|
Name |
Accession |
Description |
Interval |
E-value |
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
28-436 |
0e+00 |
|
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: 550.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPNLCTPSRATLLTGKYPIHTGMQHFVIITDEPWGLP 107
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEPYGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 108 QRERLMPEIFRDAGYSTHLVGKWHLGFWRKDLTPTMRGFDHHFGYYNGYIDYYDHQVRMLDRNYsaGLDFRRDLEPCPEA 187
Cdd:cd16029 81 LNETLLPQYLKELGYATHLVGKWHLGFYTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGGANDYG--NDDLRDNEEPAWDY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 188 NGTYATEAFTSEAKRIIEQHDKSKPLFMVLSHLAVHTGNEDSPMQAPEEEVaKFPHIRDPKRRTYAGMISSLDKSVAQTI 267
Cdd:cd16029 159 NGTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPYED-KFAHIKDEDRRTYAAMVSALDESVGNVV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 268 GALKDNGMLNNSIILLYSDNGAPTIGIHsnAGSNYPYRGQKESPWEGGIRSAGALWSPLLKE-RGYVSNQAIHAVDWLPT 346
Cdd:cd16029 238 DALKAKGMLDNTLIVFTSDNGGPTGGGD--GGSNYPLRGGKNTLWEGGVRVPAFVWSPLLPPkRGTVSDGLMHVTDWLPT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 347 LAGAAGVSLPQDLPLDGINLWPMLSGNEEPKPRTMIHVLDEVF---GYSSYMRDTLKYVNGssfkgrydQWLGELetnED 423
Cdd:cd16029 316 LLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNIDDITrttGGAAIRVGDWKLIVG--------KPLFNI---EN 384
|
410
....*....|...
gi 24666175 424 DPlgesYEQHVLA 436
Cdd:cd16029 385 DP----CERNDLA 393
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
27-383 |
7.97e-100 |
|
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: 308.34 E-value: 7.97e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 27 KPNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVP-NLCTPSRATLLTGKYPIHTGMQHFVIITDEPWG 105
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAaPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 106 LPQRERLMPEIFRDAGYSTHLVGKWHLGfWRKDLTPTMRGFDHHFG--------YYNGYIDYYDHQVRMLDRNYSagldf 177
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLG-HQPEFLPTRHGFDEYFGipysndmwPFPLYRNDPPGPLPPLMENEE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 178 rrdlEPCPEANGTYATEAFTSEAKRIIEQHDKsKPLFMVLSHLAVHTgnedsPMQAPEeevaKFphiRDPKRR-TYAGMI 256
Cdd:cd16026 155 ----VIEQPADQSSLTQRYTDEAVDFIERNKD-QPFFLYLAHTMPHV-----PLFASE----KF---KGRSGAgLYGDVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 257 SSLDKSVAQTIGALKDNGMLNNSIILLYSDNGaPTIGIHSNAGSNYPYRGQKESPWEGGIRSAGALWSPLLKERGYVSNQ 336
Cdd:cd16026 218 EELDWSVGRILDALKELGLEENTLVIFTSDNG-PWLEYGGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDE 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24666175 337 AIHAVDWLPTLAGAAGVSLPQDLPLDGINLWPMLSGNEEPKPRTMIH 383
Cdd:cd16026 297 LASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFY 343
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-379 |
8.85e-96 |
|
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: 298.69 E-value: 8.85e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTGMQHFV--------- 97
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAApVCSPSRASILTGQYPARLGITDVIpgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 98 ---IITDEPWGLPQRERLMPEIFRDAGYSTHLVGKWHLGFwRKDLTPTMRGFDHHFGYYNGYIDYYdhqvrmldrNYSAG 174
Cdd:cd16144 81 tklIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGG-EGGYGPEDQGFDVNIGGTGNGGPPS---------YYFPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 175 LDFRRDLEPCPEanGTYATEAFTSEAKRIIEQHdKSKPLFMVLSHLAVHTgnedsPMQAPEEEVAKFPHIRDPKRR---- 250
Cdd:cd16144 151 GKPNPDLEDGPE--GEYLTDRLTDEAIDFIEQN-KDKPFFLYLSHYAVHT-----PIQARPELIEKYEKKKKGLRKgqkn 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 251 -TYAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGApTIGIHSNAGSNYPYRGQKESPWEGGIRsagalwSPLL-- 327
Cdd:cd16144 223 pVYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNGG-LSTRGGPPTSNAPLRGGKGSLYEGGIR------VPLIvr 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 24666175 328 ----KERGYVSNQAIHAVDWLPTLAGAAGVSLPQDLPLDGINLWPMLSGNEEPKPR 379
Cdd:cd16144 296 wpgvIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPR 351
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-521 |
3.77e-94 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 293.71 E-value: 3.77e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 1 MTSGKILVLLVVSSILSLAYgsgySTKPNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSR 79
Cdd:COG3119 1 MKRLLLLLLALLAAAAAAAA----AKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSpVCSPSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 80 ATLLTGKYPIHTGMQHfvIITDEPWGLPQRERLMPEIFRDAGYSTHLVGKWHLgfwrkdltptmrgfdhhfgyyngyidy 159
Cdd:COG3119 77 ASLLTGRYPHRTGVTD--NGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 160 ydhqvrmldrnysagldfrrdlepcpeangtYATEAFTSEAKRIIEQH-DKSKPLFMVLSHLAVHTgnedsPMQAPEEEV 238
Cdd:COG3119 128 -------------------------------YLTDLLTDKAIDFLERQaDKDKPFFLYLAFNAPHA-----PYQAPEEYL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 239 AKF-----------------PHIRDPKRRTYAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGaPTIGIHSnagsn 301
Cdd:COG3119 172 DKYdgkdiplppnlaprdltEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNG-PSLGEHG----- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 302 ypYRGQKESPWEGGIRSAGALWSPLLKERGYVSNQAIHAVDWLPTLAGAAGVSLPQDlpLDGINLWPMLSGNEEPKPRTM 381
Cdd:COG3119 246 --LRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYL 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 382 IHVLDEVFGYSSYMRDTLKYVngssfkgRYDQWLGELEtneddplgesyeqhvlasdvqsllgnrgltkdrirqmrseat 461
Cdd:COG3119 322 YWEYPRGGGNRAIRTGRWKLI-------RYYDDDGPWE------------------------------------------ 352
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 462 etcppiegqnpleshfkceplkapcFFDLAKDPCERYNLAQMYPLQLQQLADELEQIRKT 521
Cdd:COG3119 353 -------------------------LYDLKNDPGETNNLAADYPEVVAELRALLEAWLKE 387
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
28-442 |
2.90e-83 |
|
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: 265.95 E-value: 2.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPNLCTPSRATLLTGKYPIHTGmqhfviITDEPWGlp 107
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTG------VWHTILG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 108 qRERL------MPEIFRDAGYSTHLVGKWHLGFwRKDLTPTMRGFDHHFGYYNGYI-DYYDHqvrmLDRNYSAGLDFRrd 180
Cdd:cd16146 73 -RERMrldettLAEVFKDAGYRTGIFGKWHLGD-NYPYRPQDRGFDEVLGHGGGGIgQYPDY----WGNDYFDDTYYH-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 181 lepcpeaNGT------YATEAFTSEAKRIIEQHdKSKPLFMVLSHLAVHtgnedSPMQAPEEEVAKFPHIR-DPKRRTYA 253
Cdd:cd16146 145 -------NGKfvktegYCTDVFFDEAIDFIEEN-KDKPFFAYLATNAPH-----GPLQVPDKYLDPYKDMGlDDKLAAFY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 254 GMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGaPTIGIHS--NAGsnypYRGQKESPWEGGIRSAGALWSPLLKERG 331
Cdd:cd16146 212 GMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNG-PAGGVPKrfNAG----MRGKKGSVYEGGHRVPFFIRWPGKILAG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 332 YVSNQAIHAVDWLPTLAGAAGVSLPQDLPLDGINLWPMLSGNEEPKPRTMI--H-----VLDEVFGYSSYMRDTLKYVNG 404
Cdd:cd16146 287 KDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLftHsgrwpPPPKKKRNAAVRTGRWRLVSP 366
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 24666175 405 SSFKGR-YDQwlgeletnEDDPlgesYEQHVLASD----VQSL 442
Cdd:cd16146 367 KGFQPElYDI--------ENDP----GEENDVADEhpevVKRL 397
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-379 |
3.54e-75 |
|
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: 244.81 E-value: 3.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKypiHTGmqHFVII----TDE 102
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGApVCAPSRASLLTGL---HTG--HTRVRgnsePGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 103 PWGLPQRERLMPEIFRDAGYSTHLVGKWHLGFWRKDLTPTMRGFDHHFGYY------NGYIDYYDH--QVRMLDRNYSAG 174
Cdd:cd16145 76 QDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHPTKQGFDYFYGYLdqvhahNYYPEYLWRngEKVPLPNNVIPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 175 LDFRRDLEPcpeANGTYATEAFTSEAKRIIEQHdKSKPLFMVLSHLAVHtgnedSPMQAPEEEVAKFPHIRDP------- 247
Cdd:cd16145 156 LDEGNNAGG---GGGTYSHDLFTDEALDFIREN-KDKPFFLYLAYTLPH-----APLQVPDDGPYKYKPKDPGiyaylpw 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 248 --KRRTYAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGAptigiHSNAG---------SNYPYRGQKESPWEGGI 316
Cdd:cd16145 227 pqPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGP-----HSEGGsehdpdffdSNGPLRGYKRSLYEGGI 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24666175 317 RSAGALWSPLLKERGYVSNQAIHAVDWLPTLAGAAGVSLPQDlpLDGINLWPMLSGNEEPKPR 379
Cdd:cd16145 302 RVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQH 362
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
28-365 |
2.49e-72 |
|
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: 231.56 E-value: 2.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTGMQHFViitDEPWGL 106
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASpVCSPSRASLLTGRYPHRHGVRGNV---GNGGGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 107 PQRERLMPEIFRDAGYSTHLVGKWHlgfwrkdltptmrgfdhhfgyyngyidyydhqvrmldrnysagldfrrdlepcpe 186
Cdd:cd16022 78 PPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 187 angtyateaftSEAKRIIEQHDKSKPLFMVLSHLAVHTgnedsPMqapeeevakfphirdpkrrTYAGMISSLDKSVAQT 266
Cdd:cd16022 103 -----------DEAIDFIERRDKDKPFFLYVSFNAPHP-----PF-------------------AYYAMVSAIDDQIGRI 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 267 IGALKDNGMLNNSIILLYSDNGAPTiGIHSNagsnypyRGQKESPWEGGIRSAGALWSPLLKERGYVSNQAIHAVDWLPT 346
Cdd:cd16022 148 LDALEELGLLDNTLIVFTSDHGDML-GDHGL-------RGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPT 219
|
330
....*....|....*....
