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Conserved domains on  [gi|321267567|ref|NP_001189445|]
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CASP8 and FADD-like apoptosis regulator isoform 4 [Homo sapiens]

Protein Classification

DED_c-FLIP_r2 and CASc domain-containing protein( domain architecture ID 10871149)

protein containing domains DED_c-FLIP_r1, DED_c-FLIP_r2, and CASc

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 ...
 209-444 7.23e-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: 308.40  E-value: 7.23e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   209 YKMKSKPLGICLIIDCIGNE-----------TELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVL 277
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHslprrngtdvdAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVCVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   278 VSRGGSQSVYGVDqtHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYvvsEGQLEDSSLLEVDGPAmkNVEFKAQKRGL 357
Cdd:smart00115  81 LSHGEEGGIYGTD--GDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQAC---RGDELDGGVPVEDSVA--DPESEGEDDAI 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   358 CTVHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQ-ERKRPLLDLHIELNGYMYDWNSRVSAKEKYYVWLQHTL 436
Cdd:smart00115 154 YKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEyARSLDLLDILTEVNRKVADKFESVNAKKQMPTIESMTL 233


                   ....*...
gi 321267567   437 RKKLILSY 444
Cdd:smart00115 234 TKKLYFFP 241
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 91-171 6.39e-38

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: 132.48  E-value: 6.39e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  91 SDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQK 170
Cdd:cd08340    1 SDYRVLMVCVSEELDKSDLRSLIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLLEDCLRNIRRIDLCKKIQK 80


                 .
gi 321267567 171 Y 171
Cdd:cd08340   81 Y 81
DED_c-FLIP_r1 cd08337
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 1-80 2.68e-34

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: 122.91  E-value: 2.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   1 MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVE 80
Cdd:cd08337    1 VSAEVLHQVEEELDTDEDEMLLFLCRDAAPDCTTAQLRDALCALNERGKLTLAGLAELLYRVKRFDLLKRILHLSKETVE 80
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 209-444 7.23e-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: 308.40  E-value: 7.23e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   209 YKMKSKPLGICLIIDCIGNE-----------TELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVL 277
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHslprrngtdvdAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVCVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   278 VSRGGSQSVYGVDqtHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYvvsEGQLEDSSLLEVDGPAmkNVEFKAQKRGL 357
Cdd:smart00115  81 LSHGEEGGIYGTD--GDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQAC---RGDELDGGVPVEDSVA--DPESEGEDDAI 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   358 CTVHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQ-ERKRPLLDLHIELNGYMYDWNSRVSAKEKYYVWLQHTL 436
Cdd:smart00115 154 YKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEyARSLDLLDILTEVNRKVADKFESVNAKKQMPTIESMTL 233


                   ....*...
gi 321267567   437 RKKLILSY 444
Cdd:smart00115 234 TKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 208-442 3.39e-81

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: 250.60  E-value: 3.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567 208 RYKMKSKPLGICLII------------DCIGNETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACmPEHRDYDSFVC 275
Cdd:cd00032    1 IYKMNSKRRGLALIInnenfdkglkdrDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSFVC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567 276 VLVSRGGSQSVYGVDqtHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYVVSEGQLEDSSLLEVDGPAMknVEFKAQKR 355
Cdd:cd00032   80 VILSHGEEGGIYGTD--GDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPD--VETEAEDD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567 356 GLCTVHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQER-KRPLLDLHIELNGYMYDWNSRVSAKeKYYVWLQH 434
Cdd:cd00032  156 AVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAhSLDLLDILTKVNRKVAEKFESVNGK-KQMPCFRS 234


                 ....*...
gi 321267567 435 TLRKKLIL 442
Cdd:cd00032  235 TLTKKLYF 242
Peptidase_C14 pfam00656
Caspase domain;
217-441 3.50e-39

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 140.53  E-value: 3.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  217 GICLII----------DCIG--NETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLV---SRG 281
Cdd:pfam00656   2 GLALIIgnnnypgtkaPLRGcdNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGHG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  282 GSQ---SVYGVDQTHsgLPLHHIRRMFMGDSC-PYLAGKPKMFFIQnyvVSEGQLEDSSLLevdgpamknvefkaqkrgl 357
Cdd:pfam00656  82 EQVpggDIYGTDEYL--VPVDALTNLFTGDDClPSLVGKPKLFIID---ACRGNLEDGGVV------------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  358 ctvhrEADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQER-KRPLLDLHIELNGYMYDWnsrvSAKEKYYVWLQHTL 436
Cdd:pfam00656 138 -----EADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGhGLDLLSLLTKVRRRVAEA----TGKKQMPCLSSSTL 208


