arylsulfatase K isoform 2 [Mus musculus]
Protein Classification
alkaline phosphatase family protein( domain architecture ID 581061)
alkaline phosphatase (ALP) family protein may catalyze the hydrolysis of substrates; the ALP superfamily includes alkaline phosphatases and sulfatases
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 ... |
36-342 | 3.14e-160 | |||||
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 cd16171: Pssm-ID: 474031 [Multi-domain] Cd Length: 366 Bit Score: 457.00 E-value: 3.14e-160
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| Name | Accession | Description | Interval | E-value | |||||
| ARSK | cd16171 | arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
36-342 | 3.14e-160 | |||||
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. 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: 293781 [Multi-domain] Cd Length: 366 Bit Score: 457.00 E-value: 3.14e-160
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| AslA | COG3119 | Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
77-363 | 1.57e-67 | |||||
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 220.52 E-value: 1.57e-67
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| PRK13759 | PRK13759 | arylsulfatase; Provisional |
80-348 | 1.45e-39 | |||||
arylsulfatase; Provisional Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 148.28 E-value: 1.45e-39
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| Sulfatase | pfam00884 | Sulfatase; |
137-265 | 2.71e-17 | |||||
Sulfatase; Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 82.09 E-value: 2.71e-17
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| Name | Accession | Description | Interval | E-value | ||||||
| ARSK | cd16171 | arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
36-342 | 3.14e-160 | ||||||
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. 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: 293781 [Multi-domain] Cd Length: 366 Bit Score: 457.00 E-value: 3.14e-160
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| AslA | COG3119 | Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
77-363 | 1.57e-67 | ||||||
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 220.52 E-value: 1.57e-67
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| sulfatase_like | cd16037 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
70-342 | 2.61e-66 | ||||||
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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 215.10 E-value: 2.61e-66
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| sulfatase_like | cd16155 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
70-350 | 2.21e-50 | ||||||
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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 175.06 E-value: 2.21e-50
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| iduronate-2-sulfatase | cd16030 | iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
72-348 | 3.03e-49 | ||||||
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome. Pssm-ID: 293754 [Multi-domain] Cd Length: 435 Bit Score: 173.53 E-value: 3.03e-49
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| choline-sulfatase | cd16032 | choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
120-342 | 3.35e-48 | ||||||
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon. Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 167.76 E-value: 3.35e-48
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| SGSH | cd16027 | N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
73-363 | 8.59e-47 | ||||||
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: 165.37 E-value: 8.59e-47
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| sulfatase_like | cd16033 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
77-363 | 2.79e-44 | ||||||
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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 159.69 E-value: 2.79e-44
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| G6S_like | cd16031 | unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
76-363 | 3.97e-44 | ||||||
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: 159.62 E-value: 3.97e-44
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| sulfatase_like | cd16034 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
73-347 | 9.54e-44 | ||||||
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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 158.12 E-value: 9.54e-44
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| PMH | cd16028 | Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
77-348 | 3.57e-43 | ||||||
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile. Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 157.42 E-value: 3.57e-43
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| sulfatase_like | cd16152 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
77-362 | 1.40e-41 | ||||||
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: 293771 [Multi-domain] Cd Length: 373 Bit Score: 151.61 E-value: 1.40e-41
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| ARS_like | cd16146 | uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
70-362 | 3.12e-40 | ||||||
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: 148.85 E-value: 3.12e-40
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| PRK13759 | PRK13759 | arylsulfatase; Provisional |
80-348 | 1.45e-39 | ||||||
arylsulfatase; Provisional Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 148.28 E-value: 1.45e-39
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| sulfatase_like | cd16022 | sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
78-275 | 3.41e-39 | ||||||
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: 141.04 E-value: 3.41e-39
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| sulfatase_like | cd16150 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
71-362 | 3.13e-38 | ||||||
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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 143.53 E-value: 3.13e-38
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| ARS_like | cd16144 | uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
77-364 | 7.88e-36 | ||||||
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: 136.90 E-value: 7.88e-36
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| G6S | cd16147 | glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
77-348 | 2.14e-29 | ||||||
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); 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. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs). Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 118.42 E-value: 2.14e-29
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| ARS_like | cd16145 | uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
77-352 | 2.48e-29 | ||||||
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: 118.85 E-value: 2.48e-29
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| ARS_like | cd16143 | uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
77-348 | 1.26e-27 | ||||||
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: 113.45 E-value: 1.26e-27
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| sulfatase_like | cd16148 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
174-277 | 2.28e-27 | ||||||
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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 110.33 E-value: 2.28e-27
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| PAS_like | cd16025 | Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
70-347 | 3.64e-24 | ||||||
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: 103.68 E-value: 3.64e-24
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| sulfatase_like | cd16035 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
173-287 | 1.47e-23 | ||||||
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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 100.36 E-value: 1.47e-23
