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Conserved domains on  [gi|1482818008|ref|WP_119861300|]
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sulfatase-like hydrolase/transferase [Pseudoalteromonas sp. MSK9-3]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 10888421)

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
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
155-532 0e+00

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: 604.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYSTDLPKTPILDSLATSGVVFDNAWATPACTTTRGTIMTGMHGVNSGVSFVPAVMDTSLT 234
Cdd:cd16154     1 PNILLIIADDQGLDSSAQYSLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGVLAVPDELLLSEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 235 TLPRFLAENDASKAYSMAVFGKWHLGGGDPDLSHPNsaGVGHYVGNITGTLDDYSDWTLTDNGSQTQVTQYHTSKVTDLA 314
Cdd:cd16154    81 TLLQLLIKDATTAGYSSAVIGKWHLGGNDNSPNNPG--GIPYYAGILGGGVQDYYNWNLTNNGQTTNSTEYATTKLTNLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 315 MDWITQQTSPWFVWLAYVAPHSPFHLPPNELHTRSELSGSAeDIAQNPRPYYLAAIEAMDTEIGRLLASLPTDERENTLV 394
Cdd:cd16154   159 IDWIDQQTKPWFLWLAYNAPHTPFHLPPAELHSRSLLGDSA-DIEANPRPYYLAAIEAMDTEIGRLLASIDEEERENTII 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 395 IFIGDNGTPAPVIDTSvYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSF 474
Cdd:cd16154   238 IFIGDNGTPGQVVDLP-YTRNHAKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAEIHDSVSF 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1482818008 475 YDTLFDVvpNPSVRQYNYADFQRNGVAGWAVRNQDYKLLSIDSQQQALFDMNVDINEQ 532
Cdd:cd16154   317 KPLLSDV--NASTRQYNYTEYESPTTTGWATRNQYYKLIESENGQEELYDLINDPSEQ 372
 
Name Accession Description Interval E-value
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
155-532 0e+00

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: 604.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYSTDLPKTPILDSLATSGVVFDNAWATPACTTTRGTIMTGMHGVNSGVSFVPAVMDTSLT 234
Cdd:cd16154     1 PNILLIIADDQGLDSSAQYSLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGVLAVPDELLLSEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 235 TLPRFLAENDASKAYSMAVFGKWHLGGGDPDLSHPNsaGVGHYVGNITGTLDDYSDWTLTDNGSQTQVTQYHTSKVTDLA 314
Cdd:cd16154    81 TLLQLLIKDATTAGYSSAVIGKWHLGGNDNSPNNPG--GIPYYAGILGGGVQDYYNWNLTNNGQTTNSTEYATTKLTNLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 315 MDWITQQTSPWFVWLAYVAPHSPFHLPPNELHTRSELSGSAeDIAQNPRPYYLAAIEAMDTEIGRLLASLPTDERENTLV 394
Cdd:cd16154   159 IDWIDQQTKPWFLWLAYNAPHTPFHLPPAELHSRSLLGDSA-DIEANPRPYYLAAIEAMDTEIGRLLASIDEEERENTII 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 395 IFIGDNGTPAPVIDTSvYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSF 474
Cdd:cd16154   238 IFIGDNGTPGQVVDLP-YTRNHAKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAEIHDSVSF 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1482818008 475 YDTLFDVvpNPSVRQYNYADFQRNGVAGWAVRNQDYKLLSIDSQQQALFDMNVDINEQ 532
Cdd:cd16154   317 KPLLSDV--NASTRQYNYTEYESPTTTGWATRNQYYKLIESENGQEELYDLINDPSEQ 372
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
150-551 2.46e-83

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 265.20  E-value: 2.46e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 150 PPVSKPNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFV--- 225
Cdd:COG3119    19 AAAKRPNILFILADDLGYGDLG--CYGNPLIKTPNIDRLAAEGVRFTNAYVTsPVCSPSRASLLTGRYPHRTGVTDNgeg 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 226 -PAVMDTSLTTLPRFLAENDaskaYSMAVFGKWHLgggdpdlshpnsagvghyvgnitgtlddysdwtltdngsqtqvtq 304
Cdd:COG3119    97 yNGGLPPDEPTLAELLKEAG----YRTALFGKWHL--------------------------------------------- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 305 YHTSKVTDLAMDWITQQTS---PWFVWLAYVAPHSPFHLPPN----------ELHTRSELSGSAEDIAQNPRPYYLAAIE 371
Cdd:COG3119   128 YLTDLLTDKAIDFLERQADkdkPFFLYLAFNAPHAPYQAPEEyldkydgkdiPLPPNLAPRDLTEEELRRARAAYAAMIE 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 372 AMDTEIGRLLASLptDE---RENTLVIFIGDNGTPAPVidtsvYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLV 448
Cdd:COG3119   208 EVDDQVGRLLDAL--EElglADNTIVVFTSDNGPSLGE-----HGLRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALV 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 449 NSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSVRQYNYADFQRNGvAGWAVRNQDYKLL--SIDSQQQALFDMN 526
Cdd:COG3119   281 SLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTG--EKAEWRDYLYWEYPRGG-GNRAIRTGRWKLIryYDDDGPWELYDLK 357
                         410       420
                  ....*....|....*....|....*
gi 1482818008 527 VDINEQNDLlqsGDDWSALVLELAE 551
Cdd:COG3119   358 NDPGETNNL---AADYPEVVAELRA 379
Sulfatase pfam00884
Sulfatase;
155-462 1.04e-45

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 162.98  E-value: 1.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYStdLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFVPAV-MDTS 232
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYP--RPTTPFLDRLAEEGLLFSNFYSGgTLTAPSRFALLTGLPPHNFGSYVSTPVgLPRT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 233 LTTLPRFLAEndasKAYSMAVFGKWHLGGGDPDlsHPNSAGVGHYVGNITGtLDDYSDWTltDNGSQTQVTQYHTSKVTD 312
Cdd:pfam00884  79 EPSLPDLLKR----AGYNTGAIGKWHLGWYNNQ--SPCNLGFDKFFGRNTG-SDLYADPP--DVPYNCSGGGVSDEALLD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 313 LAMDWITQQTSPWFVWLAYVAPHSPFHLPpNELHTRSELSGSAEDIAQNPRPYYLAAIEAMDTEIGRLLASLPTDE-REN 391
Cdd:pfam00884 150 EALEFLDNNDKPFFLVLHTLGSHGPPYYP-DRYPEKYATFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGlLDN 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1482818008 392 TLVIFIGDNGtpAPVIDTSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAG 462
Cdd:pfam00884 229 TLVVYTSDHG--ESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
PRK13759 PRK13759
arylsulfatase; Provisional
153-555 6.73e-31

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 125.94  E-value: 6.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 153 SKPNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAW-ATPACTTTRGTIMTGMHGVNSG-VSFVPAVMD 230
Cdd:PRK13759    5 KKPNIILIMVDQMRGDCLG--CNGNKAVETPNLDMLASEGYNFENAYsAVPSCTPARAALLTGLSQWHHGrVGYGDVVPW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 231 TSLTTLPRFLAENDaskaYSMAVFGKWH------LGGGDPDLSHPNSAGVGH-YVGNITGTLDDYSDW----------TL 293
Cdd:PRK13759   83 NYKNTLPQEFRDAG----YYTQCIGKMHvfpqrnLLGFHNVLLHDGYLHSGRnEDKSQFDFVSDYLAWlrekapgkdpDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 294 TDNG--SQTQVT-------QYH-TSKVTDLAMDWIT--QQTSPWFVWLAYVAPHSPFHlPPN------------------ 343
Cdd:PRK13759  159 TDIGwdCNSWVArpwdleeRLHpTNWVGSESIEFLRrrDPTKPFFLKMSFARPHSPYD-PPKryfdmykdadipdphigd 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 344 -ELHTRSELSGSA---------EDIAQNPRPYYLAAIEAMDTEIGRLLASLPT-DERENTLVIFIGDNGtpapvidtSVY 412
Cdd:PRK13759  238 wEYAEDQDPEGGSidalrgnlgEEYARRARAAYYGLITHIDHQIGRFLQALKEfGLLDNTIILFVSDHG--------DML 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 413 ARQH--SKNSLYEGGIRVPLLVS--GNLLNKQNTRES-RLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSV 487
Cdd:PRK13759  310 GDHYlfRKGYPYEGSAHIPFIIYdpGGLLAGNRGTVIdQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFG--QYEGW 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 488 RQY-------NYADFQrngvagWAVRNQD-YKLLSIDSQQQaLFDMNVDINEQNDLLQSG------DDW-SALVLELAEY 552
Cdd:PRK13759  388 RPYlhgehalGYSSDN------YLTDGKWkYIWFSQTGEEQ-LFDLKKDPHELHNLSPSEkyqprlREMrKKLVDHLRGR 460

                  ...
gi 1482818008 553 GQS 555
Cdd:PRK13759  461 EEG 463
 
Name Accession Description Interval E-value
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
155-532 0e+00

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: 604.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYSTDLPKTPILDSLATSGVVFDNAWATPACTTTRGTIMTGMHGVNSGVSFVPAVMDTSLT 234
Cdd:cd16154     1 PNILLIIADDQGLDSSAQYSLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGVLAVPDELLLSEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 235 TLPRFLAENDASKAYSMAVFGKWHLGGGDPDLSHPNsaGVGHYVGNITGTLDDYSDWTLTDNGSQTQVTQYHTSKVTDLA 314
Cdd:cd16154    81 TLLQLLIKDATTAGYSSAVIGKWHLGGNDNSPNNPG--GIPYYAGILGGGVQDYYNWNLTNNGQTTNSTEYATTKLTNLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 315 MDWITQQTSPWFVWLAYVAPHSPFHLPPNELHTRSELSGSAeDIAQNPRPYYLAAIEAMDTEIGRLLASLPTDERENTLV 394
Cdd:cd16154   159 IDWIDQQTKPWFLWLAYNAPHTPFHLPPAELHSRSLLGDSA-DIEANPRPYYLAAIEAMDTEIGRLLASIDEEERENTII 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 395 IFIGDNGTPAPVIDTSvYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSF 474
Cdd:cd16154   238 IFIGDNGTPGQVVDLP-YTRNHAKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAEIHDSVSF 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1482818008 475 YDTLFDVvpNPSVRQYNYADFQRNGVAGWAVRNQDYKLLSIDSQQQALFDMNVDINEQ 532
Cdd:cd16154   317 KPLLSDV--NASTRQYNYTEYESPTTTGWATRNQYYKLIESENGQEELYDLINDPSEQ 372
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
150-551 2.46e-83

