|
Name |
Accession |
Description |
Interval |
E-value |
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
35-468 |
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: 651.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 35 KPNFVIILADDMGWGDLGANWAET-KDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGG 113
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNaILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 194 dcytdvalplyenlniveqpvnlSSLAQKYAEKATQFIQRAS-SGRPFLLYVALAHMHVPLPVTQLPAAP-RGRSLYGAG 271
Cdd:cd16161 132 -----------------------SSLADRYAQFATDFIQRASaKDRPFFLYAALAHVHVPLANLPRFQSPtSGRGPYGDA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 272 LWEMDSLVGQIKDKVDH-TVKENTFLWFTGDNGPWAQKCELAgsVGPFTGFWQTRQGGSPAKQTTWEGGHRVPALAYWPG 350
Cdd:cd16161 189 LQEMDDLVGQIMDAVKHaGLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 351 RVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGeFGALQTVRLERYKAF 430
Cdd:cd16161 267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAH 345
|
410 420 430
....*....|....*....|....*....|....*...
gi 1209857069 431 YITGGARACDGSTGPELQHKFPLIFNLEDDTAEAVPLE 468
Cdd:cd16161 346 YATGGALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT 383
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-467 |
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: 525.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRN-FAVTSVGG 113
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDMGCTDTPGYNHPPCPAcpqgdgpsrnlqr 193
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 194 dcytdvalPLYENLNIVEQPVNLSSLAQKYAEKATQFIQRaSSGRPFLLYVALAHMHVPLPVTQLPAAPRGRSLYGAGLW 273
Cdd:cd16026 148 --------PLMENEEVIEQPADQSSLTQRYTDEAVDFIER-NKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 274 EMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRVPALAYWPGRV 352
Cdd:cd16026 219 ELDWSVGRILDALKELgLEENTLVIFTSDNGPWLEYGGHGGSAGPLRG----------GKGTTWEGGVRVPFIAWWPGVI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 353 PVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQ-PGHRVLFHPNSgaagefGALQTVRLERYKAFY 431
Cdd:cd16026 289 PAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKsPPHPFFYYYDG------GDLQAVRSGRWKLHL 362
|
410 420 430
....*....|....*....|....*....|....*.
gi 1209857069 432 ITGGARACDGSTGPELQHKFPLIFNLEDDTAEAVPL 467
Cdd:cd16026 363 PTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGETYNV 398
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
35-521 |
9.92e-119 |
|
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: 358.30 E-value: 9.92e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRN-FAVTSVGG 113
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGvFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 114 LPLNETTLAEVLQQAGYVTGIIGKWHL--GHHGSYHPNFRGFDYYFGIPYSHDMG-CTD-TPGYNHPPC-PACPQGDGPs 188
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLgvGLNGTYLPTHQGFDHYLGIPYSHDQGpCQNlTCFPPNIPCfGGCDQGEVP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 189 rnlqrdcytdvaLPLYENLNIVEQPVNLSSLAQKYAEKATQFIQR-ASSGRPFLLYVALAHMHVPLPVTQLPAAPRGRSL 267
Cdd:cd16158 160 ------------CPLFYNESIVQQPVDLLTLEERYAKFAKDFIADnAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 268 YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFtgfwqtRQGgspaKQTTWEGGHRVPALA 346
Cdd:cd16158 228 FGDALAELDGSVGELLQTLKENgIDNNTLVFFTSDNGPSTMRKSRGGNAGLL------KCG----KGTTYEGGVREPAIA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 347 YWPGRVPVNVTStALLSVLDIFPTVVALAQASLPQgRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGEFGALqTVRLER 426
Cdd:cd16158 298 YWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLPN-VTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVF-AVRWGK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 427 YKAFYITGGA--------RACDGSTgPELQHKFPLIFNLEDDTAEAVPLErGGAEYQAVLPEVRKVLADVLQDIANDNiS 498
Cdd:cd16158 375 YKAHFYTQGAahsgttpdKDCHPSA-ELTSHDPPLLFDLSQDPSENYNLL-GLPEYNQVLKQIQQVKERFEASMKFGE-S 451
|
490 500
....*....|....*....|....*..