gi 24666175 347 LAGAAGVSLPQdlPLDGIN 365
Cdd:cd16022 220 LLDLAGIEPPE--GLDGRS 236
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-414 |
1.30e-70 |
|
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: 231.65 E-value: 1.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQIL---TPNIDALAYNGILLNKHYVPNLCTPSRATLLTGKYPIHTGMqHFVIITDEPW 104
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGL-TTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 105 GLPQRERLMPEIFRDAGYSTHLVGKWHLGFwRKDLTPTMRGFDHHFGYYNGYIDyydhqvrmlDRNYSAGLDFrrdlepc 184
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGD-EDGRLPTDHGFDEFYGNLYHTID---------EEIVDKAIDF------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 185 peangtyateaftseakriIEQHDKS-KPLFMVLSHLAVHTGNEDSPmqapeeevaKFPHiRDPKRRTYAGMISSLDKSV 263
Cdd:cd16142 143 -------------------IKRNAKAdKPFFLYVNFTKMHFPTLPSP---------EFEG-KSSGKGKYADSMVELDDHV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 264 AQTIGALKDNGMLNNSIILLYSDNGAptiGIHSNAGSNY-PYRGQKESPWEGGIRSAGALWSPLLKERGYVSNQAIHAVD 342
Cdd:cd16142 194 GQILDALDELGIADNTIVIFTTDNGP---EQDVWPDGGYtPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLD 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666175 343 WLPTLAGAAGVSLP------QDLPLDGINLWPMLSGNEEPKPRtmihvlDEVFgyssymrdtlkYVNGSSFKG-RYDQW 414
Cdd:cd16142 271 WFPTLAALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRR------SEFF-----------YFGEGELGAvRWKNW 332
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
26-414 |
1.31e-68 |
|
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: 227.33 E-value: 1.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 26 TKPNIVIILIDDMGMNDVSFHGSnQILTPNIDALAYNGILLNKHYVPNLCTPSRATLLTGKYPIHTGMQHFV-IITDEPW 104
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGG-EIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTMAeLATGKPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 105 G---LPQRERLMPEIFRDAGYSTHLVGKWHLGFwrkdltptmrgfdhhfgyyNGYidyydhqvrmldrnysagldfrrdl 181
Cdd:cd16025 80 YegyLPDSAATIAEVLKDAGYHTYMSGKWHLGP-------------------DDY------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 182 epcpeangtYATEAFTSEAKRII-EQHDKSKPLFMVLSHLAVHtgnedSPMQAPEEEVAKF------------------- 241
Cdd:cd16025 116 ---------YSTDDLTDKAIEYIdEQKAPDKPFFLYLAFGAPH-----APLQAPKEWIDKYkgkydagwdalreerlerq 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 242 ----------------PHIR-----DPKRR--------TYAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGA-PT 291
Cdd:cd16025 182 kelglipadtkltprpPGVPawdslSPEEKklearrmeVYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGAsAE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 292 IGIhSNAgSNYPYRGQKESPWEGGIRSAGALWSP-LLKERGYVSNQAIHAVDWLPTLAGAAGVSLPQD------LPLDGI 364
Cdd:cd16025 262 PGW-ANA-SNTPFRLYKQASHEGGIRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTvngvpqLPLDGV 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 24666175 365 NLWPMLSGNEEPKPRTMIHVldEVFGYSSYMRDTLKYVNGSSFKGRYDQW 414
Cdd:cd16025 340 SLLPTLDGAAAPSRRRTQYF--ELFGNRAIRKGGWKAVALHPPPGWGDQW 387
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
27-524 |
1.10e-62 |
|
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: 213.48 E-value: 1.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 27 KPNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTG-------MQHFVI 98
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANpLCSPSRAALLTGRLPIRNGfyttnahARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 99 ITDEPWGLPQRERLMPEIFRDAGYSTHLVGKWHLGFwRKDLTPTMRGFDHHFGYYNGYIDYYDHQVR----------MLD 168
Cdd:cd16157 81 PQNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLGH-RPQYHPLKHGFDEWFGAPNCHFGPYDNKAYpnipvyrdweMIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 169 RNYSaglDFRRDLEPcPEANgtyATEAFTSEAKRIIE-QHDKSKPLFMVLSHLAVHTgnedsPMQAPEeevakfPHIRDP 247
Cdd:cd16157 160 RYYE---EFKIDKKT-GESN---LTQIYLQEALEFIEkQHDAQKPFFLYWAPDATHA-----PVYASK------PFLGTS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 248 KRRTYAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGAPTIGIHSNAGSNYPYRGQKESPWEGGIRSAGALWSPLL 327
Cdd:cd16157 222 QRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALISAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGH 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 328 KERGYVSNQAIHAVDWLPTLAGAAGVSLPQDLPLDGINLWPMLSGNEEpKPRTMIHvldevfgyssYMRDTLKYVNGSSF 407
Cdd:cd16157 302 IKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKE-KDRPIFY----------YRGDELMAVRLGQY 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 408 KGRYDQWLGeletneddplgesyeqhvlasdvqsllgnrglTKDRIRQmrseATETCPpieGQN--PLESHFKCEPLKAP 485
Cdd:cd16157 371 KAHFWTWSN--------------------------------SWEEFRK----GINFCP---GQNvpGVTTHNQTDHTKLP 411
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24666175 486 CFFDLAKDPCERYNLAQM---YPLQLQQLADELEQIRKTAIP 524
Cdd:cd16157 412 LLFHLGRDPGEKYPISFKsaeYKQAMPRISKVVQQHQKTLVP 453
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
28-353 |
2.46e-62 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 207.66 E-value: 2.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVP-NLCTPSRATLLTGKYPIHTGMQHFViitdePWGL 106
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGgTLTAPSRFALLTGLPPHNFGSYVST-----PVGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 107 PQRERLMPEIFRDAGYSTHLVGKWHLGFWRKDlTPTMRGFDHHFGYYNGYIDYYDhqvrmldrnysagldfRRDLEPCPE 186
Cdd:pfam00884 76 PRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQ-SPCNLGFDKFFGRNTGSDLYAD----------------PPDVPYNCS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 187 aNGTYATEAFTSEAKRIIEQHDksKPLFMVLSHLAVHTGNEDSpmQAPEEEVAKFPHIRDPKRR---TYAGMISSLDKSV 263
Cdd:pfam00884 139 -GGGVSDEALLDEALEFLDNND--KPFFLVLHTLGSHGPPYYP--DRYPEKYATFKPSSCSEEQllnSYDNTLLYTDDAI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 264 AQTIGALKDNGMLNNSIILLYSDNGAptigiHSNAGSNYPYRGQKESPWEGGIRSAGALWSPLLKERGYVSNQAIHAVDW 343
Cdd:pfam00884 214 GRVLDKLEENGLLDNTLVVYTSDHGE-----SLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDL 288
|
330
....*....|
gi 24666175 344 LPTLAGAAGV 353
Cdd:pfam00884 289 FPTILDLAGI 298
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-382 |
2.60e-62 |
|
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: 209.76 E-value: 2.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPNLCTPSRATLLTGKYPIHTGMQHFViitdepwgLP 107
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVFGY--------LD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 108 QRERLMPEIFRDAGYSTHLVGKWHLGFWRKDL-TPTMRGFDHHFGY-YNGYIDYYDHqvRMLDRNYSagldfrRDLEPCP 185
