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Conserved domains on  [gi|330864823|ref|NP_001193453|]
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caspase-10 isoform 6 preproprotein [Homo sapiens]

Protein Classification

caspase family protein( domain architecture ID 10971746)

caspase family protein similar to caspases which are cysteine class enzymes that drive the terminal stages of apoptosis as well as other cellular remodeling and inflammatory events

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 ...
 241-447 1.69e-99

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: 297.61  E-value: 1.69e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823   241 EILSHVFQWLGFTVHIHNNVTKVEMEMVLQKQKCNPAHADGDCFVFCILTHGRFGAVYSSDEALIPIREIMSHFTALQCP 320
Cdd:smart00115  33 ENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVCVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCP 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823   321 RLAEKPKLFFIQACQGEEIQPSVSIEADALNPE--QAPTSLQdSIPAEADFLLGLATVPGYVSFRHVEEGSWYIQSLCNH 398
Cdd:smart00115 113 SLAGKPKLFFIQACRGDELDGGVPVEDSVADPEseGEDDAIY-KIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQV 191

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 330864823   399 LKKlVPRHEDILSILTAVNDDVSRRVDKQGTKKQMPQPAF-TLRKKLVFP 447
Cdd:smart00115 192 LKE-YARSLDLLDILTEVNRKVADKFESVNAKKQMPTIESmTLTKKLYFF 240
DED_Caspase_10_r2 cd08814
Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in ...
 112-190 8.89e-40

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: 137.54  E-value: 8.89e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330864823 112 VSLFRNLLYELSEGIDSENLKDMIFLLKDSLPKTEMTSLSFLAFLEKQGKIDEDNLTCLEDLCKTVVPKLLRNIEKYKR 190
Cdd:cd08814    1 VSSYRQMLYELSENITSEDLKRIIFLLRDSKPKTEMTSLELLRHLEKQGLLTENNLQILEDICKKVSPDLLKIIEKYKR 79
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 18-99 9.22e-36

Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. 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. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.


The actual alignment was detected with superfamily member cd08341:

Pssm-ID: 472698  Cd Length: 82  Bit Score: 127.17  E-value: 9.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823  18 VSFREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEKSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQHLNC 97
Cdd:cd08341    1 IKFNQQLLIIDENLGVEDIEALKFLCSDLLSNKKLEKVESGHDLFQHLMAEDLLNEEDYFLLAELLYIIRHHKLLQKLGY 80


                 ..
gi 330864823  98 TK 99
Cdd:cd08341   81 TK 82
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 241-447 1.69e-99

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: 297.61  E-value: 1.69e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823   241 EILSHVFQWLGFTVHIHNNVTKVEMEMVLQKQKCNPAHADGDCFVFCILTHGRFGAVYSSDEALIPIREIMSHFTALQCP 320
Cdd:smart00115  33 ENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVCVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCP 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823   321 RLAEKPKLFFIQACQGEEIQPSVSIEADALNPE--QAPTSLQdSIPAEADFLLGLATVPGYVSFRHVEEGSWYIQSLCNH 398
Cdd:smart00115 113 SLAGKPKLFFIQACRGDELDGGVPVEDSVADPEseGEDDAIY-KIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQV 191

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 330864823   399 LKKlVPRHEDILSILTAVNDDVSRRVDKQGTKKQMPQPAF-TLRKKLVFP 447
Cdd:smart00115 192 LKE-YARSLDLLDILTEVNRKVADKFESVNAKKQMPTIESmTLTKKLYFF 240
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 241-447 3.53e-95

