|
Name |
Accession |
Description |
Interval |
E-value |
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
61-496 |
0e+00 |
|
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: 530.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 61 GAPNILLVLLDDVGFGAASTFGGPVDTPTLEQLAQHGLRYNEFHTTAMCSPTRAALLSGRNHHSVHTGQIMEMATGYPGY 140
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTMAELATGKPGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 DSLVGRDTAGIGEILRQNGWNTAWFGKDHNVPDwetsqagpfdrwptglgfekfygfiggdmnqwrpllfdnttpiepyv 220
Cdd:cd16025 81 EGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 221 gkpDYNLDYDLADQAIKYVQTQHsmAPDKPFFIYYAPGATHAPHHPRKEWVDMYRGKFDQGWDVLREQTLARQKQLGIVP 300
Cdd:cd16025 114 ---DYYSTDDLTDKAIEYIDEQK--APDKPFFLYLAFGAPHAPLQAPKEWIDKYKGKYDAGWDALREERLERQKELGLIP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 301 QDTDLTKRSPGIPAWDSLSADDRKLYSRMMEIYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIYIvGDNgasgeggvggs 380
Cdd:cd16025 189 ADTKLTPRPPGVPAWDSLSPEEKKLEARRMEVYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFL-SDN----------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 381 tnleGAmNGVvpttaqmlpkiddlgtwktynhfpVGWAHALDTPFQWTKQiASHFGGTRNGMVISWPAHIKEDGQIRSQW 460
Cdd:cd16025 257 ----GA-SAE------------------------PGWANASNTPFRLYKQ-ASHEGGIRTPLIVSWPKGIKAKGGIRHQF 306
|
410 420 430
....*....|....*....|....*....|....*.
gi 2071673385 461 HHVIDILPTVLDVSHVPQPVEVNGVKQRPIEGVSMA 496
Cdd:cd16025 307 AHVIDIAPTILELAGVEYPKTVNGVPQLPLDGVSLL 342
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
52-490 |
3.88e-74 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 240.55 E-value: 3.88e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 52 FPRQTTAPAGAPNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRYNEFH-TTAMCSPTRAALLSGRNHHsvHTGq 129
Cdd:COG3119 13 AAAAAAAAAKRPNILFILADDLGYGDLGCYGNPlIKTPNIDRLAAEGVRFTNAYvTSPVCSPSRASLLTGRYPH--RTG- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 130 imeMATGYPGYDSLVGRDTAGIGEILRQNGWNTAWFGKDHNvpdwetsqagpfdrwptglgfekfygfiggdmnqwrpll 209
Cdd:COG3119 90 ---VTDNGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 210 fdnttpiepyvgkpdyNLDYDLADQAIKYVQTQHsmAPDKPFFIYYAPGATHAPHHPRKEWVDMYRGKFDQgwdvlreqt 289
Cdd:COG3119 128 ----------------YLTDLLTDKAIDFLERQA--DKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIP--------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 290 larqkqlgivpqdtdltkrspgIPAWDSLSADDRKLYSRMMEIYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIYiVGDN 369
Cdd:COG3119 181 ----------------------LPPNLAPRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVF-TSDN 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 370 gasgeggvggstnleGAMNGvvpttaqmlpkiddlgtwktynhfpvgwAHAldtpFQWTKQIAsHFGGTRNGMVISWPAH 449
Cdd:COG3119 238 ---------------GPSLG----------------------------EHG----LRGGKGTL-YEGGIRVPLIVRWPGK 269
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2071673385 450 IKEdGQIRSQWHHVIDILPTVLDVSHVPQPVEVNGVKQRPI 490
Cdd:COG3119 270 IKA-GSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPL 309
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
63-496 |
1.83e-50 |
|
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: 178.51 E-value: 1.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRYNEFHTTAMCSPTRAALLSGRNHHSV---HTgqimematgYP 138
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPiLKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTgvwHT---------IL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 139 GyDSLVGRDTAGIGEILRQNGWNTAWFGKdhnvpdWETSQAGPFDrwPTGLGFEKFYGFIGGDMNQ-WRPLLFDNTTPIE 217
Cdd:cd16146 72 G-RERMRLDETTLAEVFKDAGYRTGIFGK------WHLGDNYPYR--PQDRGFDEVLGHGGGGIGQyPDYWGNDYFDDTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 218 PYVGKPD----YNLDyDLADQAIKYVQTQHsmapDKPFFIYYAPGATHAPHHPRKEWVDMYRgkfDQGWDvlreqtlarq 293
Cdd:cd16146 143 YHNGKFVktegYCTD-VFFDEAIDFIEENK----DKPFFAYLATNAPHGPLQVPDKYLDPYK---DMGLD---------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 294 kqlgivpqdtdltkrspgipawdslsaDDRKLYSRMMeiyagylEQTDYNVGRVIKAIDDMGLSDNTLVIYIvGDNGASG 373
Cdd:cd16146 205 ---------------------------DKLAAFYGMI-------ENIDDNVGRLLAKLKELGLEENTIVIFM-SDNGPAG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 374 EGGVGGSTNLEGamngvvpttaqmlpkiddlgtWKTynhfpvgwahaldTPFQwtkqiashfGGTRNGMVISWPAHIKED 453
Cdd:cd16146 250 GVPKRFNAGMRG---------------------KKG-------------SVYE---------GGHRVPFFIRWPGKILAG 286
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2071673385 454 GQIrSQWHHVIDILPTVLDVSHVPQPVEVngvkqrPIEGVSMA 496
Cdd:cd16146 287 KDV-DTLTAHIDLLPTLLDLCGVKLPEGI------KLDGRSLL 322
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
63-476 |
9.78e-50 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 173.38 E-value: 9.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGPV-DTPTLEQLAQHGLRYNEFHTTA-MCSPTRAALLSGRNHHSVHtgqimematGYPGY 140
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRpTTPFLDRLAEEGLLFSNFYSGGtLTAPSRFALLTGLPPHNFG---------SYVST 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 DSLVGRDTAGIGEILRQNGWNTAWFGKDHNVPDWETSqagpfdrwPTGLGFEKFYGFIGGDMNQWRPllfdnttPIEPYV 220
Cdd:pfam00884 72 PVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS--------PCNLGFDKFFGRNTGSDLYADP-------PDVPYN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 221 GKPDYNLDYDLADQAIKYVQtqhsmAPDKPFFIYYAPGATHAPHHPRKEWVDMYRGKFDQGWDVlreqtlarqkqlgivp 300
Cdd:pfam00884 137 CSGGGVSDEALLDEALEFLD-----NNDKPFFLVLHTLGSHGPPYYPDRYPEKYATFKPSSCSE---------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 301 qdtdltkrspgipawdslsaddrklySRMMEIYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIYIvGDngasgeggvggs 380
Cdd:pfam00884 196 --------------------------EQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYT-SD------------ 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 381 tNLEGAMNGvvpttaqmlpkiddlgtwktynhfpvgwahalDTPFQWTKQIASHFGGTRNGMVISWPAHIKEdGQIRSQW 460
Cdd:pfam00884 237 -HGESLGEG--------------------------------GGYLHGGKYDNAPEGGYRVPLLIWSPGGKAK-GQKSEAL 282
|
410
....*....|....*.
