Alpha-L-fucosidase; O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that ...
82-509
7.78e-173
Alpha-L-fucosidase; O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis.
:
Pssm-ID: 214829 Cd Length: 384 Bit Score: 494.12 E-value: 7.78e-173
Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of ...
478-554
5.77e-07
Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of eight anti-parallel-strands packed into two-sheets of five and three strands, respectively, forming a two-layer-sandwich containing a Greek key motif.
The actual alignment was detected with superfamily member pfam16757:
Pssm-ID: 465259 Cd Length: 90 Bit Score: 47.66 E-value: 5.77e-07
Alpha-L-fucosidase; O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that ...
82-509
7.78e-173
Alpha-L-fucosidase; O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis.
Pssm-ID: 214829 Cd Length: 384 Bit Score: 494.12 E-value: 7.78e-173
Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of ...
478-554
5.77e-07
Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of eight anti-parallel-strands packed into two-sheets of five and three strands, respectively, forming a two-layer-sandwich containing a Greek key motif.
Pssm-ID: 465259 Cd Length: 90 Bit Score: 47.66 E-value: 5.77e-07
Alpha-L-fucosidase; O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that ...
82-509
7.78e-173
Alpha-L-fucosidase; O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis.
Pssm-ID: 214829 Cd Length: 384 Bit Score: 494.12 E-value: 7.78e-173
Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of ...
478-554
5.77e-07
Alpha-L-fucosidase C-terminal domain; The C-terminal domain of PDB:1hl8 is constructed of eight anti-parallel-strands packed into two-sheets of five and three strands, respectively, forming a two-layer-sandwich containing a Greek key motif.
Pssm-ID: 465259 Cd Length: 90 Bit Score: 47.66 E-value: 5.77e-07
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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