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGdYPHEFGFDEYCLWqLTETGEKYSR--PATPTFNI------RNGKLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 186 EANGTYATEAFTSEAKRIIEQHdKSKPLF----MVLSHlAVHTGNEDSPMQAPEEEVAKfphiRDPKRrtYAGMISSLDK 261
Cdd:cd16151 145 TTEGDYGPDLFADFLIDFIERN-KDQPFFayypMVLVH-DPFVPTPDSPDWDPDDKRKK----DDPEY--FPDMVAYMDK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 262 SVAQTIGALKDNGMLNNSIILLYSDNG-APTIGIHSNAGsnyPYRGQKESPWEGGIRSAGALWSPLLKERGYVSNQAIHA 340
Cdd:cd16151 217 LVGKLVDKLEELGLRENTIIIFTGDNGtHRPITSRTNGR---EVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDF 293
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 24666175 341 VDWLPTLAGAAGVSLPQDLPLDGINLWPMLSGnEEPKPRTMI 382
Cdd:cd16151 294 SDFLPTLAELAGAPLPEDYPLDGRSFAPQLLG-KTGSPRREW 334
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-383 |
1.96e-61 |
|
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: 208.21 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVS-FHGSNQILTPNIDALAYNGILLNKHYVP-NLCTPSRATLLTGKYPIHTGMQHFVIITDEPWG 105
Cdd:cd16143 1 PNIVIILADDLGYGDIScYNPDSKIPTPNIDRLAAEGMRFTDAHSPsSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 106 LPQRERLMPEIFRDAGYSTHLVGKWHLGF-WRK--------------DLT------PTMRGFDHHFGYyngyidyydhqv 164
Cdd:cd16143 81 IEPDRVTLAKMLKQAGYRTAMVGKWHLGLdWKKkdgkkaatgtgkdvDYSkpikggPLDHGFDYYFGI------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 165 rmldrnysagldfrrdlePCPEANGTyateaFTSEAKRIIEQH-DKSKPLFMVLSHLAVHTgnedsPMQAPEEEVAKfph 243
Cdd:cd16143 149 ------------------PASEVLPT-----LTDKAVEFIDQHaKKDKPFFLYFALPAPHT-----PIVPSPEFQGK--- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 244 irdPKRRTYAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGA---PTIGIHSNAG--SNYPYRGQKESPWEGGIRS 318
Cdd:cd16143 198 ---SGAGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPspyADYKELEKFGhdPSGPLRGMKADIYEGGHRV 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24666175 319 AGALWSPLLKERGYVSNQAIHAVDWLPTLAGAAGVSLPQDLPLDGINLWPMLSGNEEPKPR-TMIH 383
Cdd:cd16143 275 PFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVReSLVH 340
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
27-383 |
7.65e-58 |
|
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: 198.46 E-value: 7.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 27 KPNIVIILIDDMGMNDVSFHGS-NQILTPNIDALAYNGI-LLNKHYVPNLCTPSRATLLTGKYPIHTGMQHFVIITDEPw 104
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTrFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 105 GLPQRERLMPEIFRDAGYSTHLVGKWHLGFwRKDLTPTMRGFDHHFGyyngyidyydhqvrmldrnysagldfrrdlepC 184
Cdd:cd16161 80 GLPLNETTLAEVLRQAGYATGMIGKWHLGQ-REAYLPNSRGFDYYFG--------------------------------I 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 185 PEANGTYATEAFTSEAKRIIEQH-DKSKPLFMVLSHLAVHTGNEDSPMqapeeevakfPHIRDPKRRTYAGMISSLDKSV 263
Cdd:cd16161 127 PFSHDSSLADRYAQFATDFIQRAsAKDRPFFLYAALAHVHVPLANLPR----------FQSPTSGRGPYGDALQEMDDLV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 264 AQTIGALKDNGMLNNSIILLYSDNGAPTIGIHSNAG-------SNYPYRGQKESPWEGGIRSAGALWSPLLKERGYVSNQ 336
Cdd:cd16161 197 GQIMDAVKHAGLKDNTLTWFTSDNGPWEVKCELAVGpgtgdwqGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAA 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24666175 337 AIHAVDWLPTLAGAAGVSLPQDLPLDGINLWPMLSGNEEPKPRTMIH 383
Cdd:cd16161 277 LVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFH 323
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
28-517 |
2.07e-56 |
|
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: 194.26 E-value: 2.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGsNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTGMQHFviiTDEPWGL 106
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGG-NVVKTPNLDRLAAEGVRFTNAFTTApVCSPSRSALLTGLYPHQNGAHGL---RSRGFPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 107 PQRERLMPEIFRDAGYSTHLVGKWHLGFWRKDltptmrgfdhhfgYYNGYIDYYDHQVRMLDRNYSAGLDFRrdlepcpe 186
Cdd:cd16027 77 PDGVKTLPELLREAGYYTGLIGKTHYNPDAVF-------------PFDDEMRGPDDGGRNAWDYASNAADFL-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 187 angtyateaftseakriiEQHDKSKPLFMVL----SHLAVHTGNEDSPMQAPEE-EVAKF----PHIRDpKRRTYAGMIS 257
Cdd:cd16027 136 ------------------NRAKKGQPFFLWFgfhdPHRPYPPGDGEEPGYDPEKvKVPPYlpdtPEVRE-DLADYYDEIE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 258 SLDKSVAQTIGALKDNGMLNNSIILLYSDNGAPtigihsnagsnYPyRGqKESPWEGGIRSAGALWSPLLKERGYVSNQA 337
Cdd:cd16027 197 RLDQQVGEILDELEEDGLLDNTIVIFTSDHGMP-----------FP-RA-KGTLYDSGLRVPLIVRWPGKIKPGSVSDAL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 338 IHAVDWLPTLAGAAGVSLPQDlpLDGINLWPMLSGNEEPKPrtmihvlDEVFGYSSYMrdtlkyvngssfkgrydqwlge 417
Cdd:cd16027 264 VSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGR-------DYVFAERDRH---------------------- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 418 letneddplGESYEQhvlasdvqsllgNRGLTKDR---IRQMRSEAtetcppiegqnpleshfkceplkapcFFDLAKDP 494
Cdd:cd16027 313 ---------DETYDP------------IRSVRTGRykyIRNYMPEE--------------------------LYDLKNDP 345
|
490 500
....*....|....*....|....*
gi 24666175 495 CERYNLAQMYPLQ--LQQLADELEQ 517
Cdd:cd16027 346 DELNNLADDPEYAevLEELRAALDA 370
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
27-383 |
2.40e-56 |
|
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: 197.90 E-value: 2.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 27 KPNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTGMQHF----VII-T 100
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAApLCTPSRAAFLTGRYPIRSGMASShgmrVILfT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 101 DEPWGLPQRERLMPEIFRDAGYSTHLVGKWHLGFWRKDLT-----PTMRGFDHHFGY-----------YNGYIDY----- 159
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNdfchhPLNHGFDYFYGLpltnlkdcgdgSNGEYDLsfdpl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 160 ---------------------------------------------YDHQVRMLD----RNYsagldfrrDLEPCPeANGT 190
Cdd:cd16159 161 fplltafvlitaltiflllylgavskrffvfllilsllfislfflLLITNRYFNcilmRNH--------EVVEQP-MSLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 191 YATEAFTSEAKRIIEQHdKSKPLFMVLSHLAVHTgnedsPMQAPEEEVAKFPHIRdpkrrtYAGMISSLDKSVAQTIGAL 270
Cdd:cd16159 232 NLTQRLTKEAISFLERN-KERPFLLVMSFLHVHT-----ALFTSKKFKGRSKHGR------YGDNVEEMDWSVGQILDAL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 271 KDNGMLNNSIILLYSDNGAP----TIGIHSNAGSNYPYRGQKESPWEGGIRSAGALWSPLLKERGYVSNQAIHAVDWLPT 346
Cdd:cd16159 300 DELGLKDNTFVYFTSDNGGHleeiSVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPT 379
|
410 420 430
....*....|....*....|....*....|....*...