gi 2071673385 461 HHVIDILPTVLDVSHV 476
Cdd:pfam00884 283 VSHVDLFPTILDLAGI 298
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
63-496 |
1.93e-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: 293763 [Multi-domain] Cd Length: 421 Bit Score: 170.42 E-value: 1.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRYNEFHTTA-MCSPTRAALLSGR--------NHHSVHTGQIME 132
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKfYETPNIDRLAKEGMRFTQAYAAApVCSPSRASILTGQyparlgitDVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 133 MATGYPGYDSLVGRDTAGIGEILRQNGWNTAWFGKDHnvpdwetsQAGPFDRWPTGLGFEKFYGFIGGDMNQWRPLLFDN 212
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWH--------LGGEGGYGPEDQGFDVNIGGTGNGGPPSYYFPPGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 213 TTPIEPYVGKPDYnLDYDLADQAIKYVQTQHsmapDKPFFIYYAPGATHAPHHPRKEWVDMYRGKFDQGWDVLREQTlar 292
Cdd:cd16144 153 PNPDLEDGPEGEY-LTDRLTDEAIDFIEQNK----DKPFFLYLSHYAVHTPIQARPELIEKYEKKKKGLRKGQKNPV--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 293 qkqlgivpqdtdltkrspgipawdslsaddrklysrmmeiYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIYIvGDNgas 372
Cdd:cd16144 225 ----------------------------------------YAAMIESLDESVGRILDALEELGLADNTLVIFT-SDN--- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 373 geggvggstnleGAMNGVVPTTAQMLPkiddLGTWKtynhfpvGWAHAldtpfqwtkqiashfGGTRNGMVISWPAHIKE 452
Cdd:cd16144 261 ------------GGLSTRGGPPTSNAP----LRGGK-------GSLYE---------------GGIRVPLIVRWPGVIKP 302
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2071673385 453 DGQIRSQWHHvIDILPTVLDVSHVPQPvevngvKQRPIEGVSMA 496
Cdd:cd16144 303 GSVSDVPVIG-TDLYPTFLELAGGPLP------PPQHLDGVSLV 339
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
63-495 |
2.32e-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: 293761 [Multi-domain] Cd Length: 372 Bit Score: 152.69 E-value: 2.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGPV----DTPTLEQLAQHGLRYNEFHTTAMCSPTRAALLSGRnhHSVHTGQIMEMATGYP 138
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIgrgaPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGR--HPIRTGLTTVGLPGSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 139 GYdsLVGRDTAgIGEILRQNGWNTAWFGKDH--NVPdwetsqagpfDRWPTGLGFEKFYGFiggdmnqwrpllfdnttpi 216
Cdd:cd16142 79 GG--LPPWEPT-LAELLKDAGYATAQFGKWHlgDED----------GRLPTDHGFDEFYGN------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 217 epyvgkPDYNLDYDLADQAIKYVQTQHsmAPDKPFFIYYAPGATHAPHHPRKEwvdmYRGKfdqgwdvlreqtlarqkql 296
Cdd:cd16142 127 ------LYHTIDEEIVDKAIDFIKRNA--KADKPFFLYVNFTKMHFPTLPSPE----FEGK------------------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 297 givpqdtdltkrSPGIPAWdslsADDrklysrMMEIyagyleqtDYNVGRVIKAIDDMGLSDNTLVIYIvGDNgasgegg 376
Cdd:cd16142 176 ------------SSGKGKY----ADS------MVEL--------DDHVGQILDALDELGIADNTIVIFT-TDN------- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 377 vggstnleGAMNGVVPttaqmlpkidDLGTwktynhfpvgwahaldTPFQWTKqiASHF-GGTRNGMVISWPAHIKEdGQ 455
Cdd:cd16142 218 --------GPEQDVWP----------DGGY----------------TPFRGEK--GTTWeGGVRVPAIVRWPGKIKP-GR 260
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2071673385 456 IRSQWHHVIDILPTVLDVSHVPQPVEVNGVKQRPIEGVSM 495
Cdd:cd16142 261 VSNEIVSHLDWFPTLAALAGAPDPKDKLLGKDRHIDGVDQ 300
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
63-496 |
2.54e-41 |
|
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: 153.49 E-value: 2.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRYNEFHTTA-MCSPTRAALLSGRnhHSVHTGqiMEMATGYPGY 140
Cdd:cd16026 2 PNIVVILADDLGYGDLGCYGSPlIKTPNIDRLAAEGVRFTDFYAAApVCSPSRAALLTGR--YPVRVG--LPGVVGPPGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 DSLVGRDTAGIGEILRQNGWNTAWFGKDH--NVPDWetsqagpfdrWPTGLGFEKFYGFIGG-DMN-----------QWR 206
Cdd:cd16026 78 KGGLPPDEITIAEVLKKAGYRTALVGKWHlgHQPEF----------LPTRHGFDEYFGIPYSnDMWpfplyrndppgPLP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 207 PLLFDNTTPIEPyvgkPDY-NLDYDLADQAIKYVQTQHsmapDKPFFIYYAPGATHAPHHPRKEWvdmyRGKFDQGwdvl 285
Cdd:cd16026 148 PLMENEEVIEQP----ADQsSLTQRYTDEAVDFIERNK----DQPFFLYLAHTMPHVPLFASEKF----KGRSGAG---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 286 reqtlarqkqlgivpqdtdltkrspgipawdsLSADDrklysrMMEIyagyleqtDYNVGRVIKAIDDMGLSDNTLVIYI 365
Cdd:cd16026 212 --------------------------------LYGDV------VEEL--------DWSVGRILDALKELGLEENTLVIFT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 366 vGDNgasgeggvggstnlegamngvvpttaqmlpkiddlGTWKTYnhfpvgWAHALDT-PFQWTKQiASHFGGTRNGMVI 444
Cdd:cd16026 246 -SDN-----------------------------------GPWLEY------GGHGGSAgPLRGGKG-TTWEGGVRVPFIA 282
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2071673385 445 SWPAHIKEdGQIRSQWHHVIDILPTVLDVSHVPQPvevngvKQRPIEGVSMA 496
Cdd:cd16026 283 WWPGVIPA-GTVSDELASTMDLLPTLAALAGAPLP------EDRVIDGKDIS 327
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
63-473 |
2.36e-37 |
|
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: 142.34 E-value: 2.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGG--PVDTPTLEQLAQHGLRYNEFHTT-AMCSPTRAALLSGRNHH-SVHTGQIMematgYP 138
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPdsKIPTPNIDRLAAEGMRFTDAHSPsSVCTPSRYGLLTGRYPWrSRLKGGVL-----GG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 139 GYDSLVGRDTAGIGEILRQNGWNTAWFGKDH------------------NVPDWEtsqaGPFDRWPTGLGFEKFYGFIGG 200
Cdd:cd16143 76 FSPPLIEPDRVTLAKMLKQAGYRTAMVGKWHlgldwkkkdgkkaatgtgKDVDYS----KPIKGGPLDHGFDYYFGIPAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 201 DMnqwrpllfdnttpiepyvgkpdynlDYDLADQAIKYVQTQHsmAPDKPFFIYYAPGATHAPHHPRKEWVdmyrGKfdq 280
Cdd:cd16143 152 EV-------------------------LPTLTDKAVEFIDQHA--KKDKPFFLYFALPAPHTPIVPSPEFQ----GK--- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 281 gwdvlreqtlarqkqlgivpqdtdlTKRSPgipawdslsaddrklysrmmeiYAGYLEQTDYNVGRVIKAIDDMGLSDNT 360
Cdd:cd16143 198 -------------------------SGAGP----------------------YGDFVYELDWVVGRILDALKELGLAENT 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 361 LVIYiVGDNgasgeggvggstnleGamnGVVPTTAQMLPKiddlgtwktYNHFPVGwahaldtPFQWTKqiASHF-GGTR 439
Cdd:cd16143 231 LVIF-TSDN---------------G---PSPYADYKELEK---------FGHDPSG-------PLRGMK--ADIYeGGHR 273
|
410 420 430
....*....|....*....|....*....|....
gi 2071673385 440 NGMVISWPAHIKEdGQIRSQWHHVIDILPTVLDV 473
Cdd:cd16143 274 VPFIVRWPGKIPA-GSVSDQLVSLTDLFATLAAI 306
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-364 |
7.82e-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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 135.39 E-value: 7.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGG-PVDTPTLEQLAQHGLRYNEFHTT-AMCSPTRAALLSGRNHHSvhtgqimemaTGYPGY 140
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDdPVKTPNLDRLAKEGVVFTNAVSNyPVCSPYRASLLTGQYPLT----------NGVFGN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 DSLVGRDTAGIGEILRQNGWNTAWFGKDH------NVPDWETSQAGPFDRwptgLGFEKFYGFiGGDMNQWRPLLFDNTT 214
Cdd:cd16034 72 DVPLPPDAPTIADVLKDAGYRTGYIGKWHldgperNDGRADDYTPPPERR----HGFDYWKGY-ECNHDHNNPHYYDDDG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 215 PIEPYVGK-PDYnldydLADQAIKYVQTQHSmaPDKPFFIYYAPGATHAPHHP-RKEWVDMYRGKfdqgwdvlreqtlar 292
Cdd:cd16034 147 KRIYIKGYsPDA-----ETDLAIEYLENQAD--KDKPFALVLSWNPPHDPYTTaPEEYLDMYDPK--------------- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2071673385 293 qkqlgivpqdtDLTKRsPGIPAWDSLSADDRklysRMMEIYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIY 364
Cdd:cd16034 205 -----------KLLLR-PNVPEDKKEEAGLR----EDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVF 260
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
63-485 |
8.71e-35 |
|
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: 131.02 E-value: 8.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRYNEFHTTA-MCSPTRAALLSGRNHHsvHTGqimemATGYPGY 140
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPdIKTPNLDRLAAEGVRFTNAYVASpVCSPSRASLLTGRYPH--RHG-----VRGNVGN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 DSLVGRDTAGIGEILRQNGWNTAWFGKDHnvpdwetsqagpfdrwptglgfekfygfiggdmnqwrpllfdnttpiepyv 220
Cdd:cd16022 74 GGGLPPDEPTLAELLKEAGYRTALIGKWH--------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 221 gkpdynldydlaDQAIKYVQTQhsmAPDKPFFIYYAPgatHAPHHPrkewvdmyrgkfdqgwdvlreqtlarqkqlgivp 300
Cdd:cd16022 103 ------------DEAIDFIERR---DKDKPFFLYVSF---NAPHPP---------------------------------- 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 301 qdtdltkrspgipawdslsaddrklysrmmEIYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIYiVGDNgasgeggvggs 380
Cdd:cd16022 131 ------------------------------FAYYAMVSAIDDQIGRILDALEELGLLDNTLIVF-TSDH----------- 168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 381 tnleGAMNGvvpttaqmlpkiddlgtwktynhfpvgwAHALdtpfQWTKqiASHF-GGTRNGMVISWPAHIKEdGQIRSQ 459
Cdd:cd16022 169 ----GDMLG----------------------------DHGL----RGKK--GSLYeGGIRVPFIVRWPGKIPA-GQVSDA 209
|
410 420
....*....|....*....|....*.
