|
Name |
Accession |
Description |
Interval |
E-value |
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
17-393 |
1.23e-175 |
|
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: 498.23 E-value: 1.23e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGLQHSIIRPTQPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGFYRKECMPTRRGFDTFFGSLLGSGDYYTHYKC 96
Cdd:cd16029 59 RYPIHTGMQHGVILAGEPYGLPLNETLLPQYLKELGYATHLVGKWHLGFYTWEYTPTNRGFDSFYGYYGGAEDYYTHTSG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 97 DSPGMCGYDLYENDNAAWDYdNGIYSTQMYTQRVQQILASHNPTKPIFLYIAYQAVHSPLQAPGRYFEHY----RSIINI 172
Cdd:cd16029 139 GANDYGNDDLRDNEEPAWDY-NGTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPYedkfAHIKDE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 173 NRRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQPTAG--GSNWPLRGSKGTYWEGGIRAVGFVHSPLLKN 250
Cdd:cd16029 218 DRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGdgGSNYPLRGGKNTLWEGGVRVPAFVWSPLLPP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 251 K-GTVCKELVHITDWYPTLISLAEGQIDEDIQLDGYDIWETISEGLRSPRVDILHNIDPIYTkakngswaagygiwnTAI 329
Cdd:cd16029 298 KrGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNIDDITR---------------TTG 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385566 330 QSAIRVQHWKLLTGNPgysdwvppqsfsnlgpnrwhneritlstgksvwLFNITADPYERVDLS 393
Cdd:cd16029 363 GAAIRVGDWKLIVGKP---------------------------------LFNIENDPCERNDLA 393
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
25-410 |
4.50e-67 |
|
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: 221.26 E-value: 4.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 25 QHSIIRPTQPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGFyRKECMPTRRGFD-TFFGSLLGSG-DYYTHYKCDSPGMc 102
Cdd:cd16144 80 NTKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGG-EGGYGPEDQGFDvNIGGTGNGGPpSYYFPPGKPNPDL- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 103 gydlyendnaaWDYDNGIYSTQMYTQRVQQILASHNpTKPIFLYIAYQAVHSPLQAPGRYFEHYRSIININRRR-----Y 177
Cdd:cd16144 158 -----------EDGPEGEYLTDRLTDEAIDFIEQNK-DKPFFLYLSHYAVHTPIQARPELIEKYEKKKKGLRKGqknpvY 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 178 AAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQPTAGG---SNWPLRGSKGTYWEGGIRAVGFVHSPLLKNKGTV 254
Cdd:cd16144 226 AAMIESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGpptSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGSV 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 255 CKELVHITDWYPTLISLAEGQIDEDIQLDGYDIWETIS-EGLRSPRvdilhniDPIYtkakngsW-AAGYGIWNTAIQSA 332
Cdd:cd16144 306 SDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKgGEADLPR-------RALF-------WhFPHYHGQGGRPASA 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385566 333 IRVQHWKLLtgnpgysdwvppqsfsnlgpnRWHNeritlstGKSVWLFNITADPYERVDLSNRYPGIVKKLLRRLSQF 410
Cdd:cd16144 372 IRKGDWKLI---------------------EFYE-------DGRVELYNLKNDIGETNNLAAEMPEKAAELKKKLDAW 421
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
17-393 |
6.03e-64 |
|
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: 212.42 E-value: 6.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGLQHSIIRPTQPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGFyRKECMPTRRGFDTFFGsLLGSGD--YYTHY 94
Cdd:cd16026 61 RYPVRVGLPGVVGPPGSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGH-QPEFLPTRHGFDEYFG-IPYSNDmwPFPLY 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 95 KCDSPGmCGYDLYENDNA-AWDYDngiYS--TQMYTQRVQQILASHNPtKPIFLYIAYQAVHSPLQAPGRYFEHYRsiin 171
Cdd:cd16026 139 RNDPPG-PLPPLMENEEViEQPAD---QSslTQRYTDEAVDFIERNKD-QPFFLYLAHTMPHVPLFASEKFKGRSG---- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 172 inRRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNG---GQPTAGGSNWPLRGSKGTYWEGGIRAVGFVHSPLL 248
Cdd:cd16026 210 --AGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwlEYGGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 249 KNKGTVCKELVHITDWYPTLISLAEGQIDEDIQLDGYDIWETISEGLRSPRVDILHNIDpiytkakngswaagygiwNTA 328
Cdd:cd16026 288 IPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYD------------------GGD 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385566 329 IQsAIRVQHWKLLtgnpgysdwVPPQSFSNLGPNRWHNeritlSTGKSVWLFNITADPYERVDLS 393
Cdd:cd16026 350 LQ-AVRSGRWKLH---------LPTTYRTGTDPGGLDP-----TKLEPPLLYDLEEDPGETYNVA 399
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
17-413 |
7.76e-58 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 195.87 E-value: 7.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGLQHsiIRPTQPNCLPLDNATLPQKLKEVGYSTHMVGKWHLgfyrkecmptrrgfdtffgsllgsgdyythykc 96
Cdd:COG3119 83 RYPHRTGVTD--NGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------------------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 97 dspgmcgydlyendnaawdydngiYSTQMYTQRVQQILASH-NPTKPIFLYIAYQAVHSPLQAPGRYFEHYR-------- 167
Cdd:COG3119 128 ------------------------YLTDLLTDKAIDFLERQaDKDKPFFLYLAFNAPHAPYQAPEEYLDKYDgkdiplpp 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 168 ---------SIININRRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQPTAGGsnwpLRGSKGTYWEGGIR 238
Cdd:COG3119 184 nlaprdlteEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHG----LRGGKGTLYEGGIR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 239 AVGFVHSPLLKNKGTVCKELVHITDWYPTLISLAEGQIDEDiqLDGYDIWETISEGLRSPRvdilhniDPIYTkakngSW 318
Cdd:COG3119 260 VPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWR-------DYLYW-----EY 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 319 AAGYGiwntaiQSAIRVQHWKLLtgnpgysdwvppqsfsnlgpnRWHNEritlstGKSVWLFNITADPYERVDLSNRYPG 398
Cdd:COG3119 326 PRGGG------NRAIRTGRWKLI---------------------RYYDD------DGPWELYDLKNDPGETNNLAADYPE 372
|
410
....*....|....*
gi 1229385566 399 IVKKLLRRLSQFNKT 413
Cdd:COG3119 373 VVAELRALLEAWLKE 387
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
17-410 |
1.48e-57 |
|
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: 195.85 E-value: 1.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGLQHSII-RptqpNCLPLDNATLPQKLKEVGYSTHMVGKWHLGF---YRkecmPTRRGFDTFFGSLLGS-GDYY 91
Cdd:cd16146 59 RYPFRTGVWHTILgR----ERMRLDETTLAEVFKDAGYRTGIFGKWHLGDnypYR----PQDRGFDEVLGHGGGGiGQYP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 92 THYKCDSPgmcgYDLYENdNAAWDYDNGiYSTQMYTQR----VQQilashNPTKPIFLYIAYQAVHSPLQAPGRYFEHYR 167
Cdd:cd16146 131 DYWGNDYF----DDTYYH-NGKFVKTEG-YCTDVFFDEaidfIEE-----NKDKPFFAYLATNAPHGPLQVPDKYLDPYK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 168 SI-ININRRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQP-TAGGSNWPLRGSKGTYWEGGIRAVGFVHS 245
Cdd:cd16146 200 DMgLDDKLAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGgVPKRFNAGMRGKKGSVYEGGHRVPFFIRW 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 246 PLLKNKGTVCKELVHITDWYPTLISLAEGQIDEDIQLDGYDIWETISEGLRS--PRVDILHNIDPIYTKAKNGswaagyg 323
Cdd:cd16146 280 PGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPwpERTLFTHSGRWPPPPKKKR------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 324 iwntaiQSAIRVQHWKLltgnpgysdwvppqsfsnLGPNRWHNEritlstgksvwLFNITADPYERVDLSNRYPGIVKKL 403
Cdd:cd16146 353 ------NAAVRTGRWRL------------------VSPKGFQPE-----------LYDIENDPGEENDVADEHPEVVKRL 397
|
....*..
