|
Name |
Accession |
Description |
Interval |
E-value |
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
35-363 |
4.19e-171 |
|
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: 483.90 E-value: 4.19e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 35 KPNFVIILADDMGWGDLGANWAET-KDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGG 113
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNaILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 194 dcytdvalplyenlniveqpvnlSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQLPAAP-RGRSLYGAG 272
Cdd:cd16161 132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPtSGRGPYGDA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 273 LWEMDSLVGQIKDKVDH-TVKENTFLWFTGDNGPWAQKCELAgsVGPFTGFWQTRQGGSPAKQTTWEGGHRVPALAYWPG 351
Cdd:cd16161 189 LQEMDDLVGQIMDAVKHaGLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
|
330
....*....|..
gi 1034598824 352 RVPVNVTSTALL 363
Cdd:cd16161 267 RIPANSTSAALV 278
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-363 |
2.69e-149 |
|
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: 428.91 E-value: 2.69e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRN-FAVTSVGG 113
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDMGCTDTPGYNHPPCPAcpqgdgpsrnlqr 193
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 194 dcytdvalPLYENLNIVEQPVNLSSLAQKYAEKATQFIQRAstSGRPFLLYVALAHMHVPLPVTQLPAAPRGRSLYGAGL 273
Cdd:cd16026 148 --------PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 274 WEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRVPALAYWPGR 352
Cdd:cd16026 218 EELDWSVGRILDALKELgLEENTLVIFTSDNGPWLEYGGHGGSAGPLRG----------GKGTTWEGGVRVPFIAWWPGV 287
|
330
....*....|.
gi 1034598824 353 VPVNVTSTALL 363
Cdd:cd16026 288 IPAGTVSDELA 298
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
35-359 |
6.37e-93 |
|
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: 287.80 E-value: 6.37e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRN-FAVTSVGG 113
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGvFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 114 LPLNETTLAEVLQQAGYVTGIIGKWHL--GHHGSYHPNFRGFDYYFGIPYSHDMG-CTD-TPGYNHPPC-PACPQGDGPs 188
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLgvGLNGTYLPTHQGFDHYLGIPYSHDQGpCQNlTCFPPNIPCfGGCDQGEVP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 189 rnlqrdcytdvaLPLYENLNIVEQPVNLSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQLPAAPRGRSL 268
Cdd:cd16158 160 ------------CPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 269 YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFtgfwqtRQGgspaKQTTWEGGHRVPALA 347
Cdd:cd16158 228 FGDALAELDGSVGELLQTLKENgIDNNTLVFFTSDNGPSTMRKSRGGNAGLL------KCG----KGTTYEGGVREPAIA 297
|
330
....*....|..
gi 1034598824 348 YWPGRVPVNVTS 359
Cdd:cd16158 298 YWPGRIKPGVTH 309
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
35-360 |
2.13e-88 |
|
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: 275.08 E-value: 2.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV---TRNFAVTSV 111
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 112 GGLPLNETTLAEVLQQAGYVTGIIGKWHLG-----HHGSYH-PNFRGFDYY-FGIPYSHDMGCTDTPGYNhppcpacpqg 184
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDFVgTNLPFTNSWACDDTGRHV---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 185 DGPSRNLqrdCYtdvalpLYENLNIVEQPVNLSSLAQKYAEKATQFIQraSTSGRPFLLYVALAHMHVPLPVTQLPAAPR 264
Cdd:cd16160 151 DFPDRSA---CF------LYYNDTIVEQPIQHEHLTETLVGDAKSFIE--DNQENPFFLYFSFPQTHTPLFASKRFKGKS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 265 GRSLYGAGLWEMDSLVGQIKDK-VDHTVKENTFLWFTGDNGPWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRV 343
Cdd:cd16160 220 KRGRYGDNINEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKG----------GKGNSWEGGIRV 289
|
330
....*....|....*..
gi 1034598824 344 PALAYWPGRVPVNVTST 360
Cdd:cd16160 290 PFIAYWPGTIKPRVSHE 306
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-359 |
3.20e-84 |
|
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: 265.10 E-value: 3.20e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG--VTRNFAVTS-- 110
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 111 ----VGGLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHdMGCTDTPGYNHPPcpacpqgdg 186
Cdd:cd16157 81 pqniVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCH-FGPYDNKAYPNIP--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 187 psrnLQRDcyTDVALPLYENLNIvEQPVNLSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQLPAAPRGR 266
Cdd:cd16157 151 ----VYRD--WEMIGRYYEEFKI-DKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 267 SLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNG-PWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRVP 344
Cdd:cd16157 224 GLYGDAVMELDSSVGKILESLKSLgIENNTFVFFSSDNGaALISAPEQGGSNGPFLC----------GKQTTFEGGMREP 293
|
330
....*....|....*
