|
Name |
Accession |
Description |
Interval |
E-value |
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
35-469 |
0e+00 |
|
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: 656.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 35 KPNFVIILADDMGWGDLGANWAET-KDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGG 113
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNaILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 194 dcytdvalplyenlniveqpvnlSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQLPAAP-RGRSLYGAG 272
Cdd:cd16161 132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPtSGRGPYGDA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 273 LWEMDSLVGQIKDKVDH-TVKENTFLWFTGDNGPWAQKCELAgsVGPFTGFWQTRQGGSPAKQTTWEGGHRVPALAYWPG 351
Cdd:cd16161 189 LQEMDDLVGQIMDAVKHaGLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 352 RVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGeFGALQTVRLERYKAF 431
Cdd:cd16161 267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAH 345
|
410 420 430
....*....|....*....|....*....|....*...
gi 45430057 432 YITGGARACDGSTGPELQHKFPLIFNLEDDTAEAVPLE 469
Cdd:cd16161 346 YATGGALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT 383
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-468 |
0e+00 |
|
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: 524.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRN-FAVTSVGG 113
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDMGCTDTPGYNHPPCPAcpqgdgpsrnlqr 193
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 194 dcytdvalPLYENLNIVEQPVNLSSLAQKYAEKATQFIQRAstSGRPFLLYVALAHMHVPLPVTQLPAAPRGRSLYGAGL 273
Cdd:cd16026 148 --------PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 274 WEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRVPALAYWPGR 352
Cdd:cd16026 218 EELDWSVGRILDALKELgLEENTLVIFTSDNGPWLEYGGHGGSAGPLRG----------GKGTTWEGGVRVPFIAWWPGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 353 VPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQ-PGHRVLFHPNSgaagefGALQTVRLERYKAF 431
Cdd:cd16026 288 IPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKsPPHPFFYYYDG------GDLQAVRSGRWKLH 361
|
410 420 430
....*....|....*....|....*....|....*..
gi 45430057 432 YITGGARACDGSTGPELQHKFPLIFNLEDDTAEAVPL 468
Cdd:cd16026 362 LPTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGETYNV 398
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
35-522 |
3.41e-120 |
|
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: 361.76 E-value: 3.41e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRN-FAVTSVGG 113
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGvFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 114 LPLNETTLAEVLQQAGYVTGIIGKWHL--GHHGSYHPNFRGFDYYFGIPYSHDMG-CTD-TPGYNHPPC-PACPQGDGPs 188
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLgvGLNGTYLPTHQGFDHYLGIPYSHDQGpCQNlTCFPPNIPCfGGCDQGEVP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 189 rnlqrdcytdvaLPLYENLNIVEQPVNLSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQLPAAPRGRSL 268
Cdd:cd16158 160 ------------CPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 269 YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFtgfwqtRQGgspaKQTTWEGGHRVPALA 347
Cdd:cd16158 228 FGDALAELDGSVGELLQTLKENgIDNNTLVFFTSDNGPSTMRKSRGGNAGLL------KCG----KGTTYEGGVREPAIA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 348 YWPGRVPVNVTStALLSVLDIFPTVVALAQASLPQgRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGEFGALqTVRLER 427
Cdd:cd16158 298 YWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLPN-VTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVF-AVRWGK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 428 YKAFYITGGA--------RACDGSTgPELQHKFPLIFNLEDDTAEAVPLErGGAEYQAVLPEVRKVLADVLQDIANDNiS 499
Cdd:cd16158 375 YKAHFYTQGAahsgttpdKDCHPSA-ELTSHDPPLLFDLSQDPSENYNLL-GLPEYNQVLKQIQQVKERFEASMKFGE-S 451
|
490 500
....*....|....*....|....*..
gi 45430057 500 SADYTQDPSVTPCCN----PYQIACRC 522
Cdd:cd16158 452 EINKGEDPALEPCCKpgctPKPSCCQC 478
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
35-487 |
1.75e-113 |
|
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: 343.64 E-value: 1.75e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV---TRNFAVTSV 111
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 112 GGLPLNETTLAEVLQQAGYVTGIIGKWHLG-----HHGSYH-PNFRGFDYY-FGIPYSHDMGCTDTPGYNhppcpacpqg 184
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDFVgTNLPFTNSWACDDTGRHV---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 185 DGPSRNLqrdCYtdvalpLYENLNIVEQPVNLSSLAQKYAEKATQFIQraSTSGRPFLLYVALAHMHVPLPVTQLPAAPR 264
Cdd:cd16160 151 DFPDRSA---CF------LYYNDTIVEQPIQHEHLTETLVGDAKSFIE--DNQENPFFLYFSFPQTHTPLFASKRFKGKS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 265 GRSLYGAGLWEMDSLVGQIKDK-VDHTVKENTFLWFTGDNGPWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRV 343
Cdd:cd16160 220 KRGRYGDNINEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKG----------GKGNSWEGGIRV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 344 PALAYWPGRVPVNVtSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQ-PGHRVLFHPNSgaagefgALQT 422
Cdd:cd16160 290 PFIAYWPGTIKPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADsPHDDILYYCCS-------RLMA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 423 VRLERYKAFYITG--------GARACDGSTGPEL------------QHKFPLIFNLEDDTAEAVPLERGGAEYqaVLPEV 482
Cdd:cd16160 362 VRYGSYKIHFKTQplpsqeslDPNCDGGGPLSDYivcydcedecvtKHNPPLIFDVEKDPGEQYPLQPSVYEH--MLEAV 439
|
....*
gi 45430057 483 RKVLA 487
Cdd:cd16160 440 EKLIA 444
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-488 |
1.23e-104 |
|
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: 321.34 E-value: 1.23e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG--VTRNFAVTS-- 110
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 111 ----VGGLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHdMGCTDTPGYNHPPcpacpqgdg 186
Cdd:cd16157 81 pqniVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCH-FGPYDNKAYPNIP--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 187 psrnLQRDcyTDVALPLYENLNIvEQPVNLSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQLPAAPRGR 266
Cdd:cd16157 151 ----VYRD--WEMIGRYYEEFKI-DKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 267 SLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNG-PWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRVP 344
Cdd:cd16157 224 GLYGDAVMELDSSVGKILESLKSLgIENNTFVFFSSDNGaALISAPEQGGSNGPFLC----------GKQTTFEGGMREP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 345 ALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSgaagefgALQTVR 424