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: 286.80  E-value: 3.53e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823 241 EILSHVFQWLGFTVHIHNNVTKVEMEMVLQKQKCnPAHADGDCFVFCILTHGRFGAVYSSDEALIPIREIMSHFTALQCP 320
Cdd:cd00032   35 ENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSFVCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCP 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823 321 RLAEKPKLFFIQACQGEEIQPSVSIEADALNP----EQAPTSLQDSIPAEADFLLGLATVPGYVSFRHVEEGSWYIQSLC 396
Cdd:cd00032  114 SLAGKPKLFFIQACRGDELDLGVEVDSGADEPpdveTEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLC 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 330864823 397 NHLKKLVPRhEDILSILTAVNDDVSRRVDKQGTKKQMPQPAFTLRKKLVFP 447
Cdd:cd00032  194 QVLRKYAHS-LDLLDILTKVNRKVAEKFESVNGKKQMPCFRSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
243-445 1.73e-52

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 175.59  E-value: 1.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823  243 LSHVFQWLGFTVHIHNNVTKVEMEMVLQKQKCNPAHADGDCFVFCIL---THG---RFGAVYSSDEALIPIREIMSHFTA 316
Cdd:pfam00656  29 LAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGHGeqvPGGDIYGTDEYLVPVDALTNLFTG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823  317 LQC-PRLAEKPKLFFIQACQGEEiqpsvsieadalnpeqaptslQDSIPAEADFLLGLATVPGYVSFRHVEEGSWYIQSL 395
Cdd:pfam00656 109 DDClPSLVGKPKLFIIDACRGNL---------------------EDGGVVEADFLVAYSTAPGQVSWRNTGSGSWFIQAL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 330864823  396 CNHLKKLVPRhEDILSILTAVNDDVSRRvdkqGTKKQMPQP-AFTLRKKLV 445
Cdd:pfam00656 168 CQVLREYGHG-LDLLSLLTKVRRRVAEA----TGKKQMPCLsSSTLTKKFY 213
DED_Caspase_10_r2 cd08814
Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in ...
 112-190 8.89e-40

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: 137.54  E-value: 8.89e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330864823 112 VSLFRNLLYELSEGIDSENLKDMIFLLKDSLPKTEMTSLSFLAFLEKQGKIDEDNLTCLEDLCKTVVPKLLRNIEKYKR 190
Cdd:cd08814    1 VSSYRQMLYELSENITSEDLKRIIFLLRDSKPKTEMTSLELLRHLEKQGLLTENNLQILEDICKKVSPDLLKIIEKYKR 79
DED_Caspase_10_r1 cd08341
Death effector domain, repeat 1, of Caspase-10; Death effector domain (DED) found in ...
 18-99 9.22e-36

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: 127.17  E-value: 9.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823  18 VSFREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEKSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQHLNC 97
Cdd:cd08341    1 IKFNQQLLIIDENLGVEDIEALKFLCSDLLSNKKLEKVESGHDLFQHLMAEDLLNEEDYFLLAELLYIIRHHKLLQKLGY 80


                 ..
gi 330864823  98 TK 99
Cdd:cd08341   81 TK 82
DED pfam01335
Death effector domain;
20-101 2.07e-23

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 93.31  E-value: 2.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823   20 FREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEKSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQHLNCTK 99
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 330864823  100 EE 101
Cdd:pfam01335  81 RE 82
DED pfam01335
Death effector domain;
115-191 3.75e-21

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 87.15  E-value: 3.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823  115 FRNLLYELSEGIDSENLKDMIFLLKDSLPKTEM----TSLSFLAFLEKQGKIDEDNLTCLEDLCKTVVPK-LLRNIEKYK 189
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLekikSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQdLLKKIEKYE 80


                  ..
gi 330864823  190 RE 191
Cdd:pfam01335  81 RE 82
DED smart00031
Death effector domain;
19-97 9.16e-19

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 80.41  E-value: 9.16e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330864823    19 SFREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEkSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQHLNC 97
Cdd:smart00031   2 PYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLE-IKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED smart00031
Death effector domain;
113-188 1.88e-17

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 76.55  E-value: 1.88e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330864823   113 SLFRNLLYELSEGIDSENLKDMIFLLKDSLPKTE---MTSLSFLAFLEKQGKIDEDNLTCLEDLCKTVVPKLLRNIEKY 188
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKleiKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
 
