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Conserved domains on  [gi|578815634|ref|XP_006716504|]
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extracellular sulfatase Sulf-1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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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 ...
 5-143 1.07e-70

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 cd16147:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 396  Bit Score: 238.99  E-value: 1.07e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634   5 TPSYNYAPNMDKHWIMQYTGPMLPiHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFG 84
Cdd:cd16147  209 PPPNNPDVSDKPHWLRRLPPLNPT-QIAYIDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHR 287

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578815634  85 LVKGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKS 143
Cdd:cd16147  288 LPPGKRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
DUF3740 pfam12548
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ...
 293-438 3.51e-67

Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and 173 amino acids in length. The family is found in association with pfam00884.


:

Pssm-ID: 463628  Cd Length: 142  Bit Score: 219.91  E-value: 3.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  293 KPRFVHTRQTRSLSVEFEGEIYDINLEEEEelQVLQPRNIAKRH--DEGHKGPRDLQASSGGnrgrMLADSSNAVGPPTT 370
Cdd:pfam12548   1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEEY--QPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPAS 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578815634  371 VRVTHKCFILPNDSIHCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPEECSCSK 438
Cdd:pfam12548  75 VKVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
ALP_like super family cl23718
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 527-576 8.21e-19

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 cd16147:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 396  Bit Score: 89.53  E-value: 8.21e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 578815634 527 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTV 576
Cdd:cd16147  347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
 
Name Accession Description Interval E-value
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 5-143 1.07e-70

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: 238.99  E-value: 1.07e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634   5 TPSYNYAPNMDKHWIMQYTGPMLPiHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFG 84
Cdd:cd16147  209 PPPNNPDVSDKPHWLRRLPPLNPT-QIAYIDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHR 287

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578815634  85 LVKGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKS 143
Cdd:cd16147  288 LPPGKRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
DUF3740 pfam12548
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ...
 293-438 3.51e-67

Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and 173 amino acids in length. The family is found in association with pfam00884.


Pssm-ID: 463628  Cd Length: 142  Bit Score: 219.91  E-value: 3.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  293 KPRFVHTRQTRSLSVEFEGEIYDINLEEEEelQVLQPRNIAKRH--DEGHKGPRDLQASSGGnrgrMLADSSNAVGPPTT 370
Cdd:pfam12548   1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEEY--QPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPAS 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578815634  371 VRVTHKCFILPNDSIHCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPEECSCSK 438
Cdd:pfam12548  75 VKVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
16-173 1.14e-36

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 142.71  E-value: 1.14e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  16 KHWIMQYTG-----PMLPIHMEFTNILQRKRLQT----LMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLV 86
Cdd:COG3119  168 EEYLDKYDGkdiplPPNLAPRDLTEEELRRARAAyaamIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLR 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  87 KGKSMPYDFDIRVPFFIRGP-SVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLdpekpgnrfrTNKKAKi 165
Cdd:COG3119  248 GGKGTLYEGGIRVPLIVRWPgKIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLL----------TGEKAE- 316


                 ....*...
gi 578815634 166 WRDTFLVE 173
Cdd:COG3119  317 WRDYLYWE 324
Sulfatase pfam00884
Sulfatase;
39-133 2.93e-20

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 92.10  E-value: 2.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634   39 RKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFG--LVKGKSM-PYDFDIRVPFFIRGPSVEP-GSIV 114
Cdd:pfam00884 200 NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKAkGQKS 279

                          90
                  ....*....|....*....
gi 578815634  115 PQIVLNIDLAPTILDIAGL 133
Cdd:pfam00884 280 EALVSHVDLFPTILDLAGI 298
PRK13759 PRK13759
arylsulfatase; Provisional
 48-156 3.83e-20

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 94.74  E-value: 3.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKgKSMPYDFDIRVPFFIRGPS----VEPGSIVPQIVLNIDL 123
Cdd:PRK13759 277 IDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDI 355

                         90       100       110
                 ....*....|....*....|....*....|...
gi 578815634 124 APTILDIAGLDTPPDVDGKSVLKLLDPEKPGNR 156
Cdd:PRK13759 356 MPTLLDLAGGTIPDDVDGRSLKNLIFGQYEGWR 388
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 527-576 8.21e-19

