FANCI family protein similar to FANCI domain region of Homo sapiens fanconi anemia group I protein (FANCI), which plays an essential role in the repair of DNA double-strand breaks by homologous recombination and in the repair of interstrand DNA cross-links (ICLs) by promoting FANCD2 monoubiquitination by FANCL and participating in recruitment to DNA repair sites; FANCI/FANCD2 family protein similar to Homo sapiens fanconi anemia group I protein (FANCI) and fanconi anemia group D2 protein (FANCD2)
Fanconi anemia I protein; The Fanconi anemia ID complex consists of two subunits, Fanconi ...
43-1290
0e+00
Fanconi anemia I protein; The Fanconi anemia ID complex consists of two subunits, Fanconi anemia I and Fanconi anemia D2 (FANCI-FANCD2) and plays a central role in the repair of DNA interstrand cross-links (ICLs). The complex is activated via DNA damage-induced phosphorylation by ATR (ataxia telangiectasia and Rad3-related) and monoubiquitination by the FA core complex ubiquitin ligase, and it binds to DNA at the ICL site, recognizing branched DNA structures. Defects in the complex cause Fanconi anemia, a cancer predisposition syndrome. The phosphorylation of FANCI may function as a molecular switch to turn on the FA pathway.
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Pssm-ID: 212594 [Multi-domain] Cd Length: 1202 Bit Score: 1308.07 E-value: 0e+00
Fanconi anemia I protein; The Fanconi anemia ID complex consists of two subunits, Fanconi ...
43-1290
0e+00
Fanconi anemia I protein; The Fanconi anemia ID complex consists of two subunits, Fanconi anemia I and Fanconi anemia D2 (FANCI-FANCD2) and plays a central role in the repair of DNA interstrand cross-links (ICLs). The complex is activated via DNA damage-induced phosphorylation by ATR (ataxia telangiectasia and Rad3-related) and monoubiquitination by the FA core complex ubiquitin ligase, and it binds to DNA at the ICL site, recognizing branched DNA structures. Defects in the complex cause Fanconi anemia, a cancer predisposition syndrome. The phosphorylation of FANCI may function as a molecular switch to turn on the FA pathway.
Pssm-ID: 212594 [Multi-domain] Cd Length: 1202 Bit Score: 1308.07 E-value: 0e+00
Fanconi anemia I protein; The Fanconi anemia ID complex consists of two subunits, Fanconi ...
43-1290
0e+00
Fanconi anemia I protein; The Fanconi anemia ID complex consists of two subunits, Fanconi anemia I and Fanconi anemia D2 (FANCI-FANCD2) and plays a central role in the repair of DNA interstrand cross-links (ICLs). The complex is activated via DNA damage-induced phosphorylation by ATR (ataxia telangiectasia and Rad3-related) and monoubiquitination by the FA core complex ubiquitin ligase, and it binds to DNA at the ICL site, recognizing branched DNA structures. Defects in the complex cause Fanconi anemia, a cancer predisposition syndrome. The phosphorylation of FANCI may function as a molecular switch to turn on the FA pathway.
Pssm-ID: 212594 [Multi-domain] Cd Length: 1202 Bit Score: 1308.07 E-value: 0e+00
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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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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Others (non-specific hits) and
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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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