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Conserved domains on  [gi|1696176449|ref|XP_029623367|]
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tumor necrosis factor receptor type 1-associated DEATH domain protein-like [Salmo trutta]

Protein Classification

protein kinase family protein( domain architecture ID 10557181)

protein kinase family protein, 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
TRADD_N pfam09034
TRADD, N-terminal domain; The N terminal domain of 'Tumour necrosis factor receptor type 1 ...
 58-169 2.90e-61

TRADD, N-terminal domain; The N terminal domain of 'Tumour necrosis factor receptor type 1 associated death domain protein' (TRADD) folds into an alpha-beta sandwich with a four-stranded beta sheet and six alpha helices, each forming one layer of the structure. The domain allows docking of TRADD onto 'tumour necrosis factor receptor-associated factor' (TRAF): the binding is at the beta-sandwich domain, away from the coiled-coil domain. Binding ensures the recruitment of cIAPs to the signaling complex, which may be important for direct caspase-8 inhibition and the immediate suppression of apoptosis at the apical point of the cascade.


:

Pssm-ID: 430379  Cd Length: 112  Bit Score: 189.83  E-value: 2.90e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696176449  58 DSAGGLEGYEILKLHDADPLLGVEVKFVDVAACRRFLQSYGSGAVQQSLSQHACRLLHCPQELVLETQLKAGTHTLDFCL 137
Cdd:pfam09034   1 DSAGGLDGYEILKIHDSDPQLIVQLKFCGVEACRRFLQSYREGALRQSLQQHLCRLLALPQELPLETELKAGTERLDSCL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1696176449 138 DDLELCLQHIHQSQPGRLRDDEIAELDQQLQS 169
Cdd:pfam09034  81 DDEERCLQHIHQSKPDRLRDEEITELEQQLQS 112
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 209-295 1.60e-41

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 cd08780:

Pssm-ID: 472698  Cd Length: 90  Bit Score: 138.87  E-value: 1.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696176449 209 DLQRFSNGVGRDWRKVGRALGKNCRALKGPAIDNLAYEYEREGLYEQAYQLLSRFIQAEGSAARLGRLVRALEDSKLTSL 288
Cdd:cd08780     4 DQQHFAKSVGKKWKPVGRSLQKNCRALRDPAIDNLAYEYDREGLYEQAYQLLRRFIQSEGKKATLQRLVQALEENGLTSL 83


                  ....*..
gi 1696176449 289 AENILDI 295
Cdd:cd08780    84 AEDLLGL 90
 
Name Accession Description Interval E-value
TRADD_N pfam09034
TRADD, N-terminal domain; The N terminal domain of 'Tumour necrosis factor receptor type 1 ...
 58-169 2.90e-61

TRADD, N-terminal domain; The N terminal domain of 'Tumour necrosis factor receptor type 1 associated death domain protein' (TRADD) folds into an alpha-beta sandwich with a four-stranded beta sheet and six alpha helices, each forming one layer of the structure. The domain allows docking of TRADD onto 'tumour necrosis factor receptor-associated factor' (TRAF): the binding is at the beta-sandwich domain, away from the coiled-coil domain. Binding ensures the recruitment of cIAPs to the signaling complex, which may be important for direct caspase-8 inhibition and the immediate suppression of apoptosis at the apical point of the cascade.


Pssm-ID: 430379  Cd Length: 112  Bit Score: 189.83  E-value: 2.90e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696176449  58 DSAGGLEGYEILKLHDADPLLGVEVKFVDVAACRRFLQSYGSGAVQQSLSQHACRLLHCPQELVLETQLKAGTHTLDFCL 137
Cdd:pfam09034   1 DSAGGLDGYEILKIHDSDPQLIVQLKFCGVEACRRFLQSYREGALRQSLQQHLCRLLALPQELPLETELKAGTERLDSCL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1696176449 138 DDLELCLQHIHQSQPGRLRDDEIAELDQQLQS 169
Cdd:pfam09034  81 DDEERCLQHIHQSKPDRLRDEEITELEQQLQS 112
Death_TRADD cd08780
Death Domain of Tumor Necrosis Factor Receptor 1-Associated Death Domain protein; Death domain ...
 209-295 1.60e-41

