Recombination activating protein 2; V-D-J recombination is the combinatorial process by which ...
51-390
0e+00
Recombination activating protein 2; V-D-J recombination is the combinatorial process by which the huge range of immunoglobulin and T cell binding specificity is generated from a limited amount of genetic material. This process is synergistically activated by RAG1 and RAG2 in developing lymphocytes. Defects in RAG2 in humans are a cause of severe combined immunodeficiency B cell negative and Omenn syndrome.
The actual alignment was detected with superfamily member pfam03089:
Pssm-ID: 427128 Cd Length: 339 Bit Score: 655.65 E-value: 0e+00
RAG2 PHD domain; This domain is found at the C-terminus of the RAG2 protein. The structure of ...
417-495
6.36e-45
RAG2 PHD domain; This domain is found at the C-terminus of the RAG2 protein. The structure of this domain has been shown bound to histone H3 trimethylated at lysine 4 (H3K4me3).
:
Pssm-ID: 404256 Cd Length: 78 Bit Score: 152.63 E-value: 6.36e-45
Recombination activating protein 2; V-D-J recombination is the combinatorial process by which ...
51-390
0e+00
Recombination activating protein 2; V-D-J recombination is the combinatorial process by which the huge range of immunoglobulin and T cell binding specificity is generated from a limited amount of genetic material. This process is synergistically activated by RAG1 and RAG2 in developing lymphocytes. Defects in RAG2 in humans are a cause of severe combined immunodeficiency B cell negative and Omenn syndrome.
Pssm-ID: 427128 Cd Length: 339 Bit Score: 655.65 E-value: 0e+00
RAG2 PHD domain; This domain is found at the C-terminus of the RAG2 protein. The structure of ...
417-495
6.36e-45
RAG2 PHD domain; This domain is found at the C-terminus of the RAG2 protein. The structure of this domain has been shown bound to histone H3 trimethylated at lysine 4 (H3K4me3).
Pssm-ID: 404256 Cd Length: 78 Bit Score: 152.63 E-value: 6.36e-45
PHD finger found in V(D)J recombination-activating protein 2 (RAG-2) and similar proteins; ...
418-485
1.28e-38
PHD finger found in V(D)J recombination-activating protein 2 (RAG-2) and similar proteins; RAG-2 is an essential component of the lymphoid-specific recombination activating gene RAG1/2 V(D)J recombinase mediating antigen-receptor gene assembly. It contains an acidic hinge region implicated in histone-binding, a non-canonical plant homeodomain (PHD) finger followed by a C-terminal extension of 40 amino acids that is essential for phosphoinositide (PtdIns)-binding. The PHD finger is a chromatin-binding module that specifically recognizes histone H3 trimethylated at lysine 4 (H3K4me3) and influences V(D)J recombination.
Pssm-ID: 277044 Cd Length: 67 Bit Score: 135.43 E-value: 1.28e-38
Recombination activating protein 2; V-D-J recombination is the combinatorial process by which ...
51-390
0e+00
Recombination activating protein 2; V-D-J recombination is the combinatorial process by which the huge range of immunoglobulin and T cell binding specificity is generated from a limited amount of genetic material. This process is synergistically activated by RAG1 and RAG2 in developing lymphocytes. Defects in RAG2 in humans are a cause of severe combined immunodeficiency B cell negative and Omenn syndrome.
Pssm-ID: 427128 Cd Length: 339 Bit Score: 655.65 E-value: 0e+00
RAG2 PHD domain; This domain is found at the C-terminus of the RAG2 protein. The structure of ...
417-495
6.36e-45
RAG2 PHD domain; This domain is found at the C-terminus of the RAG2 protein. The structure of this domain has been shown bound to histone H3 trimethylated at lysine 4 (H3K4me3).
Pssm-ID: 404256 Cd Length: 78 Bit Score: 152.63 E-value: 6.36e-45
PHD finger found in V(D)J recombination-activating protein 2 (RAG-2) and similar proteins; ...
418-485
1.28e-38
PHD finger found in V(D)J recombination-activating protein 2 (RAG-2) and similar proteins; RAG-2 is an essential component of the lymphoid-specific recombination activating gene RAG1/2 V(D)J recombinase mediating antigen-receptor gene assembly. It contains an acidic hinge region implicated in histone-binding, a non-canonical plant homeodomain (PHD) finger followed by a C-terminal extension of 40 amino acids that is essential for phosphoinositide (PtdIns)-binding. The PHD finger is a chromatin-binding module that specifically recognizes histone H3 trimethylated at lysine 4 (H3K4me3) and influences V(D)J recombination.
Pssm-ID: 277044 Cd Length: 67 Bit Score: 135.43 E-value: 1.28e-38
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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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
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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Domains are color coded according to superfamilies
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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
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
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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