Radial spokehead-like protein; This family includes the radial spoke head proteins RSP4 and ...
195-630
0e+00
Radial spokehead-like protein; This family includes the radial spoke head proteins RSP4 and RSP6 from Chlamydomonas reinhardtii, and several eukaryotic homologs, including mammalian RSHL1, the protein product of a familial ciliary dyskinesia candidate gene.
:
Pssm-ID: 461405 [Multi-domain] Cd Length: 406 Bit Score: 564.97 E-value: 0e+00
Radial spokehead-like protein; This family includes the radial spoke head proteins RSP4 and ...
195-630
0e+00
Radial spokehead-like protein; This family includes the radial spoke head proteins RSP4 and RSP6 from Chlamydomonas reinhardtii, and several eukaryotic homologs, including mammalian RSHL1, the protein product of a familial ciliary dyskinesia candidate gene.
Pssm-ID: 461405 [Multi-domain] Cd Length: 406 Bit Score: 564.97 E-value: 0e+00
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
191-238
9.14e-18
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 4 (RSP4) and similar proteins; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. The radial spoke head is made of five different polypeptides (RSP1, RSP4, RSP6, RSP9, and RSP10). This family includes the radial spoke head proteins RSP4 and RSP6 from Chlamydomonas reinhardtii, and several eukaryotic homologs, including mammalian RSHL1 (also called RSPH6A) and RSHL3 (also called RSPH4A), the protein products of familial ciliary dyskinesia candidate genes. RSHL1 is essential for sperm flagellar assembly and male fertility. RSHL3 is a component of the axonemal radial spoke head which plays an important role in ciliary motility. It is required for triplet radial spokes (RS1, RS2 and RS3) head assembly in the motile cilia. Members of this family contain an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.
Pssm-ID: 438532 Cd Length: 51 Bit Score: 77.14 E-value: 9.14e-18
Radial spokehead-like protein; This family includes the radial spoke head proteins RSP4 and ...
195-630
0e+00
Radial spokehead-like protein; This family includes the radial spoke head proteins RSP4 and RSP6 from Chlamydomonas reinhardtii, and several eukaryotic homologs, including mammalian RSHL1, the protein product of a familial ciliary dyskinesia candidate gene.
Pssm-ID: 461405 [Multi-domain] Cd Length: 406 Bit Score: 564.97 E-value: 0e+00
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
191-238
9.14e-18
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 4 (RSP4) and similar proteins; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. The radial spoke head is made of five different polypeptides (RSP1, RSP4, RSP6, RSP9, and RSP10). This family includes the radial spoke head proteins RSP4 and RSP6 from Chlamydomonas reinhardtii, and several eukaryotic homologs, including mammalian RSHL1 (also called RSPH6A) and RSHL3 (also called RSPH4A), the protein products of familial ciliary dyskinesia candidate genes. RSHL1 is essential for sperm flagellar assembly and male fertility. RSHL3 is a component of the axonemal radial spoke head which plays an important role in ciliary motility. It is required for triplet radial spokes (RS1, RS2 and RS3) head assembly in the motile cilia. Members of this family contain an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.
Pssm-ID: 438532 Cd Length: 51 Bit Score: 77.14 E-value: 9.14e-18
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.
Click here to see more details.
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
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
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)
mapped to the query sequence.
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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