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Conserved domains on  [gi|1958750462|ref|XP_038958169|]
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arylsulfatase L isoform X2 [Rattus norvegicus]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 581061)

alkaline phosphatase (ALP) family protein may catalyze the hydrolysis of substrates; the ALP superfamily includes alkaline phosphatases and sulfatases

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 ...
 34-386 9.32e-122

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 cd16159:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 521  Bit Score: 365.07  E-value: 9.32e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGHRVLQWA 113
Cdd:cd16159     1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 114 AGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTVSDLCHHPLNHGFHHFLGLPLGMMGDCAGAEPSEKRAGLeRR 193
Cdd:cd16159    81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSF-DP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 194 LRGAGRALAAVAVAIAALAWGRGrglapaCWAPWAAIALGAVAAIFEAGSYVVGGAVARYDCFLMRNATVTQQPLQLDHV 273
Cdd:cd16159   160 LFPLLTAFVLITALTIFLLLYLG------AVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 274 TPLLLREAKDFLR------------------------------------------------------------------- 286
Cdd:cd16159   234 TQRLTKEAISFLErnkerpfllvmsflhvhtalftskkfkgrskhgrygdnveemdwsvgqildaldelglkdntfvyft 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 287 ------------------------------------------------------------------------------RE 288
Cdd:cd16159   314 sdngghleeisvggeygggnggiyggkkmggweggirvptivrwpgvippgsvideptslmdifptvaalagaplpsdRI 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 289 IDGRDLLPLLRGETWHSAHEVLLHYCEVFLHAVRWVQRDSGQVWKAHFVTPTFDPLgsgscSGAGGAAAVCPCVGK-VEE 367
Cdd:cd16159   394 IDGRDLMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPG-----TEGCCGTLLCRCFGDsVTH 468

                         490
                  ....*....|....*....
gi 1958750462 368 HDPPLLFELTSDPGEVRPL 386
Cdd:cd16159   469 HDPPLLFDLSADPSESNPL 487
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
 34-386 9.32e-122

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: 365.07  E-value: 9.32e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGHRVLQWA 113
Cdd:cd16159     1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 114 AGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTVSDLCHHPLNHGFHHFLGLPLGMMGDCAGAEPSEKRAGLeRR 193
Cdd:cd16159    81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSF-DP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 194 LRGAGRALAAVAVAIAALAWGRGrglapaCWAPWAAIALGAVAAIFEAGSYVVGGAVARYDCFLMRNATVTQQPLQLDHV 273
Cdd:cd16159   160 LFPLLTAFVLITALTIFLLLYLG------AVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 274 TPLLLREAKDFLR------------------------------------------------------------------- 286
Cdd:cd16159   234 TQRLTKEAISFLErnkerpfllvmsflhvhtalftskkfkgrskhgrygdnveemdwsvgqildaldelglkdntfvyft 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 287 ------------------------------------------------------------------------------RE 288
Cdd:cd16159   314 sdngghleeisvggeygggnggiyggkkmggweggirvptivrwpgvippgsvideptslmdifptvaalagaplpsdRI 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 289 IDGRDLLPLLRGETWHSAHEVLLHYCEVFLHAVRWVQRDSGQVWKAHFVTPTFDPLgsgscSGAGGAAAVCPCVGK-VEE 367
Cdd:cd16159   394 IDGRDLMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPG-----TEGCCGTLLCRCFGDsVTH 468

                         490
                  ....*....|....*....
gi 1958750462 368 HDPPLLFELTSDPGEVRPL 386
Cdd:cd16159   469 HDPPLLFDLSADPSESNPL 487
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
17-148 1.16e-51

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 179.30  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  17 IVLLGLQYVDALRSPPPRPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYP 96
Cdd:COG3119     6 LLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYP 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958750462  97 IRSGMTsGNGHrvlqwaAGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLS 148
Cdd:COG3119    86 HRTGVT-DNGE------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYLT 130
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
305-458 2.41e-34

