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Conserved domains on  [gi|15718704|ref|NP_001219|]
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caspase-8 isoform 1 precursor [Homo sapiens]

Protein Classification

caspase( domain architecture ID 10170020)

caspase is a cysteine-dependent aspartate-directed protease that mediates programmed cell death; belongs to the peptidase C14 family

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 242-494 5.50e-116

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: 341.50  E-value: 5.50e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704 242 VYQMKSKPRGYCLIINNHNFakarekvpkLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDH 321
Cdd:cd00032   1 IYKMNSKRRGLALIINNENF---------DKGLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDH 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704 322 SNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMD 401
Cdd:cd00032  72 SDSDSFVCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPDVETE 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704 402 LSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRgDDILTILTEVNYEVSNKDDKKNMGKQMP 481
Cdd:cd00032 152 AEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHS-LDLLDILTKVNRKVAEKFESVNGKKQMP 230

                       250
                ....*....|...
gi 15718704 482 QPTFTLRKKLVFP 494
Cdd:cd00032 231 CFRSTLTKKLYFF 243
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 3-84 1.33e-42

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: 146.00  E-value: 1.33e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704   3 FSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTR 82
Cdd:cd08333   1 FRKLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALFLALQEKGMLEEGNLSFLKELLFRIGRIDLLTSHLGVS 80


                ..
gi 15718704  83 KE 84
Cdd:cd08333  81 RE 82
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 134-212 6.06e-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 cd08813:

Pssm-ID: 472698  Cd Length: 83  Bit Score: 128.38  E-value: 6.06e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15718704 134 RVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEE 212
Cdd:cd08813   5 RVLLFQLSENVTRDELKSFKFLLQNELPKSKLDDETTLLDIFIEMEKKGILGEDNLDMLKRICAKINKSLLKKIEDYEE 83
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 242-494 5.50e-116

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: 341.50  E-value: 5.50e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704 242 VYQMKSKPRGYCLIINNHNFakarekvpkLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDH 321
Cdd:cd00032   1 IYKMNSKRRGLALIINNENF---------DKGLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDH 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704 322 SNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMD 401
Cdd:cd00032  72 SDSDSFVCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPDVETE 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704 402 LSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRgDDILTILTEVNYEVSNKDDKKNMGKQMP 481
Cdd:cd00032 152 AEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHS-LDLLDILTKVNRKVAEKFESVNGKKQMP 230

                       250
                ....*....|...
gi 15718704 482 QPTFTLRKKLVFP 494
Cdd:cd00032 231 CFRSTLTKKLYFF 243
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 243-494 2.53e-111

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: 329.20  E-value: 2.53e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704    243 YQMKSKPRGYCLIINNHNFakarekvpklHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCT-VEQIYEILKIYQLMDH 321
Cdd:smart00115   1 YKMNSKPRGLALIINNENF----------HSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTaEEMLEELKEFAAMPEH 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704    322 SNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPyLEMD 401
Cdd:smart00115  71 SDSDSFVCVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPE-SEGE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704    402 LSSPQTryIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERcPRGDDILTILTEVNYEVSNKDDKKNMGKQMP 481
Cdd:smart00115 150 DDAIYK--IPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEY-ARSLDLLDILTEVNRKVADKFESVNAKKQMP 226

                          250
                   ....*....|....
gi 15718704    482 QPTF-TLRKKLVFP 494
Cdd:smart00115 227 TIESmTLTKKLYFF 240
Peptidase_C14 pfam00656
Caspase domain;
250-492 1.30e-66

