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Conserved domains on  [gi|255653026|ref|NP_001157425|]
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steryl-sulfatase precursor [Equus caballus]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 10888433)

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
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
21-545 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: 891.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  21 RPNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKVGVFLFS 100
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 101 ASSGGLPTSEITFAKLLKNQGYSTALIGKWHLGTNCHNKTDFCHHPLSHGFDYFHGLPVTNLRDCKPGEGTVFTTGIRML 180
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 181 VSVPLQLIAIALLTLAVLKCLGLLPtpGLVFFCLLFLAAVILGLVVCFLYYFRPLNCFLMRNHEITQQPLSYDHLTQRLT 260
Cdd:cd16159  161 FPLLTAFVLITALTIFLLLYLGAVS--KRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 261 EDAAEFIRRNAETPFLLVLSYLHVHTALFSSKDFAGKSKHGAYGDTAEEMDWSVGQILNVLDELRLANNTLIYFSSDQGA 340
Cdd:cd16159  239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 341 HVEEVTTRGEVHGGSNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDRIIDGRD 420
Cdd:cd16159  319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 421 LMPLLQGKSQRSDHEFLFHYCNFYLNAVRWHPRNSTSIWKAFFFTPKFTPEGaNGCFSTHVCFCHGDYITHHHPPLLFDI 500
Cdd:cd16159  399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGT-EGCCGTLLCRCFGDSVTHHDPPLLFDL 477
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 255653026 501 SKDPRERNPLTMTTEPrFQEILEAMQQAADHHTKTLQEVPNQLSL 545
Cdd:cd16159  478 SADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLSF 521
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
21-545 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: 891.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  21 RPNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKVGVFLFS 100
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 101 ASSGGLPTSEITFAKLLKNQGYSTALIGKWHLGTNCHNKTDFCHHPLSHGFDYFHGLPVTNLRDCKPGEGTVFTTGIRML 180
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 181 VSVPLQLIAIALLTLAVLKCLGLLPtpGLVFFCLLFLAAVILGLVVCFLYYFRPLNCFLMRNHEITQQPLSYDHLTQRLT 260
Cdd:cd16159  161 FPLLTAFVLITALTIFLLLYLGAVS--KRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 261 EDAAEFIRRNAETPFLLVLSYLHVHTALFSSKDFAGKSKHGAYGDTAEEMDWSVGQILNVLDELRLANNTLIYFSSDQGA 340
Cdd:cd16159  239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 341 HVEEVTTRGEVHGGSNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDRIIDGRD 420
Cdd:cd16159  319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 421 LMPLLQGKSQRSDHEFLFHYCNFYLNAVRWHPRNSTSIWKAFFFTPKFTPEGaNGCFSTHVCFCHGDYITHHHPPLLFDI 500
Cdd:cd16159  399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGT-EGCCGTLLCRCFGDSVTHHDPPLLFDL 477
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 255653026 501 SKDPRERNPLTMTTEPrFQEILEAMQQAADHHTKTLQEVPNQLSL 545
Cdd:cd16159  478 SADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLSF 521
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
13-540 1.68e-111

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 338.39  E-value: 1.68e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  13 ETQSCATSRPNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASqs 92
Cdd:COG3119   15 AAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD-- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  93 kvgvfLFSASSGGLPTSEITFAKLLKNQGYSTALIGKWHLgtnchnktdfchhplshgfdyfhglpvtnlrdckpgegtv 172
Cdd:COG3119   93 -----NGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL---------------------------------------- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 173 fttgirmlvsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplncflmrnheitqqplsy 252
Cdd:COG3119      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 253 dHLTQRLTEDAAEFIRRNA--ETPFLLVLSYLHVHT---------ALFSSKDFA--------------GKSKHGAYGDTA 307
Cdd:COG3119  128 -YLTDLLTDKAIDFLERQAdkDKPFFLYLAFNAPHApyqapeeylDKYDGKDIPlppnlaprdlteeeLRRARAAYAAMI 206
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 308 EEMDWSVGQILNVLDELRLANNTLIYFSSDQGAHVEEvttrgevHGgsngiYKGGKANNWEGGIRVPGILRWPGVIPAGL 387
Cdd:COG3119  207 EEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGE-------HG-----LRGGKGTLYEGGIRVPLIVRWPGKIKAGS 274
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 388 EIDEPTSNMDIFPTVAKLAGSPLPEDriIDGRDLMPLLQGKSQRSDHEFLFHYCNFYLN-AVRWHPrnstsiWKAFFFTP 466
Cdd:COG3119  275 VSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNrAIRTGR------WKLIRYYD 346
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255653026 467 KftpegangcfsthvcfchgdyithHHPPLLFDISKDPRERNPLTmttePRFQEILEAMQQAADHHTKTLQEVP 540
Cdd:COG3119  347 D------------------------DGPWELYDLKNDPGETNNLA----ADYPEVVAELRALLEAWLKELGDPP 392
Sulfatase pfam00884
Sulfatase;
22-408 1.29e-61

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 205.73  E-value: 1.29e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026   22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKVGvflfsa 101
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVG------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  102 ssggLPTSEITFAKLLKNQGYSTALIGKWHLGTNchNKTDFCHHplshGFDYF--HGLPVTNLRDCkpgegtvfttgirm 179
Cdd:pfam00884  75 ----LPRTEPSLPDLLKRAGYNTGAIGKWHLGWY--NNQSPCNL----GFDKFfgRNTGSDLYADP-------------- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  180 lvsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyYFRPLNCFLMRnheitqqplsydHLTQRL 259
Cdd:pfam00884 131 ---------------------------------------------------PDVPYNCSGGG------------VSDEAL 147
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  260 TEDAAEFIRRNAEtPFLLVLSYLHVHTALFSSKDFAGKSK------------HGAYGDTAEEMDWSVGQILNVLDELRLA 327
Cdd:pfam00884 148 LDEALEFLDNNDK-PFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLL 226
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  328 NNTLIYFSSDQGAHVEEvttrgevhggSNGIYKGGK-ANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLA 406
Cdd:pfam00884 227 DNTLVVYTSDHGESLGE----------GGGYLHGGKyDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLA 296

                  ..
gi 255653026  407 GS 408
Cdd:pfam00884 297 GI 298
PRK13759 PRK13759
arylsulfatase; Provisional
18-527 4.74e-39

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 149.43  E-value: 4.74e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  18 ATSRPNFVLLMADDLGiGDP-GCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKVGV 96
Cdd:PRK13759   3 QTKKPNIILIMVDQMR-GDClGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  97 FLFsassgglptsEITFAKLLKNQGYSTALIGKWHLgtnchnktdfchHP--LSHGFDYfhglpvTNLRDCKPGEGTVFT 174
Cdd:PRK13759  82 WNY----------KNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHDGYLHSGRNED 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 175 TGIRMLVSVPLQLIAialltlavLKCLGLLPTpglvffcllflaAVILGlvvcflyyfrpLNCflmrnHEITQQPLSYD- 253
Cdd:PRK13759 134 KSQFDFVSDYLAWLR--------EKAPGKDPD------------LTDIG-----------WDC-----NSWVARPWDLEe 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 254 --HLTQRLTEDAAEFIRRNAET-PFLLVLSYLHVH---------------------------------------TALFS- 290
Cdd:PRK13759 178 rlHPTNWVGSESIEFLRRRDPTkPFFLKMSFARPHspydppkryfdmykdadipdphigdweyaedqdpeggsiDALRGn 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 291 -SKDFAGKSKHGAYGDTAeEMDWSVGQILNVLDELRLANNTLIYFSSDqgahveevttrgevHG---GSNGIYKggKANN 366
Cdd:PRK13759 258 lGEEYARRARAAYYGLIT-HIDHQIGRFLQALKEFGLLDNTIILFVSD--------------HGdmlGDHYLFR--KGYP 320
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 367 WEGGIRVPGILRWPG---VIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDriIDGRDLMPLLQGKSQ--RS--DHEFLFH 439
Cdd:PRK13759 321 YEGSAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYEgwRPylHGEHALG 398
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 440 YCNF-YLNAVRWhprnsTSIWkaffftpkFTPEGANGcfsthvcfchgdyithhhpplLFDISKDPRERNPLtmTTEPRF 518
Cdd:PRK13759 399 YSSDnYLTDGKW-----KYIW--------FSQTGEEQ---------------------LFDLKKDPHELHNL--SPSEKY 442

                 ....*....
gi 255653026 519 QEILEAMQQ 527
Cdd:PRK13759 443 QPRLREMRK 451
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
21-545 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: 891.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  21 RPNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKVGVFLFS 100
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 101 ASSGGLPTSEITFAKLLKNQGYSTALIGKWHLGTNCHNKTDFCHHPLSHGFDYFHGLPVTNLRDCKPGEGTVFTTGIRML 180
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 181 VSVPLQLIAIALLTLAVLKCLGLLPtpGLVFFCLLFLAAVILGLVVCFLYYFRPLNCFLMRNHEITQQPLSYDHLTQRLT 260
Cdd:cd16159  161 FPLLTAFVLITALTIFLLLYLGAVS--KRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 261 EDAAEFIRRNAETPFLLVLSYLHVHTALFSSKDFAGKSKHGAYGDTAEEMDWSVGQILNVLDELRLANNTLIYFSSDQGA 340
Cdd:cd16159  239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 341 HVEEVTTRGEVHGGSNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDRIIDGRD 420
Cdd:cd16159  319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 421 LMPLLQGKSQRSDHEFLFHYCNFYLNAVRWHPRNSTSIWKAFFFTPKFTPEGaNGCFSTHVCFCHGDYITHHHPPLLFDI 500
Cdd:cd16159  399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGT-EGCCGTLLCRCFGDSVTHHDPPLLFDL 477
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 255653026 501 SKDPRERNPLTMTTEPrFQEILEAMQQAADHHTKTLQEVPNQLSL 545
Cdd:cd16159  478 SADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLSF 521
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
21-511 0e+00

