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Conserved domains on  [gi|1034606539|ref|XP_016881891|]
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DNA-binding death effector domain-containing protein 2 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 14-119 1.04e-55

Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.


The actual alignment was detected with superfamily member cd08791:

Pssm-ID: 472698  Cd Length: 106  Bit Score: 177.73  E-value: 1.04e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606539  14 EDECLDYYGMLSLHRMFEVVGGQLTECELELLAFLLDEAPGAAGGLARARSGLELLLELERRGQCDESNLRLLGQLLRVL 93
Cdd:cd08791     1 EDECLSYYGMLSLHRMFEVVGSQLTETCGGELAFLLDETYPGKHPLDRPKSGVELLLELERRGYCDESNLRPLLQLLRVL 80

                          90       100
                  ....*....|....*....|....*.
gi 1034606539  94 ARHDLLPHLARKRRRPVSPERYSYGT 119
Cdd:cd08791    81 TRHDLLPFVSQKRRRTVSPERYKYGY 106
 
Name Accession Description Interval E-value
DED_DEDD2 cd08791
Death Effector Domain of DEDD2; Death Effector Domain (DED) found in DEDD2. DEDD2 has been ...
 14-119 1.04e-55

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: 177.73  E-value: 1.04e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606539  14 EDECLDYYGMLSLHRMFEVVGGQLTECELELLAFLLDEAPGAAGGLARARSGLELLLELERRGQCDESNLRLLGQLLRVL 93
Cdd:cd08791     1 EDECLSYYGMLSLHRMFEVVGSQLTETCGGELAFLLDETYPGKHPLDRPKSGVELLLELERRGYCDESNLRPLLQLLRVL 80

                          90       100
                  ....*....|....*....|....*.
gi 1034606539  94 ARHDLLPHLARKRRRPVSPERYSYGT 119
Cdd:cd08791    81 TRHDLLPFVSQKRRRTVSPERYKYGY 106
DED pfam01335
Death effector domain;
26-108 2.51e-08

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 50.56  E-value: 2.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606539  26 LHRMFEVVGGQLTECELELLAFLL-DEAPgaAGGLARARSGLELLLELERRGQCDESNLRLLGQLLRVLARHDLLPHLAR 104
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCkDHIP--KRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEK 78


                  ....
gi 1034606539 105 KRRR 108
Cdd:pfam01335  79 YERE 82
DED smart00031
Death effector domain;
25-102 2.12e-06

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 44.97  E-value: 2.12e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034606539   25 SLHRMFEVVGGQLTECELELLAFLL-DEAPGAAGGlarARSGLELLLELERRGQCDESNLRLLGQLLRVLARHDLLPHL 102
Cdd:smart00031   2 PYRVLLLLISEELDSEELEVLLFLCkDLIPKRKLE---IKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRL 77
 
Name Accession Description Interval E-value
DED_DEDD2 cd08791
Death Effector Domain of DEDD2; Death Effector Domain (DED) found in DEDD2. DEDD2 has been ...
 14-119 1.04e-55

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: 177.73  E-value: 1.04e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606539  14 EDECLDYYGMLSLHRMFEVVGGQLTECELELLAFLLDEAPGAAGGLARARSGLELLLELERRGQCDESNLRLLGQLLRVL 93
Cdd:cd08791     1 EDECLSYYGMLSLHRMFEVVGSQLTETCGGELAFLLDETYPGKHPLDRPKSGVELLLELERRGYCDESNLRPLLQLLRVL 80

                          90       100
                  ....*....|....*....|....*.
gi 1034606539  94 ARHDLLPHLARKRRRPVSPERYSYGT 119
Cdd:cd08791    81 TRHDLLPFVSQKRRRTVSPERYKYGY 106
DED_DEDD-like cd08339
Death Effector Domain of DEDD and DEDD2; Death Effector Domain (DED) found in DEDD and DEDD2. ...
 22-118 6.94e-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: 105.15  E-value: 6.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606539  22 GMLSLHRMFEVVGGQLTECELELLAFLLDEAPGAAGGLaRARSGLELLLELERRGQCDESNLRLLGQLLRVLARHDLLPH 101
Cdd:cd08339     1 GLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDYERG-MIRSGRDFLLALERQGRCDETNFRQVLQLLRIITRHDLLPY 79

                          90
                  ....*....|....*..
gi 1034606539 102 LARKRRRPVSPERYSYG 118
Cdd:cd08339    80 VTLKRRRAVCPDLVDKY 96
DED_DEDD cd08790
Death Effector Domain of DEDD; Death Effector Domain (DED) found in DEDD. DEDD has been shown ...
 22-113 3.93e-16

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: 73.23  E-value: 3.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606539  22 GMLSLHRMFEVVGGQLTECELELLAFLLDEAPGAAGgLARARSGLELLLELERRGQCDESNLRLLGQLLRVLARHDLLPH 101
Cdd:cd08790     1 GLYSLHRMFDIVGDQLTHRDVRVLSFLFVDVIDEYE-RGRIRDGRDFLLALEKQGRCDETNFRQVLQLLRIITRHDLLPY 79

                          90
                  ....*....|..
gi 1034606539 102 LARKRRRPVSPE 113
Cdd:cd08790    80 VTLRKRRAVCPD 91
DED pfam01335
Death effector domain;
26-108 2.51e-08

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 50.56  E-value: 2.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606539  26 LHRMFEVVGGQLTECELELLAFLL-DEAPgaAGGLARARSGLELLLELERRGQCDESNLRLLGQLLRVLARHDLLPHLAR 104
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCkDHIP--KRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEK 78


                  ....
gi 1034606539 105 KRRR 108
Cdd:pfam01335  79 YERE 82
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 26-99 1.01e-06

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: 46.04  E-value: 1.01e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034606539  26 LHRMFEVVGGQLTECELELLAFLL-DEAPgaAGGLARARSGLELLLELERRGQCDESNLRLLGQLLRVLARHDLL 99
Cdd:cd00045     1 YRQLLLKISDELTSEELRSLKFLCkDVIP--AGKLERISRGRDLFTELEKQGKISPGNLSLLEELLRSIGRRDLL 73
DED smart00031
Death effector domain;
25-102 2.12e-06

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 44.97  E-value: 2.12e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034606539   25 SLHRMFEVVGGQLTECELELLAFLL-DEAPGAAGGlarARSGLELLLELERRGQCDESNLRLLGQLLRVLARHDLLPHL 102
Cdd:smart00031   2 PYRVLLLLISEELDSEELEVLLFLCkDLIPKRKLE---IKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRL 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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