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Conserved domains on  [gi|119626650|gb|EAX06245|]
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caspase 6, apoptosis-related cysteine peptidase, isoform CRA_b [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 ...
14-200 5.19e-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: 249.82  E-value: 5.19e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650  14 VSTVSHADADCFVCVFLSHGEGNHIYAYDAK-IEIQTLTGLFKGDKCHSLVGKPKIFIIQACRGNQHDVPVIPLDVVDNQ 92
Cdd:cd00032   66 FASPDHSDSDSFVCVILSHGEEGGIYGTDGDvVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEP 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650  93 TEkldtNITEVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLGKYGSSLEFTELLTLVNRKVSQRRV 172
Cdd:cd00032  146 PD----VETEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFE 221
                        170       180
                 ....*....|....*....|....*...
gi 119626650 173 dfckdpSAIGKKQVPCFASMLTKKLHFF 200
Cdd:cd00032  222 ------SVNGKKQMPCFRSTLTKKLYFF 243
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
14-200 5.19e-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: 249.82  E-value: 5.19e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650  14 VSTVSHADADCFVCVFLSHGEGNHIYAYDAK-IEIQTLTGLFKGDKCHSLVGKPKIFIIQACRGNQHDVPVIPLDVVDNQ 92
Cdd:cd00032   66 FASPDHSDSDSFVCVILSHGEEGGIYGTDGDvVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEP 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650  93 TEkldtNITEVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLGKYGSSLEFTELLTLVNRKVSQRRV 172
Cdd:cd00032  146 PD----VETEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFE 221
                        170       180
                 ....*....|....*....|....*...
gi 119626650 173 dfckdpSAIGKKQVPCFASMLTKKLHFF 200
Cdd:cd00032  222 ------SVNGKKQMPCFRSTLTKKLYFF 243
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
18-201 2.14e-81

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: 245.61  E-value: 2.14e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650    18 SHADADCFVCVFLSHGEGNHIYAYD-AKIEIQTLTGLFKGDKCHSLVGKPKIFIIQACRGNQHDVPVIPLDVVDNQTekl 96
Cdd:smart00115  69 EHSDSDSFVCVLLSHGEEGGIYGTDgDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPE--- 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650    97 dtniTEVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLGKYGSSLEFTELLTLVNRKVSqrrvdfCK 176
Cdd:smart00115 146 ----SEGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVA------DK 215
                          170       180
                   ....*....|....*....|....*.
gi 119626650   177 DPSAIGKKQVPCFASM-LTKKLHFFP 201
Cdd:smart00115 216 FESVNAKKQMPTIESMtLTKKLYFFP 241
Peptidase_C14 pfam00656
Caspase domain;
13-199 3.02e-66

Caspase domain;


Pssm-ID: 307001  Cd Length: 234  Bit Score: 206.80  E-value: 3.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650   13 AVSTVSHADADCFVCVFLSHG-EGNHIYAYDAK--IEIQTLTGLFKGDKCHSLVGKPKIFIIQACRGNQHDVPVIPLDVV 89
Cdd:pfam00656  56 LAKRADHSDGDSFVVVYSGHGeQVGYIYPVDAGgvIPDDEIFDLFNGDNCPSLAGKPKVFIIQACRGGPLDEGVELDSGG 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650   90 DNQTEKldtnITEVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLGKYGSSLEFTELLTLVNRKVSQ 169
Cdd:pfam00656 136 DEGSSS----ESKPEKDGLSKIPVEADFLVAYSTAPGQVSWRGTGNGSWFIQALCQVLREPGKKLDLLDLLTKVRRRVAR 211
                         170       180       190
                  ....*....|....*....|....*....|.
gi 119626650  170 rrvdfckdPSAIGKKQVPCF-ASMLTKKLHF 199
Cdd:pfam00656 212 --------SKDGGGKQIPCLsSSTLTKKFYF 234
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
14-200 5.19e-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: 249.82  E-value: 5.19e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650  14 VSTVSHADADCFVCVFLSHGEGNHIYAYDAK-IEIQTLTGLFKGDKCHSLVGKPKIFIIQACRGNQHDVPVIPLDVVDNQ 92
Cdd:cd00032   66 FASPDHSDSDSFVCVILSHGEEGGIYGTDGDvVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEP 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650  93 TEkldtNITEVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLGKYGSSLEFTELLTLVNRKVSQRRV 172
Cdd:cd00032  146 PD----VETEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHSLDLLDILTKVNRKVAEKFE 221
                        170       180
                 ....*....|....*....|....*...
gi 119626650 173 dfckdpSAIGKKQVPCFASMLTKKLHFF 200
Cdd:cd00032  222 ------SVNGKKQMPCFRSTLTKKLYFF 243
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
18-201 2.14e-81

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: 245.61  E-value: 2.14e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650    18 SHADADCFVCVFLSHGEGNHIYAYD-AKIEIQTLTGLFKGDKCHSLVGKPKIFIIQACRGNQHDVPVIPLDVVDNQTekl 96
Cdd:smart00115  69 EHSDSDSFVCVLLSHGEEGGIYGTDgDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPE--- 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650    97 dtniTEVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLGKYGSSLEFTELLTLVNRKVSqrrvdfCK 176
Cdd:smart00115 146 ----SEGEDDAIYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEYARSLDLLDILTEVNRKVA------DK 215
                          170       180
                   ....*....|....*....|....*.
gi 119626650   177 DPSAIGKKQVPCFASM-LTKKLHFFP 201
Cdd:smart00115 216 FESVNAKKQMPTIESMtLTKKLYFFP 241
Peptidase_C14 pfam00656
Caspase domain;
13-199 3.02e-66

Caspase domain;


Pssm-ID: 307001  Cd Length: 234  Bit Score: 206.80  E-value: 3.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650   13 AVSTVSHADADCFVCVFLSHG-EGNHIYAYDAK--IEIQTLTGLFKGDKCHSLVGKPKIFIIQACRGNQHDVPVIPLDVV 89
Cdd:pfam00656  56 LAKRADHSDGDSFVVVYSGHGeQVGYIYPVDAGgvIPDDEIFDLFNGDNCPSLAGKPKVFIIQACRGGPLDEGVELDSGG 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626650   90 DNQTEKldtnITEVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLGKYGSSLEFTELLTLVNRKVSQ 169
Cdd:pfam00656 136 DEGSSS----ESKPEKDGLSKIPVEADFLVAYSTAPGQVSWRGTGNGSWFIQALCQVLREPGKKLDLLDLLTKVRRRVAR 211
                         170       180       190
                  ....*....|....*....|....*....|.
gi 119626650  170 rrvdfckdPSAIGKKQVPCF-ASMLTKKLHF 199
Cdd:pfam00656 212 --------SKDGGGKQIPCLsSSTLTKKFYF 234
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
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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