Cdd:cd16157 294 AIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGD-------ELMAVR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 425 LERYKAFYIT---------GGARACDG------STGPELQH-KFPLIFNLEDDTAEAVPLERGGAEYQAVLPEVRKVLAD 488
Cdd:cd16157 367 LGQYKAHFWTwsnsweefrKGINFCPGqnvpgvTTHNQTDHtKLPLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVVQQ 446
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
35-494 |
6.96e-101 |
|
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: 313.46 E-value: 6.96e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGR------LGLRNGVTRNFAV 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRypirsgMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 109 TSVGGLPLNETTLAEVLQQAGYVTGIIGKWHLGHH------GSYHPNFRGFDYYFGIPYSHDMGCTDTPG--YNHPPCPA 180
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHcesrndFCHHPLNHGFDYFYGLPLTNLKDCGDGSNgeYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 181 CPQgdgpSRNLQRDCYTDVALPLY--------------------------------------ENLNIVEQPVNLSSLAQK 222
Cdd:cd16159 161 FPL----LTAFVLITALTIFLLLYlgavskrffvfllilsllfislfflllitnryfncilmRNHEVVEQPMSLENLTQR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 223 YAEKATQFIQRasTSGRPFLLYVALAHMHvplpvTQLPAAP--RGRS---LYGAGLWEMDSLVGQIKDKVDHT-VKENTF 296
Cdd:cd16159 237 LTKEAISFLER--NKERPFLLVMSFLHVH-----TALFTSKkfKGRSkhgRYGDNVEEMDWSVGQILDALDELgLKDNTF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 297 LWFTGDNGPWAqkcELAGSVGPFTGFWQTRQGGSpaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALA 376
Cdd:cd16159 310 VYFTSDNGGHL---EEISVGGEYGGGNGGIYGGK--KMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 377 QASLPQGRRFDGVDVSEVLFGRSQ-PGHRVLFH------------PNSGAAgefgalqtvrleRYKAFYIT-----GGAR 438
Cdd:cd16159 385 GAPLPSDRIIDGRDLMPLLTGQEKrSPHEFLFHycgaelhavryrPRDGGA------------VWKAHYFTpnfypGTEG 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45430057 439 A-------CDGSTGpeLQHKFPLIFNLEDDTAEAVPLERGGAEYQAVLPEVRKVLADVLQDIA 494
Cdd:cd16159 453 CcgtllcrCFGDSV--THHDPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIE 513
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-470 |
1.63e-93 |
|
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: 289.43 E-value: 1.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGAN---WAETKDTANLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTRNFAVTSVG 112
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYgggIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 113 GLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHdmgctdtpgynhppcpacpqgdgpsrnlq 192
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYHT----------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 193 rdcytdvalplyenlniveqpvnlssLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVP-LPVTQLPAAPRGRSLYGA 271
Cdd:cd16142 131 --------------------------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPtLPSPEFEGKSSGKGKYAD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 272 GLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSvGPFTGfwqtrqggspAKQTTWEGGHRVPALAYWP 350
Cdd:cd16142 185 SMVELDDHVGQILDALDELgIADNTIVIFTTDNGPEQDVWPDGGY-TPFRG----------EKGTTWEGGVRVPAIVRWP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 351 GRVPVNVTSTALLSVLDIFPTVVALAQASLP------QGRRFDGVDVSEVLFGRS-QPGHRVLFHpnsGAAGEFGAlqtV 423
Cdd:cd16142 254 GKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSeKSRRSEFFY---FGEGELGA---V 327
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 45430057 424 RLERYKA-FYITGGARAcdGSTGPELQHKFPLIFNLEDDtaeavPLER 470
Cdd:cd16142 328 RWKNWKVhFKAQEDTGG--PTGEPFYVLTFPLIFNLRRD-----PKER 368
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
34-497 |
4.88e-89 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 278.69 E-value: 4.88e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvTSVGG 113
Cdd:COG3119 22 KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE-GYNGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 114 LPLNETTLAEVLQQAGYVTGIIGKWHLghhgsyhpnfrgfdyyfgipYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:COG3119 101 LPPDEPTLAELLKEAGYRTALFGKWHL--------------------YLTD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 194 dcytdvalplyenlniveqpvnlsslaqKYAEKATQFIQRASTSGRPFLLYVALAHMHVP-----------------LPV 256
Cdd:COG3119 132 ----------------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPyqapeeyldkydgkdipLPP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 257 TQLPAA------PRGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAqkcelagsvgpftGFWQTRQGg 329
Cdd:COG3119 184 NLAPRDlteeelRRARAAYAAMIEEVDDQVGRLLDALEELgLADNTIVVFTSDNGPSL-------------GEHGLRGG- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 330 spaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHRVLFHp 409
Cdd:COG3119 250 ---KGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYW- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 410 nsgAAGEFGALQTVRLERYKAFYITGGARAcdgstgPELqhkfpliFNLEDDTAEAVPLergGAEYqavlPEVRKVLADV 489
Cdd:COG3119 324 ---EYPRGGGNRAIRTGRWKLIRYYDDDGP------WEL-------YDLKNDPGETNNL---AADY----PEVVAELRAL 380
|
....*...
gi 45430057 490 LQDIANDN 497
Cdd:COG3119 381 LEAWLKEL 388
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-492 |
1.35e-84 |
|
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: 268.26 E-value: 1.35e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTG----RLGL---------RNGV 102
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGqypaRLGItdvipgrrgPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 103 TRNFAVTSVGGLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGI-PYSHDMGCTDTPGYNHPPCPAC 181
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIGGtGNGGPPSYYFPPGKPNPDLEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 182 PQGDgpsrnlqrdcytdvalplyenlniveqpvnlsSLAQKYAEKATQFIQRAstSGRPFLLYvaLAH--MHVPLPVTQ- 258
Cdd:cd16144 161 PEGE--------------------------------YLTDRLTDEAIDFIEQN--KDKPFFLY--LSHyaVHTPIQARPe 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 259 -------LPAAPRGR---SLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFtgfwqtRQ 327
Cdd:cd16144 205 liekyekKKKGLRKGqknPVYAAMIESLDESVGRILDALEELgLADNTLVIFTSDNGGLSTRGGPPTSNAPL------RG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 328 GgspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHR--V 405
Cdd:cd16144 279 G----KGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRraL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 406 LFH-PN-SGAAGEFGAlqTVRLERYK--AFYITGgaracdgstGPELqhkfpliFNLEDDTAEAVPLerggAEYQavlPE 481
Cdd:cd16144 355 FWHfPHyHGQGGRPAS--AIRKGDWKliEFYEDG---------RVEL-------YNLKNDIGETNNL----AAEM---PE 409
|
490
....*....|.