gi 24666175 347 LAGAAGVSLPQDLPLDGINLWPMLSGNEE-PKPRTMIH 383
Cdd:cd16159 380 VAALAGAPLPSDRIIDGRDLMPLLTGQEKrSPHEFLFH 417
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
27-411 |
3.25e-56 |
|
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: 195.73 E-value: 3.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 27 KPNIVIILIDDMGMNDVSFHG-SNQILTPnIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTGM--QHFVIITDE 102
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGhPTQERGP-IDDMAAEGIRFTQAYSADsVCTPSRAALLTGRLPIRSGMygGTRVFLPWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 103 PWGLPQRERLMPEIFRDAGYSTHLVGKWHLGFWRKDLT-----PTMRGFD---HHFGYYNGYI-DyyDHQVRMLDRNYSA 173
Cdd:cd16160 80 IGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSdgahlPSHHGFDfvgTNLPFTNSWAcD--DTGRHVDFPDRSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 174 GLDFRRDLEPCPEANGTYATEAFTSEAKRIIEQHDKsKPLFMVLSHLAVHTgnedsPMQAPEEEVAKfphirdPKRRTYA 253
Cdd:cd16160 158 CFLYYNDTIVEQPIQHEHLTETLVGDAKSFIEDNQE-NPFFLYFSFPQTHT-----PLFASKRFKGK------SKRGRYG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 254 GMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGaPTIGIHSNAGSNYPYRGQKESPWEGGIR-SAGALWSPLLKERgy 332
Cdd:cd16160 226 DNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHG-PHVEYCLEGGSTGGLKGGKGNSWEGGIRvPFIAYWPGTIKPR-- 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666175 333 VSNQAIHAVDWLPTLAGAAGVSLPQDLPLDGINLWPMLSGNEEPKPRTMIHvldevfgyssYMRDTLKYVNGSSFKGRY 411
Cdd:cd16160 303 VSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDILY----------YCCSRLMAVRYGSYKIHF 371
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
27-459 |
8.22e-55 |
|
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: 191.59 E-value: 8.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 27 KPNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTGMQHFVIITDEPWg 105
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTsICAPSRASILTGQYSHRHGVTDNNGPLFDAS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 106 lpqrERLMPEIFRDAGYSTHLVGKWHLGFwRKDLTPTmrGFDHHFGYYnGYIDYYDhqvrmLDRNYSAGLDFRRDlepcp 185
Cdd:cd16031 81 ----QPTYPKLLRKAGYQTAFIGKWHLGS-GGDLPPP--GFDYWVSFP-GQGSYYD-----PEFIENGKRVGQKG----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 186 eangtYATEAFTSEAKRIIEQHDKSKPLFMVLSHLAVHTGNEDSPMQAPEEEVAKFP----------------------- 242
Cdd:cd16031 143 -----YVTDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPepetfddddyagrpewareqrnr 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 243 -HIRDPKR-----------RTYAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGApTIGIHSNAGsnypyrgqKES 310
Cdd:cd16031 218 iRGVLDGRfdtpekyqrymKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGF-FLGEHGLFD--------KRL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 311 PWEGGIRsagalwSPLL------KERGYVSNQAIHAVDWLPTLAGAAGVSLPQDlpLDGINLWPMLSGNEEPKPRTMihV 384
Cdd:cd16031 289 MYEESIR------VPLIirdprlIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDWRKE--F 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 385 LDEVFGYSSYM---------RDTLKYVNgssFKGRYDQWlgELETNEDDPlgesYEQHVLASDVQsllgnrglTKDRIRQ 455
Cdd:cd16031 359 YYEYYEEPNFHnvpthegvrTERYKYIY---YYGVWDEE--ELYDLKKDP----LELNNLANDPE--------YAEVLKE 421
|
....
gi 24666175 456 MRSE 459
Cdd:cd16031 422 LRKR 425
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-379 |
3.48e-54 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 188.93 E-value: 3.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 27 KPNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHY--VPnLCTPSRATLLTGKYPIHTGMQHfviitdEPW 104
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVsnYP-VCSPYRASLLTGQYPLTNGVFG------NDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 105 GLPQRERLMPEIFRDAGYSTHLVGKWHLGFWRKDL--------TPTMR-GFDHHFGYYNgyidYYDHQVRMLDRNysagl 175
Cdd:cd16034 74 PLPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDgraddytpPPERRhGFDYWKGYEC----NHDHNNPHYYDD----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 176 dfrrdlEPCPEANGTYATEAFTSEAKRIIEQH-DKSKPLFMVLSHLAVHTGNEdspmQAPEEEVAKFPH----------- 243
Cdd:cd16034 145 ------DGKRIYIKGYSPDAETDLAIEYLENQaDKDKPFALVLSWNPPHDPYT----TAPEEYLDMYDPkklllrpnvpe 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 244 ---IRDPKRRTYAG---MISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGApTIGIHSNAGSNYPYRgqkES---P--- 311
Cdd:cd16034 215 dkkEEAGLREDLRGyyaMITALDDNIGRLLDALKELGLLENTIVVFTSDHGD-MLGSHGLMNKQVPYE---ESirvPfii 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666175 312 -WEGGIRSAGalwspllkergyVSNQAIHAVDWLPTLAGAAGVSLPQDlpLDGINLWPMLSGNEEPKPR 379
Cdd:cd16034 291 rYPGKIKAGR------------VVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPD 345
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
27-519 |
1.58e-48 |
|
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: 175.71 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 27 KPNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTGMQHFVIITDEPWG 105
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSpVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 106 LPQRERLMPEIFRDAGYSTHLVGKWHLGF-WRKDLTPTMRGFDHHFGyyngyIDYYDHQVRMLDR-----NYSAGLDFRR 179
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLGVgLNGTYLPTHQGFDHYLG-----IPYSHDQGPCQNLtcfppNIPCFGGCDQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 180 DLEPCP----------EANGTYATEAFTSEAKRIIEQHDK-SKPLFMVLSHLAVHtgnedSPMQAPEEEVAKFPhirdpk 248
Cdd:cd16158 156 GEVPCPlfynesivqqPVDLLTLEERYAKFAKDFIADNAKeGKPFFLYYASHHTH-----YPQFAGQKFAGRSS------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 249 RRTYAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGaPTIGIHSNAGSNYPYRGQKESPWEGGIRSAG-ALWSPLL 327
Cdd:cd16158 225 RGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNG-PSTMRKSRGGNAGLLKCGKGTTYEGGVREPAiAYWPGRI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 328 KERgyVSNQAIHAVDWLPTLAGAAGVSLPqDLPLDGINLWPMLSgNEEPKPRtmihvlDEVFGYSSYMRdtlkyVNGSSF 407
Cdd:cd16158 304 KPG--VTHELASTLDILPTIAKLAGAPLP-NVTLDGVDMSPILF-EQGKSPR------QTFFYYPTSPD-----PDKGVF 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 408 KGRYDQWLGELetneddplgesYEQHVLASDvqsllgnrgltkdrirqmrSEATETCPPIEgqnPLESHfkcEPlkaPCF 487
Cdd:cd16158 369 AVRWGKYKAHF-----------YTQGAAHSG-------------------TTPDKDCHPSA---ELTSH---DP---PLL 409
|
490 500 510
....*....|....*....|....*....|..