gi 1034598824 345 ALAYWPGRVPVNVTS 359
Cdd:cd16157 294 AIAWWPGHIKPGQVS 308
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
35-354 |
1.26e-78 |
|
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: 251.82 E-value: 1.26e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGR------LGLRNGVTRNFAV 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRypirsgMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 109 TSVGGLPLNETTLAEVLQQAGYVTGIIGKWHLGHH------GSYHPNFRGFDYYFGIPYSHDMGCTDTPG--YNHPPCPA 180
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHcesrndFCHHPLNHGFDYFYGLPLTNLKDCGDGSNgeYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 181 CPQgdgpSRNLQRDCYTDVALPLY--------------------------------------ENLNIVEQPVNLSSLAQK 222
Cdd:cd16159 161 FPL----LTAFVLITALTIFLLLYlgavskrffvfllilsllfislfflllitnryfncilmRNHEVVEQPMSLENLTQR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 223 YAEKATQFIQRasTSGRPFLLYVALAHMHvplpvTQLPAAP--RGRS---LYGAGLWEMDSLVGQIKDKVDHT-VKENTF 296
Cdd:cd16159 237 LTKEAISFLER--NKERPFLLVMSFLHVH-----TALFTSKkfKGRSkhgRYGDNVEEMDWSVGQILDALDELgLKDNTF 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034598824 297 LWFTGDNGPWAqkcELAGSVGPFTGFWQTRQGGSpaKQTTWEGGHRVPALAYWPGRVP 354
Cdd:cd16159 310 VYFTSDNGGHL---EEISVGGEYGGGNGGIYGGK--KMGGWEGGIRVPTIVRWPGVIP 362
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-359 |
3.86e-76 |
|
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: 240.90 E-value: 3.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGAN---WAETKDTANLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTRNFAVTSVG 112
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYgggIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 113 GLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHdmgctdtpgynhppcpacpqgdgpsrnlq 192
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYHT----------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 193 rdcytdvalplyenlniveqpvnlssLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVP-LPVTQLPAAPRGRSLYGA 271
Cdd:cd16142 131 --------------------------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPtLPSPEFEGKSSGKGKYAD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 272 GLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSvGPFTGfwqtrqggspAKQTTWEGGHRVPALAYWP 350
Cdd:cd16142 185 SMVELDDHVGQILDALDELgIADNTIVIFTTDNGPEQDVWPDGGY-TPFRG----------EKGTTWEGGVRVPAIVRWP 253
|
....*....
gi 1034598824 351 GRVPVNVTS 359
Cdd:cd16142 254 GKIKPGRVS 262
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-362 |
5.59e-72 |
|
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: 230.94 E-value: 5.59e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETK-DTANLDKMASEGMRFVDFHAAASTCSPSRASLLTG----RLGLRNGVTRNFavts 110
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGrypwRSRLKGGVLGGF---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 111 vgGLPL---NETTLAEVLQQAGYVTGIIGKWHLG-----------HHGSYH-----------PNFRGFDYYFGIPYShdm 165
Cdd:cd16143 77 --SPPLiepDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkaATGTGKdvdyskpikggPLDHGFDYYFGIPAS--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 166 gctdtpgynhppcpacpqgdgpsrnlqrdcytDVaLPLyenlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYV 245
Cdd:cd16143 152 --------------------------------EV-LPT-------------------LTDKAVEFIDQHAKKDKPFFLYF 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 246 ALAHMHVPLpvtqLPAAP-RGRS---LYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGPwaqkcelagsvGPFT 320
Cdd:cd16143 180 ALPAPHTPI----VPSPEfQGKSgagPYGDFVYELDWVVGRILDALKeLGLAENTLVIFTSDNGP-----------SPYA 244
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1034598824 321 GFWQT-RQGGSPA------KQTTWEGGHRVPALAYWPGRVPVNVTSTAL 362
Cdd:cd16143 245 DYKELeKFGHDPSgplrgmKADIYEGGHRVPFIVRWPGKIPAGSVSDQL 293
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
34-362 |
2.00e-71 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 229.38 E-value: 2.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvTSVGG 113
Cdd:COG3119 22 KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE-GYNGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 114 LPLNETTLAEVLQQAGYVTGIIGKWHLghhgsyhpnfrgfdyyfgipYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:COG3119 101 LPPDEPTLAELLKEAGYRTALFGKWHL--------------------YLTD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 194 dcytdvalplyenlniveqpvnlsslaqKYAEKATQFIQRASTSGRPFLLYVALAHMHVP-----------------LPV 256
Cdd:COG3119 132 ----------------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPyqapeeyldkydgkdipLPP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 257 TQLPAA------PRGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAqkcelagsvgpftGFWQTRQGg 329
Cdd:COG3119 184 NLAPRDlteeelRRARAAYAAMIEEVDDQVGRLLDALEELgLADNTIVVFTSDNGPSL-------------GEHGLRGG- 249
|
330 340 350
....*....|....*....|....*....|...