                  ....*
gi 321267567  437 RKKLI 441
Cdd:pfam00656 209 TKKFY 213
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 91-171 6.39e-38

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: 132.48  E-value: 6.39e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  91 SDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQK 170
Cdd:cd08340    1 SDYRVLMVCVSEELDKSDLRSLIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLLEDCLRNIRRIDLCKKIQK 80


                 .
gi 321267567 171 Y 171
Cdd:cd08340   81 Y 81
DED_c-FLIP_r1 cd08337
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 1-80 2.68e-34

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: 122.91  E-value: 2.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   1 MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVE 80
Cdd:cd08337    1 VSAEVLHQVEEELDTDEDEMLLFLCRDAAPDCTTAQLRDALCALNERGKLTLAGLAELLYRVKRFDLLKRILHLSKETVE 80
DED pfam01335
Death effector domain;
93-174 4.68e-24

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 95.24  E-value: 4.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   93 YRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKYK 172
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 321267567  173 QS 174
Cdd:pfam01335  81 RE 82
DED smart00031
Death effector domain;
91-170 1.07e-17

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 77.32  E-value: 1.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567    91 SDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKeKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQK 170
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLEI-KTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED smart00031
Death effector domain;
7-73 7.92e-12

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 60.76  E-value: 7.92e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 321267567     7 HQVEEALDTDEKEMLLFLCRDVAID--VVPPNVRDLLDILRERGKLSVGD---LAELLYRVRRFDLLKRILK 73
Cdd:smart00031   8 LLISEELDSEELEVLLFLCKDLIPKrkLEIKTFLDLFSALEEQGLLSEDNlslLAELLYRLRRLDLLRRLFG 79
DED pfam01335
Death effector domain;
4-77 7.68e-10

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 55.18  E-value: 7.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567    4 EVIHQVEEALDTDEKEMLLFLCRDVaidvVPP-------NVRDLLDILRERGKLSVGD---LAELLYRVRRFDLLKRILK 73
Cdd:pfam01335   3 KLLLEISEELTEEELESLKFLCKDH----IPKrklekikSALDLFIELEKQGLLSEDNldlLEELLRRIGRQDLLKKIEK 78


                  ....
gi 321267567   74 MDRK 77
Cdd:pfam01335  79 YERE 82
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 209-444 7.23e-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: 308.40  E-value: 7.23e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   209 YKMKSKPLGICLIIDCIGNE-----------TELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVL 277
Cdd:smart00115   1 YKMNSKPRGLALIINNENFHslprrngtdvdAENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVCVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   278 VSRGGSQSVYGVDqtHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYvvsEGQLEDSSLLEVDGPAmkNVEFKAQKRGL 357
Cdd:smart00115  81 LSHGEEGGIYGTD--GDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQAC---RGDELDGGVPVEDSVA--DPESEGEDDAI 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   358 CTVHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQ-ERKRPLLDLHIELNGYMYDWNSRVSAKEKYYVWLQHTL 436
Cdd:smart00115 154 YKIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEyARSLDLLDILTEVNRKVADKFESVNAKKQMPTIESMTL 233


                   ....*...
gi 321267567   437 RKKLILSY 444
Cdd:smart00115 234 TKKLYFFP 241
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 208-442 3.39e-81

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: 250.60  E-value: 3.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567 208 RYKMKSKPLGICLII------------DCIGNETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACmPEHRDYDSFVC 275
Cdd:cd00032    1 IYKMNSKRRGLALIInnenfdkglkdrDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSFVC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567 276 VLVSRGGSQSVYGVDqtHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYVVSEGQLEDSSLLEVDGPAMknVEFKAQKR 355
Cdd:cd00032   80 VILSHGEEGGIYGTD--GDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPD--VETEAEDD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567 356 GLCTVHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQER-KRPLLDLHIELNGYMYDWNSRVSAKeKYYVWLQH 434
Cdd:cd00032  156 AVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAhSLDLLDILTKVNRKVAEKFESVNGK-KQMPCFRS 234