gi 45430057 482 VRKVLADVLQD 492
Cdd:cd16144 410 KAAELKKKLDA 420
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-464 |
3.23e-83 |
|
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: 263.68 E-value: 3.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETK-DTANLDKMASEGMRFVDFHAAASTCSPSRASLLTG----RLGLRNGVTRNFavts 110
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGrypwRSRLKGGVLGGF---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 111 vgGLPL---NETTLAEVLQQAGYVTGIIGKWHLG-----------HHGSYH-----------PNFRGFDYYFGIPYShdm 165
Cdd:cd16143 77 --SPPLiepDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkaATGTGKdvdyskpikggPLDHGFDYYFGIPAS--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 166 gctdtpgynhppcpacpqgdgpsrnlqrdcytDVaLPLyenlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYV 245
Cdd:cd16143 152 --------------------------------EV-LPT-------------------LTDKAVEFIDQHAKKDKPFFLYF 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 246 ALAHMHVPLpvtqLPAAP-RGRS---LYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGPwaqkcelagsvGPFT 320
Cdd:cd16143 180 ALPAPHTPI----VPSPEfQGKSgagPYGDFVYELDWVVGRILDALKeLGLAENTLVIFTSDNGP-----------SPYA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 321 GFWQT-RQGGSPA------KQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSE 393
Cdd:cd16143 245 DYKELeKFGHDPSgplrgmKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLP 324
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45430057 394 VLFGRSQPGHRV-LFHpnSGAAGEFgalqTVRLERYKAFYITGGARACDGSTGPELQHKFPLIFNLEDDTAE 464
Cdd:cd16143 325 ALLGPKKQEVREsLVH--HSGNGSF----AIRKGDWKLIDGTGSGGFSYPRGKEKLGLPPGQLYNLSTDPGE 390
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-464 |
5.50e-80 |
|
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: 255.98 E-value: 5.50e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGGLP 115
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 116 LNETTLAEVLQQAGYVTGIIGKWHLGHHGSY-HPNFRGFDYYFGIpYSHdmgctdTPGYNHPPcpacPQGDgpsRNLQRd 194
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYGY-LDQ------VHAHNYYP----EYLW---RNGEK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 195 cytdvaLPLYENLNIVEQPVNLSSLAQK-YAE-----KATQFIQRAstSGRPFLLYVALAHMHVPLPVTQLPAA---PRG 265
Cdd:cd16145 146 ------VPLPNNVIPPLDEGNNAGGGGGtYSHdlftdEALDFIREN--KDKPFFLYLAYTLPHAPLQVPDDGPYkykPKD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 266 RSLYGAGLWE------------MDSLVGQIKDKV-DHTVKENTFLWFTGDNGP-----WAQKCELAGSVGPFTGFwqtrq 327
Cdd:cd16145 218 PGIYAYLPWPqpekayaamvtrLDRDVGRILALLkELGIDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 328 ggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPG-HRVL 406
Cdd:cd16145 293 -----KRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPE--DIDGISLLPTLLGKPQQQqHDYL 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 45430057 407 FHpnsgAAGEFGALQTVRLERYKAFYItggaracDGSTGP-ELqhkfpliFNLEDDTAE 464
Cdd:cd16145 366 YW----EFYEGGGAQAVRMGGWKAVRH-------GKKDGPfEL-------YDLSTDPGE 406
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
36-407 |
1.76e-76 |
|
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: 246.69 E-value: 1.76e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTRnfavTSVGG-- 113
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWH----TILGRer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgcTDTPGYnhppcpacpqgdgpsrnLQR 193
Cdd:cd16146 76 MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGGGI---GQYPDY-----------------WGN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 194 DCYTDValpLYENlNIVEQpvnlsslAQKYA-----EKATQFIQRASTsgRPFLLYVALAHMHVPLPVTQLPAAP----- 263
Cdd:cd16146 136 DYFDDT---YYHN-GKFVK-------TEGYCtdvffDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPykdmg 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 264 --RGRSLYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGPWaqkcelAGSVGPFTGFWQtrqgGSpaKQTTWEGG 340
Cdd:cd16146 203 ldDKLAAFYGMIENIDDNVGRLLAKLKeLGLEENTIVIFMSDNGPA------GGVPKRFNAGMR----GK--KGSVYEGG 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45430057 341 HRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQP-GHRVLF 407
Cdd:cd16146 271 HRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPwPERTLF 338
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
36-390 |
2.73e-68 |
|
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: 219.62 E-value: 2.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNfaVTSVGGLP 115
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 116 LNETTLAEVLQQAGYVTGIIGKWHlghhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsrnlqrdc 195
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 196 ytdvalplyenlniveqpvnlsslaqkyaEKATQFIQRASTSgRPFLLYVALAHMHVPLpvtqlpaaprgrsLYGAGLWE 275
Cdd:cd16022 103 -----------------------------DEAIDFIERRDKD-KPFFLYVSFNAPHPPF-------------AYYAMVSA 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 276 MDSLVGQIKDKVDHT-VKENTFLWFTGDNgpwaqkcelagsvGPFTGFWQTRQGgspaKQTTWEGGHRVPALAYWPGRVP 354
Cdd:cd16022 140 IDDQIGRILDALEELgLLDNTLIVFTSDH-------------GDMLGDHGLRGK----KGSLYEGGIRVPFIVRWPGKIP 202
|
330 340 350
....*....|....*....|....*....|....*.
gi 45430057 355 VNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVD 390
Cdd:cd16022 203 AGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
36-470 |
2.39e-67 |
|
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: 222.43 E-value: 2.39e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFvDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSV-GGL 114
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVIL-NNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEpYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 115 PLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYH-PNFRGFDYYFGiPYShdmGCTDtpGYNHPPCPACP------QGDGP 187
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYTWEYtPTNRGFDSFYG-YYG---GAED--YYTHTSGGANDygnddlRDNEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 188 SRNLQRDCY-TDValplyenlniveqpvnlsslaqkYAEKATQFIQRASTSgRPFLLYVALAHMHVPLPVTQLPAAP--- 263
Cdd:cd16029 154 PAWDYNGTYsTDL-----------------------FTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPyed 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 264 -------RGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCElAGSVGPFTGfwqtrqggspAKQT 335
Cdd:cd16029 210 kfahikdEDRRTYAAMVSALDESVGNVVDALKAKgMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRG----------GKNT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 336 TWEGGHRVPALAYWPGRVPV-NVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHR-VLFHPNSGA 413
Cdd:cd16029 279 LWEGGVRVPAFVWSPLLPPKrGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTeILLNIDDIT 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 45430057 414 AGEFGAlqTVRLERYKafYITGgaracdgstgpelqhkFPLiFNLEDDtaeavPLER 470
Cdd:cd16029 359 RTTGGA--AIRVGDWK--LIVG----------------KPL-FNIEND-----PCER 389
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-435 |
7.49e-63 |
|
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: 210.15 E-value: 7.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTRnfavtsvGGLP 115
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPL-CTPSRVQLMTGKYNFRNYVVF-------GYLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 116 LNETTLAEVLQQAGYVTGIIGKWHLG---HHGSYHPNFrGFDYY--FGipyshdmGCTDTPGYNHPPCPACPQGDGPSRN 190
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGKWQLGggrGDGDYPHEF-GFDEYclWQ-------LTETGEKYSRPATPTFNIRNGKLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 191 LQRDCY-TDValplyenlniveqpvnlsslaqkYAEKATQFIQRAstSGRPFLLY--VALAH-MHVPLPVTQLPAAPRGR 266
Cdd:cd16151 145 TTEGDYgPDL-----------------------FADFLIDFIERN--KDQPFFAYypMVLVHdPFVPTPDSPDWDPDDKR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 267 S-----LYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNgpwaqkcelaGSVGPFTGFW--QTRQGGspaKQTTWE 338
Cdd:cd16151 200 KkddpeYFPDMVAYMDKLVGKLVDKLEELgLRENTIIIFTGDN----------GTHRPITSRTngREVRGG---KGKTTD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 339 GGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGEFG 418
Cdd:cd16151 267 AGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWYYRNPHKKF 346
|
410
....*....|....*..