Death Domain of Tumor Necrosis Factor Receptor 1-Associated Death Domain protein; Death domain (DD) of TRADD (TNF Receptor 1-Associated Death Domain or TNFRSF1A-associated via death domain) protein. TRADD is a central signaling adaptor for TNF-receptor 1 (TNFR1), mediating activation of Nuclear Factor -kappaB (NF-kB) and c-Jun N-terminal kinase (JNK), as well as caspase-dependent apoptosis. It also carries important immunological roles including germinal center formation, DR3-mediated T-cell stimulation, and TNFalpha-mediated inflammatory responses. 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 (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260050  Cd Length: 90  Bit Score: 138.87  E-value: 1.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696176449 209 DLQRFSNGVGRDWRKVGRALGKNCRALKGPAIDNLAYEYEREGLYEQAYQLLSRFIQAEGSAARLGRLVRALEDSKLTSL 288
Cdd:cd08780     4 DQQHFAKSVGKKWKPVGRSLQKNCRALRDPAIDNLAYEYDREGLYEQAYQLLRRFIQSEGKKATLQRLVQALEENGLTSL 83


                  ....*..
gi 1696176449 289 AENILDI 295
Cdd:cd08780    84 AEDLLGL 90
Death pfam00531
Death domain;
215-295 2.30e-09

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 53.52  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696176449 215 NGVGRDWRKVGRALGkncraLKGPAIDNLAYEYERegLYEQAYQLLSRFIQAEGSAARLGRLVRALEDSKLTSLAENILD 294
Cdd:pfam00531  12 PPLGKDWRELARKLG-----LSENEIDEIESENPR--LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAAEKIQS 84


                  .
gi 1696176449 295 I 295
Cdd:pfam00531  85 I 85
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 209-294 1.00e-08

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: 51.64  E-value: 1.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696176449  209 DLQRFSNGV-GRDWRKVGRALGKNCRALKGPAIDNLayeyerEGLYEQAYQLLSRFIQAEGSAARLGRLVRALEDSKLTS 287
Cdd:smart00005   7 KLAKLLDHPlGLDWRELARKLGLSEADIDQIRTEAP------RDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                   ....*..
gi 1696176449  288 LAENILD 294
Cdd:smart00005  81 AVELLRS 87
 
Name Accession Description Interval E-value
TRADD_N pfam09034
TRADD, N-terminal domain; The N terminal domain of 'Tumour necrosis factor receptor type 1 ...
 58-169 2.90e-61

TRADD, N-terminal domain; The N terminal domain of 'Tumour necrosis factor receptor type 1 associated death domain protein' (TRADD) folds into an alpha-beta sandwich with a four-stranded beta sheet and six alpha helices, each forming one layer of the structure. The domain allows docking of TRADD onto 'tumour necrosis factor receptor-associated factor' (TRAF): the binding is at the beta-sandwich domain, away from the coiled-coil domain. Binding ensures the recruitment of cIAPs to the signaling complex, which may be important for direct caspase-8 inhibition and the immediate suppression of apoptosis at the apical point of the cascade.


Pssm-ID: 430379  Cd Length: 112  Bit Score: 189.83  E-value: 2.90e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696176449  58 DSAGGLEGYEILKLHDADPLLGVEVKFVDVAACRRFLQSYGSGAVQQSLSQHACRLLHCPQELVLETQLKAGTHTLDFCL 137
Cdd:pfam09034   1 DSAGGLDGYEILKIHDSDPQLIVQLKFCGVEACRRFLQSYREGALRQSLQQHLCRLLALPQELPLETELKAGTERLDSCL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1696176449 138 DDLELCLQHIHQSQPGRLRDDEIAELDQQLQS 169
Cdd:pfam09034  81 DDEERCLQHIHQSKPDRLRDEEITELEQQLQS 112
Death_TRADD cd08780
Death Domain of Tumor Necrosis Factor Receptor 1-Associated Death Domain protein; Death domain ...
 209-295 1.60e-41

Death Domain of Tumor Necrosis Factor Receptor 1-Associated Death Domain protein; Death domain (DD) of TRADD (TNF Receptor 1-Associated Death Domain or TNFRSF1A-associated via death domain) protein. TRADD is a central signaling adaptor for TNF-receptor 1 (TNFR1), mediating activation of Nuclear Factor -kappaB (NF-kB) and c-Jun N-terminal kinase (JNK), as well as caspase-dependent apoptosis. It also carries important immunological roles including germinal center formation, DR3-mediated T-cell stimulation, and TNFalpha-mediated inflammatory responses. 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 (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260050  Cd Length: 90  Bit Score: 138.87  E-value: 1.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696176449 209 DLQRFSNGVGRDWRKVGRALGKNCRALKGPAIDNLAYEYEREGLYEQAYQLLSRFIQAEGSAARLGRLVRALEDSKLTSL 288
Cdd:cd08780     4 DQQHFAKSVGKKWKPVGRSLQKNCRALRDPAIDNLAYEYDREGLYEQAYQLLRRFIQSEGKKATLQRLVQALEENGLTSL 83


                  ....*..
gi 1696176449 289 AENILDI 295
Cdd:cd08780    84 AEDLLGL 90
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 209-292 5.15e-15