gi 1034598824 330 spaKQTTWEGGHRVPALAYWPGRVPVNVTSTAL 362
Cdd:COG3119 250 ---KGTLYEGGIRVPLIVRWPGKIKAGSVSDAL 279
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-362 |
8.26e-71 |
|
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: 228.58 E-value: 8.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTG----RLGL---------RNGV 102
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGqypaRLGItdvipgrrgPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 103 TRNFAVTSVGGLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGI-PYSHDMGCTDTPGYNHPPCPAC 181
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIGGtGNGGPPSYYFPPGKPNPDLEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 182 PQGDgpsrnlqrdcytdvalplyenlniveqpvnlsSLAQKYAEKATQFIQRAstSGRPFLLYvaLAH--MHVPLPVTQ- 258
Cdd:cd16144 161 PEGE--------------------------------YLTDRLTDEAIDFIEQN--KDKPFFLY--LSHyaVHTPIQARPe 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 259 -------LPAAPRGR---SLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFtgfwqtRQ 327
Cdd:cd16144 205 liekyekKKKGLRKGqknPVYAAMIESLDESVGRILDALEELgLADNTLVIFTSDNGGLSTRGGPPTSNAPL------RG 278
|
330 340 350
....*....|....*....|....*....|....*
gi 1034598824 328 GgspaKQTTWEGGHRVPALAYWPGRVPVNVTSTAL 362
Cdd:cd16144 279 G----KGSLYEGGIRVPLIVRWPGVIKPGSVSDVP 309
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-359 |
2.18e-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: 293764 [Multi-domain] Cd Length: 415 Bit Score: 227.48 E-value: 2.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGGLP 115
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 116 LNETTLAEVLQQAGYVTGIIGKWHLGHHGSY-HPNFRGFDYYFGIpYSHdmgctdTPGYNHPPcpacPQGDgpsRNLQRd 194
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYGY-LDQ------VHAHNYYP----EYLW---RNGEK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 195 cytdvaLPLYENLNIVEQPVNLSSLAQK-YAE-----KATQFIQRAstSGRPFLLYVALAHMHVPLPVTQLPAA---PRG 265
Cdd:cd16145 146 ------VPLPNNVIPPLDEGNNAGGGGGtYSHdlftdEALDFIREN--KDKPFFLYLAYTLPHAPLQVPDDGPYkykPKD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 266 RSLYGAGLWE------------MDSLVGQIKDKV-DHTVKENTFLWFTGDNGP-----WAQKCELAGSVGPFTGFwqtrq 327
Cdd:cd16145 218 PGIYAYLPWPqpekayaamvtrLDRDVGRILALLkELGIDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY----- 292
|
330 340 350
....*....|....*....|....*....|..
gi 1034598824 328 ggspaKQTTWEGGHRVPALAYWPGRVPVNVTS 359
Cdd:cd16145 293 -----KRSLYEGGIRVPFIARWPGKIPAGSVS 319
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
36-362 |
1.41e-63 |
|
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: 209.71 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTRnfavTSVGG-- 113
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWH----TILGRer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgcTDTPGYnhppcpacpqgdgpsrnLQR 193
Cdd:cd16146 76 MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGGGI---GQYPDY-----------------WGN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 194 DCYTDValpLYENlNIVEQpvnlsslAQKYA-----EKATQFIQRASTsgRPFLLYVALAHMHVPLPVTQLPAAP----- 263
Cdd:cd16146 136 DYFDDT---YYHN-GKFVK-------TEGYCtdvffDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPykdmg 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 264 --RGRSLYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGPWaqkcelAGSVGPFTGFWQtrqgGSpaKQTTWEGG 340
Cdd:cd16146 203 ldDKLAAFYGMIENIDDNVGRLLAKLKeLGLEENTIVIFMSDNGPA------GGVPKRFNAGMR----GK--KGSVYEGG 270
|
330 340
....*....|....*....|..
gi 1034598824 341 HRVPALAYWPGRVPVNVTSTAL 362
Cdd:cd16146 271 HRVPFFIRWPGKILAGKDVDTL 292
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
36-362 |
1.31e-58 |
|
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: 191.11 E-value: 1.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNfaVTSVGGLP 115
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 116 LNETTLAEVLQQAGYVTGIIGKWHlghhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsrnlqrdc 195
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 196 ytdvalplyenlniveqpvnlsslaqkyaEKATQFIQRASTSgRPFLLYVALAHMHVPLpvtqlpaaprgrsLYGAGLWE 275
Cdd:cd16022 103 -----------------------------DEAIDFIERRDKD-KPFFLYVSFNAPHPPF-------------AYYAMVSA 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 276 MDSLVGQIKDKVDHT-VKENTFLWFTGDNgpwaqkcelagsvGPFTGFWQTRQGgspaKQTTWEGGHRVPALAYWPGRVP 354
Cdd:cd16022 140 IDDQIGRILDALEELgLLDNTLIVFTSDH-------------GDMLGDHGLRGK----KGSLYEGGIRVPFIVRWPGKIP 202
|
....*...
gi 1034598824 355 VNVTSTAL 362
Cdd:cd16022 203 AGQVSDAL 210
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
36-354 |
1.67e-56 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 190.45 E-value: 1.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFvDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSV-GGL 114
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVIL-NNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEpYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 115 PLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYH-PNFRGFDYYFGiPYShdmGCTDtpGYNHPPCPACP------QGDGP 187
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYTWEYtPTNRGFDSFYG-YYG---GAED--YYTHTSGGANDygnddlRDNEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 188 SRNLQRDCY-TDValplyenlniveqpvnlsslaqkYAEKATQFIQRASTSgRPFLLYVALAHMHVPLPVTQLPAAP--- 263
Cdd:cd16029 154 PAWDYNGTYsTDL-----------------------FTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPyed 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 264 -------RGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCElAGSVGPFTGfwqtrqggspAKQT 335
Cdd:cd16029 210 kfahikdEDRRTYAAMVSALDESVGNVVDALKAKgMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRG----------GKNT 278
|
330
....*....|....*....
gi 1034598824 336 TWEGGHRVPALAYWPGRVP 354
Cdd:cd16029 279 LWEGGVRVPAFVWSPLLPP 297
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
36-362 |
4.49e-51 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 173.76 E-value: 4.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrnfaVTSVGGLP 115
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSY----VSTPVGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 116 LNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFG-IPYSHDMGCTDTPGYNHPPcpacpqgdgpsrnlqRD 194
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLYADPPDVPYNCSG---------------GG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 195 CYTDValplyenlniveqpvnlsslaqkYAEKATQFIQRAStsgRPFLLYVALAHMHVPLPVTQLPAAP----------- 263
Cdd:pfam00884 142 VSDEA-----------------------LLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscse 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 264 -RGRSLYGAGLWEMDSLVGQIKDKV-DHTVKENTFLWFTGDNGPwaqkcelagSVGPFTGFWQTRQGGspakqTTWEGGH 341
Cdd:pfam00884 196 eQLLNSYDNTLLYTDDAIGRVLDKLeENGLLDNTLVVYTSDHGE---------SLGEGGGYLHGGKYD-----NAPEGGY 261
|
330 340
....*....|....*....|.