Name Accession Description Interval E-value
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 241-447 1.69e-99

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: 297.61  E-value: 1.69e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823   241 EILSHVFQWLGFTVHIHNNVTKVEMEMVLQKQKCNPAHADGDCFVFCILTHGRFGAVYSSDEALIPIREIMSHFTALQCP 320
Cdd:smart00115  33 ENLTELFQSLGYEVQVKNNLTAEEMLEELKEFAAMPEHSDSDSFVCVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCP 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823   321 RLAEKPKLFFIQACQGEEIQPSVSIEADALNPE--QAPTSLQdSIPAEADFLLGLATVPGYVSFRHVEEGSWYIQSLCNH 398
Cdd:smart00115 113 SLAGKPKLFFIQACRGDELDGGVPVEDSVADPEseGEDDAIY-KIPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQV 191

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 330864823   399 LKKlVPRHEDILSILTAVNDDVSRRVDKQGTKKQMPQPAF-TLRKKLVFP 447
Cdd:smart00115 192 LKE-YARSLDLLDILTEVNRKVADKFESVNAKKQMPTIESmTLTKKLYFF 240
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 241-447 3.53e-95

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: 286.80  E-value: 3.53e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823 241 EILSHVFQWLGFTVHIHNNVTKVEMEMVLQKQKCnPAHADGDCFVFCILTHGRFGAVYSSDEALIPIREIMSHFTALQCP 320
Cdd:cd00032   35 ENLTKLFESLGYEVEVKNNLTAEEILEELKEFAS-PDHSDSDSFVCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCP 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823 321 RLAEKPKLFFIQACQGEEIQPSVSIEADALNP----EQAPTSLQDSIPAEADFLLGLATVPGYVSFRHVEEGSWYIQSLC 396
Cdd:cd00032  114 SLAGKPKLFFIQACRGDELDLGVEVDSGADEPpdveTEAEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLC 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 330864823 397 NHLKKLVPRhEDILSILTAVNDDVSRRVDKQGTKKQMPQPAFTLRKKLVFP 447
Cdd:cd00032  194 QVLRKYAHS-LDLLDILTKVNRKVAEKFESVNGKKQMPCFRSTLTKKLYFF 243
Peptidase_C14 pfam00656
Caspase domain;
243-445 1.73e-52

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 175.59  E-value: 1.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823  243 LSHVFQWLGFTVHIHNNVTKVEMEMVLQKQKCNPAHADGDCFVFCIL---THG---RFGAVYSSDEALIPIREIMSHFTA 316
Cdd:pfam00656  29 LAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARADHSDGDSFVVVLLyysGHGeqvPGGDIYGTDEYLVPVDALTNLFTG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823  317 LQC-PRLAEKPKLFFIQACQGEEiqpsvsieadalnpeqaptslQDSIPAEADFLLGLATVPGYVSFRHVEEGSWYIQSL 395
Cdd:pfam00656 109 DDClPSLVGKPKLFIIDACRGNL---------------------EDGGVVEADFLVAYSTAPGQVSWRNTGSGSWFIQAL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 330864823  396 CNHLKKLVPRhEDILSILTAVNDDVSRRvdkqGTKKQMPQP-AFTLRKKLV 445
Cdd:pfam00656 168 CQVLREYGHG-LDLLSLLTKVRRRVAEA----TGKKQMPCLsSSTLTKKFY 213
DED_Caspase_10_r2 cd08814
Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in ...
 112-190 8.89e-40

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: 137.54  E-value: 8.89e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330864823 112 VSLFRNLLYELSEGIDSENLKDMIFLLKDSLPKTEMTSLSFLAFLEKQGKIDEDNLTCLEDLCKTVVPKLLRNIEKYKR 190
Cdd:cd08814    1 VSSYRQMLYELSENITSEDLKRIIFLLRDSKPKTEMTSLELLRHLEKQGLLTENNLQILEDICKKVSPDLLKIIEKYKR 79
DED_Caspase_10_r1 cd08341
Death effector domain, repeat 1, of Caspase-10; Death effector domain (DED) found in ...
 18-99 9.22e-36