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: 68.85  E-value: 5.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696176449 209 DLQRFSNGVGRDWRKVGRALGkncraLKGPAIDNLAYEYeREGLYEQAYQLLSRFIQAEGSAARLGRLVRALEDSKLTSL 288
Cdd:cd01670     1 YFDLVAEELGRDWKKLARKLG-----LSEGDIDQIEEDN-RDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDL 74


                  ....
gi 1696176449 289 AENI 292
Cdd:cd01670    75 AEKL 78
Death pfam00531
Death domain;
215-295 2.30e-09

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 53.52  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696176449 215 NGVGRDWRKVGRALGkncraLKGPAIDNLAYEYERegLYEQAYQLLSRFIQAEGSAARLGRLVRALEDSKLTSLAENILD 294
Cdd:pfam00531  12 PPLGKDWRELARKLG-----LSENEIDEIESENPR--LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAAEKIQS 84


                  .
gi 1696176449 295 I 295
Cdd:pfam00531  85 I 85
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
 210-281 5.68e-09

Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal DD, which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. 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 (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260048  Cd Length: 86  Bit Score: 52.43  E-value: 5.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1696176449 210 LQRFSNGVGRDWRKVGRALGkncraLKGPAIDNLAYEYEREGLYEQAYQLLSRFIQAEGS-AARLGRLVRALE 281
Cdd:cd08777     5 LDLLRENLGKKWKRCARRLG-----LTEVEIEEIDHDYERDGLKEKVHQMLEKWKMKEGSkGATVGKLAKALE 72
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 209-294 1.00e-08

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: 51.64  E-value: 1.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696176449  209 DLQRFSNGV-GRDWRKVGRALGKNCRALKGPAIDNLayeyerEGLYEQAYQLLSRFIQAEGSAARLGRLVRALEDSKLTS 287
Cdd:smart00005   7 KLAKLLDHPlGLDWRELARKLGLSEADIDQIRTEAP------RDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                   ....*..
gi 1696176449  288 LAENILD 294
Cdd:smart00005  81 AVELLRS 87
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 214-285 3.16e-06

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: 44.59  E-value: 3.16e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1696176449 214 SNGVGRDWRKVGRALGkncraLKGPAIDNLAYEYEREgLYEQAYQLLSRFIQAEGSAARLGRLVRALEDSKL 285
Cdd:cd08306     9 CENLGRDWRQLARKLG-----LSETKIESISEAHPRN-LREQVRQSLREWKKIKKAEATVADLIKALRDCQL 74
Death_TRAILR_DR4_DR5 cd08315
Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death ...
 219-295 1.37e-04

Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death Domain (DD) found in Tumor necrosis factor-Related Apoptosis-Inducing Ligand (TRAIL) Receptors. In mammals, this family includes TRAILR1 (also called DR4 or TNFRSF10A) and TRAILR2 (also called DR5, TNFRSF10B, or KILLER). They function as receptors for the cytokine TRAIL and are involved in apoptosis signaling pathways. TRAIL preferentially induces apoptosis in cancer cells while exhibiting little toxicity in normal cells. 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 can recruit other proteins into signaling complexes.


Pssm-ID: 260027  Cd Length: 88  Bit Score: 39.95  E-value: 1.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1696176449 219 RDWRKVGRALGkncraLKGPAIDnLAyEYEREGLYEQAYQLLSRFIQAEGSAARLGRLVRALEDSKLTSLAENILDI 295
Cdd:cd08315    12 KSWKRLMRALG-----LSDNEIK-LA-EANDPGSQEPLYQMLNKWLNKTGRKASVNTLLDALEDLGLRGAAETIADK 81
Death_FAS_TNFRSF6 cd08316
Death domain of FAS or TNF receptor superfamily member 6; Death Domain (DD) found in the ...
 254-295 3.89e-03

Death domain of FAS or TNF receptor superfamily member 6; Death Domain (DD) found in the FS7-associated cell surface antigen (FAS). FAS, also known as TNFRSF6 (TNF receptor superfamily member 6), APT1, CD95, FAS1, or APO-1, together with FADD (Fas-associating via Death Domain) and caspase 8, is an integral part of the death inducing signalling complex (DISC), which plays an important role in the induction of apoptosis and is activated by binding of the ligand FasL to FAS. FAS also plays a critical role in self-tolerance by eliminating cell types (autoreactive T and B cells) that contribute to autoimmunity. 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 can recruit other proteins into signaling complexes.


Pssm-ID: 260028  Cd Length: 94  Bit Score: 36.12  E-value: 3.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1696176449 254 EQAYQLLSRFIQAEGSAARLGRLVRALEDSKLTSLAENILDI 295
Cdd:cd08316    47 EQKVQLLRAWYQKHGKKGAYRTLIKTLRKAGKRAKADKIQDI 88
 
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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