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 213.34  E-value: 1.30e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704   250 RGYCLIINNHNFAkarekvpklHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILK-IYQLMDHSNMDCFI 328
Cdd:pfam00656   1 RGLALIIGNNNYP---------GTKAPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRdFAARADHSDGDSFV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704   329 CCIL---SHG---DKGIIYGTDGQEAPIYELTSQFTGLKC-PSLAGKPKVFFIQACQGDNYQKGipvetdseeqpylemd 401
Cdd:pfam00656  72 VVLLyysGHGeqvPGGDIYGTDEYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLEDGG---------------- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704   402 lsspqtryiPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPrGDDILTILTEVNYEVSnkddKKNMGKQMP 481
Cdd:pfam00656 136 ---------VVEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGH-GLDLLSLLTKVRRRVA----EATGKKQMP 201

                         250
                  ....*....|..
gi 15718704   482 QPTF-TLRKKLV 492
Cdd:pfam00656 202 CLSSsTLTKKFY 213
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 3-84 1.33e-42

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: 146.00  E-value: 1.33e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704   3 FSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTR 82
Cdd:cd08333   1 FRKLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALFLALQEKGMLEEGNLSFLKELLFRIGRIDLLTSHLGVS 80


                ..
gi 15718704  83 KE 84
Cdd:cd08333  81 RE 82
DED_Caspase_8_r2 cd08813
Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 134-212 6.06e-36

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: 128.38  E-value: 6.06e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15718704 134 RVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEE 212
Cdd:cd08813   5 RVLLFQLSENVTRDELKSFKFLLQNELPKSKLDDETTLLDIFIEMEKKGILGEDNLDMLKRICAKINKSLLKKIEDYEE 83
DED pfam01335
Death effector domain;
3-84 2.56e-25

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 99.09  E-value: 2.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704     3 FSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTR 82
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 15718704    83 KE 84
Cdd:pfam01335  81 RE 82
DED smart00031
Death effector domain;
1-80 6.01e-22

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 89.65  E-value: 6.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704      1 MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEpIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLN 80
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLE-IKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED pfam01335
Death effector domain;
134-212 7.75e-22

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 89.46  E-value: 7.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704   134 RVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKS-LLKIINDYEE 212
Cdd:pfam01335   2 RKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQdLLKKIEKYER 81
DED smart00031
Death effector domain;
134-210 3.65e-17

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 76.17  E-value: 3.65e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15718704    134 RVMLYQISEEVSRSELRSFKFLLQEEISKCKLdDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDY 210
Cdd:smart00031   4 RVLLLLISEELDSEELEVLLFLCKDLIPKRKL-EIKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
 
Name Accession Description Interval E-value
CASc cd00032
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 242-494 5.50e-116

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: 341.50  E-value: 5.50e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704 242 VYQMKSKPRGYCLIINNHNFakarekvpkLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDH 321
Cdd:cd00032   1 IYKMNSKRRGLALIINNENF---------DKGLKDRDGTDVDAENLTKLFESLGYEVEVKNNLTAEEILEELKEFASPDH 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704 322 SNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMD 401
Cdd:cd00032  72 SDSDSFVCVILSHGEEGGIYGTDGDVVPIDEITSLFNGDNCPSLAGKPKLFFIQACRGDELDLGVEVDSGADEPPDVETE 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704 402 LSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRgDDILTILTEVNYEVSNKDDKKNMGKQMP 481
Cdd:cd00032 152 AEDDAVQTIPVEADFLVAYSTVPGYVSWRNTKKGSWFIQSLCQVLRKYAHS-LDLLDILTKVNRKVAEKFESVNGKKQMP 230

                       250
                ....*....|...
gi 15718704 482 QPTFTLRKKLVFP 494
Cdd:cd00032 231 CFRSTLTKKLYFF 243
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 243-494 2.53e-111

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: 329.20  E-value: 2.53e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704    243 YQMKSKPRGYCLIINNHNFakarekvpklHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCT-VEQIYEILKIYQLMDH 321
Cdd:smart00115   1 YKMNSKPRGLALIINNENF----------HSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTaEEMLEELKEFAAMPEH 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704    322 SNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPyLEMD 401
Cdd:smart00115  71 SDSDSFVCVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPE-SEGE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704    402 LSSPQTryIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERcPRGDDILTILTEVNYEVSNKDDKKNMGKQMP 481
Cdd:smart00115 150 DDAIYK--IPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEY-ARSLDLLDILTEVNRKVADKFESVNAKKQMP 226