gi 1229385566 404 LRRLSQF 410
Cdd:cd16146 398 KAAYEAW 404
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
21-397 |
1.31e-47 |
|
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: 169.31 E-value: 1.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 21 HTGlqHSIIR----PTQPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGFYRKECMPTRRGFDTFFGSL--LGSGDYYTHY 94
Cdd:cd16145 61 HTG--HTRVRgnsePGGQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHPTKQGFDYFYGYLdqVHAHNYYPEY 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 95 ------KCDSPGMCGYDLYENDNAawDYDNGIYSTQMYTQRVQQILASHNpTKPIFLYIAYQAVHSPLQAPGRYFEHYRS 168
Cdd:cd16145 139 lwrngeKVPLPNNVIPPLDEGNNA--GGGGGTYSHDLFTDEALDFIRENK-DKPFFLYLAYTLPHAPLQVPDDGPYKYKP 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 169 II---------NINRRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQPTAGG--------SNWPLRGSKGT 231
Cdd:cd16145 216 KDpgiyaylpwPQPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSEGGSehdpdffdSNGPLRGYKRS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 232 YWEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYPTLISLAEGQIDEDIqlDGYDIWETisegLRSPRVDILHniDPIYt 311
Cdd:cd16145 296 LYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDI--DGISLLPT----LLGKPQQQQH--DYLY- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 312 kakngswaagYGIWNTAIQSAIRVQHWKLLtgnpgysdwvppqsfsnlgpnrwhneRITLSTGKsVWLFNITADPYERVD 391
Cdd:cd16145 367 ----------WEFYEGGGAQAVRMGGWKAV--------------------------RHGKKDGP-FELYDLSTDPGETNN 409
|
....*.
gi 1229385566 392 LSNRYP 397
Cdd:cd16145 410 LAAQHP 415
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
15-393 |
1.04e-41 |
|
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: 153.13 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 15 PYRYQIHTG-------LQHSIIRPTQPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGFYRKecmptRRGFDTFFGSLLGS 87
Cdd:cd16143 52 PSRYGLLTGrypwrsrLKGGVLGGFSPPLIEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWK-----KKDGKKAATGTGKD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 88 GDYYTHYKcDSPGMCGYDlyendnaawdYDNGIYSTQM---YTQRVQQILASH-NPTKPIFLYIAYQAVHSPLQAPGRYf 163
Cdd:cd16143 127 VDYSKPIK-GGPLDHGFD----------YYFGIPASEVlptLTDKAVEFIDQHaKKDKPFFLYFALPAPHTPIVPSPEF- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 164 eHYRSIINinrrRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQPTAGG---------SNWPLRGSKGTYWE 234
Cdd:cd16143 195 -QGKSGAG----PYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPYADYkelekfghdPSGPLRGMKADIYE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 235 GGIRaVGF-VHSPLLKNKGTVCKELVHITDWYPTLISLAEGQIDEDIQLDGYDI---WetISEGLRSPRVDILHNidpiy 310
Cdd:cd16143 270 GGHR-VPFiVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFlpaL--LGPKKQEVRESLVHH----- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 311 tkAKNGSwaagygiwntaiqSAIRVQHWKLLTGNPGYSDWVPPQSfsnlgpnrwhneriTLSTGKSVWLFNITADPYERV 390
Cdd:cd16143 342 --SGNGS-------------FAIRKGDWKLIDGTGSGGFSYPRGK--------------EKLGLPPGQLYNLSTDPGESN 392
|
...
gi 1229385566 391 DLS 393
Cdd:cd16143 393 NLY 395
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
17-392 |
3.49e-40 |
|
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: 148.45 E-value: 3.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGLqHSIIRPTQPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGfYRKECMPTRRGFDTFFGSLlgsgdYYThykC 96
Cdd:cd16142 62 RHPIRTGL-TTVGLPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG-DEDGRLPTDHGFDEFYGNL-----YHT---I 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 97 DspgmcgydlyendnaawdydngiystQMYTQRVQQILASHNPT-KPIFLYIAYQAVHSP-LQAPGryFEHYRSIINinr 174
Cdd:cd16142 132 D--------------------------EEIVDKAIDFIKRNAKAdKPFFLYVNFTKMHFPtLPSPE--FEGKSSGKG--- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 175 rRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQPTA--GGSNWPLRGSKGTYWEGGIRAVGFVHSPLLKNKG 252
Cdd:cd16142 181 -KYADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGPEQDVwpDGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 253 TVCKELVHITDWYPTLISLAEGQIDE------DIQLDGYDIwetiseglrSPrvdilhnidpiYTKAKNGSWAAGYGIWN 326
Cdd:cd16142 260 RVSNEIVSHLDWFPTLAALAGAPDPKdkllgkDRHIDGVDQ---------SP-----------FLLGKSEKSRRSEFFYF 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385566 327 TAIQ-SAIRVQHWKLltgnpgYSDWVPPQSFSNLGPnrwhneritLSTGKSVWLFNITADPYERVDL 392
Cdd:cd16142 320 GEGElGAVRWKNWKV------HFKAQEDTGGPTGEP---------FYVLTFPLIFNLRRDPKERYDV 371
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
17-272 |
1.52e-39 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 144.87 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGLQHSIIRPTQ--PNCLPLDNATLPQKLKEVGYSTHMVGKWHLGFYRKECmPTRRGFDTFFGSLLGSGDYYTHY 94
Cdd:pfam00884 53 RFALLTGLPPHNFGSYVstPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS-PCNLGFDKFFGRNTGSDLYADPP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 95 KCDspgmcgydlyendnaaWDYDNGIYSTQMYTQRVQQILAshNPTKPIFLYIAYQAVHSPLQAPGRY------FEHYRS 168
Cdd:pfam00884 132 DVP----------------YNCSGGGVSDEALLDEALEFLD--NNDKPFFLVLHTLGSHGPPYYPDRYpekyatFKPSSC 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 169 IININRRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGgqPTAGGSNWPLRGSKG-TYWEGGIRAVGFVHSPL 247
Cdd:pfam00884 194 SEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHG--ESLGEGGGYLHGGKYdNAPEGGYRVPLLIWSPG 271
|
250 260
....*....|....*....|....*
gi 1229385566 248 LKNKGTVCKELVHITDWYPTLISLA 272
Cdd:pfam00884 272 GKAKGQKSEALVSHVDLFPTILDLA 296
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
17-308 |
7.25e-38 |
|
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: 142.22 E-value: 7.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGLQHSIIrPTQPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGfYRKECMPTRRGFDTFFGsllgsgdyyTHYKC 96
Cdd:cd16161 62 RLGLRNGVGHNFL-PTSVGGLPLNETTLAEVLRQAGYATGMIGKWHLG-QREAYLPNSRGFDYYFG---------IPFSH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 97 DSpgmcgydlyendnaawdydngiYSTQMYTQRVQQILASH-NPTKPIFLYIAYQAVHSPLQAPGRYfeHYRSIIninRR 175
Cdd:cd16161 131 DS----------------------SLADRYAQFATDFIQRAsAKDRPFFLYAALAHVHVPLANLPRF--QSPTSG---RG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 176 RYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNG---------GQPTAGG--SNWPLRGSKGTYWEGGIRAVGFVH 244
Cdd:cd16161 184 PYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcelaVGPGTGDwqGNLGGSVAKASTWEGGHREPAIVY 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229385566 245 SPLLKNKGTVCKELVHITDWYPTLISLAEGQIDEDIQLDGYDIWETISEGLRSPRVDILHNIDP 308