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 124.73  E-value: 2.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 305 SAHEVLLHYCEVFLHAVRWVQrdsgqvWKAHFVTPTFDPlgsgscsgaGGAAAVCPCVGKVEEHDPPLLFELTSDPGEVR 384
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDP---------PGAEGCYGSKVPVTHHDPPLLFDLERDPSEKY 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958750462 385 PLraPAKMSEAPNLTAAITseavtaamataarvrQEYDMLRPTAGHVPQQMGSLYNLWLPWLQPCCGHFPACAC 458
Cdd:pfam14707  66 PL--SPDSPEYPEVLAEIK---------------AAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
PRK13759 PRK13759
arylsulfatase; Provisional
 34-168 1.79e-16

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 81.64  E-value: 1.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGiGD-LGCYGNTSIRTPNIDRLAEDGVRLTQ-YLAAESvCTPSRAAFLTGRYPIRSGMTsgnghrvlq 111
Cdd:PRK13759    6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENaYSAVPS-CTPARAALLTGLSQWHHGRV--------- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958750462 112 waaGAGGLPPK--EITFARILQGQGYVTGLVGKWHLglscrtvsdlchHPLN--HGFHHFL 168
Cdd:PRK13759   75 ---GYGDVVPWnyKNTLPQEFRDAGYYTQCIGKMHV------------FPQRnlLGFHNVL 120
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
 34-386 9.32e-122

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: 365.07  E-value: 9.32e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGHRVLQWA 113
Cdd:cd16159     1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 114 AGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTVSDLCHHPLNHGFHHFLGLPLGMMGDCAGAEPSEKRAGLeRR 193
Cdd:cd16159    81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSF-DP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 194 LRGAGRALAAVAVAIAALAWGRGrglapaCWAPWAAIALGAVAAIFEAGSYVVGGAVARYDCFLMRNATVTQQPLQLDHV 273
Cdd:cd16159   160 LFPLLTAFVLITALTIFLLLYLG------AVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 274 TPLLLREAKDFLR------------------------------------------------------------------- 286
Cdd:cd16159   234 TQRLTKEAISFLErnkerpfllvmsflhvhtalftskkfkgrskhgrygdnveemdwsvgqildaldelglkdntfvyft 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 287 ------------------------------------------------------------------------------RE 288
Cdd:cd16159   314 sdngghleeisvggeygggnggiyggkkmggweggirvptivrwpgvippgsvideptslmdifptvaalagaplpsdRI 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 289 IDGRDLLPLLRGETWHSAHEVLLHYCEVFLHAVRWVQRDSGQVWKAHFVTPTFDPLgsgscSGAGGAAAVCPCVGK-VEE 367
Cdd:cd16159   394 IDGRDLMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPG-----TEGCCGTLLCRCFGDsVTH 468

                         490
                  ....*....|....*....
gi 1958750462 368 HDPPLLFELTSDPGEVRPL 386
Cdd:cd16159   469 HDPPLLFDLSADPSESNPL 487
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 34-171 2.41e-66

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: 218.20  E-value: 2.41e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGHrvlqwA 113
Cdd:cd16026     1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGP-----P 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750462 114 AGAGGLPPKEITFARILQGQGYVTGLVGKWHLGlscrtvsDL-CHHPLNHGFHHFLGLP 171
Cdd:cd16026    76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIP 127
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
17-148 1.16e-51

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 179.30  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  17 IVLLGLQYVDALRSPPPRPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYP 96
Cdd:COG3119     6 LLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYP 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958750462  97 IRSGMTsGNGHrvlqwaAGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLS 148
Cdd:COG3119    86 HRTGVT-DNGE------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHLYLT 130
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
 34-290 6.13e-50

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: 176.08  E-value: 6.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGIGDLGCYGN-TSIRTPnIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGhRVLQW 112
Cdd:cd16160     1 KPNIVLFFADDMGYGDLASYGHpTQERGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTR-VFLPW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 113 aaGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTVSDLCHHPLNHGFhHFLG--LPLGMMGDCAgaepsekragl 190
Cdd:cd16160    79 --DIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGF-DFVGtnLPFTNSWACD----------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 191 errlrgagralaavavaiaalAWGRgrglapacwapwaaialgavaaifeagsYVVGGAVARydCFLMRNATVTQQPLQL 270
Cdd:cd16160   145 ---------------------DTGR----------------------------HVDFPDRSA--CFLYYNDTIVEQPIQH 173

