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Conserved domains on  [gi|1083330322|ref|XP_018615687|]
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death effector domain-containing protein [Scleropages formosus]

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 ...
 107-203 1.23e-59

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: 188.79  E-value: 1.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083330322 107 GLYSLHRMFEIVGAQLTHRDVRVLSFLFVDVIDEYERGGIRSGRDFLLALERQGRCDETNFRHVLQLLRIITRHDLLPYV 186
Cdd:cd08790     1 GLYSLHRMFDIVGDQLTHRDVRVLSFLFVDVIDEYERGRIRDGRDFLLALEKQGRCDETNFRQVLQLLRIITRHDLLPYV 80

                          90
                  ....*....|....*..
gi 1083330322 187 TLRKRQTVCPDPVDKYL 203
Cdd:cd08790    81 TLRKRRAVCPDPVDKYL 97
AvrBs3 super family cl49339
type III secretion system effector avirulence protein AvrBs3;
196-299 4.51e-03

type III secretion system effector avirulence protein AvrBs3;


The actual alignment was detected with superfamily member NF041308:

Pssm-ID: 469205 [Multi-domain]  Cd Length: 1179  Bit Score: 39.56  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083330322  196 PDPVDKYLEETSVRYVSPRG----GENKEPTSHRRTG--PQPVICCSPTGPQVCPPRVKPGPPVPSRKRKRAHTAADC-- 267
Cdd:NF041308    78 PSLFDPSLFDSSPAFGAHHAdaapGEMDEVQSGLRAAddPQSHLSAAVTAPSPTPPRTQAAARRRSAQTSDASPAESVdl 157

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1083330322  268 -----REKQTCDIRLRVRAEYCQHESALQGNVFSNKQ 299
Cdd:NF041308   158 stlgyTQQQQEQIKPNARSTVAQHHAALVGHGFTHAH 194
 
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 ...
 107-203 1.23e-59

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: 188.79  E-value: 1.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083330322 107 GLYSLHRMFEIVGAQLTHRDVRVLSFLFVDVIDEYERGGIRSGRDFLLALERQGRCDETNFRHVLQLLRIITRHDLLPYV 186
Cdd:cd08790     1 GLYSLHRMFDIVGDQLTHRDVRVLSFLFVDVIDEYERGRIRDGRDFLLALEKQGRCDETNFRQVLQLLRIITRHDLLPYV 80

                          90
                  ....*....|....*..
gi 1083330322 187 TLRKRQTVCPDPVDKYL 203
Cdd:cd08790    81 TLRKRRAVCPDPVDKYL 97
DED smart00031
Death effector domain;
109-187 9.36e-18

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 77.32  E-value: 9.36e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083330322  109 YSLHRMFEIVGAQLTHRDVRVLSFLFVDVIDEyERGGIRSGRDFLLALERQGRCDETNFRHVLQLLRIITRHDLLPYVT 187
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPK-RKLEIKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLF 78
DED pfam01335
Death effector domain;
111-192 6.72e-16

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 72.13  E-value: 6.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083330322 111 LHRMFEIVGAQLTHRDVRVLSFLFVDVIDEYERGGIRSGRDFLLALERQGRCDETNFRHVLQLLRIITRHDLLPYVTLRK 190
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 1083330322 191 RQ 192
Cdd:pfam01335  81 RE 82
AvrBs3 NF041308
type III secretion system effector avirulence protein AvrBs3;
196-299 4.51e-03

type III secretion system effector avirulence protein AvrBs3;


Pssm-ID: 469205 [Multi-domain]  Cd Length: 1179  Bit Score: 39.56  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083330322  196 PDPVDKYLEETSVRYVSPRG----GENKEPTSHRRTG--PQPVICCSPTGPQVCPPRVKPGPPVPSRKRKRAHTAADC-- 267
Cdd:NF041308    78 PSLFDPSLFDSSPAFGAHHAdaapGEMDEVQSGLRAAddPQSHLSAAVTAPSPTPPRTQAAARRRSAQTSDASPAESVdl 157

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1083330322  268 -----REKQTCDIRLRVRAEYCQHESALQGNVFSNKQ 299
Cdd:NF041308   158 stlgyTQQQQEQIKPNARSTVAQHHAALVGHGFTHAH 194
 
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 ...
 107-203 1.23e-59

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: 188.79  E-value: 1.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083330322 107 GLYSLHRMFEIVGAQLTHRDVRVLSFLFVDVIDEYERGGIRSGRDFLLALERQGRCDETNFRHVLQLLRIITRHDLLPYV 186
Cdd:cd08790     1 GLYSLHRMFDIVGDQLTHRDVRVLSFLFVDVIDEYERGRIRDGRDFLLALEKQGRCDETNFRQVLQLLRIITRHDLLPYV 80

                          90
                  ....*....|....*..
gi 1083330322 187 TLRKRQTVCPDPVDKYL 203
Cdd:cd08790    81 TLRKRRAVCPDPVDKYL 97
DED_DEDD2 cd08791
Death Effector Domain of DEDD2; Death Effector Domain (DED) found in DEDD2. DEDD2 has been ...
 106-197 5.97e-29

