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Conserved domains on  [gi|530421114|ref|XP_005274578|]
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arylsulfatase L isoform X2 [Homo sapiens]

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 ...
9-506 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: 694.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTGASGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16159   27 TPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTASSGGLPPNETTFAEVLKQQGYSTAL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVNLEQKLNFLFQVLALVALTLVAGKLthLIPV 168
Cdd:cd16159  107 IGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPLFPLLTAFVLITALTIFLLLY--LGAV 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 SWMPVIWSALSAVLLLASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLILQEVASFLKRNKHGPFLLFVSFLHVHI 248
Cdd:cd16159  185 SKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLTKEAISFLERNKERPFLLVMSFLHVHT 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 249 PLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLGNTQYGGWNGIYKGGKGMGG 328
Cdd:cd16159  265 ALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLEEISVGGEYGGGNGGIYGGKKMGG 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 329 WEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLH 408
Cdd:cd16159  345 WEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLMPLLTGQEKRSPHEFLFHYCGAELH 424
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 409 AARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDLSRDPSETHILTPASEPvFYQVMERVQ 488
Cdd:cd16159  425 AVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDLSADPSESNPLDPTDEP-YQEIIKKIL 502
                        490
                 ....*....|....*...
gi 530421114 489 QAVWEHQRTLSPVPLQLD 506
Cdd:cd16159  503 EAVAEHQSSIEPVESQLS 520
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
9-506 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: 694.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTGASGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16159   27 TPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTASSGGLPPNETTFAEVLKQQGYSTAL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVNLEQKLNFLFQVLALVALTLVAGKLthLIPV 168
Cdd:cd16159  107 IGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPLFPLLTAFVLITALTIFLLLY--LGAV 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 SWMPVIWSALSAVLLLASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLILQEVASFLKRNKHGPFLLFVSFLHVHI 248
Cdd:cd16159  185 SKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLTKEAISFLERNKERPFLLVMSFLHVHT 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 249 PLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLGNTQYGGWNGIYKGGKGMGG 328
Cdd:cd16159  265 ALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLEEISVGGEYGGGNGGIYGGKKMGG 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 329 WEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLH 408
Cdd:cd16159  345 WEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLMPLLTGQEKRSPHEFLFHYCGAELH 424
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 409 AARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDLSRDPSETHILTPASEPvFYQVMERVQ 488
Cdd:cd16159  425 AVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDLSADPSESNPLDPTDEP-YQEIIKKIL 502
                        490
                 ....*....|....*...
gi 530421114 489 QAVWEHQRTLSPVPLQLD 506
Cdd:cd16159  503 EAVAEHQSSIEPVESQLS 520
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
9-470 1.65e-74

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 241.32  E-value: 1.65e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqwtGASGGLPTNETTFAKILKEKGYATGL 88
Cdd:COG3119   49 TPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTAL 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGLncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqklnflfqvlalvaltlvagklthlipv 168
Cdd:COG3119  122 FGKWHLYL------------------------------------------------------------------------ 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 swmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrtTPLILQEVASFLKRNKHG--PFLLFVSFLHV 246
Cdd:COG3119  130 -------------------------------------------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAP 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 247 HIPLITMENFLGK-----------------------SLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGS 303
Cdd:COG3119  161 HAPYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS 240
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 304 LENQlG-----NTQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrv 377
Cdd:COG3119  241 LGEH-GlrggkGTLYeGG-----------------IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED-- 300
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 378 IDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRdrgtmWKVHFvtpvfqpegagaCYGRKvcpcfgekvvhhDPP 457
Cdd:COG3119  301 LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTGR-----WKLIR------------YYDDD------------GPW 351
                        490
                 ....*....|...
gi 530421114 458 LLFDLSRDPSETH 470
Cdd:COG3119  352 ELYDLKNDPGETN 364
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
394-528 1.12e-57

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 187.91  E-value: 1.12e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  394 SDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGACYGRKVCpcfgekVVHHDPPLLFDLSRDPSETHILT 473
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530421114  474 PASePVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWC 528
Cdd:pfam14707  69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
PRK13759 PRK13759
arylsulfatase; Provisional
9-477 2.35e-29

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 120.93  E-value: 2.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssiGYrvlqwtgASGGLPTNETTFAKILKEKGYATGL 88
Cdd:PRK13759  32 TPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY-------GDVVPWNYKNTLPQEFRDAGYYTQC 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLglncesasdhchHPLH--HGFDHfygmpfSLMGDcarWELSEKRVNLEQKLNFLFQVLALVALTLVaGKLTHLI 166
Cdd:PRK13759 102 IGKMHV------------FPQRnlLGFHN------VLLHD---GYLHSGRNEDKSQFDFVSDYLAWLREKAP-GKDPDLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 167 PVSWMPVIWSAlsavlllassyfvgalivhadcflmRNHTITEQpmcfQRTTPLILQEVASFLKR-NKHGPFLLFVSFLH 245
Cdd:PRK13759 160 DIGWDCNSWVA-------------------------RPWDLEER----LHPTNWVGSESIEFLRRrDPTKPFFLKMSFAR 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 246 VHIPLITMENFL-------------------------GKSLHGLYGD---------------NVEEMDWMVGRILDTLDV 285
Cdd:PRK13759 211 PHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeeyarraraayygLITHIDHQIGRFLQALKE 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 286 EGLSNSTLIYFTSDHGgsleNQLGNTQ-------YGGwngiykggkgmggwegGIRVPGIFRWPG---VLPAGRVIGEPT 355
Cdd:PRK13759 291 FGLLDNTIILFVSDHG----DMLGDHYlfrkgypYEG----------------SAHIPFIIYDPGgllAGNRGTVIDQVV 350
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 356 SLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-TAQHSDHEFLMH-YCERFLHaarWHQRDRGT-MWkvHFVTPVFQp 432
Cdd:PRK13759 351 ELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGqYEGWRPYLHGEHaLGYSSDN---YLTDGKWKyIW--FSQTGEEQ- 422
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 530421114 433 egagacygrkvcpcfgekvvhhdpplLFDLSRDPSETHILTPASE 477
Cdd:PRK13759 423 --------------------------LFDLKKDPHELHNLSPSEK 441
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
9-506 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: 694.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTGASGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16159   27 TPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTASSGGLPPNETTFAEVLKQQGYSTAL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVNLEQKLNFLFQVLALVALTLVAGKLthLIPV 168
Cdd:cd16159  107 IGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPLFPLLTAFVLITALTIFLLLY--LGAV 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 SWMPVIWSALSAVLLLASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLILQEVASFLKRNKHGPFLLFVSFLHVHI 248
Cdd:cd16159  185 SKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLTKEAISFLERNKERPFLLVMSFLHVHT 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 249 PLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLGNTQYGGWNGIYKGGKGMGG 328
Cdd:cd16159  265 ALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLEEISVGGEYGGGNGGIYGGKKMGG 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 329 WEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLH 408
Cdd:cd16159  345 WEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLMPLLTGQEKRSPHEFLFHYCGAELH 424
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 409 AARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDLSRDPSETHILTPASEPvFYQVMERVQ 488
Cdd:cd16159  425 AVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDLSADPSESNPLDPTDEP-YQEIIKKIL 502
                        490
                 ....*....|....*...
gi 530421114 489 QAVWEHQRTLSPVPLQLD 506
Cdd:cd16159  503 EAVAEHQSSIEPVESQLS 520
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
9-470 2.32e-138

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: 405.79  E-value: 2.32e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRVLQWTGASGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16026   27 TPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPPGSKGGLPPDEITIAEVLKKAGYRTAL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGlncesasDH-CHHPLHHGFDHFYGMPFSLMGDCARWELSEKRvnleqklnflfqvlalvaltlvagklthlip 167
Cdd:cd16026  102 VGKWHLG-------HQpEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPP------------------------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 168 vswmpviwsalsavlllassyfvgalivHADCFLMRNHTITEQPMcFQRT-TPLILQEVASFLKRNKHGPFLLFVSFLHV 246
Cdd:cd16026  144 ----------------------------GPLPPLMENEEVIEQPA-DQSSlTQRYTDEAVDFIERNKDQPFFLYLAHTMP 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 247 HIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSD---------HGGSleNQL-----GNTQ 312
Cdd:cd16026  195 HVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDngpwleyggHGGS--AGPlrggkGTTW 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 313 YGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQ 392
Cdd:cd16026  273 EGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSK 335
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530421114 393 HSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGacygrkvcpcfGEKVVHHDPPLLFDLSRDPSETH 470
Cdd:cd16026  336 SPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDPG-----------GLDPTKLEPPLLYDLEEDPGETY 396
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
3-487 4.53e-120