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: 556.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  21 RPNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMAsqskvGVFLFS 100
Cdd:cd16026    1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLP-----GVVGPP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 101 ASSGGLPTSEITFAKLLKNQGYSTALIGKWHLGTNchnktdFCHHPLSHGFDYFHGLPVTNLRDCKPGEGTVFttgirml 180
Cdd:cd16026   76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQ------PEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDP------- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 181 vsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfRPLNCFLMRNHEITQQPLSYDHLTQRLT 260
Cdd:cd16026  143 ----------------------------------------------------PGPLPPLMENEEVIEQPADQSSLTQRYT 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 261 EDAAEFIRRNAETPFLLVLSYLHVHTALFSSKDFAGKSKHGAYGDTAEEMDWSVGQILNVLDELRLANNTLIYFSSDQGA 340
Cdd:cd16026  171 DEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGP 250
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 341 HVEEVTtrgevHGGSNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDRIIDGRD 420
Cdd:cd16026  251 WLEYGG-----HGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKD 325
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 421 LMPLLQGKSQRSDHEFLFHYCNFYLNAVRWHPrnstsiWKAFFFTPKFTPEGANgcfsthvcfchGDYITHHHPPLLFDI 500
Cdd:cd16026  326 ISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDPG-----------GLDPTKLEPPLLYDL 388
                        490
                 ....*....|.
gi 255653026 501 SKDPRERNPLT 511
Cdd:cd16026  389 EEDPGETYNVA 399
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
21-531 5.67e-154

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: 448.80  E-value: 5.67e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  21 RPNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKVgvfLFS 100
Cdd:cd16160    1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRV---FLP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 101 ASSGGLPTSEITFAKLLKNQGYSTALIGKWHLGTNCHNKTDFCHHPLSHGFDYF-HGLPVTNLRDCKPgegtvftTGIRm 179
Cdd:cd16160   78 WDIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFDFVgTNLPFTNSWACDD-------TGRH- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 180 lvsVPLqliaialltlavlkclgllPTPGLvffcllflaavilglvvCFLYYfrplncflmrNHEITQQPLSYDHLTQRL 259
Cdd:cd16160  150 ---VDF-------------------PDRSA-----------------CFLYY----------NDTIVEQPIQHEHLTETL 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 260 TEDAAEFIRRNAETPFLLVLSYLHVHTALFSSKDFAGKSKHGAYGDTAEEMDWSVGQILNVLDELRLANNTLIYFSSDQG 339
Cdd:cd16160  181 VGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHG 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 340 AHVEEVTtrgevHGGSNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEiDEPTSNMDIFPTVAKLAGSPLPEDRIIDGR 419
Cdd:cd16160  261 PHVEYCL-----EGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIKPRVS-HEVVSTMDIFPTFVDLAGGTLPTDRIYDGL 334
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 420 DLMPLLQGKSQRSDHEFLFHYCNfYLNAVRWHPrnstsiWKAFFFT------PKFTPEGANGCFSTH--VC-FCHGDYIT 490
Cdd:cd16160  335 SITDLLLGEADSPHDDILYYCCS-RLMAVRYGS------YKIHFKTqplpsqESLDPNCDGGGPLSDyiVCyDCEDECVT 407
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 255653026 491 HHHPPLLFDISKDPRERNPLtmTTEPRfQEILEAMQQAADH 531
Cdd:cd16160  408 KHNPPLIFDVEKDPGEQYPL--QPSVY-EHMLEAVEKLIAH 445
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
22-558 9.47e-118

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: 357.53  E-value: 9.47e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASqskvGVFlFSA 101
Cdd:cd16158    2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYP----GVF-YPG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 SSGGLPTSEITFAKLLKNQGYSTALIGKWHLGTNCHNKtdfcHHPLSHGFDYFHGLPVTNlRDCKPGEGTVFTTGIrmlv 181
Cdd:cd16158   77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSH-DQGPCQNLTCFPPNI---- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 182 svplqliaialltlavlKCLGLLPTpglvffcllflaavilGLVVCFLYYfrplncflmrNHEITQQPLSYDHLTQRLTE 261
Cdd:cd16158  148 -----------------PCFGGCDQ----------------GEVPCPLFY----------NESIVQQPVDLLTLEERYAK 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 262 DAAEFIRRNAE--TPFLLVLSYLHVHTALFSSKDFAGKSKHGAYGDTAEEMDWSVGQILNVLDELRLANNTLIYFSSDQG 339
Cdd:cd16158  185 FAKDFIADNAKegKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNG 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 340 AHveevTTRgEVHGGSNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIdEPTSNMDIFPTVAKLAGSPLPEdRIIDGR 419
Cdd:cd16158  265 PS----TMR-KSRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLPN-VTLDGV 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 420 DLMPLL--QGKSQRSDheFLFHYC----NFYLNAVRWHPrnstsiWKAFFFTpkftpEGANGCFSTHVCFCHGD-YITHH 492
Cdd:cd16158  338 DMSPILfeQGKSPRQT--FFYYPTspdpDKGVFAVRWGK------YKAHFYT-----QGAAHSGTTPDKDCHPSaELTSH 404
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255653026 493 HPPLLFDISKDPRERNPLTMTtePRFQEILEAMQQAADHHTKTLQEVPNQLSLGNivwKPWLQMCC 558
Cdd:cd16158  405 DPPLLFDLSQDPSENYNLLGL--PEYNQVLKQIQQVKERFEASMKFGESEINKGE---DPALEPCC 465
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
22-527 3.30e-114

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: 346.45  E-value: 3.30e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGM-------ASQSKV 94
Cdd:cd16144    1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdvipgrRGPPDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  95 GVFLFSASSGGLPTSEITFAKLLKNQGYSTALIGKWHLGTNchnktdFCHHPLSHGFDYFHGlpvtnlrDCKPGEGTvft 174
Cdd:cd16144   81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGE------GGYGPEDQGFDVNIG-------GTGNGGPP--- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 175 tgirmlvsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflYYFRPLNcFLMRNHEITQQPlsyDH 254
Cdd:cd16144  145 -------------------------------------------------------SYYFPPG-KPNPDLEDGPEG---EY 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 255 LTQRLTEDAAEFIRRNAETPFLLVLSYLHVHTALFSSKDF-----AGKSKHGAYGDTA------EEMDWSVGQILNVLDE 323
Cdd:cd16144  166 LTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELiekyeKKKKGLRKGQKNPvyaamiESLDESVGRILDALEE 245
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 324 LRLANNTLIYFSSDQGAHVEEVTTrgevhGGSNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVA 403
Cdd:cd16144  246 LGLADNTLVIFTSDNGGLSTRGGP-----PTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFL 320
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 404 KLAGSPLPEDRIIDGRDLMPLLQGKSQRSDHEFLFHYCNFYLNAVRwhpRNSTSI----WK--AFFFTPKFtpegangcf 477
Cdd:cd16144  321 ELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFWHFPHYHGQGG---RPASAIrkgdWKliEFYEDGRV--------- 388
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 255653026 478 sthvcfchgdyithhhppLLFDISKDPRERNPLTMTTEPRFQEILEAMQQ 527
Cdd:cd16144  389 ------------------ELYNLKNDIGETNNLAAEMPEKAAELKKKLDA 420
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
13-540 1.68e-111

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 338.39  E-value: 1.68e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  13 ETQSCATSRPNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASqs 92
Cdd:COG3119   15 AAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD-- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  93 kvgvfLFSASSGGLPTSEITFAKLLKNQGYSTALIGKWHLgtnchnktdfchhplshgfdyfhglpvtnlrdckpgegtv 172
Cdd:COG3119   93 -----NGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL---------------------------------------- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 173 fttgirmlvsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplncflmrnheitqqplsy 252
Cdd:COG3119      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 253 dHLTQRLTEDAAEFIRRNA--ETPFLLVLSYLHVHT---------ALFSSKDFA--------------GKSKHGAYGDTA 307
Cdd:COG3119  128 -YLTDLLTDKAIDFLERQAdkDKPFFLYLAFNAPHApyqapeeylDKYDGKDIPlppnlaprdlteeeLRRARAAYAAMI 206
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 308 EEMDWSVGQILNVLDELRLANNTLIYFSSDQGAHVEEvttrgevHGgsngiYKGGKANNWEGGIRVPGILRWPGVIPAGL 387
Cdd:COG3119  207 EEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGE-------HG-----LRGGKGTLYEGGIRVPLIVRWPGKIKAGS 274
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 388 EIDEPTSNMDIFPTVAKLAGSPLPEDriIDGRDLMPLLQGKSQRSDHEFLFHYCNFYLN-AVRWHPrnstsiWKAFFFTP 466
Cdd:COG3119  275 VSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNrAIRTGR------WKLIRYYD 346
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255653026 467 KftpegangcfsthvcfchgdyithHHPPLLFDISKDPRERNPLTmttePRFQEILEAMQQAADHHTKTLQEVP 540
Cdd:COG3119  347 D------------------------DGPWELYDLKNDPGETNNLA----ADYPEVVAELRALLEAWLKELGDPP 392
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
22-508 2.75e-105

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: 322.23  E-value: 2.75e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYG-NKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGmasqSKVGVFLFS 100
Cdd:cd16143    1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSR----LKGGVLGGF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 101 ASSGgLPTSEITFAKLLKNQGYSTALIGKWHLGTNCHNKTDFCHH----------------PLSHGFDYFHGLPVTNLrd 164
Cdd:cd16143   77 SPPL-IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIPASEV-- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 165 ckpgegtvfttgirmlvsvplqliaialltlavlkclglLPTpglvffcllflaavilglvvcflyyfrplncflmrnhe 244
Cdd:cd16143  154 ---------------------------------------LPT-------------------------------------- 156
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 245 itqqplsydhltqrLTEDAAEFIRRNA--ETPFLLVLSYLHVHTALFSSKDFAGKSKHGAYGDTAEEMDWSVGQILNVLD 322
Cdd:cd16143  157 --------------LTDKAVEFIDQHAkkDKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALK 222
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 323 ELRLANNTLIYFSSDQGAHVEEVTTRGEVHGG-SNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPT 401
Cdd:cd16143  223 ELGLAENTLVIFTSDNGPSPYADYKELEKFGHdPSGPLRGMKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFAT 302
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 402 VAKLAGSPLPEDRIIDGRDLMPLLQGKSQRSDHEFLFHYCNFYLNAVRWHPrnstsiWKAFFftpkftpEGANGCFSTHV 481
Cdd:cd16143  303 LAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGSFAIRKGD------WKLID-------GTGSGGFSYPR 369
                        490       500
                 ....*....|....*....|....*..
gi 255653026 482 CFCHGDYithhHPPLLFDISKDPRERN 508
Cdd:cd16143  370 GKEKLGL----PPGQLYNLSTDPGESN 392
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
22-511 6.03e-104