gi 1209857069 499 SADYTQDPSVTPCCN----PYQIACRC 521
Cdd:cd16158 452 EINKGEDPALEPCCKpgctPKPSCCQC 478
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
35-486 |
7.22e-114 |
|
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: 344.41 E-value: 7.22e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV---TRNFAVTSV 111
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 112 GGLPLNETTLAEVLQQAGYVTGIIGKWHLG-----HHGSYH-PNFRGFDYY-FGIPYSHDMGCTDTPGYNhppcpacpqg 184
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDFVgTNLPFTNSWACDDTGRHV---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 185 DGPSRNLqrdCYtdvalpLYENLNIVEQPVNLSSLAQKYAEKATQFIQrASSGRPFLLYVALAHMHVPLPVTQLPAAPRG 264
Cdd:cd16160 151 DFPDRSA---CF------LYYNDTIVEQPIQHEHLTETLVGDAKSFIE-DNQENPFFLYFSFPQTHTPLFASKRFKGKSK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 265 RSLYGAGLWEMDSLVGQIKDK-VDHTVKENTFLWFTGDNGPWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRVP 343
Cdd:cd16160 221 RGRYGDNINEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKG----------GKGNSWEGGIRVP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 344 ALAYWPGRVPVNVtSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQ-PGHRVLFHPNSgaagefgALQTV 422
Cdd:cd16160 291 FIAYWPGTIKPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADsPHDDILYYCCS-------RLMAV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 423 RLERYKAFYITG--------GARACDGSTGPEL------------QHKFPLIFNLEDDTAEAVPLERGGAEYqaVLPEVR 482
Cdd:cd16160 363 RYGSYKIHFKTQplpsqeslDPNCDGGGPLSDYivcydcedecvtKHNPPLIFDVEKDPGEQYPLQPSVYEH--MLEAVE 440
|
....
gi 1209857069 483 KVLA 486
Cdd:cd16160 441 KLIA 444
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-487 |
3.45e-103 |
|
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: 317.87 E-value: 3.45e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG--VTRNFAVTS-- 110
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 111 ----VGGLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHdMGCTDTPGYNHPPcpacpqgdg 186
Cdd:cd16157 81 pqniVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCH-FGPYDNKAYPNIP--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 187 psrnLQRDcyTDVALPLYENLNIvEQPVNLSSLAQKYAEKATQFIQR-ASSGRPFLLYVALAHMHVPLPVTQLPAAPRGR 265
Cdd:cd16157 151 ----VYRD--WEMIGRYYEEFKI-DKKTGESNLTQIYLQEALEFIEKqHDAQKPFFLYWAPDATHAPVYASKPFLGTSQR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 266 SLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNG-PWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRVP 343
Cdd:cd16157 224 GLYGDAVMELDSSVGKILESLKSLgIENNTFVFFSSDNGaALISAPEQGGSNGPFLC----------GKQTTFEGGMREP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 344 ALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSgaagefgALQTVR 423
Cdd:cd16157 294 AIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGD-------ELMAVR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 424 LERYKAFYIT---------GGARACDG------STGPELQH-KFPLIFNLEDDTAEAVPLERGGAEYQAVLPEVRKVLAD 487
Cdd:cd16157 367 LGQYKAHFWTwsnsweefrKGINFCPGqnvpgvTTHNQTDHtKLPLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVVQQ 446
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
35-493 |
1.69e-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: 315.00 E-value: 1.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGR------LGLRNGVTRNFAV 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRypirsgMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 109 TSVGGLPLNETTLAEVLQQAGYVTGIIGKWHLGHH------GSYHPNFRGFDYYFGIPYSHDMGCTDTPG--YNHPPCPA 180
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHcesrndFCHHPLNHGFDYFYGLPLTNLKDCGDGSNgeYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 181 CPQgdgpSRNLQRDCYTDVALPLY--------------------------------------ENLNIVEQPVNLSSLAQK 222