gi 1034598824 342 RVPALAYWPGRVPVNVTSTAL 362
Cdd:pfam00884 262 RVPLLIWSPGGKAKGQKSEAL 282
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-362 |
1.04e-50 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 175.10 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTRnfavtsvGGLP 115
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPL-CTPSRVQLMTGKYNFRNYVVF-------GYLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 116 LNETTLAEVLQQAGYVTGIIGKWHLG---HHGSYHPNFrGFDYY--FGipyshdmGCTDTPGYNHPPCPACPQGDGPSRN 190
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGKWQLGggrGDGDYPHEF-GFDEYclWQ-------LTETGEKYSRPATPTFNIRNGKLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 191 LQRDCY-TDValplyenlniveqpvnlsslaqkYAEKATQFIQRAstSGRPFLLY--VALAH-MHVPLPVTQLPAAPRGR 266
Cdd:cd16151 145 TTEGDYgPDL-----------------------FADFLIDFIERN--KDQPFFAYypMVLVHdPFVPTPDSPDWDPDDKR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 267 S-----LYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNgpwaqkcelaGSVGPFTGFW--QTRQGGspaKQTTWE 338
Cdd:cd16151 200 KkddpeYFPDMVAYMDKLVGKLVDKLEELgLRENTIIIFTGDN----------GTHRPITSRTngREVRGG---KGKTTD 266
|
330 340
....*....|....*....|....
gi 1034598824 339 GGHRVPALAYWPGRVPVNVTSTAL 362
Cdd:cd16151 267 AGTHVPLIVNWPGLIPAGGVSDDL 290
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
34-353 |
1.35e-46 |
|
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: 164.54 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 34 QKPNFVIILADDMGWGDLGANWAETkDTANLDKMASEGMRFVDFHAAAsTCSPSRASLLTGRLGLRNGVtRNFAVTSVGG 113
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEI-PTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 114 ------LPLNETTLAEVLQQAGYVTGIIGKWHLGHHgsyhpnfrgfDYYFgipySHDmgctdtpgynhppcpacpqgdgp 187
Cdd:cd16025 78 pgyegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------DYYS----TDD----------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 188 srnlqrdcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYVALAHMHVPL------------- 254
Cdd:cd16025 121 -----------------------------------LTDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLqapkewidkykgk 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 255 -----------------------PVTQLPAAPRG-----------RSLYG------AGLWE-MDSLVGQIKDKVDHT-VK 292
Cdd:cd16025 166 ydagwdalreerlerqkelglipADTKLTPRPPGvpawdslspeeKKLEArrmevyAAMVEhMDQQIGRLIDYLKELgEL 245
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034598824 293 ENTFLWFTGDNGP-----WAQkcelAGSvGPFTGFwqtrqggspaKQTTWEGGHRVPALAYWPGRV 353
Cdd:cd16025 246 DNTLIIFLSDNGAsaepgWAN----ASN-TPFRLY----------KQASHEGGIRTPLIVSWPKGI 296
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
36-362 |
2.91e-41 |
|
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: 149.58 E-value: 2.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGA--NWAETkdtANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFavTSVGG 113
Cdd:cd16027 1 PNILWIIADDLSPDLGGYggNVVKT---PNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR--SRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAWD----------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 194 dcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQRAStSGRPFLLYVALAHMH-----------------VPLPv 256
Cdd:cd16027 127 -----------------------------YASNAADFLNRAK-KGQPFFLWFGFHDPHrpyppgdgeepgydpekVKVP- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 257 TQLPAAPRGR---SLYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGpwaqkcelagsvGPFTGfwqtrqggspA 332
Cdd:cd16027 176 PYLPDTPEVRedlADYYDEIERLDQQVGEILDELEeDGLLDNTIVIFTSDHG------------MPFPR----------A 233
|
330 340 350
....*....|....*....|....*....|
gi 1034598824 333 KQTTWEGGHRVPALAYWPGRVPVNVTSTAL 362
Cdd:cd16027 234 KGTLYDSGLRVPLIVRWPGKIKPGSVSDAL 263
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-363 |
3.64e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 144.63 E-value: 3.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVtsvggL 114
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 115 PLNETTLAEVLQQAGYVTGIIGKWHL-GHHGSYH--------PNFR-GFDYYFGipyshdMGCTDtpGYNHPPCpacpQG 184
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGraddytppPERRhGFDYWKG------YECNH--DHNNPHY----YD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 185 DGPSRNlQRDCYTDVALplyenlniveqpvnlsslaqkyAEKATQFIQRASTSGRPFLLYVALAHMHVP----------- 253
Cdd:cd16034 144 DDGKRI-YIKGYSPDAE----------------------TDLAIEYLENQADKDKPFALVLSWNPPHDPyttapeeyldm 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 254 -----------LPVTQLPAAPRGRSL---YGA--GLwemDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSV 316
Cdd:cd16034 201 ydpkklllrpnVPEDKKEEAGLREDLrgyYAMitAL---DDNIGRLLDALKELgLLENTIVVFTSDHG------DMLGSH 271
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1034598824 317 GPFtgfwqtrqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALL 363
Cdd:cd16034 272 GLM------------NKQVPYEESIRVPFIIRYPGKIKAGRVVDLLI 306
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
34-362 |
2.52e-35 |
|
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.