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: 360.59  E-value: 4.53e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   3 HLHHSWTPnIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSsiGYRV-LQWTgaSGGLPTNETTFAKILKE 81
Cdd:cd16160   22 HPTQERGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG--GTRVfLPWD--IGGLPKTEVTMAEALKE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  82 KGYATGLIGKWHLGLNCESASDHCHHPLHHGFDhFYG--MPFSLMGDCARWELSekrvnleqklnflfqvlalvaltlva 159
Cdd:cd16160   97 AGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGtnLPFTNSWACDDTGRH-------------------------- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 160 gklthlipvswmpviwsalsavlllassyfvgalIVHAD---CFLMRNHTITEQPMCFQRTTPLILQEVASFLKRNKHGP 236
Cdd:cd16160  150 ----------------------------------VDFPDrsaCFLYYNDTIVEQPIQHEHLTETLVGDAKSFIEDNQENP 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 237 FLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG------------GSL 304
Cdd:cd16160  196 FFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGphveycleggstGGL 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 305 ENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPaGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLL 384
Cdd:cd16160  276 KGGKGNSWEGG-----------------IRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSIT 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 385 PLLLGTAQHSDHEFLMHYCERfLHAARWHQrdrgtmWKVHFVT---PVFQPEGAGACYGRKVCP------CFGEKVVHHD 455
Cdd:cd16160  338 DLLLGEADSPHDDILYYCCSR-LMAVRYGS------YKIHFKTqplPSQESLDPNCDGGGPLSDyivcydCEDECVTKHN 410
                        490       500       510
                 ....*....|....*....|....*....|..
gi 530421114 456 PPLLFDLSRDPSETHILTPASEPVFYQVMERV 487
Cdd:cd16160  411 PPLIFDVEKDPGEQYPLQPSVYEHMLEAVEKL 442
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
7-528 1.17e-85

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: 273.17  E-value: 1.17e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   7 SWTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYrvlqwTGASGGLPTNETTFAKILKEKGYAT 86
Cdd:cd16158   25 SSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFY-----PGSRGGLPLNETTIAEVLKTVGYQT 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  87 GLIGKWHLGLNCESAsdhcHHPLHHGFDHFYGMPFSL-MGDCArwelsekrvnleqklnflfqvlalvaltlvagKLTHL 165
Cdd:cd16158  100 AMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSHdQGPCQ--------------------------------NLTCF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 166 IPvswmpviwsalsavlllASSYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLILQEVASFL----KRNKhgPFLLFV 241
Cdd:cd16158  144 PP-----------------NIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIadnaKEGK--PFFLYY 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 242 SFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG------------GSLENQLG 309
Cdd:cd16158  205 ASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGpstmrksrggnaGLLKCGKG 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 310 NTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIgEPTSLMDVFPTVVRLAGGEVPqDRVIDGQDLLPLLLG 389
Cdd:cd16158  285 TTYEGG-----------------VREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLP-NVTLDGVDMSPILFE 345
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 390 TAQHSDHEFLMHYC----ERFLHAARWHQrdrgtmWKVHFVT---PVFQPEGAGACYGRKvcpcfgeKVVHHDPPLLFDL 462
Cdd:cd16158  346 QGKSPRQTFFYYPTspdpDKGVFAVRWGK------YKAHFYTqgaAHSGTTPDKDCHPSA-------ELTSHDPPLLFDL 412
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 463 SRDPSETHILTpaSEPVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNiwrPWLQPC----CGPFPLCWC 528
Cdd:cd16158  413 SQDPSENYNLL--GLPEYNQVLKQIQQVKERFEASMKFGESEINKGED---PALEPCckpgCTPKPSCCQ 477
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
9-473 4.41e-81

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: 257.85  E-value: 4.41e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssigYRVlQWTGASGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16142   29 TPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGL-----TTV-GLPGSPGGLPPWEPTLAELLKDAGYATAQ 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGLNCEsasdhcHHPLHHGFDHFYGMPFSLMGDcarwELSEKRVNleqklnflfqvlalvaltlvagklthlipv 168
Cdd:cd16142  102 FGKWHLGDEDG------RLPTDHGFDEFYGNLYHTIDE----EIVDKAID------------------------------ 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 swmpviwsalsavlllassyfvgalivhadcFLMRNHtiteqpmcfqrttplilqevasflKRNKhgPFLLFVSFLHVHI 248
Cdd:cd16142  142 -------------------------------FIKRNA------------------------KADK--PFFLYVNFTKMHF 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 249 PLITMENFLGKSL-HGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG-----------GSLENQLGNTQYGGW 316
Cdd:cd16142  165 PTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvwpdggyTPFRGEKGTTWEGGV 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 317 ngiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVP------QDRVIDGQDLLPLLLGT 390
Cdd:cd16142  245 -----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRHIDGVDQSPFLLGK 307
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 391 AQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVtpVFQPEGAGACYGRKVCPCfgekvvhhdpPLLFDLSRDPSETH 470
Cdd:cd16142  308 SEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTGEPFYVLTF----------PLIFNLRRDPKERY 369

                 ...
gi 530421114 471 ILT 473
Cdd:cd16142  370 DVT 372
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
9-473 3.07e-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: 255.86  E-value: 3.07e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRvlqwtgASGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16161   28 TPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT------SVGGLPLNETTLAEVLRQAGYATGM 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGLNcesasdHCHHPLHHGFDHFYGMPFSlmGDCarwELSEKRVNLeqklnflfqvlalvaltlvagklthlipv 168
Cdd:cd16161  102 IGKWHLGQR------EAYLPNSRGFDYYFGIPFS--HDS---SLADRYAQF----------------------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 swmpviwsalsavlllassyfvgalivhADCFLMRNhtiteqpmcfqrttplilqevasflkRNKHGPFLLFVSFLHVHI 248
Cdd:cd16161  142 ----------------------------ATDFIQRA--------------------------SAKDRPFFLYAALAHVHV 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 249 PLITMENFLGKSLH-GLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG-----GSLENQLGNTQY---GGWNGI 319
Cdd:cd16161  168 PLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkCELAVGPGTGDWqgnLGGSVA 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 320 YKGGKGMGgweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQhSDHEFL 399
Cdd:cd16161  248 KASTWEGG-----HREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSK-TGHRCL 321
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530421114 400 MHYCE-----RFLHAARWHQrdrgtmWKVHFVTpvfqpEGAGACygrkvCPCFGEKvVHHDPPLLFDLSRDPSETHILT 473
Cdd:cd16161  322 FHPNSgaagaGALSAVRCGD------YKAHYAT-----GGALAC-----CGSTGPK-LYHDPPLLFDLEVDPAESFPLT 383
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
9-470 1.65e-74

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 241.32  E-value: 1.65e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqwtGASGGLPTNETTFAKILKEKGYATGL 88
Cdd:COG3119   49 TPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTAL 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGLncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqklnflfqvlalvaltlvagklthlipv 168
Cdd:COG3119  122 FGKWHLYL------------------------------------------------------------------------ 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 swmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrtTPLILQEVASFLKRNKHG--PFLLFVSFLHV 246
Cdd:COG3119  130 -------------------------------------------------TDLLTDKAIDFLERQADKdkPFFLYLAFNAP 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 247 HIPLITMENFLGK-----------------------SLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGS 303
Cdd:COG3119  161 HAPYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS 240
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 304 LENQlG-----NTQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrv 377
Cdd:COG3119  241 LGEH-GlrggkGTLYeGG-----------------IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED-- 300
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 378 IDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRdrgtmWKVHFvtpvfqpegagaCYGRKvcpcfgekvvhhDPP 457
Cdd:COG3119  301 LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTGR-----WKLIR------------YYDDD------------GPW 351
                        490
                 ....*....|...
gi 530421114 458 LLFDLSRDPSETH 470
Cdd:COG3119  352 ELYDLKNDPGETN 364
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
9-506 3.62e-74

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: 242.76  E-value: 3.62e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTGAS--GGLPTNETTFAKILKEKGYAT 86
Cdd:cd16157   27 TPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTPQNivGGIPDSEILLPELLKKAGYRN 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  87 GLIGKWHLGLNCEsasdhcHHPLHHGFDHFYGMPfslmgDCARWELSEKRvnleqklnflfqvlalvaltlvagklTHLI 166
Cdd:cd16157  107 KIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NCHFGPYDNKA--------------------------YPNI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 167 PV--SWmpviwsalsavlLLASSYFVGALIvhadcflmrNHTITEQPMcfqrtTPLILQEVASFLKR--NKHGPFLLFVS 242
Cdd:cd16157  150 PVyrDW------------EMIGRYYEEFKI---------DKKTGESNL-----TQIYLQEALEFIEKqhDAQKPFFLYWA 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 243 FLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLenqLGNTQYGGWNgIYKG 322
Cdd:cd16157  204 PDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAAL---ISAPEQGGSN-GPFL 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 323 GKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLgtAQHSDHEFLMHY 402
Cdd:cd16157  280 CGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLL--NGKEKDRPIFYY 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 403 CERFLHAARWHQrdrgtmWKVHFVT----PVFQPEGAGACYGRKVCPCFGEKVVHH-DPPLLFDLSRDPSETHILTPASe 477
Cdd:cd16157  358 RGDELMAVRLGQ------YKAHFWTwsnsWEEFRKGINFCPGQNVPGVTTHNQTDHtKLPLLFHLGRDPGEKYPISFKS- 430
                        490       500
                 ....*....|....*....|....*....
gi 530421114 478 PVFYQVMERVQQAVWEHQRTLSPVPLQLD 506
Cdd:cd16157  431 AEYKQAMPRISKVVQQHQKTLVPGEPQLN 459
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
9-470 5.31e-74

