CFAP61 family protein is a DUF4821 domain-containing protein; similar to Tetrahymena thermophila cilia- and flagella-associated protein 61 (CFAP61) that acts as a component of a spoke-associated complex that regulates ciliary mobility by mediating a stable and functional assembly of the radial spoke 3 (RS3)
Cilia- and flagella-associated protein 61, N-terminal domain; This entry represents the ...
2-204
3.18e-72
Cilia- and flagella-associated protein 61, N-terminal domain; This entry represents the N-terminal domain of proteins described as cilia- and flagella-associated protein. Proteins containing this domain includes FAP61 from Chlamydomonas reinhardtii. FAP61 is part of the calmodulin and spoke-associated complex (CSC) required for wild-type motility and for the stable assembly of a subset of radial spokes in motile cilia.
:
Pssm-ID: 465016 Cd Length: 264 Bit Score: 241.38 E-value: 3.18e-72
Cilia- and flagella-associated protein 61, N-terminal domain; This entry represents the ...
339-473
9.59e-03
Cilia- and flagella-associated protein 61, N-terminal domain; This entry represents the N-terminal domain of proteins described as cilia- and flagella-associated protein. Proteins containing this domain includes FAP61 from Chlamydomonas reinhardtii. FAP61 is part of the calmodulin and spoke-associated complex (CSC) required for wild-type motility and for the stable assembly of a subset of radial spokes in motile cilia.
The actual alignment was detected with superfamily member pfam16092:
Pssm-ID: 465016 Cd Length: 264 Bit Score: 39.15 E-value: 9.59e-03
Cilia- and flagella-associated protein 61, N-terminal domain; This entry represents the ...
2-204
3.18e-72
Cilia- and flagella-associated protein 61, N-terminal domain; This entry represents the N-terminal domain of proteins described as cilia- and flagella-associated protein. Proteins containing this domain includes FAP61 from Chlamydomonas reinhardtii. FAP61 is part of the calmodulin and spoke-associated complex (CSC) required for wild-type motility and for the stable assembly of a subset of radial spokes in motile cilia.
Pssm-ID: 465016 Cd Length: 264 Bit Score: 241.38 E-value: 3.18e-72
Cilia- and flagella-associated protein 61, N-terminal domain; This entry represents the ...
339-473
9.59e-03
Cilia- and flagella-associated protein 61, N-terminal domain; This entry represents the N-terminal domain of proteins described as cilia- and flagella-associated protein. Proteins containing this domain includes FAP61 from Chlamydomonas reinhardtii. FAP61 is part of the calmodulin and spoke-associated complex (CSC) required for wild-type motility and for the stable assembly of a subset of radial spokes in motile cilia.
Pssm-ID: 465016 Cd Length: 264 Bit Score: 39.15 E-value: 9.59e-03
Cilia- and flagella-associated protein 61, N-terminal domain; This entry represents the ...
2-204
3.18e-72
Cilia- and flagella-associated protein 61, N-terminal domain; This entry represents the N-terminal domain of proteins described as cilia- and flagella-associated protein. Proteins containing this domain includes FAP61 from Chlamydomonas reinhardtii. FAP61 is part of the calmodulin and spoke-associated complex (CSC) required for wild-type motility and for the stable assembly of a subset of radial spokes in motile cilia.
Pssm-ID: 465016 Cd Length: 264 Bit Score: 241.38 E-value: 3.18e-72
Cilia- and flagella-associated protein 61, N-terminal domain; This entry represents the ...
339-473
9.59e-03
Cilia- and flagella-associated protein 61, N-terminal domain; This entry represents the N-terminal domain of proteins described as cilia- and flagella-associated protein. Proteins containing this domain includes FAP61 from Chlamydomonas reinhardtii. FAP61 is part of the calmodulin and spoke-associated complex (CSC) required for wild-type motility and for the stable assembly of a subset of radial spokes in motile cilia.
Pssm-ID: 465016 Cd Length: 264 Bit Score: 39.15 E-value: 9.59e-03
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.
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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,
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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.
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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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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
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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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