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: 108.78  E-value: 5.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083330322 106 YGLYSLHRMFEIVGAQLTHRDVRVLSFLfvdvIDEYERGG-----IRSGRDFLLALERQGRCDETNFRHVLQLLRIITRH 180
Cdd:cd08791     8 YGMLSLHRMFEVVGSQLTETCGGELAFL----LDETYPGKhpldrPKSGVELLLELERRGYCDESNLRPLLQLLRVLTRH 83

                          90
                  ....*....|....*..
gi 1083330322 181 DLLPYVTLRKRQTVCPD 197
Cdd:cd08791    84 DLLPFVSQKRRRTVSPE 100
DED_DEDD-like cd08339
Death Effector Domain of DEDD and DEDD2; Death Effector Domain (DED) found in DEDD and DEDD2. ...
 107-197 1.05e-26

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: 102.46  E-value: 1.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083330322 107 GLYSLHRMFEIVGAQLTHRDVRVLSFLFVDVIDEYERGGIRSGRDFLLALERQGRCDETNFRHVLQLLRIITRHDLLPYV 186
Cdd:cd08339     1 GLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDYERGMIRSGRDFLLALERQGRCDETNFRQVLQLLRIITRHDLLPYV 80

                          90
                  ....*....|.
gi 1083330322 187 TLRKRQTVCPD 197
Cdd:cd08339    81 TLKRRRAVCPD 91
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 111-187 2.64e-20

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: 84.18  E-value: 2.64e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083330322 111 LHRMFEIVGAQLTHRDVRVLSFLFVDVIDEYERGGIRSGRDFLLALERQGRCDETNFRHVLQLLRIITRHDLLPYVT 187
Cdd:cd00045     1 YRQLLLKISDELTSEELRSLKFLCKDVIPAGKLERISRGRDLFTELEKQGKISPGNLSLLEELLRSIGRRDLLEKVE 77
DED smart00031
Death effector domain;
109-187 9.36e-18

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 77.32  E-value: 9.36e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083330322  109 YSLHRMFEIVGAQLTHRDVRVLSFLFVDVIDEyERGGIRSGRDFLLALERQGRCDETNFRHVLQLLRIITRHDLLPYVT 187
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPK-RKLEIKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLF 78
DED pfam01335
Death effector domain;
111-192 6.72e-16

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 72.13  E-value: 6.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083330322 111 LHRMFEIVGAQLTHRDVRVLSFLFVDVIDEYERGGIRSGRDFLLALERQGRCDETNFRHVLQLLRIITRHDLLPYVTLRK 190
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80


                  ..
gi 1083330322 191 RQ 192
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) ...
 111-183 1.17e-07

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: 48.75  E-value: 1.17e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083330322 111 LHRMFEIVGAQLTHRDVRVLSFLFVDVIDEYERGGIRSGRDFLLALERQGRCDETNFRHVLQLLRIITRHDLL 183
Cdd:cd08792     1 FRKLLLDIDEELDSDDLDALKFLCTDVLPRNKLEKVESGLDLFSRLEEQGLLSEEDPFLLAELLYRIGRKDLL 73
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 114-183 1.01e-03

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: 37.76  E-value: 1.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083330322 114 MFEIvGAQLTHRDVRVLSFLFVDVIDEYERGGIRSGRDFLLALERQGRCDETNFRHVLQLLRIITRHDLL 183
Cdd:cd08333     5 LFAI-SEELDREDLAALKFLSLDHIPRRKQENIKDALALFLALQEKGMLEEGNLSFLKELLFRIGRIDLL 73
AvrBs3 NF041308
type III secretion system effector avirulence protein AvrBs3;
196-299 4.51e-03

type III secretion system effector avirulence protein AvrBs3;


Pssm-ID: 469205 [Multi-domain]  Cd Length: 1179  Bit Score: 39.56  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083330322  196 PDPVDKYLEETSVRYVSPRG----GENKEPTSHRRTG--PQPVICCSPTGPQVCPPRVKPGPPVPSRKRKRAHTAADC-- 267
Cdd:NF041308    78 PSLFDPSLFDSSPAFGAHHAdaapGEMDEVQSGLRAAddPQSHLSAAVTAPSPTPPRTQAAARRRSAQTSDASPAESVdl 157

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1083330322  268 -----REKQTCDIRLRVRAEYCQHESALQGNVFSNKQ 299
Cdd:NF041308   158 stlgyTQQQQEQIKPNARSTVAQHHAALVGHGFTHAH 194
DED_FADD cd08336
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ...
 118-187 7.28e-03

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: 35.24  E-value: 7.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083330322 118 VGAQLTHRDVRVLSFLFVDVIDEYERGGIRSGRDFLLALERQGRCDETNFRHVLQLLRIITRHDLLPYVT 187
Cdd:cd08336    10 ISKSLSDEELESLKFLCKDHIGKRKLEEVQSGLDLFEALEERDKLSPENTAFLRELLKSIGREDLIRKLE 79
 
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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