SGNH/GDSL hydrolase family protein is a hydrolytic enzyme such as an esterase or lipase; may have multifunctional properties including broad substrate specificity and regiospecificity
N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate ...
43-348
7.77e-151
N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. This N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains.
:
Pssm-ID: 270207 Cd Length: 310 Bit Score: 431.74 E-value: 7.77e-151
C-terminal carbohydrate-binding module; CBM_26 is a family of bacterial carbohydrate-binding ...
346-468
5.24e-77
C-terminal carbohydrate-binding module; CBM_26 is a family of bacterial carbohydrate-binding modules frequently found at the C-terminus of enzymes. The combination is not unusual as the CBMs function to bring the relevant polysaccharide into close proximity to the active site.
:
Pssm-ID: 435600 Cd Length: 125 Bit Score: 236.30 E-value: 5.24e-77
N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate ...
43-348
7.77e-151
N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. This N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains.
Pssm-ID: 270207 Cd Length: 310 Bit Score: 431.74 E-value: 7.77e-151
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The ...
64-325
2.35e-100
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The domain demonstrates catalytic activity similar to that of the SGNH hydrolase-like domain, with the typical Ser-His-Asp triad found in this enzyme. Alginate is an exopolysaccharide that contributes to biofilm formation. ALGX is secreted into the biofilm and is responsible for the acetylation of biofilm polymers that help protect them from host destruction.
Pssm-ID: 435599 Cd Length: 267 Bit Score: 301.57 E-value: 2.35e-100
C-terminal carbohydrate-binding module; CBM_26 is a family of bacterial carbohydrate-binding ...
346-468
5.24e-77
C-terminal carbohydrate-binding module; CBM_26 is a family of bacterial carbohydrate-binding modules frequently found at the C-terminus of enzymes. The combination is not unusual as the CBMs function to bring the relevant polysaccharide into close proximity to the active site.
Pssm-ID: 435600 Cd Length: 125 Bit Score: 236.30 E-value: 5.24e-77
C-terminal carbohydrate-binding domain of the alginate O-acetyltranferase AlgX; The alginate ...
337-461
1.74e-59
C-terminal carbohydrate-binding domain of the alginate O-acetyltranferase AlgX; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. This N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains.
Pssm-ID: 271153 Cd Length: 128 Bit Score: 191.41 E-value: 1.74e-59
N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate ...
43-348
7.77e-151
N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. This N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains.
Pssm-ID: 270207 Cd Length: 310 Bit Score: 431.74 E-value: 7.77e-151
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The ...
64-325
2.35e-100
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The domain demonstrates catalytic activity similar to that of the SGNH hydrolase-like domain, with the typical Ser-His-Asp triad found in this enzyme. Alginate is an exopolysaccharide that contributes to biofilm formation. ALGX is secreted into the biofilm and is responsible for the acetylation of biofilm polymers that help protect them from host destruction.
Pssm-ID: 435599 Cd Length: 267 Bit Score: 301.57 E-value: 2.35e-100
N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins; The ...
40-340
3.40e-83
N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. This wider family includes AlgX, AlgJ, AlgV, and a number of uncharacterized families, some of which may have been mis-annotated in sequence databases.
Pssm-ID: 270205 [Multi-domain] Cd Length: 316 Bit Score: 259.31 E-value: 3.40e-83
C-terminal carbohydrate-binding module; CBM_26 is a family of bacterial carbohydrate-binding ...
346-468
5.24e-77
C-terminal carbohydrate-binding module; CBM_26 is a family of bacterial carbohydrate-binding modules frequently found at the C-terminus of enzymes. The combination is not unusual as the CBMs function to bring the relevant polysaccharide into close proximity to the active site.
Pssm-ID: 435600 Cd Length: 125 Bit Score: 236.30 E-value: 5.24e-77
C-terminal carbohydrate-binding domain of the alginate O-acetyltranferase AlgX; The alginate ...
337-461
1.74e-59
C-terminal carbohydrate-binding domain of the alginate O-acetyltranferase AlgX; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. This N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains.
Pssm-ID: 271153 Cd Length: 128 Bit Score: 191.41 E-value: 1.74e-59
putative alginate O-acetyltranferases AlgJ, AlgV, and similar proteins; The alginate ...
68-324
4.75e-36
putative alginate O-acetyltranferases AlgJ, AlgV, and similar proteins; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this family have been annotated as AlgJ or AlgV, and they closely resemble AlgX in sequence and function, although they lack the C-terminal carbohydrate binding domain of AlgX.
Pssm-ID: 270208 Cd Length: 321 Bit Score: 135.89 E-value: 4.75e-36
Uncharacterized proteins similar to putative alginate O-acetyltranferase; The alginate ...
69-324
3.93e-34
Uncharacterized proteins similar to putative alginate O-acetyltranferase; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such those as by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this uncharacterized family similar to AlgX_N have been annotated as cell division proteins FtsQ, although they share little or no similarity with experimentally characterized members of the FtsQ family.
Pssm-ID: 270210 Cd Length: 298 Bit Score: 129.74 E-value: 3.93e-34
Uncharacterized proteins similar to putative alginate O-acetyltranferase; The alginate ...
65-324
3.69e-12
Uncharacterized proteins similar to putative alginate O-acetyltranferase; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Some members of this uncharacterized family, which resembles AlgX_N, have been annotated as twin-arginine translocation signal, although they share little or no similarity with experimentally characterized proteins that bear the same name.
Pssm-ID: 270209 Cd Length: 313 Bit Score: 67.05 E-value: 3.69e-12
Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate ...
69-288
2.80e-05
Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this uncharacterized protein family resemble AlgX_N.
Pssm-ID: 270206 [Multi-domain] Cd Length: 315 Bit Score: 45.81 E-value: 2.80e-05
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