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: 89.53  E-value: 8.21e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 578815634 527 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTV 576
Cdd:cd16147  347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
 
Name Accession Description Interval E-value
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 5-143 1.07e-70

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: 238.99  E-value: 1.07e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634   5 TPSYNYAPNMDKHWIMQYTGPMLPiHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFG 84
Cdd:cd16147  209 PPPNNPDVSDKPHWLRRLPPLNPT-QIAYIDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHR 287

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578815634  85 LVKGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKS 143
Cdd:cd16147  288 LPPGKRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
DUF3740 pfam12548
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ...
 293-438 3.51e-67

Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and 173 amino acids in length. The family is found in association with pfam00884.


Pssm-ID: 463628  Cd Length: 142  Bit Score: 219.91  E-value: 3.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  293 KPRFVHTRQTRSLSVEFEGEIYDINLEEEEelQVLQPRNIAKRH--DEGHKGPRDLQASSGGnrgrMLADSSNAVGPPTT 370
Cdd:pfam12548   1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEEY--QPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPAS 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578815634  371 VRVTHKCFILPNDSIHCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPEECSCSK 438
Cdd:pfam12548  75 VKVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
 39-173 2.31e-40

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: 154.61  E-value: 2.31e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  39 RKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGP-SVEPGSIVPQI 117
Cdd:cd16031  237 KDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIRVPLIIRDPrLIKAGTVVDAL 315

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578815634 118 VLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDpekpgnrfrtNKKAKIWRDTFLVE 173
Cdd:cd16031  316 VLNIDFAPTILDLAGVPIPEDMQGRSLLPLLE----------GEKPVDWRKEFYYE 361
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
16-173 1.14e-36

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 142.71  E-value: 1.14e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  16 KHWIMQYTG-----PMLPIHMEFTNILQRKRLQT----LMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLV 86
Cdd:COG3119  168 EEYLDKYDGkdiplPPNLAPRDLTEEELRRARAAyaamIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLR 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  87 KGKSMPYDFDIRVPFFIRGP-SVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLdpekpgnrfrTNKKAKi 165
Cdd:COG3119  248 GGKGTLYEGGIRVPLIVRWPgKIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLL----------TGEKAE- 316


                 ....*...
gi 578815634 166 WRDTFLVE 173
Cdd:COG3119  317 WRDYLYWE 324
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 48-143 4.84e-30

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: 119.08  E-value: 4.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SVEPGSIVPQIVLNIDLAPT 126
Cdd:cd16022  140 IDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPgKIPAGQVSDALVSLLDLLPT 219

                         90
                 ....*....|....*..
gi 578815634 127 ILDIAGLDTPPDVDGKS 143
Cdd:cd16022  220 LLDLAGIEPPEGLDGRS 236
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 48-146 8.04e-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: 110.72  E-value: 8.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMP-YDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPT 126
Cdd:cd16148  172 VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGKEPGKRVDALVSHIDIAPT 251

                         90       100
                 ....*....|....*....|
gi 578815634 127 ILDIAGLDTPPDVDGKSVLK 146
Cdd:cd16148  252 LLDLLGVEPPDYSDGRSLLP 271
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 42-156 2.28e-26

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: 111.83  E-value: 2.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  42 LQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYhigqfGLVKGKSMPYDFDIRVPFFIRGPS-VEPGSIVPQIVLN 120
Cdd:cd16027  192 YDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkIKPGSVSDALVSF 266

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 578815634 121 IDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNR 156
Cdd:cd16027  267 IDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGR 302
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 48-156 5.52e-26

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: 110.73  E-value: 5.52e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTI 127
Cdd:cd16155  201 LDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM-GKQNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTL 279

                         90       100
                 ....*....|....*....|....*....
gi 578815634 128 LDIAGLDTPPDVDGKSVLKLLDPEKPGNR 156
Cdd:cd16155  280 CELAGIEIPESVEGKSLLPVIRGEKKAVR 308
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 48-173 1.61e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 104.23  E-value: 1.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLV-KGKSMpYDFDIRVPFFIRGP-SVEPGSIVPQIVLNIDLAP 125
Cdd:cd16033  226 IDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIPLIIKWPgVIAAGQVVDEFVSLLDLAP 304