gi 45430057 419 ALQTVRLERYKaFYITG 435
Cdd:cd16151 347 GSRFVRTKRYK-LYADG 362
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
36-378 |
8.41e-56 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 188.79 E-value: 8.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrnfaVTSVGGLP 115
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSY----VSTPVGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 116 LNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFG-IPYSHDMGCTDTPGYNHPPcpacpqgdgpsrnlqRD 194
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLYADPPDVPYNCSG---------------GG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 195 CYTDValplyenlniveqpvnlsslaqkYAEKATQFIQRAStsgRPFLLYVALAHMHVPLPVTQLPAAP----------- 263
Cdd:pfam00884 142 VSDEA-----------------------LLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscse 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 264 -RGRSLYGAGLWEMDSLVGQIKDKV-DHTVKENTFLWFTGDNGPwaqkcelagSVGPFTGFWQTRQGGspakqTTWEGGH 341
Cdd:pfam00884 196 eQLLNSYDNTLLYTDDAIGRVLDKLeENGLLDNTLVVYTSDHGE---------SLGEGGGYLHGGKYD-----NAPEGGY 261
|
330 340 350
....*....|....*....|....*....|....*..
gi 45430057 342 RVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQA 378
Cdd:pfam00884 262 RVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
34-468 |
2.06e-54 |
|
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: 188.42 E-value: 2.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 34 QKPNFVIILADDMGWGDLGANWAETkDTANLDKMASEGMRFVDFHAAAsTCSPSRASLLTGRLGLRNGVtRNFAVTSVGG 113
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEI-PTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 114 ------LPLNETTLAEVLQQAGYVTGIIGKWHLGHHgsyhpnfrgfDYYFgipySHDmgctdtpgynhppcpacpqgdgp 187
Cdd:cd16025 78 pgyegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------DYYS----TDD----------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 188 srnlqrdcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYVALAHMHVPL------------- 254
Cdd:cd16025 121 -----------------------------------LTDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLqapkewidkykgk 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 255 -----------------------PVTQLPAAPRG-----------RSLYG------AGLWE-MDSLVGQIKDKVDHT-VK 292
Cdd:cd16025 166 ydagwdalreerlerqkelglipADTKLTPRPPGvpawdslspeeKKLEArrmevyAAMVEhMDQQIGRLIDYLKELgEL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 293 ENTFLWFTGDNGP-----WAQkcelAGSvGPFTGFwqtrqggspaKQTTWEGGHRVPALAYWPGRV-PVNVTSTALLSVL 366
Cdd:cd16025 246 DNTLIIFLSDNGAsaepgWAN----ASN-TPFRLY----------KQASHEGGIRTPLIVSWPKGIkAKGGIRHQFAHVI 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 367 DIFPTVVALAQASLPQGRR------FDGVDVSEVLFGRSQPG-HRVLFHPNSGAAGefgalqtVRLERYKAFYITGGAra 439
Cdd:cd16025 311 DIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSrRRTQYFELFGNRA-------IRKGGWKAVALHPPP-- 381
|
490 500
....*....|....*....|....*....
gi 45430057 440 cDGSTGPELqhkfpliFNLEDDTAEAVPL 468
Cdd:cd16025 382 -GWGDQWEL-------YDLAKDPSETHDL 402
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
36-433 |
5.11e-51 |
|
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: 178.47 E-value: 5.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGA--NWAETkdtANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFavTSVGG 113
Cdd:cd16027 1 PNILWIIADDLSPDLGGYggNVVKT---PNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR--SRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAWD----------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 194 dcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQRAStSGRPFLLYVALAHMH-----------------VPLPv 256
Cdd:cd16027 127 -----------------------------YASNAADFLNRAK-KGQPFFLWFGFHDPHrpyppgdgeepgydpekVKVP- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 257 TQLPAAPRGR---SLYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGpwaqkcelagsvGPFTGfwqtrqggspA 332
Cdd:cd16027 176 PYLPDTPEVRedlADYYDEIERLDQQVGEILDELEeDGLLDNTIVIFTSDHG------------MPFPR----------A 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 333 KQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHRVLF----- 407
Cdd:cd16027 234 KGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGRDYVFaerdr 311
|
410 420
....*....|....*....|....*..
gi 45430057 408 HpnsgaaGEFGALQ-TVRLERYKafYI 433
Cdd:cd16027 312 H------DETYDPIrSVRTGRYK--YI 330
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-461 |
1.34e-49 |
|
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: 175.45 E-value: 1.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVtsvggL 114
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 115 PLNETTLAEVLQQAGYVTGIIGKWHL-GHHGSYH--------PNFR-GFDYYFGipyshdMGCTDtpGYNHPPCpacpQG 184
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGraddytppPERRhGFDYWKG------YECNH--DHNNPHY----YD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 185 DGPSRNlQRDCYTDVALplyenlniveqpvnlsslaqkyAEKATQFIQRASTSGRPFLLYVALAHMHVP----------- 253
Cdd:cd16034 144 DDGKRI-YIKGYSPDAE----------------------TDLAIEYLENQADKDKPFALVLSWNPPHDPyttapeeyldm 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 254 -----------LPVTQLPAAPRGRSL---YGA--GLwemDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSV 316
Cdd:cd16034 201 ydpkklllrpnVPEDKKEEAGLREDLrgyYAMitAL---DDNIGRLLDALKELgLLENTIVVFTSDHG------DMLGSH 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 317 GPFtgfwqtrqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLF 396
Cdd:cd16034 272 GLM------------NKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLL 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 397 GRSQPGHR----VLFHPNSG-AAGEFGALQTVRLERYKafYitggarACDGSTGpelqhkfPLIFNLEDD 461
Cdd:cd16034 338 GGKDDEPDsvllQCFVPFGGgSARDGGEWRGVRTDRYT--Y------VRDKNGP-------WLLFDNEKD 392
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
34-484 |
3.97e-44 |
|
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: 161.54 E-value: 3.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvGG 113
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG----PL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGsYHPNfRGFDYYFGIPyshdmgctdtpgynhppcpacPQGDgpsrnlqr 193
Cdd:cd16031 77 FDASQPTYPKLLRKAGYQTAFIGKWHLGSGG-DLPP-PGFDYWVSFP---------------------GQGS-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 194 dcYTDvaLPLYENLNIVEQPVNLSSLaqkYAEKATQFIQRAStSGRPFLLYV-----------ALAHMHV------PLPV 256
Cdd:cd16031 126 --YYD--PEFIENGKRVGQKGYVTDI---ITDKALDFLKERD-KDKPFCLSLsfkaphrpftpAPRHRGLyedvtiPEPE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 257 TQLPA--APRGRSL---------------------------YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpw 306
Cdd:cd16031 198 TFDDDdyAGRPEWAreqrnrirgvldgrfdtpekyqrymkdYLRTVTGVDDNVGRILDYLEEQgLADNTIIIYTSDNG-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 307 aqkcELAGSVGpFTGfwqtrqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPqgRRF 386
Cdd:cd16031 276 ----FFLGEHG-LFD-----------KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIP--EDM 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 387 DGVDVSEVLFGRSQPGHR------VLFHPNS-GAAGEFGalqtVRLERYKAFYITGGARAcdgstgPELqhkfpliFNLE 459
Cdd:cd16031 338 QGRSLLPLLEGEKPVDWRkefyyeYYEEPNFhNVPTHEG----VRTERYKYIYYYGVWDE------EEL-------YDLK 400
|
490 500
....*....|....*....|....*....
