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Conserved domains on  [gi|1751216177|ref|XP_030772216|]
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CASP8 and FADD-like apoptosis regulator isoform X2 [Rhinopithecus roxellana]

Protein Classification

protein kinase family protein( domain architecture ID 10170031)

protein kinase family protein containing a Death domain (DD), may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 119-199 8.71e-38

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


:

Pssm-ID: 260046  Cd Length: 81  Bit Score: 127.08  E-value: 8.71e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177 119 SDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQK 198
Cdd:cd08340     1 SDYRVLMVCVSEELDKSDLRSLIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLLEDCLRNIRRIDLCKKIQK 80


                  .
gi 1751216177 199 Y 199
Cdd:cd08340    81 Y 81
DED_c-FLIP_r1 cd08337
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 29-108 3.42e-34

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


:

Pssm-ID: 260044  Cd Length: 80  Bit Score: 117.90  E-value: 3.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177  29 MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVE 108
Cdd:cd08337     1 VSAEVLHQVEEELDTDEDEMLLFLCRDAAPDCTTAQLRDALCALNERGKLTLAGLAELLYRVKRFDLLKRILHLSKETVE 80
 
Name Accession Description Interval E-value
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 119-199 8.71e-38

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


Pssm-ID: 260046  Cd Length: 81  Bit Score: 127.08  E-value: 8.71e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177 119 SDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQK 198
Cdd:cd08340     1 SDYRVLMVCVSEELDKSDLRSLIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLLEDCLRNIRRIDLCKKIQK 80


                  .
gi 1751216177 199 Y 199
Cdd:cd08340    81 Y 81
DED_c-FLIP_r1 cd08337
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 29-108 3.42e-34

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


Pssm-ID: 260044  Cd Length: 80  Bit Score: 117.90  E-value: 3.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177  29 MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVE 108
Cdd:cd08337     1 VSAEVLHQVEEELDTDEDEMLLFLCRDAAPDCTTAQLRDALCALNERGKLTLAGLAELLYRVKRFDLLKRILHLSKETVE 80
DED pfam01335
Death effector domain;
121-202 2.47e-24

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 92.16  E-value: 2.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177 121 YRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKYK 200
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 1751216177 201 QS 202
Cdd:pfam01335  81 RE 82
DED smart00031
Death effector domain;
119-198 7.62e-18

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 75.40  E-value: 7.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177  119 SDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKeKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQK 198
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLEI-KTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED smart00031
Death effector domain;
35-101 1.07e-11

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 58.83  E-value: 1.07e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751216177   35 HQVEEALDTDEKEMLLFLCRDVAID--VVPPNVRDLLDILRERGKLSVGD---LAELLYRVRRFDLLKRILK 101
Cdd:smart00031   8 LLISEELDSEELEVLLFLCKDLIPKrkLEIKTFLDLFSALEEQGLLSEDNlslLAELLYRLRRLDLLRRLFG 79
DED pfam01335
Death effector domain;
32-105 1.63e-09

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 53.25  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177  32 EVIHQVEEALDTDEKEMLLFLCRDVaidvVPP-------NVRDLLDILRERGKLSVGD---LAELLYRVRRFDLLKRILK 101
Cdd:pfam01335   3 KLLLEISEELTEEELESLKFLCKDH----IPKrklekikSALDLFIELEKQGLLSEDNldlLEELLRRIGRQDLLKKIEK 78


                  ....
gi 1751216177 102 MDRK 105
Cdd:pfam01335  79 YERE 82
 
Name Accession Description Interval E-value
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 119-199 8.71e-38

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


Pssm-ID: 260046  Cd Length: 81  Bit Score: 127.08  E-value: 8.71e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177 119 SDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQK 198
Cdd:cd08340     1 SDYRVLMVCVSEELDKSDLRSLIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLLEDCLRNIRRIDLCKKIQK 80


                  .
gi 1751216177 199 Y 199
Cdd:cd08340    81 Y 81
DED_c-FLIP_r1 cd08337
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 29-108 3.42e-34

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


Pssm-ID: 260044  Cd Length: 80  Bit Score: 117.90  E-value: 3.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177  29 MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVE 108
Cdd:cd08337     1 VSAEVLHQVEEELDTDEDEMLLFLCRDAAPDCTTAQLRDALCALNERGKLTLAGLAELLYRVKRFDLLKRILHLSKETVE 80
DED pfam01335
Death effector domain;
121-202 2.47e-24

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 92.16  E-value: 2.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177 121 YRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKYK 200
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 1751216177 201 QS 202
Cdd:pfam01335  81 RE 82
DED_Caspase_8_10_r2 cd08334
Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 118-201 3.52e-18

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


Pssm-ID: 260042  Cd Length: 83  Bit Score: 76.47  E-value: 3.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177 118 VSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIhRIDLKTKIQ 197
Cdd:cd08334     1 ISPYRVLLYEISEDLTSEDLKSLKFLLSSKLPRRKLEKNKSALDVFVEMEKRGLLSEDNLDELKKILKSL-RPDLAKKIN 79


                  ....
gi 1751216177 198 KYKQ 201
Cdd:cd08334    80 QYKE 83
DED smart00031
Death effector domain;
119-198 7.62e-18

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 75.40  E-value: 7.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177  119 SDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKeKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQK 198
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLEI-KTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED_Caspase-like_r2 cd08775
Death effector domain, repeat 2, of initator caspase-like proteins; Death Effector Domain (DED) ...
 119-199 4.16e-14

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


Pssm-ID: 176753  Cd Length: 81  Bit Score: 65.65  E-value: 4.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177 119 SDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQK 198
Cdd:cd08775     1 SAYRVMLYQVSEELSRSELRSLKFLLQEEISSCKLDDDMNFLDIVIEMENRVLLGPGKVDILKRMLRQLRRKDLLKQIND 80