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 578815634 126 TILDIAGLDTPPDVDGKSVLKLLDPEKPGNrfrtnkkakiWRDTFLVE 173
Cdd:cd16033  305 TILDLAGVDVPPKVDGRSLLPLLRGEQPED----------WRDEVVTE 342
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 47-156 3.63e-23

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: 103.39  E-value: 3.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  47 SVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLV-------KGKSMPYDFDIRVPFFIRGPSV-EPGSIVPQIV 118
Cdd:cd16144  231 SLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGGKGSLYEGGIRVPLIVRWPGViKPGSVSDVPV 310

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 578815634 119 LNIDLAPTILDIAGLDTPP--DVDGKSVLKLL-DPEKPGNR 156
Cdd:cd16144  311 IGTDLYPTFLELAGGPLPPpqHLDGVSLVPLLkGGEADLPR 351
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 47-156 4.35e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 102.31  E-value: 4.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  47 SVDDSVERLYNMLVETGELENTYIIYTADHGYHigqFGLVKG--KSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLA 124
Cdd:cd16152  183 RLDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHESSIRVPLVIYGPGFNGGGRVEELVSLIDLP 259

                         90       100       110
                 ....*....|....*....|....*....|..
gi 578815634 125 PTILDIAGLDTPPDVDGKSVLKLLDPEKPGNR 156
Cdd:cd16152  260 PTLLDAAGIDVPEEMQGRSLLPLVDGKVEDWR 291
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 48-157 1.80e-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: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 99.15  E-value: 1.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTI 127
Cdd:cd16037  171 LDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTI 249

                         90       100       110
                 ....*....|....*....|....*....|
gi 578815634 128 LDIAGLDTPPDVDGKSVLKLLDPEKPGNRF 157
Cdd:cd16037  250 LEAAGAPPPPDLDGRSLLPLAEGPDDPDRV 279
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 47-159 1.25e-21

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: 98.41  E-value: 1.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  47 SVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSV-EPGSIVPQIVLNIDLAP 125
Cdd:cd16034  235 ALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVPYEESIRVPFIIRYPGKiKAGRVVDLLINTVDIMP 313

                         90       100       110
                 ....*....|....*....|....*....|....
gi 578815634 126 TILDIAGLDTPPDVDGKSVLKLLDPEKPGNRFRT 159
Cdd:cd16034  314 TLLGLCGLPIPDTVEGRDLSPLLLGGKDDEPDSV 347
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
 48-170 6.37e-21

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: 96.56  E-value: 6.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSVE----PGSIVPQIVLNIDL 123
Cdd:cd16028  247 VDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREadatRGQVVDAFTESVDV 325

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 578815634 124 APTILDIAGLDTPPDVDGKSVLKLLDPEKPGNrfrtNKKAKIWRDTF 170
Cdd:cd16028  326 MPTILDWLGGEIPHQCDGRSLLPLLAGAQPSD----WRDAVHYEYDF 368
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 48-156 1.78e-20

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: 95.33  E-value: 1.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSV-EPGSIVPQIVLNIDLAPT 126
Cdd:cd16030  270 VDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHW-GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPT 348

                         90       100       110
                 ....*....|....*....|....*....|.
gi 578815634 127 ILDIAGLDTPPDVDGKSVLKLL-DPEKPGNR 156
Cdd:cd16030  349 LAELAGLPAPPCLEGKSLVPLLkNPSAKWKD 379
Sulfatase pfam00884
Sulfatase;
39-133 2.93e-20

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 92.10  E-value: 2.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634   39 RKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFG--LVKGKSM-PYDFDIRVPFFIRGPSVEP-GSIV 114
Cdd:pfam00884 200 NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKAkGQKS 279

                          90
                  ....*....|....*....
gi 578815634  115 PQIVLNIDLAPTILDIAGL 133
Cdd:pfam00884 280 EALVSHVDLFPTILDLAGI 298
PRK13759 PRK13759
arylsulfatase; Provisional
 48-156 3.83e-20

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 94.74  E-value: 3.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKgKSMPYDFDIRVPFFIRGPS----VEPGSIVPQIVLNIDL 123
Cdd:PRK13759 277 IDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDI 355

