Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
559-636
1.33e-10
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.
:
Pssm-ID: 436869 [Multi-domain] Cd Length: 75 Bit Score: 57.62 E-value: 1.33e-10
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
559-636
1.33e-10
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.
Pssm-ID: 436869 [Multi-domain] Cd Length: 75 Bit Score: 57.62 E-value: 1.33e-10
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
559-636
4.27e-09
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.
Pssm-ID: 275036 [Multi-domain] Cd Length: 72 Bit Score: 53.18 E-value: 4.27e-09
uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily; ...
396-522
2.14e-08
uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules.
Pssm-ID: 271154 Cd Length: 132 Bit Score: 53.08 E-value: 2.14e-08
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
559-637
1.28e-07
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).
Pssm-ID: 468356 [Multi-domain] Cd Length: 868 Bit Score: 55.04 E-value: 1.28e-07
type IX secretion system sortase PorU; PorU, part of type IX secretion systems (T9SS), is the ...
558-638
1.66e-06
type IX secretion system sortase PorU; PorU, part of type IX secretion systems (T9SS), is the protease responsible for both removing the C-terminal sorting signal found in substrates and for its replacement by anionic LPS, through which most T9SS substrates become attached to the cell surface after secretion.
Pssm-ID: 468145 [Multi-domain] Cd Length: 1056 Bit Score: 51.40 E-value: 1.66e-06
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
559-636
1.33e-10
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.
Pssm-ID: 436869 [Multi-domain] Cd Length: 75 Bit Score: 57.62 E-value: 1.33e-10
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
559-636
4.27e-09
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.
Pssm-ID: 275036 [Multi-domain] Cd Length: 72 Bit Score: 53.18 E-value: 4.27e-09
uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily; ...
396-522
2.14e-08
uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules.
Pssm-ID: 271154 Cd Length: 132 Bit Score: 53.08 E-value: 2.14e-08
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
559-637
1.28e-07
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).
Pssm-ID: 468356 [Multi-domain] Cd Length: 868 Bit Score: 55.04 E-value: 1.28e-07
type IX secretion system sortase PorU; PorU, part of type IX secretion systems (T9SS), is the ...
558-638
1.66e-06
type IX secretion system sortase PorU; PorU, part of type IX secretion systems (T9SS), is the protease responsible for both removing the C-terminal sorting signal found in substrates and for its replacement by anionic LPS, through which most T9SS substrates become attached to the cell surface after secretion.
Pssm-ID: 468145 [Multi-domain] Cd Length: 1056 Bit Score: 51.40 E-value: 1.66e-06
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,
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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