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 265.20  E-value: 2.46e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 150 PPVSKPNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFV--- 225
Cdd:COG3119    19 AAAKRPNILFILADDLGYGDLG--CYGNPLIKTPNIDRLAAEGVRFTNAYVTsPVCSPSRASLLTGRYPHRTGVTDNgeg 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 226 -PAVMDTSLTTLPRFLAENDaskaYSMAVFGKWHLgggdpdlshpnsagvghyvgnitgtlddysdwtltdngsqtqvtq 304
Cdd:COG3119    97 yNGGLPPDEPTLAELLKEAG----YRTALFGKWHL--------------------------------------------- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 305 YHTSKVTDLAMDWITQQTS---PWFVWLAYVAPHSPFHLPPN----------ELHTRSELSGSAEDIAQNPRPYYLAAIE 371
Cdd:COG3119   128 YLTDLLTDKAIDFLERQADkdkPFFLYLAFNAPHAPYQAPEEyldkydgkdiPLPPNLAPRDLTEEELRRARAAYAAMIE 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 372 AMDTEIGRLLASLptDE---RENTLVIFIGDNGTPAPVidtsvYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLV 448
Cdd:COG3119   208 EVDDQVGRLLDAL--EElglADNTIVVFTSDNGPSLGE-----HGLRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALV 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 449 NSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSVRQYNYADFQRNGvAGWAVRNQDYKLL--SIDSQQQALFDMN 526
Cdd:COG3119   281 SLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTG--EKAEWRDYLYWEYPRGG-GNRAIRTGRWKLIryYDDDGPWELYDLK 357
                         410       420
                  ....*....|....*....|....*
gi 1482818008 527 VDINEQNDLlqsGDDWSALVLELAE 551
Cdd:COG3119   358 NDPGETNNL---AADYPEVVAELRA 379
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
155-535 3.10e-68

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: 226.28  E-value: 3.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDasnqysystDL-----P--KTPILDSLATSGVVFDNAWATPACTTTRGTIMTGMHGVNSGVSFVPA 227
Cdd:cd16146     1 PNVILILTDDQGYG---------DLgfhgnPilKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTGVWHTIL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 228 V---MDTSLTTLPRFLAENdaskAYSMAVFGKWHLGGGDPdlSHPNSAG----VGHYVGNITGTLD----DYSDWTLTDN 296
Cdd:cd16146    72 GrerMRLDETTLAEVFKDA----GYRTGIFGKWHLGDNYP--YRPQDRGfdevLGHGGGGIGQYPDywgnDYFDDTYYHN 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 297 GSQTQVTQYHTSKVTDLAMDWI-TQQTSPWFVWLAYVAPHSPFHLPPnelhtrsELSGSAEDIAQNP-RPYYLAAIEAMD 374
Cdd:cd16146   146 GKFVKTEGYCTDVFFDEAIDFIeENKDKPFFAYLATNAPHGPLQVPD-------KYLDPYKDMGLDDkLAAFYGMIENID 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 375 TEIGRLLASL-PTDERENTLVIFIGDNGTPAPVIDTSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDL 453
Cdd:cd16146   219 DNVGRLLAKLkELGLEENTIVIFMSDNGPAGGVPKRFNAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDL 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 454 YATIVQIAGGDITQV--YNSHSFYDTLFDVVPNPSVRQYNYADFQRNGV----AGWAVRNQDYKLLSIDSQQQALFDMNV 527
Cdd:cd16146   299 LPTLLDLCGVKLPEGikLDGRSLLPLLKGESDPWPERTLFTHSGRWPPPpkkkRNAAVRTGRWRLVSPKGFQPELYDIEN 378

                  ....*...
gi 1482818008 528 DINEQNDL 535
Cdd:cd16146   379 DPGEENDV 386
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
155-538 9.48e-65

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: 217.41  E-value: 9.48e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGV-DASnqySYSTDLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFVPAV---- 228
Cdd:cd16144     1 PNIVLILVDDLGWaDLG---CYGSKFYETPNIDRLAKEGMRFTQAYAAaPVCSPSRASILTGQYPARLGITDVIPGrrgp 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 229 --------------MDTSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPdlSHPNSAGvghYVGNITGT------LDDY 288
Cdd:cd16144    78 pdntklipppsttrLPLEEVTIAEALKDAG----YATAHFGKWHLGGEGG--YGPEDQG---FDVNIGGTgnggppSYYF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 289 SDWTLTDNGSQTQVTQYHTSKVTDLAMDWI-TQQTSPWFVWLAYVAPHSPFHlPPNELHTRSELSGSAEDIAQNpRPYYL 367
Cdd:cd16144   149 PPGKPNPDLEDGPEGEYLTDRLTDEAIDFIeQNKDKPFFLYLSHYAVHTPIQ-ARPELIEKYEKKKKGLRKGQK-NPVYA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 368 AAIEAMDTEIGRLLASLptDE---RENTLVIFIGDNG--TPAPVIDTSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNT 442
Cdd:cd16144   227 AMIESLDESVGRILDAL--EElglADNTLVIFTSDNGglSTRGGPPTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGS 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 443 RESRLVNSTDLYATIVQIAGGDITQVYN--SHSFYDTLFDVVPNPSVR-----QYNYADfQRNGVAGwAVRNQDYKLL-S 514
Cdd:cd16144   305 VSDVPVIGTDLYPTFLELAGGPLPPPQHldGVSLVPLLKGGEADLPRRalfwhFPHYHG-QGGRPAS-AIRKGDWKLIeF 382
                         410       420
                  ....*....|....*....|....
gi 1482818008 515 IDSQQQALFDMNVDINEQNDLLQS 538
Cdd:cd16144   383 YEDGRVELYNLKNDIGETNNLAAE 406
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
155-535 3.42e-62

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: 208.90  E-value: 3.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASnqySYSTDLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGV---SFVPAVMD 230
Cdd:cd16027     1 PNILWIIADDLSPDLG---GYGGNVVKTPNLDRLAAEGVRFTNAFTTaPVCSPSRSALLTGLYPHQNGAhglRSRGFPLP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 231 TSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPDLSHPNSAGVGHYVGNITGTLDDYSDWTLTDNGSQtqvtqyhtskv 310
Cdd:cd16027    78 DGVKTLPELLREAG----YYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRAKKGQ----------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 311 tdlamdwitqqtsPWFVWLAYVAPHSPFHLPPNE--LHTRSELS---------GSAEDIAQnprpyYLAAIEAMDTEIGR 379
Cdd:cd16027   143 -------------PFFLWFGFHDPHRPYPPGDGEepGYDPEKVKvppylpdtpEVREDLAD-----YYDEIERLDQQVGE 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 380 LLASLPTD-ERENTLVIFIGDNGTPAPvidtsvyarqHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIV 458
Cdd:cd16027   205 ILDELEEDgLLDNTIVIFTSDHGMPFP----------RAKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLL 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 459 QIAGGDITQVYNSHSFYDTLFDvvPNPSVRQYNYADFQRNGVAGW---AVRNQDYKLL-SIDSQQqaLFDMNVDINEQND 534
Cdd:cd16027   275 DLAGIEPPEYLQGRSFLPLLKG--EKDPGRDYVFAERDRHDETYDpirSVRTGRYKYIrNYMPEE--LYDLKNDPDELNN 350

                  .
gi 1482818008 535 L 535
Cdd:cd16027   351 L 351
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
155-535 3.58e-59

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: 201.29  E-value: 3.58e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQY---SYstdlpKTPILDSLATSGVVFDNAWATPACTTTRGTIMTGMHGVNSGVSFvpAVMDT 231
Cdd:cd16151     1 PNIILIMADDLGYECIGCYggeSY-----KTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVF--GYLDP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SLTTLPRFLAEndasKAYSMAVFGKWHLGGGDPDLSHPNSAGvghyvgnitgtLDDYSDWTLTD---------------- 295
Cdd:cd16151    74 KQKTFGHLLKD----AGYATAIAGKWQLGGGRGDGDYPHEFG-----------FDEYCLWQLTEtgekysrpatptfnir 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 296 NGSQTQVT--QYHTSKVTDLAMDWITQQTS-PWFVWLAYVAPHSPF-HLPPNELHTRSElsgsaEDIAQNPRpYYLAAIE 371
Cdd:cd16151   139 NGKLLETTegDYGPDLFADFLIDFIERNKDqPFFAYYPMVLVHDPFvPTPDSPDWDPDD-----KRKKDDPE-YFPDMVA 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 372 AMDTEIGRLLASLptDE---RENTLVIFIGDNGTPAPVidTSVY---ARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRES 445
Cdd:cd16151   213 YMDKLVGKLVDKL--EElglRENTIIIFTGDNGTHRPI--TSRTngrEVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSD 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 446 RLVNSTDLYATIVQIAGGDITQVYNS--HSFYDTLFDVVPNPSVRQY--NYADFQRNGVAGWaVRNQDYKLLSIDSqqqa 521
Cdd:cd16151   289 DLVDFSDFLPTLAELAGAPLPEDYPLdgRSFAPQLLGKTGSPRREWIywYYRNPHKKFGSRF-VRTKRYKLYADGR---- 363
                         410
                  ....*....|....
gi 1482818008 522 LFDMNVDINEQNDL 535
Cdd:cd16151   364 FFDLREDPLEKNPL 377
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
155-535 6.19e-56

