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Conserved domains on  [gi|51859065|gb|AAH81583|]
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Caspase 8, apoptosis-related cysteine peptidase [Danio rerio]

Protein Classification

caspase( domain architecture ID 10172010)

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 ...
 229-474 2.22e-106

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: 316.08  E-value: 2.22e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065 229 YYILTQRPLGYCLIINNYNFLKstNLLKRTGTDMDKDRLAKLFSRMHFQIEVRNDLEAWAIKDEIKQFANRNHASMGAFV 308
Cdd:cd00032   1 IYKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065 309 CCILSHGEKGTVLGTDGKPVEIREVTLPFAG--CRTLASKPKLFFIQACQGDENQAGVWTSDGREDAPEEDEKYEEDAgi 386
Cdd:cd00032  79 CVILSHGEEGGIYGTDGDVVPIDEITSLFNGdnCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPDVETEAEDDA-- 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065 387 ivLRKIPIEADFLIGMATVEHYLSYRHTKEGSIFIQELCKKMEELCpKKEDMLSILTKVNFEVSKR--ILKGYKQMPEPR 464
Cdd:cd00032 157 --VQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYA-HSLDLLDILTKVNRKVAEKfeSVNGKKQMPCFR 233

                       250
                ....*....|
gi 51859065 465 YTLTKKLVLP 474
Cdd:cd00032 234 STLTKKLYFF 243
DED_Caspase_8_10_r2 cd08334
Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 96-176 6.55e-29

Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) found in caspase-8 and caspase-10, repeat 2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis, and they play partially redundant roles. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. They contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260042  Cd Length: 83  Bit Score: 108.82  E-value: 6.55e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065  96 VSAYRKMLLKISEDMTEENFRAAKFLL--DLPRAKLGRSTSFLDALIEMEKQQRLGPDNLDELYRILEKCDKQLAVMIER 173
Cdd:cd08334   1 ISPYRVLLYEISEDLTSEDLKSLKFLLssKLPRRKLEKNKSALDVFVEMEKRGLLSEDNLDELKKILKSLRPDLAKKINQ 80


                ...
gi 51859065 174 FRN 176
Cdd:cd08334  81 YKE 83
DED_Caspase_8_10_r1 cd08792
Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 2-76 2.95e-23

Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) found in caspase-8 and caspase-10, repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis, and they play partially redundant roles. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. They contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260059  Cd Length: 77  Bit Score: 93.04  E-value: 2.95e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51859065   2 DPQIFHEIDENLTSGDVDQLKFLCLDFIPKRRLESVTDAKDLILRLDEQGLL--EDELLFPELLITIGRIDLLEILK 76
Cdd:cd08792   1 FRKLLLDIDEELDSDDLDALKFLCTDVLPRNKLEKVESGLDLFSRLEEQGLLseEDPFLLAELLYRIGRKDLLRKLG 77
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 229-474 2.22e-106

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: 316.08  E-value: 2.22e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065 229 YYILTQRPLGYCLIINNYNFLKstNLLKRTGTDMDKDRLAKLFSRMHFQIEVRNDLEAWAIKDEIKQFANRNHASMGAFV 308
Cdd:cd00032   1 IYKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065 309 CCILSHGEKGTVLGTDGKPVEIREVTLPFAG--CRTLASKPKLFFIQACQGDENQAGVWTSDGREDAPEEDEKYEEDAgi 386
Cdd:cd00032  79 CVILSHGEEGGIYGTDGDVVPIDEITSLFNGdnCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPDVETEAEDDA-- 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065 387 ivLRKIPIEADFLIGMATVEHYLSYRHTKEGSIFIQELCKKMEELCpKKEDMLSILTKVNFEVSKR--ILKGYKQMPEPR 464
Cdd:cd00032 157 --VQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYA-HSLDLLDILTKVNRKVAEKfeSVNGKKQMPCFR 233

                       250
                ....*....|
gi 51859065 465 YTLTKKLVLP 474
Cdd:cd00032 234 STLTKKLYFF 243
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 230-474 2.32e-86