                         250       260
                  ....*....|....*....|
gi 1958750462 271 DHVTPLLLREAKDFLRREID 290
Cdd:cd16160   174 EHLTETLVGDAKSFIEDNQE 193
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 35-166 7.78e-48

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: 170.03  E-value: 7.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTS-GNGHRVLQWA 113
Cdd:cd16144     1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDvIPGRRGPPDN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750462 114 A------GAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRtvsdlcHHPLNHGFHH 166
Cdd:cd16144    81 TklipppSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGG------YGPEDQGFDV 133
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 35-144 6.26e-47

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: 162.22  E-value: 6.26e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRsgmtsgngHRVLQWAA 114
Cdd:cd16022     1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHR--------HGVRGNVG 72

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958750462 115 GAGGLPPKEITFARILQGQGYVTGLVGKWH 144
Cdd:cd16022    73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH 102
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 35-172 1.58e-46

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: 165.01  E-value: 1.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIR---TPNIDRLAEDGVRLTQYLAaESVCTPSRAAFLTGRYPIRSGMTSgnghrvLQ 111
Cdd:cd16142     1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYV-EPSCTPGRAAFITGRHPIRTGLTT------VG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750462 112 WAAGAGGLPPKEITFARILQGQGYVTGLVGKWHLGlscrtvsDLCHH-PLNHGFHHFLGLPL 172
Cdd:cd16142    74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG-------DEDGRlPTDHGFDEFYGNLY 128
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 35-171 2.78e-45

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: 162.37  E-value: 2.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTS-IRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNghrvlQWA 113
Cdd:cd16143     1 PNIVIILADDLGYGDISCYNPDSkIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGV-----LGG 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958750462 114 AGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTVSDLCHH----------------PLNHGFHHFLGLP 171
Cdd:cd16143    76 FSPPLIEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIP 149
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
 35-171 3.38e-45

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: 164.16  E-value: 3.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGnghrVLQwAA 114
Cdd:cd16158     2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPG----VFY-PG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958750462 115 GAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTVsdlcHHPLNHGFHHFLGLP 171
Cdd:cd16158    77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIP 129
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 35-169 4.22e-45

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: 162.38  E-value: 4.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTgrypirsGMTSGNGH-RVLQWA 113
Cdd:cd16145     1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLT-------GLHTGHTRvRGNSEP 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958750462 114 AGAGGLPPKEITFARILQGQGYVTGLVGKWHLGlsCRTVSDlchHPLNHGFHHFLG 169
Cdd:cd16145    74 GGQDPLPPDDVTLAEVLKKAGYATAAFGKWGLG--GPGTPG---HPTKQGFDYFYG 124
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
 35-173 1.09e-43

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: 158.48  E-value: 1.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAeSVCTPSRAAFLTGRYPIRSGM--TSGNGHRvlqw 112
Cdd:cd16146     1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVwhTILGRER---- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958750462 113 aagaggLPPKEITFARILQGQGYVTGLVGKWHLGLSCRtvsdlcHHPLNHGFHHFLGLPLG 173
Cdd:cd16146    76 ------MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYP------YRPQDRGFDEVLGHGGG 124
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
 35-174 2.93e-42

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: 154.25  E-value: 2.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAeSVCTPSRAAFLTGRYPIRSGMtsgnGHRVLqWAA 114
Cdd:cd16029     1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGM----QHGVI-LAG 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 115 GAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTvsdlcHHPLNHGFHHFLGLPLGM 174
Cdd:cd16029    75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLGFYTWE-----YTPTNRGFDSFYGYYGGA 129
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
 34-171 2.35e-41

