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Conserved domains on  [gi|1958800854|ref|XP_038938890|]
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CASP8 and FADD-like apoptosis regulator isoform X3 [Rattus norvegicus]

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_r1 cd08337
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 6-85 4.72e-32

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: 114.05  E-value: 4.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854   6 VSAEVIHQVEESLDEDEKEMMLFLCRDVTENLAPPNVRDLLDCLSERGQLSFAALAELLYRVRRFDLLKRILKTDKAAVE 85
Cdd:cd08337     1 VSAEVLHQVEEELDTDEDEMLLFLCRDAAPDCTTAQLRDALCALNERGKLTLAGLAELLYRVKRFDLLKRILHLSKETVE 80
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 96-176 8.11e-32

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: 113.60  E-value: 8.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854  96 SDYRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTKIQK 175
Cdd:cd08340     1 SDYRVLMVCVSEELDKSDLRSLIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLLEDCLRNIRRIDLCKKIQK 80


                  .
gi 1958800854 176 Y 176
Cdd:cd08340    81 Y 81
CASc super family cl00042
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ...
 249-268 8.99e-04

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.


The actual alignment was detected with superfamily member smart00115:

Pssm-ID: 444667  Cd Length: 241  Bit Score: 39.91  E-value: 8.99e-04
                           10        20
                   ....*....|....*....|
gi 1958800854  249 YRMQSKPLGICLIIDCIGND 268
Cdd:smart00115   1 YKMNSKPRGLALIINNENFH 20
 
Name Accession Description Interval E-value
DED_c-FLIP_r1 cd08337
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 6-85 4.72e-32

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: 114.05  E-value: 4.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854   6 VSAEVIHQVEESLDEDEKEMMLFLCRDVTENLAPPNVRDLLDCLSERGQLSFAALAELLYRVRRFDLLKRILKTDKAAVE 85
Cdd:cd08337     1 VSAEVLHQVEEELDTDEDEMLLFLCRDAAPDCTTAQLRDALCALNERGKLTLAGLAELLYRVKRFDLLKRILHLSKETVE 80
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 96-176 8.11e-32

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: 113.60  E-value: 8.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854  96 SDYRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTKIQK 175
Cdd:cd08340     1 SDYRVLMVCVSEELDKSDLRSLIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLLEDCLRNIRRIDLCKKIQK 80


                  .
gi 1958800854 176 Y 176
Cdd:cd08340    81 Y 81
DED pfam01335
Death effector domain;
98-179 1.72e-24

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 94.08  E-value: 1.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854  98 YRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTKIQKYT 177
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 1958800854 178 QS 179
Cdd:pfam01335  81 RE 82
DED smart00031
Death effector domain;
96-175 1.04e-19

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 81.56  E-value: 1.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854   96 SDYRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAkDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTKIQK 175
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLE-IKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED smart00031
Death effector domain;
12-78 2.37e-16

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 72.32  E-value: 2.37e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958800854   12 HQVEESLDEDEKEMMLFLCRDV--TENLAPPNVRDLLDCLSERGQLS---FAALAELLYRVRRFDLLKRILK 78
Cdd:smart00031   8 LLISEELDSEELEVLLFLCKDLipKRKLEIKTFLDLFSALEEQGLLSednLSLLAELLYRLRRLDLLRRLFG 79
DED pfam01335
Death effector domain;
9-81 1.57e-09

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 53.64  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854   9 EVIHQVEESLDEDEKEMMLFLCRDV-----TENLAppNVRDLLDCLSERGQLS---FAALAELLYRVRRFDLLKRILKTD 80
Cdd:pfam01335   3 KLLLEISEELTEEELESLKFLCKDHipkrkLEKIK--SALDLFIELEKQGLLSednLDLLEELLRRIGRQDLLKKIEKYE 80


                  .
gi 1958800854  81 K 81
Cdd:pfam01335  81 R 81
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 249-268 8.99e-04

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: 39.91  E-value: 8.99e-04
                           10        20
                   ....*....|....*....|
gi 1958800854  249 YRMQSKPLGICLIIDCIGND 268
Cdd:smart00115   1 YKMNSKPRGLALIINNENFH 20
 
Name Accession Description Interval E-value
DED_c-FLIP_r1 cd08337
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 6-85 4.72e-32

