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Conserved domains on  [gi|321267564|ref|NP_001189444|]
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CASP8 and FADD-like apoptosis regulator isoform 3 [Homo sapiens]

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 ...
1-234 4.96e-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: 300.69  E-value: 4.96e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564     1 MKSKPLGICLIIDCIGNE-----------TELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLVS 69
Cdd:smart00115   3 MNSKPRGLALIINNENFHslprrngtdvdAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVCVLLS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564    70 RGGSQSVYGVDqtHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYvvsEGQLEDSSLLEVDGPAmkNVEFKAQKRGLCT 149
Cdd:smart00115  83 HGEEGGIYGTD--GDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQAC---RGDELDGGVPVEDSVA--DPESEGEDDAIYK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564   150 VHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQ-ERKRPLLDLHIELNGYMYDWNSRVSAKEKYYVWLQHTLRK 228
Cdd:smart00115 156 IPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEyARSLDLLDILTEVNRKVADKFESVNAKKQMPTIESMTLTK 235

                   ....*.
gi 321267564   229 KLILSY 234
Cdd:smart00115 236 KLYFFP 241
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
1-234 4.96e-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: 300.69  E-value: 4.96e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564     1 MKSKPLGICLIIDCIGNE-----------TELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLVS 69
Cdd:smart00115   3 MNSKPRGLALIINNENFHslprrngtdvdAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVCVLLS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564    70 RGGSQSVYGVDqtHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYvvsEGQLEDSSLLEVDGPAmkNVEFKAQKRGLCT 149
Cdd:smart00115  83 HGEEGGIYGTD--GDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQAC---RGDELDGGVPVEDSVA--DPESEGEDDAIYK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564   150 VHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQ-ERKRPLLDLHIELNGYMYDWNSRVSAKEKYYVWLQHTLRK 228
Cdd:smart00115 156 IPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEyARSLDLLDILTEVNRKVADKFESVNAKKQMPTIESMTLTK 235

                   ....*.
gi 321267564   229 KLILSY 234
Cdd:smart00115 236 KLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
1-232 2.31e-82

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: 245.97  E-value: 2.31e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564   1 MKSKPLGICLII------------DCIGNETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACmPEHRDYDSFVCVLV 68
Cdd:cd00032    4 MNSKRRGLALIInnenfdkglkdrDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSFVCVIL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564  69 SRGGSQSVYGVDqtHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYVVSEGQLEDSSLLEVDGPAMknVEFKAQKRGLC 148
Cdd:cd00032   83 SHGEEGGIYGTD--GDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPD--VETEAEDDAVQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564 149 TVHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQER-KRPLLDLHIELNGYMYDWNSRVSAKeKYYVWLQHTLR 227
Cdd:cd00032  159 TIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAhSLDLLDILTKVNRKVAEKFESVNGK-KQMPCFRSTLT 237

                 ....*
gi 321267564 228 KKLIL 232
Cdd:cd00032  238 KKLYF 242
Peptidase_C14 pfam00656
Caspase domain;
7-231 9.83e-42

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 141.31  E-value: 9.83e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564    7 GICLII----------DCIG--NETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLV---SRG 71
Cdd:pfam00656   2 GLALIIgnnnypgtkaPLRGcdNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGHG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564   72 GSQ---SVYGVDQTHsgLPLHHIRRMFMGDSC-PYLAGKPKMFFIQnyvVSEGQLEDSSLLevdgpamknvefkaqkrgl 147
Cdd:pfam00656  82 EQVpggDIYGTDEYL--VPVDALTNLFTGDDClPSLVGKPKLFIID---ACRGNLEDGGVV------------------- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564  148 ctvhrEADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQER-KRPLLDLHIELNGYMYDWnsrvSAKEKYYVWLQHTL 226
Cdd:pfam00656 138 -----EADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGhGLDLLSLLTKVRRRVAEA----TGKKQMPCLSSSTL 208

                  ....*
gi 321267564  227 RKKLI 231
Cdd:pfam00656 209 TKKFY 213
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
1-234 4.96e-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: 300.69  E-value: 4.96e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564     1 MKSKPLGICLIIDCIGNE-----------TELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLVS 69
Cdd:smart00115   3 MNSKPRGLALIINNENFHslprrngtdvdAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVCVLLS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564    70 RGGSQSVYGVDqtHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYvvsEGQLEDSSLLEVDGPAmkNVEFKAQKRGLCT 149
Cdd:smart00115  83 HGEEGGIYGTD--GDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQAC---RGDELDGGVPVEDSVA--DPESEGEDDAIYK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564   150 VHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQ-ERKRPLLDLHIELNGYMYDWNSRVSAKEKYYVWLQHTLRK 228
Cdd:smart00115 156 IPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEyARSLDLLDILTEVNRKVADKFESVNAKKQMPTIESMTLTK 235

                   ....*.
gi 321267564   229 KLILSY 234
Cdd:smart00115 236 KLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
1-232 2.31e-82

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: 245.97  E-value: 2.31e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564   1 MKSKPLGICLII------------DCIGNETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACmPEHRDYDSFVCVLV 68
Cdd:cd00032    4 MNSKRRGLALIInnenfdkglkdrDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSFVCVIL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564  69 SRGGSQSVYGVDqtHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYVVSEGQLEDSSLLEVDGPAMknVEFKAQKRGLC 148
Cdd:cd00032   83 SHGEEGGIYGTD--GDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPD--VETEAEDDAVQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564 149 TVHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQER-KRPLLDLHIELNGYMYDWNSRVSAKeKYYVWLQHTLR 227
Cdd:cd00032  159 TIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAhSLDLLDILTKVNRKVAEKFESVNGK-KQMPCFRSTLT 237

                 ....*
gi 321267564 228 KKLIL 232
Cdd:cd00032  238 KKLYF 242
Peptidase_C14 pfam00656
Caspase domain;
7-231 9.83e-42

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 141.31  E-value: 9.83e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564    7 GICLII----------DCIG--NETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLV---SRG 71
Cdd:pfam00656   2 GLALIIgnnnypgtkaPLRGcdNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGHG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564   72 GSQ---SVYGVDQTHsgLPLHHIRRMFMGDSC-PYLAGKPKMFFIQnyvVSEGQLEDSSLLevdgpamknvefkaqkrgl 147
Cdd:pfam00656  82 EQVpggDIYGTDEYL--VPVDALTNLFTGDDClPSLVGKPKLFIID---ACRGNLEDGGVV------------------- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267564  148 ctvhrEADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQER-KRPLLDLHIELNGYMYDWnsrvSAKEKYYVWLQHTL 226
Cdd:pfam00656 138 -----EADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGhGLDLLSLLTKVRRRVAEA----TGKKQMPCLSSSTL 208

                  ....*
gi 321267564  227 RKKLI 231
Cdd:pfam00656 209 TKKFY 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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