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: 193.15  E-value: 6.19e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVdasNQYSY-STDLPKTPILDSLATSGVVFDNAWATPACTTTRGTIMTGMHGVNSGVSF------VPA 227
Cdd:cd16029     1 PHIVFILADDLGW---NDVGFhGSDQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHgvilagEPY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 228 VMDTSLTTLPRFLAENdaskAYSMAVFGKWHLGGGDPDLSHPN----------SAGVGHYVGNITGTLDDYSDWTLTDNG 297
Cdd:cd16029    78 GLPLNETLLPQYLKEL----GYATHLVGKWHLGFYTWEYTPTNrgfdsfygyyGGAEDYYTHTSGGANDYGNDDLRDNEE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 298 S-QTQVTQYHTSKVTDLAMDWITQ--QTSPWFVWLAYVAPHSPFHLPPNELhtrSELSGSAEDIAQNPRPYYLAAIEAMD 374
Cdd:cd16029   154 PaWDYNGTYSTDLFTDRAVDIIENhdPSKPLFLYLAFQAVHAPLQVPPEYA---DPYEDKFAHIKDEDRRTYAAMVSALD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 375 TEIGRLLASLptDER---ENTLVIFIGDNGTPAPVIDT-SVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESR-LVN 449
Cdd:cd16029   231 ESVGNVVDAL--KAKgmlDNTLIVFTSDNGGPTGGGDGgSNYPLRGGKNTLWEGGVRVPAFVWSPLLPPKRGTVSDgLMH 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 450 STDLYATIVQIAGGDITQVYN--SHSFYDTLFDvvPNPSVRQ---YNYaDFQRNGVAGWAVRNQDYKLLSIDSqqqaLFD 524
Cdd:cd16029   309 VTDWLPTLLSLAGGDPDDLPPldGVDQWDALSG--GAPSPRTeilLNI-DDITRTTGGAAIRVGDWKLIVGKP----LFN 381
                         410
                  ....*....|.
gi 1482818008 525 MNVDINEQNDL 535
Cdd:cd16029   382 IENDPCERNDL 392
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
155-465 9.89e-55

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


Pssm-ID: 293746 [Multi-domain]  Cd Length: 236  Bit Score: 184.95  E-value: 9.89e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYSTDlpKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFV---PAVMD 230
Cdd:cd16022     1 PNILLIMTDDLGYDDLGCYGNPDI--KTPNLDRLAAEGVRFTNAYVAsPVCSPSRASLLTGRYPHRHGVRGNvgnGGGLP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 231 TSLTTLPRFLAENDaskaYSMAVFGKWHlgggdpdlshpnsagvghyvgnitgtlddysdwtltdngsqtqvtqyhtskv 310
Cdd:cd16022    79 PDEPTLAELLKEAG----YRTALIGKWH---------------------------------------------------- 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 311 tDLAMDWITQQ--TSPWFVWLAYVAPHSPFHlppnelhtrselsgsaediaqnprpyYLAAIEAMDTEIGRLLASL-PTD 387
Cdd:cd16022   103 -DEAIDFIERRdkDKPFFLYVSFNAPHPPFA--------------------------YYAMVSAIDDQIGRILDALeELG 155
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1482818008 388 ERENTLVIFIGDNGTPapvidTSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAGGDI 465
Cdd:cd16022   156 LLDNTLIVFTSDHGDM-----LGDHGLRGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEP 228
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
154-535 8.19e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 179.30  E-value: 8.19e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDdqgvdasnQYSYST-----DLP-KTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFVP 226
Cdd:cd16034     1 KPNILFIFAD--------QHRAQAlgcagDDPvKTPNLDRLAKEGVVFTNAVSNyPVCSPYRASLLTGQYPLTNGVFGND 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 227 AVMDTSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPDLSHPNSA--------GVGHYVGNitGTLDDYSD---WTltD 295
Cdd:cd16034    73 VPLPPDAPTIADVLKDAG----YRTGYIGKWHLDGPERNDGRADDYtppperrhGFDYWKGY--ECNHDHNNphyYD--D 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 296 NGSQTQVTQYHTSKVTDLAMDWITQQTS---PWFVWLAYVAPHSPFHL---------PPNELHTRSELSGSAEDIAQNPR 363
Cdd:cd16034   145 DGKRIYIKGYSPDAETDLAIEYLENQADkdkPFALVLSWNPPHDPYTTapeeyldmyDPKKLLLRPNVPEDKKEEAGLRE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 364 --PYYLAAIEAMDTEIGRLLASLP-TDERENTLVIFIGDNGTpapvidtsvyarQH------SKNSLYEGGIRVPLLVSG 434
Cdd:cd16034   225 dlRGYYAMITALDDNIGRLLDALKeLGLLENTIVVFTSDHGD------------MLgshglmNKQVPYEESIRVPFIIRY 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 435 NLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDVVPNPSVRQYNY------ADFQRNGVAGWAVRNQ 508
Cdd:cd16034   293 PGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKDDEPDSVLLQcfvpfgGGSARDGGEWRGVRTD 372
                         410       420
                  ....*....|....*....|....*..
gi 1482818008 509 DYKLLSIDSQQQALFDMNVDINEQNDL 535
Cdd:cd16034   373 RYTYVRDKNGPWLLFDNEKDPYQLNNL 399
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
155-535 3.14e-50

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: 177.78  E-value: 3.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGV-DASnqySYSTD-LPKTPILDSLATSGVVFDNAWATPA-CTTTRGTIMTGMH----GVNSGV--SFV 225
Cdd:cd16143     1 PNIVIILADDLGYgDIS---CYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSvCTPSRYGLLTGRYpwrsRLKGGVlgGFS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 226 PAVMDTSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPDLShpnsagvGHYVGNITGTLDDYSDWTL---TDNG----- 297
Cdd:cd16143    78 PPLIEPDRVTLAKMLKQAG----YRTAMVGKWHLGLDWKKKD-------GKKAATGTGKDVDYSKPIKggpLDHGfdyyf 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 298 --SQTQVTQYHTSKvtdlAMDWITQQ---TSPWFVWLAYVAPHSPfHLPPNELHTRSELSGsaediaqnprpyYLAAIEA 372
Cdd:cd16143   147 giPASEVLPTLTDK----AVEFIDQHakkDKPFFLYFALPAPHTP-IVPSPEFQGKSGAGP------------YGDFVYE 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 373 MDTEIGRLLASL-PTDERENTLVIFIGDNGTPAPVIDTSVYARQH--------SKNSLYEGGIRVPLLVSGNLLNKQNTR 443
Cdd:cd16143   210 LDWVVGRILDALkELGLAENTLVIFTSDNGPSPYADYKELEKFGHdpsgplrgMKADIYEGGHRVPFIVRWPGKIPAGSV 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 444 ESRLVNSTDLYATIVQIAGGDI--TQVYNSHSFYDTLFDvVPNPSVRQYNyadFQRNGVAGWAVRNQDYKLL-------- 513
Cdd:cd16143   290 SDQLVSLTDLFATLAAIVGQKLpdNAAEDSFSFLPALLG-PKKQEVRESL---VHHSGNGSFAIRKGDWKLIdgtgsggf 365
                         410       420
                  ....*....|....*....|....*....
gi 1482818008 514 SIDSQQQA-------LFDMNVDINEQNDL 535
Cdd:cd16143   366 SYPRGKEKlglppgqLYNLSTDPGESNNL 394
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
153-535 7.34e-49

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: 175.02  E-value: 7.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 153 SKPNIILIISDDQGVDA-SnqySYSTDLPKTPILDSLATSGVVFDNAWATPA-CTTTRGTIMTGM----HGVNsgvSFVP 226
Cdd:cd16031     1 KRPNIIFILTDDHRYDAlG---CYGNPIVKTPNIDRLAKEGVRFDNAFVTTSiCAPSRASILTGQyshrHGVT---DNNG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 227 AVMDTSLTTLPRFLAENdaskAYSMAVFGKWHLGGGDpdlSHPNsAGVGHYV---GNItgtldDYSDWTLTDNGSQTQVT 303
Cdd:cd16031    75 PLFDASQPTYPKLLRKA----GYQTAFIGKWHLGSGG---DLPP-PGFDYWVsfpGQG-----SYYDPEFIENGKRVGQK 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 304 QYHTSKVTDLAMDWI--TQQTSPWFVWLAYVAPHSPF-------------HLPPNELHTRSELSGSAEdIAQNPRPY--- 365
Cdd:cd16031   142 GYVTDIITDKALDFLkeRDKDKPFCLSLSFKAPHRPFtpaprhrglyedvTIPEPETFDDDDYAGRPE-WAREQRNRirg 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 366 ------------------YLAAIEAMDTEIGRLLASLptDER---ENTLVIFIGDNGtpapvidtsVYARQH---SKNSL 421
Cdd:cd16031   221 vldgrfdtpekyqrymkdYLRTVTGVDDNVGRILDYL--EEQglaDNTIIIYTSDNG---------FFLGEHglfDKRLM 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 422 YEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSVRQ----YNYADFQR 497
Cdd:cd16031   290 YEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEG--EKPVDWRkefyYEYYEEPN 367
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1482818008 498 -NGVAGW-AVRNQDYKLLSIDSQQQA--LFDMNVDINEQNDL 535
Cdd:cd16031   368 fHNVPTHeGVRTERYKYIYYYGVWDEeeLYDLKKDPLELNNL 409
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
155-535 7.21e-48

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


Pssm-ID: 293764 [Multi-domain]  Cd Length: 415  Bit Score: 172.01  E-value: 7.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGV-DASnqySYSTDLPKTPILDSLATSGVVFDNAWA-TPACTTTRGTIMTGMHGVNSGV-SFVPAVMDT 231
Cdd:cd16145     1 PNIIFILADDLGYgDLG---CYGQKKIKTPNLDRLAAEGMRFTQHYAgAPVCAPSRASLLTGLHTGHTRVrGNSEPGGQD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SLTTLPRFLAENDASKAYSMAVFGKWHLGGGDPDlSHPNSAGVGHYVGNIT---------------GTLDDY----SDWT 292
Cdd:cd16145    78 PLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTP-GHPTKQGFDYFYGYLDqvhahnyypeylwrnGEKVPLpnnvIPPL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 293 LTDNGSQTQVTQYHTSKVTDLAMDWI-TQQTSPWFVWLAYVAPHSPFHLP---PNELHTRSELSGSAEDIAQnPRPYYLA 368
Cdd:cd16145   157 DEGNNAGGGGGTYSHDLFTDEALDFIrENKDKPFFLYLAYTLPHAPLQVPddgPYKYKPKDPGIYAYLPWPQ-PEKAYAA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 369 AIEAMDTEIGRLLASLptDE---RENTLVIFIGDNG-------TPAPVIDTSVYARQHSKNSLYEGGIRVPLLVSGNLLN 438
Cdd:cd16145   236 MVTRLDRDVGRILALL--KElgiDENTLVVFTSDNGphseggsEHDPDFFDSNGPLRGYKRSLYEGGIRVPFIARWPGKI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 439 KQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvVPNPSVRQYNYADFQRNGvAGWAVRNQDYKLLSIDSQ 518
Cdd:cd16145   314 PAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTLLG-KPQQQQHDYLYWEFYEGG-GAQAVRMGGWKAVRHGKK 391
                         410
                  ....*....|....*....
gi 1482818008 519 QQA--LFDMNVDINEQNDL 535
Cdd:cd16145   392 DGPfeLYDLSTDPGETNNL 410
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
154-535 6.22e-47