Cdd:cd16159 161 FPL----LTAFVLITALTIFLLLYlgavskrffvfllilsllfislfflllitnryfncilmRNHEVVEQPMSLENLTQR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 223 YAEKATQFIQRaSSGRPFLLYVALAHMHvplpvTQLPAAP--RGRS---LYGAGLWEMDSLVGQIKDKVDHT-VKENTFL 296
Cdd:cd16159 237 LTKEAISFLER-NKERPFLLVMSFLHVH-----TALFTSKkfKGRSkhgRYGDNVEEMDWSVGQILDALDELgLKDNTFV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 297 WFTGDNGPWAqkcELAGSVGPFTGFWQTRQGGSpaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQ 376
Cdd:cd16159 311 YFTSDNGGHL---EEISVGGEYGGGNGGIYGGK--KMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 377 ASLPQGRRFDGVDVSEVLFGRSQ-PGHRVLFH------------PNSGAAgefgalqtvrleRYKAFYIT-----GGARA 438
Cdd:cd16159 386 APLPSDRIIDGRDLMPLLTGQEKrSPHEFLFHycgaelhavryrPRDGGA------------VWKAHYFTpnfypGTEGC 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209857069 439 -------CDGSTGpeLQHKFPLIFNLEDDTAEAVPLERGGAEYQAVLPEVRKVLADVLQDIA 493
Cdd:cd16159 454 cgtllcrCFGDSV--THHDPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIE 513
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-469 |
1.03e-92 |
|
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: 287.51 E-value: 1.03e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGAN---WAETKDTANLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTRNFAVTSVG 112
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYgggIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 113 GLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHdmgctdtpgynhppcpacpqgdgpsrnlq 192
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYHT----------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 193 rdcytdvalplyenlniveqpvnlssLAQKYAEKATQFIQR-ASSGRPFLLYVALAHMHVP-LPVTQLPAAPRGRSLYGA 270
Cdd:cd16142 131 --------------------------IDEEIVDKAIDFIKRnAKADKPFFLYVNFTKMHFPtLPSPEFEGKSSGKGKYAD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 271 GLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSvGPFTGfwqtrqggspAKQTTWEGGHRVPALAYWP 349
Cdd:cd16142 185 SMVELDDHVGQILDALDELgIADNTIVIFTTDNGPEQDVWPDGGY-TPFRG----------EKGTTWEGGVRVPAIVRWP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 350 GRVPVNVTSTALLSVLDIFPTVVALAQASLP------QGRRFDGVDVSEVLFGRS-QPGHRVLFHpnsGAAGEFGAlqtV 422
Cdd:cd16142 254 GKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSeKSRRSEFFY---FGEGELGA---V 327
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1209857069 423 RLERYKA-FYITGGARAcdGSTGPELQHKFPLIFNLEDDtaeavPLER 469
Cdd:cd16142 328 RWKNWKVhFKAQEDTGG--PTGEPFYVLTFPLIFNLRRD-----PKER 368
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
34-496 |
1.89e-87 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 274.45 E-value: 1.89e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvTSVGG 113
Cdd:COG3119 22 KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE-GYNGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 114 LPLNETTLAEVLQQAGYVTGIIGKWHLghhgsyhpnfrgfdyyfgipYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:COG3119 101 LPPDEPTLAELLKEAGYRTALFGKWHL--------------------YLTD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 194 dcytdvalplyenlniveqpvnlsslaqKYAEKATQFI-QRASSGRPFLLYVALAHMHVP-----------------LPV 255
Cdd:COG3119 132 ----------------------------LLTDKAIDFLeRQADKDKPFFLYLAFNAPHAPyqapeeyldkydgkdipLPP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 256 TQLPAA------PRGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAqkcelagsvgpftGFWQTRQGg 328
Cdd:COG3119 184 NLAPRDlteeelRRARAAYAAMIEEVDDQVGRLLDALEELgLADNTIVVFTSDNGPSL-------------GEHGLRGG- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 329 spaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHRVLFHp 408
Cdd:COG3119 250 ---KGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYW- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 409 nsgAAGEFGALQTVRLERYKAFYITGGARAcdgstgPELqhkfpliFNLEDDTAEAVPLergGAEYqavlPEVRKVLADV 488
Cdd:COG3119 324 ---EYPRGGGNRAIRTGRWKLIRYYDDDGP------WEL-------YDLKNDPGETNNL---AADY----PEVVAELRAL 380
|
....*...