gi 45430057 460 DDtaeavPLER----GGAEYQAVLPEVRK 484
Cdd:cd16031 401 KD-----PLELnnlaNDPEYAEVLKELRK 424
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-388 |
1.07e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 150.08 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV-----TRNFAVTS 110
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 111 VG-GLPLNETTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd16149 81 KPeGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 190 nlqrdcytdvalplyenlniveqpvnlsslaqkyaEKATQFIQRASTSGRPFLLYVAlahmhvplpvTQLPAAPRGrslY 269
Cdd:cd16149 113 -----------------------------------DDAADFLRRRAEAEKPFFLSVN----------YTAPHSPWG---Y 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 270 GAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcelagsvgpFT----GFWQTRQGGSPakQTTWEGGHRVP 344
Cdd:cd16149 145 FAAVTGVDRNVGRLLDELEELgLTENTLVIFTSDNG--------------FNmghhGIWGKGNGTFP--LNMYDNSVKVP 208
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 45430057 345 ALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDG 388
Cdd:cd16149 209 FIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPG 252
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-439 |
6.10e-38 |
|
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: 143.26 E-value: 6.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWgDLGANWAETKD---TANLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTrnfavtSVG 112
Cdd:cd16154 1 PNILLIIADDQGL-DSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVL------AVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 113 G-LPLNETTL--AEVLQQ--AGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIpyshdMGctdtpgynhppcpacpqGDGP 187
Cdd:cd16154 73 DeLLLSEETLlqLLIKDAttAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGI-----LG-----------------GGVQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 188 SrnlqrdcYTDVALplyeNLNIVEQPVN------LSSLAQKYAEKATQfiqrastsgrPFLLYVALAHMHVPLpvtQLPA 261
Cdd:cd16154 131 D-------YYNWNL----TNNGQTTNSTeyattkLTNLAIDWIDQQTK----------PWFLWLAYNAPHTPF---HLPP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 262 A---PRG------------RSLYGAGLWEMDSLVGQIKDKVDHTVKENTFLWFTGDNG-PwaqkcelagsvGPFTGFWQT 325
Cdd:cd16154 187 AelhSRSllgdsadieanpRPYYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGtP-----------GQVVDLPYT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 326 RQGgspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPGHRV 405
Cdd:cd16154 256 RNH---AKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNASTRQY 330
|
410 420 430
....*....|....*....|....*....|....
gi 45430057 406 LFHPNSGAAGEFGAlqtVRLERYKAFYITGGARA 439
Cdd:cd16154 331 NYTEYESPTTTGWA---TRNQYYKLIESENGQEE 361
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
35-388 |
6.14e-35 |
|
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: 135.37 E-value: 6.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 35 KPNFVIILADDMGWgDLGANWAETKdTANLdkMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtSVGGL 114
Cdd:cd16147 1 RPNIVLILTDDQDV-ELGSMDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSP--PGGGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 115 P------LNETTLAEVLQQAGYVTGIIGK----WHLGHHGSYHPnfRGFDYYFGI-------PYSHDMGCTDTPGYNHPp 177
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYVP--PGWDEWDGLvgnstyyNYTLSNGGNGKHGVSYP- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 178 cpacpqgdgpsrnlqRDCYTDValplyenlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYVA----------- 246
Cdd:cd16147 152 ---------------GDYLTDV-----------------------IANKALDFLRRAAADDKPFFLVVAppaphgpftpa 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 247 --LAHMHVPLPVT------------------QLPAAP-----------RGRslygaglWE----MDSLVGQIKDKVDHT- 290
Cdd:cd16147 194 prYANLFPNVTAPprpppnnpdvsdkphwlrRLPPLNptqiayidelyRKR-------LRtlqsVDDLVERLVNTLEATg 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 291 VKENTFLWFTGDNgpwaqkcelagsvgpftGFW--QTRQGgsPAKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDI 368
Cdd:cd16147 267 QLDNTYIIYTSDN-----------------GYHlgQHRLP--PGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDL 326
|
410 420
....*....|....*....|
gi 45430057 369 FPTVVALAQASLPqgRRFDG 388
Cdd:cd16147 327 APTILDLAGAPPP--SDMDG 344
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-491 |
1.32e-34 |
|
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: 134.66 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNF--AVTSVGG 113
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSyhPNFRGFDYYFgiPYSH-------DMGC--------TDTP-----GY 173
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVGPEET--PLDYGFDEYL--PVETtieyflaDRAIemleelaaDDKPfflrvNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 174 NHPPCPACPqgdgPSRNLqrDCYTDVALPLYENLNiveqpvnlSSLAQK---YAEKATQFIQRASTSG--RPfllyvALA 248
Cdd:cd16033 157 WGPHDPYIP----PEPYL--DMYDPEDIPLPESFA--------DDFEDKpyiYRRERKRWGVDTEDEEdwKE-----IIA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 249 HmhvplpvtqlpaaprgrslYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGPFTgfwqtrQ 327
Cdd:cd16033 218 H-------------------YWGYITLIDDAIGRILDALEELgLADDTLVIFTSDHG------DALGAHRLWD------K 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 328 GGSPAKQTtweggHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGRSQPGHR--V 405
Cdd:cd16033 267 GPFMYEET-----YRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVP--PKVDGRSLLPLLRGEQPEDWRdeV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 406 L--FHPNsgaagEFGALQT-VRLERYKafYItggaraCDGSTGPELqhkfpliFNLEDDTAEAVPLeRGGAEYQAVLPEV 482
Cdd:cd16033 340 VteYNGH-----EFYLPQRmVRTDRYK--YV------FNGFDIDEL-------YDLESDPYELNNL-IDDPEYEEILREM 398
|
....*....
