Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
428-616
6.34e-37
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
:
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 137.79 E-value: 6.34e-37
Clip-domain serine protease homolog Scarface; The clip domain is a structural/regulatory unit ...
343-408
4.90e-35
Clip-domain serine protease homolog Scarface; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. The most prominent family member of carrying this clip domain is Scarface proteins in drosophila, which bear an inactive catalytic site, representing a subgroup of serine protease homologs (SPH). Loss-of-function induces defects in JNK-controlled morphogenetic events such as embryonic dorsal closure and adult male terminalia rotation.
The actual alignment was detected with superfamily member pfam18399:
Pssm-ID: 465747 [Multi-domain] Cd Length: 66 Bit Score: 126.75 E-value: 4.90e-35
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
63-338
1.02e-04
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: 45.53 E-value: 1.02e-04
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
428-616
6.34e-37
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 137.79 E-value: 6.34e-37
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
428-616
8.02e-36
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 134.73 E-value: 8.02e-36
Clip-domain serine protease homolog Scarface; The clip domain is a structural/regulatory unit ...
343-408
4.90e-35
Clip-domain serine protease homolog Scarface; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. The most prominent family member of carrying this clip domain is Scarface proteins in drosophila, which bear an inactive catalytic site, representing a subgroup of serine protease homologs (SPH). Loss-of-function induces defects in JNK-controlled morphogenetic events such as embryonic dorsal closure and adult male terminalia rotation.
Pssm-ID: 465747 [Multi-domain] Cd Length: 66 Bit Score: 126.75 E-value: 4.90e-35
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
63-338
1.02e-04
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: 45.53 E-value: 1.02e-04
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
428-616
6.34e-37
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 137.79 E-value: 6.34e-37
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
428-616
8.02e-36
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 134.73 E-value: 8.02e-36
Clip-domain serine protease homolog Scarface; The clip domain is a structural/regulatory unit ...
343-408
4.90e-35
Clip-domain serine protease homolog Scarface; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. The most prominent family member of carrying this clip domain is Scarface proteins in drosophila, which bear an inactive catalytic site, representing a subgroup of serine protease homologs (SPH). Loss-of-function induces defects in JNK-controlled morphogenetic events such as embryonic dorsal closure and adult male terminalia rotation.
Pssm-ID: 465747 [Multi-domain] Cd Length: 66 Bit Score: 126.75 E-value: 4.90e-35
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
63-338
1.02e-04
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: 45.53 E-value: 1.02e-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.
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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.
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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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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
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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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