gi 24666175 488 FDLAKDPCERYNLAQmyPLQLQQLADELEQIR 519
Cdd:cd16158 410 FDLSQDPSENYNLLG--LPEYNQVLKQIQQVK 439
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-389 |
1.15e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 154.31 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 27 KPNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTGMQHFVIitdepwG 105
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQpVCGPARACLQTGLYPTETGCFRNGI------P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 106 LPQRERLMPEIFRDAGYSTHLVGKWHLgfwrkdltptmrgfdhhfgyyngyidyydhqvrmldrnysAGldfrrdlepcp 185
Cdd:cd16152 75 LPADEKTLAHYFRDAGYETGYVGKWHL----------------------------------------AG----------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 186 eangtYATEAFTSEAKRIIEQHDKSKPLFMVLSHLAVHTGNEDSPMQAPE---EEVAKFPHIRDPKRRT---------YA 253
Cdd:cd16152 104 -----YRVDALTDFAIDYLDNRQKDKPFFLFLSYLEPHHQNDRDRYVAPEgsaERFANFWVPPDLAALPgdwaeelpdYL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 254 GMISSLDKSVAQTIGALKDNGMLNNSIILLYSDngaptigiHsnaGSNYPYRGQ--KESPWEGGIRsagalwSPLLK--- 328
Cdd:cd16152 179 GCCERLDENVGRIRDALKELGLYDNTIIVFTSD--------H---GCHFRTRNAeyKRSCHESSIR------VPLVIygp 241
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24666175 329 --ERGYVSNQAIHAVDWLPTLAGAAGVSLPQDlpLDGINLWPMLSGNEEPKPrtmihvlDEVF 389
Cdd:cd16152 242 gfNGGGRVEELVSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWR-------NEVF 295
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
25-459 |
2.31e-41 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 155.98 E-value: 2.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 25 STKPNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHY--VPNlCTPSRATLLTGKYPIHTGMqhfVIITDE 102
Cdd:PRK13759 4 TKKPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYsaVPS-CTPARAALLTGLSQWHHGR---VGYGDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 103 -PWGLPQRerlMPEIFRDAGYSTHLVGKWHLGFWRKDLtptmrGFDH---HFGYYNG----------YIDYYDHQVRMLD 168
Cdd:PRK13759 80 vPWNYKNT---LPQEFRDAGYYTQCIGKMHVFPQRNLL-----GFHNvllHDGYLHSgrnedksqfdFVSDYLAWLREKA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 169 RNYSAGL------DFRRDLEPCPEANGTYATEAFTSEAKRIIEQHDKSKPLFMVLSHLAVHtgnedSPMQAP-------E 235
Cdd:PRK13759 152 PGKDPDLtdigwdCNSWVARPWDLEERLHPTNWVGSESIEFLRRRDPTKPFFLKMSFARPH-----SPYDPPkryfdmyK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 236 EEVAKFPHIRDPK---------------------------RRTYAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNG 288
Cdd:PRK13759 227 DADIPDPHIGDWEyaedqdpeggsidalrgnlgeeyarraRAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 289 aPTIGIHSNAGSNYPYRGQKESP----WEGGIRSAGalwspllkeRGYVSNQAIHAVDWLPTLAGAAGVSLPQDlpLDGI 364
Cdd:PRK13759 307 -DMLGDHYLFRKGYPYEGSAHIPfiiyDPGGLLAGN---------RGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 365 NLWPMLSGNeEPKPRTMIHvLDEVFGYSS--YMRD-TLKYVNGSSfKGRYdqwlgELETNEDDPlgesYEQHVLASDVQS 441
Cdd:PRK13759 375 SLKNLIFGQ-YEGWRPYLH-GEHALGYSSdnYLTDgKWKYIWFSQ-TGEE-----QLFDLKKDP----HELHNLSPSEKY 442
|
490
....*....|....*...
gi 24666175 442 llgnrgltKDRIRQMRSE 459
Cdd:PRK13759 443 --------QPRLREMRKK 452
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-372 |
5.87e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 138.25 E-value: 5.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFH--GSNQILTPNIDALAYNGILLNKHYVPNLCTPSRATLLTGKYPIHTGmqhfVIITDEPWG 105
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYslSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTG----VLAVPDELL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 106 LPQRERLMPEI--FRDAGYSTHLVGKWHLGfwRKDLTPT-MRGFDHHFGYYNGYI-DYYDHQVRMLDRNysagldfrrdl 181
Cdd:cd16154 77 LSEETLLQLLIkdATTAGYSSAVIGKWHLG--GNDNSPNnPGGIPYYAGILGGGVqDYYNWNLTNNGQT----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 182 epcpEANGTYATEAFTSEAKRIIEQhdKSKPLFMVLSHLAVHTgnedsPMQAPEEEV------AKFPHIRDPKRRTYAGM 255
Cdd:cd16154 144 ----TNSTEYATTKLTNLAIDWIDQ--QTKPWFLWLAYNAPHT-----PFHLPPAELhsrsllGDSADIEANPRPYYLAA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 256 ISSLDKSVAQTIGALKDNgMLNNSIILLYSDNGAPtigihsNAGSNYPY--RGQKESPWEGGIRS----AGAlwspLLKE 329
Cdd:cd16154 213 IEAMDTEIGRLLASIDEE-ERENTIIIFIGDNGTP------GQVVDLPYtrNHAKGSLYEGGINVplivSGA----GVER 281
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24666175 330 RGYVSNQAIHAVDWLPTLAGAAGVSLPQdlPLDGINLWPMLSG 372
Cdd:cd16154 282 ANERESALVNATDLYATIAELAGVDAAE--IHDSVSFKPLLSD 322
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
26-421 |
9.21e-36 |
|
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: 139.24 E-value: 9.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 26 TKPNIVIILIDDMgmND-VSFHGSNQILTPNIDALAYNGILLNKHY--VPnLCTPSRATLLTGKYPIHTGMqhfviitde 102
Cdd:cd16030 1 KKPNVLFIAVDDL--RPwLGCYGGHPAKTPNIDRLAARGVLFTNAYcqQP-VCGPSRASLLTGRRPDTTGV--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 103 pWGLPQRER-------LMPEIFRDAGYSTHLVGK-WHLGFWRKDLTPtmRGFDHHFGYYNGyiDYYDHQVRMLDRNYSAG 174
Cdd:cd16030 69 -YDNNSYFRkvapdavTLPQYFKENGYTTAGVGKiFHPGIPDGDDDP--ASWDEPPNPPGP--EKYPPGKLCPGKKGGKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 175 LDFRRDLEPCPEANGTYATEAFTSEAKRIIEQ-HDKSKPLFMVLS----HL---------------AVHTGNEDSPMQAP 234
Cdd:cd16030 144 GGGGPAWEAADVPDEAYPDGKVADEAIEQLRKlKDSDKPFFLAVGfykpHLpfvapkkyfdlypleSIPLPNPFDPIDLP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 235 E------EEVAKFPHIRDPKRRTYAGMISS----------------LDKSVAQTIGALKDNGMLNNSIILLYSDNGApTI 292
Cdd:cd16030 224 EvawndlDDLPKYGDIPALNPGDPKGPLPDeqarelrqayyasvsyVDAQVGRVLDALEELGLADNTIVVLWSDHGW-HL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 293 GIHSNAGsnypyrgqKESPWEGGIRSAGALWSPLLKERGYVSNQAIHAVDWLPTLAGAAGvsLPQDLPLDGINLWPMLSG 372
Cdd:cd16030 303 GEHGHWG--------KHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKN 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 373 -NEEPKPRTMIHvldevFGYSSYMRDTLK--------YVNGSSFKGR--YDQWLGELETN 421
Cdd:cd16030 373 pSAKWKDAAFSQ-----YPRPSIMGYSIRteryryteWVDFDKVGAEelYDHKNDPNEWK 427
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-459 |
8.81e-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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 135.00 E-value: 8.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 27 KPNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-----LCTPSRATLLTGKYPIHTGMQHFVIItd 101
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGgwsgaVCVPSRAMLMTGRTLFHAPEGGKAAI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 102 epwglPQRERLMPEIFRDAGYSTHLVGKWHLGFwrkdltptmrgfdhhfgyyngyidyydhqvrmldrnysagldfrrdl 181
Cdd:cd16155 80 -----PSDDKTWPETFKKAGYRTFATGKWHNGF----------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 182 epcpeANgtyateaftsEAKRIIEQHDKS-KPLFMVLSHLAVHtgnedSPMQAPEEEVAKFP------------------ 242
Cdd:cd16155 108 -----AD----------AAIEFLEEYKDGdKPFFMYVAFTAPH-----DPRQAPPEYLDMYPpetiplpenflpqhpfdn 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 243 ---HIRDPK----RRT----------YAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNG-AptIGIHSNAGsnypy 304
Cdd:cd16155 168 gegTVRDEQlapfPRTpeavrqhlaeYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGlA--VGSHGLMG----- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 305 rgqKESPWEGGIRsagalwSPL-LKERGYVSNQAIHA----VDWLPTLAGAAGVSLPQdlPLDGINLWPMLSGnEEPKPR 379
Cdd:cd16155 241 ---KQNLYEHSMR------VPLiISGPGIPKGKRRDAlvylQDVFPTLCELAGIEIPE--SVEGKSLLPVIRG-EKKAVR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 380 tmihvlDEVFGyssYMRDTLKYVNGSSFKG-RYD-----QWLGELETnedDPLgesyEQHVLASDVQsllgnrglTKDRI 453
Cdd:cd16155 309 ------DTLYG---AYRDGQRAIRDDRWKLiIYVpgvkrTQLFDLKK---DPD----ELNNLADEPE--------YQERL 364
|
....*.