                          250
                   ....*....|....
gi 15718704    482 QPTF-TLRKKLVFP 494
Cdd:smart00115 227 TIESmTLTKKLYFF 240
Peptidase_C14 pfam00656
Caspase domain;
250-492 1.30e-66

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 213.34  E-value: 1.30e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704   250 RGYCLIINNHNFAkarekvpklHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILK-IYQLMDHSNMDCFI 328
Cdd:pfam00656   1 RGLALIIGNNNYP---------GTKAPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRdFAARADHSDGDSFV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704   329 CCIL---SHG---DKGIIYGTDGQEAPIYELTSQFTGLKC-PSLAGKPKVFFIQACQGDNYQKGipvetdseeqpylemd 401
Cdd:pfam00656  72 VVLLyysGHGeqvPGGDIYGTDEYLVPVDALTNLFTGDDClPSLVGKPKLFIIDACRGNLEDGG---------------- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704   402 lsspqtryiPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPrGDDILTILTEVNYEVSnkddKKNMGKQMP 481
Cdd:pfam00656 136 ---------VVEADFLVAYSTAPGQVSWRNTGSGSWFIQALCQVLREYGH-GLDLLSLLTKVRRRVA----EATGKKQMP 201

                         250
                  ....*....|..
gi 15718704   482 QPTF-TLRKKLV 492
Cdd:pfam00656 202 CLSSsTLTKKFY 213
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 3-84 1.33e-42

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: 146.00  E-value: 1.33e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704   3 FSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTR 82
Cdd:cd08333   1 FRKLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALFLALQEKGMLEEGNLSFLKELLFRIGRIDLLTSHLGVS 80


                ..
gi 15718704  83 KE 84
Cdd:cd08333  81 RE 82
DED_Caspase_8_r2 cd08813
Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 134-212 6.06e-36

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: 128.38  E-value: 6.06e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15718704 134 RVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEE 212
Cdd:cd08813   5 RVLLFQLSENVTRDELKSFKFLLQNELPKSKLDDETTLLDIFIEMEKKGILGEDNLDMLKRICAKINKSLLKKIEDYEE 83
DED_Caspase-like_r2 cd08775
Death effector domain, repeat 2, of initator caspase-like proteins; Death Effector Domain (DED) ...
 134-210 6.13e-30

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: 111.87  E-value: 6.13e-30
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15718704 134 RVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQI-NKSLLKIINDY 210
Cdd:cd08775   4 RVMLYQVSEELSRSELRSLKFLLQEEISSCKLDDDMNFLDIVIEMENRVLLGPGKVDILKRMLRQLrRKDLLKQINDY 81
DED_Caspase_8_10_r2 cd08334
Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 134-212 1.84e-27

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: 104.97  E-value: 1.84e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15718704 134 RVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEE 212
Cdd:cd08334   5 RVLLYEISEDLTSEDLKSLKFLLSSKLPRRKLEKNKSALDVFVEMEKRGLLSEDNLDELKKILKSLRPDLAKKINQYKE 83
DED pfam01335
Death effector domain;
3-84 2.56e-25

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 99.09  E-value: 2.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704     3 FSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTR 82
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 15718704    83 KE 84
Cdd:pfam01335  81 RE 82
DED smart00031
Death effector domain;
1-80 6.01e-22

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 89.65  E-value: 6.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704      1 MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEpIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLN 80
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLE-IKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED pfam01335
Death effector domain;
134-212 7.75e-22

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 89.46  E-value: 7.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704   134 RVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKS-LLKIINDYEE 212
Cdd:pfam01335   2 RKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQdLLKKIEKYER 81
DED_Caspase_8_10_r1 cd08792
Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 3-75 1.16e-21