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: 317.94  E-value: 6.03e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLR---TPNIDRLAEGGVKLTQHLAaSPLCTPSRAAFMTGRYPIRSGMasqSKVGvfl 98
Cdd:cd16142    1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYV-EPSCTPGRAAFITGRHPIRTGL---TTVG--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  99 FSASSGGLPTSEITFAKLLKNQGYSTALIGKWHLGtnchNKTDfcHHPLSHGFDYFHGlpvtnlrdckpgegtvfttgir 178
Cdd:cd16142   74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG----DEDG--RLPTDHGFDEFYG---------------------- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 179 mlvsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcFLYYFrplncflmrnheitqqplsydhLTQR 258
Cdd:cd16142  126 -------------------------------------------------NLYHT----------------------IDEE 134
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 259 LTEDAAEFIRRNAET--PFLLVLSYLHVHTALFSSKDFAGKSK-HGAYGDTAEEMDWSVGQILNVLDELRLANNTLIYFS 335
Cdd:cd16142  135 IVDKAIDFIKRNAKAdkPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFT 214
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 336 SDQGAHVEEVttrgevHGGSNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPLPE--- 412
Cdd:cd16142  215 TDNGPEQDVW------PDGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPKdkl 288
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 413 ---DRIIDGRDLMPLLQGKSQRSDHEFLFHYCNFYLNAVRWHPrnstsiWKAFFFTpkFTPEGANGCFSTHVCFChgdyi 489
Cdd:cd16142  289 lgkDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFKA--QEDTGGPTGEPFYVLTF----- 355
                        490       500
                 ....*....|....*....|..
gi 255653026 490 thhhpPLLFDISKDPRERNPLT 511
Cdd:cd16142  356 -----PLIFNLRRDPKERYDVT 372
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
21-511 1.36e-100

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: 309.78  E-value: 1.36e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  21 RPNFVLLMADDLGIGDPGCYGNKTLR-TPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMAsqskvGVFLf 99
Cdd:cd16161    1 KPNFLLLFADDLGWGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVG-----HNFL- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 100 SASSGGLPTSEITFAKLLKNQGYSTALIGKWHLGtncHNKTdfcHHPLSHGFDYFHGLPVTNlrDckpgegtvfttgirm 179
Cdd:cd16161   75 PTSVGGLPLNETTLAEVLRQAGYATGMIGKWHLG---QREA---YLPNSRGFDYYFGIPFSH--D--------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 180 lvsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplncflmrnheitqqplsyDHLTQRL 259
Cdd:cd16161  132 -------------------------------------------------------------------------SSLADRY 138
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 260 TEDAAEFIRRNAET--PFLLVLSYLHVHTALFSSKDF-AGKSKHGAYGDTAEEMDWSVGQILNVLDELRLANNTLIYFSS 336
Cdd:cd16161  139 AQFATDFIQRASAKdrPFFLYAALAHVHVPLANLPRFqSPTSGRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTS 218
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 337 DQGAHVEEVTTRGEVHGG---SNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPLPED 413
Cdd:cd16161  219 DNGPWEVKCELAVGPGTGdwqGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPG 298
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 414 RIIDGRDLMPLLQGKSQrSDHEFLFHYCNFY-----LNAVRWHPrnstsiWKAFFFTPKFTPEGANGCfsthvcfchgdY 488
Cdd:cd16161  299 RIYDGKDLSPVLFGGSK-TGHRCLFHPNSGAagagaLSAVRCGD------YKAHYATGGALACCGSTG-----------P 360
                        490       500
                 ....*....|....*....|...
gi 255653026 489 ITHHHPPLLFDISKDPRERNPLT 511
Cdd:cd16161  361 KLYHDPPLLFDLEVDPAESFPLT 383
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
21-557 2.67e-97

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: 304.39  E-value: 2.67e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  21 RPNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKVGVFLFS 100
Cdd:cd16157    1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 101 ASS--GGLPTSEITFAKLLKNQGYSTALIGKWHLGtnchNKTDFchHPLSHGFDYFHGLPvtnlrDC--KPGEGTVFTtg 176
Cdd:cd16157   81 PQNivGGIPDSEILLPELLKKAGYRNKIVGKWHLG----HRPQY--HPLKHGFDEWFGAP-----NChfGPYDNKAYP-- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 177 irmlvSVPLqliaialltlavlkclgllptpglvffcllFLAAVILGLvvcflYYfrplncflmrnheitqQPLSYDH-- 254
Cdd:cd16157  148 -----NIPV------------------------------YRDWEMIGR-----YY----------------EEFKIDKkt 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 255 ----LTQRLTEDAAEFIRR--NAETPFLLVLSYLHVHTALFSSKDFAGKSKHGAYGDTAEEMDWSVGQILNVLDELRLAN 328
Cdd:cd16157  172 gesnLTQIYLQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIEN 251
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 329 NTLIYFSSDQGAhveeVTTRGEVHGGSNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGS 408
Cdd:cd16157  252 NTFVFFSSDNGA----ALISAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGL 327
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 409 PLPEDRIIDGRDLMPLLqgKSQRSDHEFLFHYCNFYLNAVRWhprnstSIWKAFFFTPKFTPEGangcFSTHVCFCHGDY 488
Cdd:cd16157  328 PIPSDRAIDGIDLLPVL--LNGKEKDRPIFYYRGDELMAVRL------GQYKAHFWTWSNSWEE----FRKGINFCPGQN 395
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255653026 489 IT---------HHHPPLLFDISKDPRERNPLTmTTEPRFQEILEAMQQAADHHTKTLqeVPNQlslgnivwkPWLQMC 557
Cdd:cd16157  396 VPgvtthnqtdHTKLPLLFHLGRDPGEKYPIS-FKSAEYKQAMPRISKVVQQHQKTL--VPGE---------PQLNVC 461
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
22-508 3.62e-91

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: 286.80  E-value: 3.62e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKVGVFLfsa 101
Cdd:cd16145    1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQD--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 ssgGLPTSEITFAKLLKNQGYSTALIGKWHLGTNCHNKtdfchHPLSHGFDYFHGlpvtnlrdckpgegtvfttgirmlv 181
Cdd:cd16145   78 ---PLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPG-----HPTKQGFDYFYG------------------------- 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 182 svplqliaialltlavlkclgllptpglvffcllflaavILGLVVCFLYYFRplncFLMRNHEI---------------T 246
Cdd:cd16145  125 ---------------------------------------YLDQVHAHNYYPE----YLWRNGEKvplpnnvippldegnN 161
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 247 QQPLSYDHLTQRLTEDAAEFIRRNAETPFLLVLSYLHVHTALF---SSKDFAGKSKHGAYGDTAEE------------MD 311
Cdd:cd16145  162 AGGGGGTYSHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQvpdDGPYKYKPKDPGIYAYLPWPqpekayaamvtrLD 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 312 WSVGQILNVLDELRLANNTLIYFSSDQGAHVEEVTTRGEVHGGSNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDE 391
Cdd:cd16145  242 RDVGRILALLKELGIDENTLVVFTSDNGPHSEGGSEHDPDFFDSNGPLRGYKRSLYEGGIRVPFIARWPGKIPAGSVSDH 321
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 392 PTSNMDIFPTVAKLAGSPLPEDriIDGRDLMPLLQGKSQRSDHEFLfhYCNFYLN----AVRWHPrnstsiWKAFFFTPK 467
Cdd:cd16145  322 PSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFYEGggaqAVRMGG------WKAVRHGKK 391
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 255653026 468 ftpegaNGcfsthvcfchgdyithhhPPLLFDISKDPRERN 508
Cdd:cd16145  392 ------DG------------------PFELYDLSTDPGETN 408
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
22-528 1.84e-82

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: 263.64  E-value: 1.84e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQ-HlaASPLCTPSRAAFMTGRYPIRSGMASQSKVGVFLFS 100
Cdd:cd16146    1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfH--VSPVCAPTRAALLTGRYPFRTGVWHTILGRERMRL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 101 assgglptSEITFAKLLKNQGYSTALIGKWHLGTNchnktdFCHHPLSHGFDYFHGLpvtnlrdckpGEGtvfttGIrml 180
Cdd:cd16146   79 --------DETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLGH----------GGG-----GI--- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 181 vsvplqliaialltlavlkclGLLPTPGLVFfcllflaavilglvvcflyYFRPlncFLMRNHEITQqplsYD-HLTQRL 259
Cdd:cd16146  127 ---------------------GQYPDYWGND-------------------YFDD---TYYHNGKFVK----TEgYCTDVF 159
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 260 TEDAAEFIRRNAETPFLLVLSY------LHVHTALFssKDFAGKSKH----GAYGdTAEEMDWSVGQILNVLDELRLANN 329
Cdd:cd16146  160 FDEAIDFIEENKDKPFFAYLATnaphgpLQVPDKYL--DPYKDMGLDdklaAFYG-MIENIDDNVGRLLAKLKELGLEEN 236
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 330 TLIYFSSDQGahveevtTRGEVHGGSNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSP 409
Cdd:cd16146  237 TIVIFMSDNG-------PAGGVPKRFNAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVK 309
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 410 LPEDRIIDGRDLMPLLQGKSQRSDHEFLF-HYCNFYLNAVRWHPrnsTSIWKaffftpkftpegangcfsthvcfchGDY 488
Cdd:cd16146  310 LPEGIKLDGRSLLPLLKGESDPWPERTLFtHSGRWPPPPKKKRN---AAVRT-------------------------GRW 361
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 255653026 489 ---ITHHHPPLLFDISKDPRERNPLTmTTEPrfqEILEAMQQA 528
Cdd:cd16146  362 rlvSPKGFQPELYDIENDPGEENDVA-DEHP---EVVKRLKAA 400
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
22-420 5.99e-80

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: 251.20  E-value: 5.99e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSgmasqskvGVFLFSA 101
Cdd:cd16022    1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRH--------GVRGNVG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 SSGGLPTSEITFAKLLKNQGYSTALIGKWHlgtnchnktdfchhplshgfdyfhglpvtnlrdckpgegtvfttgirmlv 181
Cdd:cd16022   73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 182 svplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplncflmrnheitqqplsydhltqrltE 261
Cdd:cd16022  103 -------------------------------------------------------------------------------D 103
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 262 DAAEFIRRNA-ETPFLLVLSYLHVHTALfsskdfagkskhgAYGDTAEEMDWSVGQILNVLDELRLANNTLIYFSSDQGA 340
Cdd:cd16022  104 EAIDFIERRDkDKPFFLYVSFNAPHPPF-------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 341 HVEEvttrgevHGGsngiyKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDriIDGRD 420
Cdd:cd16022  171 MLGD-------HGL-----RGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
22-510 3.55e-75