gi 24666175 454 RQMRSE 459
Cdd:cd16155 365 KKLLAE 370
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-368 |
4.71e-33 |
|
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: 127.66 E-value: 4.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILID----DMgmndVSFHGSNQILTPNIDALAYNGILLNKHYVP-NLCTPSRATLLTGKYPIHTGMQHFViitde 102
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGsNPTLPSRFSLFTGLYPFYHGVWGGP----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 103 pwgLPQRERLMPEIFRDAGYSTHLVGkwhlgfwrkdltptmrGFDHHFGYYnGYIDYYDHqvrmldrnysagLDFRRDLE 182
Cdd:cd16148 72 ---LEPDDPTLAEILRKAGYYTAAVS----------------SNPHLFGGP-GFDRGFDT------------FEDFRGQE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 183 PCPEANGTYATEAFTSEAKRIIEQHDKSKPLFMVLSHLAVHTgnedspmqapeeevakfphirdPKRrtYAGMISSLDKS 262
Cdd:cd16148 120 GDPGEEGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPHE----------------------PYL--YDAEVRYVDEQ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 263 VAQTIGALKDNGMLNNSIILLYSDNGApTIGIHS-NAGSNYPYrgqkespWEGGIRsagalwSPLL-----KERGYVSNQ 336
Cdd:cd16148 176 IGRLLDKLKELGLLEDTLVIVTSDHGE-EFGEHGlYWGHGSNL-------YDEQLH------VPLIirwpgKEPGKRVDA 241
|
330 340 350
....*....|....*....|....*....|..
gi 24666175 337 AIHAVDWLPTLAGAAGVSLPQDlpLDGINLWP 368
Cdd:cd16148 242 LVSHIDIAPTLLDLLGVEPPDY--SDGRSLLP 271
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-463 |
3.96e-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: 119.63 E-value: 3.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTGMQHFVIITDEPW-G 105
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSpVCCPARASLLTGLYPHEHGVLNNVENAGAYSrG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 106 LPQRERLMPEIFRDAGYSTHLVGKWHLGfwrKDLTPTMRGFDHHFGYyngyidyydhqvrmldrnysagldfrrdlepcp 185
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVG---PEETPLDYGFDEYLPV--------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 186 EANGTYATeafTSEAKRIIEQH-DKSKPLFMVLSHLAVHTgnedsPMQAPEE--------EVAKFPHIRDP--------- 247
Cdd:cd16033 125 ETTIEYFL---ADRAIEMLEELaADDKPFFLRVNFWGPHD-----PYIPPEPyldmydpeDIPLPESFADDfedkpyiyr 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 248 ---KRRT---------------YAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGAPTiGIHsnagsnypyRG--Q 307
Cdd:cd16033 197 rerKRWGvdtedeedwkeiiahYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDAL-GAH---------RLwdK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 308 KESPWEGGIRSAGALWSPLLKERGYVSNQAIHAVDWLPTLAGAAGVSLPQdlPLDGINLWPMLSGNEEPKPRtmihvlDE 387
Cdd:cd16033 267 GPFMYEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPP--KVDGRSLLPLLRGEQPEDWR------DE 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 388 V--------FGYSSYM--RDTLKYV-NGSSFKGRYDQwlgeletnEDDPlgesYEQHVLASDVQsllgNRGLTKDRIRQM 456
Cdd:cd16033 339 VvteyngheFYLPQRMvrTDRYKYVfNGFDIDELYDL--------ESDP----YELNNLIDDPE----YEEILREMRTRL 402
|
....*..
gi 24666175 457 RSEATET 463
Cdd:cd16033 403 YEWMEET 409
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-366 |
8.28e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 115.94 E-value: 8.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 27 KPNIVIILIDDMGMNDVSFHGS----------NQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTGMQH 95
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSpVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 96 FviitdePWGLPQ---RERLMPEIFRDAGYSTHLVGKWHlgfwrkdltptmrgfdhhfgyyngyidyYDHQVRMLDRNYS 172
Cdd:cd16153 81 F------EAAHPAldhGLPTFPEVLKKAGYQTASFGKSH----------------------------LEAFQRYLKNANQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 173 agldfrrdlepcpeangtyateAFTSEAKRIIEQHDKSKPLFMVLSHLAVHTgnedsPMQAPEEEVAKFphirdpkrrTY 252
Cdd:cd16153 127 ----------------------SYKSFWGKIAKGADSDKPFFVRLSFLQPHT-----PVLPPKEFRDRF---------DY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 253 AGMISSLDKSVAQTIGALKDNGMLN---NSIILLYSDNGAP--TIGIHSnagsnypyrgqKESPWEGGIR-SAGALWS-P 325
Cdd:cd16153 171 YAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHlgEQGILA-----------KFTFWPQSHRvPLIVVSSdK 239
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24666175 326 LLKERGYVSNQAIHAVDWLPTLAGAAGVSLPQDLPLDGINL 366
Cdd:cd16153 240 LKAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-358 |
8.48e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 115.03 E-value: 8.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYP----IHTGM-QHFVIITD 101
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSpVCSPARASLLTGRMPsqhgIHDWIvEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 102 EPWGLPQRERLMPEIFRDAGYSTHLVGKWHLGfwrkdltptmrgfdhhfgyyngyidyyDHQVRMLDRNysagldfrrdl 181
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG---------------------------DDAADFLRRR----------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 182 epcpeangtyateaftseakriieqHDKSKPLFMVLSHLAVHtgnedSPMQapeeevakfphirdpkrrtYAGMISSLDK 261
Cdd:cd16149 123 -------------------------AEAEKPFFLSVNYTAPH-----SPWG-------------------YFAAVTGVDR 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 262 SVAQTIGALKDNGMLNNSIILLYSDNGAptigihsNAGSN-YPYRGQKESP---WEGGIRSAGALWSPLLKERGYVSNQA 337
Cdd:cd16149 154 NVGRLLDELEELGLTENTLVIFTSDNGF-------NMGHHgIWGKGNGTFPlnmYDNSVKVPFIIRWPGVVPAGRVVDSL 226
|
330 340
....*....|....*....|.
gi 24666175 338 IHAVDWLPTLAGAAGVSLPQD 358
Cdd:cd16149 227 VSAYDFFPTLLELAGVDPPAD 247
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
28-382 |
1.92e-28 |
|
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: 115.75 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTGMQhfviitDEPWGL 106
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSpLCAPSRASMMTGRLPSRIGAY------DNAAEF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 107 PQRERLMPEIFRDAGYSTHLVGKWHLgfwrkdltptmRGFDHHFGYyngyiDYyDHQVrmldrnysagldfrrdlepcpe 186
Cdd:cd16032 75 PADIPTFAHYLRAAGYRTALSGKMHF-----------VGPDQLHGF-----DY-DEEV---------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 187 angTYATEAFTSEAKRiieQHDKsKPLFMVLSHLAVHtgnedSPMQAPEEEVAKfpHIRDpKRRTYAGMISSLDKSVAQT 266
Cdd:cd16032 116 ---AFKAVQKLYDLAR---GEDG-RPFFLTVSFTHPH-----DPYVIPQEYWDL--YVRR-ARRAYYGMVSYVDDKVGQL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 267 IGALKDNGMLNNSIILLYSDNGaPTIGihsnagsnypYRG--QKESPWEGGIRSAGALWSPLLKERGYVSnQAIHAVDWL 344
Cdd:cd16032 181 LDTLERTGLADDTIVIFTSDHG-DMLG----------ERGlwYKMSFFEGSARVPLIISAPGRFAPRRVA-EPVSLVDLL 248
|
330 340 350
....*....|....*....|....*....|....*....