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: 151.47  E-value: 2.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGIGDLGCYGN-TSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGhrvlqw 112
Cdd:cd16161     1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFL------ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750462 113 AAGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRtvsdlcHHPLNHGFHHFLGLP 171
Cdd:cd16161    75 PTSVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQREA------YLPNSRGFDYYFGIP 127
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 35-168 2.29e-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: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 145.82  E-value: 2.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQ-YlaAESVCTPSRAAFLTGRYPIRSGmtsgnghrvlqwa 113
Cdd:cd16151     1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNaY--AQPLCTPSRVQLMTGKYNFRNY------------- 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958750462 114 AGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLScRTVSDlchHPLNHGFHHFL 168
Cdd:cd16151    66 VVFGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGG-RGDGD---YPHEFGFDEYC 116
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
 34-146 5.24e-39

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: 145.66  E-value: 5.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGIGDLGCYGNtSIRTPNIDRLAEDGVRLTQYLAAeSVCTPSRAAFLTGRYPIRSGMtsGNghrVLQWA 113
Cdd:cd16025     2 RPNILLILADDLGFSDLGCFGG-EIPTPNLDALAAEGLRFTNFHTT-ALCSPTRAALLTGRNHHQVGM--GT---MAELA 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958750462 114 AGAGG----LPPKEITFARILQGQGYVTGLVGKWHLG 146
Cdd:cd16025    75 TGKPGyegyLPDSAATIAEVLKDAGYHTYMSGKWHLG 111
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 34-170 3.18e-38

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 143.48  E-value: 3.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTsGNGHRvlqwa 113
Cdd:cd16034     1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF-GNDVP----- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958750462 114 agaggLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTVSDLCHH----PLNHGFHHFLGL 170
Cdd:cd16034    75 -----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY 130
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 34-171 2.14e-37

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: 142.61  E-value: 2.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGHrvlqwA 113
Cdd:cd16157     1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAH-----A 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958750462 114 AGA-------GGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRtvsdlcHHPLNHGFHHFLGLP 171
Cdd:cd16157    76 RNAytpqnivGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP 134
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 35-146 2.97e-35

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: 134.56  E-value: 2.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIgDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTsgnGHRVLQWAa 114
Cdd:cd16027     1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAH---GLRSRGFP- 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958750462 115 gaggLPPKEITFARILQGQGYVTGLVGKWHLG 146
Cdd:cd16027    76 ----LPDGVKTLPELLREAGYYTGLIGKTHYN 103
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
 34-171 5.63e-35

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: 134.96  E-value: 5.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGHrvlqwa 113
Cdd:cd16031     2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP------ 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958750462 114 agagGLPPKEITFARILQGQGYVTGLVGKWHLGLScrtvsdlcHHPLNHGFHHFLGLP 171
Cdd:cd16031    76 ----LFDASQPTYPKLLRKAGYQTAFIGKWHLGSG--------GDLPPPGFDYWVSFP 121
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 35-146 2.00e-34

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: 129.28  E-value: 2.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPirsgmtsgNGHRVLQW-- 112
Cdd:cd16149     1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMP--------SQHGIHDWiv 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958750462 113 ------AAGAGGLPPKEITFARILQGQGYVTGLVGKWHLG 146
Cdd:cd16149    73 egshgkTKKPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG 112
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
305-458 2.41e-34

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 124.73  E-value: 2.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462 305 SAHEVLLHYCEVFLHAVRWVQrdsgqvWKAHFVTPTFDPlgsgscsgaGGAAAVCPCVGKVEEHDPPLLFELTSDPGEVR 384
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDP---------PGAEGCYGSKVPVTHHDPPLLFDLERDPSEKY 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958750462 385 PLraPAKMSEAPNLTAAITseavtaamataarvrQEYDMLRPTAGHVPQQMGSLYNLWLPWLQPCCGHFPACAC 458
Cdd:pfam14707  66 PL--SPDSPEYPEVLAEIK---------------AAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
Sulfatase pfam00884
Sulfatase;
35-173 3.32e-33

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 127.15  E-value: 3.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGhrvlqwaa 114
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750462 115 gaGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTvsdlchHPLNHGFHHFLGLPLG 173
Cdd:pfam00884  73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQ------SPCNLGFDKFFGRNTG 123
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 35-168 1.71e-28

