beta-trefoil domain found in interleukin-33 (IL-33) and similar proteins; IL-33, also called ...
145-292
3.16e-87
beta-trefoil domain found in interleukin-33 (IL-33) and similar proteins; IL-33, also called interleukin-1 family member 11, or IL-1F11, or nuclear factor from high endothelial venules (NF-HEV), acts as cytokine that binds to and signals through the IL1RL1/ST2 receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells. It is involved in the maturation of Th2 cells inducing the secretion of T-helper type 2-associated cytokines. It is also involved in activation of mast cells, basophils, eosinophils, and natural killer cells. It acts as a chemoattractant for Th2 cells, and may function as an 'alarmin', that amplifies immune responses during tissue injury. IL-33 contains a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.
Pssm-ID: 466781 Cd Length: 153 Bit Score: 257.39 E-value: 3.16e-87
beta-trefoil domain found in interleukin-33 (IL-33) and similar proteins; IL-33, also called ...
145-292
3.16e-87
beta-trefoil domain found in interleukin-33 (IL-33) and similar proteins; IL-33, also called interleukin-1 family member 11, or IL-1F11, or nuclear factor from high endothelial venules (NF-HEV), acts as cytokine that binds to and signals through the IL1RL1/ST2 receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells. It is involved in the maturation of Th2 cells inducing the secretion of T-helper type 2-associated cytokines. It is also involved in activation of mast cells, basophils, eosinophils, and natural killer cells. It acts as a chemoattractant for Th2 cells, and may function as an 'alarmin', that amplifies immune responses during tissue injury. IL-33 contains a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.
Pssm-ID: 466781 Cd Length: 153 Bit Score: 257.39 E-value: 3.16e-87
beta-trefoil domain found in the interleukin-1 (IL-1) family of cytokines; The IL-1 family of ...
150-291
1.49e-07
beta-trefoil domain found in the interleukin-1 (IL-1) family of cytokines; The IL-1 family of cytokines comprises 11 members, including 7 pro-inflammatory agonists (IL-1alpha, IL-1beta, IL-18, IL-33, IL-36alpha, IL-36beta, IL-36gamma) and 4 defined or putative antagonists (IL-1R antagonist (IL-1Ra), IL-36Ra, IL-37, and IL-38) exerting anti-inflammatory activities. These members can have complimentary or distinct biological functions. All family members share a common structure at the C-terminus, which is comprised by of a typical beta-trefoil fold consisting of 12-beta-strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.
Pssm-ID: 466776 Cd Length: 145 Bit Score: 49.63 E-value: 1.49e-07
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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