Cdd:cd16161 264 WPGRIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSG 327
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
37-392 |
9.44e-38 |
|
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: 142.20 E-value: 9.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 37 LPLDNATLPQKLKEVGYSTHMVGKWHLGFyrkecmptrrgfdtffgsllgsgdyythykcdspgmcgydlyendnaawdy 116
Cdd:cd16025 84 LPDSAATIAEVLKDAGYHTYMSGKWHLGP--------------------------------------------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 117 dNGIYSTQMYTQR-VQQILASHNPTKPIFLYIAYQAVHSPLQAP--------GRY---FEHYRS----------II---- 170
Cdd:cd16025 113 -DDYYSTDDLTDKaIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPkewidkykGKYdagWDALREerlerqkelgLIpadt 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 171 ---------------NINRRR--------YAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQPTAG---GSNWP 224
Cdd:cd16025 192 kltprppgvpawdslSPEEKKlearrmevYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEPGwanASNTP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 225 LRGSKGTYWEGGIRAVGFVHSP-LLKNKGTVCKELVHITDWYPTLISLAEGQIDEDI------QLDGYDIWETIS-EGLR 296
Cdd:cd16025 272 FRLYKQASHEGGIRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVngvpqlPLDGVSLLPTLDgAAAP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 297 SPRvdilhniDPIYtkakngswaagygiWNTAIQSAIRVQHWKLLTGNPGYSDwvppqsfsnlgPNRWHneritlstgks 376
Cdd:cd16025 352 SRR-------RTQY--------------FELFGNRAIRKGGWKAVALHPPPGW-----------GDQWE----------- 388
|
410
....*....|....*.
gi 1229385566 377 vwLFNITADPYERVDL 392
Cdd:cd16025 389 --LYDLAKDPSETHDL 402
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
17-303 |
2.37e-37 |
|
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: 142.18 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGLqHSIIRPTQPNC---LPLDNATLPQKLKEVGYSTHMVGKWHLGF--YRKE---CMPTRRGFDtFFGSLLgsg 88
Cdd:cd16160 61 RLPIRSGM-YGGTRVFLPWDiggLPKTEVTMAEALKEAGYTTGMVGKWHLGIneNNHSdgaHLPSHHGFD-FVGTNL--- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 89 DYYTHYKCDS---------PGMCGydLYENDNAAWDYDNGIYSTQMYTQRVQQILAShNPTKPIFLYIAYQAVHSPLQAP 159
Cdd:cd16160 136 PFTNSWACDDtgrhvdfpdRSACF--LYYNDTIVEQPIQHEHLTETLVGDAKSFIED-NQENPFFLYFSFPQTHTPLFAS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 160 GRYFEHYRsiininRRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQPT---AGGSNWPLRGSKGTYWEGG 236
Cdd:cd16160 213 KRFKGKSK------RGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEyclEGGSTGGLKGGKGNSWEGG 286
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229385566 237 IRAVGFVHSPllknkGT----VCKELVHITDWYPTLISLAEGQIDEDIQLDGYDIWETISEGLRSPRVDIL 303
Cdd:cd16160 287 IRVPFIAYWP-----GTikprVSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDIL 352
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
17-286 |
2.63e-37 |
|
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: 136.80 E-value: 2.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGLQHSIIRPTQpncLPLDNATLPQKLKEVGYSTHMVGKWHlgfyrkecmptrrgfdtffgsllgsgdyythykc 96
Cdd:cd16022 60 RYPHRHGVRGNVGNGGG---LPPDEPTLAELLKEAGYRTALIGKWH---------------------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 97 dspgmcgydlyendnaawdydngiystqmytQRVQQILASHNPTKPIFLYIAYQAVHSPLqapgryfehyrsiininrrR 176
Cdd:cd16022 103 -------------------------------DEAIDFIERRDKDKPFFLYVSFNAPHPPF-------------------A 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 177 YAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQPTAGGsnwpLRGSKGTYWEGGIRAVGFVHSPLLKNKGTVCK 256
Cdd:cd16022 133 YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHG----LRGKKGSLYEGGIRVPFIVRWPGKIPAGQVSD 208
|
250 260 270
....*....|....*....|....*....|
gi 1229385566 257 ELVHITDWYPTLISLAegQIDEDIQLDGYD 286
Cdd:cd16022 209 ALVSLLDLLPTLLDLA--GIEPPEGLDGRS 236
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
37-416 |
2.97e-34 |
|
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: 134.13 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 37 LPLDNATLPQKLKEVGYSTHMVGKWHLGfYRKECMPTRRGFDTFFGSLlgsgdyYTHYKC-DSPGMCGYDLYENDNAAWD 115
Cdd:cd16157 88 IPDSEILLPELLKKAGYRNKIVGKWHLG-HRPQYHPLKHGFDEWFGAP------NCHFGPyDNKAYPNIPVYRDWEMIGR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 116 Y--------DNGIYS-TQMYTQR-VQQILASHNPTKPIFLYIAYQAVHSPLQAPgryfEHYRSiiNINRRRYAAMLSCLD 185
Cdd:cd16157 161 YyeefkidkKTGESNlTQIYLQEaLEFIEKQHDAQKPFFLYWAPDATHAPVYAS----KPFLG--TSQRGLYGDAVMELD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 186 EAINNVTLALKTYGFYNNSIIIYSSDNG----GQPTAGGSNWPLRGSKGTYWEGGIRAVGFVHSPLLKNKGTVCKELVHI 261
Cdd:cd16157 235 SSVGKILESLKSLGIENNTFVFFSSDNGaaliSAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 262 TDWYPTLISLAEGQIDEDIQLDGYDIWETISEGLRSPRVDILHNIDPIYtKAKNGSWAAGYGIWNTAIQSAIRVQHwkll 341
Cdd:cd16157 315 MDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGDELM-AVRLGQYKAHFWTWSNSWEEFRKGIN---- 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229385566 342 tgnpgysdWVPPQSFSNLGPnrwHNEriTLSTGKSVwLFNITADPYERVDL---SNRYPGIVKKLLRRLSQFNKTAVP 416
Cdd:cd16157 390 --------FCPGQNVPGVTT---HNQ--TDHTKLPL-LFHLGRDPGEKYPIsfkSAEYKQAMPRISKVVQQHQKTLVP 453
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
17-428 |
2.49e-32 |
|
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: 128.72 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGLQHSIIRPTQPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGF-YRKECMPTRRGFDTFFGsLLGSGD------ 89
Cdd:cd16158 61 RYQVRSGVYPGVFYPGSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVgLNGTYLPTHQGFDHYLG-IPYSHDqgpcqn 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 90 ---YYTHYKCDS---PGMCGYDLYENDNAAWDYDNGIYSTQMYTQRVQQILA-SHNPTKPIFLYIAYQAVHSPLQAPGRY 162
Cdd:cd16158 140 ltcFPPNIPCFGgcdQGEVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIAdNAKEGKPFFLYYASHHTHYPQFAGQKF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 163 FEhyRSIininRRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQ---PTAGGSNWPLRGSKGTYWEGGIRA 239
Cdd:cd16158 220 AG--RSS----RGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPStmrKSRGGNAGLLKCGKGTTYEGGVRE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 240 VGFVHSPLLKNKGtVCKELVHITDWYPTLISLAeGQIDEDIQLDGYDIWETISEGLRSPRVDILHNidPIYTKAKNGSWA 319
Cdd:cd16158 294 PAIAYWPGRIKPG-VTHELASTLDILPTIAKLA-GAPLPNVTLDGVDMSPILFEQGKSPRQTFFYY--PTSPDPDKGVFA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 320 AGYGIWNTaiqsairvqHWklLTGNPGYSDWVPPQSFSNLGPNRWHNERItlstgksvwLFNITADPYERVDLSN--RYP 397
Cdd:cd16158 370 VRWGKYKA---------HF--YTQGAAHSGTTPDKDCHPSAELTSHDPPL---------LFDLSQDPSENYNLLGlpEYN 429
|
410 420 430
....*....|....*....|....*....|....*..
