arylsulfatase G isoform 4 [Mus musculus]
List of domain hits
Name | Accession | Description | Interval | E-value | ||
ALP_like super family | cl23718 | alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
5-48 | 9.09e-18 | ||
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 cd16161: Pssm-ID: 474031 [Multi-domain] Cd Length: 383 Bit Score: 74.43 E-value: 9.09e-18
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Name | Accession | Description | Interval | E-value | ||
ARSG | cd16161 | arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
5-48 | 9.09e-18 | ||
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder. Pssm-ID: 293780 [Multi-domain] Cd Length: 383 Bit Score: 74.43 E-value: 9.09e-18
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AslA | COG3119 | Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
10-39 | 6.19e-10 | ||
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 52.19 E-value: 6.19e-10
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Name | Accession | Description | Interval | E-value | ||
ARSG | cd16161 | arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
5-48 | 9.09e-18 | ||
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder. Pssm-ID: 293780 [Multi-domain] Cd Length: 383 Bit Score: 74.43 E-value: 9.09e-18
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GALNS_like | cd16026 | galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
5-40 | 1.53e-13 | ||
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A. Pssm-ID: 293750 [Multi-domain] Cd Length: 399 Bit Score: 62.58 E-value: 1.53e-13
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ARS_like | cd16142 | uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
5-36 | 2.88e-10 | ||
uncharacterized arylsulfatase subfamily; 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. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases. Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 53.31 E-value: 2.88e-10
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spARS_like | cd16160 | sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
5-37 | 4.49e-10 | ||
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its homologous proteins. 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. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases. Pssm-ID: 293779 [Multi-domain] Cd Length: 445 Bit Score: 52.82 E-value: 4.49e-10
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AslA | COG3119 | Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
10-39 | 6.19e-10 | ||
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 52.19 E-value: 6.19e-10
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ARS_like | cd16143 | uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
1-39 | 8.54e-10 | ||
uncharacterized arylsulfatase subfamily; 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. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases. Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 51.82 E-value: 8.54e-10
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GALNS | cd16157 | galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
10-45 | 1.87e-08 | ||
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A. Pssm-ID: 293776 [Multi-domain] Cd Length: 466 Bit Score: 48.23 E-value: 1.87e-08
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sulfatase_like | cd16022 | sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
10-39 | 5.43e-08 | ||
sulfatase; 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. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases. Pssm-ID: 293746 [Multi-domain] Cd Length: 236 Bit Score: 46.66 E-value: 5.43e-08
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ARS_like | cd16145 | uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
10-36 | 6.28e-08 | ||
uncharacterized arylsulfatase subfamily; 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. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases. Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 46.82 E-value: 6.28e-08
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ARS_like | cd16144 | uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
10-39 | 1.93e-07 | ||
uncharacterized arylsulfatase subfamily; 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. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases. Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 45.23 E-value: 1.93e-07
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ARS_like | cd16146 | uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
9-39 | 2.87e-07 | ||
uncharacterized arylsulfatase; 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. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases. Pssm-ID: 293765 [Multi-domain] Cd Length: 409 Bit Score: 44.85 E-value: 2.87e-07
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ARSA | cd16158 | Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
10-36 | 3.29e-07 | ||
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form. Pssm-ID: 293777 [Multi-domain] Cd Length: 479 Bit Score: 44.74 E-value: 3.29e-07
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ES | cd16159 | Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
2-33 | 5.91e-05 | ||
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen. Pssm-ID: 293778 [Multi-domain] Cd Length: 521 Bit Score: 38.42 E-value: 5.91e-05
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sulfatase_like | cd16151 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
10-39 | 6.71e-05 | ||
uncharacterized sulfatase subfamily; 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. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases. Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 37.96 E-value: 6.71e-05
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SGSH | cd16027 | N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
10-39 | 1.33e-04 | ||
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities. Pssm-ID: 293751 [Multi-domain] Cd Length: 373 Bit Score: 37.10 E-value: 1.33e-04
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PAS_like | cd16025 | Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
9-32 | 4.46e-04 | ||
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; 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. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases. Pssm-ID: 293749 [Multi-domain] Cd Length: 402 Bit Score: 35.88 E-value: 4.46e-04
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G6S_like | cd16031 | unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
10-39 | 7.50e-03 | ||
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. Pssm-ID: 293755 [Multi-domain] Cd Length: 429 Bit Score: 32.50 E-value: 7.50e-03
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