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Conserved domains on  [gi|1864524949|ref|XP_035145522|]
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arylsulfatase L isoform X7 [Callithrix jacchus]

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 ...
21-518 0e+00

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: 693.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTGASGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16159    27 TPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTASSGGLPPNETTFAEVLKQQGYSTAL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGLNCESAGDHCHHPLHHGFDYFYGMPLSMTGDCAHweLSEKRVDLEQKLNFLFQVLALVTLTLAAGKFMHLISI 180
Cdd:cd16159   107 IGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGD--GSNGEYDLSFDPLFPLLTAFVLITALTIFLLLYLGAV 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 SWMPVIwsALLAVFLLTTSYFAGALIVHAD--CFLMRNHTITEQPMRFQRVTPLILQEVKSFLKRNKLGPFLLLVSFLHV 258
Cdd:cd16159   185 SKRFFV--FLLILSLLFISLFFLLLITNRYfnCILMRNHEVVEQPMSLENLTQRLTKEAISFLERNKERPFLLVMSFLHV 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 259 HIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFANSQYGGWNGIYKGGKGM 338
Cdd:cd16159   263 HTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLEEISVGGEYGGGNGGIYGGKKM 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 339 GGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMHYCERF 418
Cdd:cd16159   343 GGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLMPLLTGQEKRSPHEFLFHYCGAE 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 419 LHAARWHQRDRGTLWKVHFVTPVFQPEGAGaCYGRKVCPCSGEKVVHHDPPLLFDLSRDPSEAHVLTPASEPlFYHVMER 498
Cdd:cd16159   423 LHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDLSADPSESNPLDPTDEP-YQEIIKK 500
                         490       500
                  ....*....|....*....|
gi 1864524949 499 VQQAVWEHQQTLSPVALQLD 518
Cdd:cd16159   501 ILEAVAEHQSSIEPVESQLS 520
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
21-518 0e+00

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: 693.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTGASGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16159    27 TPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTASSGGLPPNETTFAEVLKQQGYSTAL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGLNCESAGDHCHHPLHHGFDYFYGMPLSMTGDCAHweLSEKRVDLEQKLNFLFQVLALVTLTLAAGKFMHLISI 180
Cdd:cd16159   107 IGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGD--GSNGEYDLSFDPLFPLLTAFVLITALTIFLLLYLGAV 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 SWMPVIwsALLAVFLLTTSYFAGALIVHAD--CFLMRNHTITEQPMRFQRVTPLILQEVKSFLKRNKLGPFLLLVSFLHV 258
Cdd:cd16159   185 SKRFFV--FLLILSLLFISLFFLLLITNRYfnCILMRNHEVVEQPMSLENLTQRLTKEAISFLERNKERPFLLVMSFLHV 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 259 HIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFANSQYGGWNGIYKGGKGM 338
Cdd:cd16159   263 HTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLEEISVGGEYGGGNGGIYGGKKM 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 339 GGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMHYCERF 418
Cdd:cd16159   343 GGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLMPLLTGQEKRSPHEFLFHYCGAE 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 419 LHAARWHQRDRGTLWKVHFVTPVFQPEGAGaCYGRKVCPCSGEKVVHHDPPLLFDLSRDPSEAHVLTPASEPlFYHVMER 498
Cdd:cd16159   423 LHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDLSADPSESNPLDPTDEP-YQEIIKK 500
                         490       500
                  ....*....|....*....|
gi 1864524949 499 VQQAVWEHQQTLSPVALQLD 518
Cdd:cd16159   501 ILEAVAEHQSSIEPVESQLS 520
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
21-482 9.51e-72

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 234.39  E-value: 9.51e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGyrvlqwtGASGGLPTNETTFAKILKEKGYATGL 100
Cdd:COG3119    49 TPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTAL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGLncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisi 180
Cdd:COG3119   122 FGKWHLYL------------------------------------------------------------------------ 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 swmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvTPLILQEVKSFLKRNKLG--PFLLLVSFLHV 258
Cdd:COG3119   130 -------------------------------------------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAP 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 259 HIPLITTKNFLGK-----------------------SAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGS 315
Cdd:COG3119   161 HAPYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS 240
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 316 LENQ-FA---NSQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvI 390
Cdd:COG3119   241 LGEHgLRggkGTLYeGG-----------------IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--L 301
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 391 DGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRdrgtlWKVHFvtpvfqpegagaCYGRKvcpcsgekvvhhDPPL 470
Cdd:COG3119   302 DGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTGR-----WKLIR------------YYDDD------------GPWE 352
                         490
                  ....*....|..
gi 1864524949 471 LFDLSRDPSEAH 482
Cdd:COG3119   353 LYDLKNDPGETN 364
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
406-540 3.28e-56

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 184.44  E-value: 3.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 406 SDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVTPVFQPEGAGACYGRKVCpcsgekVVHHDPPLLFDLSRDPSEAHVLT 485
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1864524949 486 PASePLFYHVMERVQQAVWEHQQTLSPVALQLDSLGNLWRPWLQPCCGPFPLCWC 540
Cdd:pfam14707  69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
PRK13759 PRK13759
arylsulfatase; Provisional
10-402 1.06e-26

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 113.23  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  10 RGDMLHLQ-HSW--TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvGYrvlqwtgASGGLPTNETT 86
Cdd:PRK13759   18 RGDCLGCNgNKAveTPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY-------GDVVPWNYKNT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  87 FAKILKEKGYATGLIGKWHLglncesagdhchHPLH--HGFDYfygmplSMTGDcahWELSEKRVDLEQKLNFLFQVLAL 164
Cdd:PRK13759   88 LPQEFRDAGYYTQCIGKMHV------------FPQRnlLGFHN------VLLHD---GYLHSGRNEDKSQFDFVSDYLAW 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 165 VTLTlAAGKFMHLISISWMPVIWSAllavfllttsyfagalivhadcflmRNHTITEQpmrfQRVTPLILQEVKSFLKR- 243
Cdd:PRK13759  147 LREK-APGKDPDLTDIGWDCNSWVA-------------------------RPWDLEER----LHPTNWVGSESIEFLRRr 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 244 NKLGPFLLLVSFLHVHIPLITTKNFL-------------------------GKSAHGLYGD---------------NVEE 283
Cdd:PRK13759  197 DPTKPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeeyarraraayygLITH 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 284 MDWMVGQILDALDTEGLTNSTLIYFASDHGGSL--ENQFANS-QYGGwngiykggkgmggwegGIRVPGIFRWPG---VL 357
Cdd:PRK13759  277 IDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLgdHYLFRKGyPYEG----------------SAHIPFIIYDPGgllAG 340
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1864524949 358 PAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGT 402
Cdd:PRK13759  341 NRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQ 383
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
21-518 0e+00

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: 693.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTGASGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16159    27 TPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTASSGGLPPNETTFAEVLKQQGYSTAL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGLNCESAGDHCHHPLHHGFDYFYGMPLSMTGDCAHweLSEKRVDLEQKLNFLFQVLALVTLTLAAGKFMHLISI 180
Cdd:cd16159   107 IGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGD--GSNGEYDLSFDPLFPLLTAFVLITALTIFLLLYLGAV 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 SWMPVIwsALLAVFLLTTSYFAGALIVHAD--CFLMRNHTITEQPMRFQRVTPLILQEVKSFLKRNKLGPFLLLVSFLHV 258
Cdd:cd16159   185 SKRFFV--FLLILSLLFISLFFLLLITNRYfnCILMRNHEVVEQPMSLENLTQRLTKEAISFLERNKERPFLLVMSFLHV 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 259 HIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFANSQYGGWNGIYKGGKGM 338
Cdd:cd16159   263 HTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLEEISVGGEYGGGNGGIYGGKKM 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 339 GGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSDHEFLMHYCERF 418
Cdd:cd16159   343 GGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLMPLLTGQEKRSPHEFLFHYCGAE 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 419 LHAARWHQRDRGTLWKVHFVTPVFQPEGAGaCYGRKVCPCSGEKVVHHDPPLLFDLSRDPSEAHVLTPASEPlFYHVMER 498
Cdd:cd16159   423 LHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDLSADPSESNPLDPTDEP-YQEIIKK 500
                         490       500
                  ....*....|....*....|
gi 1864524949 499 VQQAVWEHQQTLSPVALQLD 518
Cdd:cd16159   501 ILEAVAEHQSSIEPVESQLS 520
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
21-485 9.83e-134