gi 1229385566 398 GIVKKLLRRLSQFNKTavpVRYPP------KDPRSNP 428
Cdd:cd16158 430 QVLKQIQQVKERFEAS---MKFGEseinkgEDPALEP 463
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
33-407 |
4.83e-29 |
|
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: 118.40 E-value: 4.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 33 QPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGFYRKECmptRRGFDtFFGSLLGSGDYYThykcdspgmcgydlYENDNA 112
Cdd:cd16031 73 NGPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLP---PPGFD-YWVSFPGQGSYYD--------------PEFIEN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 113 AWDYDNGIYSTQMYTQRVQQILASHNPTKPIFLYIAYQAVHSPLQAPGRYFEHYRSI----------------------- 169
Cdd:cd16031 135 GKRVGQKGYVTDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVtipepetfddddyagrpewareq 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 170 ININR-----------------RRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQptAGGSNWplrGSKGTY 232
Cdd:cd16031 215 RNRIRgvldgrfdtpekyqrymKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFF--LGEHGL---FDKRLM 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 233 WEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYPTLISLAEGQIDEDIQldGYDIWETIS-EGLRSPRVDILHNidpiYt 311
Cdd:cd16031 290 YEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQ--GRSLLPLLEgEKPVDWRKEFYYE----Y- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 312 kakngswaagYGIWN---TAIQSAIRVQHWKLLtgnpgysdwvppqsfsnlgpnRWHNERITlstgksvW-LFNITADPY 387
Cdd:cd16031 363 ----------YEEPNfhnVPTHEGVRTERYKYI---------------------YYYGVWDE-------EeLYDLKKDPL 404
|
410 420
....*....|....*....|..
gi 1229385566 388 ERVDLSN--RYPGIVKKLLRRL 407
Cdd:cd16031 405 ELNNLANdpEYAEVLKELRKRL 426
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
17-419 |
4.64e-28 |
|
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: 117.00 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGLQHS-----IIRPTQPNCLPLDNATLPQKLKEVGYSTHMVGKWHLGFYRKE----CM-PTRRGFDTFFG---- 82
Cdd:cd16159 61 RYPIRSGMASShgmrvILFTASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESrndfCHhPLNHGFDYFYGlplt 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 83 -------------------------------SLLGSGDYYTHYKCDSPGMC-------------GYD---------LYEN 109
Cdd:cd16159 141 nlkdcgdgsngeydlsfdplfplltafvlitALTIFLLLYLGAVSKRFFVFllilsllfislffLLLitnryfnciLMRN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 110 DNAA---WDYDNgiySTQMYTQRVQQILaSHNPTKPIFLYIAYQAVHSPLQAPGRYFEHYRsiininRRRYAAMLSCLDE 186
Cdd:cd16159 221 HEVVeqpMSLEN---LTQRLTKEAISFL-ERNKERPFLLVMSFLHVHTALFTSKKFKGRSK------HGRYGDNVEEMDW 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 187 AINNVTLALKTYGFYNNSIIIYSSDNGGQPT--------AGGSNWPLRGSKGTYWEGGIRAVGFVHSPLLKNKGTVCKEL 258
Cdd:cd16159 291 SVGQILDALDELGLKDNTFVYFTSDNGGHLEeisvggeyGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 259 VHITDWYPTLISLAEGQIDEDIQLDGYDIWETIS-EGLRSPRVDILH----NIDPIYTKAKNGswaagygiwnTAIqsai 333
Cdd:cd16159 371 TSLMDIFPTVAALAGAPLPSDRIIDGRDLMPLLTgQEKRSPHEFLFHycgaELHAVRYRPRDG----------GAV---- 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 334 rvqhWKLLTGNPgysDWVPpqsfsnlGPNRWHNERITLSTGKSV------WLFNITADPYERVDLS---NRYPGIVKKLL 404
Cdd:cd16159 437 ----WKAHYFTP---NFYP-------GTEGCCGTLLCRCFGDSVthhdppLLFDLSADPSESNPLDptdEPYQEIIKKIL 502
|
490
....*....|....*
gi 1229385566 405 RRLSQFNKTAVPVRY 419
Cdd:cd16159 503 EAVAEHQSSIEPVES 517
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
15-392 |
6.08e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 114.97 E-value: 6.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 15 PYR-------YQIHTGLQHsiirptqpNCLPLDNA--TLPQKLKEVGYSTHMVGKWHL-GFYRKECM-------PTRR-G 76
Cdd:cd16034 52 PYRaslltgqYPLTNGVFG--------NDVPLPPDapTIADVLKDAGYRTGYIGKWHLdGPERNDGRaddytppPERRhG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 77 FDTFFGsLLGSGDYYTHYkcdspgmcgydlYENDNAAWDYDNGiYSTQMYTQRVQQILASH-NPTKPIFLYIAYQAVHSP 155
Cdd:cd16034 124 FDYWKG-YECNHDHNNPH------------YYDDDGKRIYIKG-YSPDAETDLAIEYLENQaDKDKPFALVLSWNPPHDP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 156 -LQAPGRYFEHYRSIININR-----------------RRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQpt 217
Cdd:cd16034 190 yTTAPEEYLDMYDPKKLLLRpnvpedkkeeaglredlRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDM-- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 218 aGGSNWPLRgsKGTYWEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYPTLISLAEGQIDEDIQldGYDiwetISEGLRS 297
Cdd:cd16034 268 -LGSHGLMN--KQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVE--GRD----LSPLLLG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 298 PRvDILHNIDPIYTKAKNGSWAAGYGIWntaiQSAIRVQHWKLLtgnpgYSDWVPPqsfsnlgpnrwhneritlstgksv 377
Cdd:cd16034 339 GK-DDEPDSVLLQCFVPFGGGSARDGGE----WRGVRTDRYTYV-----RDKNGPW------------------------ 384
|
410
....*....|....*
gi 1229385566 378 WLFNITADPYERVDL 392
Cdd:cd16034 385 LLFDNEKDPYQLNNL 399
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
15-407 |
1.89e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 104.57 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 15 PYRYQIHTG--LQHSIIRPTQPncLPLDNATLPQKLKEVGYSTHMVGKWHLGFYrkecmptrrgfdtffgsllgsgdyyt 92
Cdd:cd16155 57 PSRAMLMTGrtLFHAPEGGKAA--IPSDDKTWPETFKKAGYRTFATGKWHNGFA-------------------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 93 hykcdspgmcgydlyendNAAWDYdngiystqmytqrvqqILASHNPTKPIFLYIAYQAVHSPLQAPGRYFEHY------ 166
Cdd:cd16155 109 ------------------DAAIEF----------------LEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYppetip 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 167 -----------------------------RSIININRRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGgqpT 217
Cdd:cd16155 155 lpenflpqhpfdngegtvrdeqlapfprtPEAVRQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHG---L 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 218 AGGSNwPLRGsKGTYWEGGIRAVGFVHSPLLKnKGTVCKELVHITDWYPTLISLAEGQIDEDIqlDGYDIWETISEGLRS 297
Cdd:cd16155 232 AVGSH-GLMG-KQNLYEHSMRVPLIISGPGIP-KGKRRDALVYLQDVFPTLCELAGIEIPESV--EGKSLLPVIRGEKKA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 298 PRvdilhniDPIYTKAKNGswaagygiwntaiQSAIRVQHWKLltgnpgysDWVPPQSfsnlgpnrwhneRITLstgksv 377
Cdd:cd16155 307 VR-------DTLYGAYRDG-------------QRAIRDDRWKL--------IIYVPGV------------KRTQ------ 340
|
410 420 430
....*....|....*....|....*....|..