gi 24666175 345 PTLAGAAGVSLPQD-LPLDGINLWPMLSGNEEPKPRTMI 382
Cdd:cd16032 249 PTLVDLAGGGTAPHvPPLDGRSLLPLLEGGDSGGEDEVI 287
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-414 |
3.04e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 115.33 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTGmqhfviITDEPWGL 106
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSpICVPSRASFLTGRYVHETG------VWDNADPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 107 PQRERLMPEIFRDAGYSTHLVGKWHLgfwrkdltptmrgfdHHFGYYNGYidYYDHQVrmldrnysagldfrrdlepcpe 186
Cdd:cd16037 75 DGDVPSWGHALRAAGYETVLIGKLHF---------------RGEDQRHGF--RYDRDV---------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 187 angTYATEAFTSEAKRiieqhdKSKPLFMVLSHLAVHtgnedSPMQAPEEEVAKFphIRDpKRRTYAGMISSLDKSVAQT 266
Cdd:cd16037 116 ---TEAAVDWLREEAA------DDKPWFLFVGFVAPH-----FPLIAPQEFYDLY--VRR-ARAAYYGLVEFLDENIGRV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 267 IGALKDNGMLNNSIILLYSDNGAptigihsNAGsnypYRG--QKESPWEGGIRSAGALWSPLLKErGYVSNQAIHAVDWL 344
Cdd:cd16037 179 LDALEELGLLDNTLIIYTSDHGD-------MLG----ERGlwGKSTMYEESVRVPMIISGPGIPA-GKRVKTPVSLVDLA 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 345 PTLAGAAGVSLPQDlpLDGINLWPMLSGNEEPKprtmihvlDEVFgySSYMRDtlkYVNGSSFKGRYDQW 414
Cdd:cd16037 247 PTILEAAGAPPPPD--LDGRSLLPLAEGPDDPD--------RVVF--SEYHAH---GSPSGAFMLRKGRW 301
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
27-363 |
4.29e-27 |
|
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: 113.41 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 27 KPNIVIILIDDMgmnDVSfHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPIHTGMQHfVIITDEPWG 105
Cdd:cd16147 1 RPNIVLILTDDQ---DVE-LGSMDPMPKTKKLLADQGTTFTNAFVTTpLCCPSRASILTGQYAHNHGVTN-NSPPGGGYP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 106 LPQRERLMPEIF----RDAGYSTHLVGKwHLGFW--RKDLTPTMRGFDHHFGYYNGYIDYYdhqvrmldRNYSAGldfrR 179
Cdd:cd16147 76 KFWQNGLERSTLpvwlQEAGYRTAYAGK-YLNGYgvPGGVSYVPPGWDEWDGLVGNSTYYN--------YTLSNG----G 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 180 DLEPCPEANGTYATEAFTSEAKRIIEQHDKS-KPLFMVLSHLAVHtgnedSPMQAPEEEVAKFPHIRDPKRRTY------ 252
Cdd:cd16147 143 NGKHGVSYPGDYLTDVIANKALDFLRRAAADdKPFFLVVAPPAPH-----GPFTPAPRYANLFPNVTAPPRPPPnnpdvs 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 253 ---------AGMIS------------------SLDKSVAQTIGALKDNGMLNNSIILLYSDNGApTIGIHS-NAGSNYPY 304
Cdd:cd16147 218 dkphwlrrlPPLNPtqiayidelyrkrlrtlqSVDDLVERLVNTLEATGQLDNTYIIYTSDNGY-HLGQHRlPPGKRTPY 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666175 305 ----------RGqkesPwegGIRsagalwspllkeRGYVSNQAIHAVDWLPTLAGAAGVSLPQDlpLDG 363
Cdd:cd16147 297 eedirvpllvRG----P---GIP------------AGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDG 344
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
28-383 |
4.21e-24 |
|
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: 105.42 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYV-PNLCTPSRATLLTGKYPihtgMQHFVIITDEPwgL 106
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTqAAPCGPSRASLYTGRYL----MNHRSVWNGTP--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 107 PQRERLMPEIFRDAGYSTHLVGKWHL-----GFWRKDLTPT-----MRGFDH--HFGYY-----------NGYIDYYDHQ 163
Cdd:cd16028 75 DARHLTLALELRKAGYDPALFGYTDTspdprGLAPLDPRLLsyelaMPGFDPvdRLDEYpaedsdtafltDRAIEYLDER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 164 VrmlDRNYSAGLDFRR------------------DLEPcPEANGTYATEAftseakriiEQHDKSKPLFMVLSHLAVHTG 225
Cdd:cd16028 155 Q---DEPWFLHLSYIRphppfvapapyhalydpaDVPP-PIRAESLAAEA---------AQHPLLAAFLERIESLSFSPG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 226 nEDSPMQAPEEEVAKFphirdpkRRTYAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGApTIGIHsnagsnypYR 305
Cdd:cd16028 222 -AANAADLDDEEVAQM-------RATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGE-QLGDH--------WL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 306 GQKESPWEGGIRsagalwSPLL-----KERGYVSNQAIHA----VDWLPTLAGAAGVslPQDLPLDGINLWPMLSGNEEP 376
Cdd:cd16028 285 WGKDGFFDQAYR------VPLIvrdprREADATRGQVVDAftesVDVMPTILDWLGG--EIPHQCDGRSLLPLLAGAQPS 356
|
....*..
gi 24666175 377 KPRTMIH 383
Cdd:cd16028 357 DWRDAVH 363
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-374 |
1.20e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 101.52 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVP-NLCTPSRATLLTGKYPIHTGMqhfvIITDEPWGL 106
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAaCMCSPSRSTLYTGLHPQQTGV----TDTLGSPMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 107 PQRERLMPEI---FRDAGYSTHLVGKWHLGfwrkdltptmrgfdhhfGYYNGYIDYydhqvrmlDRNYSAG-LDFRRDLe 182
Cdd:cd16035 77 PLLSPDVPTLghmLRAAGYYTAYKGKWHLS-----------------GAAGGGYKR--------DPGIAAQaVEWLRER- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 183 pcpeangtyateaftseakriIEQHDKSKPLFMVLSHLAVHtgneDspMQAPEEEVAKFPHIRDpkrrTYAGMISSLDKS 262
Cdd:cd16035 131 ---------------------GAKNADGKPWFLVVSLVNPH----D--IMFPPDDEERWRRFRN----FYYNLIRDVDRQ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 263 VAQTIGALKDNGMLNNSIILLYSDNGApTIGIHSNAGSNY-PYRGQKESPWeggirsagaLWS-PLLKERGYVSNQAIHA 340
Cdd:cd16035 180 IGRVLDALDASGLADNTIVVFTSDHGE-MGGAHGLRGKGFnAYEEALHVPL---------IIShPDLFGTGQTTDALTSH 249
|
330 340 350
....*....|....*....|....*....|....*...
gi 24666175 341 VDWLPTLAGAAGVSLPQ----DLPLDGINLWPMLSGNE 374
Cdd:cd16035 250 IDLLPTLLGLAGVDAEArateAPPLPGRDLSPLLTDAD 287
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-288 |
3.04e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 93.45 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPN-LCTPSRATLLTGKYPiHT----GMQHFViitdE 102
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNpVCSPSRCSFLTGWYP-HVnghrTLHHLL----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 103 PWglpqrERLMPEIFRDAGYSTHLVGKwhlgfwrkdltptmrgfdhhfgyyngyidyydhqvrmldrnysagldfrRDLE 182
Cdd:cd16150 76 PD-----EPNLLKTLKDAGYHVAWAGK-------------------------------------------------NDDL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 183 PCPEANGTYAT--EAFTSEAKRIIEQHDKSKPLFMVLSHLAVHT------------GNEDSPMQAPEEEVAKFPHIRDPK 248
Cdd:cd16150 102 PGEFAAEAYCDsdEACVRTAIDWLRNRRPDKPFCLYLPLIFPHPpygveepwfsmiDREKLPPRRPPGLRAKGKPSMLEG 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 24666175 249 RR-----------------TYAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNG 288
Cdd:cd16150 182 IEkqgldrwseerwrelraTYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHG 238
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
28-351 |
6.58e-19 |
|
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: 86.32 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYV--PNLCTPSRATLLTGKYPIHTGM----QHFVIITD 101
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVspPTSSAPNHAALLTGAYPTLHGYtgngSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 102 EPWGLPQRERLMPEIFRDAGYSTHLVGkwhlgfwrkdltptmrgfdhhfgyyngyidyydhqvrmldrnysagldfrrdl 181
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 182 epcpeangtyateaftseAKRIIEQHDKSKPLFMVLSHLAVHTGNedspmqapeeevakfpHIRDPKRRTYAGMISSLDK 261
Cdd:cd00016 108 ------------------LLKAIDETSKEKPFVLFLHFDGPDGPG----------------HAYGPNTPEYYDAVEEIDE 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 262 SVAQTIGALKDNGMLNNSIILLYSDNGAPTIGIHsnagsNYPYRGQKESPWEGGIRSAGALWSPLLKeRGYVSNQAIHAV 341