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: 394.24  E-value: 9.83e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgYRVLQWTGASGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16026    27 TPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPPGSKGGLPPDEITIAEVLKKAGYRTAL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGlncesagDH-CHHPLHHGFDYFYGMPLSMTGDCAHWELSEKRVDLeqklnflfqvlalvtltlaagkfmhlis 179
Cdd:cd16026   102 VGKWHLG-------HQpEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPL---------------------------- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 180 iswmpviwsallavfllttsyfagalivhadCFLMRNHTITEQPMRFQRVTPLILQEVKSFLKRNKLGPFLLLVSFLHVH 259
Cdd:cd16026   147 -------------------------------PPLMENEEVIEQPADQSSLTQRYTDEAVDFIERNKDQPFFLYLAHTMPH 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 260 IPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFAN-----------SQY-GG 327
Cdd:cd16026   196 VPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHGgsagplrggkgTTWeGG 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 328 wngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLGTAQHSD 407
Cdd:cd16026   276 -----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPP 338
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864524949 408 HEFLMHYCERFLHAARWHQrdrgtlWKVHFVTPVFQPEGAGacygrkvcpcsGEKVVHHDPPLLFDLSRDPSEAHVLT 485
Cdd:cd16026   339 HPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDPG-----------GLDPTKLEPPLLYDLEEDPGETYNVA 399
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
11-503 3.07e-119

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: 359.05  E-value: 3.07e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  11 GDML---HLQHSWTPnIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSsvGYRV-LQWTgaSGGLPTNETT 86
Cdd:cd16160    15 GDLAsygHPTQERGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG--GTRVfLPWD--IGGLPKTEVT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  87 FAKILKEKGYATGLIGKWHLGLNCESAGDHCHHPLHHGFDyFYGMPLSMTGdcaHWELSekrvdleqklnflfqvlalvt 166
Cdd:cd16160    90 MAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGTNLPFTN---SWACD--------------------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 167 ltlaagkfmhlisiswmpviwsallavfllTTSYFagalIVHAD---CFLMRNHTITEQPMRFQRVTPLILQEVKSFLKR 243
Cdd:cd16160   145 ------------------------------DTGRH----VDFPDrsaCFLYYNDTIVEQPIQHEHLTETLVGDAKSFIED 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 244 NKLGPFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG---------- 313
Cdd:cd16160   191 NQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGphveyclegg 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 314 --GSLENQFANSQYGGwngiykggkgmggweggIRVPGIFRWPGVLPaGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVID 391
Cdd:cd16160   271 stGGLKGGKGNSWEGG-----------------IRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTFVDLAGGTLPTDRIYD 332
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 392 GRDLLPLLLGTAQHSDHEFLMHYCERfLHAARWHQrdrgtlWKVHFVT---PVFQPEGAGACYGRKVCP------CSGEK 462
Cdd:cd16160   333 GLSITDLLLGEADSPHDDILYYCCSR-LMAVRYGS------YKIHFKTqplPSQESLDPNCDGGGPLSDyivcydCEDEC 405
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 1864524949 463 VVHHDPPLLFDLSRDPSEAHVLTPAsepLFYHVMERVQQAV 503
Cdd:cd16160   406 VTKHNPPLIFDVEKDPGEQYPLQPS---VYEHMLEAVEKLI 443
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
19-540 3.59e-83

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: 267.00  E-value: 3.59e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  19 SWTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYrvlqwTGASGGLPTNETTFAKILKEKGYAT 98
Cdd:cd16158    25 SSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFY-----PGSRGGLPLNETTIAEVLKTVGYQT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  99 GLIGKWHLGLNCESAgdhcHHPLHHGFDYFYGMPLSMT-GDCAHwelsekrvdleqklnflfqvlalvtltlaagkfmhl 177
Cdd:cd16158   100 AMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSHDqGPCQN------------------------------------ 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 178 isiswmpviwsalLAVFLLTTSYFAGALIVHADCFLMRNHTITEQPMRFQRVTPLILQEVKSFL----KRNKlgPFLLLV 253
Cdd:cd16158   140 -------------LTCFPPNIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIadnaKEGK--PFFLYY 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 254 SFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQfansQYGGwNGIYK 333
Cdd:cd16158   205 ASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRK----SRGG-NAGLL 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 334 GGKGMGGWEGGIRVPGIFRWPGVLPAGRVIgEPTSLMDVFPTVVQLAGGEVPqDRVIDGRDLLPLLLGTAQHSDHEFLMH 413
Cdd:cd16158   280 KCGKGTTYEGGVREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYY 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 414 YC----ERFLHAARWHQrdrgtlWKVHFVT---PVFQPEGAGACYGRKvcpcsgeKVVHHDPPLLFDLSRDPSEAHVLTP 486
Cdd:cd16158   358 PTspdpDKGVFAVRWGK------YKAHFYTqgaAHSGTTPDKDCHPSA-------ELTSHDPPLLFDLSQDPSENYNLLG 424
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1864524949 487 ASEplFYHVMERVQQAVWEHQQTLSPVALQLDSLGNlwrPWLQPC----CGPFPLCWC 540
Cdd:cd16158   425 LPE--YNQVLKQIQQVKERFEASMKFGESEINKGED---PALEPCckpgCTPKPSCCQ 477
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
21-485 2.67e-80

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: 256.63  E-value: 2.67e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRvlqwtgASGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16161    28 TPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT------SVGGLPLNETTLAEVLRQAGYATGM 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGLNcesagdHCHHPLHHGFDYFYGMPLSMTGdcahwELSEKRVDleqklnflfqvlalvtltlaagkfmhlisi 180
Cdd:cd16161   102 IGKWHLGQR------EAYLPNSRGFDYYFGIPFSHDS-----SLADRYAQ------------------------------ 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 swmpviwsallavfllttsyFAGAlivhadcFLMRNHTITEqpmrfqrvtplilqevksflkrnklgPFLLLVSFLHVHI 260
Cdd:cd16161   141 --------------------FATD-------FIQRASAKDR--------------------------PFFLYAALAHVHV 167
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 261 PLITTKNFLGKSAH-GLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG---------GSLENQFANSQyGGWNG 330
Cdd:cd16161   168 PLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcelaVGPGTGDWQGN-LGGSV 246
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 331 IYKGGKGMGgweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLGTAQhSDHEF 410
Cdd:cd16161   247 AKASTWEGG-----HREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSK-TGHRC 320
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 411 LMHYCE-----RFLHAARWHQrdrgtlWKVHFVTpvfqpEGAGACYGRKvCPcsgekVVHHDPPLLFDLSRDPSEAHVLT 485
Cdd:cd16161   321 LFHPNSgaagaGALSAVRCGD------YKAHYAT-----GGALACCGST-GP-----KLYHDPPLLFDLEVDPAESFPLT 383
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
21-480 7.94e-80

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: 254.77  E-value: 7.94e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvSSVGyrvlqWTGASGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16142    29 TPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGL-TTVG-----LPGSPGGLPPWEPTLAELLKDAGYATAQ 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGlncESAGdhcHHPLHHGFDYFYGMPLsmtgdcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisi 180
Cdd:cd16142   102 FGKWHLG---DEDG---RLPTDHGFDEFYGNLY----------------------------------------------- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 swmpviwsallavfllttsyfagalivhadcflmrnHTITEQpmrfqrvtplILQEVKSFLKRNKLG--PFLLLVSFLHV 258
Cdd:cd16142   129 ------------------------------------HTIDEE----------IVDKAIDFIKRNAKAdkPFFLYVNFTKM 162
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 259 HIPLITTKNFLGKS-AHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLeNQFANSQY------------ 325
Cdd:cd16142   163 HFPTLPSPEFEGKSsGKGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGPEQ-DVWPDGGYtpfrgekgttwe 241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 326 GGWngiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVP------QDRVIDGRDLLPLL 399
Cdd:cd16142   242 GGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRHIDGVDQSPFL 304
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 400 LGTAQHSDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVtpVFQPEGAGACYGRKVCPCsgekvvhhdpPLLFDLSRDPS 479
Cdd:cd16142   305 LGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTGEPFYVLTF----------PLIFNLRRDPK 366

                  .
gi 1864524949 480 E 480
Cdd:cd16142   367 E 367
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
21-482 7.11e-73

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: 237.48  E-value: 7.11e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVgyrvlqWTGASGGL-PTNETTFAKILKEKGYATG 99
Cdd:cd16143    27 TPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGV------LGGFSPPLiEPDRVTLAKMLKQAGYRTA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 100 LIGKWHLGLN-CESAGDHCHH---------------PLHHGFDYFYGMPLSmtgdcahwelsekrvdleqklnflfqvla 163
Cdd:cd16143   101 MVGKWHLGLDwKKKDGKKAATgtgkdvdyskpikggPLDHGFDYYFGIPAS----------------------------- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 164 lvtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqRVTPLILQEVKSFLKR 243
Cdd:cd16143   152 ----------------------------------------------------------------EVLPTLTDKAVEFIDQ 167
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 244 NKLG--PFLLLVSFLHVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQF- 320
Cdd:cd16143   168 HAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPYADYk 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 321 --------ANSQY---------GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGE 383
Cdd:cd16143   248 elekfghdPSGPLrgmkadiyeGG-----------------HRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQK 310
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 384 VPQDRVIDGRDLLPLLLGTAQHSDHEFLMHycerflHAARWHQRDRGTLWKVhfvtpVFQPEGAGACYGRKvcpcsgeKV 463
Cdd:cd16143   311 LPDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSFAIRKGDWKL-----IDGTGSGGFSYPRG-------KE 372
                         490       500
                  ....*....|....*....|
gi 1864524949 464 VHHDPP-LLFDLSRDPSEAH 482
Cdd:cd16143   373 KLGLPPgQLYNLSTDPGESN 392
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
21-518 3.04e-72

