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Conserved domains on  [gi|21759089|sp|O75618|]
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RecName: Full=Death effector domain-containing protein; AltName: Full=DEDPro1; AltName: Full=Death effector domain-containing testicular molecule; AltName: Full=FLDED-1

Protein Classification

protein kinase family protein( domain architecture ID 10172004)

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_DEDD cd08790
Death Effector Domain of DEDD; Death Effector Domain (DED) found in DEDD. DEDD has been shown ...
 22-118 1.64e-53

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: 170.30  E-value: 1.64e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21759089  22 GLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYV 101
Cdd:cd08790   1 GLYSLHRMFDIVGDQLTHRDVRVLSFLFVDVIDEYERGRIRDGRDFLLALEKQGRCDETNFRQVLQLLRIITRHDLLPYV 80

                        90
                ....*....|....*..
gi 21759089 102 TLKRRRAVCPDLVDKYL 118
Cdd:cd08790  81 TLRKRRAVCPDPVDKYL 97
 
Name Accession Description Interval E-value
DED_DEDD cd08790
Death Effector Domain of DEDD; Death Effector Domain (DED) found in DEDD. DEDD has been shown ...
 22-118 1.64e-53

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: 170.30  E-value: 1.64e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21759089  22 GLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYV 101
Cdd:cd08790   1 GLYSLHRMFDIVGDQLTHRDVRVLSFLFVDVIDEYERGRIRDGRDFLLALEKQGRCDETNFRQVLQLLRIITRHDLLPYV 80

                        90
                ....*....|....*..
gi 21759089 102 TLKRRRAVCPDLVDKYL 118
Cdd:cd08790  81 TLRKRRAVCPDPVDKYL 97
DED smart00031
Death effector domain;
24-102 9.85e-19

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 79.25  E-value: 9.85e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21759089     24 YSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGlIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYVT 102
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLE-IKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLF 78
DED pfam01335
Death effector domain;
26-107 1.23e-12

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 62.50  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21759089    26 LHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYVTLKR 105
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 21759089   106 RR 107
Cdd:pfam01335  81 RE 82
 
Name Accession Description Interval E-value
DED_DEDD cd08790
Death Effector Domain of DEDD; Death Effector Domain (DED) found in DEDD. DEDD has been shown ...
 22-118 1.64e-53

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: 170.30  E-value: 1.64e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21759089  22 GLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYV 101
Cdd:cd08790   1 GLYSLHRMFDIVGDQLTHRDVRVLSFLFVDVIDEYERGRIRDGRDFLLALEKQGRCDETNFRQVLQLLRIITRHDLLPYV 80

                        90
                ....*....|....*..
gi 21759089 102 TLKRRRAVCPDLVDKYL 118
Cdd:cd08790  81 TLRKRRAVCPDPVDKYL 97
DED_DEDD-like cd08339
Death Effector Domain of DEDD and DEDD2; Death Effector Domain (DED) found in DEDD and DEDD2. ...
 22-112 5.27e-28

Death Effector Domain of DEDD and DEDD2; Death Effector Domain (DED) found in DEDD and DEDD2. Both proteins have a single N-terminal DED and a long C-terminal portion with no known domains. DEDD has been shown to block mitotic progression by inhibiting Cdk1 and to be involved in regulating the insulin signaling cascade. DEDD and DEDD2 can bind to themselves, to each other, 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 they can recruit other proteins into signaling complexes.


Pssm-ID: 176750  Cd Length: 97  Bit Score: 104.38  E-value: 5.27e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21759089  22 GLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYV 101
Cdd:cd08339   1 GLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDYERGMIRSGRDFLLALERQGRCDETNFRQVLQLLRIITRHDLLPYV 80

                        90
                ....*....|.
gi 21759089 102 TLKRRRAVCPD 112
Cdd:cd08339  81 TLKRRRAVCPD 91
DED_DEDD2 cd08791
Death Effector Domain of DEDD2; Death Effector Domain (DED) found in DEDD2. DEDD2 has been ...
 21-112 2.04e-27

Death Effector Domain of DEDD2; Death Effector Domain (DED) found in DEDD2. DEDD2 has been shown to bind to itself, DEDD, and to the two tandem DED-containing caspases, caspase-8 and -10. It may play a role in apoptosis. 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. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways.


Pssm-ID: 176769  Cd Length: 106  Bit Score: 103.00  E-value: 2.04e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21759089  21 HGLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVID-DHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLP 99
Cdd:cd08791   8 YGMLSLHRMFEVVGSQLTETCGGELAFLLDETYPgKHPLDRPKSGVELLLELERRGYCDESNLRPLLQLLRVLTRHDLLP 87

                        90
                ....*....|...
gi 21759089 100 YVTLKRRRAVCPD 112
Cdd:cd08791  88 FVSQKRRRTVSPE 100
DED smart00031
Death effector domain;
24-102 9.85e-19

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 79.25  E-value: 9.85e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21759089     24 YSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGlIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYVT 102
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLE-IKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLF 78
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 26-102 1.89e-18

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: 78.40  E-value: 1.89e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21759089  26 LHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYVT 102
Cdd:cd00045   1 YRQLLLKISDELTSEELRSLKFLCKDVIPAGKLERISRGRDLFTELEKQGKISPGNLSLLEELLRSIGRRDLLEKVE 77
DED pfam01335
Death effector domain;
26-107 1.23e-12

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 62.50  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21759089    26 LHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYVTLKR 105
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 21759089   106 RR 107
Cdd:pfam01335  81 RE 82
DED_Caspase_8_10_r1 cd08792
Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 26-98 1.22e-06

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: 45.66  E-value: 1.22e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21759089  26 LHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLL 98
Cdd:cd08792   1 FRKLLLDIDEELDSDDLDALKFLCTDVLPRNKLEKVESGLDLFSRLEEQGLLSEEDPFLLAELLYRIGRKDLL 73
 
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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