Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain; This family consists of bacterial ...
619-869
2.58e-10
Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain; This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
The actual alignment was detected with superfamily member pfam17389:
Pssm-ID: 481215 Cd Length: 340 Bit Score: 63.10 E-value: 2.58e-10
Glycosyl hydrolases family 28; Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2. ...
108-405
3.82e-25
Glycosyl hydrolases family 28; Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes is important in cell wall metabolism.
Pssm-ID: 425588 [Multi-domain] Cd Length: 319 Bit Score: 107.47 E-value: 3.82e-25
Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain; This family consists of bacterial ...
619-869
2.58e-10
Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain; This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
Pssm-ID: 407469 Cd Length: 340 Bit Score: 63.10 E-value: 2.58e-10
Glycosyl hydrolases family 28; Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2. ...
108-405
3.82e-25
Glycosyl hydrolases family 28; Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes is important in cell wall metabolism.
Pssm-ID: 425588 [Multi-domain] Cd Length: 319 Bit Score: 107.47 E-value: 3.82e-25
Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain; This family consists of bacterial ...
619-869
2.58e-10
Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain; This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
Pssm-ID: 407469 Cd Length: 340 Bit Score: 63.10 E-value: 2.58e-10
Amylo-alpha-1,6-glucosidase; This family includes human glycogen branching enzyme Swiss:P35573. ...
683-874
1.32e-03
Amylo-alpha-1,6-glucosidase; This family includes human glycogen branching enzyme Swiss:P35573. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog Swiss:O93808 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).
Pssm-ID: 428822 Cd Length: 370 Bit Score: 42.32 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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