Pssm-ID: 293755 [Multi-domain] Cd Length: 429 Bit Score: 134.96 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvGG 113
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG----PL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGsYHPNfRGFDYYFGIPyshdmgctdtpgynhppcpacPQGDgpsrnlqr 193
Cdd:cd16031 77 FDASQPTYPKLLRKAGYQTAFIGKWHLGSGG-DLPP-PGFDYWVSFP---------------------GQGS-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 194 dcYTDvaLPLYENLNIVEQPVNLSSLaqkYAEKATQFIQRAStSGRPFLLYV-----------ALAHMHV------PLPV 256
Cdd:cd16031 126 --YYD--PEFIENGKRVGQKGYVTDI---ITDKALDFLKERD-KDKPFCLSLsfkaphrpftpAPRHRGLyedvtiPEPE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 257 TQLPA--APRGRSL---------------------------YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpw 306
Cdd:cd16031 198 TFDDDdyAGRPEWAreqrnrirgvldgrfdtpekyqrymkdYLRTVTGVDDNVGRILDYLEEQgLADNTIIIYTSDNG-- 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034598824 307 aqkcELAGSVGpFTGfwqtrqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTAL 362
Cdd:cd16031 276 ----FFLGEHG-LFD-----------KRLMYEESIRVPLIIRDPRLIKAGTVVDAL 315
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-354 |
1.97e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 125.81 E-value: 1.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV-----TRNFAVTS 110
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 111 VG-GLPLNETTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd16149 81 KPeGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 190 nlqrdcytdvalplyenlniveqpvnlsslaqkyaEKATQFIQRASTSGRPFLLYVAlahmhvplpvTQLPAAPRGrslY 269
Cdd:cd16149 113 -----------------------------------DDAADFLRRRAEAEKPFFLSVN----------YTAPHSPWG---Y 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 270 GAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcelagsvgpFT----GFWQTRQGGSPakQTTWEGGHRVP 344
Cdd:cd16149 145 FAAVTGVDRNVGRLLDELEELgLTENTLVIFTSDNG--------------FNmghhGIWGKGNGTFP--LNMYDNSVKVP 208
|
330
....*....|
gi 1034598824 345 ALAYWPGRVP 354
Cdd:cd16149 209 FIIRWPGVVP 218
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-363 |
3.91e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 127.85 E-value: 3.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWgDLGANWAETKD---TANLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTrnfavtSVG 112
Cdd:cd16154 1 PNILLIIADDQGL-DSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVL------AVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 113 G-LPLNETTL--AEVLQQ--AGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIpyshdMGctdtpgynhppcpacpqGDGP 187
Cdd:cd16154 73 DeLLLSEETLlqLLIKDAttAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGI-----LG-----------------GGVQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 188 SrnlqrdcYTDVALplyeNLNIVEQPVN------LSSLAQKYAEKATQfiqrastsgrPFLLYVALAHMHVPLpvtQLPA 261
Cdd:cd16154 131 D-------YYNWNL----TNNGQTTNSTeyattkLTNLAIDWIDQQTK----------PWFLWLAYNAPHTPF---HLPP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 262 A---PRG------------RSLYGAGLWEMDSLVGQIKDKVDHTVKENTFLWFTGDNG-PwaqkcelagsvGPFTGFWQT 325
Cdd:cd16154 187 AelhSRSllgdsadieanpRPYYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGtP-----------GQVVDLPYT 255
|
330 340 350
....*....|....*....|....*....|....*...
gi 1034598824 326 RQGgspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALL 363
Cdd:cd16154 256 RNH---AKGSLYEGGINVPLIVSGAGVERANERESALV 290
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
35-362 |
4.68e-29 |
|
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: 116.88 E-value: 4.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 35 KPNFVIILADDMGWgDLGANWAETKdTANLdkMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtSVGGL 114
Cdd:cd16147 1 RPNIVLILTDDQDV-ELGSMDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSP--PGGGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 115 P------LNETTLAEVLQQAGYVTGIIGK----WHLGHHGSYHPnfRGFDYYFGI-------PYSHDMGCTDTPGYNHPp 177
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYVP--PGWDEWDGLvgnstyyNYTLSNGGNGKHGVSYP- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 178 cpacpqgdgpsrnlqRDCYTDValplyenlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYVA----------- 246
Cdd:cd16147 152 ---------------GDYLTDV-----------------------IANKALDFLRRAAADDKPFFLVVAppaphgpftpa 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 247 --LAHMHVPLPVT------------------QLPAAP-----------RGRslygaglWE----MDSLVGQIKDKVDHT- 290
Cdd:cd16147 194 prYANLFPNVTAPprpppnnpdvsdkphwlrRLPPLNptqiayidelyRKR-------LRtlqsVDDLVERLVNTLEATg 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034598824 291 VKENTFLWFTGDNgpwaqkcelagsvgpftGFW--QTRQGgsPAKQTTWEGGHRVPALAYWPGrVPVNVTSTAL 362
Cdd:cd16147 267 QLDNTYIIYTSDN-----------------GYHlgQHRLP--PGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQL 320
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-379 |
2.33e-27 |
|