                 ....*...
gi 321267567 435 TLRKKLIL 442
Cdd:cd00032  235 TLTKKLYF 242
Peptidase_C14 pfam00656
Caspase domain;
217-441 3.50e-39

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 140.53  E-value: 3.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  217 GICLII----------DCIG--NETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLV---SRG 281
Cdd:pfam00656   2 GLALIIgnnnypgtkaPLRGcdNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGHG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  282 GSQ---SVYGVDQTHsgLPLHHIRRMFMGDSC-PYLAGKPKMFFIQnyvVSEGQLEDSSLLevdgpamknvefkaqkrgl 357
Cdd:pfam00656  82 EQVpggDIYGTDEYL--VPVDALTNLFTGDDClPSLVGKPKLFIID---ACRGNLEDGGVV------------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  358 ctvhrEADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQER-KRPLLDLHIELNGYMYDWnsrvSAKEKYYVWLQHTL 436
Cdd:pfam00656 138 -----EADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGhGLDLLSLLTKVRRRVAEA----TGKKQMPCLSSSTL 208


                  ....*
gi 321267567  437 RKKLI 441
Cdd:pfam00656 209 TKKFY 213
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 91-171 6.39e-38

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: 132.48  E-value: 6.39e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  91 SDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQK 170
Cdd:cd08340    1 SDYRVLMVCVSEELDKSDLRSLIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLLEDCLRNIRRIDLCKKIQK 80


                 .
gi 321267567 171 Y 171
Cdd:cd08340   81 Y 81
DED_c-FLIP_r1 cd08337
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 1-80 2.68e-34

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: 122.91  E-value: 2.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   1 MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVE 80
Cdd:cd08337    1 VSAEVLHQVEEELDTDEDEMLLFLCRDAAPDCTTAQLRDALCALNERGKLTLAGLAELLYRVKRFDLLKRILHLSKETVE 80
DED pfam01335
Death effector domain;
93-174 4.68e-24

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 95.24  E-value: 4.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567   93 YRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKYK 172
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 321267567  173 QS 174
Cdd:pfam01335  81 RE 82
DED_Caspase_8_10_r2 cd08334
Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 90-173 1.51e-18

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: 79.93  E-value: 1.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  90 VSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIhRIDLKTKIQ 169
Cdd:cd08334    1 ISPYRVLLYEISEDLTSEDLKSLKFLLSSKLPRRKLEKNKSALDVFVEMEKRGLLSEDNLDELKKILKSL-RPDLAKKIN 79


                 ....
gi 321267567 170 KYKQ 173
Cdd:cd08334   80 QYKE 83
DED smart00031
Death effector domain;
91-170 1.07e-17

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 77.32  E-value: 1.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567    91 SDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKeKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQK 170
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLEI-KTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED_Caspase-like_r2 cd08775
Death effector domain, repeat 2, of initator caspase-like proteins; Death Effector Domain (DED) ...
 91-171 2.95e-14

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: 67.57  E-value: 2.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  91 SDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQK 170
Cdd:cd08775    1 SAYRVMLYQVSEELSRSELRSLKFLLQEEISSCKLDDDMNFLDIVIEMENRVLLGPGKVDILKRMLRQLRRKDLLKQIND 80


                 .
gi 321267567 171 Y 171
Cdd:cd08775   81 Y 81
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 93-168 1.31e-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: 65.69  E-value: 1.31e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 321267567  93 YRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKI 168
Cdd:cd00045    1 YRQLLLKISDELTSEELRSLKFLCKDVIPAGKLERISRGRDLFTELEKQGKISPGNLSLLEELLRSIGRRDLLEKV 76
DED smart00031
Death effector domain;
7-73 7.92e-12

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 60.76  E-value: 7.92e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 321267567     7 HQVEEALDTDEKEMLLFLCRDVAID--VVPPNVRDLLDILRERGKLSVGD---LAELLYRVRRFDLLKRILK 73
Cdd:smart00031   8 LLISEELDSEELEVLLFLCKDLIPKrkLEIKTFLDLFSALEEQGLLSEDNlslLAELLYRLRRLDLLRRLFG 79
DED_Caspase_8_10_r1 cd08792
Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 93-164 1.14e-11