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: 238.14  E-value: 3.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTGAS--GGLPTNETTFAKILKEKGYAT 98
Cdd:cd16157    27 TPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTPQNivGGIPDSEILLPELLKKAGYRN 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  99 GLIGKWHLGLNCEsagdhcHHPLHHGFDYFYGMPlsmtgDCaHWelseKRVDLEQKLNflfqvLALVTLTLAAGKFMHLI 178
Cdd:cd16157   107 KIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NC-HF----GPYDNKAYPN-----IPVYRDWEMIGRYYEEF 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 179 SIswmpviwsallavfllttsyfagalivhadcflmrNHTITEQpmrfqRVTPLILQEVKSFLKR--NKLGPFLLLVSFL 256
Cdd:cd16157   166 KI-----------------------------------DKKTGES-----NLTQIYLQEALEFIEKqhDAQKPFFLYWAPD 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 257 HVHIPLITTKNFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLenqFANSQYGGWNGIYKGGK 336
Cdd:cd16157   206 ATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAAL---ISAPEQGGSNGPFLCGK 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 337 GMGGWEGgIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLgtAQHSDHEFLMHYCE 416
Cdd:cd16157   283 QTTFEGG-MREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLL--NGKEKDRPIFYYRG 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 417 RFLHAARWHQrdrgtlWKVHFVT----PVFQPEGAGACYGRKVCPCSGEKVVHH-DPPLLFDLSRDPSEAHVLTPASePL 491
Cdd:cd16157   360 DELMAVRLGQ------YKAHFWTwsnsWEEFRKGINFCPGQNVPGVTTHNQTDHtKLPLLFHLGRDPGEKYPISFKS-AE 432
                         490       500
                  ....*....|....*....|....*..
gi 1864524949 492 FYHVMERVQQAVWEHQQTLSPVALQLD 518
Cdd:cd16157   433 YKQAMPRISKVVQQHQKTLVPGEPQLN 459
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
21-482 3.26e-72

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: 236.67  E-value: 3.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGM--VSSVGYRVLQWTGA-----SGGLPTNETTFAKILKE 93
Cdd:cd16144    26 TPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdVIPGRRGPPDNTKLipppsTTRLPLEEVTIAEALKD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  94 KGYATGLIGKWHLGlncesaGDHCHHPLHHGFDYFYGmplsmtGDCAHwelsekrvdleqklnflfqvlalvtltlaAGK 173
Cdd:cd16144   106 AGYATAHFGKWHLG------GEGGYGPEDQGFDVNIG------GTGNG-----------------------------GPP 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 174 fmhlisiswmpviwsallavfllttSYFAGALIVHADCFLmrnhtITEQPMRFQRVTplilQEVKSFLKRNKLGPFLLLV 253
Cdd:cd16144   145 -------------------------SYYFPPGKPNPDLED-----GPEGEYLTDRLT----DEAIDFIEQNKDKPFFLYL 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 254 SFLHVHIPLITTK----NFLGKSAHGLYGDN-------VEEMDWMVGQILDALDTEGLTNSTLIYFASDHGG-SLENQFA 321
Cdd:cd16144   191 SHYAVHTPIQARPelieKYEKKKKGLRKGQKnpvyaamIESLDESVGRILDALEELGLADNTLVIFTSDNGGlSTRGGPP 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 322 NSQY-----------GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVI 390
Cdd:cd16144   271 TSNAplrggkgslyeGG-----------------IRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHL 333
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 391 DGRDLLPLLLGTAQHSDHEFLMhycerflhaarWHQrdrgtlwkvhfvtPVFQPEGAGacygrkvcPCS----GE-KVVH 465
Cdd:cd16144   334 DGVSLVPLLKGGEADLPRRALF-----------WHF-------------PHYHGQGGR--------PASairkGDwKLIE 381
                         490       500
                  ....*....|....*....|
gi 1864524949 466 H---DPPLLFDLSRDPSEAH 482
Cdd:cd16144   382 FyedGRVELYNLKNDIGETN 401
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
21-482 9.51e-72

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 234.39  E-value: 9.51e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGyrvlqwtGASGGLPTNETTFAKILKEKGYATGL 100
Cdd:COG3119    49 TPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTAL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGLncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisi 180
Cdd:COG3119   122 FGKWHLYL------------------------------------------------------------------------ 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 swmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvTPLILQEVKSFLKRNKLG--PFLLLVSFLHV 258
Cdd:COG3119   130 -------------------------------------------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAP 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 259 HIPLITTKNFLGK-----------------------SAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGS 315
Cdd:COG3119   161 HAPYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS 240
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 316 LENQ-FA---NSQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvI 390
Cdd:COG3119   241 LGEHgLRggkGTLYeGG-----------------IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--L 301
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 391 DGRDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRdrgtlWKVHFvtpvfqpegagaCYGRKvcpcsgekvvhhDPPL 470
Cdd:COG3119   302 DGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTGR-----WKLIR------------YYDDD------------GPWE 352
                         490
                  ....*....|..
gi 1864524949 471 LFDLSRDPSEAH 482
Cdd:COG3119   353 LYDLKNDPGETN 364
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
21-482 5.74e-58

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: 198.59  E-value: 5.74e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyRVLQWTGASGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16145    26 TPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPGGQDPLPPDDVTLAEVLKKAGYATAA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGLNcESAGdhchHPLHHGFDYFYGmplsmtgdcahwelsekrvdleqklnFLFQVLAlvtltlaagkfmHlisi 180
Cdd:cd16145   100 FGKWGLGGP-GTPG----HPTKQGFDYFYG--------------------------YLDQVHA------------H---- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 swmpviwsallavfllttSYFAGALIVHADCFLMRNHTIT-------EQPMRFQRVTPLILQEVKSFLKRNKLGPFLLLV 253
Cdd:cd16145   133 ------------------NYYPEYLWRNGEKVPLPNNVIPpldegnnAGGGGGTYSHDLFTDEALDFIRENKDKPFFLYL 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 254 SFLHVHIPLITTK---NFLGKSAHGLYGDN------------VEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLE- 317
Cdd:cd16145   195 AYTLPHAPLQVPDdgpYKYKPKDPGIYAYLpwpqpekayaamVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSEg 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 318 -----NQFANSQ----------Y-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAG 381
Cdd:cd16145   275 gsehdPDFFDSNgplrgykrslYeGG-----------------IRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAG 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 382 GEVPQDrvIDGRDLLPLLLGTAQHSDHEFLmhYCERFLH----AARWHQrdrgtlWKVhfvtpVFQPEGAGacygrkvcp 457
Cdd:cd16145   338 AEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFYEGggaqAVRMGG------WKA-----VRHGKKDG--------- 393
                         490       500
                  ....*....|....*....|....*
gi 1864524949 458 csgekvvhhdPPLLFDLSRDPSEAH 482
Cdd:cd16145   394 ----------PFELYDLSTDPGETN 408
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
406-540 3.28e-56

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 184.44  E-value: 3.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 406 SDHEFLMHYCERFLHAARWHQrdrgtlWKVHFVTPVFQPEGAGACYGRKVCpcsgekVVHHDPPLLFDLSRDPSEAHVLT 485
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1864524949 486 PASePLFYHVMERVQQAVWEHQQTLSPVALQLDSLGNLWRPWLQPCCGPFPLCWC 540
Cdd:pfam14707  69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
21-394 2.80e-55

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: 186.10  E-value: 2.80e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGmvssvgyrVLQWTGASGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16022    26 TPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVGNGGGLPPDEPTLAELLKEAGYRTAL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHlglncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisi 180
Cdd:cd16022    98 IGKWH--------------------------------------------------------------------------- 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 swmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplilQEVKSFLKRN-KLGPFLLLVSFLHVH 259
Cdd:cd16022   103 ------------------------------------------------------DEAIDFIERRdKDKPFFLYVSFNAPH 128
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 260 IPLIttknflgksahglYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQfaNSQYGGWNGIYKGgkgmg 339
Cdd:cd16022   129 PPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDH--GLRGKKGSLYEGG----- 188
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1864524949 340 gweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRD 394
Cdd:cd16022   189 -----IRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
21-424 5.60e-53