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: 243.66  E-value: 3.55e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTqHLAASPLCTPSRAAFMTGRYPIRSGMasqskvgVFlfsa 101
Cdd:cd16151    1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYV-------VF---- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 ssGGLPTSEITFAKLLKNQGYSTALIGKWHLGTNCHNKTdfchHPLSHGFDYFHGLPVTNLRDCKPGEGTvFTTGIRMLV 181
Cdd:cd16151   69 --GYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGD----YPHEFGFDEYCLWQLTETGEKYSRPAT-PTFNIRNGK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 182 SVPLqliaialltlavlkclgllpTPGlvffcllflaavilglvvcflyYFRPlncflmrnhEITQqplsyDHLTqrlte 261
Cdd:cd16151  142 LLET--------------------TEG----------------------DYGP---------DLFA-----DFLI----- 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 262 daaEFIRRNAETPFLLVLSYLHVHT----------ALFSSKDFAGKSKHgaYGDTAEEMDWSVGQILNVLDELRLANNTL 331
Cdd:cd16151  161 ---DFIERNKDQPFFAYYPMVLVHDpfvptpdspdWDPDDKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTI 235
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 332 IYFSSDQGahveevtTRGEVHGGSNG-IYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPL 410
Cdd:cd16151  236 IIFTGDNG-------THRPITSRTNGrEVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPL 308
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 411 PEDRIIDGRDLMPLLQGKSQRSDHEFLFhycnfylnavrWHPRNSTSIWKA-FFFTPKFTPegangcfsthvcfchgdYI 489
Cdd:cd16151  309 PEDYPLDGRSFAPQLLGKTGSPRREWIY-----------WYYRNPHKKFGSrFVRTKRYKL-----------------YA 360
                        490       500
                 ....*....|....*....|.
gi 255653026 490 THHhpplLFDISKDPRERNPL 510
Cdd:cd16151  361 DGR----FFDLREDPLEKNPL 377
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
20-527 2.04e-74

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: 243.59  E-value: 2.04e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  20 SRPNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMasqskvgVFLF 99
Cdd:cd16031    1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGV-------TDNN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 100 SASsggLPTSEITFAKLLKNQGYSTALIGKWHLGTNchnktdfcHHPLSHGFDYFHGLpvtnlrdckPGEGTvfttgirm 179
Cdd:cd16031   74 GPL---FDASQPTYPKLLRKAGYQTAFIGKWHLGSG--------GDLPPPGFDYWVSF---------PGQGS-------- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 180 lvsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyYFRPLNcFLMRNHEITQQplsydHLTQRL 259
Cdd:cd16031  126 ---------------------------------------------------YYDPEF-IENGKRVGQKG-----YVTDII 148
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 260 TEDAAEFIRRN-AETPFLLVLSYLHVHT--------------------ALFSSKDFAGKSK---------HGAYGD---- 305
Cdd:cd16031  149 TDKALDFLKERdKDKPFCLSLSFKAPHRpftpaprhrglyedvtipepETFDDDDYAGRPEwareqrnriRGVLDGrfdt 228
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 306 -------------TAEEMDWSVGQILNVLDELRLANNTLIYFSSDQGAHVeevttrGEvHGgsngiyKGGKANNWEGGIR 372
Cdd:cd16031  229 pekyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL------GE-HG------LFDKRLMYEESIR 295
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 373 VPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDriIDGRDLMPLLQGKSQRS-DHEFLFHYcnfylnavRWH 451
Cdd:cd16031  296 VPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEY--------YEE 365
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 452 PrnstsiwkAFFFTPKftpegangcfsthvcfCHG------DYIT-HHHPPL--LFDISKDPRERNPLtmTTEPRFQEIL 522
Cdd:cd16031  366 P--------NFHNVPT----------------HEGvrteryKYIYyYGVWDEeeLYDLKKDPLELNNL--ANDPEYAEVL 419

                 ....*
gi 255653026 523 EAMQQ 527
Cdd:cd16031  420 KELRK 424
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
22-510 2.32e-73

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: 239.37  E-value: 2.32e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAAsPLCTPSRAAFMTGRYPIRSGMasQSKVgvfLFSA 101
Cdd:cd16029    1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGM--QHGV---ILAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 SSGGLPTSEITFAKLLKNQGYSTALIGKWHLGtnchnktdFCHH---PLSHGFDYFHGlpvtnlrdCKPGEGTVFTTGIR 178
Cdd:cd16029   75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYG--------YYGGAEDYYTHTSG 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 179 MLVSVPlqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplNCFLMRNHEITQqplSYD--HLT 256
Cdd:cd16029  139 GANDYG---------------------------------------------------NDDLRDNEEPAW---DYNgtYST 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 257 QRLTEDAAEFIRR-NAETPFLLVLSYLHVHTALFSSKDFAGKSKHGAYGDTAE----------EMDWSVGQILNVLDELR 325
Cdd:cd16029  165 DLFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKDEdrrtyaamvsALDESVGNVVDALKAKG 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 326 LANNTLIYFSSDQGAHVeevttrGEVHGGSNGIYKGGKANNWEGGIRVPGILRWPGVIP-AGLEIDEPTSNMDIFPTVAK 404
Cdd:cd16029  245 MLDNTLIVFTSDNGGPT------GGGDGGSNYPLRGGKNTLWEGGVRVPAFVWSPLLPPkRGTVSDGLMHVTDWLPTLLS 318
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 405 LAGSPLPEDRIIDGRDLMPLLQG--KSQRSD--HEFLFHYCNFYLNAVRWHPrnstsiWKAFFFTPkftpegangcfsth 480
Cdd:cd16029  319 LAGGDPDDLPPLDGVDQWDALSGgaPSPRTEilLNIDDITRTTGGAAIRVGD------WKLIVGKP-------------- 378
                        490       500       510
                 ....*....|....*....|....*....|
gi 255653026 481 vcfchgdyithhhpplLFDISKDPRERNPL 510
Cdd:cd16029  379 ----------------LFNIENDPCERNDL 392
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
21-510 4.13e-70

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: 231.30  E-value: 4.13e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  21 RPNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKVgvflfs 100
Cdd:cd16034    1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 101 assggLPTSEITFAKLLKNQGYSTALIGKWHLGTNCHNKTDFCHH----PLSHGFDYFHGLpvtnlrdckpgegtvfttg 176
Cdd:cd16034   75 -----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY------------------- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 177 irmlvsvplqliaialltlavlkclgllptpglvffcllflaavilglvVCFLYYFRPlncFLMRNHEITQQPLSYDhlT 256
Cdd:cd16034  131 -------------------------------------------------ECNHDHNNP---HYYDDDGKRIYIKGYS--P 156
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 257 QRLTEDAAEFIRRNA--ETPFLLVLSYLHVHT-------------------------ALFSSKDFAGKSKHGAYGdTAEE 309
Cdd:cd16034  157 DAETDLAIEYLENQAdkDKPFALVLSWNPPHDpyttapeeyldmydpkklllrpnvpEDKKEEAGLREDLRGYYA-MITA 235
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 310 MDWSVGQILNVLDELRLANNTLIYFSSDqgahveevttrgevHG---GSNGIYkgGKANNWEGGIRVPGILRWPGVIPAG 386
Cdd:cd16034  236 LDDNIGRLLDALKELGLLENTIVVFTSD--------------HGdmlGSHGLM--NKQVPYEESIRVPFIIRYPGKIKAG 299
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 387 LEIDEPTSNMDIFPTVAKLAGSPLPEDriIDGRDLMPLLQGKSQRSDHEFLFhYCNFYLNavrWHPRNSTSIWKAfFFTP 466
Cdd:cd16034  300 RVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLL-QCFVPFG---GGSARDGGEWRG-VRTD 372
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 255653026 467 KFTpegangcfsthvcfchgdY-ITHHHPPLLFDISKDPRERNPL 510
Cdd:cd16034  373 RYT------------------YvRDKNGPWLLFDNEKDPYQLNNL 399
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
22-534 3.02e-63

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: 212.37  E-value: 3.02e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDpGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASqskvgvflFSA 101
Cdd:cd16027    1 PNILWIIADDLSPDL-GGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHG--------LRS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 SSGGLPTSEITFAKLLKNQGYSTALIGKWHLG--TNCHNKTDFCHHPLSHGFDYFHGLPVTNLRDCKPGEgtvfttgirm 179
Cdd:cd16027   72 RGFPLPDGVKTLPELLREAGYYTGLIGKTHYNpdAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRAKKG---------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 180 lvsvplqliaialltlavlkclgllpTPglvFFcllflaavilgLVVCFlyyFRPlncflmrnHEitqqplSYDHLTQRL 259
Cdd:cd16027  142 --------------------------QP---FF-----------LWFGF---HDP--------HR------PYPPGDGEE 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 260 TEDAAEFIRrnaetpfllVLSYLhVHTALFsSKDFAgkskhgAYGDTAEEMDWSVGQILNVLDELRLANNTLIYFSSDQG 339
Cdd:cd16027  165 PGYDPEKVK---------VPPYL-PDTPEV-REDLA------DYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG 227
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 340 ahveevttrgevhggsnGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDriIDGR 419
Cdd:cd16027  228 -----------------MPFPRAKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGR 288
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 420 DLMPLLQGKSQRSdHEFLFHYCNF----YLN--AVRwhprnstsiwkafffTPKFTpegangcfsthvcfchgdYITHHH 493
Cdd:cd16027  289 SFLPLLKGEKDPG-RDYVFAERDRhdetYDPirSVR---------------TGRYK------------------YIRNYM 334
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 255653026 494 PPLLFDISKDPRERNPLtmTTEPRFQEILEAMQQAADHHTK 534
Cdd:cd16027  335 PEELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
Sulfatase pfam00884
Sulfatase;
22-408 1.29e-61