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: 112.31 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNF--AVTSVGG 113
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSyhPNFRGFDYYFgiPYSH-------DMGC--------TDTP-----GY 173
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVGPEET--PLDYGFDEYL--PVETtieyflaDRAIemleelaaDDKPfflrvNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 174 NHPPCPACPqgdgPSRNLqrDCYTDVALPLYENLNiveqpvnlSSLAQK---YAEKATQFIQRASTSG--RPfllyvALA 248
Cdd:cd16033 157 WGPHDPYIP----PEPYL--DMYDPEDIPLPESFA--------DDFEDKpyiYRRERKRWGVDTEDEEdwKE-----IIA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 249 HmhvplpvtqlpaaprgrslYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGPFTgfwqtrQ 327
Cdd:cd16033 218 H-------------------YWGYITLIDDAIGRILDALEELgLADDTLVIFTSDHG------DALGAHRLWD------K 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034598824 328 GGSPAKQTtweggHRVPALAYWPGRVPVNVTSTALLRCCS-TPT----AGQL-------ESLEP 379
Cdd:cd16033 267 GPFMYEET-----YRIPLIIKWPGVIAAGQVVDEFVSLLDlAPTildlAGVDvppkvdgRSLLP 325
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
31-351 |
6.43e-26 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 109.37 E-value: 6.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 31 TRGQKPNFVIILADDMGwGD-LGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNGV 102
Cdd:PRK13759 2 VQTKKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 103 TRNFavtsvgglplnETTLAEVLQQAGYVTGIIGKWHlghhgsYHP--NFRGFD--------YYFGIPYSH---DMgCTD 169
Cdd:PRK13759 81 PWNY-----------KNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHnvllhdgyLHSGRNEDKsqfDF-VSD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 170 --------TPGYNhppcpACPQGDGpsrnlqRDCYTDVALP--LYENLNiveqPVNLSslaqkyAEKATQFIQRAStSGR 239
Cdd:PRK13759 143 ylawlrekAPGKD-----PDLTDIG------WDCNSWVARPwdLEERLH----PTNWV------GSESIEFLRRRD-PTK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 240 PFLLYVALAHMHVPL--PV--------TQLPAAPRGRSLYGAGLW----EMDSLVGQIKDK---------------VDH- 289
Cdd:PRK13759 201 PFFLKMSFARPHSPYdpPKryfdmykdADIPDPHIGDWEYAEDQDpeggSIDALRGNLGEEyarraraayyglithIDHq 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034598824 290 ------TVKE-----NTFLWFTGDNGpwaqkcELAGSVGPFTgfwqtrqggspaKQTTWEGGHRVPALAYWPG 351
Cdd:PRK13759 281 igrflqALKEfglldNTIILFVSDHG------DMLGDHYLFR------------KGYPYEGSAHIPFIIYDPG 335
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-362 |
1.41e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 103.80 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAAST----CSPSRASLLTGRLGLRNGVTRNFAvt 109
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFHAPEGGKAA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 110 svggLPLNETTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd16155 79 ----IPSDDKTWPETFKKAGYRTFATGKWHNG------------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 190 nlqrdcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYVALAHMH-----------------V 252
Cdd:cd16155 107 ---------------------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHdprqappeyldmyppetI 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 253 PLPVTQLPAAP------------------------RGRSLYGAGLWEMDSLVGQIKDKVDHTVK-ENTFLWFTGDNGpwa 307
Cdd:cd16155 154 PLPENFLPQHPfdngegtvrdeqlapfprtpeavrQHLAEYYAMITHLDAQIGRILDALEASGElDNTIIVFTSDHG--- 230
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034598824 308 qkceLAgsVGpftgfwqtrQGGSPAKQTTWEGGHRVPALAYWPGrVPVNVTSTAL 362
Cdd:cd16155 231 ----LA--VG---------SHGLMGKQNLYEHSMRVPLIISGPG-IPKGKRRDAL 269
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-360 |
6.86e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 97.23 E-value: 6.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILAD----DMgwgdLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrnfavtsV 111
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW-------G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 112 GGLPLNETTLAEVLQQAGYVTGIIGKWhlgHHGSYHPNF-RGFDYYFGIPYSHdmgcTDTPGYNHPPCPACpqgdgpsrn 190
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAVSSN---PHLFGGPGFdRGFDTFEDFRGQE----GDPGEEGDERAERV--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 191 lqrdcyTDVALplyenlniveqpvnlsslaqkyaekatQFIQRASTSgRPFLLYValaHMHvplpvtqlpaAPRGRSLYG 270
Cdd:cd16148 134 ------TDRAL---------------------------EWLDRNADD-DPFFLFL---HYF----------DPHEPYLYD 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 271 AGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGpwaqkcELAGSVGPFTGFWqtrqggspakQTTWEGGHRVPALAYW 349
Cdd:cd16148 167 AEVRYVDEQIGRLLDKLKeLGLLEDTLVIVTSDHG------EEFGEHGLYWGHG----------SNLYDEQLHVPLIIRW 230
|
330
....*....|.
gi 1034598824 350 PGRVPVNVTST 360
Cdd:cd16148 231 PGKEPGKRVDA 241
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-140 |
3.18e-21 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 94.22 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNfavtsVGGL 114
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPL 75
|
90 100
....*....|....*....|....*.