Cdd:cd00016 154 RIGKVLDALKKAGDADDTVIIVTADHGGIDKGHG-----GDPKADGKADKSHTGMRVPFIAYGPGVK-KGGVKHELISQY 227
|
330
....*....|
gi 24666175 342 DWLPTLAGAA 351
Cdd:cd00016 228 DIAPTLADLL 237
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
28-252 |
3.06e-18 |
|
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: 87.82 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHY-VPNLCTPSRATLLTGKYPIHTGMqhfviitdepWG- 105
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYtTQPVCGPARSGLFTGLYPHTNGS----------WTn 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 106 ---LPQRERLMPEIFRDAGYSTHLVGKWHLGfwrkdltptmrGFDhHFGY---YNGY-IDY-YDhqvrMldRNYSAGLD- 176
Cdd:cd16156 71 cmaLGDNVKTIGQRLSDNGIHTAYIGKWHLD-----------GGD-YFGNgicPQGWdPDYwYD----M--RNYLDELTe 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 177 ----FRRDLEPCPEANG-----TYATEAfTSEAKRIIEQHdKSKPLFMVLSHLAVHtgnedSPMQAPEEEVAKFPHIRDP 247
Cdd:cd16156 133 eerrKSRRGLTSLEAEGikeefTYGHRC-TNRALDFIEKH-KDEDFFLVVSYDEPH-----HPFLCPKPYASMYKDFEFP 205
|
....*
gi 24666175 248 KRRTY 252
Cdd:cd16156 206 KGENA 210
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
28-352 |
4.30e-16 |
|
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: 78.88 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPNLCTPSRATL---LTGKYPIHTGMQHFVIITDEPw 104
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGEfevLTGLPPLPLGSGSYTLYKLNP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 105 gLPQrerlMPEIFRDAGYSTHLVGKWHLGFW-RKDLTPTMrGFDHHFGyyngyIDYYDHQVRMLDRNYsagldfrrdlep 183
Cdd:cd16015 80 -LPS----LPSILKEQGYETIFIHGGDASFYnRDSVYPNL-GFDEFYD-----LEDFPDDEKETNGWG------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 184 cpeangtYATEAFTSEAKRIIEQHDKsKPLFMVL----SHlavhtgnedSPMQAPEEEVAKFPHIRDPKR--RTYAGMIS 257
Cdd:cd16015 137 -------VSDESLFDQALEELEELKK-KPFFIFLvtmsNH---------GPYDLPEEKKDEPLKVEEDKTelENYLNAIH 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 258 SLDKSVAQTIGALKDNGMLNNSIILLYSDNGAPTIGIHSNAGSNYPYRgqKESPWeggirsagALWSPLLKErGYVSNQA 337
Cdd:cd16015 200 YTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDL--YRTPL--------LIYSPGLKK-PKKIDRV 268
|
330
....*....|....*
gi 24666175 338 IHAVDWLPTLAGAAG 352
Cdd:cd16015 269 GSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
21-436 |
3.56e-12 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 68.91 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 21 GSGYSTKPNIVIILIDDMGMNDVSFHGSNQILTPNIDALAYNGILLNKHYVPNLCTpSRA--TLLTGKYPIHTGmqhfvI 98
Cdd:COG1368 228 PFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRT-SRGefAVLTGLPPLPGG-----S 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 99 ITDEPWGLPQRerLMPEIFRDAGYSTHLvgkWH---LGFW-RKDLTPTMrGFDHHFGyyngyIDYYDHqvrmldrnysag 174
Cdd:COG1368 302 PYKRPGQNNFP--SLPSILKKQGYETSF---FHggdGSFWnRDSFYKNL-GFDEFYD-----REDFDD------------ 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 175 ldfrrdlepcpEANGTYAT--EAFTSEAKRIIEQHDKskPLFMVL----SHlavhtgnedSPMQAPEEEvAKFPHIRDPK 248
Cdd:COG1368 359 -----------PFDGGWGVsdEDLFDKALEELEKLKK--PFFAFLitlsNH---------GPYTLPEED-KKIPDYGKTT 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 249 RRTYAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGAPTIGIH--SNAGSNY--PYrgqkespweggirsagALWS 324
Cdd:COG1368 416 LNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTdyENPLERYrvPL----------------LIYS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 325 PLLKeRGYVSNQAIHAVDWLPTLAGAAGVSLPQDLPLdGINLwpmLSGNEEPKPrtmihvldevFGYSSYMRDTLKYVng 404
Cdd:COG1368 480 PGLK-KPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDL---LSPDTDPFA----------FRNGGFITDDYVYV-- 542
|
410 420 430
....*....|....*....|....*....|..
gi 24666175 405 ssfkgrydqwlgeLETNEDDPLGESYEQHVLA 436
Cdd:COG1368 543 -------------LKTGELTEEDKELEEEALA 561
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
28-402 |
1.87e-10 |
|
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: 62.94 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 28 PNIVIILIDDMGmNDVSFHGSNQILT-PNIDALAYNGIL-LNKHYVPNLCTPSRATLLTGKYPIHTgmqhfviitdEPW- 104
Cdd:cd16171 1 PNVVMVMSDSFD-GRLTFRPGNQVVDlPYINFMKQHGSVfLNAYTNSPICCPSRAAMWSGLFTHLT----------ESWn 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 105 ---GLPQRERLMPEIFRDAGYSTHLVGKwhlgfwrkdltptmrgFDHHFGYYNgyidyYDHQVRMLDRNYSAGLdfRRDL 181
Cdd:cd16171 70 nykGLDPNYPTWMDRLEKHGYHTQKYGK----------------LDYTSGHHS-----VSNRVEAWTRDVPFLL--RQEG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 182 EPCPEANGTYATE-------AFTSEAKRII--EQHDKSKPLFMVLSHlavhtgneDSPMQAPEEEVAK-FPHIRDpKRRT 251
Cdd:cd16171 127 RPTVNLVGDRSTVrvmlkdwQNTDKAVHWIrkEAPNLTQPFALYLGL--------NLPHPYPSPSMGEnFGSIRN-IRAF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 252 YAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNGAPTIgihsnagsnyPYRG-QKESPWEGGIRSAGALWSPLLKER 330
Cdd:cd16171 198 YYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAM----------EHRQfYKMSMYEGSSHVPLLIMGPGIKAG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 331 GYVSNqAIHAVDWLPTLAGAAGVSLPQDlpLDGINLWPMLSGN-EEPKPRTMIH---VLDEVFG----YSSYM--RDTLK 400
Cdd:cd16171 268 QQVSD-VVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLLSESsIKESPSRVPHpdwVLSEFHGcnvnASTYMlrTNSWK 344
|
..
gi 24666175 401 YV 402
Cdd:cd16171 345 YI 346
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
5-288 |
1.20e-07 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 53.98 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 5 KILVLLVVSSILsLAYGSGYSTKPNIVIILIDDMGMNDVSFHgsnqiLTPNIDALAYNGILLNKHY--VPNLCTPSRATL 82
Cdd:COG1524 2 KRGLSLLLASLL-AAAAAAAPPAKKVVLILVDGLRADLLERA-----HAPNLAALAARGVYARPLTsvFPSTTAPAHTTL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 83 LTGKYPIHTGMQHFViitdepWGLPQRERLMPEIfrdagySTHLVGKWHLGFWRkdlTPTM------RGFD---HHFGYY 153
Cdd:COG1524 76 LTGLYPGEHGIVGNG------WYDPELGRVVNSL------SWVEDGFGSNSLLP---VPTIferaraAGLTtaaVFWPSF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 154 NGYidyydhqvRMLDRNYSAGLDFRRDLEPCPEANgtyatEAFTSEAKRIIEQHDkskPLFMVLSHLAV-HTGnedspmq 232
Cdd:COG1524 141 EGS--------GLIDAARPYPYDGRKPLLGNPAAD-----RWIAAAALELLREGR---PDLLLVYLPDLdYAG------- 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 24666175 233 apeeevakfpHIRDPKRRTYAGMISSLDKSVAQTIGALKDNGMLNNSIILLYSDNG 288
Cdd:COG1524 198 ----------HRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
31-292 |
1.48e-07 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 53.58 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 31 VIILIDDMGMNDVSFHGsnqiLTPNIDALAYNGILLNKHY--VPNLCTPSRATLLTGKYPIHTGMQHFVII---TDEPWG 105
Cdd:pfam01663 2 LVISLDGFRADYLDRFE----LTPNLAALAKEGVSAPNLTpvFPTLTFPNHYTLVTGLYPGSHGIVGNTFYdpkTGEYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 106 LPQRERLMPEIFRD---------AGYSTHLVgkwhlgFWrkdltPTMrGFDHHfgyyngyiDYYDHQVRMLDRNYSAGLD 176
Cdd:pfam01663 78 FVISDPEDPRWWQGepiwdtaakAGVRAAAL------FW-----PGS-EVDYS--------TYYGTPPRYLKDDYNNSVP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666175 177 FRRDLepcpeanGTYATEAFTSEAkriiEQHDKSKPLFMVLSHLavhtgnedspmqapeEEVAKFPHIRDPKRRTYAGMI 256
Cdd:pfam01663 138 FEDRV-------DTAVLQTWLDLP----FADVAAERPDLLLVYL---------------EEPDYAGHRYGPDSPEVEDAL 191
|
250 260 270
....*....|....*....|....*....|....*.
gi 24666175 257 SSLDKSVAQTIGALKDNGMLNNSIILLYSDNGAPTI 292
Cdd:pfam01663 192 RRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPV 227
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