gi 2071673385 460 WHHVIDILPTVLDVSHVPQPVEVNGV 485
Cdd:cd16022 210 LVSLLDLLPTLLDLAGIEPPEGLDGR 235
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
63-484 |
3.21e-34 |
|
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: 134.19 E-value: 3.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRY-NEFHTTAMCSPTRAALLSG---RNHHSV--HTGQIMEMAT 135
Cdd:cd16031 3 PNIIFILTDDHRYDALGCYGNPiVKTPNIDRLAKEGVRFdNAFVTTSICAPSRASILTGqysHRHGVTdnNGPLFDASQP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 136 GYPgydslvgrdtagigEILRQNGWNTAWFGKDHNVPDWETSQAGpFDRWptglgfekfYGFIG-GdmNQWRPLLFDNtt 214
Cdd:cd16031 83 TYP--------------KLLRKAGYQTAFIGKWHLGSGGDLPPPG-FDYW---------VSFPGqG--SYYDPEFIEN-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 215 piEPYVGKPDYNLDYdLADQAIKYVQTQHsmaPDKPFFIYYAPGATHAPHHPRKEWVDMYRGKfdqgwDVLREQTLARQk 294
Cdd:cd16031 135 --GKRVGQKGYVTDI-ITDKALDFLKERD---KDKPFCLSLSFKAPHRPFTPAPRHRGLYEDV-----TIPEPETFDDD- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 295 qlGIVPQDTDLTKRSPGIPAWDSLSADDRKLYSRMMEIYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIYiVGDNgasge 374
Cdd:cd16031 203 --DYAGRPEWAREQRNRIRGVLDGRFDTPEKYQRYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIY-TSDN----- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 375 ggvggstnleGAMNGvvpttaqmlpkiddlgtwktyNHfpvGWAhalDtpfqwtKQIAsHFGGTRNGMVISWPAHIKEdG 454
Cdd:cd16031 275 ----------GFFLG---------------------EH---GLF---D------KRLM-YEESIRVPLIIRDPRLIKA-G 309
|
410 420 430
....*....|....*....|....*....|
gi 2071673385 455 QIRSQWHHVIDILPTVLDVSHVPQPVEVNG 484
Cdd:cd16031 310 TVVDALVLNIDFAPTILDLAGVPIPEDMQG 339
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
63-369 |
4.58e-34 |
|
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: 133.06 E-value: 4.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAAStFGGP--VDTPTLEQLAQHGLRYNEFHTTAMCSPTRAALLSGRnhHSVHTGqiMEMATGYPGY 140
Cdd:cd16029 1 PHIVFILADDLGWNDVG-FHGSdqIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGR--YPIHTG--MQHGVILAGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 DSLVGRDTAGIGEILRQNGWNTAWFGKDHnvpdwetsqAGpFDRW---PTGLGFEKFYGFIGGDMNQW-----------R 206
Cdd:cd16029 76 PYGLPLNETLLPQYLKELGYATHLVGKWH---------LG-FYTWeytPTNRGFDSFYGYYGGAEDYYthtsggandygN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 207 PLLFDNTTPIEPYVGKpdynldY--DL-ADQAIKYVQtQHsmAPDKPFFIYYAPGATHAPHHPRKEWVDMYRGKFDQGWD 283
Cdd:cd16029 146 DDLRDNEEPAWDYNGT------YstDLfTDRAVDIIE-NH--DPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 284 vlreqtlarqkqlgivpqdtdltkrspgipawdslsaDDRKLYSRMMeiyagylEQTDYNVGRVIKAIDDMGLSDNTLVI 363
Cdd:cd16029 217 -------------------------------------EDRRTYAAMV-------SALDESVGNVVDALKAKGMLDNTLIV 252
|
....*.
gi 2071673385 364 YIvGDN 369
Cdd:cd16029 253 FT-SDN 257
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
63-485 |
1.04e-33 |
|
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: 132.33 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGPV-DTPTLEQLAQHGLRYNEFHTTAM-CSPTRAALLSGRnhHSVHTGqiMEMATGYPGY 140
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKiKTPNLDRLAAEGMRFTQHYAGAPvCAPSRASLLTGL--HTGHTR--VRGNSEPGGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 DSLVGRDTAgIGEILRQNGWNTAWFGKdhnvpdWETSQAGPFDRwPTGLGFEKFYGFiggdMNQ------WRPLLFDN-- 212
Cdd:cd16145 77 DPLPPDDVT-LAEVLKKAGYATAAFGK------WGLGGPGTPGH-PTKQGFDYFYGY----LDQvhahnyYPEYLWRNge 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 213 TTPIEPYVGKPDYNLDYD-----------LADQAIKYVQTQHsmapDKPFFIYYAPGATHAPHHPRKEWVDMYRGKFDQG 281
Cdd:cd16145 145 KVPLPNNVIPPLDEGNNAgggggtyshdlFTDEALDFIRENK----DKPFFLYLAYTLPHAPLQVPDDGPYKYKPKDPGI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 282 wdvlreqtlarqkqlgivpqdtdltkrsPGIPAWDslsaDDRKLYSRMMEiyagYLeqtDYNVGRVIKAIDDMGLSDNTL 361
Cdd:cd16145 221 ----------------------------YAYLPWP----QPEKAYAAMVT----RL---DRDVGRILALLKELGIDENTL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 362 VIYiVGDNgasgeggvggstnleGAMNgvvpttaqmlpkidDLGTWKTYNHFpvgwahalDT--PFQWTKQiASHFGGTR 439
Cdd:cd16145 262 VVF-TSDN---------------GPHS--------------EGGSEHDPDFF--------DSngPLRGYKR-SLYEGGIR 302
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2071673385 440 NGMVISWPAHIKEDGQIRSQWHHViDILPTVLDVSHVPQPVEVNGV 485
Cdd:cd16145 303 VPFIARWPGKIPAGSVSDHPSAFW-DFMPTLADLAGAEPPEDIDGI 347
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
63-484 |
1.65e-33 |
|
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: 131.09 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGPVDTPTLEQLAQHGLRYNEFHTTA-MCSPTRAALLSGRNHHSvhTGQIMEMATGYPGYD 141
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTApVCSPSRSALLTGLYPHQ--NGAHGLRSRGFPLPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 142 slvgrDTAGIGEILRQNGWNTAWFGKDHNVPDWEtsqaGPFDRwptglgfekfygfiggdmnqwrpllfdnttpiEPYVG 221
Cdd:cd16027 79 -----GVKTLPELLREAGYYTGLIGKTHYNPDAV----FPFDD--------------------------------EMRGP 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 222 KPDYNLDYDLADQAIKYVQTQhsmAPDKPFFIYYAPGATHAPHHPRKEWVDMYRGKfdqgwDVlreqtlarqkqlgIVP- 300
Cdd:cd16027 118 DDGGRNAWDYASNAADFLNRA---KKGQPFFLWFGFHDPHRPYPPGDGEEPGYDPE-----KV-------------KVPp 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 301 --QDTDLTKrspgipawdslsaddrklysrmmEIYAGYL---EQTDYNVGRVIKAIDDMGLSDNTLVIYIvGDNgasgeg 375
Cdd:cd16027 177 ylPDTPEVR-----------------------EDLADYYdeiERLDQQVGEILDELEEDGLLDNTIVIFT-SDH------ 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 376 gvggstnlegamngvvpttaqmlpkiddlgtwktynhfpvGWahaldtPFQWTKQiASHFGGTRNGMVISWPAHIKEdGQ 455
Cdd:cd16027 227 ----------------------------------------GM------PFPRAKG-TLYDSGLRVPLIVRWPGKIKP-GS 258
|
410 420
....*....|....*....|....*....