gi 1034598824 115 PLNETTLAEVLQQAGYVTGIIGKWHL 140
Cdd:cd16152 76 PADEKTLAHYFRDAGYETGYVGKWHL 101
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
36-361 |
6.62e-21 |
|
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: 90.94 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCS-PSRASLLTGRLGLRNGVTRNFAVT----- 109
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSaPNHAALLTGAYPTLHGYTGNGSADpelps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 110 SVGGLPLNETTLAEVLQQAGYVTGIIGKWhlghhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIGLL--------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 190 nlqrdcytdvalplyenlniveqpvnlsslaqkyaekatQFIQRaSTSGRPFLLYVALAHMHVPL--PVTQLPaaprgrs 267
Cdd:cd00016 110 ---------------------------------------KAIDE-TSKEKPFVLFLHFDGPDGPGhaYGPNTP------- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 268 LYGAGLWEMDSLVGQIKDKV-DHTVKENTFLWFTGDNGpwaqkcelAGSVGPftgfwqTRQGGSPAKQTTWEGGHRVPAL 346
Cdd:cd00016 143 EYYDAVEEIDERIGKVLDALkKAGDADDTVIIVTADHG--------GIDKGH------GGDPKADGKADKSHTGMRVPFI 208
|
330
....*....|....*....
gi 1034598824 347 AYWPG----RVPVNVTSTA 361
Cdd:cd00016 209 AYGPGvkkgGVKHELISQY 227
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-360 |
1.73e-20 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 91.45 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVtsvggLP 115
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP-----YD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 116 LNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHpnfrGFDYyfgipyshDMGCTDTpgynhppcpacpqgdgpsrnlqrdc 195
Cdd:cd16037 76 GDVPSWGHALRAAGYETVLIGKLHFRGEDQRH----GFRY--------DRDVTEA------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 196 ytdvalplyenlniveqpvnlsslaqkyaekATQFIQRASTSGRPFLLYVALAHMHVPLPVTQ---LPAAPRGRSLYGAG 272
Cdd:cd16037 119 -------------------------------AVDWLREEAADDKPWFLFVGFVAPHFPLIAPQefyDLYVRRARAAYYGL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 273 LWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSvgpfTGFWQtrqggspaKQTTWEGGHRVPALAYWPG 351
Cdd:cd16037 168 VEFLDENIGRVLDALEELgLLDNTLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMIISGPG 229
|
....*....
gi 1034598824 352 RVPVNVTST 360
Cdd:cd16037 230 IPAGKRVKT 238
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-355 |
9.43e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 88.59 E-value: 9.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 35 KPNFVIILADDMGWGDLGA-NWAETKD---------TANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTR 104
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCyNNAHTGKsesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 105 NFAVTSVGGLPLneTTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqg 184
Cdd:cd16153 81 FEAAHPALDHGL--PTFPEVLKKAGYQTASFGKSHLE------------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 185 dgpsrNLQRdcYTDVALPLYENLNIVEqpvnlsslaqkyaekatqfIQRASTSGrPFLLYVALAHMHVP-LPvtqlPAAP 263
Cdd:cd16153 116 -----AFQR--YLKNANQSYKSFWGKI-------------------AKGADSDK-PFFVRLSFLQPHTPvLP----PKEF 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 264 RGRSLYGAGLWEMDSLVGQIKDKVD----HTVKENTFLWFTGDNGpwaqkcelagsvgpftgfWQTRQGGSPAKQTTWEG 339
Cdd:cd16153 165 RDRFDYYAFCAYGDAQVGRAVEAFKayslKQDRDYTIVYVTGDHG------------------WHLGEQGILAKFTFWPQ 226
|
330
....*....|....*.
gi 1034598824 340 GHRVPALAYWPGRVPV 355
Cdd:cd16153 227 SHRVPLIVVSSDKLKA 242
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-362 |
6.79e-19 |
|
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: 86.49 E-value: 6.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDM-GWGDLGANWAETKDTAnLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGGL 114
Cdd:cd16035 1 PNILLILTDQErYPPPWPAGWAALNLPA-RERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 115 PLNETTLAEVLQQAGYVTGIIGKWHLGHHGsyhpnfRGfdyyfgipyshdmgctdtpGYNHPPcpacpqgdgpsrnlqrd 194
Cdd:cd16035 80 SPDVPTLGHMLRAAGYYTAYKGKWHLSGAA------GG-------------------GYKRDP----------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 195 cytdvalplyenlniveqpvnlsslaqKYAEKATQFIQRASTS---GRPFLLYVALAHMH-VPLPVTQLPAAPRGRSLYG 270
Cdd:cd16035 118 ---------------------------GIAAQAVEWLRERGAKnadGKPWFLVVSLVNPHdIMFPPDDEERWRRFRNFYY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 271 AGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGpftgfwQTRQGGSPAKQTTwegghRVPALAYW 349
Cdd:cd16035 171 NLIRDVDRQIGRVLDALDASgLADNTIVVFTSDHG------EMGGAHG------LRGKGFNAYEEAL-----HVPLIISH 233
|
330
....*....|...