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: 169.16  E-value: 6.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGvdasnqysYStDLP------KTPILDSLATSGVVFDNAWATPACTTTRGTIMTGM--HGVNSGVsfv 225
Cdd:cd16025     2 RPNILLILADDLG--------FS-DLGcfggeiPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRnhHQVGMGT--- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 226 pavMDTSLT--------------TLPRFLAENDaskaYSMAVFGKWHLGGGDpdlshpnsagvghyvgnitgtlddysdw 291
Cdd:cd16025    70 ---MAELATgkpgyegylpdsaaTIAEVLKDAG----YHTYMSGKWHLGPDD---------------------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 292 tltdngsqtqvtqYHTSKV-TDLAMDWITQQTS---PWFVWLAYVAPHSPFHLPP------------------NELHTR- 348
Cdd:cd16025   115 -------------YYSTDDlTDKAIEYIDEQKApdkPFFLYLAFGAPHAPLQAPKewidkykgkydagwdalrEERLERq 181
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 349 ---------SELSGSAEDIA------QNPRPY-------YLAAIEAMDTEIGRLLASLP-TDERENTLVIFIGDNG---- 401
Cdd:cd16025   182 kelglipadTKLTPRPPGVPawdslsPEEKKLearrmevYAAMVEHMDQQIGRLIDYLKeLGELDNTLIIFLSDNGasae 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 402 --------TPapvidtsvyARQHsKNSLYEGGIRVPLLVSG-NLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSH 472
Cdd:cd16025   262 pgwanasnTP---------FRLY-KQASHEGGIRTPLIVSWpKGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNGV 331
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1482818008 473 --------SFYDTLFD-VVPNPSVRQYnyadFQRNGvaGWAVRNQDYKLLSI-----DSQQQALFDMNVDINEQNDL 535
Cdd:cd16025   332 pqlpldgvSLLPTLDGaAAPSRRRTQY----FELFG--NRAIRKGGWKAVALhpppgWGDQWELYDLAKDPSETHDL 402
Sulfatase pfam00884
Sulfatase;
155-462 1.04e-45

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 162.98  E-value: 1.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYStdLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFVPAV-MDTS 232
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYP--RPTTPFLDRLAEEGLLFSNFYSGgTLTAPSRFALLTGLPPHNFGSYVSTPVgLPRT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 233 LTTLPRFLAEndasKAYSMAVFGKWHLGGGDPDlsHPNSAGVGHYVGNITGtLDDYSDWTltDNGSQTQVTQYHTSKVTD 312
Cdd:pfam00884  79 EPSLPDLLKR----AGYNTGAIGKWHLGWYNNQ--SPCNLGFDKFFGRNTG-SDLYADPP--DVPYNCSGGGVSDEALLD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 313 LAMDWITQQTSPWFVWLAYVAPHSPFHLPpNELHTRSELSGSAEDIAQNPRPYYLAAIEAMDTEIGRLLASLPTDE-REN 391
Cdd:pfam00884 150 EALEFLDNNDKPFFLVLHTLGSHGPPYYP-DRYPEKYATFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGlLDN 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1482818008 392 TLVIFIGDNGtpAPVIDTSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAG 462
Cdd:pfam00884 229 TLVVYTSDHG--ESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
154-535 4.96e-45

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: 163.89  E-value: 4.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGvdasnqY----SYSTDLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFVPAV 228
Cdd:cd16026     1 KPNIVVILADDLG------YgdlgCYGSPLIKTPNIDRLAAEGVRFTDFYAAaPVCSPSRAALLTGRYPVRVGLPGVVGP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 229 ------MDTSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPdlSHPNSAGVGHYVG---------NITGTLDDYSDW-- 291
Cdd:cd16026    75 pgskggLPPDEITIAEVLKKAG----YRTALVGKWHLGHQPE--FLPTRHGFDEYFGipysndmwpFPLYRNDPPGPLpp 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 292 ------TLTDNGSQTQVTQYHTSKvtdlAMDWITQQT-SPWFVWLAYVAPHSPfhlppneLHTRSELSGSAEDIAqnprp 364
Cdd:cd16026   149 lmeneeVIEQPADQSSLTQRYTDE----AVDFIERNKdQPFFLYLAHTMPHVP-------LFASEKFKGRSGAGL----- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 365 yYLAAIEAMDTEIGRLLASLptDE---RENTLVIFIGDNGtpaPVIDTSVYA-----RQHSKNSLYEGGIRVPLLVSGNL 436
Cdd:cd16026   213 -YGDVVEELDWSVGRILDAL--KElglEENTLVIFTSDNG---PWLEYGGHGgsagpLRGGKGTTWEGGVRVPFIAWWPG 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 437 LNKQNTRESRLVNSTDLYATIVQIAGGDITQ--VYNSHSFYDTLFDVvpNPSVRQ---YNYADFQRNgvagwAVRNQDYK 511
Cdd:cd16026   287 VIPAGTVSDELASTMDLLPTLAALAGAPLPEdrVIDGKDISPLLLGG--SKSPPHpffYYYDGGDLQ-----AVRSGRWK 359
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1482818008 512 LL-------------SIDSQQQA--LFDMNVDINEQNDL 535
Cdd:cd16026   360 LHlpttyrtgtdpggLDPTKLEPplLYDLEEDPGETYNV 398
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
153-535 1.60e-41

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


Pssm-ID: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 153.49  E-value: 1.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 153 SKPNIILIISDDQGVDASNQYSySTDLpKTPILDSLATSGVVFDNA-----WATPACTTTRGTIMTGMHGVNSGVSfVPA 227
Cdd:cd16155     1 KKPNILFILADDQRADTIGALG-NPEI-QTPNLDRLARRGTSFTNAynmggWSGAVCVPSRAMLMTGRTLFHAPEG-GKA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 228 VMDTSLTTLPRFLAENdaskAY-SMAVfGKWHLGggdpdlshpnsagvghyvgnitgtlddysdwtltdngsqtqvtqyh 306
Cdd:cd16155    78 AIPSDDKTWPETFKKA----GYrTFAT-GKWHNG---------------------------------------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 307 tskVTDLAMDWITQQTS---PWFVWLAYVAPHSP------FH---------LPPN----------ELHTRSEL----SGS 354
Cdd:cd16155   107 ---FADAAIEFLEEYKDgdkPFFMYVAFTAPHDPrqappeYLdmyppetipLPENflpqhpfdngEGTVRDEQlapfPRT 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 355 AEDIAQNPRPYYlAAIEAMDTEIGRLLASL-PTDERENTLVIFIGDNGTpapvidtsvyAR-QHS---KNSLYEGGIRVP 429
Cdd:cd16155   184 PEAVRQHLAEYY-AMITHLDAQIGRILDALeASGELDNTIIVFTSDHGL----------AVgSHGlmgKQNLYEHSMRVP 252
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 430 LLVSGNLLnKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSVRQY---NYADFQRngvagwAVR 506
Cdd:cd16155   253 LIISGPGI-PKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRG--EKKAVRDTlygAYRDGQR------AIR 323
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1482818008 507 NQDYKLL----SIDSQQqaLFDMNVDINEQNDL 535
Cdd:cd16155   324 DDRWKLIiyvpGVKRTQ--LFDLKKDPDELNNL 354
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
153-535 5.84e-38

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: 145.02  E-value: 5.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 153 SKPNIILIISDD--------QGVDAsnqysystdlpKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVS 223
Cdd:cd16030     1 KKPNVLFIAVDDlrpwlgcyGGHPA-----------KTPNIDRLAARGVLFTNAYCQqPVCGPSRASLLTGRRPDTTGVY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 224 FVPAVMDTSL---TTLPRFLAENDaskaYSMAVFGK-WHlGGGDPDLSHPNS--------------AGVGHYVGNITGTL 285
Cdd:cd16030    70 DNNSYFRKVApdaVTLPQYFKENG----YTTAGVGKiFH-PGIPDGDDDPASwdeppnppgpekypPGKLCPGKKGGKGG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 286 DDYSDWTLTDNGSqtqvTQYHTSKVTDLAMDWITQ---QTSPWFVWLAYVAPHSPFH----------------------- 339
Cdd:cd16030   145 GGGPAWEAADVPD----EAYPDGKVADEAIEQLRKlkdSDKPFFLAVGFYKPHLPFVapkkyfdlyplesiplpnpfdpi 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 340 -LPPNELHTRSELSGSAEDIAQNPRPY---------------YLAAIEAMDTEIGRLLASLptDE---RENTLVIFIGDN 400
Cdd:cd16030   221 dLPEVAWNDLDDLPKYGDIPALNPGDPkgplpdeqarelrqaYYASVSYVDAQVGRVLDAL--EElglADNTIVVLWSDH 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 401 GtpapvidtsvyarQH-------SKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHS 473
Cdd:cd16030   299 G-------------WHlgehghwGKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKS 365
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1482818008 474 FYDTLFDvvPNPSVRQYNYADFQRNGVAGWAVRNQDYKL----LSIDSQQQALFDMNVDINEQNDL 535
Cdd:cd16030   366 LVPLLKN--PSAKWKDAAFSQYPRPSIMGYSIRTERYRYtewvDFDKVGAEELYDHKNDPNEWKNL 429
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
155-537 9.60e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 138.51  E-value: 9.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAWA-TPACTTTRGTIMTGM----HGVNSGVSFVPAV- 228
Cdd:cd16033     1 PNILFIMTDQQRYDTLG--CYGNPIVKTPNIDRLAAEGVRFTNAYTpSPVCCPARASLLTGLypheHGVLNNVENAGAYs 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 229 --MDTSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPDLSHpnsagvgHYvgnitgtlDDYSDwtltdngsqtqVTQYH 306
Cdd:cd16033    79 rgLPPGVETFSEDLREAG----YRNGYVGKWHVGPEETPLDY-------GF--------DEYLP-----------VETTI 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 307 TSKVTDLAMDWI---TQQTSPWFVWLAYVAPHSPFHLP-------------------------P----NELHTRSELSGS 354
Cdd:cd16033   129 EYFLADRAIEMLeelAADDKPFFLRVNFWGPHDPYIPPepyldmydpediplpesfaddfedkPyiyrRERKRWGVDTED 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 355 AEDIAQNPRpYYLAAIEAMDTEIGRLLASLP-TDERENTLVIFIGDNGtpapviDTSVYARQHSK-NSLYEGGIRVPLLV 432
Cdd:cd16033   209 EEDWKEIIA-HYWGYITLIDDAIGRILDALEeLGLADDTLVIFTSDHG------DALGAHRLWDKgPFMYEETYRIPLII 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 433 SGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDVVPnPSVRQYNYADFQRNGVAGW--AVRNQDY 510
Cdd:cd16033   282 KWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQP-EDWRDEVVTEYNGHEFYLPqrMVRTDRY 360
                         410       420
                  ....*....|....*....|....*..
gi 1482818008 511 KLLSIDSQQQALFDMNVDINEQNDLLQ 537
Cdd:cd16033   361 KYVFNGFDIDELYDLESDPYELNNLID 387
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
155-464 2.48e-35