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: 116.55  E-value: 1.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSgNGHRVLqwaA 114
Cdd:cd16033     1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLN-NVENAG---A 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958750462 115 GAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRtvsdlchhPLNHGFHHFL 168
Cdd:cd16033    77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEET--------PLDYGFDEYL 122
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 35-145 1.09e-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: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 102.70  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPirsgmtSGNGHRVLQWAa 114
Cdd:cd16150     1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYP------HVNGHRTLHHL- 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958750462 115 gaggLPPKEITFARILQGQGYVTGLVGKWHL 145
Cdd:cd16150    74 ----LRPDEPNLLKTLKDAGYHVAWAGKNDD 100
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 34-145 3.93e-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: 100.38  E-value: 3.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMtsgngHRvlqwa 113
Cdd:cd16152     1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR----- 70

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958750462 114 aGAGGLPPKEITFARILQGQGYVTGLVGKWHL 145
Cdd:cd16152    71 -NGIPLPADEKTLAHYFRDAGYETGYVGKWHL 101
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 34-146 1.74e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 98.41  E-value: 1.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQ-YLA---AESVCTPSRAAFLTGRYPIRSGMtsgnghrv 109
Cdd:cd16155     2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNMggwSGAVCVPSRAMLMTGRTLFHAPE-------- 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958750462 110 lqwaAGAGGLPPKEITFARILQGQGYVTGLVGKWHLG 146
Cdd:cd16155    74 ----GGKAAIPSDDKTWPETFKKAGYRTFATGKWHNG 106
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 35-144 9.53e-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: 95.69  E-value: 9.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPirsgmtSGNGHrvlqWaA 114
Cdd:cd16037     1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYV------HETGV----W-D 69

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958750462 115 GAGGLPPKEITFARILQGQGYVTGLVGKWH 144
Cdd:cd16037    70 NADPYDGDVPSWGHALRAAGYETVLIGKLH 99
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 34-142 9.85e-22

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: 97.26  E-value: 9.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGiGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTsGNGHRvlqWA 113
Cdd:cd16030     2 KPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVY-DNNSY---FR 76

                          90       100
                  ....*....|....*....|....*....
gi 1958750462 114 AGAgglpPKEITFARILQGQGYVTGLVGK 142
Cdd:cd16030    77 KVA----PDAVTLPQYFKENGYTTAGVGK 101
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 35-145 1.99e-21

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: 96.68  E-value: 1.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNghrvlqwaa 114
Cdd:cd16156     1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNC--------- 71

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958750462 115 gaggLPPKE--ITFARILQGQGYVTGLVGKWHL 145
Cdd:cd16156    72 ----MALGDnvKTIGQRLSDNGIHTAYIGKWHL 100
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 35-165 2.25e-20

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: 90.69  E-value: 2.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLgIGD-LGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRsgmtsgnghrvlqWA 113
Cdd:cd16148     1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFY-------------HG 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958750462 114 AGAGGLPPKEITFARILQGQGYVTGLvgkwhlglscrtVSDLCHHPLNHGFH 165
Cdd:cd16148    67 VWGGPLEPDDPTLAEILRKAGYYTAA------------VSSNPHLFGGPGFD 106
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 34-146 6.28e-20

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: 89.74  E-value: 6.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGIGDLGCYGN----------TSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTs 103
Cdd:cd16153     1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958750462 104 GNG--HRVLQWAagagglppkEITFARILQGQGYVTGLVGKWHLG 146
Cdd:cd16153    80 GFEaaHPALDHG---------LPTFPEVLKKAGYQTASFGKSHLE 115
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
 35-144 8.03e-20

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: 89.95  E-value: 8.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSgnghrvlqwaa 114
Cdd:cd16032     1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYD----------- 69

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958750462 115 GAGGLPPKEITFARILQGQGYVTGLVGKWH 144
Cdd:cd16032    70 NAAEFPADIPTFAHYLRAAGYRTALSGKMH 99
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 35-146 1.11e-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: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 90.49  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYG-NTSI-RTPNIDRLAEDGVRLTQYLAAeSVCTPSRAAFLTGRYPIRSGMTsgnghrvlqW 112
Cdd:cd16154     1 PNILLIIADDQGLDSSAQYSlSSDLpVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVL---------A 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958750462 113 AAGAGGLPPKEITFARILQG--QGYVTGLVGKWHLG 146
Cdd:cd16154    71 VPDELLLSEETLLQLLIKDAttAGYSSAVIGKWHLG 106
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
 35-144 5.19e-17