gi 1034598824 350 PGRVPVNVTSTAL 362
Cdd:cd16035 234 PDLFGTGQTTDAL 246
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
34-344 |
2.42e-18 |
|
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: 86.47 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 34 QKPNFVIILADDM----GWgdLGANWAETkdtANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrNFAVT 109
Cdd:cd16030 1 KKPNVLFIAVDDLrpwlGC--YGGHPAKT---PNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVY-DNNSY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 110 SVGGLPlNETTLAEVLQQAGYVTGIIGK-WHlGHHGSYHPNFRGFDYYFGIP--------YSHDMGCTDTPGYNHPPCPA 180
Cdd:cd16030 75 FRKVAP-DAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPPgpekyppgKLCPGKKGGKGGGGGPAWEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 181 CPQGDGPsrnlqrdcYTDvalplyenlniveqpvnlsslaQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQ-- 258
Cdd:cd16030 153 ADVPDEA--------YPD----------------------GKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKky 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 259 ------------------------------LPAAPRGRSLYG--------AGLWE------------MDSLVGQIKDKVD 288
Cdd:cd16030 203 fdlyplesiplpnpfdpidlpevawndlddLPKYGDIPALNPgdpkgplpDEQARelrqayyasvsyVDAQVGRVLDALE 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034598824 289 -HTVKENTFLWFTGDNGpWA--QKcelagsvgpftGFWqtrqggspAKQTTWEGGHRVP 344
Cdd:cd16030 283 eLGLADNTIVVLWSDHG-WHlgEH-----------GHW--------GKHTLFEEATRVP 321
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
36-357 |
8.81e-16 |
|
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: 77.62 E-value: 8.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvgGLP 115
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-----EFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 116 LNETTLAEVLQQAGYVTGIIGKWHL-G---HHgsyhpnfrGFDYyfgipyshDmgctdtpgynhppcpacpqgdgpsrnl 191
Cdd:cd16032 76 ADIPTFAHYLRAAGYRTALSGKMHFvGpdqLH--------GFDY--------D--------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 192 qrdcyTDVALplyenlniveqpvnlsslaqkyaeKATQFI-QRA-STSGRPFLLYVALAHMHVPLPVTQ------LPAAp 263
Cdd:cd16032 113 -----EEVAF------------------------KAVQKLyDLArGEDGRPFFLTVSFTHPHDPYVIPQeywdlyVRRA- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 264 RgRSLYGAGLWeMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSvgpfTGFWQtrqggspaKQTTWEGGHR 342
Cdd:cd16032 163 R-RAYYGMVSY-VDDKVGQLLDTLERTgLADDTIVIFTSDHG------DMLGE----RGLWY--------KMSFFEGSAR 222
|
330 340
....*....|....*....|
gi 1034598824 343 VPALAYWPG-----RVPVNV 357
Cdd:cd16032 223 VPLIISAPGrfaprRVAEPV 242
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
36-142 |
2.26e-14 |
|
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: 74.34 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGvtrnfAVTSVGGLP 115
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNG-----SWTNCMALG 75
|
90 100
....*....|....*....|....*...
gi 1034598824 116 LNETTLAEVLQQAGYVTGIIGKWHL-GH 142
Cdd:cd16156 76 DNVKTIGQRLSDNGIHTAYIGKWHLdGG 103
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
36-157 |
2.81e-14 |
|
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: 74.22 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvgGLP 115
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT-----PLD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034598824 116 LNETTLAEVLQQAGYVTGIIGKWHL-----GHH------GSYHPNFRGFDYYF 157
Cdd:cd16028 76 ARHLTLALELRKAGYDPALFGYTDTspdprGLApldprlLSYELAMPGFDPVD 128
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-95 |
1.07e-10 |
|
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: 63.02 E-value: 1.07e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGR 95
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGW 60
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
36-351 |
3.74e-06 |
|
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: 48.69 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGrlgLRNGVTRNFavTSVGGLP 115
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG---LFTHLTESW--NNYKGLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 116 LNETTLAEVLQQAGYVTGIIGK--WHLGHHGSYHpnfRGFDYYFGIPYShdmgctdtpgynhppcpaCPQGDGPSRNLQR 193
Cdd:cd16171 76 PNYPTWMDRLEKHGYHTQKYGKldYTSGHHSVSN---RVEAWTRDVPFL------------------LRQEGRPTVNLVG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 194 DCYTDvalplyenlniveqpvNLSSLAQKYAEKATQFIQRASTS-GRPFLLYVALAHMHvPLPVTQLPAAPRG----RSL 268
Cdd:cd16171 135 DRSTV----------------RVMLKDWQNTDKAVHWIRKEAPNlTQPFALYLGLNLPH-PYPSPSMGENFGSirniRAF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 269 YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAgsvgpftgfWQTRQGgspAKQTTWEGGHRVPALA 347
Cdd:cd16171 198 YYAMCAETDAMLGEIISALKDTgLLDKTYVFFTSDHG------ELA---------MEHRQF---YKMSMYEGSSHVPLLI 259
|
....
gi 1034598824 348 YWPG 351
Cdd:cd16171 260 MGPG 263
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
28-161 |
6.86e-06 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 48.11 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 28 SGKTRGQKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVtrnfA 107
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGS----P 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 108 VTSVGGLPLNetTLAEVLQQAGYVTGIIgkwHlGHHGS------YHPNFrGFDYYFGIPY 161
Cdd:COG1368 303 YKRPGQNNFP--SLPSILKKQGYETSFF---H-GGDGSfwnrdsFYKNL-GFDEFYDRED 355
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
14-162 |
5.46e-04 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 41.66 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 14 SFSGFLYPLVDFCISGKTRGQKPnFVIILADDMGWGDLGANwaetkDTANLDKMASEGMRFVDFHAA--ASTCsPSRASL 91
Cdd:COG1524 3 RGLSLLLASLLAAAAAAAPPAKK-VVLILVDGLRADLLERA-----HAPNLAALAARGVYARPLTSVfpSTTA-PAHTTL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598824 92 LTGRLGLRNGVTRNF--------AVTSVGGLP--------LNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPN----FR 151
Cdd:COG1524 76 LTGLYPGEHGIVGNGwydpelgrVVNSLSWVEdgfgsnslLPVPTIFERARAAGLTTAAVFWPSFEGSGLIDAArpypYD 155
|
170
....*....|.
gi 1034598824 152 GFDYYFGIPYS 162
Cdd:COG1524 156 GRKPLLGNPAA 166
|
|
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