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 205.73  E-value: 1.29e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026   22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKVGvflfsa 101
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVG------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  102 ssggLPTSEITFAKLLKNQGYSTALIGKWHLGTNchNKTDFCHHplshGFDYF--HGLPVTNLRDCkpgegtvfttgirm 179
Cdd:pfam00884  75 ----LPRTEPSLPDLLKRAGYNTGAIGKWHLGWY--NNQSPCNL----GFDKFfgRNTGSDLYADP-------------- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  180 lvsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyYFRPLNCFLMRnheitqqplsydHLTQRL 259
Cdd:pfam00884 131 ---------------------------------------------------PDVPYNCSGGG------------VSDEAL 147
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  260 TEDAAEFIRRNAEtPFLLVLSYLHVHTALFSSKDFAGKSK------------HGAYGDTAEEMDWSVGQILNVLDELRLA 327
Cdd:pfam00884 148 LDEALEFLDNNDK-PFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLL 226
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  328 NNTLIYFSSDQGAHVEEvttrgevhggSNGIYKGGK-ANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLA 406
Cdd:pfam00884 227 DNTLVVYTSDHGESLGE----------GGGYLHGGKyDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLA 296

                  ..
gi 255653026  407 GS 408
Cdd:pfam00884 297 GI 298
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
21-510 2.49e-58

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: 199.98  E-value: 2.49e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  21 RPNFVLLMADDLGIGDPGCYGNKtLRTPNIDRLAEGGVKLTQ-HlaASPLCTPSRAAFMTGRYPIRSGMASQSKVgVFLF 99
Cdd:cd16025    2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGMGTMAEL-ATGK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 100 SASSGGLPTSEITFAKLLKNQGYSTALIGKWHLGtnchnKTDFcHhpLSHGF-DYFhglpVTNLRDCKPGEGTVF----T 174
Cdd:cd16025   78 PGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG-----PDDY-Y--STDDLtDKA----IEYIDEQKAPDKPFFlylaF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 175 TGIRMLVSVPLQLI------------AIALLTLAVLKCLGLLPtpglvffcllflaavilglvvcflyyfrplncflmRN 242
Cdd:cd16025  146 GAPHAPLQAPKEWIdkykgkydagwdALREERLERQKELGLIP-----------------------------------AD 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 243 HEITQQPLSYDHLTQrLTEDAAEFIRRNAETpfllvlsylhvhtalfsskdFAGkskhgaygdTAEEMDWSVGQILNVLD 322
Cdd:cd16025  191 TKLTPRPPGVPAWDS-LSPEEKKLEARRMEV--------------------YAA---------MVEHMDQQIGRLIDYLK 240
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 323 ELRLANNTLIYFSSDQGAhveevttrgEVHGG----SNGIYKGGKANNWEGGIRVPGILRWPGVIPAGLEI-DEPTSNMD 397
Cdd:cd16025  241 ELGELDNTLIIFLSDNGA---------SAEPGwanaSNTPFRLYKQASHEGGIRTPLIVSWPKGIKAKGGIrHQFAHVID 311
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 398 IFPTVAKLAGSPLPEDR------IIDGRDLMPLLQGKSQRSDHEFLFhycnFYLNAVRwhprnstSIWkaffftpkftpe 471
Cdd:cd16025  312 IAPTILELAGVEYPKTVngvpqlPLDGVSLLPTLDGAAAPSRRRTQY----FELFGNR-------AIR------------ 368
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 255653026 472 gangcfsthvcfcHGDY-ITHHHPPL-------LFDISKDPRERNPL 510
Cdd:cd16025  369 -------------KGGWkAVALHPPPgwgdqweLYDLAKDPSETHDL 402
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
432-567 3.36e-52

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 174.42  E-value: 3.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  432 SDHEFLFHYCNFYLNAVRWHPrnstsiWKAFFFTPKFTPEGANGCFSTHVCfchgdyITHHHPPLLFDISKDPRERNPLT 511
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 255653026  512 MTTePRFQEILEAMQQAADHHTKTLQEVPNQLSLGNIVWKPWLQMCCSSSGLsCQC 567
Cdd:pfam14707  69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPA-CTC 122
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
22-423 1.14e-51

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: 177.82  E-value: 1.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPirsgmaSQSKVGVFLFSA 101
Cdd:cd16149    1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMP------SQHGIHDWIVEG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 SSG------GLPTSEITFAKLLKNQGYSTALIGKWHLGTnchnktdfchhplshgfdyfhglpvtnlrdckpgegtvftt 175
Cdd:cd16149   75 SHGktkkpeGYLEGQTTLPEVLQDAGYRCGLSGKWHLGD----------------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 176 girmlvsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplncflmrnheitqqplsydhl 255
Cdd:cd16149      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 256 tqrlteDAAEFIRRNA--ETPFLLVLSYLHVHtalfsskdfagkSKHGAYGDTAeEMDWSVGQILNVLDELRLANNTLIY 333
Cdd:cd16149  114 ------DAADFLRRRAeaEKPFFLSVNYTAPH------------SPWGYFAAVT-GVDRNVGRLLDELEELGLTENTLVI 174
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 334 FSSDQGAHVeevttrgevhgGSNGIYKGGKA----NNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSP 409
Cdd:cd16149  175 FTSDNGFNM-----------GHHGIWGKGNGtfplNMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVD 243
                        410
                 ....*....|....
gi 255653026 410 LPEDRIIDGRDLMP 423
Cdd:cd16149  244 PPADPRLPGRSFAD 257
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
22-504 9.67e-50

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


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 174.65  E-value: 9.67e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPirsgmasqSKVGVFLFSA 101
Cdd:cd16037    1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYV--------HETGVWDNAD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 SSGGLPTseiTFAKLLKNQGYSTALIGKWHLGTNCHNktdfchhplsHGFDYfhglpvtnlrdckpgegtvfttgirmlv 181
Cdd:cd16037   73 PYDGDVP---SWGHALRAAGYETVLIGKLHFRGEDQR----------HGFRY---------------------------- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 182 svplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplncflmrnheitqqplsydhlTQRLTE 261
Cdd:cd16037  112 --------------------------------------------------------------------------DRDVTE 117
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 262 DAAEFIRRNA--ETPFLLVLSYLHVHTALFSSKDFAGKSKHGA----YGDTaEEMDWSVGQILNVLDELRLANNTLIYFS 335
Cdd:cd16037  118 AAVDWLREEAadDKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraayYGLV-EFLDENIGRVLDALEELGLLDNTLIIYT 196
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 336 SDQGAHVeevttrgevhgGSNGIYkgGKANNWEGGIRVPGILRWPGvIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDRi 415
Cdd:cd16037  197 SDHGDML-----------GERGLW--GKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL- 261
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 416 iDGRDLMPLLQGKSQRSD---HEFLFHYCNFYLNAVRWHPrnstsiWKaffftpkftpegangcfsthvcfchgdYITHH 492
Cdd:cd16037  262 -DGRSLLPLAEGPDDPDRvvfSEYHAHGSPSGAFMLRKGR------WK---------------------------YIYYV 307
                        490
                 ....*....|...
gi 255653026 493 -HPPLLFDISKDP 504
Cdd:cd16037  308 gYPPQLFDLENDP 320
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
22-504 3.03e-49

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: 173.53  E-value: 3.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPirsgmasqSKVGVFLFSA 101
Cdd:cd16032    1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLP--------SRIGAYDNAA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 SsggLPTSEITFAKLLKNQGYSTALIGKWHlgtnchnktdFCHHPLSHGFDYfhglpvtnlrDckpgEGTVFtTGIRMLv 181
Cdd:cd16032   73 E---FPADIPTFAHYLRAAGYRTALSGKMH----------FVGPDQLHGFDY----------D----EEVAF-KAVQKL- 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 182 svplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplncflmrnheitqqplsYDHltqrlte 261
Cdd:cd16032  124 ----------------------------------------------------------------------YDL------- 126
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 262 daaefIRRNAETPFLLVLSYLHVHTALFSSKDF----AGKSKHGAYGDTAeEMDWSVGQILNVLDELRLANNTLIYFSSD 337
Cdd:cd16032  127 -----ARGEDGRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYGMVS-YVDDKVGQLLDTLERTGLADDTIVIFTSD 200
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 338 QGAHVEEvttRGEVHggsngiykggKANNWEGGIRVPGILRWPGvIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDRI-I 416
Cdd:cd16032  201 HGDMLGE---RGLWY----------KMSFFEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpL 266
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 417 DGRDLMPLLQGKSQRSDHEFLFHYCnfylnavrwhprnstsiwkaffftpkftpegANGCFSTHVCFCHGDY---ITHHH 493
Cdd:cd16032  267 DGRSLLPLLEGGDSGGEDEVISEYL-------------------------------AEGAVAPCVMIRRGRWkfiYCPGD 315
                        490
                 ....*....|.
gi 255653026 494 PPLLFDISKDP 504
Cdd:cd16032  316 PDQLFDLEADP 326
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
20-434 2.35e-44

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: 163.13  E-value: 2.35e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  20 SRPNFVLLMADDLgigDP--GCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPirsgmasqSKVGVF 97
Cdd:cd16030    1 KKPNVLFIAVDDL---RPwlGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRP--------DTTGVY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  98 LF-SASSGGLPTSeITFAKLLKNQGYSTALIGK-WHlgtncHNKTDFCHHPLSHGFDYFHGLPVTNLRDCKPGEGTVFTT 175
Cdd:cd16030   70 DNnSYFRKVAPDA-VTLPQYFKENGYTTAGVGKiFH-----PGIPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 176 GIRMLVSVPLQL-------IAIALLTLAVLKCLGLLPTPglvFFcllflaavilgLVVCF---------------LYyfr 233
Cdd:cd16030  144 GGGGPAWEAADVpdeaypdGKVADEAIEQLRKLKDSDKP---FF-----------LAVGFykphlpfvapkkyfdLY--- 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 234 PLNCFLMRNHEITQQ--PLSYDHLtqrltEDAAEFIRRNAETPfllvlsylHVHTALFsSKDFAGKSKHGAYGDTAeEMD 311
Cdd:cd16030  207 PLESIPLPNPFDPIDlpEVAWNDL-----DDLPKYGDIPALNP--------GDPKGPL-PDEQARELRQAYYASVS-YVD 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 312 WSVGQILNVLDELRLANNTLIYFSSDQGAHVeevttrGEvhggsNGIYkgGKANNWEGGIRVPGILRWPGVIPAGLEIDE 391
Cdd:cd16030  272 AQVGRVLDALEELGLADNTIVVLWSDHGWHL------GE-----HGHW--GKHTLFEEATRVPLIIRAPGVTKPGKVTDA 338
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 255653026 392 PTSNMDIFPTVAKLAGSPLPEDriIDGRDLMPLLQGKSQRSDH 434
Cdd:cd16030  339 LVELVDIYPTLAELAGLPAPPC--LEGKSLVPLLKNPSAKWKD 379
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
20-526 9.30e-44

