N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins; The ...
59-347
1.52e-57
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.
The actual alignment was detected with superfamily member cd14440:
Pssm-ID: 450039 [Multi-domain] Cd Length: 315 Bit Score: 189.10 E-value: 1.52e-57
Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate ...
59-347
1.52e-57
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: 189.10 E-value: 1.52e-57
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The ...
89-257
2.35e-12
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: 66.21 E-value: 2.35e-12
Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate ...
59-347
1.52e-57
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: 189.10 E-value: 1.52e-57
N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins; The ...
54-345
9.38e-25
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: 102.53 E-value: 9.38e-25
putative alginate O-acetyltranferases AlgJ, AlgV, and similar proteins; The alginate ...
55-254
5.05e-14
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: 71.95 E-value: 5.05e-14
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The ...
89-257
2.35e-12
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: 66.21 E-value: 2.35e-12
Uncharacterized proteins similar to putative alginate O-acetyltranferase; The alginate ...
88-311
2.82e-05
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: 45.48 E-value: 2.82e-05
DHHW protein; This family of proteins is found in bacteria. Proteins in this family are ...
161-224
8.55e-04
DHHW protein; This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 404 amino acids in length. There is a conserved DHHW motif. There is some distant homology to the Lipase_GDSL_2 family.
Pssm-ID: 405044 [Multi-domain] Cd Length: 385 Bit Score: 40.84 E-value: 8.55e-04
N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate ...
83-306
4.12e-03
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: 38.45 E-value: 4.12e-03
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.
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