gi 1229385566 378 wLFNITADPYERVDLS--NRYPGIVKKLLRRL 407
Cdd:cd16155 341 -LFDLKKDPDELNNLAdePEYQERLKKLLAEL 371
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-392 |
1.28e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 101.91 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGLQHSIIRPTQPnclpldnaTLPQKLKEVGYSTHMVGKWHLG-FYRKECMPTRRGFDTFfgSLLGsgdyYTHYK 95
Cdd:cd16151 59 KYNFRNYVVFGYLDPKQK--------TFGHLLKDAGYATAIAGKWQLGgGRGDGDYPHEFGFDEY--CLWQ----LTETG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 96 CDSPGMCGYDLYENDNAAWDYDNGIYSTQMYTQRV-QQIlaSHNPTKPIFLYIAYQAVHSPLQ----------APGRYFE 164
Cdd:cd16151 125 EKYSRPATPTFNIRNGKLLETTEGDYGPDLFADFLiDFI--ERNKDQPFFAYYPMVLVHDPFVptpdspdwdpDDKRKKD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 165 HYRsiininrrRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQPT----AGGSNwpLRGSKGTYWEGGIRAV 240
Cdd:cd16151 203 DPE--------YFPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrTNGRE--VRGGKGKTTDAGTHVP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 241 GFVHSPLLKNKGTVCKELVHITDWYPTLISLAEGQIDEDIQLDGYDIWETISEGLRSPRVDILHnidpIYTKAKNGSWAA 320
Cdd:cd16151 273 LIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIY----WYYRNPHKKFGS 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385566 321 GygiwntaiqsAIRVQHWKLltgnpgYSDwvppqsfsnlgpnrwhneritlstGKsvwLFNITADPYERVDL 392
Cdd:cd16151 349 R----------FVRTKRYKL------YAD------------------------GR---FFDLREDPLEKNPL 377
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
43-408 |
1.48e-21 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 97.05 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 43 TLPQKLKEVGYSTHMVGKWHLGFYRKECmptrrGFDtffGSLLGSG-----------------DYYTHYKCDSPG----M 101
Cdd:PRK13759 87 TLPQEFRDAGYYTQCIGKMHVFPQRNLL-----GFH---NVLLHDGylhsgrnedksqfdfvsDYLAWLREKAPGkdpdL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 102 CGYDLYENDNAA--WDYDNGIYSTQMYTQRVQQILASHNPTKPIFLYIAYQAVHSPLQAPGRYFEHY------------- 166
Cdd:PRK13759 159 TDIGWDCNSWVArpWDLEERLHPTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSPYDPPKRYFDMYkdadipdphigdw 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 167 -------RSIININ--------------RRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQptAGGSNWpL 225
Cdd:PRK13759 239 eyaedqdPEGGSIDalrgnlgeeyarraRAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDM--LGDHYL-F 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 226 RgsKGTYWEGGIRAVGFVHSP---LLKNKGTVCKELVHITDWYPTLISLAEGQIDEDiqLDGYDIWETISEGLRSPRvDI 302
Cdd:PRK13759 316 R--KGYPYEGSAHIPFIIYDPgglLAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYEGWR-PY 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 303 LHnidpiytkaknGSWAAGYgiwntaiQSairvQHWkLLTGNPGYSdWvppqsFSNLGPNRwhneritlstgksvwLFNI 382
Cdd:PRK13759 391 LH-----------GEHALGY-------SS----DNY-LTDGKWKYI-W-----FSQTGEEQ---------------LFDL 426
|
410 420 430
....*....|....*....|....*....|..
gi 1229385566 383 TADPYERVDLSN--RYPGIV----KKLLRRLS 408
Cdd:PRK13759 427 KKDPHELHNLSPseKYQPRLremrKKLVDHLR 458
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
17-281 |
2.54e-21 |
|
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: 95.27 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGLQHsiIRPTQPNcLPLDNATLPQKLKEVGYSTHMVGKWHLGFyrkecmPTRRGFDTFFGSLLGSGDYythykc 96
Cdd:cd16027 59 LYPHQNGAHG--LRSRGFP-LPDGVKTLPELLREAGYYTGLIGKTHYNP------DAVFPFDDEMRGPDDGGRN------ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 97 dspgmcgydlyendnaAWDYDngiystqmytQRVQQILASHNPTKPIFLYIAYQAVHSPLQAPGRYFEHYR-SIINI--- 172
Cdd:cd16027 124 ----------------AWDYA----------SNAADFLNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDpEKVKVppy 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 173 ------NRR---RYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGgqptaggsnWPLRGSKGTYWEGGIRaVGF- 242
Cdd:cd16027 178 lpdtpeVREdlaDYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG---------MPFPRAKGTLYDSGLR-VPLi 247
|
250 260 270
....*....|....*....|....*....|....*....