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: 160.04  E-value: 9.30e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  20 SRPNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQ-HLAAS---PLCTPSRAAFMTGRYpirsgmasqskvg 95
Cdd:cd16155    1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNMGGwsgAVCVPSRAMLMTGRT------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  96 vfLFSASSGG---LPTSEITFAKLLKNQGYSTALIGKWHLGtnCHNKTDfchhplshgfDYFHGLPVTNlrdcKPgegtv 172
Cdd:cd16155   68 --LFHAPEGGkaaIPSDDKTWPETFKKAGYRTFATGKWHNG--FADAAI----------EFLEEYKDGD----KP----- 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 173 fttgirmlvsvplqliaialltlavlkclgllptpglvFFCLL-FLAavilglvvcflyyfrPlncflmrnHEITQQPls 251
Cdd:cd16155  125 --------------------------------------FFMYVaFTA---------------P--------HDPRQAP-- 141
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 252 ydhltqrltedaAEFIRR-NAETPfLLVLSYLHVHT---ALFSSKDFAG----------KSKHGAYGDTAEEMDWSVGQI 317
Cdd:cd16155  142 ------------PEYLDMyPPETI-PLPENFLPQHPfdnGEGTVRDEQLapfprtpeavRQHLAEYYAMITHLDAQIGRI 208
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 318 LNVLDELRLANNTLIYFSSDQGAHVeevttrgevhgGSNGIYkgGKANNWEGGIRVPGILRWPGvIPAGLEIDEPTSNMD 397
Cdd:cd16155  209 LDALEASGELDNTIIVFTSDHGLAV-----------GSHGLM--GKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQD 274
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 398 IFPTVAKLAGSPLPEDriIDGRDLMPLLQGKSQRSdHEFLFHYCNFYLNAVRwhprnsTSIWKAFFFTPKftpegangcf 477
Cdd:cd16155  275 VFPTLCELAGIEIPES--VEGKSLLPVIRGEKKAV-RDTLYGAYRDGQRAIR------DDRWKLIIYVPG---------- 335
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 255653026 478 STHVcfchgdyithhhppLLFDISKDPRERNPLtmTTEPRFQEILEAMQ 526
Cdd:cd16155  336 VKRT--------------QLFDLKKDPDELNNL--ADEPEYQERLKKLL 368
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
22-528 1.21e-43

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: 160.46  E-value: 1.21e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKVGVflfsA 101
Cdd:cd16033    1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAG----A 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 SSGGLPTSEITFAKLLKNQGYSTALIGKWHLGTNchnktdfcHHPLSHGFDYFHglpvtnlrdckPGEGTVfttgirmlv 181
Cdd:cd16033   77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPE--------ETPLDYGFDEYL-----------PVETTI--------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 182 svplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplncflmrnheitqqplsyDHltqRLTE 261
Cdd:cd16033  129 -----------------------------------------------------------------------EY---FLAD 134
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 262 DAAEFIRRNA--ETPFLLVLSYLHVHTALFSSK-------------------DFAGK-------SKHGAyGDTAEEMDWS 313
Cdd:cd16033  135 RAIEMLEELAadDKPFFLRVNFWGPHDPYIPPEpyldmydpediplpesfadDFEDKpyiyrreRKRWG-VDTEDEEDWK 213
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 314 ----------------VGQILNVLDELRLANNTLIYFSSDqgaHveevttrGEVHGGSNGIYKGgkANNWEGGIRVPGIL 377
Cdd:cd16033  214 eiiahywgyitliddaIGRILDALEELGLADDTLVIFTSD---H-------GDALGAHRLWDKG--PFMYEETYRIPLII 281
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 378 RWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDriIDGRDLMPLLQGKSQ---RSDHEFLFHYCNFYLNAVRWHPRN 454
Cdd:cd16033  282 KWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK--VDGRSLLPLLRGEQPedwRDEVVTEYNGHEFYLPQRMVRTDR 359
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255653026 455 stsiWKaFFFTPKFTPEgangcfsthvcfchgdyithhhpplLFDISKDPRERNPLtmTTEPRFQEILEAMQQA 528
Cdd:cd16033  360 ----YK-YVFNGFDIDE-------------------------LYDLESDPYELNNL--IDDPEYEEILREMRTR 401
PRK13759 PRK13759
arylsulfatase; Provisional
18-527 4.74e-39

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 149.43  E-value: 4.74e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  18 ATSRPNFVLLMADDLGiGDP-GCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKVGV 96
Cdd:PRK13759   3 QTKKPNIILIMVDQMR-GDClGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  97 FLFsassgglptsEITFAKLLKNQGYSTALIGKWHLgtnchnktdfchHP--LSHGFDYfhglpvTNLRDCKPGEGTVFT 174
Cdd:PRK13759  82 WNY----------KNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHDGYLHSGRNED 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 175 TGIRMLVSVPLQLIAialltlavLKCLGLLPTpglvffcllflaAVILGlvvcflyyfrpLNCflmrnHEITQQPLSYD- 253
Cdd:PRK13759 134 KSQFDFVSDYLAWLR--------EKAPGKDPD------------LTDIG-----------WDC-----NSWVARPWDLEe 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 254 --HLTQRLTEDAAEFIRRNAET-PFLLVLSYLHVH---------------------------------------TALFS- 290
Cdd:PRK13759 178 rlHPTNWVGSESIEFLRRRDPTkPFFLKMSFARPHspydppkryfdmykdadipdphigdweyaedqdpeggsiDALRGn 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 291 -SKDFAGKSKHGAYGDTAeEMDWSVGQILNVLDELRLANNTLIYFSSDqgahveevttrgevHG---GSNGIYKggKANN 366
Cdd:PRK13759 258 lGEEYARRARAAYYGLIT-HIDHQIGRFLQALKEFGLLDNTIILFVSD--------------HGdmlGDHYLFR--KGYP 320
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 367 WEGGIRVPGILRWPG---VIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDriIDGRDLMPLLQGKSQ--RS--DHEFLFH 439
Cdd:PRK13759 321 YEGSAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYEgwRPylHGEHALG 398
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 440 YCNF-YLNAVRWhprnsTSIWkaffftpkFTPEGANGcfsthvcfchgdyithhhpplLFDISKDPRERNPLtmTTEPRF 518
Cdd:PRK13759 399 YSSDnYLTDGKW-----KYIW--------FSQTGEEQ---------------------LFDLKKDPHELHNL--SPSEKY 442

                 ....*....
gi 255653026 519 QEILEAMQQ 527
Cdd:PRK13759 443 QPRLREMRK 451
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
22-423 6.98e-39

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 143.46  E-value: 6.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLM-----ADDLGigdpgCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPirsgmasqskvgv 96
Cdd:cd16148    1 MNVILIVidslrADHLG-----CYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  97 FLFSASSGGLPTSEITFAKLLKNQGYSTALIgkwhlgtnchnkTDFCHHPLSHGFD--YFHGLPVTNLRDCKPGEGtvft 174
Cdd:cd16148   63 FYHGVWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFDrgFDTFEDFRGQEGDPGEEG---- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 175 tgirmlvsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplncflmrnheitqqplsyDH 254
Cdd:cd16148  127 ------------------------------------------------------------------------------DE 128
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 255 LTQRLTEDAAEFIRRNAET-PFllvlsYLHVHtaLFSSkdfagkskHGAYGDTAE--EMDWSVGQILNVLDELRLANNTL 331
Cdd:cd16148  129 RAERVTDRALEWLDRNADDdPF-----FLFLH--YFDP--------HEPYLYDAEvrYVDEQIGRLLDKLKELGLLEDTL 193
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 332 IYFSSDQGahvEEVttrGEvhggsNGIYKGGKANNWEGGIRVPGILRWPGVIPAGlEIDEPTSNMDIFPTVAKLAGSPLP 411
Cdd:cd16148  194 VIVTSDHG---EEF---GE-----HGLYWGHGSNLYDEQLHVPLIIRWPGKEPGK-RVDALVSHIDIAPTLLDLLGVEPP 261
                        410
                 ....*....|..
gi 255653026 412 EDriIDGRDLMP 423
Cdd:cd16148  262 DY--SDGRSLLP 271
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
21-419 2.54e-38

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: 145.39  E-value: 2.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  21 RPNFVLLMADDLGIGDPG-CYGNKTLRtpnidRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKVGVFLF 99
Cdd:cd16147    1 RPNIVLILTDDQDVELGSmDPMPKTKK-----LLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPPGGGYP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 100 SASSGGLPTSeiTFAKLLKNQGYSTALIGKwHLgtNCHNKTDFCHH-PLshGFDYFHGLpVTNLRdckpgegtvfttgir 178
Cdd:cd16147   76 KFWQNGLERS--TLPVWLQEAGYRTAYAGK-YL--NGYGVPGGVSYvPP--GWDEWDGL-VGNST--------------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 179 mlvsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflYYFRPLNcflmrNHEITQQPLSY--DHLT 256
Cdd:cd16147  133 ---------------------------------------------------YYNYTLS-----NGGNGKHGVSYpgDYLT 156
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 257 QRLTEDAAEFIRRNAET--PFLLVLSYL--HV-------HTALFS--------SKDFAGKSKHGAY-----GDTAEEMDW 312
Cdd:cd16147  157 DVIANKALDFLRRAAADdkPFFLVVAPPapHGpftpaprYANLFPnvtapprpPPNNPDVSDKPHWlrrlpPLNPTQIAY 236
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 313 S-----------------VGQILNVLDELRLANNTLIYFSSDQGAHVeevttrGEvHGgsngiYKGGKANNWEGGIRVPG 375
Cdd:cd16147  237 IdelyrkrlrtlqsvddlVERLVNTLEATGQLDNTYIIYTSDNGYHL------GQ-HR-----LPPGKRTPYEEDIRVPL 304
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 255653026 376 ILRWPGvIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDriIDGR 419
Cdd:cd16147  305 LVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
22-406 2.30e-37