gi 45430057 483 RKVLADVLQ 491
Cdd:cd16033 399 RTRLYEWME 407
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
31-492 |
2.44e-33 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 132.49 E-value: 2.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 31 TRGQKPNFVIILADDMGwGD-LGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNGV 102
Cdd:PRK13759 2 VQTKKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 103 TRNFavtsvgglplnETTLAEVLQQAGYVTGIIGKWHlghhgsYHP--NFRGFD--------YYFGIPYSH---DMgCTD 169
Cdd:PRK13759 81 PWNY-----------KNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHnvllhdgyLHSGRNEDKsqfDF-VSD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 170 --------TPGYNhppcpACPQGDGpsrnlqRDCYTDVALP--LYENLNiveqPVNLSslaqkyAEKATQFIQRAStSGR 239
Cdd:PRK13759 143 ylawlrekAPGKD-----PDLTDIG------WDCNSWVARPwdLEERLH----PTNWV------GSESIEFLRRRD-PTK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 240 PFLLYVALAHMHVPL--PV--------TQLPAAPRGRSLYGAGLW----EMDSLVGQIKDK---------------VDH- 289
Cdd:PRK13759 201 PFFLKMSFARPHSPYdpPKryfdmykdADIPDPHIGDWEYAEDQDpeggSIDALRGNLGEEyarraraayyglithIDHq 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 290 ------TVKE-----NTFLWFTGDNGpwaqkcELAGSVGPFTgfwqtrqggspaKQTTWEGGHRVPALAYWPG---RVPV 355
Cdd:PRK13759 281 igrflqALKEfglldNTIILFVSDHG------DMLGDHYLFR------------KGYPYEGSAHIPFIIYDPGgllAGNR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 356 NVTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGrSQPGHRVLFHpnsgaaGEFGALqtvrlerYKAF-YIT 434
Cdd:PRK13759 343 GTVIDQVVELRDIMPTLLDLAGGTIP--DDVDGRSLKNLIFG-QYEGWRPYLH------GEHALG-------YSSDnYLT 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45430057 435 GGaracdgstgpelQHKF--------PLIFNLEDDTAEAVPLErGGAEYQAVLPEVRKVLADVLQD 492
Cdd:PRK13759 407 DG------------KWKYiwfsqtgeEQLFDLKKDPHELHNLS-PSEKYQPRLREMRKKLVDHLRG 459
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-486 |
6.20e-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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 129.22 E-value: 6.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAAST----CSPSRASLLTGRLGLRNGVTRNFAvt 109
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFHAPEGGKAA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 110 svggLPLNETTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd16155 79 ----IPSDDKTWPETFKKAGYRTFATGKWHNG------------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 190 nlqrdcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYVALAHMH-----------------V 252
Cdd:cd16155 107 ---------------------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHdprqappeyldmyppetI 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 253 PLPVTQLPAAP------------------------RGRSLYGAGLWEMDSLVGQIKDKVDHTVK-ENTFLWFTGDNGpwa 307
Cdd:cd16155 154 PLPENFLPQHPfdngegtvrdeqlapfprtpeavrQHLAEYYAMITHLDAQIGRILDALEASGElDNTIIVFTSDHG--- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 308 qkceLAgsVGpftgfwqtrQGGSPAKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFD 387
Cdd:cd16155 231 ----LA--VG---------SHGLMGKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES--VE 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 388 GVDVSEVLFGRSQPGHRVLFhpnsgaaGEFGALQ-TVRLERYKAFYITGGAracdgstgpelqhKFPLIFNLEDDTAEAV 466
Cdd:cd16155 293 GKSLLPVIRGEKKAVRDTLY-------GAYRDGQrAIRDDRWKLIIYVPGV-------------KRTQLFDLKKDPDELN 352
|
490 500
....*....|....*....|
gi 45430057 467 PLErGGAEYQAVLPEVRKVL 486
Cdd:cd16155 353 NLA-DEPEYQERLKKLLAEL 371
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
402-522 |
1.36e-32 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 120.88 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 402 GHRVLFHpNSGAAgefgaLQTVRLERYKAFYITG-----GARACDGSTGPELQHKFPLIFNLEDDTAEAVPLERGGAEYQ 476
Cdd:pfam14707 2 PHEFLFH-YCGAA-----LHAVRWGPYKAHFFTPsfdppGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYP 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 45430057 477 AVLPEVRKVLADVLQDI--ANDNISSADYTQDPSVTPCCnPYQIACRC 522
Cdd:pfam14707 76 EVLAEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-390 |
3.07e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 113.41 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILAD----DMgwgdLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrnfavtsV 111
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW-------G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 112 GGLPLNETTLAEVLQQAGYVTGIIGKWhlgHHGSYHPNF-RGFDYYFGIPYSHdmgcTDTPGYNHPPCPACpqgdgpsrn 190
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAVSSN---PHLFGGPGFdRGFDTFEDFRGQE----GDPGEEGDERAERV--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 191 lqrdcyTDVALplyenlniveqpvnlsslaqkyaekatQFIQRASTSgRPFLLYValaHMHvplpvtqlpaAPRGRSLYG 270
Cdd:cd16148 134 ------TDRAL---------------------------EWLDRNADD-DPFFLFL---HYF----------DPHEPYLYD 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 271 AGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGpwaqkcELAGSVGPFTGFWqtrqggspakQTTWEGGHRVPALAYW 349
Cdd:cd16148 167 AEVRYVDEQIGRLLDKLKeLGLLEDTLVIVTSDHG------EEFGEHGLYWGHG----------SNLYDEQLHVPLIIRW 230
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 45430057 350 PGRVPVNVTStALLSVLDIFPTVVALAQASLPqgRRFDGVD 390
Cdd:cd16148 231 PGKEPGKRVD-ALVSHIDIAPTLLDLLGVEPP--DYSDGRS 268
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-461 |
2.49e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 112.25 E-value: 2.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVtsvggLP 115
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP-----YD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 116 LNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHpnfrGFDYyfgipyshDMGCTDTpgynhppcpacpqgdgpsrnlqrdc 195
Cdd:cd16037 76 GDVPSWGHALRAAGYETVLIGKLHFRGEDQRH----GFRY--------DRDVTEA------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 196 ytdvalplyenlniveqpvnlsslaqkyaekATQFIQRASTSGRPFLLYVALAHMHVPLPVTQ---LPAAPRGRSLYGAG 272
Cdd:cd16037 119 -------------------------------AVDWLREEAADDKPWFLFVGFVAPHFPLIAPQefyDLYVRRARAAYYGL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 273 LWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSvgpfTGFWQtrqggspaKQTTWEGGHRVPALAYWPG 351
Cdd:cd16037 168 VEFLDENIGRVLDALEELgLLDNTLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMIISGPG 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 352 RVPVNVTSTAlLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGRSQPGHRVL--FHPNSGAAGEFgalqTVRLERYK 429
Cdd:cd16037 230 IPAGKRVKTP-VSLVDLAPTILEAAGAPPP--PDLDGRSLLPLAEGPDDPDRVVFseYHAHGSPSGAF----MLRKGRWK 302
|
410 420 430
....*....|....*....|....*....|..