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| GALNS_like | cd16026 | galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
77-348 | 4.02e-23 | ||||||
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: 100.72 E-value: 4.02e-23
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| sulfatase_like | cd16151 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
164-347 | 5.15e-22 | ||||||
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: 96.90 E-value: 5.15e-22
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| sulfatase_like | cd16156 | uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
170-346 | 2.20e-19 | ||||||
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; 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: 293775 [Multi-domain] Cd Length: 468 Bit Score: 90.13 E-value: 2.20e-19
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| sulfatase_like | cd16149 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
174-277 | 6.00e-19 | ||||||
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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 86.14 E-value: 6.00e-19
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| ES | cd16159 | Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
180-354 | 1.06e-18 | ||||||
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: 88.50 E-value: 1.06e-18
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| Sulfatase | pfam00884 | Sulfatase; |
137-265 | 2.71e-17 | ||||||
Sulfatase; Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 82.09 E-value: 2.71e-17
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| sulfatase_like | cd16154 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
77-343 | 3.27e-16 | ||||||
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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 79.70 E-value: 3.27e-16
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| ARS_like | cd16142 | uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
174-348 | 7.83e-16 | ||||||
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: 78.73 E-value: 7.83e-16
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| 4-S | cd16029 | N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
77-348 | 2.31e-15 | ||||||
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme. Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 77.59 E-value: 2.31e-15
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| sulfatase_like | cd16153 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
174-276 | 6.61e-15 | ||||||
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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 74.72 E-value: 6.61e-15
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| LTA_synthase | cd16015 | Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
151-264 | 1.98e-14 | ||||||
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain. Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 73.49 E-value: 1.98e-14
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| ARSG | cd16161 | arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
139-343 | 2.05e-14 | ||||||
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: 2.05e-14
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| ARSA | cd16158 | Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
179-347 | 1.61e-13 | ||||||
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: 72.09 E-value: 1.61e-13
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| MdoB | COG1368 | Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
161-290 | 2.15e-13 | ||||||
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 71.99 E-value: 2.15e-13
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| ALP_like | cd00016 | alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
174-263 | 2.23e-13 | ||||||
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. Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 69.37 E-value: 2.23e-13
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| YejM | COG3083 | Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
58-327 | 3.64e-13 | ||||||
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms]; Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 71.47 E-value: 3.64e-13
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| spARS_like | cd16160 | sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
140-369 | 6.10e-12 | ||||||
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: 67.07 E-value: 6.10e-12
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| Enpp | cd16018 | Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
176-264 | 6.09e-11 | ||||||
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles. Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 62.60 E-value: 6.09e-11
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| DUF4994 | pfam16385 | Domain of unknown function; This family around 100 residues locates in the C-terminal of some ... |
296-362 | 6.73e-11 | ||||||
Domain of unknown function; This family around 100 residues locates in the C-terminal of some uncharacterized proteins in various Bacteroides and Prevotella species. The function of this family remains unknown. Pssm-ID: 406720 [Multi-domain] Cd Length: 98 Bit Score: 58.84 E-value: 6.73e-11
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| LptA | cd16017 | Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
181-265 | 5.85e-08 | ||||||
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane. Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 53.78 E-value: 5.85e-08
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| GALNS | cd16157 | galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
171-366 | 9.89e-07 | ||||||
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: 50.93 E-value: 9.89e-07
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| iPGM | cd16010 | 2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
178-277 | 4.99e-05 | ||||||
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity. Pssm-ID: 293734 Cd Length: 503 Bit Score: 45.48 E-value: 4.99e-05
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| AP-SPAP | cd16016 | SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
205-268 | 2.60e-04 | ||||||
SPAP is a subclass of alkaline phosphatase (AP); 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. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP. Pssm-ID: 293740 [Multi-domain] Cd Length: 457 Bit Score: 43.29 E-value: 2.60e-04
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| AtaC | COG1524 | c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
174-266 | 5.69e-04 | ||||||
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms]; Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 42.04 E-value: 5.69e-04
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| GpmI | COG0696 | Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
180-278 | 6.58e-04 | ||||||
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-independent), AlkP superfamily is part of the Pathway/BioSystem: Glycolysis Pssm-ID: 440460 Cd Length: 511 Bit Score: 41.96 E-value: 6.58e-04
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| OpgE | COG2194 | Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
181-265 | 1.34e-03 | ||||||
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 441797 [Multi-domain] Cd Length: 537 Bit Score: 40.99 E-value: 1.34e-03
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| GPI_EPT_2 | cd16024 | GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
180-270 | 5.97e-03 | ||||||
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation. Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 38.31 E-value: 5.97e-03
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| DUF229 | pfam02995 | Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
174-270 | 6.89e-03 | ||||||
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate. Pssm-ID: 397236 Cd Length: 496 Bit Score: 38.86 E-value: 6.89e-03
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