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: 127.17  E-value: 9.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823  18 VSFREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEKSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQHLNC 97
Cdd:cd08341    1 IKFNQQLLIIDENLGVEDIEALKFLCSDLLSNKKLEKVESGHDLFQHLMAEDLLNEEDYFLLAELLYIIRHHKLLQKLGY 80


                 ..
gi 330864823  98 TK 99
Cdd:cd08341   81 TK 82
DED_Caspase_8_10_r2 cd08334
Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 112-190 1.19e-25

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: 99.58  E-value: 1.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823 112 VSLFRNLLYELSEGIDSENLKDMIFLLKDSLPKTEM----TSLSFLAFLEKQGKIDEDNLTCLEDLCKTVVPKLLRNIEK 187
Cdd:cd08334    1 ISPYRVLLYEISEDLTSEDLKSLKFLLSSKLPRRKLeknkSALDVFVEMEKRGLLSEDNLDELKKILKSLRPDLAKKINQ 80


                 ...
gi 330864823 188 YKR 190
Cdd:cd08334   81 YKE 83
DED pfam01335
Death effector domain;
20-101 2.07e-23

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 93.31  E-value: 2.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823   20 FREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEKSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQHLNCTK 99
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 330864823  100 EE 101
Cdd:pfam01335  81 RE 82
DED pfam01335
Death effector domain;
115-191 3.75e-21

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 87.15  E-value: 3.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823  115 FRNLLYELSEGIDSENLKDMIFLLKDSLPKTEM----TSLSFLAFLEKQGKIDEDNLTCLEDLCKTVVPK-LLRNIEKYK 189
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLekikSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQdLLKKIEKYE 80


                  ..
gi 330864823  190 RE 191
Cdd:pfam01335  81 RE 82
DED_Caspase_8_10_r1 cd08792
Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 20-96 5.10e-20

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: 83.80  E-value: 5.10e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330864823  20 FREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEKSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQHLN 96
Cdd:cd08792    1 FRKLLLDIDEELDSDDLDALKFLCTDVLPRNKLEKVESGLDLFSRLEEQGLLSEEDPFLLAELLYRIGRKDLLRKLG 77
DED smart00031
Death effector domain;
19-97 9.16e-19

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 80.41  E-value: 9.16e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330864823    19 SFREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEkSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQHLNC 97
Cdd:smart00031   2 PYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLE-IKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED smart00031
Death effector domain;
113-188 1.88e-17

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 76.55  E-value: 1.88e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330864823   113 SLFRNLLYELSEGIDSENLKDMIFLLKDSLPKTE---MTSLSFLAFLEKQGKIDEDNLTCLEDLCKTVVPKLLRNIEKY 188
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKleiKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 20-100 4.55e-14

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: 67.42  E-value: 4.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823  20 FREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEKSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLL-QHLNCT 98
Cdd:cd08333    1 FRKLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALFLALQEKGMLEEGNLSFLKELLFRIGRIDLLtSHLGVS 80


                 ..
gi 330864823  99 KE 100
Cdd:cd08333   81 RE 82
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 20-93 1.90e-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: 65.30  E-value: 1.90e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330864823  20 FREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEKSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQ 93
Cdd:cd00045    1 YRQLLLKISDELTSEELRSLKFLCKDVIPAGKLERISRGRDLFTELEKQGKISPGNLSLLEELLRSIGRRDLLE 74
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 115-177 3.54e-10