                         90       100       110
                 ....*....|....*....|....*....|...
gi 578815634 124 APTILDIAGLDTPPDVDGKSVLKLLDPEKPGNR 156
Cdd:PRK13759 356 MPTLLDLAGGTIPDDVDGRSLKNLIFGQYEGWR 388
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
 48-149 1.79e-19

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: 90.33  E-value: 1.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTI 127
Cdd:cd16032  173 VDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTL 251

                         90       100
                 ....*....|....*....|....*
gi 578815634 128 LDIAGLDTPPDV---DGKSVLKLLD 149
Cdd:cd16032  252 VDLAGGGTAPHVpplDGRSLLPLLE 276
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 47-145 2.74e-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: 88.45  E-value: 2.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  47 SVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGlVKGK-------SMpYDFDIRVPFFIRGPS-VEPGSIVPQIV 118
Cdd:cd16149  150 GVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNSVKVPFIIRWPGvVPAGRVVDSLV 227

                         90       100
                 ....*....|....*....|....*....
gi 578815634 119 LNIDLAPTILDIAGLDTPPDVD--GKSVL 145
Cdd:cd16149  228 SAYDFFPTLLELAGVDPPADPRlpGRSFA 256
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 527-576 8.21e-19

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: 89.53  E-value: 8.21e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 578815634 527 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTV 576
Cdd:cd16147  347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 48-156 8.82e-17

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: 83.82  E-value: 8.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLV-KGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPT 126
Cdd:cd16150  209 LDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPT 288

                         90       100       110
                 ....*....|....*....|....*....|.
gi 578815634 127 ILDIAGLDTPPDVDGKSVLKLL-DPEKPGNR 156
Cdd:cd16150  289 LLDLAGIPLSHTHFGRSLLPVLaGETEEHRD 319
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 44-157 1.69e-16

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: 82.61  E-value: 1.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  44 TLMSVDDSVERLYNMLVETGELENTYIIYTADHG--YHIGQFG-----LVKGKSMPYDFDIRVPFFIRGPS-VEPGSIVP 115
Cdd:cd16026  216 VVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsagpLRGGKGTTWEGGVRVPFIAWWPGvIPAGTVSD 295

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 578815634 116 QIVLNIDLAPTILDIAGLDTPPDV--DGKSVLKLL--DPEKPGNRF 157
Cdd:cd16026  296 ELASTMDLLPTLAALAGAPLPEDRviDGKDISPLLlgGSKSPPHPF 341
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
 48-172 3.15e-16

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: 81.83  E-value: 3.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHGYHIG-----QFGLVKGKSMPYDFDIRVPFFIRGPSV-EPGSIVPQIVLNI 121
Cdd:cd16146  217 IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYEGGHRVPFFIRWPGKiLAGKDVDTLTAHI 296

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578815634 122 DLAPTILDIAGLDTPPDV--DGKSVLKLLdpekpgnrfrTNKKAKiWRDTFLV 172
Cdd:cd16146  297 DLLPTLLDLCGVKLPEGIklDGRSLLPLL----------KGESDP-WPERTLF 338
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 48-156 2.09e-15

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: 79.73  E-value: 2.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETgeLENTYIIYTADHGYHIGQFGL-VKGKSMpYDFDIRVPFFIRGPSVEPGSIVPQI-VLNIDLAP 125
Cdd:cd16156  250 VDYEIGRVLDAADEI--AEDAWVIYTSDHGDMLGAHKLwAKGPAV-YDEITNIPLIIRGKGGEKAGTVTDTpVSHIDLAP 326

                         90       100       110
                 ....*....|....*....|....*....|..
gi 578815634 126 TILDIAGLDTPPDVDGKSVLKLL-DPEKPGNR 156
Cdd:cd16156  327 TILDYAGIPQPKVLEGESILATIeDPEIPENR 358
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 38-148 1.04e-14

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: 77.25  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  38 QRKRLQTLMS-VDDSVERLYNMLVETGELENTYIIYTADHGYHI-------GQF-----GLVKGK-SMpYDFDIRVPFFI 103
Cdd:cd16145  229 PEKAYAAMVTrLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfdsngPLRGYKrSL-YEGGIRVPFIA 307