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: 88.81  E-value: 1.16e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15718704   3 FSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLL 75
Cdd:cd08792   1 FRKLLLDIDEELDSDDLDALKFLCTDVLPRNKLEKVESGLDLFSRLEEQGLLSEEDPFLLAELLYRIGRKDLL 73
DED smart00031
Death effector domain;
134-210 3.65e-17

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 76.17  E-value: 3.65e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15718704    134 RVMLYQISEEVSRSELRSFKFLLQEEISKCKLdDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDY 210
Cdd:smart00031   4 RVLLLLISEELDSEELEVLLFLCKDLIPKRKL-EIKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 7-77 5.07e-14

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: 67.23  E-value: 5.07e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15718704   7 LYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLIT 77
Cdd:cd00045   5 LLKISDELTSEELRSLKFLCKDVIPAGKLERISRGRDLFTELEKQGKISPGNLSLLEELLRSIGRRDLLEK 75
DED_FADD cd08336
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ...
 1-78 6.86e-14

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: 66.82  E-value: 6.86e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15718704   1 MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITY 78
Cdd:cd08336   1 DPFKVLLLEISKSLSDEELESLKFLCKDHIGKRKLEEVQSGLDLFEALEERDKLSPENTAFLRELLKSIGREDLIRKL 78
DED_Caspase-like_r1 cd08776
Death effector domain, repeat 1, of initator caspase-like proteins; Death Effector Domain (DED) ...
 7-79 1.31e-13

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: 65.62  E-value: 1.31e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15718704   7 LYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDAlmlFQRLQEKRMLeesNLSFLKELLFRINRLDLLITYL 79
Cdd:cd08776   5 LCEVAEKLGTDEREVLLFLLNVFIPQPTLAQLIGA---LRALKEEGRL---TLPLLAECLYRAGRRDLLRSLL 71
DED_Caspase_10_r2 cd08814
Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in ...
 134-212 1.63e-11

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


Pssm-ID: 260074  Cd Length: 79  Bit Score: 60.12  E-value: 1.63e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15718704 134 RVMLYQISEEVSRSELRSFKFLLQEEISKckldDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEE 212
Cdd:cd08814   5 RQMLYELSENITSEDLKRIIFLLRDSKPK----TEMTSLELLRHLEKQGLLTENNLQILEDICKKVSPDLLKIIEKYKR 79
DED_Caspase_8_10_r2 cd08334
Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 2-66 2.56e-10

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: 56.82  E-value: 2.56e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15718704   2 DFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELL 66
Cdd:cd08334   3 PYRVLLYEISEDLTSEDLKSLKFLLSSKLPRRKLEKNKSALDVFVEMEKRGLLSEDNLDELKKIL 67
DED_Caspase_10_r1 cd08341
Death effector domain, repeat 1, of Caspase-10; Death effector domain (DED) found in ...
 1-75 4.11e-09

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: 53.21  E-value: 4.11e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15718704   1 MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLL 75
Cdd:cd08341   1 IKFNQQLLIIDENLGVEDIEALKFLCSDLLSNKKLEKVESGHDLFQHLMAEDLLNEEDYFLLAELLYIIRHHKLL 75
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 134-201 2.77e-07

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: 47.97  E-value: 2.77e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15718704 134 RVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINK 201
Cdd:cd00045   2 RQLLLKISDELTSEELRSLKFLCKDVIPAGKLERISRGRDLFTELEKQGKISPGNLSLLEELLRSIGR 69
DED_PEA15 cd08338
Death Effector Domain of Astrocyte phosphoprotein PEA-15; Death Effector Domain (DED) similar ...
 2-84 5.29e-06

Death Effector Domain of Astrocyte phosphoprotein PEA-15; Death Effector Domain (DED) similar to that found in PEA-15 (Astrocyte phosphoprotein PEA-15). PEA-15 is a multifunctional phosphoprotein that modulates signaling pathways, like the ERK MAP kinase cascade by binding to ERK and changing its subcellular localization. It has been implicated in apoptosis, cell proliferation, and glucose metabolism. It does not possess enzymatic activity and mainly acts as an adaptor protein. PEA-15 contains an N-terminal DED domain and a C-terminal disordered region. 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 they can recruit other proteins into signaling complexes.