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: 138.32  E-value: 2.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVkLTQHLAASPLC--TPSRAAFMTGRYPIRSGMASQSKVGVFLF 99
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGA-TFNFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 100 SaSSGGLPTSEITFAKLLKNQGYSTALIGkwhlgtnchnktdfchhplshgfdyfhglpvtnlrdckpgegtvfttgirm 179
Cdd:cd00016   80 S-RAAGKDEDGPTIPELLKQAGYRTGVIG--------------------------------------------------- 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 180 lvsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplncflmrnheitqqplsydhltqrl 259
Cdd:cd00016      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 260 tedAAEFIRRNA-ETPFLLVLSYLHVHTALFSSKdfagkSKHGAYGDTAEEMDWSVGQILNVLDELRLANNTLIYFSSDQ 338
Cdd:cd00016  108 ---LLKAIDETSkEKPFVLFLHFDGPDGPGHAYG-----PNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADH 179
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255653026 339 GAHVEEvttrgevHGGSNGiyKGGKANNWEGGIRVPGILRWPGViPAGLEIDEPTSNMDIFPTVAKLA 406
Cdd:cd00016  180 GGIDKG-------HGGDPK--ADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
21-527 1.14e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 140.44  E-value: 1.14e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  21 RPNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPirsgmasqSKVGVFlfs 100
Cdd:cd16152    1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYP--------TETGCF--- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 101 ASSGGLPTSEITFAKLLKNQGYSTALIGKWHLGTnchNKTDFchhplshgfdyfhglpvtnlrdckpgegtvfttgirml 180
Cdd:cd16152   70 RNGIPLPADEKTLAHYFRDAGYETGYVGKWHLAG---YRVDA-------------------------------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 181 vsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplncflmrnheitqqplsydhltqrLT 260
Cdd:cd16152  109 ------------------------------------------------------------------------------LT 110
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 261 EDAAEFIR-RNAETPFLLVLSYLHVH----TALFSSKDFAgKSKHGAY----------GDTAEE----------MDWSVG 315
Cdd:cd16152  111 DFAIDYLDnRQKDKPFFLFLSYLEPHhqndRDRYVAPEGS-AERFANFwvppdlaalpGDWAEElpdylgccerLDENVG 189
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 316 QILNVLDELRLANNTLIYFSSDQGAHVEevtTRgevhggsNGIYkggKANNWEGGIRVPGILRWPGvIPAGLEIDEPTSN 395
Cdd:cd16152  190 RIRDALKELGLYDNTIIVFTSDHGCHFR---TR-------NAEY---KRSCHESSIRVPLVIYGPG-FNGGGRVEELVSL 255
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 396 MDIFPTVAKLAGSPLPEDriIDGRDLMPLLQGKSQRSDHEFLFHYCNFYL-NAVRwhprnsTSIWKAFFFTPKFTPEGAN 474
Cdd:cd16152  256 IDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNEVFIQISESQVgRAIR------TDRWKYSVAAPDKDGWKDS 327
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255653026 475 GcfSTHvcfchgdYITHHhpplLFDISKDPRERNPLtmTTEPRFQEILEAMQQ 527
Cdd:cd16152  328 G--SDV-------YVEDY----LYDLEADPYELVNL--IGRPEYREVAAELRE 365
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
22-437 1.30e-33

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: 133.66  E-value: 1.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSkvgvflfsa 101
Cdd:cd16156    1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNC--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 ssggLPTSE--ITFAKLLKNQGYSTALIGKWHLgtnchnktdfchhplsHGFDYFhGLPVtnlrdCKPG-EGTVFTTGIR 178
Cdd:cd16156   72 ----MALGDnvKTIGQRLSDNGIHTAYIGKWHL----------------DGGDYF-GNGI-----CPQGwDPDYWYDMRN 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 179 MLVSVPLQLIAIALLTLAVLKclgllptpglvffcllflaavilglvvcflyyfrplncflmrNHEITQQpLSYDHltqR 258
Cdd:cd16156  126 YLDELTEEERRKSRRGLTSLE------------------------------------------AEGIKEE-FTYGH---R 159
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 259 LTEDAAEFIRRNAETPFLLVLSYLHVH-----TALFSSK--------------DFAGKSKH------GAYGDTAEEM--- 310
Cdd:cd16156  160 CTNRALDFIEKHKDEDFFLVVSYDEPHhpflcPKPYASMykdfefpkgenaydDLENKPLHqrlwagAKPHEDGDKGtik 239
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 311 -----------DWSVGQILNVLDElrLANNTLIYFSSDqgahveevttrgevHG---GSNGIYKGGKAnNWEGGIRVPGI 376
Cdd:cd16156  240 hplyfgcnsfvDYEIGRVLDAADE--IAEDAWVIYTSD--------------HGdmlGAHKLWAKGPA-VYDEITNIPLI 302
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255653026 377 LRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEdrIIDGRDLMPLLQGKSQRSDHEFL 437
Cdd:cd16156  303 IRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPK--VLEGESILATIEDPEIPENRGVF 361
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
22-528 2.24e-31

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: 126.99  E-value: 2.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMAsQSKVgvflfsa 101
Cdd:cd16028    1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV-WNGT------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 ssgGLPTSEITFAKLLKNQGYSTALIGkwhlgtnchnKTDFchhplshgfdyfhglpVTNLRDCKPGegtvfttGIRMLV 181
Cdd:cd16028   73 ---PLDARHLTLALELRKAGYDPALFG----------YTDT----------------SPDPRGLAPL-------DPRLLS 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 182 SvplqliaialltlavlkclgLLPTPGlvffcllflaavilglvvcflyyFRPLNcflmRNHEITQQplsyDHLTQRLTE 261
Cdd:cd16028  117 Y--------------------ELAMPG-----------------------FDPVD----RLDEYPAE----DSDTAFLTD 145
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 262 DAAEFIRRNAETPFLLVLSYLHVHTALF----------------------------------------SSKDFAGKSKHG 301
Cdd:cd16028  146 RAIEYLDERQDEPWFLHLSYIRPHPPFVapapyhalydpadvpppiraeslaaeaaqhpllaafleriESLSFSPGAANA 225
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 302 AYGDTAE-------------EMDWSVGQILNVLDELRLANNTLIYFSSDQGAHVeevttrGEVH-GGSNGIYkggkannw 367
Cdd:cd16028  226 ADLDDEEvaqmratylgliaEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQL------GDHWlWGKDGFF-------- 291
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 368 EGGIRVPGILRWPGViPA----GLEIDEPTSNMDIFPTVAKLAGSPLPedRIIDGRDLMPLLQGkSQRSDHEFLFHYCNF 443
Cdd:cd16028  292 DQAYRVPLIVRDPRR-EAdatrGQVVDAFTESVDVMPTILDWLGGEIP--HQCDGRSLLPLLAG-AQPSDWRDAVHYEYD 367
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 444 YLNAVRWHPRNSTSIwkaffftpkfTPEGANGC--FSTHVcfchgDYItHH--HPPLLFDISKDPRERNPLtmTTEPRFQ 519
Cdd:cd16028  368 FRDVSTRRPQEALGL----------SPDECSLAviRDERW-----KYV-HFaaLPPLLFDLKNDPGELRDL--AADPAYA 429

                 ....*....
gi 255653026 520 EILEAMQQA 528
Cdd:cd16028  430 AVVLRYAQK 438
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
21-421 6.78e-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: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 121.71  E-value: 6.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  21 RPNFVLLMADDLGIGDPGCYGNKT----------LRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSgmas 90
Cdd:cd16153    1 KPNILWIITDDQRVDSLSCYNNAHtgksesrlgyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRT---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  91 qskvGVFLFSASSGGLPTSEITFAKLLKNQGYSTALIGKWHLGTnchnktdfchhplshgfdyfhglpvtnlrdckpgeg 170
Cdd:cd16153   77 ----GVYGFEAAHPALDHGLPTFPEVLKKAGYQTASFGKSHLEA------------------------------------ 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 171 tvFTtgiRMLVsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfRPLNCFLMRNHEITQQPL 250
Cdd:cd16153  117 --FQ---RYLK---------------------------------------------------NANQSYKSFWGKIAKGAD 140
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 251 SydhltqrltedaaefirrnaETPFLLVLSYLHVHTALFSSKDFAGK-SKHG--AYGDTaeemdwSVGQILNVLDELRLA 327
Cdd:cd16153  141 S--------------------DKPFFVRLSFLQPHTPVLPPKEFRDRfDYYAfcAYGDA------QVGRAVEAFKAYSLK 194
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 328 N---NTLIYFSSDQGAHVeevttrgevhgGSNGIYkgGKANNWEGGIRVPGILRWPGVI--PAGLEIDEPTSNMDIFPTV 402
Cdd:cd16153  195 QdrdYTIVYVTGDHGWHL-----------GEQGIL--AKFTFWPQSHRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTL 261
                        410
                 ....*....|....*....
gi 255653026 403 AKLAGSPLPEDRIIDGRDL 421
Cdd:cd16153  262 LAAAGVDVDAPDYLDGRDL 280
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
22-430 7.82e-30

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: 120.92  E-value: 7.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTL--RTPNIDRLAEGGVKLTqHLAASPLCTPSRAAFMTGRYPIRSGMasqskvgvflf 99
Cdd:cd16154    1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGV----------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 100 SASSGGLPTSEITFAKLLK----NQGYSTALIGKWHLGtNCHNktdfcHHPLSHGFDYFHGLPVTNLRDckpgegtvftt 175
Cdd:cd16154   69 LAVPDELLLSEETLLQLLIkdatTAGYSSAVIGKWHLG-GNDN-----SPNNPGGIPYYAGILGGGVQD----------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 176 girmlvsvplqliaialltlavlkclgllptpglvffcllflaavilglvvcflYYFRPLNcflmrNHEITQQPLSYdhL 255
Cdd:cd16154  132 ------------------------------------------------------YYNWNLT-----NNGQTTNSTEY--A 150
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 256 TQRLTEDAAEFIrRNAETPFLLVLSYLHVHT-------ALFSSKDFAGKSKHGA-----YGDTAEEMDWSVGQILNVLDE 323
Cdd:cd16154  151 TTKLTNLAIDWI-DQQTKPWFLWLAYNAPHTpfhlppaELHSRSLLGDSADIEAnprpyYLAAIEAMDTEIGRLLASIDE 229
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 324 LRLaNNTLIYFSSDQGAHVEEVTTRGEVHGGSNGIYkggkannwEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVA 403
Cdd:cd16154  230 EER-ENTIIIFIGDNGTPGQVVDLPYTRNHAKGSLY--------EGGINVPLIVSGAGVERANERESALVNATDLYATIA 300
                        410       420
                 ....*....|....*....|....*..
gi 255653026 404 KLAGSPLPEdrIIDGRDLMPLLQGKSQ 430
Cdd:cd16154  301 ELAGVDAAE--IHDSVSFKPLLSDVNA 325
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
22-440 1.00e-29