gi 45430057 430 AFYITGGAracdgstgPELqhkfpliFNLEDD 461
Cdd:cd16037 303 YIYYVGYP--------PQL-------FDLEND 319
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-405 |
1.85e-26 |
|
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: 109.60 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDM-GWGDLGANWAETKDTAnLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGGL 114
Cdd:cd16035 1 PNILLILTDQErYPPPWPAGWAALNLPA-RERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 115 PLNETTLAEVLQQAGYVTGIIGKWHLGHHGsyhpnfRGfdyyfgipyshdmgctdtpGYNHPPcpacpqgdgpsrnlqrd 194
Cdd:cd16035 80 SPDVPTLGHMLRAAGYYTAYKGKWHLSGAA------GG-------------------GYKRDP----------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 195 cytdvalplyenlniveqpvnlsslaqKYAEKATQFIQRASTS---GRPFLLYVALAHMH-VPLPVTQLPAAPRGRSLYG 270
Cdd:cd16035 118 ---------------------------GIAAQAVEWLRERGAKnadGKPWFLVVSLVNPHdIMFPPDDEERWRRFRNFYY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 271 AGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGpftgfwQTRQGGSPAKQTTwegghRVPALAYW 349
Cdd:cd16035 171 NLIRDVDRQIGRVLDALDASgLADNTIVVFTSDHG------EMGGAHG------LRGKGFNAYEEAL-----HVPLIISH 233
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 350 PGRVPVNVTSTALLSVLDIFPTVVALAQASLPQ----GRRFDGVDVSEVLfgRSQPGHRV 405
Cdd:cd16035 234 PDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEArateAPPLPGRDLSPLL--TDADADAV 291
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
36-461 |
1.42e-25 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 107.28 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvgGLP 115
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-----EFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 116 LNETTLAEVLQQAGYVTGIIGKWHL-G---HHGsyhpnfrgFDYyfgipyshdmgctdtpgynhppcpacpqgdgpsrnl 191
Cdd:cd16032 76 ADIPTFAHYLRAAGYRTALSGKMHFvGpdqLHG--------FDY------------------------------------ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 192 qrDcyTDVALplyenlniveqpvnlsslaqkyaeKATQFI-QRA-STSGRPFLLYVALAHMHVPLPVTQ------LPAAp 263
Cdd:cd16032 112 --D--EEVAF------------------------KAVQKLyDLArGEDGRPFFLTVSFTHPHDPYVIPQeywdlyVRRA- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 264 RgRSLYGAGLWeMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSvgpfTGFWQtrqggspaKQTTWEGGHR 342
Cdd:cd16032 163 R-RAYYGMVSY-VDDKVGQLLDTLERTgLADDTIVIFTSDHG------DMLGE----RGLWY--------KMSFFEGSAR 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 343 VPALAYWPGR-VPVNVTstALLSVLDIFPTVVALAQASLPQGR-RFDGVDVSEVLFGRSQPGHRVLFHPNSGaAGEFGAL 420
Cdd:cd16032 223 VPLIISAPGRfAPRRVA--EPVSLVDLLPTLVDLAGGGTAPHVpPLDGRSLLPLLEGGDSGGEDEVISEYLA-EGAVAPC 299
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 45430057 421 QTVRLERYKAFYITGgaracDGstgpelqhkfPLIFNLEDD 461
Cdd:cd16032 300 VMIRRGRWKFIYCPG-----DP----------DQLFDLEAD 325
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
34-428 |
3.76e-25 |
|
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: 108.04 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 34 QKPNFVIILADDM----GWgdLGANWAETkdtANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrNFAVT 109
Cdd:cd16030 1 KKPNVLFIAVDDLrpwlGC--YGGHPAKT---PNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVY-DNNSY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 110 SVGGLPlNETTLAEVLQQAGYVTGIIGK-WHlGHHGSYHPNFRGFDYYFGIP--------YSHDMGCTDTPGYNHPPCPA 180
Cdd:cd16030 75 FRKVAP-DAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPPgpekyppgKLCPGKKGGKGGGGGPAWEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 181 CPQGDGPsrnlqrdcYTDvalplyenlniveqpvnlsslaQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQ-- 258
Cdd:cd16030 153 ADVPDEA--------YPD----------------------GKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKky 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 259 ------------------------------LPAAPRGRSLYG--------AGLWE------------MDSLVGQIKDKVD 288
Cdd:cd16030 203 fdlyplesiplpnpfdpidlpevawndlddLPKYGDIPALNPgdpkgplpDEQARelrqayyasvsyVDAQVGRVLDALE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 289 -HTVKENTFLWFTGDNGpWA--QKcelagsvgpftGFWqtrqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSV 365
Cdd:cd16030 283 eLGLADNTIVVLWSDHG-WHlgEH-----------GHW--------GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVEL 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45430057 366 LDIFPTVVALAQasLPQGRRFDGVDVSEVLFGRSQPGHRVLF--HPNSGAAGEfgalqTVRLERY 428
Cdd:cd16030 343 VDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKDAAFsqYPRPSIMGY-----SIRTERY 400
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-393 |
1.78e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 103.22 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 35 KPNFVIILADDMGWGDLGA-NWAETKD---------TANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTR 104
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCyNNAHTGKsesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 105 NFAVTSVGGLPLneTTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqg 184
Cdd:cd16153 81 FEAAHPALDHGL--PTFPEVLKKAGYQTASFGKSHLE------------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 185 dgpsrNLQRdcYTDVALPLYENLNIVEqpvnlsslaqkyaekatqfIQRASTSGrPFLLYVALAHMHVP-LPvtqlPAAP 263
Cdd:cd16153 116 -----AFQR--YLKNANQSYKSFWGKI-------------------AKGADSDK-PFFVRLSFLQPHTPvLP----PKEF 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 264 RGRSLYGAGLWEMDSLVGQIKDKVD----HTVKENTFLWFTGDNGpwaqkcelagsvgpftgfWQTRQGGSPAKQTTWEG 339
Cdd:cd16153 165 RDRFDYYAFCAYGDAQVGRAVEAFKayslKQDRDYTIVYVTGDHG------------------WHLGEQGILAKFTFWPQ 226
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 45430057 340 GHRVPALAYWPGR--VPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSE 393
Cdd:cd16153 227 SHRVPLIVVSSDKlkAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
36-376 |
1.48e-23 |
|
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: 99.42 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCS-PSRASLLTGRLGLRNGVTRNFAVT----- 109
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSaPNHAALLTGAYPTLHGYTGNGSADpelps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 110 SVGGLPLNETTLAEVLQQAGYVTGIIGKWhlghhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIGLL--------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 190 nlqrdcytdvalplyenlniveqpvnlsslaqkyaekatQFIQRaSTSGRPFLLYVALAHMHVPL--PVTQLPaaprgrs 267
Cdd:cd00016 110 ---------------------------------------KAIDE-TSKEKPFVLFLHFDGPDGPGhaYGPNTP------- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 268 LYGAGLWEMDSLVGQIKDKV-DHTVKENTFLWFTGDNGpwaqkcelAGSVGPftgfwqTRQGGSPAKQTTWEGGHRVPAL 346
Cdd:cd00016 143 EYYDAVEEIDERIGKVLDALkKAGDADDTVIIVTADHG--------GIDKGH------GGDPKADGKADKSHTGMRVPFI 208
|
330 340 350
....*....|....*....|....*....|
gi 45430057 347 AYWPGrVPVNVTSTALLSVLDIFPTVVALA 376
Cdd:cd00016 209 AYGPG-VKKGGVKHELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-140 |
1.10e-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: 293771 [Multi-domain] Cd Length: 373 Bit Score: 93.83 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNfavtsVGGL 114
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPL 75
|
90 100
....*....|....*....|....*.
