Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyTRADD N-terminal domain8023158 4001282 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyTRADD N-terminal domain8035538 3001216 SCOP2 (2022-06-29)
BSCOP2B SuperfamilyTRAF domain-like8040736 3001027 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyTrimerization domain of TRAF8039390 3001589 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ATRADD_Ne1f3vA1 A: a+b two layersX: Alpha-beta plaitsH: TRADD, N-terminal domain/Dystroglycan, domain 2 (From Topology)T: TRADD, N-terminal domain/Dystroglycan, domain 2F: TRADD_NECOD (1.6)
BMATHe1f3vB1 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: TRAF domain-like (From Topology)T: TRAF domain-likeF: MATHECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.30.70.680 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits TRADD, N-terminal domainCATH (4.3.0)
B2.60.210.10 Mainly Beta Sandwich Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2 Chain ACATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF09034TRADD, N-terminal domain (TRADD_N)TRADD, N-terminal domainThe 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 all ...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 [1]. This domain is structurally related to the small-molecule-binding ACT domain (RRM-like fold) [2].
Domain
PF21355TRAF/meprin, MATH domain (TRAF-mep_MATH)TRAF/meprin, MATH domainIntracellular TRAFs and extracellular meprins share a conserved region of about 180 residues, the the meprin and TRAF homology (MATH) domain which adopts a beta-sandwich structure. This is the MATH domain of TNF receptor-associated factors (TRAFs) an ...Intracellular TRAFs and extracellular meprins share a conserved region of about 180 residues, the the meprin and TRAF homology (MATH) domain which adopts a beta-sandwich structure. This is the MATH domain of TNF receptor-associated factors (TRAFs) and meprins. In TRAFS, it is essential for self-association and receptor interaction [1-3]. Meprins are mammalian tissue-specific metalloendopeptidases involved developmental, normal and pathological processes.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
TUMOR NECROSIS FACTOR RECEPTOR TYPE 1 ASSOCIATED DEATH DOMAIN PROTEIN
TUMOR NECROSIS FACTOR RECEPTOR-ASSOCIATED PROTEIN

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosQ15628
PharosQ12933