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: 240.91  E-value: 5.31e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTGA-------SGGLPTNETTFAKILKE 81
Cdd:cd16144   26 TPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDNTklipppsTTRLPLEEVTIAEALKD 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  82 KGYATGLIGKWHLGLNcesasdHCHHPLHHGFDH------------FYGMPFSLMGDCARWELSEKRVNleqklnflfqv 149
Cdd:cd16144  106 AGYATAHFGKWHLGGE------GGYGPEDQGFDVniggtgnggppsYYFPPGKPNPDLEDGPEGEYLTD----------- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 150 lalvALTlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrttplilQEVASFL 229
Cdd:cd16144  169 ----RLT------------------------------------------------------------------DEAIDFI 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 230 KRNKHGPFLLFVSFLHVHIPLI----TMENFLGKSLHGLYGDN-------VEEMDWMVGRILDTLDVEGLSNSTLIYFTS 298
Cdd:cd16144  179 EQNKDKPFFLYLSHYAVHTPIQarpeLIEKYEKKKKGLRKGQKnpvyaamIESLDESVGRILDALEELGLADNTLVIFTS 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 299 DHGG-SLENQLGNTQY-----------GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVR 366
Cdd:cd16144  259 DNGGlSTRGGPPTSNAplrggkgslyeGG-----------------IRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLE 321
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 367 LAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYcerFLHAARWHQRDRGTM----WK-VHFvtpvfqpegagacygr 441
Cdd:cd16144  322 LAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFWH---FPHYHGQGGRPASAIrkgdWKlIEF---------------- 382
                        490       500       510
                 ....*....|....*....|....*....|
gi 530421114 442 kvcpcfgekvvHHDPPL-LFDLSRDPSETH 470
Cdd:cd16144  383 -----------YEDGRVeLYNLKNDIGETN 401
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
9-470 1.35e-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: 239.03  E-value: 1.35e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssiGYRVLQWTGASGgLPTNETTFAKILKEKGYATGL 88
Cdd:cd16143   27 TPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRL----KGGVLGGFSPPL-IEPDRVTLAKMLKQAGYRTAM 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGLN------CESASDHCHH----------PLHHGFDHFYGMPFSlmgdcarwelsekrvnleqklnflfQVLal 152
Cdd:cd16143  102 VGKWHLGLDwkkkdgKKAATGTGKDvdyskpikggPLDHGFDYYFGIPAS-------------------------EVL-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 153 valtlvagklthlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrttPLILQEVASFLKRN 232
Cdd:cd16143  155 ------------------------------------------------------------------PTLTDKAVEFIDQH 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 233 KHG--PFLLFVSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLGN 310
Cdd:cd16143  169 AKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPYADYKE 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 311 TQ-----------------Y-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEV 372
Cdd:cd16143  249 LEkfghdpsgplrgmkadiYeGG-----------------HRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKL 311
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 373 PQDRVIDGQDLLPLLLGTAQHSDHEFLMHycerflHAARWHQRDRGTMWKVhfvtpVFQPEGAGACYGRKvcpcfgeKVV 452
Cdd:cd16143  312 PDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSFAIRKGDWKL-----IDGTGSGGFSYPRG-------KEK 373
                        490
                 ....*....|....*....
gi 530421114 453 HHDPP-LLFDLSRDPSETH 470
Cdd:cd16143  374 LGLPPgQLYNLSTDPGESN 392
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
9-382 6.04e-59

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: 195.35  E-value: 6.04e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGmvssigyrVLQWTGASGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16022   26 TPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVGNGGGLPPDEPTLAELLKEAGYRTAL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHlglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqklnflfqvlalvaltlvagklthlipv 168
Cdd:cd16022   98 IGKWH--------------------------------------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 swmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrttplilQEVASFLKRNKHG-PFLLFVSFLHVH 247
Cdd:cd16022  103 ------------------------------------------------------DEAIDFIERRDKDkPFFLYVSFNAPH 128
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 248 IPLItmenflgkslhglYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENqlGNTQYGGWNGIYKGgkgmg 327
Cdd:cd16022  129 PPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGD--HGLRGKKGSLYEGG----- 188
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530421114 328 gweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQD 382
Cdd:cd16022  189 -----IRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
9-470 6.73e-58

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: 198.16  E-value: 6.73e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQ-HISaaSLCTPSRAAFLTGRYPVRSGMVSSIGYRVLqwtgasggLPTNETTFAKILKEKGYATG 87
Cdd:cd16146   26 TPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--------MRLDETTLAEVFKDAGYRTG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  88 LIGKWHLGLNcesasdHCHHPLHHGFDHFYGMPFSLMGDCARWELSEkrvnleqklnflfqvlalvaltlvagklthlip 167
Cdd:cd16146   96 IFGKWHLGDN------YPYRPQDRGFDEVLGHGGGGIGQYPDYWGND--------------------------------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 168 vswmpviwsalsavlllassYFvgalivhaDCFLMRNHTITE-QPMCfqrtTPLILQEVASFLKRNKHGPFLLFVSFLHV 246
Cdd:cd16146  137 --------------------YF--------DDTYYHNGKFVKtEGYC----TDVFFDEAIDFIEENKDKPFFAYLATNAP 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 247 HIPLITMEN----FLGKSLH----GLYGdNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLGN-------- 310
Cdd:cd16146  185 HGPLQVPDKyldpYKDMGLDdklaAFYG-MIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRFnagmrgkk 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 311 -TQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLL 388
Cdd:cd16146  264 gSVYeGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLK 326
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 389 GTAQHSDHEFLmhycerFLHaarWHQRDRGTMWKVHFVtpVFQPEgagacYgRKVCPcfgekvvHHDPPLLFDLSRDPSE 468
Cdd:cd16146  327 GESDPWPERTL------FTH---SGRWPPPPKKKRNAA--VRTGR-----W-RLVSP-------KGFQPELYDIENDPGE 382

                 ..
gi 530421114 469 TH 470
Cdd:cd16146  383 EN 384
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
394-528 1.12e-57

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 187.91  E-value: 1.12e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  394 SDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGACYGRKVCpcfgekVVHHDPPLLFDLSRDPSETHILT 473
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530421114  474 PASePVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWC 528
Cdd:pfam14707  69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
9-470 1.65e-57

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: 197.43  E-value: 1.65e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyRVLQWTGASGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16145   26 TPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPGGQDPLPPDDVTLAEVLKKAGYATAA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGLNcesasDHCHHPLHHGFDHFYGmpfslmgdcarwelsekrvnleqklnFLFQVLAlvaltlvagkltHlipv 168
Cdd:cd16145  100 FGKWGLGGP-----GTPGHPTKQGFDYFYG--------------------------YLDQVHA------------H---- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 swmpviwsalsavlllasSYFVGALIVHADCFLMRNHTIT-------EQPMCFQRTTPLILQEVASFLKRNKHGPFLLFV 241
Cdd:cd16145  133 ------------------NYYPEYLWRNGEKVPLPNNVIPpldegnnAGGGGGTYSHDLFTDEALDFIRENKDKPFFLYL 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 242 SFLHVHIPLIT-------MENFLGKSLHGLYGDNVEE--------MDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEn 306
Cdd:cd16145  195 AYTLPHAPLQVpddgpykYKPKDPGIYAYLPWPQPEKayaamvtrLDRDVGRILALLKELGIDENTLVVFTSDNGPHSE- 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 307 qlGNTQY--------------------GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVR 366
Cdd:cd16145  274 --GGSEHdpdffdsngplrgykrslyeGG-----------------IRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLAD 334
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 367 LAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLmhYCERFLH----AARWHQrdrgtmWKVhfvtpVFQPEGAGacygrk 442
Cdd:cd16145  335 LAGAEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFYEGggaqAVRMGG------WKA-----VRHGKKDG------ 393
                        490       500
                 ....*....|....*....|....*...
gi 530421114 443 vcpcfgekvvhhdPPLLFDLSRDPSETH 470
Cdd:cd16145  394 -------------PFELYDLSTDPGETN 408
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
9-472 3.23e-54