gi 1229385566 243 VHSPLLKNKGTVCKELVHITDWYPTLISLAEGQIDEDIQ 281
Cdd:cd16027 248 VRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQ 286
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-319 |
1.47e-20 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 93.18 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 17 RYQIHTGlqhsIIRPtqPNCLPLDNATLPQKLKE----VGYSTHMVGKWHLGfyRKECMPTRRGFDTFFGSLLGSG--DY 90
Cdd:cd16154 61 KYGFRTG----VLAV--PDELLLSEETLLQLLIKdattAGYSSAVIGKWHLG--GNDNSPNNPGGIPYYAGILGGGvqDY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 91 YThykcdspgmcgYDLYENDNAAwdyDNGIYSTQMYTQrvQQILASHNPTKPIFLYIAYQAVHSPLQAP-----GRYFEH 165
Cdd:cd16154 133 YN-----------WNLTNNGQTT---NSTEYATTKLTN--LAIDWIDQQTKPWFLWLAYNAPHTPFHLPpaelhSRSLLG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 166 YRSIININRRR-YAAMLSCLDEAINNVtLALKTYGFYNNSIIIYSSDNGGQPTAGGSNWPLRGSKGTYWEGGIRAVGFVH 244
Cdd:cd16154 197 DSADIEANPRPyYLAAIEAMDTEIGRL-LASIDEEERENTIIIFIGDNGTPGQVVDLPYTRNHAKGSLYEGGINVPLIVS 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385566 245 SPLLKNKGTVCKELVHITDWYPTLISLAEGQIDEdiQLDGYDIWETISEGLRSPRvdilhniDPIYTKAKNGSWA 319
Cdd:cd16154 276 GAGVERANERESALVNATDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNASTR-------QYNYTEYESPTTT 341
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
81-300 |
2.99e-17 |
|
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: 82.59 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 81 FGSLLGSGDYYT------HYkcdspgmcgydLYENDNAAWDYDngiystQMYTQRVQQILASHNP-TKPIFLYIAYQAVH 153
Cdd:cd16037 81 WGHALRAAGYETvligklHF-----------RGEDQRHGFRYD------RDVTEAAVDWLREEAAdDKPWFLFVGFVAPH 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 154 SPLQAPGRYFEHYRSIIninRRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQPTAGGSNWplrgsKGTYW 233
Cdd:cd16037 144 FPLIAPQEFYDLYVRRA---RAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWG-----KSTMY 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229385566 234 EGGiravgfVHSPLL-----KNKGTVCKELVHITDWYPTLISLAEGQIDEDiqLDGYDIWETISEGLRSPRV 300
Cdd:cd16037 216 EES------VRVPMIisgpgIPAGKRVKTPVSLVDLAPTILEAAGAPPPPD--LDGRSLLPLAEGPDDPDRV 279
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
39-284 |
3.03e-15 |
|
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: 77.21 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 39 LDNATLPQKLKEVGYSTHMVGKwHLGFYRKECMPTR--RGFDTFFGSLLGSGDYYTHYKCDSPGMcGYDLYENDnaawdy 116
Cdd:cd16147 82 LERSTLPVWLQEAGYRTAYAGK-YLNGYGVPGGVSYvpPGWDEWDGLVGNSTYYNYTLSNGGNGK-HGVSYPGD------ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 117 dngiYSTQMYTQRVQQILASHNPT-KPIFLYIAYQAVHSPLQAPGRYFEHY----------------------------- 166
Cdd:cd16147 154 ----YLTDVIANKALDFLRRAAADdKPFFLVVAPPAPHGPFTPAPRYANLFpnvtapprpppnnpdvsdkphwlrrlppl 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 167 -----RSIININRRRYAAMLScLDEAINNVTLALKTYGFYNNSIIIYSSDNG---GQPTaggsnwpLRGSKGTYWEGGIR 238
Cdd:cd16147 230 nptqiAYIDELYRKRLRTLQS-VDDLVERLVNTLEATGQLDNTYIIYTSDNGyhlGQHR-------LPPGKRTPYEEDIR 301
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1229385566 239 AVGFVHSPLLKnKGTVCKELVHITDWYPTLISLAEGQIDEDiqLDG 284
Cdd:cd16147 302 VPLLVRGPGIP-AGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDG 344
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
15-407 |
4.79e-15 |
|
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: 76.50 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 15 PYRYQIHTGLQhsiirPTQPNC------LPLDNATLPQKLKEVGYSTHMVGKWHLGFYRKECMptrrgfdtffgsllgsg 88
Cdd:cd16152 52 PARACLQTGLY-----PTETGCfrngipLPADEKTLAHYFRDAGYETGYVGKWHLAGYRVDAL----------------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 89 dyythykcdspgmcgydlyendnaawdydngiystqmyTQRVQQILASHNPTKPIFLYIAYQAVH---------SP---- 155
Cdd:cd16152 110 --------------------------------------TDFAIDYLDNRQKDKPFFLFLSYLEPHhqndrdryvAPegsa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 156 -----------LQA-PGRYFEHYRSiininrrrYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNggqptagGSNW 223
Cdd:cd16152 152 erfanfwvppdLAAlPGDWAEELPD--------YLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH-------GCHF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 224 PLRGS--KGTYWEGGIravgfvHSPLLK-----NKGTVCKELVHITDWYPTLISLAegQIDEDIQLDGYDIWETISEGLR 296
Cdd:cd16152 217 RTRNAeyKRSCHESSI------RVPLVIygpgfNGGGRVEELVSLIDLPPTLLDAA--GIDVPEEMQGRSLLPLVDGKVE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 297 SPRVDILHNIdpiytkakNGSWaagygiwntaIQSAIRVQHWKLLTGNPGYSDWVPPQSfsnlgpNRWHNEritlstgks 376
Cdd:cd16152 289 DWRNEVFIQI--------SESQ----------VGRAIRTDRWKYSVAAPDKDGWKDSGS------DVYVED--------- 335
|
410 420 430
....*....|....*....|....*....|...
gi 1229385566 377 vWLFNITADPYERVDLSNR--YPGIVKKLLRRL 407
Cdd:cd16152 336 -YLYDLEADPYELVNLIGRpeYREVAAELRERL 367
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-284 |
4.18e-14 |
|
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: 72.27 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 43 TLPQKLKEVGYSTHMVGKWHLGfyrkecmptrrgfdtffgsllgsgdyythykcdspgmcgydlyendnaawdydngiys 122
Cdd:cd16149 91 TLPEVLQDAGYRCGLSGKWHLG---------------------------------------------------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 123 tqmyTQRVQQILASHNPTKPIFLYIAYQAVHSPLQapgryfehyrsiininrrrYAAMLSCLDEAINNVTLALKTYGFYN 202
Cdd:cd16149 113 ----DDAADFLRRRAEAEKPFFLSVNYTAPHSPWG-------------------YFAAVTGVDRNVGRLLDELEELGLTE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 203 NSIIIYSSDNG------GQPTAGGSNWPLrgskgTYWEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYPTLISLAEGQI 276
Cdd:cd16149 170 NTLVIFTSDNGfnmghhGIWGKGNGTFPL-----NMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDP 244
|
....*...
gi 1229385566 277 DEDIQLDG 284
Cdd:cd16149 245 PADPRLPG 252
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-410 |
8.98e-14 |
|
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: 73.02 E-value: 8.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 37 LPLDNATLPQKLKEVGYSTHMVGKWHLGfyrKECMPTRRGFDTFFgSLLGSGDYYThykcdspgmcgydlyendnaawdy 116
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVG---PEETPLDYGFDEYL-PVETTIEYFL------------------------ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 117 dngiysTQMYTQRVQQILAShnpTKPIFLYIAYQAVHSPLQAPGRYF----------------------EHYRSIINI-- 172
Cdd:cd16033 133 ------ADRAIEMLEELAAD---DKPFFLRVNFWGPHDPYIPPEPYLdmydpediplpesfaddfedkpYIYRRERKRwg 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 173 -----------NRRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGgqpTAGGSNwplRG-SKGTY-WEGGIRA 239
Cdd:cd16033 204 vdtedeedwkeIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHG---DALGAH---RLwDKGPFmYEETYRI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 240 VGFVHSPLLKNKGTVCKELVHITDWYPTLISLAegQIDEDIQLDGydiwetiseglRSpRVDILHNIDPiyTKAKNGSWA 319
Cdd:cd16033 278 PLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLA--GVDVPPKVDG-----------RS-LLPLLRGEQP--EDWRDEVVT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 320 AGYGIWNTAIQSAIRVQHWKLLTGNPGYsdwvppqsfsnlgpnrwhNEritlstgksvwLFNITADPYErvdLSNR---- 395
Cdd:cd16033 342 EYNGHEFYLPQRMVRTDRYKYVFNGFDI------------------DE-----------LYDLESDPYE---LNNLiddp 389
|
410
....*....|....*.