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: 56.06  E-value: 3.54e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330864823 115 FRNLLYELSEGIDSENLKDMIFLLKDSLPKTEMTSLS----FLAFLEKQGKIDEDNLTCLEDLCKTV 177
Cdd:cd00045    1 YRQLLLKISDELTSEELRSLKFLCKDVIPAGKLERISrgrdLFTELEKQGKISPGNLSLLEELLRSI 67
DED_Caspase_8_r2 cd08813
Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 112-188 1.03e-09

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: 54.81  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823 112 VSLFRNLLYELSEGIDSENLKDMIFLLKDSLPKT----EMTSLSFLAFLEKQGKIDEDNLTCLEDLCKTVVPKLLRNIEK 187
Cdd:cd08813    1 VSAYRVLLFQLSENVTRDELKSFKFLLQNELPKSklddETTLLDIFIEMEKKGILGEDNLDMLKRICAKINKSLLKKIED 80


                 .
gi 330864823 188 Y 188
Cdd:cd08813   81 Y 81
DED_FADD cd08336
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ...
 19-96 1.34e-09

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: 54.50  E-value: 1.34e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330864823  19 SFREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEKSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQHLN 96
Cdd:cd08336    2 PFKVLLLEISKSLSDEELESLKFLCKDHIGKRKLEEVQSGLDLFEALEERDKLSPENTAFLRELLKSIGREDLIRKLE 79
DED_FADD cd08336
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ...
 115-189 3.31e-06

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: 44.87  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823 115 FRNLLYELSEGIDSENLKDMIFLLKDSLPKTEM----TSLSFLAFLEKQGKIDEDNLTCLEDLCKTVV-PKLLRNIEKYK 189
Cdd:cd08336    3 FKVLLLEISKSLSDEELESLKFLCKDHIGKRKLeevqSGLDLFEALEERDKLSPENTAFLRELLKSIGrEDLIRKLEEFE 82
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 115-173 5.34e-05

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: 41.61  E-value: 5.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330864823 115 FRNLLYELSEGIDSENLKDMIFLLKDSLPKTEM----TSLSFLAFLEKQGKIDEDNLTCLEDL 173
Cdd:cd08333    1 FRKLLFAISEELDREDLAALKFLSLDHIPRRKQenikDALALFLALQEKGMLEEGNLSFLKEL 63
DED_Caspase_8_10_r1 cd08792
Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 115-173 1.29e-04

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: 40.27  E-value: 1.29e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330864823 115 FRNLLYELSEGIDSENLKDMIFLLKDSLPK----TEMTSLSFLAFLEKQGKIDEDNLTCLEDL 173
Cdd:cd08792    1 FRKLLLDIDEELDSDDLDALKFLCTDVLPRnkleKVESGLDLFSRLEEQGLLSEEDPFLLAEL 63
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 113-188 3.23e-03

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: 36.56  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823 113 SLFRNLLYELSEGIDSENLKDMIFLLKDSLPKTEM-TSLSFLAF---LEKQGKIDEDNLTCLEDLCKTVVP-KLLRNIEK 187
Cdd:cd08340    1 SDYRVLMVCVSEELDKSDLRSLIFLLKDLNPSGSTaKSKSFLDLvveLEKLNLVSPSSVDLLEDCLRNIRRiDLCKKIQK 80


                 .
gi 330864823 188 Y 188
Cdd:cd08340   81 Y 81
DED_Caspase-like_r2 cd08775
Death effector domain, repeat 2, of initator caspase-like proteins; Death Effector Domain (DED) ...
 113-188 9.99e-03

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: 35.22  E-value: 9.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330864823 113 SLFRNLLYELSEGIDSENLKDMIFLLKDSLPKTEMT-SLSFLAF---LEKQGKIDEDNLTCLEDLCKTVVPK-LLRNIEK 187
Cdd:cd08775    1 SAYRVMLYQVSEELSRSELRSLKFLLQEEISSCKLDdDMNFLDIvieMENRVLLGPGKVDILKRMLRQLRRKdLLKQIND 80


                 .
gi 330864823 188 Y 188
Cdd:cd08775   81 Y 81
 
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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