                  .
gi 1751216177 199 Y 199
Cdd:cd08775    81 Y 81
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 121-196 7.60e-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: 61.83  E-value: 7.60e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751216177 121 YRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKI 196
Cdd:cd00045     1 YRQLLLKISDELTSEELRSLKFLCKDVIPAGKLERISRGRDLFTELEKQGKISPGNLSLLEELLRSIGRRDLLEKV 76
DED smart00031
Death effector domain;
35-101 1.07e-11

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 58.83  E-value: 1.07e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751216177   35 HQVEEALDTDEKEMLLFLCRDVAID--VVPPNVRDLLDILRERGKLSVGD---LAELLYRVRRFDLLKRILK 101
Cdd:smart00031   8 LLISEELDSEELEVLLFLCKDLIPKrkLEIKTFLDLFSALEEQGLLSEDNlslLAELLYRLRRLDLLRRLFG 79
DED_Caspase_8_10_r1 cd08792
Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 121-192 3.55e-11

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


Pssm-ID: 260059  Cd Length: 77  Bit Score: 57.61  E-value: 3.55e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751216177 121 YRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDL 192
Cdd:cd08792     1 FRKLLLDIDEELDSDDLDALKFLCTDVLPRNKLEKVESGLDLFSRLEEQGLLSEEDPFLLAELLYRIGRKDL 72
DED_FADD cd08336
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ...
 120-200 6.16e-11

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


Pssm-ID: 260043  Cd Length: 82  Bit Score: 56.81  E-value: 6.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177 120 DYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKY 199
Cdd:cd08336     2 PFKVLLLEISKSLSDEELESLKFLCKDHIGKRKLEEVQSGLDLFEALEERDKLSPENTAFLRELLKSIGREDLIRKLEEF 81


                  .
gi 1751216177 200 K 200
Cdd:cd08336    82 E 82
DED_Caspase_10_r2 cd08814
Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in ...
 118-200 1.30e-10

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


Pssm-ID: 260074  Cd Length: 79  Bit Score: 55.88  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177 118 VSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRgkinKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIhRIDLKTKIQ 197
Cdd:cd08814     1 VSSYRQMLYELSENITSEDLKRIIFLLRDSKPK----TEMTSLELLRHLEKQGLLTENNLQILEDICKKV-SPDLLKIIE 75


                  ...
gi 1751216177 198 KYK 200
Cdd:cd08814    76 KYK 78
DED pfam01335
Death effector domain;
32-105 1.63e-09

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 53.25  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177  32 EVIHQVEEALDTDEKEMLLFLCRDVaidvVPP-------NVRDLLDILRERGKLSVGD---LAELLYRVRRFDLLKRILK 101
Cdd:pfam01335   3 KLLLEISEELTEEELESLKFLCKDH----IPKrklekikSALDLFIELEKQGLLSEDNldlLEELLRRIGRQDLLKKIEK 78


                  ....
gi 1751216177 102 MDRK 105
Cdd:pfam01335  79 YERE 82
DED_Caspase-like_r1 cd08776
Death effector domain, repeat 1, of initator caspase-like proteins; Death Effector Domain (DED) ...
 30-100 2.49e-08

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


Pssm-ID: 176754  Cd Length: 71  Bit Score: 49.44  E-value: 2.49e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751216177  30 SAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRIL 100
Cdd:cd08776     1 TYEVLCEVAEKLGTDEREVLLFLLNVFIPQPTLAQLIGALRALKEEGRLTLPLLAECLYRAGRRDLLRSLL 71
DED_Caspase_8_10_r1 cd08792
Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 37-99 3.56e-08

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


Pssm-ID: 260059  Cd Length: 77  Bit Score: 49.13  E-value: 3.56e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751216177  37 VEEALDTDEKEMLLFLCRDVAIDVVPPNV---RDLLDILRERGKLSVGD---LAELLYRVRRFDLLKRI 99
Cdd:cd08792     8 IDEELDSDDLDALKFLCTDVLPRNKLEKVesgLDLFSRLEEQGLLSEEDpflLAELLYRIGRKDLLRKL 76
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 121-195 4.65e-07

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


Pssm-ID: 260041  Cd Length: 82  Bit Score: 46.23  E-value: 4.65e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751216177 121 YRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTK 195
Cdd:cd08333     1 FRKLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALFLALQEKGMLEEGNLSFLKELLFRIGRIDLLTS 75
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 32-104 6.28e-07

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


Pssm-ID: 260041  Cd Length: 82  Bit Score: 45.85  E-value: 6.28e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751216177  32 EVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDI---LRERGKLSVGDLA---ELLYRVRRFDLLKRILKMDR 104
Cdd:cd08333     3 KLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALflaLQEKGMLEEGNLSflkELLFRIGRIDLLTSHLGVSR 81
DED_Caspase_8_r2 cd08813
Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 118-201 1.72e-06

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: 44.79  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751216177 118 VSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKINKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKtKIQ 197
Cdd:cd08813     1 VSAYRVLLFQLSENVTRDELKSFKFLLQNELPKSKLDDETTLLDIFIEMEKKGILGEDNLDMLKRICAKINKSLLK-KIE 79


                  ....
gi 1751216177 198 KYKQ 201
Cdd:cd08813    80 DYEE 83
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 35-100 1.20e-04

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: 39.49  E-value: 1.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751216177  35 HQVEEALDTDEKEMLLFLCRDVaidvVPP-------NVRDLLDILRERGKLSVGD---LAELLYRVRRFDLLKRIL 100
Cdd:cd00045     6 LKISDELTSEELRSLKFLCKDV----IPAgklerisRGRDLFTELEKQGKISPGNlslLEELLRSIGRRDLLEKVE 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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