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 578815634 104 RGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLL 148
Cdd:cd16145  308 RWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTL 353
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
 38-147 1.27e-14

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: 76.71  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  38 QRKRLQTLMSV--------DDSVERLYNMLVETGELENTYIIYTADHG--YHIG--QFG---LVKGKSMPYDFDIRVPFF 102
Cdd:cd16025  210 EKKLEARRMEVyaamvehmDQQIGRLIDYLKELGELDNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLI 289

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 578815634 103 IRGPSV--EPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKL 147
Cdd:cd16025  290 VSWPKGikAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNGVPQLPL 336
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 32-181 5.46e-14

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 75.85  E-value: 5.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  32 EFTNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGyhigqfGLVKGKSmPYDFDI---RVPFFIRGPSV 108
Cdd:COG1368  410 DYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYENPLeryRVPLLIYSPGL 482

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578815634 109 EPGSIVPQIVLNIDLAPTILDIAGLDTPPDVD-GKSvlkLLDPEKPGNRFR-----TNKKAKIWRDTFLVERGKFLRKK 181
Cdd:COG1368  483 KKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAfGRD---LLSPDTDPFAFRnggfiTDDYVYVLKTGELTEEDKELEEE 558
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 48-134 5.78e-14

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: 73.78  E-value: 5.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEP-GSIVPQIVLNIDLAPT 126
Cdd:cd16035  176 VDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGtGQTTDALTSHIDLLPT 255


                 ....*...
gi 578815634 127 ILDIAGLD 134
Cdd:cd16035  256 LLGLAGVD 263
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 46-156 1.72e-13

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: 73.39  E-value: 1.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  46 MSVDDSVERLYNMLVETGELENTYIIYTADHG---YHIGQFGLVKGKSMPYDF-----DI-----RVPFFIRGPS-VEPG 111
Cdd:cd16143  208 YELDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGHDPSGPLrgmkaDIyegghRVPFIVRWPGkIPAG 287

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 578815634 112 SIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLK-LLDPEKPGNR 156
Cdd:cd16143  288 SVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPaLLGPKKQEVR 335
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
 52-153 4.87e-11

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: 65.91  E-value: 4.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  52 VERLYNMLVETGELENTYIIYTADHGYHI------GQFGLVKG-KSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLA 124
Cdd:cd16160  235 VGEVLDTLVDTGLDQNTLVFFLSDHGPHVeyclegGSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIF 314

                         90       100       110
                 ....*....|....*....|....*....|.
gi 578815634 125 PTILDIAGLDTPPD--VDGKSVLKLLDPEKP 153
Cdd:cd16160  315 PTFVDLAGGTLPTDriYDGLSITDLLLGEAD 345
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
 59-148 5.69e-11

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: 65.26  E-value: 5.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  59 LVETGELENTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPD 138
Cdd:cd16171  216 LKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPLLIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN 294

                         90
                 ....*....|
gi 578815634 139 VDGKSVLKLL 148
Cdd:cd16171  295 LSGYSLLPLL 304
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 48-131 7.77e-11

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: 63.21  E-value: 7.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGELENTYIIYTADHG---YHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLA 124
Cdd:cd00016  151 IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPGVKKGGVKHELISQYDIA 230


                 ....*..
gi 578815634 125 PTILDIA 131
Cdd:cd00016  231 PTLADLL 237
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 6-132 9.55e-11

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: 63.47  E-value: 9.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634   6 PSYNYAPNMDKH--WIMQYTGPMLPIHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQF 83
Cdd:cd16015  157 PFFIFLVTMSNHgpYDLPEEKKDEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSD 236

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 578815634  84 GLVKGKSMPYDFdiRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAG 132
Cdd:cd16015  237 YDETDEDPLDLY--RTPLLIYSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 49-148 1.46e-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: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 64.16  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  49 DDSVERLYNMLVETGELENTYIIYTADHGYHIG-----QFGLVKG-KSMPYDFDIRVPFFIRGPS-VEPGSIVPQIVLNI 121
Cdd:cd16151  215 DKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTDAGTHVPLIVNWPGlIPAGGVSDDLVDFS 294