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: 184.34  E-value: 5.60e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTqHISAASLCTPSRAAFLTGRYPVRSGMVSsvgyrvlqwtgasGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16151    26 TPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYVVF-------------GYLDPKQKTFGHLLKDAGYATAI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGLNcESAGDHchhPLHHGFDYFygmplsmtgdCAhWELSEKRVDLEQKLNFLFQVLALVTLTLAAGKFMhlisi 180
Cdd:cd16151    92 AGKWQLGGG-RGDGDY---PHEFGFDEY----------CL-WQLTETGEKYSRPATPTFNIRNGKLLETTEGDYG----- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 swmPVIWSAllavfllttsyfagalivhadcFLMRnhtiteqpmrfqrvtplilqevksFLKRNKLGPFLLLVSFLHVHI 260
Cdd:cd16151   152 ---PDLFAD----------------------FLID------------------------FIERNKDQPFFAYYPMVLVHD 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 261 PLITT----------KNFLGKSAHglYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLE-NQFANSQY--GG 327
Cdd:cd16151   183 PFVPTpdspdwdpddKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPiTSRTNGREvrGG 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 328 wngiykggkGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLLG-TAQHS 406
Cdd:cd16151   261 ---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGkTGSPR 331
                         410       420
                  ....*....|....*....|....*
gi 1864524949 407 DHEFLMHY-------CERFLHAARW 424
Cdd:cd16151   332 REWIYWYYrnphkkfGSRFVRTKRY 356
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
21-482 6.48e-52

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: 182.36  E-value: 6.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQ-HISaaSLCTPSRAAFLTGRYPVRSGMVSSVGYRVLqwtgasggLPTNETTFAKILKEKGYATG 99
Cdd:cd16146    26 TPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--------MRLDETTLAEVFKDAGYRTG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 100 LIGKWHLGLNcesagdHCHHPLHHGFDYFYGMPLSMTGDCAHWELSEkrvdleqklnflfqvlalvtltlaagkfmhlis 179
Cdd:cd16146    96 IFGKWHLGDN------YPYRPQDRGFDEVLGHGGGGIGQYPDYWGND--------------------------------- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 180 iswmpviwsallavfllttsYFagalivhaDCFLMRNHTITeqpmRFQR-VTPLILQEVKSFLKRNKLGPFLLLVSFLHV 258
Cdd:cd16146   137 --------------------YF--------DDTYYHNGKFV----KTEGyCTDVFFDEAIDFIEENKDKPFFAYLATNAP 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 259 HIPLITTKNF--------LGKSAHGLYGdNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG--GSLENQF-AN----- 322
Cdd:cd16146   185 HGPLQVPDKYldpykdmgLDDKLAAFYG-MIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGpaGGVPKRFnAGmrgkk 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 323 -SQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLPLLL 400
Cdd:cd16146   264 gSVYeGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLK 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 401 GTAQHSDHEFLmhycerFLHaarWHQRDRGTLWKVHFVtpVFQPEgagacYgRKVCPcsgekvvHHDPPLLFDLSRDPSE 480
Cdd:cd16146   327 GESDPWPERTL------FTH---SGRWPPPPKKKRNAA--VRTGR-----W-RLVSP-------KGFQPELYDIENDPGE 382

                  ..
gi 1864524949 481 AH 482
Cdd:cd16146   383 EN 384
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
21-484 2.79e-51

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: 180.44  E-value: 2.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMVSSVGyrvlqWTGASGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16029    26 TPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGMQHGVI-----LAGEPYGLPLNETLLPQYLKELGYATHL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGlncesagdHCHH---PLHHGFDYFYGMPLSMTGdcaHWelsekrvdleqklnflfqvlalvtltlaagkfmhl 177
Cdd:cd16029   100 VGKWHLG--------FYTWeytPTNRGFDSFYGYYGGAED---YY----------------------------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 178 isiswmpviwsallavfllttSYFAGALIVHADCFLMRNHTIT-EQPMRFqrVTPLILQEVKSFLKR-NKLGPFLLLVSF 255
Cdd:cd16029   134 ---------------------THTSGGANDYGNDDLRDNEEPAwDYNGTY--STDLFTDRAVDIIENhDPSKPLFLYLAF 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 256 LHVHIPLITTKNFL----GKSAHGLYGD------NVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFANSQY 325
Cdd:cd16029   191 QAVHAPLQVPPEYAdpyeDKFAHIKDEDrrtyaaMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGGSNY 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 326 -----------GGwngiykggkgmggweggIRVPGiFRWPGVLP--AGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDG 392
Cdd:cd16029   271 plrggkntlweGG-----------------VRVPA-FVWSPLLPpkRGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDG 332
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 393 RDLLPLLLGTAQHSDHEFLmhycerflhaarwHQRDRGTLWKVHfvtpvfqpegAGACYGRKvcpcsgeKVVHHDPplLF 472
Cdd:cd16029   333 VDQWDALSGGAPSPRTEIL-------------LNIDDITRTTGG----------AAIRVGDW-------KLIVGKP--LF 380
                         490
                  ....*....|..
gi 1864524949 473 DLSRDPSEAHVL 484
Cdd:cd16029   381 NIENDPCERNDL 392
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
21-482 1.24e-50

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


Pssm-ID: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 178.53  E-value: 1.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYrvlqwtgasggLPTNETTFAKILKEKGYATGL 100
Cdd:cd16034    27 TPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----------LPPDAPTIADVLKDAGYRTGY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGLNCESAGDHCHH----PLHHGFDYFYGMplsmtgDCAH-------WELSEKRVDLEQklnflfqvlalvtltl 169
Cdd:cd16034    96 IGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY------ECNHdhnnphyYDDDGKRIYIKG---------------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 170 aagkfmhlisisWMPvIWSALLAVfllttSYfagalivhadcflMRNHTITEQP-----------MRFQRVtPlilQEVK 238
Cdd:cd16034   154 ------------YSP-DAETDLAI-----EY-------------LENQADKDKPfalvlswnpphDPYTTA-P---EEYL 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 239 SFLKRNKLgpflllvsFLHVHIPLIT-TKNFLGKSAHGLYGdNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG---G 314
Cdd:cd16034   199 DMYDPKKL--------LLRPNVPEDKkEEAGLREDLRGYYA-MITALDDNIGRLLDALKELGLLENTIVVFTSDHGdmlG 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 315 SLENQFANSQYGGwngiykggkgmggwegGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRD 394
Cdd:cd16034   270 SHGLMNKQVPYEE----------------SIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRD 331
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 395 LLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTL----WKvhFVtpvfqpegagacygrkvcpcsgekVVHHDPPL 470
Cdd:cd16034   332 LSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVrtdrYT--YV------------------------RDKNGPWL 385
                         490
                  ....*....|..
gi 1864524949 471 LFDLSRDPSEAH 482
Cdd:cd16034   386 LFDNEKDPYQLN 397
Sulfatase pfam00884
Sulfatase;
21-381 8.91e-45

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 159.90  E-value: 8.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGyrvlqwtgasGGLPTNETTFAKILKEKGYATGL 100
Cdd:pfam00884  26 TPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP----------VGLPRTEPSLPDLLKRAGYNTGA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGLNCESAgdhchhPLHHGFDYFYGmplsmtgdcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisi 180
Cdd:pfam00884  96 IGKWHLGWYNNQS------PCNLGFDKFFG-------------------------------------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 swmpviwsallavFLLTTSYFAGALIVHADCFLMRNHTiteqpmrfQRVTPLILQevksFLKRNKlGPFLLLVSFLHVHI 260
Cdd:pfam00884 120 -------------RNTGSDLYADPPDVPYNCSGGGVSD--------EALLDEALE----FLDNND-KPFFLVLHTLGSHG 173
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 261 PLITTKNFLGKSA------------HGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFANSQYGGW 328
Cdd:pfam00884 174 PPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKY 253
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1864524949 329 NGIYKGGkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAG 381
Cdd:pfam00884 254 DNAPEGG---------YRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
21-425 9.80e-43

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: 156.51  E-value: 9.80e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvGYRVLQWTgasggLPTNETTFAKILKEKGYATGL 100
Cdd:cd16027    25 TPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAH---GLRSRGFP-----LPDGVKTLPELLREAGYYTGL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLglNCESAGDHCHHPLHHGFDYFYGMPlsMTGDCAHWElseKRVDLEQklnflfqvlalvtltlaagkfmhlisi 180
Cdd:cd16027    97 IGKTHY--NPDAVFPFDDEMRGPDDGGRNAWD--YASNAADFL---NRAKKGQ--------------------------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 swmPviwsallavfllttsyFagalivhadcFLMRNHTITEQPMRFQRVTPLI--LQEVKsflkrnkLGPFLllvsflhV 258
Cdd:cd16027   143 ---P----------------F----------FLWFGFHDPHRPYPPGDGEEPGydPEKVK-------VPPYL-------P 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 259 HIPLIttknflgKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGslenQFANS-----QYGgwngiyk 333
Cdd:cd16027   180 DTPEV-------REDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM----PFPRAkgtlyDSG------- 241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 334 ggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLG-TAQHSDHEFLM 412
Cdd:cd16027   242 -----------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGeKDPGRDYVFAE 308
                         410       420
                  ....*....|....*....|
gi 1864524949 413 H-------YCERFLHAARWH 425
Cdd:cd16027   309 RdrhdetyDPIRSVRTGRYK 328
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
10-425 6.46e-41