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: 136.51  E-value: 2.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVdaSNQYSYSTDLP---KTPILDSLATSGVVFDNAWATPACTTTRGTIMTGMHGVNSGVSFVPavMDT 231
Cdd:cd16142     1 PNILVILGDDIGW--GDLGCYGGGIGrgaPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGLTTVG--LPG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SL-------TTLPRFLAENDaskaYSMAVFGKWHLggGDPDLSHPNSAGVGHYVGNITGTLDDYsdwtltdngsqtqvtq 304
Cdd:cd16142    77 SPgglppwePTLAELLKDAG----YATAQFGKWHL--GDEDGRLPTDHGFDEFYGNLYHTIDEE---------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 305 yhtskVTDLAMDWITQQTS---PWFVWLAYVAPHSPFHLPPnelhtrsELSGSAEDIAQnprpyYLAAIEAMDTEIGRLL 381
Cdd:cd16142   135 -----IVDKAIDFIKRNAKadkPFFLYVNFTKMHFPTLPSP-------EFEGKSSGKGK-----YADSMVELDDHVGQIL 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 382 ASLptDE---RENTLVIFIGDNG-----------TPapvidtsvyaRQHSKNSLYEGGIRVPLLVS--GNLlnKQNTRES 445
Cdd:cd16142   198 DAL--DElgiADNTIVIFTTDNGpeqdvwpdggyTP----------FRGEKGTTWEGGVRVPAIVRwpGKI--KPGRVSN 263
                         330
                  ....*....|....*....
gi 1482818008 446 RLVNSTDLYATIVQIAGGD 464
Cdd:cd16142   264 EIVSHLDWFPTLAALAGAP 282
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
155-528 3.06e-35

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: 134.98  E-value: 3.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFVPAVMDTSL 233
Cdd:cd16037     1 PNILIIMSDEHNPDAMG--CYGHPVVRTPNLDRLAARGTRFENAYTPsPICVPSRASFLTGRYVHETGVWDNADPYDGDV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 234 TTLPRFLAEndasKAYSMAVFGKWHLGGGDPDlshpnsaGVGHYvgnitgtlDDYsdwtltdngsqtqvtqyhtskVTDL 313
Cdd:cd16037    79 PSWGHALRA----AGYETVLIGKLHFRGEDQR-------HGFRY--------DRD---------------------VTEA 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 314 AMDWIT---QQTSPWFVWLAYVAPHSPFHLPPN--ELHTRSELSGsaediaqnprpyYLAAIEAMDTEIGRLLASL-PTD 387
Cdd:cd16037   119 AVDWLReeaADDKPWFLFVGFVAPHFPLIAPQEfyDLYVRRARAA------------YYGLVEFLDENIGRVLDALeELG 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 388 ERENTLVIFIGDNGtpapviDTSVYARQHSKNSLYEGGIRVPLLVSGNlLNKQNTRESRLVNSTDLYATIVQIAGGDITQ 467
Cdd:cd16037   187 LLDNTLIIYTSDHG------DMLGERGLWGKSTMYEESVRVPMIISGP-GIPAGKRVKTPVSLVDLAPTILEAAGAPPPP 259
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1482818008 468 VYNSHSFYDTLFDvvPNPSVR----QYNYADfqrNGVAGWAVRNQDYKLLSIDSQQQALFDMNVD 528
Cdd:cd16037   260 DLDGRSLLPLAEG--PDDPDRvvfsEYHAHG---SPSGAFMLRKGRWKYIYYVGYPPQLFDLEND 319
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
154-532 3.97e-35

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: 136.06  E-value: 3.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGV-DASNQYSYSTDlpKTPILDSLATSGVVFDNaW--ATPACTTTRGTIMTGMHGVNSGVSFVPAVmd 230
Cdd:cd16161     1 KPNFLLLFADDLGWgDLGANWAPNAI--LTPNLDKLAAEGTRFVD-WysAASVCSPSRASLMTGRLGLRNGVGHNFLP-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 231 TSLTTLP---RFLAENDASKAYSMAVFGKWHLggGDPDLSHPNSAGVGHYVGnitgtlDDYSDwtltdngsQTQVTQYHT 307
Cdd:cd16161    76 TSVGGLPlneTTLAEVLRQAGYATGMIGKWHL--GQREAYLPNSRGFDYYFG------IPFSH--------DSSLADRYA 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 308 SKVTDLAMDwITQQTSPWFVWLAYVAPHSPFHLPPNELHTRSELSGsaediaqnprpyYLAAIEAMDTEIGRLLASLPTD 387
Cdd:cd16161   140 QFATDFIQR-ASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRGP------------YGDALQEMDDLVGQIMDAVKHA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 388 E-RENTLVIFIGDNGTP------APVIDTSVYARQH----SKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYAT 456
Cdd:cd16161   207 GlKDNTLTWFTSDNGPWevkcelAVGPGTGDWQGNLggsvAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPT 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 457 IVQIAGGDI--TQVYNSHSFYDTLFDVVPNPSVRQYNYADFQRNGVAGWAVRNQDYKLLSIDSQQQA------------- 521
Cdd:cd16161   287 VVALAGASLppGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAGAGALSAVRCGDYKAHYATGGALAccgstgpklyhdp 366
                         410
                  ....*....|...
gi 1482818008 522 --LFDMNVDINEQ 532
Cdd:cd16161   367 plLFDLEVDPAES 379
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
155-474 8.34e-35

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: 132.29  E-value: 8.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYstDLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVsfVPAVMDTSL 233
Cdd:cd16148     1 MNVILIVIDSLRADHLGCYGY--DRVTTPNLDRLAAEGVVFDNHYSGsNPTLPSRFSLFTGLYPFYHGV--WGGPLEPDD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 234 TTLPRFLAENDaskaYSMAVFGkwhlgggdpdlSHPNSAGVGHYVGNItgtldDYSDWTLTDNGSQTQVTQYHTSKVTDL 313
Cdd:cd16148    77 PTLAEILRKAG----YYTAAVS-----------SNPHLFGGPGFDRGF-----DTFEDFRGQEGDPGEEGDERAERVTDR 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 314 AMDWITQQTS--PWFVWLAYVAPHSPFHlppnelhtrselsgsaediaqnprpyYLAAIEAMDTEIGRLLASLP-TDERE 390
Cdd:cd16148   137 ALEWLDRNADddPFFLFLHYFDPHEPYL--------------------------YDAEVRYVDEQIGRLLDKLKeLGLLE 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 391 NTLVIF-------IGDNGtpapvidtsVYARQHSknSLYEGGIRVPLLVSGnLLNKQNTRESRLVNSTDLYATIVQIAGG 463
Cdd:cd16148   191 DTLVIVtsdhgeeFGEHG---------LYWGHGS--NLYDEQLHVPLIIRW-PGKEPGKRVDALVSHIDIAPTLLDLLGV 258
                         330
                  ....*....|.
gi 1482818008 464 DITQVYNSHSF 474
Cdd:cd16148   259 EPPDYSDGRSL 269
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
155-464 1.37e-32

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


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 125.81  E-value: 1.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDAsnQYSYSTDLPKTPILDSLATSGVVFDNAW-ATPACTTTRGTIMTG----MHGV-------NSGV 222
Cdd:cd16149     1 PNILFILTDDQGPWA--LGCYGNSEAVTPNLDRLAAEGVRFENFFcTSPVCSPARASLLTGrmpsQHGIhdwivegSHGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 223 SFVPAVMDTSLTTLPRFLAENdaskAYSMAVFGKWHLGggdpdlshpnsagvghyvgnitgtlDDYSDWTLTDNGSQTqv 302
Cdd:cd16149    79 TKKPEGYLEGQTTLPEVLQDA----GYRCGLSGKWHLG-------------------------DDAADFLRRRAEAEK-- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 303 tqyhtskvtdlamdwitqqtsPWFVWLAYVAPHSPFHlppnelhtrselsgsaediaqnprpyYLAAIEAMDTEIGRLLA 382
Cdd:cd16149   128 ---------------------PFFLSVNYTAPHSPWG--------------------------YFAAVTGVDRNVGRLLD 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 383 SLPT-DERENTLVIFIGDNGtpapvidtsVYARQH---------SKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTD 452
Cdd:cd16149   161 ELEElGLTENTLVIFTSDNG---------FNMGHHgiwgkgngtFPLNMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYD 231
                         330
                  ....*....|..
gi 1482818008 453 LYATIVQIAGGD 464
Cdd:cd16149   232 FFPTLLELAGVD 243
PRK13759 PRK13759
arylsulfatase; Provisional
153-555 6.73e-31