gi 2071673385 456 IRSQWHHVIDILPTVLDVSHVPQPVEVNG 484
Cdd:cd16027 259 VSDALVSFIDLAPTLLDLAGIEPPEYLQG 287
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-496 |
2.49e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 127.72 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGG-PVDTPTLEQLAQHGLRYNEFHTTAMCSPTRAALLSGR--NHHSVHTGQimematgypg 139
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGeSYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKynFRNYVVFGY---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 140 ydsLVGRDTAgIGEILRQNGWNTAWFGKdhnvpdWetsQAGPFDRW---PTGLGFEKFYGF--IGGDMNQWRPllFDNTT 214
Cdd:cd16151 71 ---LDPKQKT-FGHLLKDAGYATAIAGK------W---QLGGGRGDgdyPHEFGFDEYCLWqlTETGEKYSRP--ATPTF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 215 PIEPYVGKPDYNLDY--DL-ADQAIKYVQTQHsmapDKPFFIYYAPGATHAPHHPrkewvdmyrgkfdqgwdvlreqtla 291
Cdd:cd16151 136 NIRNGKLLETTEGDYgpDLfADFLIDFIERNK----DQPFFAYYPMVLVHDPFVP------------------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 292 rqkqlgivpqdtdlTKRSPGIPAWDSLSADDRKLYSRMMEiyagYLeqtDYNVGRVIKAIDDMGLSDNTLVIYIvGDNga 371
Cdd:cd16151 187 --------------TPDSPDWDPDDKRKKDDPEYFPDMVA----YM---DKLVGKLVDKLEELGLRENTIIIFT-GDN-- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 372 sgeggvggSTNLE--GAMNGVVPTTAQMLPKIDdlgtwktynhfpvgwahaldtpfqwtkqiashfgGTRNGMVISWPAH 449
Cdd:cd16151 243 --------GTHRPitSRTNGREVRGGKGKTTDA----------------------------------GTHVPLIVNWPGL 280
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2071673385 450 IKEDGQIrSQWHHVIDILPTVLDVSHVPQPvevngvKQRPIEGVSMA 496
Cdd:cd16151 281 IPAGGVS-DDLVDFSDFLPTLAELAGAPLP------EDYPLDGRSFA 320
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-490 |
1.92e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 120.40 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRYNEFHT-TAMCSPTRAALLSGRNHHsvHTGQIMEMATGYPGY 140
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPiVKTPNIDRLAAEGVRFTNAYTpSPVCCPARASLLTGLYPH--EHGVLNNVENAGAYS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 DSLVgRDTAGIGEILRQNGWNTAWFGKDHnvpdwetsqAGPfDRWPTGLGFEKFygfiggdmnqwrpllfdntTPIEPYV 220
Cdd:cd16033 79 RGLP-PGVETFSEDLREAGYRNGYVGKWH---------VGP-EETPLDYGFDEY-------------------LPVETTI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 221 gkpdynlDYDLADQAIKYVqtQHSMAPDKPFFIYYapgATHAPHHP---RKEWVDMYRG---KFDQGWDvlreqtlarqk 294
Cdd:cd16033 129 -------EYFLADRAIEML--EELAADDKPFFLRV---NFWGPHDPyipPEPYLDMYDPediPLPESFA----------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 295 qlgivpqDTDLTKrsPGIPA-----WDSLSADDRKlYSRMMEIYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIYivgdn 369
Cdd:cd16033 186 -------DDFEDK--PYIYRrerkrWGVDTEDEED-WKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIF----- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 370 gasgeggvggsTNLEGAMNGvvpttaqmlpkiddlgtwktynhfpvgwAHALdtpfqWTKQIAsHFGGT-RNGMVISWPA 448
Cdd:cd16033 251 -----------TSDHGDALG----------------------------AHRL-----WDKGPF-MYEETyRIPLIIKWPG 285
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2071673385 449 HIKEdGQIRSQWHHVIDILPTVLDVSHVPQPVEVNGVKQRPI 490
Cdd:cd16033 286 VIAA-GQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPL 326
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-369 |
2.16e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 107.65 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRYNEFH-----TTAMCSPTRAALLSGRNHHSVhtgqimematg 136
Cdd:cd16155 3 PNILFILADDQRADTIGALGNPeIQTPNLDRLARRGTSFTNAYnmggwSGAVCVPSRAMLMTGRTLFHA----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 137 YPGYDSLVGRDTAGIGEILRQNGWNTAWFGKDHNvpdwetsqagpfdrwptglgfekfygfiggdmnqwrpllfdnttpi 216
Cdd:cd16155 72 PEGGKAAIPSDDKTWPETFKKAGYRTFATGKWHN---------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 217 epyvgkpdynldyDLADQAIKYVQTQHsmAPDKPFFIYYAPGATHAPHHPRKEWVDMYRGK-------------FDQGWD 283
Cdd:cd16155 106 -------------GFADAAIEFLEEYK--DGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPEtiplpenflpqhpFDNGEG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 284 VLREQTLArqkqlgivpqdtdltkrspgipAWDSLSADDRKLYSRmmeiYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVI 363
Cdd:cd16155 171 TVRDEQLA----------------------PFPRTPEAVRQHLAE----YYAMITHLDAQIGRILDALEASGELDNTIIV 224
|
....*.
gi 2071673385 364 YiVGDN 369
Cdd:cd16155 225 F-TSDH 229
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
63-495 |
5.10e-24 |
|
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: 105.24 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGPV-DTPTLEQLAQHGLRYNEFHTTA-MCSPTRAALLSGR----------NHHSVHTGQI 130
Cdd:cd16157 2 PNIILMLMDDMGWGDLGVFGEPSrETPNLDRMAAEGMLFTDFYSANpLCSPSRAALLTGRlpirngfyttNAHARNAYTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 131 MEMATGYPGYDSLvgrdtagIGEILRQNGWNTAWFGKdhnvpdWETSQAGPFdrWPTGLGFEKFYG----FIGGDMNQWR 206
Cdd:cd16157 82 QNIVGGIPDSEIL-------LPELLKKAGYRNKIVGK------WHLGHRPQY--HPLKHGFDEWFGapncHFGPYDNKAY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 207 PLL--FDNTTPIEPY-------VGKPDYNLDYDLADQAIKYVQTQHSmaPDKPFFIYYAPGATHAPHHPRKEwvdmYRGK 277
Cdd:cd16157 147 PNIpvYRDWEMIGRYyeefkidKKTGESNLTQIYLQEALEFIEKQHD--AQKPFFLYWAPDATHAPVYASKP----FLGT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 278 fdqgwdvlreqtlarqkqlgivpqdtdltkrspgipawdslsaDDRKLY-SRMMEIyagyleqtDYNVGRVIKAIDDMGL 356
Cdd:cd16157 221 -------------------------------------------SQRGLYgDAVMEL--------DSSVGKILESLKSLGI 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 357 SDNTLVIYiVGDNgasgeGGVGGSTNLEGAMNGvvpttaqmlpkiddlgtwktynhfpvgwahaldtPFQWTKQiASHFG 436
Cdd:cd16157 250 ENNTFVFF-SSDN-----GAALISAPEQGGSNG----------------------------------PFLCGKQ-TTFEG 288
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2071673385 437 GTRNGMVISWPAHIKEdGQIRSQWHHVIDILPTVLDVSHVPQPvevngvKQRPIEGVSM 495
Cdd:cd16157 289 GMREPAIAWWPGHIKP-GQVSHQLGSLMDLFTTSLALAGLPIP------SDRAIDGIDL 340
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
63-369 |
4.27e-23 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 101.47 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGPvdtPTLEQLAQHGLRYNEFH-TTAMCSPTRAALLSGR---NHHSVHTGQimematGYP 138
Cdd:cd16147 2 PNIVLILTDDQDVELGSMDPMP---KTKKLLADQGTTFTNAFvTTPLCCPSRASILTGQyahNHGVTNNSP------PGG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 139 GYDSLV--GRDTAGIGEILRQNGWNTAWFGK---DHNVPDWETsqagpfdrwPTGLGFEKFYGFIGGDMNQWRplLFDNT 213
Cdd:cd16147 73 GYPKFWqnGLERSTLPVWLQEAGYRTAYAGKylnGYGVPGGVS---------YVPPGWDEWDGLVGNSTYYNY--TLSNG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 214 TPIEPYVGKP-DYNLDYdLADQAIKYVQTQHSMapDKPFFIYYAPGATHAPHHPRKEWVDMYRGKFDQGwdvlreqtlAR 292
Cdd:cd16147 142 GNGKHGVSYPgDYLTDV-IANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPP---------RP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 293 QKQLGIVPQDTDLTKRSPGIPAWDSLSADdrklysrmmEIYAGYLeQT----DYNVGRVIKAIDDMGLSDNTLVIYIvGD 368
Cdd:cd16147 210 PPNNPDVSDKPHWLRRLPPLNPTQIAYID---------ELYRKRL-RTlqsvDDLVERLVNTLEATGQLDNTYIIYT-SD 278
|
.
