tetratricopeptide repeat (TPR) protein may adopt a right-handed helical structure with an amphipathic channel and may function as an interaction scaffold in the formation of multi-protein complexes
An uncharacterized central domain of CLU mitochondrial proteins; Mutations in the ...
739-880
4.17e-37
An uncharacterized central domain of CLU mitochondrial proteins; Mutations in the mitochondrial CLU proteins have been shown to result in clustered mitochondria. CLU proteins include Saccharomyces cerevisiae clustered mitochondria protein (Clu1p, alias translation initiation factor 31/TIF31p), Dictyostelium discoideum clustered mitochondria protein homolog (CluA), Caenorhabditis elegans clustered mitochondria protein homolog (CLUH/ Protein KIAA0664), Drosophila clueless (alias clustered mitochondria protein homolog), Arabidopsis clustered mitochondria protein (CLU, alias friendly mitochondria protein/FMT), and human clustered mitochondria protein homolog (CLUH). Dictyostelium CluA is involved in mitochondrial dynamics and is necessary for both, mitochondrial fission and fusion. Drosophila clueless is essential for cytoplasmic localization and function of cellular mitochondria. The Drosophila clu gene interacts genetically with parkin (park, the Drosophila ortholog of a human gene responsible for many familial cases of Parkinson's disease). Arabidopsis CLU/FMT is required for correct mitochondrial distribution and morphology. The specific role CLU proteins play in mitochondrial processes in not yet known. In an early study, S. cerevisiae Clu1/TIF31p was reported as sometimes being associated with the elF3 translation initiation factor. The authors noted, however, that its tentative assignment as a subunit of elf3 was uncertain, and to date there has been no direct evidence for a role of this protein in translation.
:
Pssm-ID: 271318 Cd Length: 159 Bit Score: 137.87 E-value: 4.17e-37
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
943-1130
4.29e-13
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
The actual alignment was detected with superfamily member NF040586:
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 74.96 E-value: 4.29e-13
Mitochondrial function, CLU-N-term; CLU_N is the N-terminal domain of the Clueless protein, ...
45-115
2.82e-05
Mitochondrial function, CLU-N-term; CLU_N is the N-terminal domain of the Clueless protein, also known as TIF31-like in other organizms. The function of this domain is not known. It family is found in association with pfam13236.
The actual alignment was detected with superfamily member pfam15044:
Pssm-ID: 464466 Cd Length: 79 Bit Score: 44.17 E-value: 2.82e-05
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1649-1789
3.34e-05
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
The actual alignment was detected with superfamily member pfam03154:
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 49.00 E-value: 3.34e-05
An uncharacterized central domain of CLU mitochondrial proteins; Mutations in the ...
739-880
4.17e-37
An uncharacterized central domain of CLU mitochondrial proteins; Mutations in the mitochondrial CLU proteins have been shown to result in clustered mitochondria. CLU proteins include Saccharomyces cerevisiae clustered mitochondria protein (Clu1p, alias translation initiation factor 31/TIF31p), Dictyostelium discoideum clustered mitochondria protein homolog (CluA), Caenorhabditis elegans clustered mitochondria protein homolog (CLUH/ Protein KIAA0664), Drosophila clueless (alias clustered mitochondria protein homolog), Arabidopsis clustered mitochondria protein (CLU, alias friendly mitochondria protein/FMT), and human clustered mitochondria protein homolog (CLUH). Dictyostelium CluA is involved in mitochondrial dynamics and is necessary for both, mitochondrial fission and fusion. Drosophila clueless is essential for cytoplasmic localization and function of cellular mitochondria. The Drosophila clu gene interacts genetically with parkin (park, the Drosophila ortholog of a human gene responsible for many familial cases of Parkinson's disease). Arabidopsis CLU/FMT is required for correct mitochondrial distribution and morphology. The specific role CLU proteins play in mitochondrial processes in not yet known. In an early study, S. cerevisiae Clu1/TIF31p was reported as sometimes being associated with the elF3 translation initiation factor. The authors noted, however, that its tentative assignment as a subunit of elf3 was uncertain, and to date there has been no direct evidence for a role of this protein in translation.
Pssm-ID: 271318 Cd Length: 159 Bit Score: 137.87 E-value: 4.17e-37
Translation initiation factor eIF3 subunit 135; Translation initiation factor eIF3 is a ...