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: 114.05  E-value: 4.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854   6 VSAEVIHQVEESLDEDEKEMMLFLCRDVTENLAPPNVRDLLDCLSERGQLSFAALAELLYRVRRFDLLKRILKTDKAAVE 85
Cdd:cd08337     1 VSAEVLHQVEEELDTDEDEMLLFLCRDAAPDCTTAQLRDALCALNERGKLTLAGLAELLYRVKRFDLLKRILHLSKETVE 80
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 96-176 8.11e-32

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: 113.60  E-value: 8.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854  96 SDYRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTKIQK 175
Cdd:cd08340     1 SDYRVLMVCVSEELDKSDLRSLIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLLEDCLRNIRRIDLCKKIQK 80


                  .
gi 1958800854 176 Y 176
Cdd:cd08340    81 Y 81
DED pfam01335
Death effector domain;
98-179 1.72e-24

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 94.08  E-value: 1.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854  98 YRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTKIQKYT 177
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 1958800854 178 QS 179
Cdd:pfam01335  81 RE 82
DED smart00031
Death effector domain;
96-175 1.04e-19

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 81.56  E-value: 1.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854   96 SDYRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAkDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTKIQK 175
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLE-IKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED_Caspase_8_10_r2 cd08334
Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 95-178 6.30e-19

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


Pssm-ID: 260042  Cd Length: 83  Bit Score: 79.55  E-value: 6.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854  95 VSDYRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIhRIDLKTKIQ 174
Cdd:cd08334     1 ISPYRVLLYEISEDLTSEDLKSLKFLLSSKLPRRKLEKNKSALDVFVEMEKRGLLSEDNLDELKKILKSL-RPDLAKKIN 79


                  ....
gi 1958800854 175 KYTQ 178
Cdd:cd08334    80 QYKE 83
DED smart00031
Death effector domain;
12-78 2.37e-16

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 72.32  E-value: 2.37e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958800854   12 HQVEESLDEDEKEMMLFLCRDV--TENLAPPNVRDLLDCLSERGQLS---FAALAELLYRVRRFDLLKRILK 78
Cdd:smart00031   8 LLISEELDSEELEVLLFLCKDLipKRKLEIKTFLDLFSALEEQGLLSednLSLLAELLYRLRRLDLLRRLFG 79
DED_Caspase-like_r2 cd08775
Death effector domain, repeat 2, of initator caspase-like proteins; Death Effector Domain (DED) ...
 96-176 3.47e-13

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: 63.72  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854  96 SDYRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTKIQK 175
Cdd:cd08775     1 SAYRVMLYQVSEELSRSELRSLKFLLQEEISSCKLDDDMNFLDIVIEMENRVLLGPGKVDILKRMLRQLRRKDLLKQIND 80


                  .
gi 1958800854 176 Y 176
Cdd:cd08775    81 Y 81
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 98-173 7.28e-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: 62.99  E-value: 7.28e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958800854  98 YRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTKI 173
Cdd:cd00045     1 YRQLLLKISDELTSEELRSLKFLCKDVIPAGKLERISRGRDLFTELEKQGKISPGNLSLLEELLRSIGRRDLLEKV 76
DED_FADD cd08336
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ...
 97-176 1.18e-11

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


Pssm-ID: 260043  Cd Length: 82  Bit Score: 59.51  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854  97 DYRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTKIQKY 176
Cdd:cd08336     2 PFKVLLLEISKSLSDEELESLKFLCKDHIGKRKLEEVQSGLDLFEALEERDKLSPENTAFLRELLKSIGREDLIRKLEEF 81
DED_Caspase_8_10_r1 cd08792
Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 98-169 7.42e-10

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: 54.52  E-value: 7.42e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958800854  98 YRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDL 169
Cdd:cd08792     1 FRKLLLDIDEELDSDDLDALKFLCTDVLPRNKLEKVESGLDLFSRLEEQGLLSEEDPFLLAELLYRIGRKDL 72
DED pfam01335
Death effector domain;
9-81 1.57e-09

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 53.64  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854   9 EVIHQVEESLDEDEKEMMLFLCRDV-----TENLAppNVRDLLDCLSERGQLS---FAALAELLYRVRRFDLLKRILKTD 80
Cdd:pfam01335   3 KLLLEISEELTEEELESLKFLCKDHipkrkLEKIK--SALDLFIELEKQGLLSednLDLLEELLRRIGRQDLLKKIEKYE 80