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: 188.16  E-value: 3.23e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVsSIGYRvlqwtgasggLPTNETTFAKILKEKGYATGL 88
Cdd:cd16034   27 TPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF-GNDVP----------LPPDAPTIADVLKDAGYRTGY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGLNCESASDHCHH----PLHHGFDHFYGMpfslmgdcarwelsekrvnleqklnflfqvlalvaltlvagklth 164
Cdd:cd16034   96 IGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY--------------------------------------------- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 165 lipvswmpviwsalsavlllassyfvgalivhaDCFLMRNHTI----TEQPMCFQRTTPLILQEVA-SFLKRNKHG--PF 237
Cdd:cd16034  131 ---------------------------------ECNHDHNNPHyyddDGKRIYIKGYSPDAETDLAiEYLENQADKdkPF 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 238 LLFVSF------------------------LHVHIPLITMENF-LGKSLHGLYGdNVEEMDWMVGRILDTLDVEGLSNST 292
Cdd:cd16034  178 ALVLSWnpphdpyttapeeyldmydpkkllLRPNVPEDKKEEAgLREDLRGYYA-MITALDDNIGRLLDALKELGLLENT 256
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 293 LIYFTSDHG---GSLENQLGNTQYGGwngiykggkgmggwegGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAG 369
Cdd:cd16034  257 IVVFTSDHGdmlGSHGLMNKQVPYEE----------------SIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCG 320
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 370 GEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTM----WKvhFVtpvfqpegagacygrkvcp 445
Cdd:cd16034  321 LPIPDT--VEGRDLSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVrtdrYT--YV------------------- 377
                        490       500
                 ....*....|....*....|....*..
gi 530421114 446 cfgekVVHHDPPLLFDLSRDPSETHIL 472
Cdd:cd16034  378 -----RDKNGPWLLFDNEKDPYQLNNL 399
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
9-412 6.43e-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: 183.95  E-value: 6.43e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGMVSsigyrvlqwtgasGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16151   26 TPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYVVF-------------GYLDPKQKTFGHLLKDAGYATAI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGLNcESASDHchhPLHHGFDHFygmpfslmgdCArWELSEKRVNLEQKLNFLFQVLAlvaltlvaGKLTHLIPV 168
Cdd:cd16151   92 AGKWQLGGG-RGDGDY---PHEFGFDEY----------CL-WQLTETGEKYSRPATPTFNIRN--------GKLLETTEG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 SWMPVIWSAlsavlllassyfvgalivhadcFLMRnhtiteqpmcfqrttplilqevasFLKRNKHGPFLLFVSFLHVHI 248
Cdd:cd16151  149 DYGPDLFAD----------------------FLID------------------------FIERNKDQPFFAYYPMVLVHD 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 249 PL----------ITMENFLGKSLHglYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG--GSLENQLGNTQY-GG 315
Cdd:cd16151  183 PFvptpdspdwdPDDKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGthRPITSRTNGREVrGG 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 316 wngiykggkGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLG-TAQHS 394
Cdd:cd16151  261 ---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGkTGSPR 331
                        410       420
                 ....*....|....*....|....*
gi 530421114 395 DHEFLMHY-------CERFLHAARW 412
Cdd:cd16151  332 REWIYWYYrnphkkfGSRFVRTKRY 356
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
9-470 3.45e-52

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: 182.36  E-value: 3.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssiGYRVLqWTGASGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16029   26 TPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGM----QHGVI-LAGEPYGLPLNETLLPQYLKELGYATHL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGlncesasdHCHH---PLHHGFDHFYGMpFSLMGDcarwelsekrvnleqklnflfqvlalvaltlvagkltHL 165
Cdd:cd16029  100 VGKWHLG--------FYTWeytPTNRGFDSFYGY-YGGAED-------------------------------------YY 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 166 IPVSWMPVIWSalsavlllassyfvgalivhaDCFLMRNHTIT-EQPMCFqrTTPLILQEVASFLKR-NKHGPFLLFVSF 243
Cdd:cd16029  134 THTSGGANDYG---------------------NDDLRDNEEPAwDYNGTY--STDLFTDRAVDIIENhDPSKPLFLYLAF 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 244 LHVHIPL------ITMENFLGKSLHG----LYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLG---- 309
Cdd:cd16029  191 QAVHAPLqvppeyADPYEDKFAHIKDedrrTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGgsny 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 310 ------NTQY-GGwngiykggkgmggweggIRVPGiFRWPGVLP--AGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDG 380
Cdd:cd16029  271 plrggkNTLWeGG-----------------VRVPA-FVWSPLLPpkRGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDG 332
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 381 QDLLPLLLGTAQHSDHEFLmhycerflhaarwHQRDRgtmwkvhfvtPVFQPEGAGACYGRKvcpcfgeKVVHHDPplLF 460
Cdd:cd16029  333 VDQWDALSGGAPSPRTEIL-------------LNIDD----------ITRTTGGAAIRVGDW-------KLIVGKP--LF 380
                        490
                 ....*....|
gi 530421114 461 DLSRDPSETH 470
Cdd:cd16029  381 NIENDPCERN 390
Sulfatase pfam00884
Sulfatase;
9-369 2.44e-48

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 169.53  E-value: 2.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114    9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqwtgasGGLPTNETTFAKILKEKGYATGL 88
Cdd:pfam00884  26 TPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP----------VGLPRTEPSLPDLLKRAGYNTGA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   89 IGKWHLGLNCESAsdhchhPLHHGFDHFYGmpfslmgdcaRWELSEKRVNLEqklnflfqvlalvaltlvagklthlipv 168
Cdd:pfam00884  96 IGKWHLGWYNNQS------PCNLGFDKFFG----------RNTGSDLYADPP---------------------------- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  169 swmpviwsalsavlllassyfvgalivhadcflmRNHTITEQPMCF-QRTTPLILQevasfLKRNKHGPFLLFVSFLHVH 247
Cdd:pfam00884 132 ----------------------------------DVPYNCSGGGVSdEALLDEALE-----FLDNNDKPFFLVLHTLGSH 172
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  248 IPL------------ITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLGNTQYGG 315
Cdd:pfam00884 173 GPPyypdrypekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGK 252
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530421114  316 WNgiykggkgmGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAG 369
Cdd:pfam00884 253 YD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
9-496 1.88e-46

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: 166.53  E-value: 1.88e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssIGYRVLQWTgasggLPTNETTFAKILKEKGYATGL 88
Cdd:cd16027   25 TPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---HGLRSRGFP-----LPDGVKTLPELLREAGYYTGL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLglNCESASDHCHHPLHHGFDHFYGMPFslMGDCARWElseKRVNLEQKlnFLFQVlalvaltlvAGKLTHlipV 168
Cdd:cd16027   97 IGKTHY--NPDAVFPFDDEMRGPDDGGRNAWDY--ASNAADFL---NRAKKGQP--FFLWF---------GFHDPH---R 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 SWMPVIWSAL----SAVLLlaSSYFVgalivhaDcflmrnhtiteqpmcfqrtTPLILQEVASFLkrnkhgpfllfvsfl 244
Cdd:cd16027  156 PYPPGDGEEPgydpEKVKV--PPYLP-------D-------------------TPEVREDLADYY--------------- 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 245 hvhiplitmenflgkslhglygDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLGNTQYGGwngiykggk 324
Cdd:cd16027  193 ----------------------DEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFPRAKGTLYDSG--------- 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 325 gmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-TAQHSDHEFLMH-- 401
Cdd:cd16027  242 --------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGeKDPGRDYVFAERdr 311
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 402 -----YCERFLHAARWHqrdrgtmwkvhfvtpvfqpegagacYgrkvcpcfgekVVHHDPPLLFDLSRDPSETHILtpAS 476
Cdd:cd16027  312 hdetyDPIRSVRTGRYK-------------------------Y-----------IRNYMPEELYDLKNDPDELNNL--AD 353
                        490       500
                 ....*....|....*....|
gi 530421114 477 EPVFYQVMERVQQAVWEHQR 496
Cdd:cd16027  354 DPEYAEVLEELRAALDAWMK 373
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
9-489 7.08e-43