gi 1229385566 396 -YPGIVKKLLRRLSQF 410
Cdd:cd16033 390 eYEEILREMRTRLYEW 405
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
15-289 |
3.13e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 63.93 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 15 PYRYQIHTGL---QHSII--RPTQPNcLPLDNATLPQKLKEVGYSTHMVGKWHLGFYRKecmptrrgfdtffgsllgsgd 89
Cdd:cd16153 62 PSRTSMLTGRyphRTGVYgfEAAHPA-LDHGLPTFPEVLKKAGYQTASFGKSHLEAFQR--------------------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 90 yYThykcdspgmcgydlyENDNaawdydngiystQMYTQRVQQILASHNPTKPIFLYIAYQAVHSPLQAPGRYFEHYRsi 169
Cdd:cd16153 120 -YL---------------KNAN------------QSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEFRDRFD-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 170 ininrrrYAAMLSCLDEAINNVTLALKTYGFYN---NSIIIYSSDNGgqptaggsnWPL--RG--SKGTYWEGGIR-AVG 241
Cdd:cd16153 170 -------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHG---------WHLgeQGilAKFTFWPQSHRvPLI 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1229385566 242 FVHS-PLLKNKGTVCKELVHITDWYPTLISLAEGQIDEDIQLDGYDIWE 289
Cdd:cd16153 234 VVSSdKLKAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
40-284 |
6.49e-11 |
|
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: 63.37 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 40 DNA--------TLPQKLKEVGYSTHMVGKWHLgfyrkeCMPTR-RGFDtffgsllgsgdyythykcdspgmcgYDlyenD 110
Cdd:cd16032 69 DNAaefpadipTFAHYLRAAGYRTALSGKMHF------VGPDQlHGFD-------------------------YD----E 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 111 NAAWdydngiystqmytQRVQQI--LASHNPTKPIFLYIAYQAVHSPLQAPGRYFEHYrsIINInRRRYAAMLSCLDEAI 188
Cdd:cd16032 114 EVAF-------------KAVQKLydLARGEDGRPFFLTVSFTHPHDPYVIPQEYWDLY--VRRA-RRAYYGMVSYVDDKV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 189 NNVTLALKTYGFYNNSIIIYSSDNG---GQptaggsnwplRG--SKGTYWEGGIRAVGFVHSPLLKnKGTVCKELVHITD 263
Cdd:cd16032 178 GQLLDTLERTGLADDTIVIFTSDHGdmlGE----------RGlwYKMSFFEGSARVPLIISAPGRF-APRRVAEPVSLVD 246
|
250 260
....*....|....*....|..
gi 1229385566 264 WYPTLISLAEGQIDEDI-QLDG 284
Cdd:cd16032 247 LLPTLVDLAGGGTAPHVpPLDG 268
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
20-281 |
7.03e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 62.57 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 20 IHTGL---QHSIIRPTqpncLPLDNATLPQKLKEVGYSTHMVGKW-HLGFYRkecmPTRRGFDTFFGSLLGSGDyythyk 95
Cdd:cd16148 56 LFTGLypfYHGVWGGP----LEPDDPTLAEILRKAGYYTAAVSSNpHLFGGP----GFDRGFDTFEDFRGQEGD------ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 96 cdspgmcgydlyendnaawDYDNGIYSTQMYTQRVQQILASHNPTKPIFLYIAYQAVHSPlqapgryfehYRsiininrr 175
Cdd:cd16148 122 -------------------PGEEGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPHEP----------YL-------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 176 rYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNG---GQptaGGSNWplrGSKGTYWEGGIRAVGFVHSPLLKnKG 252
Cdd:cd16148 165 -YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGeefGE---HGLYW---GHGSNLYDEQLHVPLIIRWPGKE-PG 236
|
250 260
....*....|....*....|....*....
gi 1229385566 253 TVCKELVHITDWYPTLISLAEGQIDEDIQ 281
Cdd:cd16148 237 KRVDALVSHIDIAPTLLDLLGVEPPDYSD 265
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
105-272 |
2.03e-09 |
|
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: 57.82 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 105 DLYENDNAAWDYDN--GIYSTQMYTQRVQQILASHNPT---KPIFLYIAYQAVHSPLQAPGRYFEhyrsiininrrRYAA 179
Cdd:cd00016 78 LPSRAAGKDEDGPTipELLKQAGYRTGVIGLLKAIDETskeKPFVLFLHFDGPDGPGHAYGPNTP-----------EYYD 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 180 MLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQPtAGGSNWPLRGSKGTYWEGGIRAVGFVHSPLLKnKGTVCKELV 259
Cdd:cd00016 147 AVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGID-KGHGGDPKADGKADKSHTGMRVPFIAYGPGVK-KGGVKHELI 224
|
170
....*....|...
gi 1229385566 260 HITDWYPTLISLA 272
Cdd:cd00016 225 SQYDIAPTLADLL 237
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
15-284 |
2.91e-08 |
|
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: 55.66 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 15 PYRYQIHTGLqhsiiRPTQPNCLPL---------DNATLPQKLKEVGYSTHMVGK-WHLGFYRKECMPtrRGFDTFFGSL 84
Cdd:cd16030 52 PSRASLLTGR-----RPDTTGVYDNnsyfrkvapDAVTLPQYFKENGYTTAGVGKiFHPGIPDGDDDP--ASWDEPPNPP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 85 LGSGDYYTHYKCDSPGMCGYDLYENDNAAwDYDNGIYSTQMYTQRVQQILAS-HNPTKPIFLyiayqAV-----HSPLQA 158
Cdd:cd16030 125 GPEKYPPGKLCPGKKGGKGGGGGPAWEAA-DVPDEAYPDGKVADEAIEQLRKlKDSDKPFFL-----AVgfykpHLPFVA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 159 PGRYFEHY-RSIININ---------------------------------------------RRRYAAMLSCLDEAINNVT 192
Cdd:cd16030 199 PKKYFDLYpLESIPLPnpfdpidlpevawndlddlpkygdipalnpgdpkgplpdeqarelRQAYYASVSYVDAQVGRVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 193 LALKTYGFYNNSIIIYSSDNGgqptaggsnWPLrGSKGTY-----WEGGIRAVGFVHSPLLKNKGTVCKELVHITDWYPT 267
Cdd:cd16030 279 DALEELGLADNTIVVLWSDHG---------WHL-GEHGHWgkhtlFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPT 348
|
330
....*....|....*..