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


Pssm-ID: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 152.37  E-value: 6.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  10 RGDMLHLQHSW---TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGyrvlqWTGA-SGGLPTNET 85
Cdd:cd16033    12 RYDTLGCYGNPivkTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVE-----NAGAySRGLPPGVE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  86 TFAKILKEKGYATGLIGKWHLGLNcesagdhcHHPLHHGFDYFygMPLSMTGDcaHWeLSEKRVDLEQKLnflfqvlalv 165
Cdd:cd16033    87 TFSEDLREAGYRNGYVGKWHVGPE--------ETPLDYGFDEY--LPVETTIE--YF-LADRAIEMLEEL---------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 166 tltLAAGK-FMHLISIsWMPviwsallavfllttsyfagalivHADCF-------LMRNHTItEQPMRFQRvtPLILqev 237
Cdd:cd16033   144 ---AADDKpFFLRVNF-WGP-----------------------HDPYIppepyldMYDPEDI-PLPESFAD--DFED--- 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 238 KSFLKRNKLGPFLLLVSFLHVHIPLIttknflgksAHglYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLE 317
Cdd:cd16033   191 KPYIYRRERKRWGVDTEDEEDWKEII---------AH--YWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALG 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 318 NQfansqyGGWNGIYKGGKGMGgweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLP 397
Cdd:cd16033   260 AH------RLWDKGPFMYEETY------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK--VDGRSLLP 325
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1864524949 398 LLLGT----------AQHSDHEFLmhYCERFLHAARWH 425
Cdd:cd16033   326 LLRGEqpedwrdevvTEYNGHEFY--LPQRMVRTDRYK 361
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
17-478 1.72e-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: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 146.15  E-value: 1.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  17 QHSW------------TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyrvlqWTGASGgLPTNE 84
Cdd:cd16037    10 EHNPdamgcyghpvvrTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGV----------WDNADP-YDGDV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  85 TTFAKILKEKGYATGLIGKWHLglncESAGDHchhplhHGFDYfygmplsmtgdcahwelsekrvDLEqklnflfqvlal 164
Cdd:cd16037    79 PSWGHALRAAGYETVLIGKLHF----RGEDQR------HGFRY----------------------DRD------------ 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 165 vtltlaagkfmhlisiswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplILQEVKSFLKRN 244
Cdd:cd16037   115 --------------------------------------------------------------------VTEAAVDWLREE 126
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 245 KL--GPFLLLVSFLHVHIPLITTKNFLGKSAHGL---YGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGgslENQ 319
Cdd:cd16037   127 AAddKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHG---DML 203
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 320 FANSQYGgwngiykggkGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRviDGRDLLPLL 399
Cdd:cd16037   204 GERGLWG----------KSTMYEESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAPPPPDL--DGRSLLPLA 270
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 400 LGTAQHSDHEFlmhyCErfLHAA---------RWHQrdrgtlWK-VHFVtpvfqpegagacygrkvcpcsgekvvhHDPP 469
Cdd:cd16037   271 EGPDDPDRVVF----SE--YHAHgspsgafmlRKGR------WKyIYYV---------------------------GYPP 311

                  ....*....
gi 1864524949 470 LLFDLSRDP 478
Cdd:cd16037   312 QLFDLENDP 320
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
21-482 2.94e-39

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: 148.45  E-value: 2.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvgyrvlqwTGASGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16031    28 TPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVT----------DNNGPLFDASQPTYPKLLRKAGYQTAF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGlncesaGDHCHHPlhHGFDYFYGMPlsmtgdcahwelsekrvdlEQklnflfqvlalvtltlaagkfmhlisi 180
Cdd:cd16031    98 IGKWHLG------SGGDLPP--PGFDYWVSFP-------------------GQ--------------------------- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 swmpviwsallavflltTSYFAGALIVhadcflMRNHTITEQPmrfqrVTPLILQEVKSFLKRNKLG-PFLLLVSFLHVH 259
Cdd:cd16031   124 -----------------GSYYDPEFIE------NGKRVGQKGY-----VTDIITDKALDFLKERDKDkPFCLSLSFKAPH 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 260 -----------------IPLITT---KNFLGKS-------------------AHGLYGDNVE-------EMDWMVGQILD 293
Cdd:cd16031   176 rpftpaprhrglyedvtIPEPETfddDDYAGRPewareqrnrirgvldgrfdTPEKYQRYMKdylrtvtGVDDNVGRILD 255
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 294 ALDTEGLTNSTLIYFASDHGGSL-ENQFA-------NSqyggwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGE 365
Cdd:cd16031   256 YLEEQGLADNTIIIYTSDNGFFLgEHGLFdkrlmyeES---------------------IRVPLIIRDPRLIKAGTVVDA 314
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 366 PTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGTAQHS-DHEFLMHYCE--RFLHAARWH--QRDRgtlWK-VHFvt 439
Cdd:cd16031   315 LVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEYYEepNFHNVPTHEgvRTER---YKyIYY-- 387
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1864524949 440 pvfqpegagacygrkvcpcsgekvvHHDPPL--LFDLSRDPSEAH 482
Cdd:cd16031   388 -------------------------YGVWDEeeLYDLKKDPLELN 407
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
21-482 2.45e-35

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: 136.80  E-value: 2.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQ-HisAASLCTPSRAAFLTGRYPVRSGMvSSVGYRVLQWTGASGGLPTNETTFAKILKEKGYATG 99
Cdd:cd16025    27 TPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGKPGYEGYLPDSAATIAEVLKDAGYHTY 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 100 LIGKWHLGLN----CESAGDH-----------------------CHHPLH--------------HGFDyfygmplsmtgd 138
Cdd:cd16025   104 MSGKWHLGPDdyysTDDLTDKaieyideqkapdkpfflylafgaPHAPLQapkewidkykgkydAGWD------------ 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 139 cahwELSEKRvdLE-QKlnflfqvlalvtltlAAGkfmhlisiswmpviwsallavfllttsyfagalIVHADCFLM-RN 216
Cdd:cd16025   172 ----ALREER--LErQK---------------ELG---------------------------------LIPADTKLTpRP 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 217 HTI-------TEQPMRFQRvtpliLQEVksflkrnklgpflllvsflhvhiplittknflgksahglYGDNVEEMDWMVG 289
Cdd:cd16025   198 PGVpawdslsPEEKKLEAR-----RMEV---------------------------------------YAAMVEHMDQQIG 233
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 290 QILDALDTEGLTNSTLIYFASDHGGSLENQFAN------------SQYGGwngiykggkgmggweggIRVPGIFRWP-GV 356
Cdd:cd16025   234 RLIDYLKELGELDNTLIIFLSDNGASAEPGWANasntpfrlykqaSHEGG-----------------IRTPLIVSWPkGI 296
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 357 LPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRV------IDGRDLLPLLLGTAQHSDHEFLmhYCERFLHAARWHQRdrg 430
Cdd:cd16025   297 KAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRTQ--YFELFGNRAIRKGG--- 371
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1864524949 431 tlWKVhfvtpvfqpegagacygrkvcpcsgekVVHHDPPL------LFDLSRDPSEAH 482
Cdd:cd16025   372 --WKA---------------------------VALHPPPGwgdqweLYDLAKDPSETH 400
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
21-478 4.54e-35

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: 134.24  E-value: 4.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyrvlqWTGASGgLPTNETTFAKILKEKGYATGL 100
Cdd:cd16032    26 TPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA----------YDNAAE-FPADIPTFAHYLRAAGYRTAL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLglncesagdhCHHPLHHGFDYfygmplsmtgdcahwelsekrvDLEqklnflfqvlalvtltlaagkfmhlisi 180
Cdd:cd16032    95 SGKMHF----------VGPDQLHGFDY----------------------DEE---------------------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 swmpVIWSALLAVFllttsyfagalivhaDcfLMRNHTiteqpmrfqrvtplilqevksflKRnklgPFLLLVSFLHVHI 260
Cdd:cd16032   115 ----VAFKAVQKLY---------------D--LARGED-----------------------GR----PFFLTVSFTHPHD 146
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 261 PLITTKNFLG----KSAHGLYGdNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL--------ENQFANSqyggw 328
Cdd:cd16032   147 PYVIPQEYWDlyvrRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLgerglwykMSFFEGS----- 220
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 329 ngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRV-IDGRDLLPLLLGTAQHSD 407
Cdd:cd16032   221 ----------------ARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpLDGRSLLPLLEGGDSGGE 283
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864524949 408 HEFLMHYC-ERFLHAARWHQRDRgtlWKvhFVtpvfqpegagacygrkvcpcsgekVVHHDPPLLFDLSRDP 478
Cdd:cd16032   284 DEVISEYLaEGAVAPCVMIRRGR---WK--FI------------------------YCPGDPDQLFDLEADP 326
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
10-397 1.82e-32