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 125.94  E-value: 6.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 153 SKPNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAW-ATPACTTTRGTIMTGMHGVNSG-VSFVPAVMD 230
Cdd:PRK13759    5 KKPNIILIMVDQMRGDCLG--CNGNKAVETPNLDMLASEGYNFENAYsAVPSCTPARAALLTGLSQWHHGrVGYGDVVPW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 231 TSLTTLPRFLAENDaskaYSMAVFGKWH------LGGGDPDLSHPNSAGVGH-YVGNITGTLDDYSDW----------TL 293
Cdd:PRK13759   83 NYKNTLPQEFRDAG----YYTQCIGKMHvfpqrnLLGFHNVLLHDGYLHSGRnEDKSQFDFVSDYLAWlrekapgkdpDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 294 TDNG--SQTQVT-------QYH-TSKVTDLAMDWIT--QQTSPWFVWLAYVAPHSPFHlPPN------------------ 343
Cdd:PRK13759  159 TDIGwdCNSWVArpwdleeRLHpTNWVGSESIEFLRrrDPTKPFFLKMSFARPHSPYD-PPKryfdmykdadipdphigd 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 344 -ELHTRSELSGSA---------EDIAQNPRPYYLAAIEAMDTEIGRLLASLPT-DERENTLVIFIGDNGtpapvidtSVY 412
Cdd:PRK13759  238 wEYAEDQDPEGGSidalrgnlgEEYARRARAAYYGLITHIDHQIGRFLQALKEfGLLDNTIILFVSDHG--------DML 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 413 ARQH--SKNSLYEGGIRVPLLVS--GNLLNKQNTRES-RLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSV 487
Cdd:PRK13759  310 GDHYlfRKGYPYEGSAHIPFIIYdpGGLLAGNRGTVIdQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFG--QYEGW 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 488 RQY-------NYADFQrngvagWAVRNQD-YKLLSIDSQQQaLFDMNVDINEQNDLLQSG------DDW-SALVLELAEY 552
Cdd:PRK13759  388 RPYlhgehalGYSSDN------YLTDGKWkYIWFSQTGEEQ-LFDLKKDPHELHNLSPSEkyqprlREMrKKLVDHLRGR 460

                  ...
gi 1482818008 553 GQS 555
Cdd:PRK13759  461 EEG 463
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
154-465 9.49e-31

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: 123.81  E-value: 9.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGVDaSNQYSYstdLPKTPILdsLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGV---------- 222
Cdd:cd16147     1 RPNIVLILTDDQDVE-LGSMDP---MPKTKKL--LADQGTTFTNAFVTtPLCCPSRASILTGQYAHNHGVtnnsppgggy 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 223 -SFVPAVMDTslTTLPRFLaendaSKA-YSMAVFGKwHLGG-GDPDLSHPNSAGVGHYVGNITGTLDDYsdWTLTDNGSQ 299
Cdd:cd16147    75 pKFWQNGLER--STLPVWL-----QEAgYRTAYAGK-YLNGyGVPGGVSYVPPGWDEWDGLVGNSTYYN--YTLSNGGNG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 300 TQV----TQYHTSKVTDLAMDWIT---QQTSPWFVWLAYVAPHSPFHLPPNELHTRSELSG----SAEDIAQNPRPYYLA 368
Cdd:cd16147   145 KHGvsypGDYLTDVIANKALDFLRraaADDKPFFLVVAPPAPHGPFTPAPRYANLFPNVTApprpPPNNPDVSDKPHWLR 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 369 A--------IEAMDTE--------------IGRLLASL-PTDERENTLVIFIGDNGtpapvidtsvY-----ARQHSKNS 420
Cdd:cd16147   225 RlpplnptqIAYIDELyrkrlrtlqsvddlVERLVNTLeATGQLDNTYIIYTSDNG----------YhlgqhRLPPGKRT 294
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1482818008 421 LYEGGIRVPLLVSG-NLlnKQNTRESRLVNSTDLYATIVQIAGGDI 465
Cdd:cd16147   295 PYEEDIRVPLLVRGpGI--PAGVTVDQLVSNIDLAPTILDLAGAPP 338
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
154-484 1.13e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 120.41  E-value: 1.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAW-ATPACTTTRGTIMTGMHGVNSGVsFVPAV-MDT 231
Cdd:cd16152     1 KPNVIVFFTDQQRWDTLG--CYGQPLDLTPNLDALAEEGVLFENAFtPQPVCGPARACLQTGLYPTETGC-FRNGIpLPA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SLTTLPRFLAENDaskaYSMAVFGKWHLGGgdpdlshpnsagvghyvgnitgtlddysdwtltdngsqtqvtqYHTSKVT 311
Cdd:cd16152    78 DEKTLAHYFRDAG----YETGYVGKWHLAG-------------------------------------------YRVDALT 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 312 DLAMDWIT--QQTSPWFVWLAYVAPHspfHlpPNELHTRSELSGSAE---------DIA------QNPRPYYLAAIEAMD 374
Cdd:cd16152   111 DFAIDYLDnrQKDKPFFLFLSYLEPH---H--QNDRDRYVAPEGSAErfanfwvppDLAalpgdwAEELPDYLGCCERLD 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 375 TEIGRLLASL-PTDERENTLVIFIGDNGTpapvidtsvyarqH-------SKNSLYEGGIRVPLLVSGNLLNKqNTRESR 446
Cdd:cd16152   186 ENVGRIRDALkELGLYDNTIIVFTSDHGC-------------HfrtrnaeYKRSCHESSIRVPLVIYGPGFNG-GGRVEE 251
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1482818008 447 LVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDVVPN 484
Cdd:cd16152   252 LVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVED 289
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
154-467 1.46e-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: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 117.86  E-value: 1.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGVDA----SNQYSYSTDLP----KTPILDSLATSGVVFDNAW-ATPACTTTRGTIMTGMHGVNSGV-S 223
Cdd:cd16153     1 KPNILWIITDDQRVDSlscyNNAHTGKSESRlgyvESPNIDALAAEGVLFTNAYcNSPVCVPSRTSMLTGRYPHRTGVyG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 224 FVPA--VMDTSLTTLPRFLAENdaskAYSMAVFGKWHLgggdpdlshpnsagvghyvgnitgtlDDYSDWTltDNGSQTQ 301
Cdd:cd16153    81 FEAAhpALDHGLPTFPEVLKKA----GYQTASFGKSHL--------------------------EAFQRYL--KNANQSY 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 302 VTQYHTSKvtdlamdWITQQTSPWFVWLAYVAPHSPFhLPPNELhtRSelsgsaediaqnpRPYYLAAIEAMDTEIGRLL 381
Cdd:cd16153   129 KSFWGKIA-------KGADSDKPFFVRLSFLQPHTPV-LPPKEF--RD-------------RFDYYAFCAYGDAQVGRAV 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 382 -----ASLPTDeRENTLVIFIGDNGtpAPVIDTSVYArqhsKNSLYEGGIRVPLLV--SGNLLNKQNTRESRLVNSTDLY 454
Cdd:cd16153   186 eafkaYSLKQD-RDYTIVYVTGDHG--WHLGEQGILA----KFTFWPQSHRVPLIVvsSDKLKAPAGKVRHDFVEFVDLA 258
                         330
                  ....*....|...
gi 1482818008 455 ATIVQIAGGDITQ 467
Cdd:cd16153   259 PTLLAAAGVDVDA 271
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
155-536 4.03e-29

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: 120.56  E-value: 4.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYSTdlPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHG-VNSGVSFVPAVMDTS 232
Cdd:cd16156     1 KQFIFIMTDTQRWDMVGCYGNKA--MKTPNLDRLAAEGVRFDSAYTTqPVCGPARSGLFTGLYPhTNGSWTNCMALGDNV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 233 LtTLPRFLAENDASKAYsmavFGKWHLGGGD-------PDLSHPNsagvghYVGNITGTLDDYSD-----W-----TLTD 295
Cdd:cd16156    79 K-TIGQRLSDNGIHTAY----IGKWHLDGGDyfgngicPQGWDPD------YWYDMRNYLDELTEeerrkSrrgltSLEA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 296 NGSQTQVTQYHtsKVTDLAMDWITQ-QTSPWFVWLAYVAPHSPFHLPP-----------------------NELHTR--- 348
Cdd:cd16156   148 EGIKEEFTYGH--RCTNRALDFIEKhKDEDFFLVVSYDEPHHPFLCPKpyasmykdfefpkgenayddlenKPLHQRlwa 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 349 -SELSGSAEDIAQNPrPYYLAAIEAMDTEIGRLLASLPtDERENTLVIFIGDNGtpapvidTSVYARQ-HSKN-SLYEGG 425
Cdd:cd16156   226 gAKPHEDGDKGTIKH-PLYFGCNSFVDYEIGRVLDAAD-EIAEDAWVIYTSDHG-------DMLGAHKlWAKGpAVYDEI 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 426 IRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSVRQYNYADFQR-----NGV 500
Cdd:cd16156   297 TNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIED--PEIPENRGVFVEFGRyevdhDGF 374
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1482818008 501 AGW----AVRNQDYK----LLSIDSqqqaLFDMNVDINEQNDLL 536
Cdd:cd16156   375 GGFqpvrCVVDGRYKlvinLLSTDE----LYDLEKDPYEMHNLI 414
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
155-551 1.92e-28

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: 118.13  E-value: 1.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAWA-TPACTTTRGTIMTGMHGVNSGV--SFVPavMDT 231
Cdd:cd16028     1 RNVLFITADQWRADCLS--CLGHPLVKTPNLDRLAAEGVRFRNHYTqAAPCGPSRASLYTGRYLMNHRSvwNGTP--LDA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SLTTLPRFLAENdaskAYSMAVFGKWHLGGgDPDLSHPNSAGVGHYVGNITG-----TLDDY----SDwtltdngsqtqv 302
Cdd:cd16028    77 RHLTLALELRKA----GYDPALFGYTDTSP-DPRGLAPLDPRLLSYELAMPGfdpvdRLDEYpaedSD------------ 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 303 tqyhTSKVTDLAMDWI-TQQTSPWFVWLAYVAPHSPFHLP-P-NELHTRSELS------GSAEDIAQNP----------- 362
Cdd:cd16028   140 ----TAFLTDRAIEYLdERQDEPWFLHLSYIRPHPPFVAPaPyHALYDPADVPppiraeSLAAEAAQHPllaafleries 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 363 ---------------------RPYYLAAIEAMDTEIGRLLASL-PTDERENTLVIFIGDNGTpapvidtsvYARQH---S 417
Cdd:cd16028   216 lsfspgaanaadlddeevaqmRATYLGLIAEVDDHLGRLFDYLkETGQWDDTLIVFTSDHGE---------QLGDHwlwG 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 418 KNSLYEGGIRVPLLV---SGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHS-----------------FYDT 477
Cdd:cd16028   287 KDGFFDQAYRVPLIVrdpRREADATRGQVVDAFTESVDVMPTILDWLGGEIPHQCDGRSllpllagaqpsdwrdavHYEY 366
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1482818008 478 LFDVVPNPSVRQynYADFQRNGVAGWAVRNQDYKLLSIDSQQQALFDMNVDINEQNDLlqSGD-DWSALVLELAE 551
Cdd:cd16028   367 DFRDVSTRRPQE--ALGLSPDECSLAVIRDERWKYVHFAALPPLLFDLKNDPGELRDL--AADpAYAAVVLRYAQ 437
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
155-464 9.73e-25