                  .
gi 1958800854  81 K 81
Cdd:pfam01335  81 R 81
DED_Caspase-like_r1 cd08776
Death effector domain, repeat 1, of initator caspase-like proteins; Death Effector Domain (DED) ...
 7-77 6.57e-09

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


Pssm-ID: 176754  Cd Length: 71  Bit Score: 51.75  E-value: 6.57e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958800854   7 SAEVIHQVEESLDEDEKEMMLFLCRDVTENLAPPNVRDLLDCLSERGQLSFAALAELLYRVRRFDLLKRIL 77
Cdd:cd08776     1 TYEVLCEVAEKLGTDEREVLLFLLNVFIPQPTLAQLIGALRALKEEGRLTLPLLAECLYRAGRRDLLRSLL 71
DED_Caspase_10_r2 cd08814
Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in ...
 95-176 1.57e-08

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: 50.87  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854  95 VSDYRVLLMEIGENLNQSDVSSLIFLTKDYtgrgKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIhRIDLKTKIQ 174
Cdd:cd08814     1 VSSYRQMLYELSENITSEDLKRIIFLLRDS----KPKTEMTSLELLRHLEKQGLLTENNLQILEDICKKV-SPDLLKIIE 75


                  ..
gi 1958800854 175 KY 176
Cdd:cd08814    76 KY 77
DED_Caspase_8_r2 cd08813
Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 95-176 3.60e-07

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


Pssm-ID: 176791  Cd Length: 83  Bit Score: 47.11  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854  95 VSDYRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKtKIQ 174
Cdd:cd08813     1 VSAYRVLLFQLSENVTRDELKSFKFLLQNELPKSKLDDETTLLDIFIEMEKKGILGEDNLDMLKRICAKINKSLLK-KIE 79


                  ..
gi 1958800854 175 KY 176
Cdd:cd08813    80 DY 81
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 98-172 4.63e-07

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


Pssm-ID: 260041  Cd Length: 82  Bit Score: 47.00  E-value: 4.63e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958800854  98 YRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTK 172
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 ...
 9-81 2.53e-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: 44.69  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854   9 EVIHQVEESLDEDEKEMMLFLCRDVTENLAPPNVRDLLD--------CLSERGQLSFaaLAELLYRVRRFDLLKRILKTD 80
Cdd:cd08333     3 KLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALAlflalqekGMLEEGNLSF--LKELLFRIGRIDLLTSHLGVS 80


                  .
gi 1958800854  81 K 81
Cdd:cd08333    81 R 81
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 12-77 1.17e-05

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


Pssm-ID: 260016  Cd Length: 77  Bit Score: 42.57  E-value: 1.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958800854  12 HQVEESLDEDEKEMMLFLCRDV-----TENLAppNVRDLLDCLSERGQLS---FAALAELLYRVRRFDLLKRIL 77
Cdd:cd00045     6 LKISDELTSEELRSLKFLCKDVipagkLERIS--RGRDLFTELEKQGKISpgnLSLLEELLRSIGRRDLLEKVE 77
DED_Caspase_8_10_r1 cd08792
Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 14-76 2.43e-04

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


Pssm-ID: 260059  Cd Length: 77  Bit Score: 39.12  E-value: 2.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958800854  14 VEESLDEDEKEMMLFLCRDVtenlAPPNV-------RDLLDCLSERGQLSFAA---LAELLYRVRRFDLLKRI 76
Cdd:cd08792     8 IDEELDSDDLDALKFLCTDV----LPRNKlekvesgLDLFSRLEEQGLLSEEDpflLAELLYRIGRKDLLRKL 76
CASc smart00115
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ...
 249-268 8.99e-04

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: 39.91  E-value: 8.99e-04
                           10        20
                   ....*....|....*....|
gi 1958800854  249 YRMQSKPLGICLIIDCIGND 268
Cdd:smart00115   1 YKMNSKPRGLALIINNENFH 20
DED_PEA15 cd08338
Death Effector Domain of Astrocyte phosphoprotein PEA-15; Death Effector Domain (DED) similar ...
 97-176 9.34e-03

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: 34.74  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800854  97 DYRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTKIQKY 176
Cdd:cd08338     2 EYGSLLQDLTENITSEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLEKHNKLDQDNLSYIEHVFEISRRPDLLTMVVDY 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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