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: 60.30  E-value: 1.14e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 321267567  93 YRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDL 164
Cdd:cd08792    1 FRKLLLDIDEELDSDDLDALKFLCTDVLPRNKLEKVESGLDLFSRLEEQGLLSEEDPFLLAELLYRIGRKDL 72
DED_Caspase_10_r2 cd08814
Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in ...
 90-172 1.04e-10

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: 57.42  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  90 VSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRgkisKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIhRIDLKTKIQ 169
Cdd:cd08814    1 VSSYRQMLYELSENITSEDLKRIIFLLRDSKPK----TEMTSLELLRHLEKQGLLTENNLQILEDICKKV-SPDLLKIIE 75


                 ...
gi 321267567 170 KYK 172
Cdd:cd08814   76 KYK 78
DED_FADD cd08336
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ...
 92-172 1.32e-10

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: 57.19  E-value: 1.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  92 DYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKY 171
Cdd:cd08336    2 PFKVLLLEISKSLSDEELESLKFLCKDHIGKRKLEEVQSGLDLFEALEERDKLSPENTAFLRELLKSIGREDLIRKLEEF 81


                 .
gi 321267567 172 K 172
Cdd:cd08336   82 E 82
DED pfam01335
Death effector domain;
4-77 7.68e-10

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 55.18  E-value: 7.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567    4 EVIHQVEEALDTDEKEMLLFLCRDVaidvVPP-------NVRDLLDILRERGKLSVGD---LAELLYRVRRFDLLKRILK 73
Cdd:pfam01335   3 KLLLEISEELTEEELESLKFLCKDH----IPKrklekikSALDLFIELEKQGLLSEDNldlLEELLRRIGRQDLLKKIEK 78


                  ....
gi 321267567   74 MDRK 77
Cdd:pfam01335  79 YERE 82
DED_Caspase_8_10_r1 cd08792
Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 9-71 1.15e-08

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: 51.83  E-value: 1.15e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321267567   9 VEEALDTDEKEMLLFLCRdvaiDVVPPNV-------RDLLDILRERGKLSVGD---LAELLYRVRRFDLLKRI 71
Cdd:cd08792    8 IDEELDSDDLDALKFLCT----DVLPRNKlekvesgLDLFSRLEEQGLLSEEDpflLAELLYRIGRKDLLRKL 76
DED_Caspase-like_r1 cd08776
Death effector domain, repeat 1, of initator caspase-like proteins; Death Effector Domain (DED) ...
 2-72 1.47e-08

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: 51.37  E-value: 1.47e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 321267567   2 SAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRIL 72
Cdd:cd08776    1 TYEVLCEVAEKLGTDEREVLLFLLNVFIPQPTLAQLIGALRALKEEGRLTLPLLAECLYRAGRRDLLRSLL 71
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 93-167 3.38e-07

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: 47.77  E-value: 3.38e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 321267567  93 YRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTK 167
Cdd:cd08333    1 FRKLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALFLALQEKGMLEEGNLSFLKELLFRIGRIDLLTS 75
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 4-76 3.58e-07

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: 47.77  E-value: 3.58e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321267567   4 EVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDI---LRERGKLSVGDLA---ELLYRVRRFDLLKRILKMDR 76
Cdd:cd08333    3 KLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALflaLQEKGMLEEGNLSflkELLFRIGRIDLLTSHLGVSR 81
DED_Caspase_8_r2 cd08813
Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 90-173 6.85e-07

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: 46.72  E-value: 6.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321267567  90 VSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKtKIQ 169
Cdd:cd08813    1 VSAYRVLLFQLSENVTRDELKSFKFLLQNELPKSKLDDETTLLDIFIEMEKKGILGEDNLDMLKRICAKINKSLLK-KIE 79


                 ....
gi 321267567 170 KYKQ 173
Cdd:cd08813   80 DYEE 83
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 7-72 4.79e-05

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: 41.42  E-value: 4.79e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 321267567   7 HQVEEALDTDEKEMLLFLCRDVaidvVPP-------NVRDLLDILRERGKLSVGD---LAELLYRVRRFDLLKRIL 72
Cdd:cd00045    6 LKISDELTSEELRSLKFLCKDV----IPAgklerisRGRDLFTELEKQGKISPGNlslLEELLRSIGRRDLLEKVE 77
 
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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