gi 2071673385 369 N 369
Cdd:cd16147 279 N 279
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
63-490 |
5.52e-23 |
|
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: 102.14 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGPVD-TPTLEQLAQHGLRYNEFHTTA-MCSPTRAALLSGRNHhsVHTGQimematgYPGY 140
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSsTPNLDRLAANGLRFTDFYSSSpVCSPSRAALLTGRYQ--VRSGV-------YPGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 dsLVGRDTAG-------IGEILRQNGWNTAWFGKDHnvpdWETSQAGPFdrWPTGLGFEKFYG----------------- 196
Cdd:cd16158 73 --FYPGSRGGlplnettIAEVLKTVGYQTAMVGKWH----LGVGLNGTY--LPTHQGFDHYLGipyshdqgpcqnltcfp 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 197 -----FIGGDMNQWRPLLFDNTTPIEPYVGKPDYNLDY-DLADQAIKyvqtqHSMAPDKPFFIYYapgATHAPHHPRkew 270
Cdd:cd16158 145 pnipcFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYaKFAKDFIA-----DNAKEGKPFFLYY---ASHHTHYPQ--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 271 vdmYRGKfdqgwdvlreqtlarqkqlgivpqdtDLTKRSPGIPAWDSLsaddrklysrmMEIyagyleqtDYNVGRVIKA 350
Cdd:cd16158 214 ---FAGQ--------------------------KFAGRSSRGPFGDAL-----------AEL--------DGSVGELLQT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 351 IDDMGLSDNTLVIYiVGDNGasgeggvggstnlegamngvvPTTAQM-------LPKIddlGTWKTYNhfpvgwahaldt 423
Cdd:cd16158 246 LKENGIDNNTLVFF-TSDNG---------------------PSTMRKsrggnagLLKC---GKGTTYE------------ 288
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2071673385 424 pfqwtkqiashfGGTRNGMVISWPAHIKEDgqIRSQWHHVIDILPTVLDVSHVPQP-VEVNGVKQRPI 490
Cdd:cd16158 289 ------------GGVREPAIAYWPGRIKPG--VTHELASTLDILPTIAKLAGAPLPnVTLDGVDMSPI 342
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
62-490 |
3.66e-22 |
|
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: 98.31 E-value: 3.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 62 APNILLVLLDDVGFGAASTFGGP--VDTPTLEQLAQHGLRYNEFHTTA-MCSPTRAALLSGRnhHSVHTGqimemATGYP 138
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPnaILTPNLDKLAAEGTRFVDWYSAAsVCSPSRASLMTGR--LGLRNG-----VGHNF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 139 GYDSLVG---RDTAgIGEILRQNGWNTAWFGKdhnvpdWETSQAGPFdrWPTGLGFEKFYGFiggdmnqwrpllfdnttp 215
Cdd:cd16161 74 LPTSVGGlplNETT-LAEVLRQAGYATGMIGK------WHLGQREAY--LPNSRGFDYYFGI------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 216 iePYvgKPDYNLDYDLADQAIKYVQtQHSmAPDKPFFIYYAPGATHAP--HHPRKEWVDMYRGkfdqgwdvlreqtlarq 293
Cdd:cd16161 127 --PF--SHDSSLADRYAQFATDFIQ-RAS-AKDRPFFLYAALAHVHVPlaNLPRFQSPTSGRG----------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 294 kqlgivpqdtdltkrspgipawdslsaddrklysrmmeIYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIYiVGDNGASG 373
Cdd:cd16161 184 --------------------------------------PYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWF-TSDNGPWE 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 374 EGGVGGSTNLEGAMNGVVP-TTAQMlpkiddlGTWKtynhfpvgwahaldtpfqwtkqiashfGGTRNGMVISWPAHIKE 452
Cdd:cd16161 225 VKCELAVGPGTGDWQGNLGgSVAKA-------STWE---------------------------GGHREPAIVYWPGRIPA 270
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2071673385 453 dGQIRSQWHHVIDILPTVLDVSHVPQPV--EVNGVKQRPI 490
Cdd:cd16161 271 -NSTSAALVSTLDIFPTVVALAGASLPPgrIYDGKDLSPV 309
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-369 |
6.04e-21 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 94.72 E-value: 6.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGPVD---TPTLEQLAQHGLRYNEFHTTAMCSPTRAALLSGRnhHSVHTGQImematgYPG 139
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWATPACSPTRATILTGK--YGFRTGVL------AVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 140 YDSLVGRDTAGIGEILRQN--GWNTAWFGKdhnvpdWETSQAGPFDRWPTGLGFekFYGFIGG---DMNQWRPLLFDNTT 214
Cdd:cd16154 73 DELLLSEETLLQLLIKDATtaGYSSAVIGK------WHLGGNDNSPNNPGGIPY--YAGILGGgvqDYYNWNLTNNGQTT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 215 PIEPYVGKpdynldyDLADQAIKYVQTQHsmapdKPFFIYYAPGATHAPHH-PRKEWVdmyrgkfdqgwdvlreqtlarq 293
Cdd:cd16154 145 NSTEYATT-------KLTNLAIDWIDQQT-----KPWFLWLAYNAPHTPFHlPPAELH---------------------- 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2071673385 294 kqlgivpqDTDLTKRSPGIpawdslSADDRKLYSRMmeiyagyLEQTDYNVGRVIKAIDDMGLsDNTLVIYIvGDN 369
Cdd:cd16154 191 --------SRSLLGDSADI------EANPRPYYLAA-------IEAMDTEIGRLLASIDEEER-ENTIIIFI-GDN 243
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
61-484 |
3.03e-20 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 93.58 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 61 GAPNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRY-NEFHTTAMCSPTRAALLSGRN--HHsvhtgqimematG 136
Cdd:PRK13759 5 KKPNIILIMVDQMRGDCLGCNGNKaVETPNLDMLASEGYNFeNAYSAVPSCTPARAALLTGLSqwHH------------G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 137 YPGYDSLVGRD-TAGIGEILRQNGWNTAWFGKDHNVPdwETSQAG-----------PFDRWPTGLGFEKFygfigGDMNQ 204
Cdd:PRK13759 73 RVGYGDVVPWNyKNTLPQEFRDAGYYTQCIGKMHVFP--QRNLLGfhnvllhdgylHSGRNEDKSQFDFV-----SDYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 205 W--------RPLLFD-----NTTPIEPYVGKPDYNLDYDLADQAIKYVQTQHsmaPDKPFFIYYAPGATHAPHHPRKEWV 271
Cdd:PRK13759 146 WlrekapgkDPDLTDigwdcNSWVARPWDLEERLHPTNWVGSESIEFLRRRD---PTKPFFLKMSFARPHSPYDPPKRYF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 272 DMYrgkfdqgwdvlrEQTLARQKQLGIVPQDTDLTKRSPGIPAWDSLSADDRKlySRMMEIYAGYLEQTDYNVGRVIKAI 351
Cdd:PRK13759 223 DMY------------KDADIPDPHIGDWEYAEDQDPEGGSIDALRGNLGEEYA--RRARAAYYGLITHIDHQIGRFLQAL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 352 DDMGLSDNTLVIYiVGDNgasgeggvggstnleGAMNGvvpttaqmlpkidDLGTW-KTYnhfpvgwahaldtPFQwtkq 430
Cdd:PRK13759 289 KEFGLLDNTIILF-VSDH---------------GDMLG-------------DHYLFrKGY-------------PYE---- 322
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2071673385 431 iashfGGTRNGMVISWPAHIKE--DGQIRSQWHHVIDILPTVLDVSHVPQPVEVNG 484
Cdd:PRK13759 323 -----GSAHIPFIIYDPGGLLAgnRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDG 373
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-369 |
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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 90.68 E-value: 6.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRYNEFHTTA-MCSPTRAALLSGRnhhSVHTGQIMEMATGYPGy 140
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPvVRTPNLDRLAARGTRFENAYTPSpICVPSRASFLTGR---YVHETGVWDNADPYDG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 dslvgrDTAGIGEILRQNGWNTAWFGKDHNVpdwetsqaGPFDRWptglGFEKfygfiggdmnqwrpllfdnttpiepyv 220
Cdd:cd16037 77 ------DVPSWGHALRAAGYETVLIGKLHFR--------GEDQRH----GFRY--------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 221 gkpdynlDYDLADQAIKYVQTQhsMAPDKPFFI---YYAPgatHAPHHPRKEWVDMYRgkfdqgwdvlREQTLArqkqlg 297
