CLEC16A C-terminal; This is the C-terminal domain of C-type lectin domain family 16, member A ...
245-666
0e+00
CLEC16A C-terminal; This is the C-terminal domain of C-type lectin domain family 16, member A (CLEC16A, the Drosophila orthologue Ema and GOP-1 in C. elegans), an evolutionarily conserved endosomal membrane protein required for trafficking of fluid-phase and receptor-mediated endocytic cargos. It is required for mitophagy, autophagy and endosome maturation. This protein has been identified as a susceptibility gene for autoimmune diseases like type 1 diabetes, multiple sclerosis and adrenal dysfunction. This domain is also present in GFS9/TT9 (TRANSPARENT TESTA 9) a protein from Arabidopsis required for vacuolar development through membrane fusion at vacuoles and for membrane trafficking machinery and accumulation of flavonoids in the seed coat.
The actual alignment was detected with superfamily member pfam19439:
Pssm-ID: 466083 Cd Length: 762 Bit Score: 877.68 E-value: 0e+00
Uncharacterized conserved protein; This entry represents an N-terminal region of approximately ...
51-198
1.16e-72
Uncharacterized conserved protein; This entry represents an N-terminal region of approximately 150 residues of a family of proteins of unknown function. It contains a highly conserved FPL motif.
:
Pssm-ID: 462884 Cd Length: 148 Bit Score: 231.67 E-value: 1.16e-72
CLEC16A C-terminal; This is the C-terminal domain of C-type lectin domain family 16, member A ...
245-666
0e+00
CLEC16A C-terminal; This is the C-terminal domain of C-type lectin domain family 16, member A (CLEC16A, the Drosophila orthologue Ema and GOP-1 in C. elegans), an evolutionarily conserved endosomal membrane protein required for trafficking of fluid-phase and receptor-mediated endocytic cargos. It is required for mitophagy, autophagy and endosome maturation. This protein has been identified as a susceptibility gene for autoimmune diseases like type 1 diabetes, multiple sclerosis and adrenal dysfunction. This domain is also present in GFS9/TT9 (TRANSPARENT TESTA 9) a protein from Arabidopsis required for vacuolar development through membrane fusion at vacuoles and for membrane trafficking machinery and accumulation of flavonoids in the seed coat.
Pssm-ID: 466083 Cd Length: 762 Bit Score: 877.68 E-value: 0e+00
Uncharacterized conserved protein; This entry represents an N-terminal region of approximately ...
51-198
1.16e-72
Uncharacterized conserved protein; This entry represents an N-terminal region of approximately 150 residues of a family of proteins of unknown function. It contains a highly conserved FPL motif.
Pssm-ID: 462884 Cd Length: 148 Bit Score: 231.67 E-value: 1.16e-72
CLEC16A C-terminal; This is the C-terminal domain of C-type lectin domain family 16, member A ...
245-666
0e+00
CLEC16A C-terminal; This is the C-terminal domain of C-type lectin domain family 16, member A (CLEC16A, the Drosophila orthologue Ema and GOP-1 in C. elegans), an evolutionarily conserved endosomal membrane protein required for trafficking of fluid-phase and receptor-mediated endocytic cargos. It is required for mitophagy, autophagy and endosome maturation. This protein has been identified as a susceptibility gene for autoimmune diseases like type 1 diabetes, multiple sclerosis and adrenal dysfunction. This domain is also present in GFS9/TT9 (TRANSPARENT TESTA 9) a protein from Arabidopsis required for vacuolar development through membrane fusion at vacuoles and for membrane trafficking machinery and accumulation of flavonoids in the seed coat.
Pssm-ID: 466083 Cd Length: 762 Bit Score: 877.68 E-value: 0e+00
Uncharacterized conserved protein; This entry represents an N-terminal region of approximately ...
51-198
1.16e-72
Uncharacterized conserved protein; This entry represents an N-terminal region of approximately 150 residues of a family of proteins of unknown function. It contains a highly conserved FPL motif.
Pssm-ID: 462884 Cd Length: 148 Bit Score: 231.67 E-value: 1.16e-72
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.
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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.
(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,
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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
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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