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: 158.08  E-value: 7.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqwTGASGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16031   28 TPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVT----------DNNGPLFDASQPTYPKLLRKAGYQTAF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGLNCESASDhchhplhhGFDHFYGMP---------FSLMGDCARWELSEKRVNLEQKLNFL--------Fqvla 151
Cdd:cd16031   98 IGKWHLGSGGDLPPP--------GFDYWVSFPgqgsyydpeFIENGKRVGQKGYVTDIITDKALDFLkerdkdkpF---- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 152 lvALTlVAGKLTHLipvSWMPViwsalsavlllassyfvgalIVHADcfLMRNHTITE-----------QPMCFQRTTPL 220
Cdd:cd16031  166 --CLS-LSFKAPHR---PFTPA--------------------PRHRG--LYEDVTIPEpetfddddyagRPEWAREQRNR 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 221 I-LQEVASFLKRNKHGpfllfvsflhvhiplITMENFLGkSLHGlygdnveeMDWMVGRILDTLDVEGLSNSTLIYFTSD 299
Cdd:cd16031  218 IrGVLDGRFDTPEKYQ---------------RYMKDYLR-TVTG--------VDDNVGRILDYLEEQGLADNTIIIYTSD 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 300 HGgsleNQLGNTQYGG-WNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvI 378
Cdd:cd16031  274 NG----FFLGEHGLFDkRL----------MYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--M 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 379 DGQDLLPLLLGTAQHS-DHEFLMHYCE--RFLHAARWH--QRDRgtmWK-VHFvtpvfqpegagacygrkvcpcfgekvv 452
Cdd:cd16031  338 QGRSLLPLLEGEKPVDwRKEFYYEYYEepNFHNVPTHEgvRTER---YKyIYY--------------------------- 387
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 530421114 453 HHDPPL--LFDLSRDPSETH--ILTPASEPVFYQVMERVQQ 489
Cdd:cd16031  388 YGVWDEeeLYDLKKDPLELNnlANDPEYAEVLKELRKRLEE 428
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
6-466 1.63e-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: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 151.54  E-value: 1.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   6 HSW--TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRsgmvssIGYrvlqWTGASGgLPTNETTFAKILKEKG 83
Cdd:cd16037   21 HPVvrTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHE------TGV----WDNADP-YDGDVPSWGHALRAAG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  84 YATGLIGKWHLGLNCEsasdhchhplHHGFDHfygmpfslmgdcarwelsekrvnleqklnflfqvlalvaltlvagklt 163
Cdd:cd16037   90 YETVLIGKLHFRGEDQ----------RHGFRY------------------------------------------------ 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 164 hlipvswmpviwsalsavlllassyfvgalivhaDcflmRNhtiteqpmcfqrttplILQEVASFLKRNKH--GPFLLFV 241
Cdd:cd16037  112 ----------------------------------D----RD----------------VTEAAVDWLREEAAddKPWFLFV 137
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 242 SFLHVHIPLITMENFLGKSLHGL---YGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLG-------NT 311
Cdd:cd16037  138 GFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHG----DMLGerglwgkST 213
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 312 QYggwngiykggkgmggwEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRviDGQDLLPLLLGTA 391
Cdd:cd16037  214 MY----------------EESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAPPPPDL--DGRSLLPLAEGPD 274
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 392 QHSDHEFlmhyCErfLHAARwhQRDRGTM-----WK-VHFVtpvfqpegagacygrkvcpcfgekvvhHDPPLLFDLSRD 465
Cdd:cd16037  275 DPDRVVF----SE--YHAHG--SPSGAFMlrkgrWKyIYYV---------------------------GYPPQLFDLEND 319

                 .
gi 530421114 466 P 466
Cdd:cd16037  320 P 320
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
9-470 4.46e-40

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: 149.90  E-value: 4.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQ-HisAASLCTPSRAAFLTGRYPVRSGMvSSIGYRVLQWTGASGGLPTNETTFAKILKEKGYATG 87
Cdd:cd16025   27 TPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGKPGYEGYLPDSAATIAEVLKDAGYHTY 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  88 LIGKWHLGLN----CESASDH-----------------------CHHPLH---------HG-FDhfygmpfslMGdcarW 130
Cdd:cd16025  104 MSGKWHLGPDdyysTDDLTDKaieyideqkapdkpfflylafgaPHAPLQapkewidkyKGkYD---------AG----W 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 131 E-LSEKRvnLE-QKlnflfqvlalvALTLVAG--KLTHLIPvsWMPViWSALSAvlllassyfvgalivhadcflmrnht 206
Cdd:cd16025  171 DaLREER--LErQK-----------ELGLIPAdtKLTPRPP--GVPA-WDSLSP-------------------------- 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 207 itEQPMCFQRttpliLQEV-ASFlkrnkhgpfllfvsflhvhiplitmenflgkslhglygdnVEEMDWMVGRILDTLDV 285
Cdd:cd16025  209 --EEKKLEAR-----RMEVyAAM----------------------------------------VEHMDQQIGRLIDYLKE 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 286 EGLSNSTLIYFTSDHGGSLEN---QLGNTQY---------GGwngiykggkgmggweggIRVPGIFRWP-GVLPAGRVIG 352
Cdd:cd16025  242 LGELDNTLIIFLSDNGASAEPgwaNASNTPFrlykqasheGG-----------------IRTPLIVSWPkGIKAKGGIRH 304
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 353 EPTSLMDVFPTVVRLAGGEVPQDRV------IDGQDLLPLLLGTAQHSDHEFLmhYCERFLHAARWHQRdrgtmWKVhfv 426
Cdd:cd16025  305 QFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRTQ--YFELFGNRAIRKGG-----WKA--- 374
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 530421114 427 tpvfqpegagacygrkvcpcfgekVVHHDPPL------LFDLSRDPSETH 470
Cdd:cd16025  375 ------------------------VALHPPPGwgdqweLYDLAKDPSETH 400
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
9-493 1.51e-37

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: 143.13  E-value: 1.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqWTGA-SGGLPTNETTFAKILKEKGYATG 87
Cdd:cd16033   26 TPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVE-----NAGAySRGLPPGVETFSEDLREAGYRNG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  88 LIGKWHLGLNCESASDHC--HHPLHHGFDHFYgmpfslmGDCARWELSEkrvnLEQKlnflfqvlalvaltlvaGKlthl 165
Cdd:cd16033  101 YVGKWHVGPEETPLDYGFdeYLPVETTIEYFL-------ADRAIEMLEE----LAAD-----------------DK---- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 166 iPvsWMpvIWSAlsavlllassyFVGAlivHADCFLmrnhtitEQPMcFQRTTPLILQEVASF---------LKRNKHGP 236
Cdd:cd16033  149 -P--FF--LRVN-----------FWGP---HDPYIP-------PEPY-LDMYDPEDIPLPESFaddfedkpyIYRRERKR 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 237 FLLFVSFLHVHIPLITmeNFLGkslhglygdNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENQlgntqyGGW 316
Cdd:cd16033  202 WGVDTEDEEDWKEIIA--HYWG---------YITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAH------RLW 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 317 NGIYKGGKGMGgweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGT------ 390
Cdd:cd16033  265 DKGPFMYEETY------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK--VDGRSLLPLLRGEqpedwr 336
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 391 ----AQHSDHEFLmhYCERFLHAARWHQrdrgtmwkvhfvtpVFQPEGagacygrkvcpcFGEkvvhhdpplLFDLSRDP 466
Cdd:cd16033  337 devvTEYNGHEFY--LPQRMVRTDRYKY--------------VFNGFD------------IDE---------LYDLESDP 379
                        490       500
                 ....*....|....*....|....*..
gi 530421114 467 SETHILtpASEPVFYQVMERVQQAVWE 493
Cdd:cd16033  380 YELNNL--IDDPEYEEILREMRTRLYE 404
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
5-385 6.05e-36

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: 134.98  E-value: 6.05e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   5 HHSWTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssigyrvLQWTGASGGLPTNETTFAKILKEKGY 84
Cdd:cd16148   22 DRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP-------------FYHGVWGGPLEPDDPTLAEILRKAGY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  85 ATGLIgkwhlglncesaSDHCHHPLHHGFDH--FYGMPFSLMGDCARWELSEkrvnleqklnflfqvlalvaltlvagkl 162
Cdd:cd16148   89 YTAAV------------SSNPHLFGGPGFDRgfDTFEDFRGQEGDPGEEGDE---------------------------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 163 thlipvswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrTTPLILQEVASFLKRNKHG-PFLLFV 241
Cdd:cd16148  129 ------------------------------------------------------RAERVTDRALEWLDRNADDdPFFLFL 154
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 242 SFLHVHIPLitmenflgkslhgLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLeNQLGNTQYGGWNgiyk 321
Cdd:cd16148  155 HYFDPHEPY-------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEF-GEHGLYWGHGSN---- 216
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530421114 322 ggkgmgGWEGGIRVPGIFRWPGVLPAGRvIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLP 385
Cdd:cd16148  217 ------LYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SDGRSLLP 271
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
9-466 1.41e-33

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: 130.01  E-value: 1.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTGASGgLPTNETTFAKILKEKGYATGL 88
Cdd:cd16032   26 TPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA----------YDNAAE-FPADIPTFAHYLRAAGYRTAL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLglncesasdhCHHPLHHGFDHfygmpfslmgDcarwelsekrvnlEQklnflfqvlalvaltlvagklthlipv 168
Cdd:cd16032   95 SGKMHF----------VGPDQLHGFDY----------D-------------EE--------------------------- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 swmpVIWSALSAVLLLAssyfvgalivhadcflmRNHTiteqpmcfqrttplilqevasflKRnkhgPFLLFVSFLHVHI 248
Cdd:cd16032  115 ----VAFKAVQKLYDLA-----------------RGED-----------------------GR----PFFLTVSFTHPHD 146
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 249 PLITMENFLG----KSLHGLYGdNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGntQYGGWngiykggK 324
Cdd:cd16032  147 PYVIPQEYWDlyvrRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHG----DMLG--ERGLW-------Y 212
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 325 GMGGWEGGIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRV-IDGQDLLPLLLGTAQHSDHEFLMHYC 403
Cdd:cd16032  213 KMSFFEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpLDGRSLLPLLEGGDSGGEDEVISEYL 291
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 404 ErflhaarwhqrdrgtmwkvhfvtpvfqpEGAGAcygrkvcPCF-----GEKVVH--HDPPLLFDLSRDP 466
Cdd:cd16032  292 A----------------------------EGAVA-------PCVmirrgRWKFIYcpGDPDQLFDLEADP 326
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
9-496 1.59e-32