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: 125.35  E-value: 1.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  10 RGDML---HLQHSWTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssvgyrvLQWTGASGGLPTNETT 86
Cdd:cd16148    12 RADHLgcyGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP-------------FYHGVWGGPLEPDDPT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  87 FAKILKEKGYATGLIGkwhlglncesagDHCHHPLHHGFDyfygmplsmtgdcahwelseKRVDleqklnflfqvlalvt 166
Cdd:cd16148    79 LAEILRKAGYYTAAVS------------SNPHLFGGPGFD--------------------RGFD---------------- 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 167 ltlaagkfmhlisiSWMPVIWsallavfllttsyfagalivhadcflMRNHTITEQPMRFQRVTplilQEVKSFLKRNKL 246
Cdd:cd16148   111 --------------TFEDFRG--------------------------QEGDPGEEGDERAERVT----DRALEWLDRNAD 146
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 247 G-PFlllvsFLHVHIplittknFlgkSAHGLYG-DN-VEEMDWMVGQILDALDTEGLTNSTLIYFASDHGgslENQFANS 323
Cdd:cd16148   147 DdPF-----FLFLHY-------F---DPHEPYLyDAeVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG---EEFGEHG 208
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864524949 324 QYGGWNgiykggkgMGGWEGGIRVPGIFRWPGVLPAGRvIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLP 397
Cdd:cd16148   209 LYWGHG--------SNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SDGRSLLP 271
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
21-397 7.80e-31

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: 120.42  E-value: 7.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVLQWTGASGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16149    26 TPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTKKPEGYLEGQTTLPEVLQDAGYRCGL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLGlncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlisi 180
Cdd:cd16149   106 SGKWHLG------------------------------------------------------------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 swmpviwsallavfllttsyfagaliVHADCFLMRNHtiteqpmrfqrvtplilqevksflKRNKlgPFLLLVSFLHVHI 260
Cdd:cd16149   113 --------------------------DDAADFLRRRA------------------------EAEK--PFFLSVNYTAPHS 140
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 261 PlittknflgksaHGlYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGgslenqFANSQYGGW---------NGI 331
Cdd:cd16149   141 P------------WG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNG------FNMGHHGIWgkgngtfplNMY 201
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864524949 332 YKGgkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDLLP 397
Cdd:cd16149   202 DNS----------VKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPGRSFAD 257
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
10-506 3.68e-30

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: 123.14  E-value: 3.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  10 RGDML-HLQHSW--TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvgyrvlqWTGASggLPTNETT 86
Cdd:cd16028    12 RADCLsCLGHPLvkTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV---------WNGTP--LDARHLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  87 FAKILKEKGYATGLIGKWHLglnceSAGDHCHHPLH----------HGFDY-----FYGMPLSmtgDCAHweLSEKrvdl 151
Cdd:cd16028    81 LALELRKAGYDPALFGYTDT-----SPDPRGLAPLDprllsyelamPGFDPvdrldEYPAEDS---DTAF--LTDR---- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 152 eqklnflfqvlALVTLTLAAGK--FMHLISISWMPviwsallavfllttsyfagALIVHADCFLMRNHTITEQPMRfqRV 229
Cdd:cd16028   147 -----------AIEYLDERQDEpwFLHLSYIRPHP-------------------PFVAPAPYHALYDPADVPPPIR--AE 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 230 TPLILQEVKSFLKRnklgpflllvsflhvHIPLITTKNFLGKSAHGLYGDN-------------VEEMDWMVGQILDALD 296
Cdd:cd16028   195 SLAAEAAQHPLLAA---------------FLERIESLSFSPGAANAADLDDeevaqmratylglIAEVDDHLGRLFDYLK 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 297 TEGLTNSTLIYFASDHGGSLENQFANSQyGGWNGIYKggkgmggweggiRVPGIFRWPGVL---PAGRVIGEPTSLMDVF 373
Cdd:cd16028   260 ETGQWDDTLIVFTSDHGEQLGDHWLWGK-DGFFDQAY------------RVPLIVRDPRREadaTRGQVVDAFTESVDVM 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 374 PTVVQLAGGEVPQDrvIDGRDLLPLLLG-------TAQHSDHEFlmhycerFLHAARWHQRDRGTlwkvhfvtpvfQPEG 446
Cdd:cd16028   327 PTILDWLGGEIPHQ--CDGRSLLPLLAGaqpsdwrDAVHYEYDF-------RDVSTRRPQEALGL-----------SPDE 386
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864524949 447 AGACYGRkvcpcSGE-KVVHHD--PPLLFDLSRDPSEAHVLtpASEPLFYHVMERVQQAVWEH 506
Cdd:cd16028   387 CSLAVIR-----DERwKYVHFAalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKLLSW 442
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
21-404 2.00e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 116.56  E-value: 2.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgYRvlqwtgASGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16152    27 TPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR------NGIPLPADEKTLAHYFRDAGYETGY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLglncesAGdhchhplhhgfdYfygmplsmtgdcahwelsekRVDleqklnflfqvlalvTLTLAAGKFMHlisi 180
Cdd:cd16152    96 VGKWHL------AG------------Y--------------------RVD---------------ALTDFAIDYLD---- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 swmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplilqevksflKRNKLGPFLLLVSFLHVH- 259
Cdd:cd16152   119 -------------------------------------------------------------NRQKDKPFFLFLSYLEPHh 137
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 260 ---------------------IP--LittKNFLGKSAHGL---YGdNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 313
Cdd:cd16152   138 qndrdryvapegsaerfanfwVPpdL---AALPGDWAEELpdyLG-CCERLDENVGRIRDALKELGLYDNTIIVFTSDHG 213
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 314 gsleNQFA--NSQYggwngiykggkGMGGWEGGIRVPGIFRWPGVLpAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvID 391
Cdd:cd16152   214 ----CHFRtrNAEY-----------KRSCHESSIRVPLVIYGPGFN-GGGRVEELVSLIDLPPTLLDAAGIDVPEE--MQ 275
                         410
                  ....*....|...
gi 1864524949 392 GRDLLPLLLGTAQ 404
Cdd:cd16152   276 GRSLLPLVDGKVE 288
PRK13759 PRK13759
arylsulfatase; Provisional
10-402 1.06e-26

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 113.23  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  10 RGDMLHLQ-HSW--TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssvGYrvlqwtgASGGLPTNETT 86
Cdd:PRK13759   18 RGDCLGCNgNKAveTPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY-------GDVVPWNYKNT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  87 FAKILKEKGYATGLIGKWHLglncesagdhchHPLH--HGFDYfygmplSMTGDcahWELSEKRVDLEQKLNFLFQVLAL 164
Cdd:PRK13759   88 LPQEFRDAGYYTQCIGKMHV------------FPQRnlLGFHN------VLLHD---GYLHSGRNEDKSQFDFVSDYLAW 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 165 VTLTlAAGKFMHLISISWMPVIWSAllavfllttsyfagalivhadcflmRNHTITEQpmrfQRVTPLILQEVKSFLKR- 243
Cdd:PRK13759  147 LREK-APGKDPDLTDIGWDCNSWVA-------------------------RPWDLEER----LHPTNWVGSESIEFLRRr 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 244 NKLGPFLLLVSFLHVHIPLITTKNFL-------------------------GKSAHGLYGD---------------NVEE 283
Cdd:PRK13759  197 DPTKPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeeyarraraayygLITH 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 284 MDWMVGQILDALDTEGLTNSTLIYFASDHGGSL--ENQFANS-QYGGwngiykggkgmggwegGIRVPGIFRWPG---VL 357
Cdd:PRK13759  277 IDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLgdHYLFRKGyPYEG----------------SAHIPFIIYDPGgllAG 340
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1864524949 358 PAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPLLLGT 402
Cdd:PRK13759  341 NRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQ 383
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
21-408 1.86e-26

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: 111.90  E-value: 1.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYrvlqWTGASGglptNETTFAKILKEKGYATGL 100
Cdd:cd16030    27 TPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSY----FRKVAP----DAVTLPQYFKENGYTTAG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHlglncesagdhchhplHHGFDYFYGMPLSmtgdcahWELSEKRVDLEQKLNFLFQVLALVTLTLAAGKFMHLISI 180
Cdd:cd16030    99 VGKIF----------------HPGIPDGDDDPAS-------WDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 181 --SWMPVIWSALLAVFLLTT------SYFAGA--------LIVHADCFLMRNHTITEQPMRFQRV-TPLI----LQEVks 239
Cdd:cd16030   156 pdEAYPDGKVADEAIEQLRKlkdsdkPFFLAVgfykphlpFVAPKKYFDLYPLESIPLPNPFDPIdLPEVawndLDDL-- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 240 flkRNKLGPFLLLVSFLHVHIPLITTKNFLgksaHGLYGdNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL-EN 318
Cdd:cd16030   234 ---PKYGDIPALNPGDPKGPLPDEQARELR----QAYYA-SVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLgEH 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 319 Q----FANsqyggWNGIykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGgeVPQDRVIDGRD 394
Cdd:cd16030   306 GhwgkHTL-----FEEA-------------TRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKS 365
                         410
                  ....*....|....
gi 1864524949 395 LLPLLLGTAQHSDH 408
Cdd:cd16030   366 LVPLLKNPSAKWKD 379
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
10-514 1.46e-24