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: 104.97  E-value: 9.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAW-ATPACTTTRGTIMTGMH----GVNSGVSFVPAvm 229
Cdd:cd16032     1 PNILLIMADQLTAAALP--AYGNTVVKTPNLDRLAARGVVFDNAYcNSPLCAPSRASMMTGRLpsriGAYDNAAEFPA-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 230 dtSLTTLPRFLAendaSKAYSMAVFGKWHLGGgdPDLSHpnsagvGHyvgnitgtldDYSDwtltdngsqtQVTQYHTSK 309
Cdd:cd16032    77 --DIPTFAHYLR----AAGYRTALSGKMHFVG--PDQLH------GF----------DYDE----------EVAFKAVQK 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 310 VTDLAMDwitQQTSPWFVWLAYVAPHSPFHLPPN--ELHTRselsgsaediaqNPRPYYLAAIEAMDTEIGRLLASLP-T 386
Cdd:cd16032   123 LYDLARG---EDGRPFFLTVSFTHPHDPYVIPQEywDLYVR------------RARRAYYGMVSYVDDKVGQLLDTLErT 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 387 DERENTLVIFIGDNGtpapviDT-----SVYarqhsKNSLYEGGIRVPLLVSGNLLnKQNTRESRLVNSTDLYATIVQIA 461
Cdd:cd16032   188 GLADDTIVIFTSDHG------DMlgergLWY-----KMSFFEGSARVPLIISAPGR-FAPRRVAEPVSLVDLLPTLVDLA 255

                  ...
gi 1482818008 462 GGD 464
Cdd:cd16032   256 GGG 258
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
154-485 2.12e-24

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: 105.97  E-value: 2.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGVDASNQYSYSTDLPkTPIlDSLATSGVVFDNAWATPA-CTTTRGTIMTGMHGVNSGV-----SFVPa 227
Cdd:cd16160     1 KPNIVLFFADDMGYGDLASYGHPTQER-GPI-DDMAAEGIRFTQAYSADSvCTPSRAALLTGRLPIRSGMyggtrVFLP- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 228 vmdTSLTTLPRF---LAENDASKAYSMAVFGKWHLGGGD---PDLSH-PNSAG---VGHYV--GNI-----TGTLDDYSD 290
Cdd:cd16160    78 ---WDIGGLPKTevtMAEALKEAGYTTGMVGKWHLGINEnnhSDGAHlPSHHGfdfVGTNLpfTNSwacddTGRHVDFPD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 291 WT---LTDNGSQTQVTQYHTSKVTDLAMDWI----TQQTSPWFVWLAYVAPHSPfhlppneLHTRSELSGSAEdiaqnpR 363
Cdd:cd16160   155 RSacfLYYNDTIVEQPIQHEHLTETLVGDAKsfieDNQENPFFLYFSFPQTHTP-------LFASKRFKGKSK------R 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 364 PYYLAAIEAMDTEIGRLLASL-PTDERENTLVIFIGDNGtPAPVI-----DTSVYarQHSKNSLYEGGIRVPLLV--SGN 435
Cdd:cd16160   222 GRYGDNINEMSWAVGEVLDTLvDTGLDQNTLVFFLSDHG-PHVEYcleggSTGGL--KGGKGNSWEGGIRVPFIAywPGT 298
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1482818008 436 LlnkQNTRESRLVNSTDLYATIVQIAGGDI--TQVYNSHSFYDTLFDVVPNP 485
Cdd:cd16160   299 I---KPRVSHEVVSTMDIFPTFVDLAGGTLptDRIYDGLSITDLLLGEADSP 347
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
154-545 4.01e-22

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: 99.44  E-value: 4.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGVDASNQYSYSTDLpkTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVsfVPAVMD-T 231
Cdd:cd16158     1 PPNIVLLFADDLGYGDLGCYGHPSSS--TPNLDRLAANGLRFTDFYSSsPVCSPSRAALLTGRYQVRSGV--YPGVFYpG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SLTTLPR---FLAENDASKAYSMAVFGKWHLGGGDPDLSHPNSAGVGHYVG-----------NITGTLDDYSDWTLTDNG 297
Cdd:cd16158    77 SRGGLPLnetTIAEVLKTVGYQTAMVGKWHLGVGLNGTYLPTHQGFDHYLGipyshdqgpcqNLTCFPPNIPCFGGCDQG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 298 SQTQVTQYHTSKV-------------TDLAMDWIT---QQTSPWFVWLAYVAPHSPfhlppnelhtrsELSGsAEDIAQN 361
Cdd:cd16158   157 EVPCPLFYNESIVqqpvdlltleeryAKFAKDFIAdnaKEGKPFFLYYASHHTHYP------------QFAG-QKFAGRS 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 362 PRPYYLAAIEAMDTEIGRLLASL-PTDERENTLVIFIGDNGTpapviDTSVYARQHS-------KNSLYEGGIRVPLLV- 432
Cdd:cd16158   224 SRGPFGDALAELDGSVGELLQTLkENGIDNNTLVFFTSDNGP-----STMRKSRGGNagllkcgKGTTYEGGVREPAIAy 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 433 -SGNLlnkQNTRESRLVNSTDLYATIVQIAGGDITQV-----------YNSH-SFYDTLFDVVPNPS-------VRQYNY 492
Cdd:cd16158   299 wPGRI---KPGVTHELASTLDILPTIAKLAGAPLPNVtldgvdmspilFEQGkSPRQTFFYYPTSPDpdkgvfaVRWGKY 375
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1482818008 493 -ADFQRNGVAGWAVRN-QDYKLLSIDSQQQA--LFDMNVDINEQNDLLQSGDDWSAL 545
Cdd:cd16158   376 kAHFYTQGAAHSGTTPdKDCHPSAELTSHDPplLFDLSQDPSENYNLLGLPEYNQVL 432
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
154-465 1.98e-20

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: 94.66  E-value: 1.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGV-DASnqySYSTDLPKTPILDSLATSGV-VFDNAWATPACTTTRGTIMTGMHGVNSG-VSF------ 224
Cdd:cd16159     1 KPNIVLFMADDLGIgDVG---CFGNDTIRTPNIDRLAKEGVkLTHHLAAAPLCTPSRAAFLTGRYPIRSGmASShgmrvi 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 225 ----VPAVMDTSLTTLPRFLAENdaskAYSMAVFGKWHLG-----GGDpDLSHPNSAGVGHYVGNITGTLDDYSDwtlTD 295
Cdd:cd16159    78 lftaSSGGLPPNETTFAEVLKQQ----GYSTALIGKWHLGlhcesRND-FCHHPLNHGFDYFYGLPLTNLKDCGD---GS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 296 NGSQT--------QVTQYHTSKVTDLAMDWITQQTS----------------PWFVWLAYVAP----------------- 334
Cdd:cd16159   150 NGEYDlsfdplfpLLTAFVLITALTIFLLLYLGAVSkrffvfllilsllfisLFFLLLITNRYfncilmrnhevveqpms 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 335 --------------------HSPFHLPPNELHTRSELSGSAEDIAQNPRPYYLAAIEAMDTEIGRLLASLptDE---REN 391
Cdd:cd16159   230 lenltqrltkeaisflernkERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDAL--DElglKDN 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 392 TLVIFIGDNGtpAPVIDTSVYARQHSKNSLY---------EGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAG 462
Cdd:cd16159   308 TFVYFTSDNG--GHLEEISVGGEYGGGNGGIyggkkmggwEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAG 385

                  ...
gi 1482818008 463 GDI 465
Cdd:cd16159   386 APL 388
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
155-468 6.37e-20

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


Pssm-ID: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 90.73  E-value: 6.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDdqgvdasnQYSYSTDLPKT------PILDSLATSGVVFDNAW-ATPACTTTRGTIMTGMH----GV--NSG 221
Cdd:cd16035     1 PNILLILTD--------QERYPPPWPAGwaalnlPARERLAANGLSFENHYtAACMCSPSRSTLYTGLHpqqtGVtdTLG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 222 VSFVPaVMDTSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPDLSHpnsagvghyvgnitgtlddysdwtltdngsqtq 301
Cdd:cd16035    73 SPMQP-LLSPDVPTLGHMLRAAG----YYTAYKGKWHLSGAAGGGYK--------------------------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 302 vtqyHTSKVTDLAMDWITQQTS------PWFVWLAYVAPHSpFHLPPNElhtrselsgsaEDIAQNPRPYYLAAIEAMDT 375
Cdd:cd16035   115 ----RDPGIAAQAVEWLRERGAknadgkPWFLVVSLVNPHD-IMFPPDD-----------EERWRRFRNFYYNLIRDVDR 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 376 EIGRLLASL-PTDERENTLVIFIGDNGTPApvidtSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLY 454
Cdd:cd16035   179 QIGRVLDALdASGLADNTIVVFTSDHGEMG-----GAHGLRGKGFNAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLL 253
                         330
                  ....*....|....
gi 1482818008 455 ATIVQIAGGDITQV 468
Cdd:cd16035   254 PTLLGLAGVDAEAR 267
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
155-473 3.48e-18

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: 86.44  E-value: 3.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDdqGVDASNQYSYSTDLPKTPILDSLATSGVVFDNAWA-TPACTTTRGTIMTGM--HGVNSGVSFvpAVMDT 231
Cdd:cd16171     1 PNVVMVMSD--SFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTnSPICCPSRAAMWSGLftHLTESWNNY--KGLDP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SLTTLPRFLAENdaskAYSMAVFGKWHLGGGDpdlsHPNSAGVGHYVGNITGTLDDYSDWT--LTDNGSQTQVtQYHTSK 309
Cdd:cd16171    77 NYPTWMDRLEKH----GYHTQKYGKLDYTSGH----HSVSNRVEAWTRDVPFLLRQEGRPTvnLVGDRSTVRV-MLKDWQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 310 VTDLAMDWITQ----QTSPWFVWLAYVAPHsPFHLPpnelhTRSELSGSAEDIaqnpRPYYLAAIEAMDTEIGRLLASL- 384
Cdd:cd16171   148 NTDKAVHWIRKeapnLTQPFALYLGLNLPH-PYPSP-----SMGENFGSIRNI----RAFYYAMCAETDAMLGEIISALk 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 385 PTDERENTLVIFIGDNGtpapviDTSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNtRESRLVNSTDLYATIVQIAGGD 464
Cdd:cd16171   218 DTGLLDKTYVFFTSDHG------ELAMEHRQFYKMSMYEGSSHVPLLIMGPGIKAGQ-QVSDVVSLVDIYPTMLDIAGVP 290

                  ....*....
gi 1482818008 465 ITQVYNSHS 473
Cdd:cd16171   291 QPQNLSGYS 299
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
154-462 1.14e-16

galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.


