LPS biosynthesis-modulating metalloenzyme YejM [Erwinia amylovora]
Protein Classification
DUF3413 domain-containing protein( domain architecture ID 17609232)
DUF3413 domain-containing protein with an alkaline phosphatase/sulfatase domain, similar to Salmonella enterica membrane-anchored periplasmic protein YejM
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||
| LapC_YejM_PbgA | NF038282 | LPS biosynthesis-modulating metalloenzyme YejM; YejM (LapC, PbgA) belongs to a regulatory ... |
1-583 | 0e+00 | |||||||||
LPS biosynthesis-modulating metalloenzyme YejM; YejM (LapC, PbgA) belongs to a regulatory system that controls the activity of LpxC, the enzyme that catalyzes the first committed step in the LPS synthesis. The earlier report (2015) by Dalebroux, et al (PMID: 25856753), which assigned a role in cardiolipin transport and introduced the name PbgA (phoPQ-barrier gene A), is no longer considered accurate. : Pssm-ID: 468449 [Multi-domain] Cd Length: 584 Bit Score: 1169.76 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||||
| LapC_YejM_PbgA | NF038282 | LPS biosynthesis-modulating metalloenzyme YejM; YejM (LapC, PbgA) belongs to a regulatory ... |
1-583 | 0e+00 | |||||||||
LPS biosynthesis-modulating metalloenzyme YejM; YejM (LapC, PbgA) belongs to a regulatory system that controls the activity of LpxC, the enzyme that catalyzes the first committed step in the LPS synthesis. The earlier report (2015) by Dalebroux, et al (PMID: 25856753), which assigned a role in cardiolipin transport and introduced the name PbgA (phoPQ-barrier gene A), is no longer considered accurate. Pssm-ID: 468449 [Multi-domain] Cd Length: 584 Bit Score: 1169.76 E-value: 0e+00
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| YejM | COG3083 | Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
15-582 | 0e+00 | |||||||||
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: 868.07 E-value: 0e+00
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| DUF3413 | pfam11893 | Domain of unknown function (DUF3413); This presumed domain is functionally uncharacterized. ... |
7-252 | 4.08e-130 | |||||||||
Domain of unknown function (DUF3413); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 250 amino acids in length. This domain is found associated with pfam00884. Pssm-ID: 432169 Cd Length: 246 Bit Score: 380.44 E-value: 4.08e-130
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| sulfatase_like | cd16148 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
260-517 | 3.40e-39 | |||||||||
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: 144.61 E-value: 3.40e-39
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| PRK13759 | PRK13759 | arylsulfatase; Provisional |
406-496 | 2.73e-07 | |||||||||
arylsulfatase; Provisional Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 53.13 E-value: 2.73e-07
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| Name | Accession | Description | Interval | E-value | |||||||||
| LapC_YejM_PbgA | NF038282 | LPS biosynthesis-modulating metalloenzyme YejM; YejM (LapC, PbgA) belongs to a regulatory ... |
1-583 | 0e+00 | |||||||||
LPS biosynthesis-modulating metalloenzyme YejM; YejM (LapC, PbgA) belongs to a regulatory system that controls the activity of LpxC, the enzyme that catalyzes the first committed step in the LPS synthesis. The earlier report (2015) by Dalebroux, et al (PMID: 25856753), which assigned a role in cardiolipin transport and introduced the name PbgA (phoPQ-barrier gene A), is no longer considered accurate. Pssm-ID: 468449 [Multi-domain] Cd Length: 584 Bit Score: 1169.76 E-value: 0e+00
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| YejM | COG3083 | Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
15-582 | 0e+00 | |||||||||
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: 868.07 E-value: 0e+00
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| DUF3413 | pfam11893 | Domain of unknown function (DUF3413); This presumed domain is functionally uncharacterized. ... |
7-252 | 4.08e-130 | |||||||||
Domain of unknown function (DUF3413); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 250 amino acids in length. This domain is found associated with pfam00884. Pssm-ID: 432169 Cd Length: 246 Bit Score: 380.44 E-value: 4.08e-130
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| sulfatase_like | cd16148 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
260-517 | 3.40e-39 | |||||||||
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: 144.61 E-value: 3.40e-39
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| MdoB | COG1368 | Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
21-561 | 1.11e-26 | |||||||||
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 114.37 E-value: 1.11e-26
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| Sulfatase | pfam00884 | Sulfatase; |
260-499 | 7.17e-25 | |||||||||
Sulfatase; Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 104.81 E-value: 7.17e-25
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| AslA | COG3119 | Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
260-515 | 3.77e-17 | |||||||||
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 83.77 E-value: 3.77e-17
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| sulfatase_like | cd16022 | sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
260-495 | 1.44e-16 | |||||||||
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: 79.40 E-value: 1.44e-16
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| LTA_synthase | cd16015 | Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
278-499 | 3.30e-13 | |||||||||
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: 70.40 E-value: 3.30e-13
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| sulfatase_like | cd16035 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