gi 1209857069 489 LQDIANDN 496
Cdd:COG3119 381 LEAWLKEL 388
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-491 |
9.52e-85 |
|
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: 268.64 E-value: 9.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTG----RLGL---------RNGV 102
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGqypaRLGItdvipgrrgPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 103 TRNFAVTSVGGLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGI-PYSHDMGCTDTPGYNHPPCPAC 181
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIGGtGNGGPPSYYFPPGKPNPDLEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 182 PQGDgpsrnlqrdcytdvalplyenlniveqpvnlsSLAQKYAEKATQFIQRAsSGRPFLLYvaLAH--MHVPLPVTQ-- 257
Cdd:cd16144 161 PEGE--------------------------------YLTDRLTDEAIDFIEQN-KDKPFFLY--LSHyaVHTPIQARPel 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 258 ------LPAAPRGR---SLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFtgfwqtRQG 327
Cdd:cd16144 206 iekyekKKKGLRKGqknPVYAAMIESLDESVGRILDALEELgLADNTLVIFTSDNGGLSTRGGPPTSNAPL------RGG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 328 gspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHR--VL 405
Cdd:cd16144 280 ----KGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRraLF 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 406 FH-PN-SGAAGEFGAlqTVRLERYK--AFYITGgaracdgstGPELqhkfpliFNLEDDTAEAVPLerggAEYQavlPEV 481
Cdd:cd16144 356 WHfPHyHGQGGRPAS--AIRKGDWKliEFYEDG---------RVEL-------YNLKNDIGETNNL----AAEM---PEK 410
|
490
....*....|
gi 1209857069 482 RKVLADVLQD 491
Cdd:cd16144 411 AAELKKKLDA 420
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-463 |
3.84e-82 |
|
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: 260.98 E-value: 3.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETK-DTANLDKMASEGMRFVDFHAAASTCSPSRASLLTG----RLGLRNGVTRNFavts 110
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGrypwRSRLKGGVLGGF---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 111 vgGLPL---NETTLAEVLQQAGYVTGIIGKWHLG-----------HHGSYH-----------PNFRGFDYYFGIPYShdm 165
Cdd:cd16143 77 --SPPLiepDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkaATGTGKdvdyskpikggPLDHGFDYYFGIPAS--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 166 gctdtpgynhppcpacpqgdgpsrnlqrdcytDVaLPLyenlniveqpvnlsslaqkYAEKATQFI-QRASSGRPFLLYV 244
Cdd:cd16143 152 --------------------------------EV-LPT-------------------LTDKAVEFIdQHAKKDKPFFLYF 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 245 ALAHMHVPLpvtqLPAAP-RGRS---LYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGPwaqkcelagsvGPFT 319
Cdd:cd16143 180 ALPAPHTPI----VPSPEfQGKSgagPYGDFVYELDWVVGRILDALKeLGLAENTLVIFTSDNGP-----------SPYA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 320 GFWQT-RQGGSPA------KQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSE 392
Cdd:cd16143 245 DYKELeKFGHDPSgplrgmKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLP 324
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209857069 393 VLFGRSQPGHRV-LFHpnSGAAGEFgalqTVRLERYKAFYITGGARACDGSTGPELQHKFPLIFNLEDDTAE 463
Cdd:cd16143 325 ALLGPKKQEVREsLVH--HSGNGSF----AIRKGDWKLIDGTGSGGFSYPRGKEKLGLPPGQLYNLSTDPGE 390
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-463 |
1.81e-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: 257.14 E-value: 1.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGGLP 115
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 116 LNETTLAEVLQQAGYVTGIIGKWHLGHHGSY-HPNFRGFDYYFGIpYSHdmgctdTPGYNHPPcpacPQGDgpsRNLQRd 194
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYGY-LDQ------VHAHNYYP----EYLW---RNGEK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 195 cytdvaLPLYENLNIVEQPVNLSSLAQK-YAE-----KATQFIqRASSGRPFLLYVALAHMHVPLPVTQLPAA---PRGR 265
Cdd:cd16145 146 ------VPLPNNVIPPLDEGNNAGGGGGtYSHdlftdEALDFI-RENKDKPFFLYLAYTLPHAPLQVPDDGPYkykPKDP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 266 SLYGAGLWE------------MDSLVGQIKDKV-DHTVKENTFLWFTGDNGP-----WAQKCELAGSVGPFTGFwqtrqg 327
Cdd:cd16145 219 GIYAYLPWPqpekayaamvtrLDRDVGRILALLkELGIDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY------ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 328 gspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPG-HRVLF 406
Cdd:cd16145 293 ----KRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPE--DIDGISLLPTLLGKPQQQqHDYLY 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1209857069 407 HpnsgAAGEFGALQTVRLERYKAFYItggaracDGSTGP-ELqhkfpliFNLEDDTAE 463
Cdd:cd16145 367 W----EFYEGGGAQAVRMGGWKAVRH-------GKKDGPfEL-------YDLSTDPGE 406
