ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
406-489
2.19e-17
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 77.18 E-value: 2.19e-17
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
51-247
6.33e-11
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
Pssm-ID: 269892 [Multi-domain] Cd Length: 299 Bit Score: 63.78 E-value: 6.33e-11
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
406-489
2.19e-17
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 77.18 E-value: 2.19e-17
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
505-592
6.40e-17
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 76.03 E-value: 6.40e-17
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
609-683
4.02e-12
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 62.16 E-value: 4.02e-12
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
51-247
6.33e-11
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
Pssm-ID: 269892 [Multi-domain] Cd Length: 299 Bit Score: 63.78 E-value: 6.33e-11
Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan ...
108-195
6.83e-08
Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.
Pssm-ID: 307952 Cd Length: 347 Bit Score: 55.09 E-value: 6.83e-08
Glycoside Hydrolase Family 66; Glycoside Hydrolase Family 66 contains proteins characterized ...
163-207
1.37e-04
Glycoside Hydrolase Family 66; Glycoside Hydrolase Family 66 contains proteins characterized as cycloisomaltooligosaccharide glucanotransferase (CITase) and dextranases from a variety of bacteria. CITase cyclizes part of a (1-6)-alpha-D-glucan (dextrans) chain by formation of a (1-6)-alpha-D-glucosidic bond. Dextranases catalyze the endohydrolysis of (1-6)-alpha-D-glucosidic linkages in dextran. Some members contain Carbohydrate Binding Module 35 (CBM35) domains, either C-terminal or inserted in the domain or both.
Pssm-ID: 270613 Cd Length: 331 Bit Score: 44.54 E-value: 1.37e-04
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1, ...
113-191
7.41e-04
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes firmicutes, bacteroidetes, and proteobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
Pssm-ID: 200452 [Multi-domain] Cd Length: 336 Bit Score: 42.15 E-value: 7.41e-04
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
60-291
1.32e-03
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
Pssm-ID: 200488 [Multi-domain] Cd Length: 390 Bit Score: 41.49 E-value: 1.32e-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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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