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Conserved domains on  [gi|21355807|ref|NP_651006|]
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Fas-associated death domain [Drosophila melanogaster]

Protein Classification

DD and Death domain-containing protein( domain architecture ID 10327233)

DD and Death domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 154-234 1.82e-17

Death Domain: a protein-protein interaction domain; Death Domains (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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they 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. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


:

Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 74.24  E-value: 1.82e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355807 154 VFKKISEELGRYWRRLGRSAGIGEGQMDTIEERYPHDLKSQILRLLQLIEEDDCHDpkHFLLRLCRALGDCGRNDLRKRV 233
Cdd:cd01670   1 YFDLVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDE--ATLGRLIQALREIGRRDLAEKL 78


                .
gi 21355807 234 E 234
Cdd:cd01670  79 E 79
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 22-71 5.05e-03

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 cd08336:

Pssm-ID: 472698  Cd Length: 82  Bit Score: 34.85  E-value: 5.05e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21355807  22 ENVEQLKLIFVEEIGSRRRSDcIRTIEDLIDCLERADELSEYNVEPLRRI 71
Cdd:cd08336  17 EELESLKFLCKDHIGKRKLEE-VQSGLDLFEALEERDKLSPENTAFLREL 65
 
Name Accession Description Interval E-value
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 154-234 1.82e-17

Death Domain: a protein-protein interaction domain; Death Domains (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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they 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. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 74.24  E-value: 1.82e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355807 154 VFKKISEELGRYWRRLGRSAGIGEGQMDTIEERYPHDLKSQILRLLQLIEEDDCHDpkHFLLRLCRALGDCGRNDLRKRV 233
Cdd:cd01670   1 YFDLVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDE--ATLGRLIQALREIGRRDLAEKL 78


                .
gi 21355807 234 E 234
Cdd:cd01670  79 E 79
Death pfam00531
Death domain;
160-237 2.07e-12

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 61.23  E-value: 2.07e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355807   160 EELGRYWRRLGRSAGIGEGQMDTIEERYPhDLKSQILRLLQLIEEDdcHDPKHFLLRLCRALGDCGRNDLRKRVEQIM 237
Cdd:pfam00531  12 PPLGKDWRELARKLGLSENEIDEIESENP-RLRSQTYELLRLWEQR--EGKNATVGTLLEALRKLGRRDAAEKIQSIL 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 162-229 3.07e-03

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 35.85  E-value: 3.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355807    162 LGRYWRRLGRSAGIGEGQMDTIEERYPHDLKSQILRLLQLIEEDdcHDPKHFLLRLCRALGDCGRNDL 229
Cdd:smart00005  16 LGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQR--EGKNATLGTLLEALRKMGRDDA 81
DED_FADD cd08336
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ...
 22-71 5.05e-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: 34.85  E-value: 5.05e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21355807  22 ENVEQLKLIFVEEIGSRRRSDcIRTIEDLIDCLERADELSEYNVEPLRRI 71
Cdd:cd08336  17 EELESLKFLCKDHIGKRKLEE-VQSGLDLFEALEERDKLSPENTAFLREL 65
DED pfam01335
Death effector domain;
12-71 7.00e-03

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 34.76  E-value: 7.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355807    12 LKQIAIDGCTENVEQLKLIFVEEIGSRRRSDcIRTIEDLIDCLERADELSEYNVEPLRRI 71
Cdd:pfam01335   5 LLEISEELTEEELESLKFLCKDHIPKRKLEK-IKSALDLFIELEKQGLLSEDNLDLLEEL 63
 
Name Accession Description Interval E-value
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 154-234 1.82e-17

Death Domain: a protein-protein interaction domain; Death Domains (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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they 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. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 74.24  E-value: 1.82e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355807 154 VFKKISEELGRYWRRLGRSAGIGEGQMDTIEERYPHDLKSQILRLLQLIEEDDCHDpkHFLLRLCRALGDCGRNDLRKRV 233
Cdd:cd01670   1 YFDLVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDE--ATLGRLIQALREIGRRDLAEKL 78


                .
gi 21355807 234 E 234
Cdd:cd01670  79 E 79
Death pfam00531
Death domain;
160-237 2.07e-12

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 61.23  E-value: 2.07e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355807   160 EELGRYWRRLGRSAGIGEGQMDTIEERYPhDLKSQILRLLQLIEEDdcHDPKHFLLRLCRALGDCGRNDLRKRVEQIM 237
Cdd:pfam00531  12 PPLGKDWRELARKLGLSENEIDEIESENP-RLRSQTYELLRLWEQR--EGKNATVGTLLEALRKLGRRDAAEKIQSIL 86
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 154-236 1.37e-10

Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in FAS-associated via death domain (FADD). 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, FAS, and its DED recruits the initiator caspases, caspase-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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260020  Cd Length: 85  Bit Score: 56.15  E-value: 1.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355807 154 VFKKISEELGRYWRRLGRSAGIGEGQMDTIEERYPHDLKSQILRLLQL---IEEDDCHDPKhfllrLCRALGDCGRNDLR 230
Cdd:cd08306   4 AFDVICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREwkkIKKAEATVAD-----LIKALRDCQLNLVA 78


                ....*.
gi 21355807 231 KRVEQI 236
Cdd:cd08306  79 DLVEKK 84
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 158-229 2.19e-03

Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. In general, 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 CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260049  Cd Length: 86  Bit Score: 36.14  E-value: 2.19e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21355807 158 ISEELGRYWRRLGRSAGIGEGQMDTIEERYPHDLKSQILRLL-----QLIEEDDChdpkhfLLRLCRALGDCGRNDL 229
Cdd:cd08779   8 LAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLfswakTLPTSPDK------VGLLVTALSKSGRSDL 78
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 162-229 3.07e-03

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 35.85  E-value: 3.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355807    162 LGRYWRRLGRSAGIGEGQMDTIEERYPHDLKSQILRLLQLIEEDdcHDPKHFLLRLCRALGDCGRNDL 229
Cdd:smart00005  16 LGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQR--EGKNATLGTLLEALRKMGRDDA 81
DED_FADD cd08336
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ...
 22-71 5.05e-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: 34.85  E-value: 5.05e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21355807  22 ENVEQLKLIFVEEIGSRRRSDcIRTIEDLIDCLERADELSEYNVEPLRRI 71
Cdd:cd08336  17 EELESLKFLCKDHIGKRKLEE-VQSGLDLFEALEERDKLSPENTAFLREL 65
DED_Caspase_8_10_r2 cd08334
Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) ...
 12-87 5.58e-03

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: 34.87  E-value: 5.58e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21355807  12 LKQIAIDGCTENVEQLKLIFVEEIgSRRRSDCIRTIEDLIDCLERADELSEYNVEPLRRISGNM-PQLIEALSAYTK 87
Cdd:cd08334   8 LYEISEDLTSEDLKSLKFLLSSKL-PRRKLEKNKSALDVFVEMEKRGLLSEDNLDELKKILKSLrPDLAKKINQYKE 83
DED pfam01335
Death effector domain;
12-71 7.00e-03

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 34.76  E-value: 7.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355807    12 LKQIAIDGCTENVEQLKLIFVEEIGSRRRSDcIRTIEDLIDCLERADELSEYNVEPLRRI 71
Cdd:pfam01335   5 LLEISEELTEEELESLKFLCKDHIPKRKLEK-IKSALDLFIELEKQGLLSEDNLDLLEEL 63
 
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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