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: 83.08  E-value: 5.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIrsgmtsgnGHRVLQwaa 114
Cdd:cd16028     1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLM--------NHRSVW--- 69

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958750462 115 GAGGLPPKEITFARILQGQGYVTGLVGKWH 144
Cdd:cd16028    70 NGTPLDARHLTLALELRKAGYDPALFGYTD 99
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 35-141 1.23e-16

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: 79.00  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLtQYLAAESVC--TPSRAAFLTGRYPIRSGMTsGNGHRVLQW 112
Cdd:cd00016     1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYT-GNGSADPEL 78

                          90       100
                  ....*....|....*....|....*....
gi 1958750462 113 AAGAGGLPPKEITFARILQGQGYVTGLVG 141
Cdd:cd00016    79 PSRAAGKDEDGPTIPELLKQAGYRTGVIG 107
PRK13759 PRK13759
arylsulfatase; Provisional
 34-168 1.79e-16

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 81.64  E-value: 1.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLGiGD-LGCYGNTSIRTPNIDRLAEDGVRLTQ-YLAAESvCTPSRAAFLTGRYPIRSGMTsgnghrvlq 111
Cdd:PRK13759    6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENaYSAVPS-CTPARAALLTGLSQWHHGRV--------- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958750462 112 waaGAGGLPPK--EITFARILQGQGYVTGLVGKWHLglscrtvsdlchHPLN--HGFHHFL 168
Cdd:PRK13759   75 ---GYGDVVPWnyKNTLPQEFRDAGYYTQCIGKMHV------------FPQRnlLGFHNVL 120
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 34-170 4.63e-16

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: 79.52  E-value: 4.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  34 RPNFLIIMADDLgigDLGcYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTS----GNGHRV 109
Cdd:cd16147     1 RPNIVLILTDDQ---DVE-LGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNnsppGGGYPK 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750462 110 LQWAagagGLPPKeiTFARILQGQGYVTGLVGKWhlgL-SCRTVSDLCHHPLnhGFHHFLGL 170
Cdd:cd16147    77 FWQN----GLERS--TLPVWLQEAGYRTAYAGKY---LnGYGVPGGVSYVPP--GWDEWDGL 127
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 35-145 1.67e-13

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: 71.08  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADD--------LGIGDLGCygntsirtPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNG 106
Cdd:cd16035     1 PNILLILTDQerypppwpAGWAALNL--------PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLG 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958750462 107 hrvlqwAAGAGGLPPKEITFARILQGQGYVTGLVGKWHL 145
Cdd:cd16035    73 ------SPMQPLLSPDVPTLGHMLRAAGYYTAYKGKWHL 105
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
 35-142 3.12e-05

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: 46.00  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  35 PNFLIIMADDLGiGDLGCY-GNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPirsgmtsgngHRVLQWa 113
Cdd:cd16171     1 PNVVMVMSDSFD-GRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT----------HLTESW- 68

                          90       100
                  ....*....|....*....|....*....
gi 1958750462 114 AGAGGLPPKEITFARILQGQGYVTGLVGK 142
Cdd:cd16171    69 NNYKGLDPNYPTWMDRLEKHGYHTQKYGK 97
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 23-137 7.42e-03

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 38.87  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750462  23 QYVDALRSPPP------RPNFLIIMADDLG---IGDLGCYGNTsirTPNIDRLAEDGVRLTQYLAaeSVCTPSRA--AFL 91
Cdd:COG1368   217 KYLKSNRPTPNpfgpakKPNVVVILLESFSdffIGALGNGKDV---TPFLDSLAKESLYFGNFYS--QGGRTSRGefAVL 291

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958750462  92 TGRYPIRSG--MTSGNGHRVlqwaagagglppkeITFARILQGQGYVT 137
Cdd:COG1368   292 TGLPPLPGGspYKRPGQNNF--------------PSLPSILKKQGYET 325
 
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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