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: 106.16  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  10 RGDMLH---LQHSWTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYP-VRsgmvssvGYRVLQWTgasggLPTNET 85
Cdd:cd16150    12 RADSLGhlgNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPhVN-------GHRTLHHL-----LRPDEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  86 TFAKILKEKGYATGLIGKWHLGLNCESAGDHChhplhhgfdyfygmplsmTGDcahWELSEKRVD-LEQKLN----FLFq 160
Cdd:cd16150    80 NLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC------------------DSD---EACVRTAIDwLRNRRPdkpfCLY- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 161 vlalVTLTL------AAGKFMHLISISWMPVIWSALLavfllTTSYFAGALIvhadcfLMRNHtiteqpmRFQRVTPLIL 234
Cdd:cd16150   138 ----LPLIFphppygVEEPWFSMIDREKLPPRRPPGL-----RAKGKPSMLE------GIEKQ-------GLDRWSEERW 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 235 QEVKsflkrnklgpflllvsflhvhiplittKNFLGKsahglygdnVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG- 313
Cdd:cd16150   196 RELR---------------------------ATYLGM---------VSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGd 239
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 314 -----GSLE---NQFANSQyggwngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVQLAGgeVP 385
Cdd:cd16150   240 ytgdyGLVEkwpNTFEDCL--------------------TRVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAG--IP 296
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 386 QDRVIDGRDLLPLLLG-TAQHSDHEFlmhyCE-RFLHAARWHQRDRGTlwKVHFVTPVFQPEGAGACYGRKVCPCSGE-K 462
Cdd:cd16150   297 LSHTHFGRSLLPVLAGeTEEHRDAVF----SEgGRLHGEEQAMEGGHG--PYDLKWPRLLQQEEPPEHTKAVMIRTRRyK 370
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1864524949 463 VV--HHDPPLLFDLSRDPSEAHVLtpASEPLFYHVMERVQQAVWEHQQTLSPVA 514
Cdd:cd16150   371 YVyrLYEPDELYDLEADPLELHNL--IGDPAYAEIIAEMKQRLLRWMVETSDVV 422
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
16-395 1.18e-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: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 100.91  E-value: 1.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  16 LQHSWTPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYrvlqWTGASGGLPTnettFAKILKEKG 95
Cdd:cd16153    32 LGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFEAA----HPALDHGLPT----FPEVLKKAG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  96 YATGLIGKWHLglncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdlEQKLNFLFQvlALVTLTLAAGKfm 175
Cdd:cd16153   104 YQTASFGKSHL---------------------------------------------EAFQRYLKN--ANQSYKSFWGK-- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 176 hlisISWMPviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplilqevksflKRNKlgPFLLLVSF 255
Cdd:cd16153   135 ----IAKGA---------------------------------------------------------DSDK--PFFVRLSF 151
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 256 LHVHIPLITTKNFLGKSA-HGL--YGDNveemdwMVGQILDALDTEGLTN---STLIYFASDHGGSLENQFANSQYGGWN 329
Cdd:cd16153   152 LQPHTPVLPPKEFRDRFDyYAFcaYGDA------QVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQGILAKFTFWP 225
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864524949 330 GIykggkgmggweggIRVPGIFRWPGVL--PAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGRDL 395
Cdd:cd16153   226 QS-------------HRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL 280
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
22-414 5.05e-23

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


Pssm-ID: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 99.59  E-value: 5.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  22 PNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSVGYRVlQWTgasggLPTNETTFAKILKEKGYATGLI 101
Cdd:cd16035    27 PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPM-QPL-----LSPDVPTLGHMLRAAGYYTAYK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 102 GKWHLGlncesagdhchhplhhgfdyfygmplSMTGDCAHwelsekrvdleqklnflfqvlalvtltlaagkfmhlisis 181
Cdd:cd16035   101 GKWHLS--------------------------GAAGGGYK---------------------------------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 182 wmpviwsallavfllttsyfagalivhadcflmRNHTITEQPMRFqrvtpliLQEVKSflKRNKLGPFLLLVSFL--H-V 258
Cdd:cd16035   115 ---------------------------------RDPGIAAQAVEW-------LRERGA--KNADGKPWFLVVSLVnpHdI 152
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 259 HIPLITTKNFlgKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG---GS--LENQFANSqYGgwngiyk 333
Cdd:cd16035   153 MFPPDDEERW--RRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGemgGAhgLRGKGFNA-YE------- 222
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 334 ggkgmggweGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVID----GRDLLPLLLGTAQHSDHE 409
Cdd:cd16035   223 ---------EALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATEApplpGRDLSPLLTDADADAVRD 293

                  ....*.
gi 1864524949 410 -FLMHY 414
Cdd:cd16035   294 gILFTY 299
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
21-399 2.03e-22

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: 100.15  E-value: 2.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssvgyrvlqWTGaSGGLPTNETTFAKILKEKGYATGL 100
Cdd:cd16156    26 TPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------WTN-CMALGDNVKTIGQRLSDNGIHTAY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 101 IGKWHLglnceSAGDH-----ChhPLHHGFDYFYGMplsmtgDCAHWELSEKRVdleqklnflfqvlalvtltlaagkfm 175
Cdd:cd16156    95 IGKWHL-----DGGDYfgngiC--PQGWDPDYWYDM------RNYLDELTEEER-------------------------- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 176 hlisiswmpVIWSALLAVfllttsyfagalivhadcflMRNHTITEQPMRFQRVTPLILQevksFLKRNKLGPFLLLVSF 255
Cdd:cd16156   136 ---------RKSRRGLTS--------------------LEAEGIKEEFTYGHRCTNRALD----FIEKHKDEDFFLVVSY 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 256 LHVHIPLITTKNF----------LGKSAHglygDNVEE---------------------------------MDWMVGQIL 292
Cdd:cd16156   183 DEPHHPFLCPKPYasmykdfefpKGENAY----DDLENkplhqrlwagakphedgdkgtikhplyfgcnsfVDYEIGRVL 258
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 293 DALDtEGLTNSTLIYfASDHGgslENQFANSQYGgwngiykggKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDV 372
Cdd:cd16156   259 DAAD-EIAEDAWVIY-TSDHG---DMLGAHKLWA---------KGPAVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDL 324
                         410       420
                  ....*....|....*....|....*..
gi 1864524949 373 FPTVVQLAGgeVPQDRVIDGRDLLPLL 399
Cdd:cd16156   325 APTILDYAG--IPQPKVLEGESILATI 349
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
26-393 3.20e-22