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: 264.87  E-value: 2.32e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065    230 YILTQRPLGYCLIINNYNFlksTNLLKRTGTDMDKDRLAKLFSRMHFQIEVRNDLEAWAIKDEIKQFANR-NHASMGAFV 308
Cdd:smart00115   1 YKMNSKPRGLALIINNENF---HSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMpEHSDSDSFV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065    309 CCILSHGEKGTVLGTDGKPVEIREVTLPFAG--CRTLASKPKLFFIQACQGDENQAGVWTSDGREDAPEEdekYEEDAgi 386
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGdnCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPESE---GEDDA-- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065    387 ivLRKIPIEADFLIGMATVEHYLSYRHTKEGSIFIQELCKKMEELcPKKEDMLSILTKVNFEVSKRILK--GYKQMPEP- 463
Cdd:smart00115 153 --IYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEY-ARSLDLLDILTEVNRKVADKFESvnAKKQMPTIe 229

                          250
                   ....*....|.
gi 51859065    464 RYTLTKKLVLP 474
Cdd:smart00115 230 SMTLTKKLYFF 240
Peptidase_C14 pfam00656
Caspase domain;
238-472 1.26e-57

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 189.46  E-value: 1.26e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065   238 GYCLIINNYNFLKSTNllKRTGTDMDKDRLAKLFSRMHFQIEVRNDLEAWAIKDEIKQFANR-NHASMGAFVCCIL---S 313
Cdd:pfam00656   2 GLALIIGNNNYPGTKA--PLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARaDHSDGDSFVVVLLyysG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065   314 HGEK---GTVLGTDGKPVEIREVTLPFAG--C-RTLASKPKLFFIQACQGDENQAGVwtsdgredapeedekyeedagii 387
Cdd:pfam00656  80 HGEQvpgGDIYGTDEYLVPVDALTNLFTGddClPSLVGKPKLFIIDACRGNLEDGGV----------------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065   388 vlrkipIEADFLIGMATVEHYLSYRHTKEGSIFIQELCKKMEElCPKKEDMLSILTKVNFEVSKRilKGYKQMPEP-RYT 466
Cdd:pfam00656 137 ------VEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLRE-YGHGLDLLSLLTKVRRRVAEA--TGKKQMPCLsSST 207


                  ....*.
gi 51859065   467 LTKKLV 472
Cdd:pfam00656 208 LTKKFY 213
DED_Caspase_8_10_r2 cd08334
Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 96-176 6.55e-29

Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) found in caspase-8 and caspase-10, repeat 2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis, and they play partially redundant roles. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. They contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260042  Cd Length: 83  Bit Score: 108.82  E-value: 6.55e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065  96 VSAYRKMLLKISEDMTEENFRAAKFLL--DLPRAKLGRSTSFLDALIEMEKQQRLGPDNLDELYRILEKCDKQLAVMIER 173
Cdd:cd08334   1 ISPYRVLLYEISEDLTSEDLKSLKFLLssKLPRRKLEKNKSALDVFVEMEKRGLLSEDNLDELKKILKSLRPDLAKKINQ 80


                ...
gi 51859065 174 FRN 176
Cdd:cd08334  81 YKE 83
DED_Caspase_8_10_r1 cd08792
Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 2-76 2.95e-23

Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) found in caspase-8 and caspase-10, repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis, and they play partially redundant roles. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. They contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260059  Cd Length: 77  Bit Score: 93.04  E-value: 2.95e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51859065   2 DPQIFHEIDENLTSGDVDQLKFLCLDFIPKRRLESVTDAKDLILRLDEQGLL--EDELLFPELLITIGRIDLLEILK 76
Cdd:cd08792   1 FRKLLLDIDEELDSDDLDALKFLCTDVLPRNKLEKVESGLDLFSRLEEQGLLseEDPFLLAELLYRIGRKDLLRKLG 77
DED pfam01335
Death effector domain;
99-177 5.72e-18