                         90       100
                 ....*....|....*....|....*....
gi 578815634 122 DLAPTILDIAGLDTPPD--VDGKSVLKLL 148
Cdd:cd16151  295 DFLPTLAELAGAPLPEDypLDGRSFAPQL 323
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
 45-148 1.60e-10

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: 64.62  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  45 LMSVDDSVERLYNMLVETGELENTYIIYTADHGYHI-----------GQFGLVKGKSMP-YDFDIRVPFFIRGPSV-EPG 111
Cdd:cd16159  285 VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIYGGKKMGgWEGGIRVPTIVRWPGViPPG 364

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 578815634 112 SIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLKLL 148
Cdd:cd16159  365 SVIDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLL 403
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
 5-144 1.29e-09

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: 61.03  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634   5 TPSYNYAPNMDKHWIMQYTGPMLPIH-MEFTNILQRKR---LQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHI 80
Cdd:cd16029  182 KPLFLYLAFQAVHAPLQVPPEYADPYeDKFAHIKDEDRrtyAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPT 261

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578815634  81 GQFG------LVKGKSMPYDFDIRVPFFIRGPSVEP--GSIVPQIVLNIDLAPTILDIAGLDTP--PDVDGKSV 144
Cdd:cd16029  262 GGGDggsnypLRGGKNTLWEGGVRVPAFVWSPLLPPkrGTVSDGLMHVTDWLPTLLSLAGGDPDdlPPLDGVDQ 335
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 44-138 4.16e-09

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: 59.47  E-value: 4.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  44 TLMSVDDSVERLYNMLVETGELENTYIIYTADHG-----YHIGQFGLVKG-KSMPYDFDIRVPFFIRGPS-VEPGSIVPQ 116
Cdd:cd16142  185 SMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKGTTWEGGVRVPAIVRWPGkIKPGRVSNE 264

                         90       100
                 ....*....|....*....|..
gi 578815634 117 IVLNIDLAPTILDIAGLDTPPD 138
Cdd:cd16142  265 IVSHLDWFPTLAALAGAPDPKD 286
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 48-146 4.20e-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: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 55.46  E-value: 4.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGEL---ENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSVEP---GSIVPQIVLNI 121
Cdd:cd16153  177 GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVPLIVVSSDKLKapaGKVRHDFVEFV 255

                         90       100
                 ....*....|....*....|....*..
gi 578815634 122 DLAPTILDIAGLD--TPPDVDGKSVLK 146
Cdd:cd16153  256 DLAPTLLAAAGVDvdAPDYLDGRDLFE 282
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 45-148 8.36e-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: 55.55  E-value: 8.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  45 LMSVDDSVERLYNMLVETGELENTYIIYTADHG---YHIGQFG-----LVKGKSMPYDFDIRVPFFIRGPS-VEPGSIVP 115
Cdd:cd16157  230 VMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgsngpFLCGKQTTFEGGMREPAIAWWPGhIKPGQVSH 309

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 578815634 116 QIVLNIDLAPTILDIAGLDTPPD--VDGKSVLKLL 148
Cdd:cd16157  310 QLGSLMDLFTTSLALAGLPIPSDraIDGIDLLPVL 344
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 43-132 1.25e-07

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: 53.74  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  43 QTLMSVDDSVERLYNMLVETGELENTYIIYTADHGY-----HiGQFglvkgksmPYDFDIRVPFFIRGPSVEPGSIVPQI 117
Cdd:cd16018  183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GYD--------NELPDMRAIFIARGPAFKKGKKLGPF 253

                         90
                 ....*....|....*
gi 578815634 118 vLNIDLAPTILDIAG 132
Cdd:cd16018  254 -RNVDIYPLMCNLLG 267
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
 32-156 1.68e-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: 54.76  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  32 EFTNILQRKRL-QTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHI------GQFGLVK-GKSMPYDFDIRVPFFI 103
Cdd:cd16158  218 KFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGTTYEGGVREPAIA 297

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578815634 104 RGPS-VEPGsIVPQIVLNIDLAPTILDIAGLDTPP-DVDGKSVLKLLDPEKPGNR 156
Cdd:cd16158  298 YWPGrIKPG-VTHELASTLDILPTIAKLAGAPLPNvTLDGVDMSPILFEQGKSPR 351
COG3379 COG3379
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ...
 101-149 2.94e-06

Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];


Pssm-ID: 442606 [Multi-domain]  Cd Length: 472  Bit Score: 50.67  E-value: 2.94e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 578815634 101 FFIRGPSVEPGSIVPQIVLnIDLAPTILDIAGLDTPPDVDGKSVLKLLD 149
Cdd:COG3379  422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFA 469
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
 44-148 9.10e-06

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: 49.00  E-value: 9.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  44 TLMSVDDSVERLYNMLVETGELENTYIIYTAD---------------HGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPS- 107
Cdd:cd16161  188 ALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGHREPAIVYWPGr 267

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 578815634 108 VEPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLKLL 148
Cdd:cd16161  268 IPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVL 310
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
 42-137 2.21e-05

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: 47.98  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  42 LQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGY-----------HIGQFGlvkgksmpyDFDIRVPFFIRGPSVEP 110
Cdd:COG3083  430 RNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEefnengqnywgHNSNFS---------RYQLQVPLVIHWPGTPP 500

                         90       100
                 ....*....|....*....|....*...
gi 578815634 111 GSIvPQIVLNIDLAPTIL-DIAGLDTPP 137
Cdd:COG3083  501 QVI-SKLTSHLDIVPTLMqRLLGVQNPA 527
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 13-159 6.15e-04

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: 43.11  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  13 NMDKHW--IMQYTGPMLPIHM------------EFTNILQRKR---LQTLMSVDDSVERLYNMLVETgELENTYIIYTAD 75
Cdd:cd16154  164 QQTKPWflWLAYNAPHTPFHLppaelhsrsllgDSADIEANPRpyyLAAIEAMDTEIGRLLASIDEE-ERENTIIIFIGD 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  76 HGYHiGQ-----FGLVKGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNI-DLAPTILDIAGLDTPPDVDGKSVLKLLD 149
Cdd:cd16154  243 NGTP-GQvvdlpYTRNHAKGSLYEGGINVPLIVSGAGVERANERESALVNAtDLYATIAELAGVDAAEIHDSVSFKPLLS 321

                        170
                 ....*....|
gi 578815634 150 PEKPGNRFRT 159
Cdd:cd16154  322 DVNASTRQYN 331
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
48-146 2.23e-03

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 41.63  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  48 VDDSVERLYNMLVETGeleNTYIIyTADHG-------YHIGQfglvkgksmPY------DfdirVPFFIRGPSV---EPG 111
Cdd:PRK05434 417 VDECLGRVVDAVLKVG---GTLLI-TADHGnaeqmidPETGQ---------PHtahttnP----VPFILVGGKAlrlEGG 479

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 578815634 112 SIvpqivlnIDLAPTILDIAGLDTPPDVDGKSVLK 146
Cdd:PRK05434 480 KL-------ADIAPTILDLLGLEQPAEMTGKSLIE 507
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 49-134 3.78e-03

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: 40.30  E-value: 3.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  49 DDSVERLYNMLVETGEleNTYIIYTADHGYHIGQFGlVKGKSMPYDFD--IRVPFFI--------RGPSVEPGSIVPQIV 118
Cdd:cd16017  196 DYVLSQIIERLKKKDK--DAALIYFSDHGESLGENG-LYLHGAPYAPKeqYHVPFIIwssdsykqRYPVERLRANKDRPF 272

                         90
                 ....*....|....*.
gi 578815634 119 LNIDLAPTILDIAGLD 134
Cdd:cd16017  273 SHDNLFHTLLGLLGIK 288
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 42-127 5.38e-03

GPI ethanolamine phosphate transferase 1; PIG-N; 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: 293744  Cd Length: 294  Bit Score: 39.88  E-value: 5.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815634  42 LQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGyhIGQFGLVKGKSmpyDFDIRVPFF-----IRGPSVEPGSI--- 113
Cdd:cd16020  182 LENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHG--MTDWGSHGDGS---PDETETPFIawgagIKHPTPGRGPSfsa 256

                         90       100
                 ....*....|....*....|.
gi 578815634 114 ------VPQIVLN-IDLAPTI 127
Cdd:cd16020  257 nwgglrLPRHDLDqADLAPLM 277
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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