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: 98.78  E-value: 3.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  26 RLAEFGVKLTQHISAASLCTPSRAAFLTGRYP----VRSGMVSSVGYRVLQWTGAsgglptNETTFAKILKEKGYATGLI 101
Cdd:cd16147    28 LLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgVTNNSPPGGGYPKFWQNGL------ERSTLPVWLQEAGYRTAYA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 102 GKWhlgLN-CESAGDHCHHPLhhGFDYFYGMP---------LSMTGDCAHWELSEKR--VDL--EQKLNFLfqvlalvTL 167
Cdd:cd16147   102 GKY---LNgYGVPGGVSYVPP--GWDEWDGLVgnstyynytLSNGGNGKHGVSYPGDylTDViaNKALDFL-------RR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 168 TLAAGKfmhlisiswmPviwsallavFLLTTSYFAgaliVHAdcflmrNHTITEQPMR-FQRVTPL--------ILQEVK 238
Cdd:cd16147   170 AAADDK----------P---------FFLVVAPPA----PHG------PFTPAPRYANlFPNVTAPprpppnnpDVSDKP 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 239 SFLKRNKlgpflllvsflhvhiplittknflgksahGLYGDNVEEMDW--------------MVGQILDALDTEGLTNST 304
Cdd:cd16147   221 HWLRRLP-----------------------------PLNPTQIAYIDElyrkrlrtlqsvddLVERLVNTLEATGQLDNT 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 305 LIYFASDHG---GSLENQFANSQ-YggwngiykggkgmggwEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVQLA 380
Cdd:cd16147   272 YIIYTSDNGyhlGQHRLPPGKRTpY----------------EEDIRVPLLVRGPGI-PAGVTVDQLVSNIDLAPTILDLA 334
                         410
                  ....*....|...
gi 1864524949 381 GGEVPQDrvIDGR 393
Cdd:cd16147   335 GAPPPSD--MDGR 345
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
21-490 1.34e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 93.78  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQ-HI----SAAsLCTPSRAAFLTGRYPVRSGMvssvgyrvlqwtGASGGLPTNETTFAKILKEKG 95
Cdd:cd16155    28 TPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE------------GGKAAIPSDDKTWPETFKKAG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  96 YATGLIGKWHLGLnCESAGDHCHHP--------LHHGF----DyfygmPLSMTGdcahwELSEK--RVDLEQKLNFLFQv 161
Cdd:cd16155    95 YRTFATGKWHNGF-ADAAIEFLEEYkdgdkpffMYVAFtaphD-----PRQAPP-----EYLDMypPETIPLPENFLPQ- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 162 lalvtltlaagkfmHlisiswmPviwsallavfllttsyFAGALIVHADcflmrnhtitEQPMRFQRvTPlilQEVKSFL 241
Cdd:cd16155   163 --------------H-------P----------------FDNGEGTVRD----------EQLAPFPR-TP---EAVRQHL 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 242 KRNklgpflllvsflhvhiplittknflgksahglYGdNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL----- 316
Cdd:cd16155   192 AEY--------------------------------YA-MITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVgshgl 238
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 317 ---ENQFANSqyggwngiykggkgmggweggIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGR 393
Cdd:cd16155   239 mgkQNLYEHS---------------------MRVPLIISGPGI-PKGKRRDALVYLQDVFPTLCELAGIEIPES--VEGK 294
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 394 DLLPLLLGTAQhsdheflMHYCERFLHAARWHQRDRGTLWKVHFVTPvfqpegagacygrkvcpcsGEKVVhhdppLLFD 473
Cdd:cd16155   295 SLLPVIRGEKK-------AVRDTLYGAYRDGQRAIRDDRWKLIIYVP-------------------GVKRT-----QLFD 343
                         490
                  ....*....|....*..
gi 1864524949 474 LSRDPSEAHVLtpASEP 490
Cdd:cd16155   344 LKKDPDELNNL--ADEP 358
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
21-380 2.36e-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.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 87.48  E-value: 2.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKL-TQHISAASLCTPSRAAFLTGRYPVRSGMVSSvGYRVLQWTGASGGLPTNETTFAKILKEKGYATG 99
Cdd:cd00016    26 TPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGN-GSADPELPSRAAGKDEDGPTIPELLKQAGYRTG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 100 LIGkwhlglncesagdhchhplhhgfdyfygmplsmtgdcahwelsekrvdleqklnflfqvlalvtltlaagkfmhlis 179
Cdd:cd00016   105 VIG----------------------------------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 180 iswmpviwsallavfllttsyfagalivhadcflmrnhtiteqpmrfqrvtplilqeVKSFLKRNKLG-PFLLLVSFLHV 258
Cdd:cd00016   108 ---------------------------------------------------------LLKAIDETSKEkPFVLFLHFDGP 130
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 259 HIPLittknFLGKSAHGLYGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLEnqfansqygGWNGIYKGGKGM 338
Cdd:cd00016   131 DGPG-----HAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDK---------GHGGDPKADGKA 196
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1864524949 339 GGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVQLA 380
Cdd:cd00016   197 DKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
21-406 6.52e-18

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: 85.48  E-value: 6.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTqHISAASLCTPSRAAFLTGRYPVRSGmVSSVGYRVLQwtgasgglpTNETTFAKILKE---KGYA 97
Cdd:cd16154    28 TPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTG-VLAVPDELLL---------SEETLLQLLIKDattAGYS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  98 TGLIGKWHLGlncesaGDHCHHPLHHGFDYFYGMPLSMTGDCAHWELSEKRVDLEQKlnflfqvlalvtlTLAAGKFMHL 177
Cdd:cd16154    97 SAVIGKWHLG------GNDNSPNNPGGIPYYAGILGGGVQDYYNWNLTNNGQTTNST-------------EYATTKLTNL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 178 iSISWM-----PviWSALLAvfllttsYFAgalivhadcflmrNHTiteqpmrfqrvtplilqevksflkrnklgPFLLL 252
Cdd:cd16154   158 -AIDWIdqqtkP--WFLWLA-------YNA-------------PHT-----------------------------PFHLP 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 253 VSFLHvhiplitTKNFLGKSAHglYGDN--------VEEMDWMVGQILDALDTEGLTNsTLIYFASDHG--------GSL 316
Cdd:cd16154   186 PAELH-------SRSLLGDSAD--IEANprpyylaaIEAMDTEIGRLLASIDEEEREN-TIIIFIGDNGtpgqvvdlPYT 255
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 317 ENQFANSQY-GGwngiykggkgmggweggIRVPGIFRWPGVlpaGRVIGEPTSLM---DVFPTVVQLAGGEVPQdrVIDG 392
Cdd:cd16154   256 RNHAKGSLYeGG-----------------INVPLIVSGAGV---ERANERESALVnatDLYATIAELAGVDAAE--IHDS 313
                         410
                  ....*....|....
gi 1864524949 393 RDLLPLLLGTAQHS 406
Cdd:cd16154   314 VSFKPLLSDVNAST 327
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
248-479 3.16e-14

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: 74.11  E-value: 3.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 248 PFLLlvsFLHVHIPLITTKNFLGKSAHGL------YGDNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHGG-SLEN-Q 319
Cdd:cd16171   166 PFAL---YLGLNLPHPYPSPSMGENFGSIrnirafYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGElAMEHrQ 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 320 FAN-SQYGGwngiykggkgmggwegGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGRDLLPL 398
Cdd:cd16171   243 FYKmSMYEG----------------SSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPL 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 399 LLGTAQHSDH-----------EFlmHYCErfLHAARWHQRDrgTLWKvhFVTpvfqpegagacYGrkvcpcSGEKVvhhd 467
Cdd:cd16171   304 LSESSIKESPsrvphpdwvlsEF--HGCN--VNASTYMLRT--NSWK--YIA-----------YA------DGNSV---- 354
                         250
                  ....*....|..
gi 1864524949 468 PPLLFDLSRDPS 479
Cdd:cd16171   355 PPQLFDLSKDPD 366
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
21-381 1.42e-09

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: 59.23  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  21 TPNIDRLAEFGVKLTQHISAASLCTPSRA--AFLTGRYPVRSGMVSSVGYRvlqwtgasgglPTNETTFAKILKEKGYAT 98
Cdd:cd16015    26 TPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK-----------LNPLPSLPSILKEQGYET 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  99 GLIgkwhlglncesagdHCHHP---------LHHGFDYFYG---MPLSMTGDcAHWELSEKrvdleqklnFLFQVLALVT 166
Cdd:cd16015    95 IFI--------------HGGDAsfynrdsvyPNLGFDEFYDledFPDDEKET-NGWGVSDE---------SLFDQALEEL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 167 LTLAAGKFMhlisiswmpviwsallaVFLLTTSyfagalivhadcflmrNHtiteqpmrfqrvtplilqevksflkrnkl 246
Cdd:cd16015   151 EELKKKPFF-----------------IFLVTMS----------------NH----------------------------- 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 247 GPFLLLVSFLHVHIPLITTKNFLGKSAHGLYgdnveEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFANSQYG 326
Cdd:cd16015   169 GPYDLPEEKKDEPLKVEEDKTELENYLNAIH-----YTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDED 243
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1864524949 327 GWNGIykggkgmggweggiRVPGIFRWPGVLPaGRVIGEPTSLMDVFPTVVQLAG 381
Cdd:cd16015   244 PLDLY--------------RTPLLIYSPGLKK-PKKIDRVGSQIDIAPTLLDLLG 283
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
281-396 1.74e-07

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 53.89  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 281 VEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSLENQFANSQYggwngiykggkgmggwEGGIRVPGIFRWPGvLPAG 360
Cdd:COG1368   423 VRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENP----------------LERYRVPLLIYSPG-LKKP 485
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1864524949 361 RVIGEPTSLMDVFPTVVQLAGGEVPQDRVIdGRDLL 396
Cdd:COG1368   486 KVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
281-378 2.17e-06

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: 50.29  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949 281 VEEMDWMVGQILDALDTEGLTNSTLIYFASDHGGSL-ENQ----FANSQYGGWNgiykggkgmggweggIRVPGIFRWPG 355
Cdd:COG3083   433 VHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnENGqnywGHNSNFSRYQ---------------LQVPLVIHWPG 497
                          90       100
                  ....*....|....*....|...
gi 1864524949 356 VLPagRVIGEPTSLMDVFPTVVQ 378
Cdd:COG3083   498 TPP--QVISKLTSHLDIVPTLMQ 518
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
10-151 2.46e-05

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 46.66  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864524949  10 RGDMLHLQHswTPNIDRLAEFGVKLTQHISAA-SLCTPSRAAFLTGRYPVRSGMVSSVGYR--------VLQWTGASGGL 80
Cdd:COG1524    35 RADLLERAH--APNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGLYPGEHGIVGNGWYDpelgrvvnSLSWVEDGFGS 112
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864524949  81 PT--NETTFAKILKEKGYATGLIGKWHLGlncESAGDHCHHPLHH-GFDYFYGMPLS--MTGDCAHWELSEKRVDL 151
Cdd:COG1524   113 NSllPVPTIFERARAAGLTTAAVFWPSFE---GSGLIDAARPYPYdGRKPLLGNPAAdrWIAAAALELLREGRPDL 185
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
279-313 6.43e-03

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 38.94  E-value: 6.43e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1864524949 279 DNVEEMDWMVGQILDALDTEGLTNSTLIYFASDHG 313
Cdd:pfam01663 189 DALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHG 223
 
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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