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: 119.23  E-value: 1.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPirsgmaSQSKVGVFLFSA 101
Cdd:cd16035    1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHP------QQTGVTDTLGSP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 SSGGLPTSEITFAKLLKNQGYSTALIGKWHLgtnchnktdfchhplSHGfdyfhglpvtnlrdckPGEGTVFTTGIrmlv 181
Cdd:cd16035   75 MQPLLSPDVPTLGHMLRAAGYYTAYKGKWHL---------------SGA----------------AGGGYKRDPGI---- 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 182 svplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplncflmrnheitqqplsydhltqrlTE 261
Cdd:cd16035  120 ------------------------------------------------------------------------------AA 121
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 262 DAAEFIRR-----NAETPFLLVLSYLHVHTALFSSKDfAGKSKHGA--YGDTAEEMDWSVGQILNVLDELRLANNTLIYF 334
Cdd:cd16035  122 QAVEWLRErgaknADGKPWFLVVSLVNPHDIMFPPDD-EERWRRFRnfYYNLIRDVDRQIGRVLDALDASGLADNTIVVF 200
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 335 SSDQGahvEevttRGEVHGGSngiykgGKANN-WEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPLPED 413
Cdd:cd16035  201 TSDHG---E----MGGAHGLR------GKGFNaYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEAR 267
                        410       420       430
                 ....*....|....*....|....*....|..
gi 255653026 414 RIID----GRDLMPLLQGKSQRSDHE-FLFHY 440
Cdd:cd16035  268 ATEApplpGRDLSPLLTDADADAVRDgILFTY 299
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
22-427 1.70e-28

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 118.11  E-value: 1.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLGIGDPGCYGNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSkvgvFLfsa 101
Cdd:cd16150    1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLH----HL--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 102 ssggLPTSEITFAKLLKNQGYSTALIGKWHLGTNCHNKTDFChhplshgfdyfhglpvtnLRDckpgEGTVFTtgirmlv 181
Cdd:cd16150   74 ----LRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC------------------DSD----EACVRT------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 182 svplqliAIALLTLAVlkclglLPTPglvfFClLFLAavilglvvcflyyfrplncfLMRNHEITQQPLSYDHLTQRltE 261
Cdd:cd16150  121 -------AIDWLRNRR------PDKP----FC-LYLP--------------------LIFPHPPYGVEEPWFSMIDR--E 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 262 DAAEFIRRNAETPFLLVLSYLHVHTALFSSKDFAGKSKHGAYGDTAEEMDWSVGQILNVLDELRLANNTLIYFSSDqgah 341
Cdd:cd16150  161 KLPPRRPPGLRAKGKPSMLEGIEKQGLDRWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSD---- 236
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 342 veevttrgevHGGSNGIYkgGKANNWEGGI-----RVPGILRWPGVIPAGLeIDEPTSNMDIFPTVAKLAGSPLPEDRIi 416
Cdd:cd16150  237 ----------HGDYTGDY--GLVEKWPNTFedcltRVPLIIKPPGGPAGGV-SDALVELVDIPPTLLDLAGIPLSHTHF- 302
                        410
                 ....*....|.
gi 255653026 417 dGRDLMPLLQG 427
Cdd:cd16150  303 -GRSLLPVLAG 312
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
22-504 4.47e-20

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: 92.22  E-value: 4.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  22 PNFVLLMADDLG---IGDPGcygNKTLRTPNIDRLAEGGVKLTQHLAASPLCTPSRAAFMTGRYPIRSGMASQSKvgvfl 98
Cdd:cd16171    1 PNVVMVMSDSFDgrlTFRPG---NQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYK----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  99 fsassgGLPTSEITFAKLLKNQGYSTALIGKwhlgtnchnkTDFC--HHPLSHGFDYF----------HGLPVTNLrdck 166
Cdd:cd16171   73 ------GLDPNYPTWMDRLEKHGYHTQKYGK----------LDYTsgHHSVSNRVEAWtrdvpfllrqEGRPTVNL---- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 167 pgegtvftTGIRMLVSVplqliaialltlavlkclgllptpglvffcllflaavilglvvcflyyfrplncfLMRNHEIT 246
Cdd:cd16171  133 --------VGDRSTVRV-------------------------------------------------------MLKDWQNT 149
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 247 qqplsyDHLTQRLTEDAAefirrNAETPFLLVL--SYLHVHTALFSSKDFAGKSKHGA--YGDTAEeMDWSVGQILNVLD 322
Cdd:cd16171  150 ------DKAVHWIRKEAP-----NLTQPFALYLglNLPHPYPSPSMGENFGSIRNIRAfyYAMCAE-TDAMLGEIISALK 217
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 323 ELRLANNTLIYFSSDQGAHVEEvttrgevhggSNGIYKggkANNWEGGIRVPGILRWPGvIPAGLEIDEPTSNMDIFPTV 402
Cdd:cd16171  218 DTGLLDKTYVFFTSDHGELAME----------HRQFYK---MSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTM 283
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 403 AKLAGSPLPEDriIDGRDLMPLLQGKSQ-----RSDHEFL----FHYCNfyLNAVRWHPRnsTSIWKaffftpkftpega 473
Cdd:cd16171  284 LDIAGVPQPQN--LSGYSLLPLLSESSIkespsRVPHPDWvlseFHGCN--VNASTYMLR--TNSWK------------- 344
                        490       500       510
                 ....*....|....*....|....*....|.
gi 255653026 474 ngcfstHVCFCHGDYIthhhPPLLFDISKDP 504
Cdd:cd16171  345 ------YIAYADGNSV----PPQLFDLSKDP 365
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
257-401 2.28e-10

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: 63.39  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 257 QRLTEDAAEFI-RRNAETPFLLVLSYLHVHTALF------------------SSKDFAGKSKHGAYGDTAEEMDWSVGQI 317
Cdd:COG3083  364 RQITAQWLQWLdQRDSDRPWFSYLFLDAPHAYSFpadypkpfqpsedcnylaLDNESDPTPFKNRYRNAVHYVDSQIGRV 443
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 318 LNVLDELRLANNTLIYFSSDQGahvEEVTTRGEVHGGSNGIYkggkaNNWEggIRVPGILRWPGVIPAglEIDEPTSNMD 397
Cdd:COG3083  444 LDTLEQRGLLENTIVIITADHG---EEFNENGQNYWGHNSNF-----SRYQ--LQVPLVIHWPGTPPQ--VISKLTSHLD 511

                 ....
gi 255653026 398 IFPT 401
Cdd:COG3083  512 IVPT 515
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
259-407 8.34e-07

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: 50.76  E-value: 8.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 259 LTEDAAEFIRRNAETPFLLVL---------SYLHVHTALFSSKDfAGKSKHGAYGDTAEEMDWSVGQILNVLDELRLANN 329
Cdd:cd16015  142 LFDQALEELEELKKKPFFIFLvtmsnhgpyDLPEEKKDEPLKVE-EDKTELENYLNAIHYTDKALGEFIEKLKKSGLYEN 220
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255653026 330 TLIYFSSDqgahveevttrgevHGGSNGIYKGGKANNWEGGIRVPGILRWPGVIPaGLEIDEPTSNMDIFPTVAKLAG 407
Cdd:cd16015  221 TIIVIYGD--------------HLPSLGSDYDETDEDPLDLYRTPLLIYSPGLKK-PKKIDRVGSQIDIAPTLLDLLG 283
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
296-422 2.32e-06

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 50.42  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 296 GKSKHGAYGDTAEEMDWSVGQILNVLDELRLANNTLIYFSSDqgahveevttrgevHGGSngIYKGGKANNWEGGIRVPG 375
Cdd:COG1368  412 GKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGD--------------HGPR--SPGKTDYENPLERYRVPL 475
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 255653026 376 ILRWPGVIPAGlEIDEPTSNMDIFPTVAKLAGSPLPEDRIIdGRDLM 422
Cdd:COG1368  476 LIYSPGLKKPK-VIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
42-88 9.05e-04

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: 41.64  E-value: 9.05e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 255653026   42 NKTLRTPNIDRLAEGGVKLTQHLAASPLCT-PSRAAFMTGRYPIRSGM 88
Cdd:pfam01663  15 DRFELTPNLAALAKEGVSAPNLTPVFPTLTfPNHYTLVTGLYPGSHGI 62
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
46-161 1.60e-03

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 40.89  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026  46 RTPNIDRLAEGGVKLTQHLAASPLCT-PSRAAFMTGRYPIRSGMAS------QSKVGVFLFSASSGGLPTSEI----TFA 114
Cdd:COG1524   43 HAPNLAALAARGVYARPLTSVFPSTTaPAHTTLLTGLYPGEHGIVGngwydpELGRVVNSLSWVEDGFGSNSLlpvpTIF 122
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 255653026 115 KLLKNQGYSTALIGKWHlgtncHNKTDFCHHPLSHGFD---YFHGLPVTN 161
Cdd:COG1524  123 ERARAAGLTTAAVFWPS-----FEGSGLIDAARPYPYDgrkPLLGNPAAD 167
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
275-415 3.18e-03

GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293743 [Multi-domain]  Cd Length: 292  Bit Score: 39.65  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 275 FLLVLSYLHVHtalfsskdfaGKSKHGAYGDTAEEMDWSVGQILNvldelRLANNTLIYFSSDQGahveeVTTRGEvHGG 354
Cdd:cd16019  160 FLGLDHLGHKH----------NTTSSPELEKKLDQMDNLIRDIYD-----RMDNDTLLVVVSDHG-----MNNDGN-HGG 218
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255653026 355 SN---------GIYKGGKANNWEGGIRVPGILRWPGVIPAGLEIDEPTSNMDIFPTVAKLAGSPLPEDRI 415
Cdd:cd16019  219 SSteetssfffFISKKGFFKKRPIDQIEKIKQNNEQQKIDPSEYIRIIYQIDILPTICYLLGIPIPFNNI 288
 
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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