gi 45430057 115 PLNETTLAEVLQQAGYVTGIIGKWHL 140
Cdd:cd16152 76 PADEKTLAHYFRDAGYETGYVGKWHL 101
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
36-429 |
2.52e-19 |
|
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: 90.52 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGvtrnfAVTSVGGLP 115
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNG-----SWTNCMALG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 116 LNETTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrGFDYY-FGIpyshdmgctdtpgynhppcpaCPQGDGPSRNLQRD 194
Cdd:cd16156 76 DNVKTIGQRLSDNGIHTAYIGKWHLD----------GGDYFgNGI---------------------CPQGWDPDYWYDMR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 195 CYTD-----------VALPLYENLNIVEQpvnlSSLAQKYAEKATQFIQraSTSGRPFLLYVALAHMHVPL--------- 254
Cdd:cd16156 125 NYLDelteeerrksrRGLTSLEAEGIKEE----FTYGHRCTNRALDFIE--KHKDEDFFLVVSYDEPHHPFlcpkpyasm 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 255 --------------------PVTQLPAAPRGRSLYGAGLWEM----------DSLVGQIKDKVDHTVkENTFLWFTGDNG 304
Cdd:cd16156 199 ykdfefpkgenayddlenkpLHQRLWAGAKPHEDGDKGTIKHplyfgcnsfvDYEIGRVLDAADEIA-EDAWVIYTSDHG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 305 pwaqkcELAGSvgpftgfwQTRQGGSPAkqtTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQasLPQGR 384
Cdd:cd16156 278 ------DMLGA--------HKLWAKGPA---VYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPK 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 45430057 385 RFDGVDVSEVLFGRSQPGHRVLF---------HPNsgaageFGALQTVRL---ERYK 429
Cdd:cd16156 339 VLEGESILATIEDPEIPENRGVFvefgryevdHDG------FGGFQPVRCvvdGRYK 389
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-399 |
2.09e-14 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 75.35 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGR----LGLRngvtrnfavTSV 111
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWyphvNGHR---------TLH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 112 GGLPLNETTLAEVLQQAGYVTGIIGKWHLghhgsyhpnfrgfdyyfgIPYSHDMGCTDTPGYnhppcpacpqgdgpsrnl 191
Cdd:cd16150 72 HLLRPDEPNLLKTLKDAGYHVAWAGKNDD------------------LPGEFAAEAYCDSDE------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 192 qrdcytdvalplyenlniveqpvnlsslaqKYAEKATQFIQRASTsGRPFLLYVALAHMHVP---------------LPV 256
Cdd:cd16150 116 ------------------------------ACVRTAIDWLRNRRP-DKPFCLYLPLIFPHPPygveepwfsmidrekLPP 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 257 T--------QLPAAPRGRSLYGAGLW-----------------EMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAqkc 310
Cdd:cd16150 165 RrppglrakGKPSMLEGIEKQGLDRWseerwrelratylgmvsRLDHQFGRLLEALKETgLYDDTAVFFFSDHGDYT--- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 311 elagsvGPFtGFWQTRQGGSPAKQTtwegghRVPALAYWPGRVPVNVTStALLSVLDIFPTVVALAqaslpqgrrfdGVD 390
Cdd:cd16150 242 ------GDY-GLVEKWPNTFEDCLT------RVPLIIKPPGGPAGGVSD-ALVELVDIPPTLLDLA-----------GIP 296
|
....*....
gi 45430057 391 VSEVLFGRS 399
Cdd:cd16150 297 LSHTHFGRS 305
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
36-157 |
5.51e-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: 73.83 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvgGLP 115
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT-----PLD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 45430057 116 LNETTLAEVLQQAGYVTGIIGKWHL-----GHH------GSYHPNFRGFDYYF 157
Cdd:cd16028 76 ARHLTLALELRKAGYDPALFGYTDTspdprGLApldprlLSYELAMPGFDPVD 128
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
36-383 |
2.13e-13 |
|
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: 71.80 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGrlgLRNGVTRNFavTSVGGLP 115
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG---LFTHLTESW--NNYKGLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 116 LNETTLAEVLQQAGYVTGIIGK--WHLGHHGSYHpnfRGFDYYFGIPYShdmgctdtpgynhppcpaCPQGDGPSRNLQR 193
Cdd:cd16171 76 PNYPTWMDRLEKHGYHTQKYGKldYTSGHHSVSN---RVEAWTRDVPFL------------------LRQEGRPTVNLVG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 194 DCYTDvalplyenlniveqpvNLSSLAQKYAEKATQFIQRASTS-GRPFLLYVALAHMHvPLPVTQLPAAPRG----RSL 268
Cdd:cd16171 135 DRSTV----------------RVMLKDWQNTDKAVHWIRKEAPNlTQPFALYLGLNLPH-PYPSPSMGENFGSirniRAF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 269 YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAgsvgpftgfWQTRQGgspAKQTTWEGGHRVPALA 347
Cdd:cd16171 198 YYAMCAETDAMLGEIISALKDTgLLDKTYVFFTSDHG------ELA---------MEHRQF---YKMSMYEGSSHVPLLI 259
|
330 340 350
....*....|....*....|....*....|....*.
gi 45430057 348 YWPGrVPVNVTSTALLSVLDIFPTVVALAQASLPQG 383
Cdd:cd16171 260 MGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN 294
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
28-161 |
1.03e-05 |
|
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: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 28 SGKTRGQKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVtrnfA 107
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGS----P 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 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 |
1.17e-03 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 41.27 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 14 SFSGFLYPLVDFCISGKTRGQKPnFVIILADDMGWGDLGANwaetkDTANLDKMASEGMRFVDFHAA--ASTCsPSRASL 91
Cdd:COG1524 3 RGLSLLLASLLAAAAAAAPPAKK-VVLILVDGLRADLLERA-----HAPNLAALAARGVYARPLTSVfpSTTA-PAHTTL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 92 LTGRLGLRNGVTRNF--------AVTSVGGLP--------LNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPN----FR 151
Cdd:COG1524 76 LTGLYPGEHGIVGNGwydpelgrVVNSLSWVEdgfgsnslLPVPTIFERARAAGLTTAAVFWPSFEGSGLIDAArpypYD 155
|
170
....*....|.
gi 45430057 152 GFDYYFGIPYS 162
Cdd:COG1524 156 GRKPLLGNPAA 166
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
20-371 |
3.90e-03 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 39.89 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 20 YPLVDfcISGKTRGQKPNFVIILADDMGWGDLGAnwaetKDTANLDKMASEGMRFVDfHAAASTCSPsrasllTGRLGLR 99
Cdd:COG3083 231 YPLHP--LQFSDPAKPPNILLIVVDSLRADMLDP-----EVMPNLYAFAQRSLRFTN-HYSSGNSTR------AGLFGLF 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 100 NGVTRNFAvTSVgglpLNETT---LAEVLQQAGYVTGIigkwhlghhgsyhpnfrgfdyyfgipYSHDmgctdtpGYNHP 176
Cdd:COG3083 297 YGLPGNYW-DSI----LAERTppvLIDALQQQGYQFGL--------------------------FSSA-------GFNSP 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 177 PcpacpqgdgpsrnLQRDCYTDVALPLYENLNIVEQPvnlsslAQKYAEKATQFIQRAStSGRPFLLYVALAHMH----- 251
Cdd:COG3083 339 L-------------FRQTIFSDVSLPRLHTPGGPAQR------DRQITAQWLQWLDQRD-SDRPWFSYLFLDAPHaysfp 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430057 252 -------------VPLPVTQLPAAPRGRSLYGAGLWEMDSLVGQIKDKVDHTVK-ENTFLWFTGDNGPwaqkcelagsvg 317
Cdd:COG3083 399 adypkpfqpsedcNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLlENTIVIITADHGE------------ 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 45430057 318 PF----TGFWQTRQGGSPAkQTtwegghRVPALAYWPGRVPVNVTStaLLSVLDIFPT 371
Cdd:COG3083 467 EFnengQNYWGHNSNFSRY-QL------QVPLVIHWPGTPPQVISK--LTSHLDIVPT 515
|
|
| |