260-496 | 1.16e-12 | |||||||||
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: 69.16 E-value: 1.16e-12
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| ALP_like | cd00016 | alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
260-499 | 1.56e-12 | |||||||||
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: 67.45 E-value: 1.56e-12
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| SGSH | cd16027 | N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
414-520 | 5.82e-10 | |||||||||
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: 61.37 E-value: 5.82e-10
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| sulfatase_like | cd16034 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
405-556 | 7.48e-10 | |||||||||
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: 61.05 E-value: 7.48e-10
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| PMH | cd16028 | Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
420-497 | 9.80e-09 | |||||||||
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: 57.65 E-value: 9.80e-09
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| G6S_like | cd16031 | unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
413-515 | 1.65e-08 | |||||||||
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: 57.15 E-value: 1.65e-08
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| ARS_like | cd16145 | uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
422-506 | 2.56e-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: 56.45 E-value: 2.56e-08
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| G6S | cd16147 | glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
411-497 | 2.75e-08 | |||||||||
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: 56.02 E-value: 2.75e-08
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| sulfatase_like | cd16155 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
422-515 | 3.94e-08 | |||||||||
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: 55.65 E-value: 3.94e-08
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| sulfatase_like | cd16037 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
279-516 | 7.92e-08 | |||||||||
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: 54.47 E-value: 7.92e-08
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| choline-sulfatase | cd16032 | choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
422-496 | 1.37e-07 | |||||||||
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: 53.74 E-value: 1.37e-07
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| PRK13759 | PRK13759 | arylsulfatase; Provisional |
406-496 | 2.73e-07 | |||||||||
arylsulfatase; Provisional Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 53.13 E-value: 2.73e-07
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| ARS_like | cd16143 | uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
279-495 | 3.49e-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: 293762 [Multi-domain] Cd Length: 395 Bit Score: 52.59 E-value: 3.49e-07
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| sulfatase_like | cd16149 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
415-496 | 5.09e-07 | |||||||||
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: 51.09 E-value: 5.09e-07
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| sulfatase_like | cd16033 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
422-515 | 8.83e-07 | |||||||||
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: 51.45 E-value: 8.83e-07
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| ARS_like | cd16146 | uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
422-515 | 1.36e-06 | |||||||||
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: 51.01 E-value: 1.36e-06
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| sulfatase_like | cd16150 | uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
279-496 | 3.57e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 46.46 E-value: 3.57e-05
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| ARS_like | cd16144 | uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
379-515 | 3.75e-05 | |||||||||
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: 46.38 E-value: 3.75e-05
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| PAS_like | cd16025 | Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
381-509 | 5.41e-05 | |||||||||
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: 45.90 E-value: 5.41e-05
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| spARS_like | cd16160 | sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
385-497 | 6.99e-05 | |||||||||
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: 45.50 E-value: 6.99e-05
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| iduronate-2-sulfatase | cd16030 | iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
422-515 | 9.86e-05 | |||||||||
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: 44.87 E-value: 9.86e-05
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| ARSK | cd16171 | arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
367-496 | 8.54e-04 | |||||||||
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: 41.76 E-value: 8.54e-04
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| GALNS_like | cd16026 | galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
429-495 | 2.52e-03 | |||||||||
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: 40.62 E-value: 2.52e-03
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| AtaC | COG1524 | c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
259-472 | 3.45e-03 | |||||||||
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms]; Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 40.12 E-value: 3.45e-03
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