alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
75-508
6.68e-155
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
The actual alignment was detected with superfamily member pfam00245:
Pssm-ID: 474031 Cd Length: 418 Bit Score: 448.07 E-value: 6.68e-155
Alkaline phosphatase [Inorganic ion transport and metabolism, General function prediction only] ...
71-507
6.23e-128
Alkaline phosphatase [Inorganic ion transport and metabolism, General function prediction only]; Alkaline phosphatase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 441391 [Multi-domain] Cd Length: 401 Bit Score: 378.41 E-value: 6.23e-128
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound ...
76-508
3.91e-112
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Mammalian alkaline phosphatase is divided into four isozymes depending upon the site of tissue expression. They are Intestinal ALP, Placental ALP, Germ cell ALP and tissue nonspecific alkaline phosphatase or liver/bone/kidney (L/B/K) ALP.
Pssm-ID: 293736 Cd Length: 283 Bit Score: 333.63 E-value: 3.91e-112
Alkaline phosphatase [Inorganic ion transport and metabolism, General function prediction only] ...
71-507
6.23e-128
Alkaline phosphatase [Inorganic ion transport and metabolism, General function prediction only]; Alkaline phosphatase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 441391 [Multi-domain] Cd Length: 401 Bit Score: 378.41 E-value: 6.23e-128
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound ...
76-508
3.91e-112
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Mammalian alkaline phosphatase is divided into four isozymes depending upon the site of tissue expression. They are Intestinal ALP, Placental ALP, Germ cell ALP and tissue nonspecific alkaline phosphatase or liver/bone/kidney (L/B/K) ALP.
Pssm-ID: 293736 Cd Length: 283 Bit Score: 333.63 E-value: 3.91e-112
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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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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.
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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.
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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