736-879
3.35e-30
Translation initiation factor eIF3 subunit 135; Translation initiation factor eIF3 is a multi-subunit protein complex required for initiation of protein biosynthesis in eukaryotic cells. The complex promotes ribosome dissociation, the binding of the initiator methionyl-tRNA to the 40 S ribosomal subunit, and mRNA recruitment to the ribosome. The protein product from TIF31 genes in yeast is p135 which associates with the eIF3 but does not seem to be necessary for protein translation initiation.
Pssm-ID: 463717 Cd Length: 168 Bit Score: 118.44 E-value: 3.35e-30
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
943-1130
4.29e-13
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 74.96 E-value: 4.29e-13
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
922-1094
2.67e-08
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 59.16 E-value: 2.67e-08
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
960-1175
7.55e-06
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 51.07 E-value: 7.55e-06
Mitochondrial function, CLU-N-term; CLU_N is the N-terminal domain of the Clueless protein, ...
45-115
2.82e-05
Mitochondrial function, CLU-N-term; CLU_N is the N-terminal domain of the Clueless protein, also known as TIF31-like in other organizms. The function of this domain is not known. It family is found in association with pfam13236.
Pssm-ID: 464466 Cd Length: 79 Bit Score: 44.17 E-value: 2.82e-05
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1649-1789
3.34e-05
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 49.00 E-value: 3.34e-05
An uncharacterized central domain of CLU mitochondrial proteins; Mutations in the ...
739-880
4.17e-37
An uncharacterized central domain of CLU mitochondrial proteins; Mutations in the mitochondrial CLU proteins have been shown to result in clustered mitochondria. CLU proteins include Saccharomyces cerevisiae clustered mitochondria protein (Clu1p, alias translation initiation factor 31/TIF31p), Dictyostelium discoideum clustered mitochondria protein homolog (CluA), Caenorhabditis elegans clustered mitochondria protein homolog (CLUH/ Protein KIAA0664), Drosophila clueless (alias clustered mitochondria protein homolog), Arabidopsis clustered mitochondria protein (CLU, alias friendly mitochondria protein/FMT), and human clustered mitochondria protein homolog (CLUH). Dictyostelium CluA is involved in mitochondrial dynamics and is necessary for both, mitochondrial fission and fusion. Drosophila clueless is essential for cytoplasmic localization and function of cellular mitochondria. The Drosophila clu gene interacts genetically with parkin (park, the Drosophila ortholog of a human gene responsible for many familial cases of Parkinson's disease). Arabidopsis CLU/FMT is required for correct mitochondrial distribution and morphology. The specific role CLU proteins play in mitochondrial processes in not yet known. In an early study, S. cerevisiae Clu1/TIF31p was reported as sometimes being associated with the elF3 translation initiation factor. The authors noted, however, that its tentative assignment as a subunit of elf3 was uncertain, and to date there has been no direct evidence for a role of this protein in translation.
Pssm-ID: 271318 Cd Length: 159 Bit Score: 137.87 E-value: 4.17e-37
Translation initiation factor eIF3 subunit 135; Translation initiation factor eIF3 is a ...
736-879
3.35e-30
Translation initiation factor eIF3 subunit 135; Translation initiation factor eIF3 is a multi-subunit protein complex required for initiation of protein biosynthesis in eukaryotic cells. The complex promotes ribosome dissociation, the binding of the initiator methionyl-tRNA to the 40 S ribosomal subunit, and mRNA recruitment to the ribosome. The protein product from TIF31 genes in yeast is p135 which associates with the eIF3 but does not seem to be necessary for protein translation initiation.
Pssm-ID: 463717 Cd Length: 168 Bit Score: 118.44 E-value: 3.35e-30
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
943-1130
4.29e-13
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 74.96 E-value: 4.29e-13
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
922-1094
2.67e-08
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 59.16 E-value: 2.67e-08
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
960-1175
7.55e-06
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 51.07 E-value: 7.55e-06
Mitochondrial function, CLU-N-term; CLU_N is the N-terminal domain of the Clueless protein, ...
45-115
2.82e-05
Mitochondrial function, CLU-N-term; CLU_N is the N-terminal domain of the Clueless protein, also known as TIF31-like in other organizms. The function of this domain is not known. It family is found in association with pfam13236.
Pssm-ID: 464466 Cd Length: 79 Bit Score: 44.17 E-value: 2.82e-05
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1649-1789
3.34e-05
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 49.00 E-value: 3.34e-05
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
1658-1744
2.53e-04
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 43.32 E-value: 2.53e-04
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.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
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
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(specific hits) are drawn in bright colors.
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
(CDART).
Modify your query to search against a different database and/or use advanced search options