Cdd:cd16037 112 -------DRDVTEAAVDWLREE--AADDKPWFLfvgFVAP---HFPLIAPQEFYDLYV----------RRARAA------ 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2071673385 298 ivpqdtdltkrspgipawdslsaddrklysrmmeiYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIYIV--GDN 369
Cdd:cd16037 164 -----------------------------------YYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSdhGDM 202
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
63-368 |
7.05e-20 |
|
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: 92.25 E-value: 7.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDD----VGFgaastFGG-PVDTPTLEQLAQHGLRYNEFHTT-AMCSPTRAALLSGRnhHSVHTGQImematG 136
Cdd:cd16030 3 PNVLFIAVDDlrpwLGC-----YGGhPAKTPNIDRLAARGVLFTNAYCQqPVCGPSRASLLTGR--RPDTTGVY-----D 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 137 YPGYDSLVGRDTAGIGEILRQNGWNTAWFGK-DHNVPDWETSQAGPFDRWPTGLGFEKfYGFIGGDMNQWRPLLFDNTTP 215
Cdd:cd16030 71 NNSYFRKVAPDAVTLPQYFKENGYTTAGVGKiFHPGIPDGDDDPASWDEPPNPPGPEK-YPPGKLCPGKKGGKGGGGGPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 216 IEPYVGkPDYNL-DYDLADQAIKYVQTQHSMapDKPFFI---YYAPgatHAPHH-PRKEWvDMYRGKFDQGWDVLREQTL 290
Cdd:cd16030 150 WEAADV-PDEAYpDGKVADEAIEQLRKLKDS--DKPFFLavgFYKP---HLPFVaPKKYF-DLYPLESIPLPNPFDPIDL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 291 ARQK--QLGIVPQDTDLTKRSPGIPAWDsLSADDRKLYSRmmeiyaGYL---EQTDYNVGRVIKAIDDMGLSDNTLVIyI 365
Cdd:cd16030 223 PEVAwnDLDDLPKYGDIPALNPGDPKGP-LPDEQARELRQ------AYYasvSYVDAQVGRVLDALEELGLADNTIVV-L 294
|
...
gi 2071673385 366 VGD 368
Cdd:cd16030 295 WSD 297
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
63-495 |
9.09e-20 |
|
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: 92.06 E-value: 9.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRYNEFHTTA-MCSPTRAALLSGRNHHSvhtgqimemaTGYPGY 140
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKaMKTPNLDRLAAEGVRFDSAYTTQpVCGPARSGLFTGLYPHT----------NGSWTN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 DSLVGRDTAGIGEILRQNGWNTAWFGKDHnvpdwetSQAGpfDRWPTGL---GFEKFYGFiggDMN------------QW 205
Cdd:cd16156 71 CMALGDNVKTIGQRLSDNGIHTAYIGKWH-------LDGG--DYFGNGIcpqGWDPDYWY---DMRnyldelteeerrKS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 206 RPLLfdntTPIEPYVGKPDYNLDYDLADQAIKYVQtQHSmapDKPFFIYYAPGATHAPHHPRKEWVDMYRG-KFDQG--- 281
Cdd:cd16156 139 RRGL----TSLEAEGIKEEFTYGHRCTNRALDFIE-KHK---DEDFFLVVSYDEPHHPFLCPKPYASMYKDfEFPKGena 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 282 WDVLREQTLARQkqlgivpqdtdltkrspgIPAWDSLSADDRKLYSRMMEiYAGYLEQTDYNVGRVIKAIDDMGlsDNTL 361
Cdd:cd16156 211 YDDLENKPLHQR------------------LWAGAKPHEDGDKGTIKHPL-YFGCNSFVDYEIGRVLDAADEIA--EDAW 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 362 VIYivgdngasgeggvggsTNLEGAMNGvvpttaqmlpkiddlgtwktynhfpvgwAHALdtpfqWTKQIASHFGGTRNG 441
Cdd:cd16156 270 VIY----------------TSDHGDMLG----------------------------AHKL-----WAKGPAVYDEITNIP 300
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2071673385 442 MVISWPAHIKEDGQIRSQWHHvIDILPTVLDVSHVPQPvevngvkqRPIEGVSM 495
Cdd:cd16156 301 LIIRGKGGEKAGTVTDTPVSH-IDLAPTILDYAGIPQP--------KVLEGESI 345
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
63-364 |
1.21e-17 |
|
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: 85.39 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRY-NEFHTTAMCSPTRAALLSGR---NHHSVhtgqimemATGY 137
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPlVKTPNLDRLAAEGVRFrNHYTQAAPCGPSRASLYTGRylmNHRSV--------WNGT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 138 PgydslVGRDTAGIGEILRQNGWNTAWFGKDHNVPDWETSQagPFDrwPTGLGFEkfygfigGDMNQWRPLLFDNTTPIE 217
Cdd:cd16028 73 P-----LDARHLTLALELRKAGYDPALFGYTDTSPDPRGLA--PLD--PRLLSYE-------LAMPGFDPVDRLDEYPAE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 218 pyvgkpdynlDYD---LADQAIKYVQTQhsmaPDKPFFI---YYAPgatHAPHHPRKEWVDMYRGkfDQGWDVLREQTL- 290
Cdd:cd16028 137 ----------DSDtafLTDRAIEYLDER----QDEPWFLhlsYIRP---HPPFVAPAPYHALYDP--ADVPPPIRAESLa 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 291 --ARQ----KQLGIVPQDTDLtkrSPGIPAWDSLSADDRKlysRMMEIYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIY 364
Cdd:cd16028 198 aeAAQhpllAAFLERIESLSF---SPGAANAADLDDEEVA---QMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVF 271
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-363 |
6.44e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 83.05 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGPVD-TPTLEQLAQHGLRYNEFHTTA-MCSPTRAALLSGRNHHSvhtgqimemaTGYPGY 140
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAvTPNLDALAAEGVRFSNAYCQNpVCSPSRCSFLTGWYPHV----------NGHRTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 DSLVGRDTAGIGEILRQNGWNTAWFGKDHNVPdwetsqaGPFDRwptglgfekfygfiggdmnqwrpllFDNTTPiepyv 220
Cdd:cd16150 71 HHLLRPDEPNLLKTLKDAGYHVAWAGKNDDLP-------GEFAA-------------------------EAYCDS----- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 221 gkpdynlDYDLADQAIKYVqTQHSmaPDKPFFIYYAPGATHAPHHPRKEWVDMYRgkfdqgwdvlREQTLARqkqlgiVP 300
Cdd:cd16150 114 -------DEACVRTAIDWL-RNRR--PDKPFCLYLPLIFPHPPYGVEEPWFSMID----------REKLPPR------RP 167
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2071673385 301 QDTDLTKRSPGIP-----AWDSLSADdrklysRMMEIYAGYL---EQTDYNVGRVIKAIDDMGLSDNTLVI 363
Cdd:cd16150 168 PGLRAKGKPSMLEgiekqGLDRWSEE------RWRELRATYLgmvSRLDHQFGRLLEALKETGLYDDTAVF 232
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
63-365 |
9.49e-17 |
|
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: 82.86 E-value: 9.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGPVDTPT-LEQLAQHGLRYNEFHTTA-MCSPTRAALLSGRnhHSVHTGQIMEMATGYPGY 140
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGpIDDMAAEGIRFTQAYSADsVCTPSRAALLTGR--LPIRSGMYGGTRVFLPWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 DSLVGRDTAGIGEILRQNGWNTAWFGKDHNVPDWETSQAGPfdRWPTGLGFEkFYGFIGGDMNQWR-------------- 206
Cdd:cd16160 80 IGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGA--HLPSHHGFD-FVGTNLPFTNSWAcddtgrhvdfpdrs 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 207 -PLLFDNTTPIE-PYvgKPDYnLDYDLADQAIKYVQTQHsmapDKPFFIYYAPGATHAPHHPRKEwvdmYRGKFDQGwdv 284
Cdd:cd16160 157 aCFLYYNDTIVEqPI--QHEH-LTETLVGDAKSFIEDNQ----ENPFFLYFSFPQTHTPLFASKR----FKGKSKRG--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 285 lreqtlarqkqlgivpqdtdltkrspgipawdslsaddrklysrmmeIYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIY 364
Cdd:cd16160 223 -----------------------------------------------RYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFF 255
|
.