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: 129.69  E-value: 1.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqWTGASggLPTNETTFAKILKEKGYATGL 88
Cdd:cd16028   26 TPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV---------WNGTP--LDARHLTLALELRKAGYDPAL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHL-----GLNCESASDHCHHPLHHGFDHFYGMPFslmgdcARWELSEKRVNLEQKLNFLfqvlalvalTLVAGK-- 161
Cdd:cd16028   95 FGYTDTspdprGLAPLDPRLLSYELAMPGFDPVDRLDE------YPAEDSDTAFLTDRAIEYL---------DERQDEpw 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 162 ---LTHLIPvSWmPVIWSALSAVLLLASSyfVGALIvhadcflmRNHTITEQpmcfQRTTPLIlqevASFLKRNKHGpfl 238
Cdd:cd16028  160 flhLSYIRP-HP-PFVAPAPYHALYDPAD--VPPPI--------RAESLAAE----AAQHPLL----AAFLERIESL--- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 239 lfvSFLHVHIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQYGGwng 318
Cdd:cd16028  217 ---SFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG----EQLGDHWLWG--- 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 319 iykggkGMGGWEGGIRVPGIFRWPGVL---PAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG------ 389
Cdd:cd16028  287 ------KDGFFDQAYRVPLIVRDPRREadaTRGQVVDAFTESVDVMPTILDWLGGEIPHQ--CDGRSLLPLLAGaqpsdw 358
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 390 -TAQHSDHEFlmhycerFLHAARWHQRDRGTmwkvhfvtpvfQPEGAGACYGRkvcpcfGE--KVVHHD--PPLLFDLSR 464
Cdd:cd16028  359 rDAVHYEYDF-------RDVSTRRPQEALGL-----------SPDECSLAVIR------DErwKYVHFAalPPLLFDLKN 414
                        490       500       510
                 ....*....|....*....|....*....|..
gi 530421114 465 DPSETHILtpASEPVFYQVMERVQQAVWEHQR 496
Cdd:cd16028  415 DPGELRDL--AADPAYAAVVLRYAQKLLSWRM 444
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
9-385 2.65e-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: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 124.66  E-value: 2.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTGASGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16149   26 TPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTKKPEGYLEGQTTLPEVLQDAGYRCGL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLGlncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqklnflfqvlalvaltlvagklthlipv 168
Cdd:cd16149  106 SGKWHLG------------------------------------------------------------------------- 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 swmpviwsalsavlllassyfvgaliVHADCFLMRNHtiteqpmcfqrttplilqevasflKRNKhgPFLLFVSFLHVHI 248
Cdd:cd16149  113 --------------------------DDAADFLRRRA------------------------EAEK--PFFLSVNYTAPHS 140
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 249 PlitmenflgkslHGlYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLenqlgnTQYGGW---------NGI 319
Cdd:cd16149  141 P------------WG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNM------GHHGIWgkgngtfplNMY 201
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530421114 320 YKGgkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLP 385
Cdd:cd16149  202 DNS----------VKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPGRSFAD 257
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
9-489 4.45e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 123.88  E-value: 4.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRvlqwtgASGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16152   27 TPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR------NGIPLPADEKTLAHYFRDAGYETGY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqklnflfqvlalvaltlvAGklthlipv 168
Cdd:cd16152   96 VGKWHL----------------------------------------------------------------AG-------- 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 swmpviwsalsavlllassYFVGALIVHADCFLMrnhtiteqpmcfqrttplilqevasflKRNKHGPFLLFVSFLHVHi 248
Cdd:cd16152  104 -------------------YRVDALTDFAIDYLD---------------------------NRQKDKPFFLFLSYLEPH- 136
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 249 plitMEN------------------FLGKSLHGLYGD----------NVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDH 300
Cdd:cd16152  137 ----HQNdrdryvapegsaerfanfWVPPDLAALPGDwaeelpdylgCCERLDENVGRIRDALKELGLYDNTIIVFTSDH 212
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 301 GGSLENQlgNTQYggwngiykggkGMGGWEGGIRVPGIFRWPGVLpAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDG 380
Cdd:cd16152  213 GCHFRTR--NAEY-----------KRSCHESSIRVPLVIYGPGFN-GGGRVEELVSLIDLPPTLLDAAGIDVPEE--MQG 276
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 381 QDLLPLLLGTAQHSDHEFLMHYCE----RFLHAARW----HQRDRGtmWKVHFVTPVFQPEgagacygrkvcpcfgekvv 452
Cdd:cd16152  277 RSLLPLVDGKVEDWRNEVFIQISEsqvgRAIRTDRWkysvAAPDKD--GWKDSGSDVYVED------------------- 335
                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 530421114 453 hhdppLLFDLSRDPSETHILtpASEPVFYQVMERVQQ 489
Cdd:cd16152  336 -----YLYDLEADPYELVNL--IGRPEYREVAAELRE 365
PRK13759 PRK13759
arylsulfatase; Provisional
9-477 2.35e-29

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 120.93  E-value: 2.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssiGYrvlqwtgASGGLPTNETTFAKILKEKGYATGL 88
Cdd:PRK13759  32 TPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY-------GDVVPWNYKNTLPQEFRDAGYYTQC 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHLglncesasdhchHPLH--HGFDHfygmpfSLMGDcarWELSEKRVNLEQKLNFLFQVLALVALTLVaGKLTHLI 166
Cdd:PRK13759 102 IGKMHV------------FPQRnlLGFHN------VLLHD---GYLHSGRNEDKSQFDFVSDYLAWLREKAP-GKDPDLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 167 PVSWMPVIWSAlsavlllassyfvgalivhadcflmRNHTITEQpmcfQRTTPLILQEVASFLKR-NKHGPFLLFVSFLH 245
Cdd:PRK13759 160 DIGWDCNSWVA-------------------------RPWDLEER----LHPTNWVGSESIEFLRRrDPTKPFFLKMSFAR 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 246 VHIPLITMENFL-------------------------GKSLHGLYGD---------------NVEEMDWMVGRILDTLDV 285
Cdd:PRK13759 211 PHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgeeyarraraayygLITHIDHQIGRFLQALKE 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 286 EGLSNSTLIYFTSDHGgsleNQLGNTQ-------YGGwngiykggkgmggwegGIRVPGIFRWPG---VLPAGRVIGEPT 355
Cdd:PRK13759 291 FGLLDNTIILFVSDHG----DMLGDHYlfrkgypYEG----------------SAHIPFIIYDPGgllAGNRGTVIDQVV 350
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 356 SLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-TAQHSDHEFLMH-YCERFLHaarWHQRDRGT-MWkvHFVTPVFQp 432
Cdd:PRK13759 351 ELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGqYEGWRPYLHGEHaLGYSSDN---YLTDGKWKyIW--FSQTGEEQ- 422
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 530421114 433 egagacygrkvcpcfgekvvhhdpplLFDLSRDPSETHILTPASE 477
Cdd:PRK13759 423 --------------------------LFDLKKDPHELHNLSPSEK 441
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
9-396 4.12e-28

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: 116.52  E-value: 4.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYrvlqWTGASGglptNETTFAKILKEKGYATGL 88
Cdd:cd16030   27 TPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSY----FRKVAP----DAVTLPQYFKENGYTTAG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHlglncesasdhchhplHHGFDHFYGMPFSlmgdcarWELSEKRVNLEQKLNFLFQVLALVALTLVAGKLTHLIPV 168
Cdd:cd16030   99 VGKIF----------------HPGIPDGDDDPAS-------WDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 --SWMPVIWSALSAVLLLAS------SYFVGA--------LIVHADCFLMRNHTITEQPMCFQRT-TPLI----LQEVas 227
Cdd:cd16030  156 pdEAYPDGKVADEAIEQLRKlkdsdkPFFLAVgfykphlpFVAPKKYFDLYPLESIPLPNPFDPIdLPEVawndLDDL-- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 228 flkRNKHGPFLLFVSFLHVHIPlitmENFLGKSLHGLYGdNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGslenQ 307
Cdd:cd16030  234 ---PKYGDIPALNPGDPKGPLP----DEQARELRQAYYA-SVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGW----H 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 308 LGntQYGGW---------NgiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGgeVPQDRVI 378
Cdd:cd16030  302 LG--EHGHWgkhtlfeeaT----------------RVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCL 361
                        410
                 ....*....|....*...
gi 530421114 379 DGQDLLPLLLGTAQHSDH 396
Cdd:cd16030  362 EGKSLVPLLKNPSAKWKD 379
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
10-402 6.65e-25