Pssm-ID: 293776 [Multi-domain]  Cd Length: 466  Bit Score: 82.51  E-value: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGvdASNQYSYSTDLPKTPILDSLATSGVVFDNAW-ATPACTTTRGTIMTGMHGVNSGVSFVPAVMDTS 232
Cdd:cd16157     1 KPNIILMLMDDMG--WGDLGVFGEPSRETPNLDRMAAEGMLFTDFYsANPLCSPSRAALLTGRLPIRNGFYTTNAHARNA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 233 LT-------------TLPRFLAENdaskAYSMAVFGKWHLG----------GGDPDLSHPNsAGVGHYVGNITGTLDDYS 289
Cdd:cd16157    79 YTpqnivggipdseiLLPELLKKA----GYRNKIVGKWHLGhrpqyhplkhGFDEWFGAPN-CHFGPYDNKAYPNIPVYR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 290 DWTLTD----------NGSQTQVTQYHTSKvtdlAMDWITQQTS---PWFVWLAYVAPHSPFHLPPNELHTRSelsgsae 356
Cdd:cd16157   154 DWEMIGryyeefkidkKTGESNLTQIYLQE----ALEFIEKQHDaqkPFFLYWAPDATHAPVYASKPFLGTSQ------- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 357 diaqnpRPYYLAAIEAMDTEIGRLLASL-PTDERENTLVIFIGDNGtpAPVIDTSVYARQHS-----KNSLYEGGIRVPL 430
Cdd:cd16157   223 ------RGLYGDAVMELDSSVGKILESLkSLGIENNTFVFFSSDNG--AALISAPEQGGSNGpflcgKQTTFEGGMREPA 294
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1482818008 431 LVSGNLLNKQNTRESRLVNSTDLYATIVQIAG 462
Cdd:cd16157   295 IAWWPGHIKPGQVSHQLGSLMDLFTTSLALAG 326
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
148-492 1.88e-15

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 79.31  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 148 GEPPVSKPNIILIISDDQGVDASNQYSYSTDLpkTPILDSLATSGVVFDNAWAtPACTTTRG--TIMTGMHGVNSGvSFV 225
Cdd:COG1368   228 PFGPAKKPNVVVILLESFSDFFIGALGNGKDV--TPFLDSLAKESLYFGNFYS-QGGRTSRGefAVLTGLPPLPGG-SPY 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 226 PAVMDTSLTTLPRFLAENDASKAYsmavfgkWHlgGGDP-----DLSHPNsAGVGHYVGnitgtLDDYSD-----WTLTD 295
Cdd:COG1368   304 KRPGQNNFPSLPSILKKQGYETSF-------FH--GGDGsfwnrDSFYKN-LGFDEFYD-----REDFDDpfdggWGVSD 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 296 ngsqtqvtqyhtSKVTDLAMDWITQQTSPWFVWLAYVAPHSPFHLPPNElhtrSELSGSAEDIAQNprpyYLAAIEAMDT 375
Cdd:COG1368   369 ------------EDLFDKALEELEKLKKPFFAFLITLSNHGPYTLPEED----KKIPDYGKTTLNN----YLNAVRYADQ 428
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 376 EIGRLLASLptDER---ENTLVIFIGDNGTPAPvidtsvyarQHSKNSLYEGGIRVPLLVSGNLLnKQNTRESRLVNSTD 452
Cdd:COG1368   429 ALGEFIEKL--KKSgwyDNTIFVIYGDHGPRSP---------GKTDYENPLERYRVPLLIYSPGL-KKPKVIDTVGSQID 496
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1482818008 453 LYATIVQIAGGDITQVYnshSFYDTLFDVVPNP-SVRQYNY 492
Cdd:COG1368   497 IAPTLLDLLGIDYPSYY---AFGRDLLSPDTDPfAFRNGGF 534
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
155-462 2.13e-14

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: 73.87  E-value: 2.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDdqGVDASNQYSYSTDLPKTPILDSLATSGVVFDNAWATpacTTTRGTI------MTGMHGVNSGVSFVPAV 228
Cdd:cd16015     1 PNVIVILLE--SFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSP---GFGGGTAngefevLTGLPPLPLGSGSYTLY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 229 MDTSLTTLPRFLAENDaskaYSMAVFgkwhlgggdpdlsHPNSA------------GVGHYVG--NITGTLDDYSDWTLT 294
Cdd:cd16015    76 KLNPLPSLPSILKEQG----YETIFI-------------HGGDAsfynrdsvypnlGFDEFYDleDFPDDEKETNGWGVS 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 295 DngsqtqvtqyhtSKVTDLAMDWITQQTS-PWFVWLAYVAPHSPFHLPPNELHTRSELSGSAEDIAQnprpyYLAAIEAM 373
Cdd:cd16015   139 D------------ESLFDQALEELEELKKkPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTELEN-----YLNAIHYT 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 374 DTEIGRLLASLPT-DERENTLVIFIGDNGtpaPVIDTSVYARQHSKNSLYeggiRVPLLVSGNLLnKQNTRESRLVNSTD 452
Cdd:cd16015   202 DKALGEFIEKLKKsGLYENTIIVIYGDHL---PSLGSDYDETDEDPLDLY----RTPLLIYSPGL-KKPKKIDRVGSQID 273
                         330
                  ....*....|
gi 1482818008 453 LYATIVQIAG 462
Cdd:cd16015   274 IAPTLLDLLG 283
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
155-461 1.05e-12

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: 67.83  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYSTdlPKTPILDSLATSGVVFDNAWATPACTTT--RGTIMTGMHGVNSGVsfvpavmdts 232
Cdd:cd00016     1 KHVVLIVLDGLGADDLGKAGNPA--PTTPNLKRLASEGATFNFRSVSPPTSSApnHAALLTGAYPTLHGY---------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 233 lttlprflAENDASKAYSMAVFGKWHLGGGdpdlshpnsagvghyvgNITGTLDDysdwtltdngSQTQVTQYHTSKvtd 312
Cdd:cd00016    69 --------TGNGSADPELPSRAAGKDEDGP-----------------TIPELLKQ----------AGYRTGVIGLLK--- 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 313 lAMDWITQQtSPWFVWLAYVAPHSPFHlppnelhtrselsgsaeDIAQNPRPYYlAAIEAMDTEIGRLLASLP-TDEREN 391
Cdd:cd00016   111 -AIDETSKE-KPFVLFLHFDGPDGPGH-----------------AYGPNTPEYY-DAVEEIDERIGKVLDALKkAGDADD 170
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 392 TLVIFIGDNGtpAPVIDTSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTrESRLVNSTDLYATIVQIA 461
Cdd:cd00016   171 TVIIVTADHG--GIDKGHGGDPKADGKADKSHTGMRVPFIAYGPGVKKGGV-KHELISQYDIAPTLADLL 237
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
155-535 2.90e-11

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: 65.72  E-value: 2.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDA----SNQYSYstdlpkTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTG--MHgVNsGVSFVPA 227
Cdd:cd16150     1 PNIVIFVADQLRADSlghlGNPAAV------TPNLDALAAEGVRFSNAYCQnPVCSPSRCSFLTGwyPH-VN-GHRTLHH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 228 VMDTSLTTLPRFLAENdaskAYSMAVFGKWHlgggdpDLSHPNSAGvghyvgnitgtldDYSDWtltDngsqtqvtqyht 307
Cdd:cd16150    73 LLRPDEPNLLKTLKDA----GYHVAWAGKND------DLPGEFAAE-------------AYCDS---D------------ 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 308 SKVTDLAMDWITQQTS--PWFVWLAYVAPHSPF-------------HLPPN--------------ELHTRSELSGSAEDI 358
Cdd:cd16150   115 EACVRTAIDWLRNRRPdkPFCLYLPLIFPHPPYgveepwfsmidreKLPPRrppglrakgkpsmlEGIEKQGLDRWSEER 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 359 AQNPRPYYLAAIEAMDTEIGRLLASL-PTDERENTLVIFIGDNGTpapvidtsvYARQHS-----KNSLYEGGIRVPLLV 432
Cdd:cd16150   195 WRELRATYLGMVSRLDHQFGRLLEALkETGLYDDTAVFFFSDHGD---------YTGDYGlvekwPNTFEDCLTRVPLII 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 433 SGNLLNKQNTRESrLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSVRQYNYAD----------FQRNGV-- 500
Cdd:cd16150   266 KPPGGPAGGVSDA-LVELVDIPPTLLDLAGIPLSHTHFGRSLLPVLAG--ETEEHRDAVFSEggrlhgeeqaMEGGHGpy 342
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1482818008 501 -----------------AGWAVRNQDYKLLSIDSQQQALFDMNVDINEQNDL 535
Cdd:cd16150   343 dlkwprllqqeeppehtKAVMIRTRRYKYVYRLYEPDELYDLEADPLELHNL 394
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
364-401 2.68e-03

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 40.12  E-value: 2.68e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1482818008 364 PYYLAAIEAMDTEIGRLLASLP-TDERENTLVIFIGDNG 401
Cdd:COG1524   205 PEYRAALREVDAALGRLLDALKaRGLYEGTLVIVTADHG 243
 
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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