gi 1229385566 268 LISLAEgqIDEDIQLDG 284
Cdd:cd16030 349 LAELAG--LPAPPCLEG 363
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
15-272 |
2.88e-07 |
|
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: 52.21 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 15 PYRYQIHTGL---QHSIIRPTQPNCLPLDNATLPQ---KLKEVGYSTHMVGKWHLgfyrkecmptrrgfdtffgSLLGSG 88
Cdd:cd16035 51 PSRSTLYTGLhpqQTGVTDTLGSPMQPLLSPDVPTlghMLRAAGYYTAYKGKWHL-------------------SGAAGG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 89 dyythykcdspgmcgydlyendnaAWDYDngiystQMYTQRVQQIL----ASHNPTKPIFLYIAY---QAVHSPLQAPGR 161
Cdd:cd16035 112 ------------------------GYKRD------PGIAAQAVEWLrergAKNADGKPWFLVVSLvnpHDIMFPPDDEER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 162 YFEHyrsiininRRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQPTAGGsnwpLRGSKGTYWEGGIRaVG 241
Cdd:cd16035 162 WRRF--------RNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHG----LRGKGFNAYEEALH-VP 228
|
250 260 270
....*....|....*....|....*....|...
gi 1229385566 242 FVHS-PLLKNKGTVCKELV-HItDWYPTLISLA 272
Cdd:cd16035 229 LIIShPDLFGTGQTTDALTsHI-DLLPTLLGLA 260
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
15-407 |
1.57e-06 |
|
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: 50.34 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 15 PYRYQIHTGL---QHSIIRPTQPncLPLDNATLPQKLKEVGYSTHMVGKWHLGfyrkecmPTRRGFDTFFGSLLGSGDyy 91
Cdd:cd16028 51 PSRASLYTGRylmNHRSVWNGTP--LDARHLTLALELRKAGYDPALFGYTDTS-------PDPRGLAPLDPRLLSYEL-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 92 thykcdspGMCGYDLYENDN--AAWDYDngiysTQMYTQRVQQILASHnPTKPIFLYIAYQAVHSPLQAPGRY------- 162
Cdd:cd16028 120 --------AMPGFDPVDRLDeyPAEDSD-----TAFLTDRAIEYLDER-QDEPWFLHLSYIRPHPPFVAPAPYhalydpa 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 163 --------------------FEHYRSII------------------NINRRR--YAAMLSCLDEAINNVTLALKTYGFYN 202
Cdd:cd16028 186 dvpppiraeslaaeaaqhplLAAFLERIeslsfspgaanaadlddeEVAQMRatYLGLIAEVDDHLGRLFDYLKETGQWD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 203 NSIIIYSSDNGGQptaGGSNWpLRGsKGTYWEGGiravgfVHSPLL---------KNKGTVCKELVHITDWYPTLISLAE 273
Cdd:cd16028 266 DTLIVFTSDHGEQ---LGDHW-LWG-KDGFFDQA------YRVPLIvrdprreadATRGQVVDAFTESVDVMPTILDWLG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 274 GQIDEdiQLDGydiwetiseglRS--PrvdILHNIDPiytkakngswaagyGIWNTAIqsairvqHWKLLTGNPGYSDwv 351
Cdd:cd16028 335 GEIPH--QCDG-----------RSllP---LLAGAQP--------------SDWRDAV-------HYEYDFRDVSTRR-- 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229385566 352 pPQSFSNLGPNR-----WHNERITLS--TGKSVWLFNITADPYERVDLSNR--YPGIVKKLLRRL 407
Cdd:cd16028 376 -PQEALGLSPDEcslavIRDERWKYVhfAALPPLLFDLKNDPGELRDLAADpaYAAVVLRYAQKL 439
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
43-211 |
3.37e-06 |
|
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: 48.83 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 43 TLPQKLKEVGYSTHMVGKWHLGFY-RKECMPtRRGFDTFFGSllgsgDYYTH--YKCDSPGMCGYDLYEndnaawdydng 119
Cdd:cd16015 82 SLPSILKEQGYETIFIHGGDASFYnRDSVYP-NLGFDEFYDL-----EDFPDdeKETNGWGVSDESLFD----------- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 120 iystqmytqRVQQILASHnPTKPIFLYIA-YQAvHSPLQAPGRYFEHYRSIININR--RRYAAMLSCLDEAINNVTLALK 196
Cdd:cd16015 145 ---------QALEELEEL-KKKPFFIFLVtMSN-HGPYDLPEEKKDEPLKVEEDKTelENYLNAIHYTDKALGEFIEKLK 213
|
170
....*....|....*
gi 1229385566 197 TYGFYNNSIIIYSSD 211
Cdd:cd16015 214 KSGLYENTIIVIYGD 228
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
138-356 |
1.00e-05 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 47.54 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 138 NPTKPIFLYIAYQAVHS-PLQAPGryfEHYRSIINInRRRYAAMLSCLDEAINNVTLALKTYGFYNNSIIIYSSDNGGQP 216
Cdd:cd16171 162 NLTQPFALYLGLNLPHPyPSPSMG---ENFGSIRNI-RAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELA 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 217 TAGGSNWplrgsKGTYWEGGiravgfVHSPLLK-----NKGTVCKELVHITDWYPTLISLAEGQIDEDiqLDGYDIWETI 291
Cdd:cd16171 238 MEHRQFY-----KMSMYEGS------SHVPLLImgpgiKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLL 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229385566 292 SEGlrsprvdilhNIDPIYTKAKNGSWAAG--YGIWNTAIQSAIRVQHWKLLTGNPGYSdwVPPQSF 356
Cdd:cd16171 305 SES----------SIKESPSRVPHPDWVLSefHGCNVNASTYMLRTNSWKYIAYADGNS--VPPQLF 359
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
43-287 |
7.22e-05 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 45.41 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 43 TLPQKLKEVGYSTHMvgkWH---LGFY-RKECMPtRRGFDTFFGsllgsGDYYTHYKCDSPGMCGYDLYendnaawdydn 118
Cdd:COG1368 313 SLPSILKKQGYETSF---FHggdGSFWnRDSFYK-NLGFDEFYD-----REDFDDPFDGGWGVSDEDLF----------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 119 giystqmytQRVQQILASHNptKPIFLYIayQAV--HSPLQAPgryfEHYRSIININRRRYAAMLSCL---DEAINNVTL 193
Cdd:COG1368 373 ---------DKALEELEKLK--KPFFAFL--ITLsnHGPYTLP----EEDKKIPDYGKTTLNNYLNAVryaDQALGEFIE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229385566 194 ALKTYGFYNNSIIIYSSDNGGqptaggsnwPLRGSKGTYWEGGIRAV-GFVHSPLLKNKGTVcKELVHITDWYPTLISLA 272
Cdd:COG1368 436 KLKKSGWYDNTIFVIYGDHGP---------RSPGKTDYENPLERYRVpLLIYSPGLKKPKVI-DTVGSQIDIAPTLLDLL 505
|
250
....*....|....*
gi 1229385566 273 EGQIDEDIQLdGYDI 287
Cdd:COG1368 506 GIDYPSYYAF-GRDL 519
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
379-417 |
7.23e-04 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 39.60 E-value: 7.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1229385566 379 LFNITADPYERVDLSN---RYPGIVKKLLRRLSQFNKTAVPV 417
Cdd:pfam14707 54 LFDLERDPSEKYPLSPdspEYPEVLAEIKAAVEEHKATLVPV 95
|
|
| |