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 78.29  E-value: 5.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065    99 YRKMLLKISEDMTEENFRAAKFLL--DLPRAKLGRSTSFLDALIEMEKQQRLGPDNLDELYRILEKCDKQ-LAVMIERFR 175
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCkdHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQdLLKKIEKYE 80


                  ..
gi 51859065   176 NQ 177
Cdd:pfam01335  81 RE 82
DED pfam01335
Death effector domain;
4-81 1.68e-17

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 77.14  E-value: 1.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065     4 QIFHEIDENLTSGDVDQLKFLCLDFIPKRRLESVTDAKDLILRLDEQGLLEDELLFP--ELLITIGRIDLLEILKKSKEE 81
Cdd:pfam01335   3 KLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLleELLRRIGRQDLLKKIEKYERE 82
DED smart00031
Death effector domain;
5-77 2.00e-10

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 56.91  E-value: 2.00e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51859065      5 IFHEIDENLTSGDVDQLKFLCLDFIPKRRLESvTDAKDLILRLDEQGLLEDELLF--PELLITIGRIDLLEILKK 77
Cdd:smart00031   6 LLLLISEELDSEELEVLLFLCKDLIPKRKLEI-KTFLDLFSALEEQGLLSEDNLSllAELLYRLRRLDLLRRLFG 79
DED smart00031
Death effector domain;
97-161 7.76e-08

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 49.59  E-value: 7.76e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51859065     97 SAYRKMLLKISEDMTEENFRAAKFLL--DLPRAKLGrSTSFLDALIEMEKQQRLGPDNLDELYRILE 161
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCkdLIPKRKLE-IKTFLDLFSALEEQGLLSEDNLSLLAELLY 66
PRK14813 PRK14813
NADH dehydrogenase subunit B; Provisional
 433-468 4.90e-04

NADH dehydrogenase subunit B; Provisional


Pssm-ID: 173274  Cd Length: 189  Bit Score: 41.02  E-value: 4.90e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 51859065  433 PKKEDMLSILTKVNFEVSKRILKGYKQMPEPRYTLT 468
Cdd:PRK14813  65 PRQSDLMIVAGTVTMKMAERVVRLYEQMPEPRYVLS 100
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 229-474 2.22e-106

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: 316.08  E-value: 2.22e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065 229 YYILTQRPLGYCLIINNYNFLKstNLLKRTGTDMDKDRLAKLFSRMHFQIEVRNDLEAWAIKDEIKQFANRNHASMGAFV 308
Cdd:cd00032   1 IYKMNSKRRGLALIINNENFDK--GLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDHSDSDSFV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065 309 CCILSHGEKGTVLGTDGKPVEIREVTLPFAG--CRTLASKPKLFFIQACQGDENQAGVWTSDGREDAPEEDEKYEEDAgi 386
Cdd:cd00032  79 CVILSHGEEGGIYGTDGDVVPIDEITSLFNGdnCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPDVETEAEDDA-- 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065 387 ivLRKIPIEADFLIGMATVEHYLSYRHTKEGSIFIQELCKKMEELCpKKEDMLSILTKVNFEVSKR--ILKGYKQMPEPR 464
Cdd:cd00032 157 --VQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYA-HSLDLLDILTKVNRKVAEKfeSVNGKKQMPCFR 233

                       250
                ....*....|
gi 51859065 465 YTLTKKLVLP 474
Cdd:cd00032 234 STLTKKLYFF 243
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 230-474 2.32e-86

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: 264.87  E-value: 2.32e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065    230 YILTQRPLGYCLIINNYNFlksTNLLKRTGTDMDKDRLAKLFSRMHFQIEVRNDLEAWAIKDEIKQFANR-NHASMGAFV 308
Cdd:smart00115   1 YKMNSKPRGLALIINNENF---HSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMpEHSDSDSFV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065    309 CCILSHGEKGTVLGTDGKPVEIREVTLPFAG--CRTLASKPKLFFIQACQGDENQAGVWTSDGREDAPEEdekYEEDAgi 386
Cdd:smart00115  78 CVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGdnCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPESE---GEDDA-- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065    387 ivLRKIPIEADFLIGMATVEHYLSYRHTKEGSIFIQELCKKMEELcPKKEDMLSILTKVNFEVSKRILK--GYKQMPEP- 463
Cdd:smart00115 153 --IYKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEY-ARSLDLLDILTEVNRKVADKFESvnAKKQMPTIe 229