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: 104.98  E-value: 6.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  10 PNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVlQWTgasggLPTNETTFAKILKEKGYATGLI 89
Cdd:cd16035   27 PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPM-QPL-----LSPDVPTLGHMLRAAGYYTAYK 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  90 GKWHLglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnleqklnflfqvlalvaltlvagklthlipvs 169
Cdd:cd16035  101 GKWHL--------------------------------------------------------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 170 wmpviwsalsavlllaSSYFVGALivhadcflMRNHTITEQPMCFqrttpliLQEVASflKRNKHGPFLLFVSFL--H-V 246
Cdd:cd16035  106 ----------------SGAAGGGY--------KRDPGIAAQAVEW-------LRERGA--KNADGKPWFLVVSLVnpHdI 152
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 247 HIPLITMENFlgKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG------GSLENqlGNTQYGgwngiy 320
Cdd:cd16035  153 MFPPDDEERW--RRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGemggahGLRGK--GFNAYE------ 222
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 321 kggkgmggweGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVID----GQDLLPLLLGTAQHSDH 396
Cdd:cd16035  223 ----------EALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATEApplpGRDLSPLLTDADADAVR 292

                 ....*..
gi 530421114 397 E-FLMHY 402
Cdd:cd16035  293 DgILFTY 299
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
14-381 2.97e-23

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: 101.86  E-value: 2.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  14 RLAEDGVKLTQHISAASLCTPSRAAFLTGRYP----VRSGMVSSIGYRVLQWTGAsgglptNETTFAKILKEKGYATGLI 89
Cdd:cd16147   28 LLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgVTNNSPPGGGYPKFWQNGL------ERSTLPVWLQEAGYRTAYA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  90 GKWhlgLN-CESASDHCHHPLhhGFDHFYGMPFslmgdcarwelsekrvnleqklNFLFQVLALVALTLVAGklthliPV 168
Cdd:cd16147  102 GKY---LNgYGVPGGVSYVPP--GWDEWDGLVG----------------------NSTYYNYTLSNGGNGKH------GV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 169 SWmpviwsalsavlllASSYFvgalivhadcflmrnhtiteqpmcfqrtTPLILQEVASFLKR--NKHGPFLLFVSFLHV 246
Cdd:cd16147  149 SY--------------PGDYL----------------------------TDVIANKALDFLRRaaADDKPFFLVVAPPAP 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 247 HIPLI----TMENFLGKSLHGLYG---------------------DNVEEMDW--------------MVGRILDTLDVEG 287
Cdd:cd16147  187 HGPFTpaprYANLFPNVTAPPRPPpnnpdvsdkphwlrrlpplnpTQIAYIDElyrkrlrtlqsvddLVERLVNTLEATG 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 288 LSNSTLIYFTSDHG---GSLENQLGNTQ-YggwngiykggkgmggwEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPT 363
Cdd:cd16147  267 QLDNTYIIYTSDNGyhlGQHRLPPGKRTpY----------------EEDIRVPLLVRGPGI-PAGVTVDQLVSNIDLAPT 329
                        410
                 ....*....|....*...
gi 530421114 364 VVRLAGGEVPQDrvIDGQ 381
Cdd:cd16147  330 ILDLAGAPPPSD--MDGR 345
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
9-486 7.11e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 100.33  E-value: 7.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQ-HI----SAAsLCTPSRAAFLTGRYPVRSGMvssigyrvlqwtGASGGLPTNETTFAKILKEKG 83
Cdd:cd16155   28 TPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE------------GGKAAIPSDDKTWPETFKKAG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  84 YATGLIGKWHLGLnCESASDHCHHP--------LHHGFDH---FYGMPFSLMgdcarwelseKRVNLEqklnflfqvlal 152
Cdd:cd16155   95 YRTFATGKWHNGF-ADAAIEFLEEYkdgdkpffMYVAFTAphdPRQAPPEYL----------DMYPPE------------ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 153 valtlvagklTHLIPVSWMPViwsalsavlllassY-FVGALIVHADcflmrnhtitEQPMCFQRTTplilQEVASFLKR 231
Cdd:cd16155  152 ----------TIPLPENFLPQ--------------HpFDNGEGTVRD----------EQLAPFPRTP----EAVRQHLAE 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 232 NkhgpfllfvsflhvhiplitmenflgkslhglYGdNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG------GSLE 305
Cdd:cd16155  194 Y--------------------------------YA-MITHLDAQIGRILDALEASGELDNTIIVFTSDHGlavgshGLMG 240
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 306 NQlgNTQYGGWngiykggkgmggweggiRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLP 385
Cdd:cd16155  241 KQ--NLYEHSM-----------------RVPLIISGPGI-PKGKRRDALVYLQDVFPTLCELAGIEIPES--VEGKSLLP 298
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 386 LLLG-TAQHSDHEFLMhycerFLHAARWHQRDRgtmWKVHFVTPvfqpegagacygrkvcpcfGEKVVhhdppLLFDLSR 464
Cdd:cd16155  299 VIRGeKKAVRDTLYGA-----YRDGQRAIRDDR---WKLIIYVP-------------------GVKRT-----QLFDLKK 346
                        490       500
                 ....*....|....*....|..
gi 530421114 465 DPSETHILtpASEPVFYQVMER 486
Cdd:cd16155  347 DPDELNNL--ADEPEYQERLKK 366
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
6-470 1.24e-22

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 100.39  E-value: 1.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   6 HSWTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYP-VRsgmvssiGYRVLQWTgasggLPTNETTFAKILKEKGY 84
Cdd:cd16150   23 AAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPhVN-------GHRTLHHL-----LRPDEPNLLKTLKDAGY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  85 ATGLIGKWHLGLNCESASDHChhplhhgfdhfygmpfslmgdcarwelSEKRVNLEQKLNFLFQvlalvaltlvagkltH 164
Cdd:cd16150   91 HVAWAGKNDDLPGEFAAEAYC---------------------------DSDEACVRTAIDWLRN---------------R 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 165 LIPVSWmpviwsalsaVLLLASSY----FVgaliVHADCFLMrnhtITEQPMCFQRTTPLILQEVASFLK-RNKHGpfll 239
Cdd:cd16150  129 RPDKPF----------CLYLPLIFphppYG----VEEPWFSM----IDREKLPPRRPPGLRAKGKPSMLEgIEKQG---- 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 240 FVSflhvhiplITMENFlgKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHG-------------GSLEN 306
Cdd:cd16150  187 LDR--------WSEERW--RELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGdytgdyglvekwpNTFED 256
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 307 QLgntqyggwngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVRLAGgeVPQDRVIDGQDLLPL 386
Cdd:cd16150  257 CL------------------------TRVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAG--IPLSHTHFGRSLLPV 309
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 387 LLG-TAQHSDHEFlmhyCE-RFLHAARWHqrdrgtMWKVHFVTPVFQPEG----AGACYGRKVcpcfgeKVVHHD----- 455
Cdd:cd16150  310 LAGeTEEHRDAVF----SEgGRLHGEEQA------MEGGHGPYDLKWPRLlqqeEPPEHTKAV------MIRTRRykyvy 373
                        490
                 ....*....|....*....
gi 530421114 456 ----PPLLFDLSRDPSETH 470
Cdd:cd16150  374 rlyePDELYDLEADPLELH 392
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
9-387 8.26e-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: 98.22  E-value: 8.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTGaSGGLPTNETTFAKILKEKGYATGL 88
Cdd:cd16156   26 TPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------WTN-CMALGDNVKTIGQRLSDNGIHTAY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  89 IGKWHL------GLN-CESASDHchhplhhgfDHFYGMPFSLMgdcarwELSEKRVnleqklnflfqvlalvaltlvagk 161
Cdd:cd16156   95 IGKWHLdggdyfGNGiCPQGWDP---------DYWYDMRNYLD------ELTEEER------------------------ 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 162 lthlipvswmpVIWSalsavLLLASSYfvgalivhadcflmrNHTITEQPMCFQRTTPLILQevasFLKRNKHGPFLLFV 241
Cdd:cd16156  136 -----------RKSR-----RGLTSLE---------------AEGIKEEFTYGHRCTNRALD----FIEKHKDEDFFLVV 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 242 SFLHVHIPLI------TM-------------ENFLGKSLH------GLYGDNVEEM--------------DWMVGRILDT 282
Cdd:cd16156  181 SYDEPHHPFLcpkpyaSMykdfefpkgenayDDLENKPLHqrlwagAKPHEDGDKGtikhplyfgcnsfvDYEIGRVLDA 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 283 LDvEGLSNSTLIYfTSDHGGSLENQL----GNTQYggwngiykggkgmggwEGGIRVPGIFRWPGVLPAGRVIGEPTSLM 358
Cdd:cd16156  261 AD-EIAEDAWVIY-TSDHGDMLGAHKlwakGPAVY----------------DEITNIPLIIRGKGGEKAGTVTDTPVSHI 322
                        410       420
                 ....*....|....*....|....*....
gi 530421114 359 DVFPTVVRLAGgeVPQDRVIDGQDLLPLL 387
Cdd:cd16156  323 DLAPTILDYAG--IPQPKVLEGESILATI 349
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
4-383 1.18e-21

