [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 ...
37-277 1.15e-122

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: 349.61  E-value: 1.15e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298   37 YKMDYPEMGICIIINNKNFHKstgMSSRSGTDVDAANLRETFMGLKYQVRNKNDLTREDILELMDSVSK-EDHSKRSSFV 115
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAmPEHSDSDSFV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298  116 CVILSHGDEGVIYGTNG-PVELKKLTSFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGTD------EEMACQKIP 188
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGdPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVAdpesegEDDAIYKIP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298  189 VEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCSMLKLYAHKLEFMHILTRVNRKVATEFESfsldstFHAKKQIPCIVSM 268
Cdd:smart00115 158 VEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFES------VNAKKQMPTIESM 231
                          250
                   ....*....|
gi 1720426298  269 -LTKELYFYH 277
Cdd:smart00115 232 tLTKKLYFFP 241
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
37-277 1.15e-122

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: 349.61  E-value: 1.15e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298   37 YKMDYPEMGICIIINNKNFHKstgMSSRSGTDVDAANLRETFMGLKYQVRNKNDLTREDILELMDSVSK-EDHSKRSSFV 115
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAmPEHSDSDSFV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298  116 CVILSHGDEGVIYGTNG-PVELKKLTSFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGTD------EEMACQKIP 188
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGdPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVAdpesegEDDAIYKIP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298  189 VEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCSMLKLYAHKLEFMHILTRVNRKVATEFESfsldstFHAKKQIPCIVSM 268
Cdd:smart00115 158 VEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFES------VNAKKQMPTIESM 231
                          250
                   ....*....|
gi 1720426298  269 -LTKELYFYH 277
Cdd:smart00115 232 tLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
37-275 2.89e-120

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: 343.81  E-value: 2.89e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298  37 YKMDYPEMGICIIINNKNFHKstGMSSRSGTDVDAANLRETFMGLKYQVRNKNDLTREDILELMDSVSKEDHSKRSSFVC 116
Cdd:cd00032     2 YKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFVC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298 117 VILSHGDEGVIYGTNG-PVELKKLTSFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGTD---------EEMACQK 186
Cdd:cd00032    80 VILSHGEEGGIYGTDGdVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADeppdveteaEDDAVQT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298 187 IPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCSMLKLYAHKLEFMHILTRVNRKVATEFESfsldstFHAKKQIPCIV 266
Cdd:cd00032   160 IPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFES------VNGKKQMPCFR 233

                  ....*....
gi 1720426298 267 SMLTKELYF 275
Cdd:cd00032   234 STLTKKLYF 242
Peptidase_C14 pfam00656
Caspase domain;
44-274 1.45e-77

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 234.14  E-value: 1.45e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298  44 MGICIIINNKNFHKSTgmSSRSGTDVDAANLRETFMGLKYQVRNKNDLTREDILELMDS-VSKEDHSKRSSFVCVIL--- 119
Cdd:pfam00656   1 RGLALIIGNNNYPGTK--APLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDfAARADHSDGDSFVVVLLyys 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298 120 SHGDE---GVIYGTNG-PVELKKLTSFFRGDYC-RSLTGKPKLFIIQACRGTELDcgietdsgtdeemacqKIPVEADFL 194
Cdd:pfam00656  79 GHGEQvpgGDIYGTDEyLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLED----------------GGVVEADFL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298 195 YAYSTAPGYYSWRNSKDGSWFIQSLCSMLKLYAHKLEFMHILTRVNRKVATEfesfsldstfHAKKQIPCIVS-MLTKEL 273
Cdd:pfam00656 143 VAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEA----------TGKKQMPCLSSsTLTKKF 212

                  .
gi 1720426298 274 Y 274
Cdd:pfam00656 213 Y 213
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
37-277 1.15e-122

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: 349.61  E-value: 1.15e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298   37 YKMDYPEMGICIIINNKNFHKstgMSSRSGTDVDAANLRETFMGLKYQVRNKNDLTREDILELMDSVSK-EDHSKRSSFV 115
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHS---LPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAmPEHSDSDSFV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298  116 CVILSHGDEGVIYGTNG-PVELKKLTSFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGTD------EEMACQKIP 188
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGdPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVAdpesegEDDAIYKIP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298  189 VEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCSMLKLYAHKLEFMHILTRVNRKVATEFESfsldstFHAKKQIPCIVSM 268
Cdd:smart00115 158 VEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVADKFES------VNAKKQMPTIESM 231
                          250
                   ....*....|
gi 1720426298  269 -LTKELYFYH 277
Cdd:smart00115 232 tLTKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
37-275 2.89e-120

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: 343.81  E-value: 2.89e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298  37 YKMDYPEMGICIIINNKNFHKstGMSSRSGTDVDAANLRETFMGLKYQVRNKNDLTREDILELMDSVSKEDHSKRSSFVC 116
Cdd:cd00032     2 YKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFVC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298 117 VILSHGDEGVIYGTNG-PVELKKLTSFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGTD---------EEMACQK 186
Cdd:cd00032    80 VILSHGEEGGIYGTDGdVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADeppdveteaEDDAVQT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298 187 IPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCSMLKLYAHKLEFMHILTRVNRKVATEFESfsldstFHAKKQIPCIV 266
Cdd:cd00032   160 IPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFES------VNGKKQMPCFR 233

                  ....*....
gi 1720426298 267 SMLTKELYF 275
Cdd:cd00032   234 STLTKKLYF 242
Peptidase_C14 pfam00656
Caspase domain;
44-274 1.45e-77

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 234.14  E-value: 1.45e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298  44 MGICIIINNKNFHKSTgmSSRSGTDVDAANLRETFMGLKYQVRNKNDLTREDILELMDS-VSKEDHSKRSSFVCVIL--- 119
Cdd:pfam00656   1 RGLALIIGNNNYPGTK--APLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDfAARADHSDGDSFVVVLLyys 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298 120 SHGDE---GVIYGTNG-PVELKKLTSFFRGDYC-RSLTGKPKLFIIQACRGTELDcgietdsgtdeemacqKIPVEADFL 194
Cdd:pfam00656  79 GHGEQvpgGDIYGTDEyLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLED----------------GGVVEADFL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426298 195 YAYSTAPGYYSWRNSKDGSWFIQSLCSMLKLYAHKLEFMHILTRVNRKVATEfesfsldstfHAKKQIPCIVS-MLTKEL 273
Cdd:pfam00656 143 VAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGHGLDLLSLLTKVRRRVAEA----------TGKKQMPCLSSsTLTKKF 212

                  .
gi 1720426298 274 Y 274
Cdd:pfam00656 213 Y 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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