Pssm-ID: 260045  Cd Length: 84  Bit Score: 44.37  E-value: 5.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704   2 DFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNT 81
Cdd:cd08338   2 EYGSLLQDLTENITSEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLEKHNKLDQDNLSYIEHVFEISRRPDLLTMVVDY 81


                ...
gi 15718704  82 RKE 84
Cdd:cd08338  82 RTK 84
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 134-201 7.57e-06

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: 43.92  E-value: 7.57e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15718704 134 RVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINK 201
Cdd:cd08333   2 RKLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALFLALQEKGMLEEGNLSFLKELLFRIGR 69
DED_c-FLIP_r1 cd08337
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 7-87 3.98e-05

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


Pssm-ID: 260044  Cd Length: 80  Bit Score: 42.02  E-value: 3.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15718704   7 LYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQrlqekrmlEESNLSF--LKELLFRINRLDLLITYLNTRKE 84
Cdd:cd08337   6 LHQVEEELDTDEDEMLLFLCRDAAPDCTTAQLRDALCALN--------ERGKLTLagLAELLYRVKRFDLLKRILHLSKE 77


                ...
gi 15718704  85 EME 87
Cdd:cd08337  78 TVE 80
DED_DEDD cd08790
Death Effector Domain of DEDD; Death Effector Domain (DED) found in DEDD. DEDD has been shown ...
 10-75 1.59e-04

Death Effector Domain of DEDD; Death Effector Domain (DED) found in DEDD. DEDD has been shown to block mitotic progression by inhibiting Cdk1 and to be involved in regulating the insulin signaling cascade. DEDD can bind to itself, to DEDD2, and to the two tandem DED-containing caspases, caspase-8 and -10. In general, 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: 260058  Cd Length: 97  Bit Score: 40.87  E-value: 1.59e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15718704  10 IGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLL 75
Cdd:cd08790  12 VGDQLTHRDVRVLSFLFVDVIDEYERGRIRDGRDFLLALEKQGRCDETNFRQVLQLLRIITRHDLL 77
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 9-74 1.89e-04

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: 40.03  E-value: 1.89e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15718704   9 DIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDL 74
Cdd:cd08340   9 CVSEELDKSDLRSLIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLLEDCLRNIRRIDL 74
DED_FADD cd08336
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ...
 134-211 3.41e-04

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: 39.48  E-value: 3.41e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15718704 134 RVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKS-LLKIINDYE 211
Cdd:cd08336   4 KVLLLEISKSLSDEELESLKFLCKDHIGKRKLEEVQSGLDLFEALEERDKLSPENTAFLRELLKSIGREdLIRKLEEFE 82
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 134-192 7.16e-04

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: 38.49  E-value: 7.16e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15718704 134 RVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDIL 192
Cdd:cd08340   4 RVLMVCVSEELDKSDLRSLIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLL 62
DED_Caspase_10_r2 cd08814
Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in ...
 3-65 1.17e-03

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


Pssm-ID: 260074  Cd Length: 79  Bit Score: 37.78  E-value: 1.17e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15718704   3 FSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKqepiKDALMLFQRLQEKRMLEESNLSFLKEL 65
Cdd:cd08814   4 YRQMLYELSENITSEDLKRIIFLLRDSKPKTE----MTSLELLRHLEKQGLLTENNLQILEDI 62
DED_Caspase_8_r2 cd08813
Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 7-71 1.83e-03

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: 37.48  E-value: 1.83e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15718704   7 LYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINR 71
Cdd:cd08813   8 LFQLSENVTRDELKSFKFLLQNELPKSKLDDETTLLDIFIEMEKKGILGEDNLDMLKRICAKINK 72
 
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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