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


Pssm-ID: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 95.13  E-value: 1.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   4 LHHSWTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYrvlqWTGASGGLPtnetTFAKILKEKG 83
Cdd:cd16153   32 LGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFEAA----HPALDHGLP----TFPEVLKKAG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  84 YATGLIGKWHlglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnLEQKLNFLFQvlALVALTLVAGKlt 163
Cdd:cd16153  104 YQTASFGKSH---------------------------------------------LEAFQRYLKN--ANQSYKSFWGK-- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 164 hlipVSWMPviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrttplilqevasflKRNKhgPFLLFVSF 243
Cdd:cd16153  135 ----IAKGA---------------------------------------------------------DSDK--PFFVRLSF 151
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 244 LHVHIPLITMENFLGK-SLHGL--YGDNveemdwMVGRILDTLDVEGLSN---STLIYFTSDHGGSLENQLGNTQYGGWN 317
Cdd:cd16153  152 LQPHTPVLPPKEFRDRfDYYAFcaYGDA------QVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQGILAKFTFWP 225
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530421114 318 giykggkgmggweGGIRVPGIFRWPGVL--PAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDL 383
Cdd:cd16153  226 -------------QSHRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL 280
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
9-368 1.05e-20

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: 91.33  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKL-TQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQwTGASGGLPTNETTFAKILKEKGYATG 87
Cdd:cd00016   26 TPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPEL-PSRAAGKDEDGPTIPELLKQAGYRTG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  88 LIGkwhlglncesasdhchhplhhgfdhfygmpfslmgdcarwelsekrvnLEQKLNFLfqvlalvaltlvagklthlip 167
Cdd:cd00016  105 VIG------------------------------------------------LLKAIDET--------------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 168 vswmpviwsalsavlllassyfvgalivhadcflmrnhtiteqpmcfqrttplilqevasflkrNKHGPFLLFVSFLHVH 247
Cdd:cd00016  116 ----------------------------------------------------------------SKEKPFVLFLHFDGPD 131
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 248 IPLitmenFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLENqLGNTqyggwngiYKGGKGMG 327
Cdd:cd00016  132 GPG-----HAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKG-HGGD--------PKADGKAD 197
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 530421114 328 GWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLA 368
Cdd:cd00016  198 KSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
9-394 4.05e-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: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 92.03  E-value: 4.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGmVSSIGYRVLQwtgasgglpTNETTFAKILKE---KGYA 85
Cdd:cd16154   28 TPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTG-VLAVPDELLL---------SEETLLQLLIKDattAGYS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114  86 TGLIGKWHLGlNCESasdhcHHPLHHGFDHFYGMPFSLMGDCARWELSEKRVNLEQKlnflfqvlalvalTLVAGKLTHL 165
Cdd:cd16154   97 SAVIGKWHLG-GNDN-----SPNNPGGIPYYAGILGGGVQDYYNWNLTNNGQTTNST-------------EYATTKLTNL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 166 iPVSWmpviwsalsavlllassyfvgalivhadcflmrnhtITEQpmcfqrTTP--LILQEVASflkrnkHGPFllfvsf 243
Cdd:cd16154  158 -AIDW------------------------------------IDQQ------TKPwfLWLAYNAP------HTPF------ 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 244 lhvHIPLITMENflgKSLHGLY---GDN--------VEEMDWMVGRILDTLDVEGLSNsTLIYFTSDHG--GSLENQLGN 310
Cdd:cd16154  183 ---HLPPAELHS---RSLLGDSadiEANprpyylaaIEAMDTEIGRLLASIDEEEREN-TIIIFIGDNGtpGQVVDLPYT 255
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 311 TQY-------GGwngiykggkgmggweggIRVPGIFRWPGVlpaGRVIGEPTSLM---DVFPTVVRLAGGEVPQdrVIDG 380
Cdd:cd16154  256 RNHakgslyeGG-----------------INVPLIVSGAGV---ERANERESALVnatDLYATIAELAGVDAAE--IHDS 313
                        410
                 ....*....|....
gi 530421114 381 QDLLPLLLGTAQHS 394
Cdd:cd16154  314 VSFKPLLSDVNAST 327
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
232-467 6.92e-13

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: 70.26  E-value: 6.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 232 NKHGPFLLFVSFLHVH-IPLITM-ENFLG-KSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGgslENQL 308
Cdd:cd16171  162 NLTQPFALYLGLNLPHpYPSPSMgENFGSiRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHG---ELAM 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 309 GNTQYggwngiykggKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLL 388
Cdd:cd16171  239 EHRQF----------YKMSMYEGSSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLLS 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 389 GTAQHSDH-----------EFlmHYCErfLHAARWHQRDrgTMWKvhFVTpvfqpegagacYGRkvcpcfGEKVvhhdPP 457
Cdd:cd16171  306 ESSIKESPsrvphpdwvlsEF--HGCN--VNASTYMLRT--NSWK--YIA-----------YAD------GNSV----PP 356
                        250
                 ....*....|
gi 530421114 458 LLFDLSRDPS 467
Cdd:cd16171  357 QLFDLSKDPD 366
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
202-384 1.85e-08

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: 56.84  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 202 MRNHTITEQPMCFQRTTpLILQEVASFL-KRNKHGPFLLFVSFLHVHI------------------PLITMENFLGKSLH 262
Cdd:COG3083  348 VSLPRLHTPGGPAQRDR-QITAQWLQWLdQRDSDRPWFSYLFLDAPHAysfpadypkpfqpsedcnYLALDNESDPTPFK 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 263 GLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSL----ENQLG-NTQYGGWNgiykggkgmggweggIRVPG 337
Cdd:COG3083  427 NRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnengQNYWGhNSNFSRYQ---------------LQVPL 491
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530421114 338 IFRWPGVLPagRVIGEPTSLMDVFPTVV-RLAGGEVPqdrVID---GQDLL 384
Cdd:COG3083  492 VIHWPGTPP--QVISKLTSHLDIVPTLMqRLLGVQNP---ASDysqGEDLF 537
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
222-384 2.27e-08

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 56.59  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 222 LQEVASFLKRNKhGPFLLFVsflhvhiplITMEN---F-----------LGKSLHGLYGDNVEEMDWMVGRILDTLDVEG 287
Cdd:COG1368  372 FDKALEELEKLK-KPFFAFL---------ITLSNhgpYtlpeedkkipdYGKTTLNNYLNAVRYADQALGEFIEKLKKSG 441
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 288 LSNSTLIYFTSDHGGSLEnqlGNTQYggwngiykggkgmGGWEGGIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVRL 367
Cdd:COG1368  442 WYDNTIFVIYGDHGPRSP---GKTDY-------------ENPLERYRVPLLIYSPG-LKKPKVIDTVGSQIDIAPTLLDL 504
                        170
                 ....*....|....*..
gi 530421114 368 AGGEVPQDRVIdGQDLL 384
Cdd:COG1368  505 LGIDYPSYYAF-GRDLL 520
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
222-369 7.24e-08

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: 53.84  E-value: 7.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 222 LQEVASFLKRNKHGPFLLFVsflhvhiplITMENflgkslHGLYGDN-----------------------VEEMDWMVGR 278
Cdd:cd16015  143 FDQALEELEELKKKPFFIFL---------VTMSN------HGPYDLPeekkdeplkveedktelenylnaIHYTDKALGE 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114 279 ILDTLDVEGLSNSTLIYFTSDHGGSLENQLGNTQYGGWNGIykggkgmggweggiRVPGIFRWPGVLPaGRVIGEPTSLM 358
Cdd:cd16015  208 FIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--------------RTPLLIYSPGLKK-PKKIDRVGSQI 272
                        170
                 ....*....|.
gi 530421114 359 DVFPTVVRLAG 369
Cdd:cd16015  273 DIAPTLLDLLG 283
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
9-139 7.20e-06

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 48.21  E-value: 7.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421114   9 TPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGRYPVRSGMVSSIGYR--------VLQWTGASGGLPT--NETTFAK 77
Cdd:COG1524   44 APNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGLYPGEHGIVGNGWYDpelgrvvnSLSWVEDGFGSNSllPVPTIFE 123
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530421114  78 ILKEKGYATGLIGKWHLGlncESASDHCHHPLHH-GFDHFYGMPFS--LMGDCARWELSEKRVNL 139
Cdd:COG1524  124 RARAAGLTTAAVFWPSFE---GSGLIDAARPYPYdGRKPLLGNPAAdrWIAAAALELLREGRPDL 185
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
9-52 5.98e-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: 5.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530421114    9 TPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGRYPVRSGMVS 52
Cdd:pfam01663  20 TPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVG 64
 
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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