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Conserved domains on  [gi|1720410484|ref|XP_030109802|]
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tumor necrosis factor receptor superfamily member 25 isoform X4 [Mus musculus]

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) ...
 157-233 1.61e-43

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 cd08815:

Pssm-ID: 472698  Cd Length: 77  Bit Score: 141.69  E-value: 1.61e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720410484 157 QLYDVMDAVPARRWKEFVRTLGLREAEIEAVEVEICRFRDQQYEMLKRWRQQQPAGLGAIYAALERMGLEGCAEDLR 233
Cdd:cd08815     1 QLYAVMDAVPARRWKEFVRTLGLREAEIEAVELEIGRFRDQQYEMLKRWRQQQPAGLDAVYAALERMGLAGCAEDLR 77
 
Name Accession Description Interval E-value
Death_TNFRSF25_DR3 cd08815
Death domain of Tumor Necrosis Factor Receptor superfamily 25; Death Domain (DD) found in ...
 157-233 1.61e-43

Death domain of Tumor Necrosis Factor Receptor superfamily 25; Death Domain (DD) found in Tumor Necrosis Factor (TNF) receptor superfamily 25 (TNFRSF25), also known as TRAMP (TNF receptor-related apoptosis-mediating protein), LARD, APO-3, WSL-1, or DR3 (Death Receptor-3). TNFRSF25 is primarily expressed in T cells, is activated by binding to its ligand TL1A, and plays an important role in T-cell function. 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: 176793  Cd Length: 77  Bit Score: 141.69  E-value: 1.61e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720410484 157 QLYDVMDAVPARRWKEFVRTLGLREAEIEAVEVEICRFRDQQYEMLKRWRQQQPAGLGAIYAALERMGLEGCAEDLR 233
Cdd:cd08815     1 QLYAVMDAVPARRWKEFVRTLGLREAEIEAVELEIGRFRDQQYEMLKRWRQQQPAGLDAVYAALERMGLAGCAEDLR 77
Death pfam00531
Death domain;
157-236 1.37e-13

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 64.31  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410484 157 QLYDVMDAVPA--RRWKEFVRTLGLREAEIEAVEVEICRFRDQQYEMLKRWRQQQP--AGLGAIYAALERMGLEGCAEDL 232
Cdd:pfam00531   3 QLDRLLDPPPPlgKDWRELARKLGLSENEIDEIESENPRLRSQTYELLRLWEQREGknATVGTLLEALRKLGRRDAAEKI 82


                  ....
gi 1720410484 233 RSRL 236
Cdd:pfam00531  83 QSIL 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 152-235 1.04e-12

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: 62.04  E-value: 1.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410484  152 LQPGPQLYDVMDAVPARRWKEFVRTLGLREAEIEAVEVEICR-FRDQQYEMLKRWRQQQP--AGLGAIYAALERMGLEGC 228
Cdd:smart00005   2 ELTRQKLAKLLDHPLGLDWRELARKLGLSEADIDQIRTEAPRdLAEQSVQLLRLWEQREGknATLGTLLEALRKMGRDDA 81


                   ....*..
gi 1720410484  229 AEDLRSR 235
Cdd:smart00005  82 VELLRSE 88
 
Name Accession Description Interval E-value
Death_TNFRSF25_DR3 cd08815
Death domain of Tumor Necrosis Factor Receptor superfamily 25; Death Domain (DD) found in ...
 157-233 1.61e-43

Death domain of Tumor Necrosis Factor Receptor superfamily 25; Death Domain (DD) found in Tumor Necrosis Factor (TNF) receptor superfamily 25 (TNFRSF25), also known as TRAMP (TNF receptor-related apoptosis-mediating protein), LARD, APO-3, WSL-1, or DR3 (Death Receptor-3). TNFRSF25 is primarily expressed in T cells, is activated by binding to its ligand TL1A, and plays an important role in T-cell function. 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: 176793  Cd Length: 77  Bit Score: 141.69  E-value: 1.61e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720410484 157 QLYDVMDAVPARRWKEFVRTLGLREAEIEAVEVEICRFRDQQYEMLKRWRQQQPAGLGAIYAALERMGLEGCAEDLR 233
Cdd:cd08815     1 QLYAVMDAVPARRWKEFVRTLGLREAEIEAVELEIGRFRDQQYEMLKRWRQQQPAGLDAVYAALERMGLAGCAEDLR 77
Death_TNFR1 cd08313
Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis ...
 157-233 8.74e-30

Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis factor receptor-1 (TNFR-1). TNFR-1 has many names including TNFRSF1A, CD120a, p55, p60, and TNFR60. It activates two major intracellular signaling pathways that lead to the activation of the transcription factor NF-kB and the induction of cell death. Upon binding of its ligand TNF, TNFR-1 trimerizes which leads to the recruitment of an adaptor protein named TNFR-associated death domain protein (TRADD) through a DD/DD interaction. Mutations in the TNFRSF1A gene causes TNFR-associated periodic syndrome (TRAPS), a rare disorder characterized recurrent fever, myalgia, abdominal pain, conjunctivitis and skin eruptions. 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: 176729  Cd Length: 80  Bit Score: 106.32  E-value: 8.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410484 157 QLYDVMDAVPARRWKEFVRTLGLREAEIEAVEVEICRFRDQQYEMLKRWRQQQP---AGLGAIYAALERMGLEGCAEDLR 233
Cdd:cd08313     1 LLYTVLDEVPPRRWKEFVRRLGLSDNEIERVELDHRRCRDAQYQMLKVWKERGPrpyATLQHLLSVLRDMELVGCAEDIE 80
Death pfam00531
Death domain;
157-236 1.37e-13

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 64.31  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410484 157 QLYDVMDAVPA--RRWKEFVRTLGLREAEIEAVEVEICRFRDQQYEMLKRWRQQQP--AGLGAIYAALERMGLEGCAEDL 232
Cdd:pfam00531   3 QLDRLLDPPPPlgKDWRELARKLGLSENEIDEIESENPRLRSQTYELLRLWEQREGknATVGTLLEALRKLGRRDAAEKI 82


                  ....
gi 1720410484 233 RSRL 236
Cdd:pfam00531  83 QSIL 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 152-235 1.04e-12

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: 62.04  E-value: 1.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410484  152 LQPGPQLYDVMDAVPARRWKEFVRTLGLREAEIEAVEVEICR-FRDQQYEMLKRWRQQQP--AGLGAIYAALERMGLEGC 228
Cdd:smart00005   2 ELTRQKLAKLLDHPLGLDWRELARKLGLSEADIDQIRTEAPRdLAEQSVQLLRLWEQREGknATLGTLLEALRKMGRDDA 81


                   ....*..
gi 1720410484  229 AEDLRSR 235
Cdd:smart00005  82 VELLRSE 88
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
 158-233 2.68e-09

Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death receptors are members of the tumor necrosis factor (TNF) receptor superfamily, characterized by having a cytoplasmic DD. Known members of the family are Fas (CD95/APO-1), TNF-receptor 1 (TNFR1/TNFRSF1A/p55/CD120a), TNF-related apoptosis-inducing ligand receptor 1 (TRAIL-R1 /DR4), and receptor 2 (TRAIL-R2/DR5/APO-2/KILLER), as well as Death Receptor 3 (DR3/APO-3/TRAMP/WSL-1/LARD). They are involved in apoptosis signaling pathways. 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: 260054  Cd Length: 80  Bit Score: 52.58  E-value: 2.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720410484 158 LYDVMDAVPARRWKEFVRTLGLREAEIEAVEVEICR-FRDQQYEMLKRWRQQQP--AGLGAIYAALERMGLEGCAEDLR 233
Cdd:cd08784     2 ITTIAGVVPLSQWKGFVRKLGLNEAEIDEIKNDNVQdTAEAKYQMLRNWHQLTGrkAAYDTLIKDLKKMNLCTLAEKIQ 80
Death_TRAILR_DR4_DR5 cd08315
Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death ...
 163-236 3.40e-07

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: 46.88  E-value: 3.40e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720410484 163 DAVPARRWKEFVRTLGLREAEIEAVEVEICRFRDQQYEMLKRWRQQQpaGLGA----IYAALERMGLEGCAEDLRSRL 236
Cdd:cd08315     7 DIVPFKSWKRLMRALGLSDNEIKLAEANDPGSQEPLYQMLNKWLNKT--GRKAsvntLLDALEDLGLRGAAETIADKL 82
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 157-233 8.65e-06

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: 42.65  E-value: 8.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410484 157 QLYDVMDAVpARRWKEFVRTLGL------------REAEieaveveicrfRDQQYEMLKRWRQQQP--AGLGAIYAALER 222
Cdd:cd01670     1 YFDLVAEEL-GRDWKKLARKLGLsegdidqieednRDDL-----------KEQAYQMLERWREREGdeATLGRLIQALRE 68

                          90
                  ....*....|.
gi 1720410484 223 MGLEGCAEDLR 233
Cdd:cd01670    69 IGRRDLAEKLE 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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