gi 2071673385 365 I 365
Cdd:cd16160 256 L 256
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-483 |
8.41e-16 |
|
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: 77.28 E-value: 8.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRYNEFHTTA-MCSPTRAALLSGR--NHHSVH---TGQIMEMAT 135
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSeAVTPNLDRLAAEGVRFENFFCTSpVCSPARASLLTGRmpSQHGIHdwiVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 136 GYPGYdsLVGRDTagIGEILRQNGWNTAWFGKDHnvpdwetsqagpfdrwptglgfekfygfiggdmnqwrpllfdnttp 215
Cdd:cd16149 81 KPEGY--LEGQTT--LPEVLQDAGYRCGLSGKWH---------------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 216 iepyvgkpdynldydLADQAIKYVQTQHsmAPDKPFFIYYapgATHAPHHPrkeWvdmyrgkfdqgwdvlreQTLArqkq 295
Cdd:cd16149 111 ---------------LGDDAADFLRRRA--EAEKPFFLSV---NYTAPHSP---W-----------------GYFA---- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 296 lgivpqdtdltkrspgipawdSLSADDRklysrmmeiyagyleqtdyNVGRVIKAIDDMGLSDNTLVIYiVGDNgasgeg 375
Cdd:cd16149 147 ---------------------AVTGVDR-------------------NVGRLLDELEELGLTENTLVIF-TSDN------ 179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 376 gvggstnlegAMNgvvpttaqmlpkIDDLGTWKTYN-HFPVG-WAHALDTPFqwtkqiashfggtrngmVISWPAHIKED 453
Cdd:cd16149 180 ----------GFN------------MGHHGIWGKGNgTFPLNmYDNSVKVPF-----------------IIRWPGVVPAG 220
|
410 420 430
....*....|....*....|....*....|
gi 2071673385 454 GQIRSQWHHViDILPTVLDVSHVPQPVEVN 483
Cdd:cd16149 221 RVVDSLVSAY-DFFPTLLELAGVDPPADPR 249
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
63-495 |
3.66e-14 |
|
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: 75.02 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGG-PVDTPTLEQLAQHGLRYnEFHTTA--MCSPTRAALLSGRnhHSVHTGqimeMATGYPG 139
Cdd:cd16159 2 PNIVLFMADDLGIGDVGCFGNdTIRTPNIDRLAKEGVKL-THHLAAapLCTPSRAAFLTGR--YPIRSG----MASSHGM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 140 YDSLVGRDTAG-------IGEILRQNGWNTAWFGKDHnvPDWETSQAGPFDRWPTGLGFEKFYGF-------IGGDMNQ- 204
Cdd:cd16159 75 RVILFTASSGGlppnettFAEVLKQQGYSTALIGKWH--LGLHCESRNDFCHHPLNHGFDYFYGLpltnlkdCGDGSNGe 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 205 ---------------------------------WRPLLF---------------------------DNTTPIE-PYVGKp 223
Cdd:cd16159 153 ydlsfdplfplltafvlitaltiflllylgavsKRFFVFllilsllfislfflllitnryfncilmRNHEVVEqPMSLE- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 224 dyNLDYDLADQAIKYVQTQHsmapDKPFFIYYAPGATHAPHHPRKEwvdmYRGKFDQGwdvlreqtlarqkqlgivpqdt 303
Cdd:cd16159 232 --NLTQRLTKEAISFLERNK----ERPFLLVMSFLHVHTALFTSKK----FKGRSKHG---------------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 304 dltkrspgipawdslsaddrklysrmmeIYAGYLEQTDYNVGRVIKAIDDMGLSDNTLViYIVGDNGASGEGGVGGSTnl 383
Cdd:cd16159 280 ----------------------------RYGDNVEEMDWSVGQILDALDELGLKDNTFV-YFTSDNGGHLEEISVGGE-- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 384 EGAMNGVVPTTAQMlpkiddlGTWKtynhfpvgwahaldtpfqwtkqiashfGGTRNGMVISWPAHIKEDGQIRSQWHHv 463
Cdd:cd16159 329 YGGGNGGIYGGKKM-------GGWE---------------------------GGIRVPTIVRWPGVIPPGSVIDEPTSL- 373
|
490 500 510
....*....|....*....|....*....|..
gi 2071673385 464 IDILPTVLDVSHVPQPvevngvKQRPIEGVSM 495
Cdd:cd16159 374 MDIFPTVAALAGAPLP------SDRIIDGRDL 399
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-485 |
4.02e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 72.58 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGPVD-TPTLEQLAQHGLRYNEFHTTAM-CSPTRAALLSGR--NHHSVHTGQIMEmatgyp 138
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRVtTPNLDRLAAEGVVFDNHYSGSNpTLPSRFSLFTGLypFYHGVWGGPLEP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 139 gydslvGRDTagIGEILRQNGWNTAWFgkdhnvpdweTSQAGPFDRWPTGLGFEKFYGFIGgdmnqwrpllfdnttpIEP 218
Cdd:cd16148 75 ------DDPT--LAEILRKAGYYTAAV----------SSNPHLFGGPGFDRGFDTFEDFRG----------------QEG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 219 YVGKPDYNLDYDLADQAIKYVQTQHsmaPDKPFFIYyapgaTH--APHHPrkewvdmYRgkfdqgwdvlreqtlarqkql 296
Cdd:cd16148 121 DPGEEGDERAERVTDRALEWLDRNA---DDDPFFLF-----LHyfDPHEP-------YL--------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 297 givpqdtdltkrspgipawdslsaddrklysrmmeiYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIyIVGDNgasgegg 376
Cdd:cd16148 165 ------------------------------------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVI-VTSDH------- 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 377 vggstnleGAMNGvvpttaqmlpkidDLGTWktynhfpvgWAHAlDTPFQWTKQIAshfggtrngMVISWPAhiKEDGQI 456
Cdd:cd16148 201 --------GEEFG-------------EHGLY---------WGHG-SNLYDEQLHVP---------LIIRWPG--KEPGKR 238
|
410 420
....*....|....*....|....*....