                          250
                   ....*....|.
gi 51859065    464 RYTLTKKLVLP 474
Cdd:smart00115 230 SMTLTKKLYFF 240
Peptidase_C14 pfam00656
Caspase domain;
238-472 1.26e-57

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 189.46  E-value: 1.26e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065   238 GYCLIINNYNFLKSTNllKRTGTDMDKDRLAKLFSRMHFQIEVRNDLEAWAIKDEIKQFANR-NHASMGAFVCCIL---S 313
Cdd:pfam00656   2 GLALIIGNNNYPGTKA--PLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARaDHSDGDSFVVVLLyysG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065   314 HGEK---GTVLGTDGKPVEIREVTLPFAG--C-RTLASKPKLFFIQACQGDENQAGVwtsdgredapeedekyeedagii 387
Cdd:pfam00656  80 HGEQvpgGDIYGTDEYLVPVDALTNLFTGddClPSLVGKPKLFIIDACRGNLEDGGV----------------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065   388 vlrkipIEADFLIGMATVEHYLSYRHTKEGSIFIQELCKKMEElCPKKEDMLSILTKVNFEVSKRilKGYKQMPEP-RYT 466
Cdd:pfam00656 137 ------VEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLRE-YGHGLDLLSLLTKVRRRVAEA--TGKKQMPCLsSST 207


                  ....*.
gi 51859065   467 LTKKLV 472
Cdd:pfam00656 208 LTKKFY 213
DED_Caspase_8_10_r2 cd08334
Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 96-176 6.55e-29

Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) found in caspase-8 and caspase-10, repeat 2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis, and they play partially redundant roles. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. They contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260042  Cd Length: 83  Bit Score: 108.82  E-value: 6.55e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065  96 VSAYRKMLLKISEDMTEENFRAAKFLL--DLPRAKLGRSTSFLDALIEMEKQQRLGPDNLDELYRILEKCDKQLAVMIER 173
Cdd:cd08334   1 ISPYRVLLYEISEDLTSEDLKSLKFLLssKLPRRKLEKNKSALDVFVEMEKRGLLSEDNLDELKKILKSLRPDLAKKINQ 80


                ...
gi 51859065 174 FRN 176
Cdd:cd08334  81 YKE 83
DED_Caspase_8_10_r1 cd08792
Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 2-76 2.95e-23

Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) found in caspase-8 and caspase-10, repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis, and they play partially redundant roles. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. They contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260059  Cd Length: 77  Bit Score: 93.04  E-value: 2.95e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51859065   2 DPQIFHEIDENLTSGDVDQLKFLCLDFIPKRRLESVTDAKDLILRLDEQGLL--EDELLFPELLITIGRIDLLEILK 76
Cdd:cd08792   1 FRKLLLDIDEELDSDDLDALKFLCTDVLPRNKLEKVESGLDLFSRLEEQGLLseEDPFLLAELLYRIGRKDLLRKLG 77
DED pfam01335
Death effector domain;
99-177 5.72e-18

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 78.29  E-value: 5.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065    99 YRKMLLKISEDMTEENFRAAKFLL--DLPRAKLGRSTSFLDALIEMEKQQRLGPDNLDELYRILEKCDKQ-LAVMIERFR 175
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCkdHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQdLLKKIEKYE 80


                  ..
gi 51859065   176 NQ 177
Cdd:pfam01335  81 RE 82
DED pfam01335
Death effector domain;
4-81 1.68e-17

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 77.14  E-value: 1.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065     4 QIFHEIDENLTSGDVDQLKFLCLDFIPKRRLESVTDAKDLILRLDEQGLLEDELLFP--ELLITIGRIDLLEILKKSKEE 81
Cdd:pfam01335   3 KLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLleELLRRIGRQDLLKKIEKYERE 82
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 5-72 1.63e-15

Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 (CASP8, FLICE), repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260041  Cd Length: 82  Bit Score: 71.27  E-value: 1.63e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065   5 IFHEIDENLTSGDVDQLKFLCLDFIPKRRLESVTDAKDLILRLDEQGLLEDELLF--PELLITIGRIDLL 72
Cdd:cd08333   4 LLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALFLALQEKGMLEEGNLSflKELLFRIGRIDLL 73
DED_Caspase_8_r2 cd08813
Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 96-174 1.27e-14

Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 (CASP8, FLICE), repeat 2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176791  Cd Length: 83  Bit Score: 69.06  E-value: 1.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065  96 VSAYRKMLLKISEDMTEENFRAAKFLL--DLPRAKLGRSTSFLDALIEMEKQQRLGPDNLDELYRILEKCDKQLAVMIER 173
Cdd:cd08813   1 VSAYRVLLFQLSENVTRDELKSFKFLLqnELPKSKLDDETTLLDIFIEMEKKGILGEDNLDMLKRICAKINKSLLKKIED 80


                .
gi 51859065 174 F 174
Cdd:cd08813  81 Y 81
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 4-73 4.67e-13

Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a subfamily of the Death Domain (DD) superfamily. DED-containing proteins include Fas-Associated via Death Domain (FADD), Astrocyte phosphoprotein PEA-15, the initiator caspases (caspase-8 and -10), and FLICE-inhibitory protein (FLIP), among others. These proteins are prominent components of the programmed cell death (apoptosis) pathway. Some members also have non-apoptotic functions such as regulation of insulin signaling (DEDD and PEA15) and cell cycle progression (DEDD). DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260016  Cd Length: 77  Bit Score: 64.15  E-value: 4.67e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51859065   4 QIFHEIDENLTSGDVDQLKFLCLDFIPKRRLESVTDAKDLILRLDEQGLLEDELLFP--ELLITIGRIDLLE 73
Cdd:cd00045   3 QLLLKISDELTSEELRSLKFLCKDVIPAGKLERISRGRDLFTELEKQGKISPGNLSLleELLRSIGRRDLLE 74
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 99-166 1.78e-11

Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a subfamily of the Death Domain (DD) superfamily. DED-containing proteins include Fas-Associated via Death Domain (FADD), Astrocyte phosphoprotein PEA-15, the initiator caspases (caspase-8 and -10), and FLICE-inhibitory protein (FLIP), among others. These proteins are prominent components of the programmed cell death (apoptosis) pathway. Some members also have non-apoptotic functions such as regulation of insulin signaling (DEDD and PEA15) and cell cycle progression (DEDD). DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260016  Cd Length: 77  Bit Score: 59.91  E-value: 1.78e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065  99 YRKMLLKISEDMTEENFRAAKFLL--DLPRAKLGRSTSFLDALIEMEKQQRLGPDNLDELYRILEKCDKQ 166
Cdd:cd00045   1 YRQLLLKISDELTSEELRSLKFLCkdVIPAGKLERISRGRDLFTELEKQGKISPGNLSLLEELLRSIGRR 70
DED_FADD cd08336
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ...
 7-77 3.62e-11

Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) found in Fas-Associated via Death Domain (FADD). DEDs comprise a subfamily of the Death Domain (DD) superfamily. FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor and its DED recruits the initiator caspases 8 and 10 to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260043  Cd Length: 82  Bit Score: 59.12  E-value: 3.62e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51859065   7 HEIDENLTSGDVDQLKFLCLDFIPKRRLESVTDAKDLILRLDEQGLL--EDELLFPELLITIGRIDLLEILKK 77
Cdd:cd08336   8 LEISKSLSDEELESLKFLCKDHIGKRKLEEVQSGLDLFEALEERDKLspENTAFLRELLKSIGREDLIRKLEE 80
DED_Caspase_10_r2 cd08814
Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in ...
 96-176 9.88e-11

Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in Caspase-10, repeat 2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-10 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-8 and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260074  Cd Length: 79  Bit Score: 57.81  E-value: 9.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065  96 VSAYRKMLLKISEDMTEENFRAAKFLLDLPRAKlgRSTSFLDALIEMEKQQRLGPDNLDELYRILEKCDKQLAVMIERFR 175
Cdd:cd08814   1 VSSYRQMLYELSENITSEDLKRIIFLLRDSKPK--TEMTSLELLRHLEKQGLLTENNLQILEDICKKVSPDLLKIIEKYK 78


                .
gi 51859065 176 N 176
Cdd:cd08814  79 R 79
DED smart00031
Death effector domain;
5-77 2.00e-10

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 56.91  E-value: 2.00e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51859065      5 IFHEIDENLTSGDVDQLKFLCLDFIPKRRLESvTDAKDLILRLDEQGLLEDELLF--PELLITIGRIDLLEILKK 77
Cdd:smart00031   6 LLLLISEELDSEELEVLLFLCKDLIPKRKLEI-KTFLDLFSALEEQGLLSEDNLSllAELLYRLRRLDLLRRLFG 79
DED smart00031
Death effector domain;
97-161 7.76e-08

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 49.59  E-value: 7.76e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51859065     97 SAYRKMLLKISEDMTEENFRAAKFLL--DLPRAKLGrSTSFLDALIEMEKQQRLGPDNLDELYRILE 161
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCkdLIPKRKLE-IKTFLDLFSALEEQGLLSEDNLSLLAELLY 66
DED_Caspase_10_r1 cd08341
Death effector domain, repeat 1, of Caspase-10; Death effector domain (DED) found in ...
 9-79 4.55e-07

Death effector domain, repeat 1, of Caspase-10; Death effector domain (DED) found in caspase-10, repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-10 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-8 and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260047  Cd Length: 82  Bit Score: 47.43  E-value: 4.55e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51859065   9 IDENLTSGDVDQLKFLCLDFIPKRRLESVTDAKDLILRLDEQGLL--EDELLFPELLITIGRIDLLEILKKSK 79
Cdd:cd08341  10 IDENLGVEDIEALKFLCSDLLSNKKLEKVESGHDLFQHLMAEDLLneEDYFLLAELLYIIRHHKLLQKLGYTK 82
DED_Caspase-like_r2 cd08775
Death effector domain, repeat 2, of initator caspase-like proteins; Death Effector Domain (DED) ...
 97-160 5.78e-07

Death effector domain, repeat 2, of initator caspase-like proteins; Death Effector Domain (DED), second repeat, found in initator caspase-like proteins like caspase-8, -10 and c-FLIP. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of DISC. All members contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176753  Cd Length: 81  Bit Score: 47.16  E-value: 5.78e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51859065  97 SAYRKMLLKISEDMTEENFRAAKFLLDLP--RAKLGRSTSFLDALIEMEKQQRLGPDNLDELYRIL 160
Cdd:cd08775   1 SAYRVMLYQVSEELSRSELRSLKFLLQEEisSCKLDDDMNFLDIVIEMENRVLLGPGKVDILKRML 66
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 97-167 6.24e-07

Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain (DED), repeat 2, similar to that found in cellular FLICE-inhibitory protein (c-FLIP/CASH, also known as Casper/iFLICE/FLAME-1/CLARP/MRIT/usurpin). c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of the Death Inducing Signalling Complex (DISC). At low levels, c-FLIP has been shown to enhance apoptotic signaling by allosterically activating caspase-8. As a modulator of the initiator caspases, c-FLIP regulates life and death in various types of cells and tissues. All members contain two N-terminal DEDs and a C-terminal pseudo-caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260046  Cd Length: 81  Bit Score: 46.96  E-value: 6.24e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51859065  97 SAYRKMLLKISEDMTEENFRAAKFLL--DLPRAKLGRSTSFLDALIEMEKQQRLGPDNLDelyrILEKCDKQL 167
Cdd:cd08340   1 SDYRVLMVCVSEELDKSDLRSLIFLLkdLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVD----LLEDCLRNI 69
DED_c-FLIP_r1 cd08337
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 5-83 1.92e-05

Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain (DED), repeat 1, similar to that found in FLICE-inhibitory protein (c-FLIP/CASH, also known as Casper/iFLICE/FLAME-1/CLARP/MRIT/usurpin). c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of the Death Inducing Signalling Complex (DISC). At low levels, c-FLIP has been shown to enhance apoptotic signaling by allosterically activating caspase-8. As a modulator of the initiator caspases, c-FLIP regulates life and death in various types of cells and tissues. All members contain two N-terminal DEDs and a C-terminal pseudo-caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260044  Cd Length: 80  Bit Score: 42.79  E-value: 1.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065   5 IFHEIDENLTSGDVDQLKFLCLDFIPKRRLESVTDAKDLilrLDEQGLLEDELLfPELLITIGRIDLL-EILKKSKEEVE 83
Cdd:cd08337   5 VLHQVEEELDTDEDEMLLFLCRDAAPDCTTAQLRDALCA---LNERGKLTLAGL-AELLYRVKRFDLLkRILHLSKETVE 80
DED_FADD cd08336
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ...
 98-174 3.78e-05

Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) found in Fas-Associated via Death Domain (FADD). DEDs comprise a subfamily of the Death Domain (DD) superfamily. FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor and its DED recruits the initiator caspases 8 and 10 to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260043  Cd Length: 82  Bit Score: 42.17  E-value: 3.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51859065  98 AYRKMLLKISEDMTEENFRAAKFLL--DLPRAKLGRSTSFLDALIEMEKQQRLGPDNLDELYRILEKCDK-QLAVMIERF 174
Cdd:cd08336   2 PFKVLLLEISKSLSDEELESLKFLCkdHIGKRKLEEVQSGLDLFEALEERDKLSPENTAFLRELLKSIGReDLIRKLEEF 81
DED_Caspase-like_r1 cd08776
Death effector domain, repeat 1, of initator caspase-like proteins; Death Effector Domain (DED) ...
 8-72 1.49e-04

Death effector domain, repeat 1, of initator caspase-like proteins; Death Effector Domain (DED), first repeat, found in initator caspase-like proteins, like caspase-8 and -10 and c-FLIP. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of DISC. All members contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176754  Cd Length: 71  Bit Score: 40.20  E-value: 1.49e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51859065   8 EIDENLTSGDVDQLKFLCLDFIPKRRLESVTDAkdlILRLDEQGLLeDELLFPELLITIGRIDLL 72
Cdd:cd08776   7 EVAEKLGTDEREVLLFLLNVFIPQPTLAQLIGA---LRALKEEGRL-TLPLLAECLYRAGRRDLL 67
PRK14813 PRK14813
NADH dehydrogenase subunit B; Provisional
 433-468 4.90e-04

NADH dehydrogenase subunit B; Provisional


Pssm-ID: 173274  Cd Length: 189  Bit Score: 41.02  E-value: 4.90e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 51859065  433 PKKEDMLSILTKVNFEVSKRILKGYKQMPEPRYTLT 468
Cdd:PRK14813  65 PRQSDLMIVAGTVTMKMAERVVRLYEQMPEPRYVLS 100
DED_Caspase_10_r2 cd08814
Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in ...
 4-80 1.88e-03

Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in Caspase-10, repeat 2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-10 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-8 and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260074  Cd Length: 79  Bit Score: 37.01  E-value: 1.88e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51859065   4 QIFHEIDENLTSGDVDQLKFLCLDFIPKRRLESVtdakDLILRLDEQGLL-EDELLFPELLITIGRIDLLEILKKSKE 80
Cdd:cd08814   6 QMLYELSENITSEDLKRIIFLLRDSKPKTEMTSL----ELLRHLEKQGLLtENNLQILEDICKKVSPDLLKIIEKYKR 79
 
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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