gi 2071673385 457 RSQWHHVIDILPTVLDVSHVPQPVEVNGV 485
Cdd:cd16148 239 VDALVSHIDIAPTLLDLLGVEPPDYSDGR 267
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-364 |
2.82e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 64.54 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGF------GAASTfggpvDTPTLEQLAQHGLRYNEFHT-TAMCSPTRAALLSGrnHHSVHTGQIMemaT 135
Cdd:cd16035 1 PNILLILTDQERYpppwpaGWAAL-----NLPARERLAANGLSFENHYTaACMCSPSRSTLYTG--LHPQQTGVTD---T 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 136 GYPGYDSLVGRDTAGIGEILRQNGWNTAWFGKdhnvpdWETSQAGPfdrwptglgfekfygfiGGdmnqwrpllfdnttp 215
Cdd:cd16035 71 LGSPMQPLLSPDVPTLGHMLRAAGYYTAYKGK------WHLSGAAG-----------------GG--------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 216 iepyvgkpdYNLDYDLADQAIKYVQTQ-HSMAPDKPFFIyyapgathA-----PHhprkewvdmyrgkfdqgwDVLreqt 289
Cdd:cd16035 113 ---------YKRDPGIAAQAVEWLRERgAKNADGKPWFL--------VvslvnPH------------------DIM---- 153
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2071673385 290 larqkqlgivpqdtdltkrspgipawdsLSADDRKLYSRMMEIYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIY 364
Cdd:cd16035 154 ----------------------------FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVF 200
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
42-368 |
2.85e-11 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 65.83 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 42 ELRAKDSKVDFPRQTTAPAGA---PNILLVLLDdvGFGAAST--FGGPVD-TPTLEQLAQHGLRYNEFHTTAmcsptraa 115
Cdd:COG1368 211 EALEIKKYLKSNRPTPNPFGPakkPNVVVILLE--SFSDFFIgaLGNGKDvTPFLDSLAKESLYFGNFYSQG-------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 116 llsgrnHHSVHTgqIMEMATGYPG------YDSLVGRDTAGIGEILRQNGWNTAWFgkdH-NVPDWETsqagpFDRWPTG 188
Cdd:COG1368 281 ------GRTSRG--EFAVLTGLPPlpggspYKRPGQNNFPSLPSILKKQGYETSFF---HgGDGSFWN-----RDSFYKN 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 189 LGFEKFYgfiggDMNQWrPLLFDNTTPIEpyvgkpdynlDYDLADQAIKYVQTQhsmapDKPFFIYYAPGATHAPHHPRK 268
Cdd:COG1368 345 LGFDEFY-----DREDF-DDPFDGGWGVS----------DEDLFDKALEELEKL-----KKPFFAFLITLSNHGPYTLPE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 269 EwvDMYRGKFDQGWDVLREQTLArqkqlgivpqdtdltkrspgipawdslsaddrklYsrmmeiyagyleqTDYNVGRVI 348
Cdd:COG1368 404 E--DKKIPDYGKTTLNNYLNAVR----------------------------------Y-------------ADQALGEFI 434
|
330 340
....*....|....*....|
gi 2071673385 349 KAIDDMGLSDNTLVIyIVGD 368
Cdd:COG1368 435 EKLKKSGWYDNTIFV-IYGD 453
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-364 |
3.74e-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: 293771 [Multi-domain] Cd Length: 373 Bit Score: 64.94 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGPVD-TPTLEQLAQHGLRY-NEFHTTAMCSPTRAALLSGR--NHHSVHTGQIMEMAtgyp 138
Cdd:cd16152 2 PNVIVFFTDQQRWDTLGCYGQPLDlTPNLDALAEEGVLFeNAFTPQPVCGPARACLQTGLypTETGCFRNGIPLPA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 139 gydslvGRDTagIGEILRQNGWNTAWFGKDHnvpdwetsQAGpfdrwptglgfekfygfiggdmnqwrpllfdnttpiep 218
Cdd:cd16152 78 ------DEKT--LAHYFRDAGYETGYVGKWH--------LAG-------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 219 yvgkpdYNLDYdLADQAIKYVQTQHSmapDKPFFIYyapgATH-APHHP--RKEWV--DMYRGKFDQGWdvlreqtlarq 293
Cdd:cd16152 104 ------YRVDA-LTDFAIDYLDNRQK---DKPFFLF----LSYlEPHHQndRDRYVapEGSAERFANFW----------- 158
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2071673385 294 kqlgiVPQDTdltKRSPGIPAWDslsaddrklysrmmeiYAGYL---EQTDYNVGRVIKAIDDMGLSDNTLVIY 364
Cdd:cd16152 159 -----VPPDL---AALPGDWAEE----------------LPDYLgccERLDENVGRIRDALKELGLYDNTIIVF 208
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
63-275 |
4.33e-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: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDD-----------VGFGAASTFGGPVDTPTLEQLAQHGLRYNEFHTTAM-CSPTRAALLSGRnhHSVHTGQI 130
Cdd:cd16153 2 PNILWIITDDqrvdslscynnAHTGKSESRLGYVESPNIDALAAEGVLFTNAYCNSPvCVPSRTSMLTGR--YPHRTGVY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 131 -MEMATGYPGYDSLVgrdtagIGEILRQNGWNTAWFGKDHnvpdwetsqAGPFDRWptglgfekfygfiggdmnqwrpll 209
Cdd:cd16153 80 gFEAAHPALDHGLPT------FPEVLKKAGYQTASFGKSH---------LEAFQRY------------------------ 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2071673385 210 FDNT-TPIEPYVGKPDYNLDydladqaikyvqtqhsmaPDKPFFIYYAPGATHAPHHPRKEWVDMYR 275
Cdd:cd16153 121 LKNAnQSYKSFWGKIAKGAD------------------SDKPFFVRLSFLQPHTPVLPPKEFRDRFD 169
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
63-166 |
2.71e-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: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGPV-DTPTLEQLAQHGLRYNEFHTTAMCS--PTRAALLSGRNHHSvHTGQIMEMATGYPG 139
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPApTTPNLKRLASEGATFNFRSVSPPTSsaPNHAALLTGAYPTL-HGYTGNGSADPELP 79
|
90 100
....*....|....*....|....*....
gi 2071673385 140 YDSlVGRDTAG--IGEILRQNGWNTAWFG 166
Cdd:cd00016 80 SRA-AGKDEDGptIPELLKQAGYRTGVIG 107
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
63-368 |
3.76e-09 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 58.08 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDdvGFGAAST---FGGPVDTPTLEQLAQHGLRYNEFHTTAMCSPTRAALLSgrnhhsVHTGQIMeMATGYPG 139
Cdd:cd16015 1 PNVIVILLE--SFSDPYIdkdVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGEFE------VLTGLPP-LPLGSGS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 140 YDSLVGRDTAGIGEILRQNGWNTAWFgkdHNvpdwetSQAGpFDRWPT---GLGFEKFYGFigGDMNQwrpllfDNTTPI 216
Cdd:cd16015 72 YTLYKLNPLPSLPSILKEQGYETIFI---HG------GDAS-FYNRDSvypNLGFDEFYDL--EDFPD------DEKETN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 217 EPYVGkpdynlDYDLADQAIKYVQTQhsmaPDKPFFIYYAPGATHAPhhprkewvdmYrgkfdqgwdvlreqtlarqkql 296
Cdd:cd16015 134 GWGVS------DESLFDQALEELEEL----KKKPFFIFLVTMSNHGP----------Y---------------------- 171
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2071673385 297 givpqdtdltkrspGIPAWDSLSADDRKLYSRMMEIYAGYLEQTDYNVGRVIKAIDDMGLSDNTLVIyIVGD 368
Cdd:cd16015 172 --------------DLPEEKKDEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIV-IYGD 228
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
63-364 |
7.68e-08 |
|
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: 54.12 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDDVGFGAASTFGGP-VDTPTLEQLAQHGLRYNEFHTTA-MCSPTRAALLSGRnhhsvhtgqiMEMATGypGY 140
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTvVKTPNLDRLAARGVVFDNAYCNSpLCAPSRASMMTGR----------LPSRIG--AY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 141 D--SLVGRDTAGIGEILRQNGWNTAWFGKDHNVpdwetsqaGPfdrwptglgfEKFYGFiggdmnqwrpllfdnttpiep 218
Cdd:cd16032 69 DnaAEFPADIPTFAHYLRAAGYRTALSGKMHFV--------GP----------DQLHGF--------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 219 yvgkpDYnlDYDLADQAIKYVqTQHSM-APDKPFFI---YYAPgatHAPHHPRKEWVDMYrgkfdqgwdVLReqtlARQK 294
Cdd:cd16032 110 -----DY--DEEVAFKAVQKL-YDLARgEDGRPFFLtvsFTHP---HDPYVIPQEYWDLY---------VRR----ARRA 165
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 295 QLGIVpqdtdltkrspgipawdslSADDRKlysrmmeiyagyleqtdynVGRVIKAIDDMGLSDNTLVIY 364
Cdd:cd16032 166 YYGMV-------------------SYVDDK-------------------VGQLLDTLERTGLADDTIVIF 197
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
63-167 |
2.47e-03 |
|
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: 40.22 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071673385 63 PNILLVLLDdvGFGAASTF---GGPVDTPTLEQLAQHGLRY-NEFHTTAMCSPTRAALLSGRNHHsvhtgqIMEMATGYP 138
Cdd:cd16171 1 PNVVMVMSD--SFDGRLTFrpgNQVVDLPYINFMKQHGSVFlNAYTNSPICCPSRAAMWSGLFTH------LTESWNNYK 72
|
90 100
....*....|....*....|....*....
gi 2071673385 139 GYDSlvgrDTAGIGEILRQNGWNTAWFGK 167
Cdd:cd16171 73 GLDP----NYPTWMDRLEKHGYHTQKYGK 97
|
|
| |