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
36-406 |
7.18e-77 |
|
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: 247.46 E-value: 7.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTRnfavTSVGG-- 113
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWH----TILGRer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgcTDTPGYnhppcpacpqgdgpsrnLQR 193
Cdd:cd16146 76 MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGGGI---GQYPDY-----------------WGN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 194 DCYTDValpLYENlNIVEQpvnlsslAQKYA-----EKATQFIQRaSSGRPFLLYVALAHMHVPLPVTQLPAAP------ 262
Cdd:cd16146 136 DYFDDT---YYHN-GKFVK-------TEGYCtdvffDEAIDFIEE-NKDKPFFAYLATNAPHGPLQVPDKYLDPykdmgl 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 263 -RGRSLYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGPWaqkcelAGSVGPFTGFWQtrqgGSpaKQTTWEGGH 340
Cdd:cd16146 204 dDKLAAFYGMIENIDDNVGRLLAKLKeLGLEENTIVIFMSDNGPA------GGVPKRFNAGMR----GK--KGSVYEGGH 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1209857069 341 RVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQP-GHRVLF 406
Cdd:cd16146 272 RVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPwPERTLF 338
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
36-389 |
6.03e-70 |
|
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: 223.85 E-value: 6.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNfaVTSVGGLP 115
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 116 LNETTLAEVLQQAGYVTGIIGKWHlghhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsrnlqrdc 195
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 196 ytdvalplyenlniveqpvnlsslaqkyaEKATQFIQRASSGRPFLLYVALAHMHVPLpvtqlpaaprgrsLYGAGLWEM 275
Cdd:cd16022 103 -----------------------------DEAIDFIERRDKDKPFFLYVSFNAPHPPF-------------AYYAMVSAI 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 276 DSLVGQIKDKVDHT-VKENTFLWFTGDNgpwaqkcelagsvGPFTGFWQTRQGgspaKQTTWEGGHRVPALAYWPGRVPV 354
Cdd:cd16022 141 DDQIGRILDALEELgLLDNTLIVFTSDH-------------GDMLGDHGLRGK----KGSLYEGGIRVPFIVRWPGKIPA 203
|
330 340 350
....*....|....*....|....*....|....*
gi 1209857069 355 NVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVD 389
Cdd:cd16022 204 GQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
36-469 |
5.20e-68 |
|
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: 223.97 E-value: 5.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFvDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSV-GGL 114
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVIL-NNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEpYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 115 PLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYH-PNFRGFDYYFGiPYShdmGCTDtpGYNHPPCPACP------QGDGP 187
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYTWEYtPTNRGFDSFYG-YYG---GAED--YYTHTSGGANDygnddlRDNEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 188 SRNLQRDCY-TDValplyenlniveqpvnlsslaqkYAEKATQFIQRASSGRPFLLYVALAHMHVPLPVTQLPAAP---- 262
Cdd:cd16029 154 PAWDYNGTYsTDL-----------------------FTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPyedk 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 263 ------RGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCElAGSVGPFTGfwqtrqggspAKQTT 335
Cdd:cd16029 211 fahikdEDRRTYAAMVSALDESVGNVVDALKAKgMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRG----------GKNTL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 336 WEGGHRVPALAYWPGRVPV-NVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHR-VLFHPNSGAA 413
Cdd:cd16029 280 WEGGVRVPAFVWSPLLPPKrGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTeILLNIDDITR 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1209857069 414 GEFGAlqTVRLERYKafYITGgaracdgstgpelqhkFPLiFNLEDDtaeavPLER 469
Cdd:cd16029 360 TTGGA--AIRVGDWK--LIVG----------------KPL-FNIEND-----PCER 389
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-434 |
4.41e-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: 210.53 E-value: 4.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTRnfavtsvGGLP 115
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPL-CTPSRVQLMTGKYNFRNYVVF-------GYLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 116 LNETTLAEVLQQAGYVTGIIGKWHLG---HHGSYHPNFrGFDYY--FGipyshdmGCTDTPGYNHPPCPACPQGDGPSRN 190
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGKWQLGggrGDGDYPHEF-GFDEYclWQ-------LTETGEKYSRPATPTFNIRNGKLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 191 LQRDCY-TDValplyenlniveqpvnlsslaqkYAEKATQFIQRaSSGRPFLLY--VALAH-MHVPLPVTQLPAAPRGRS 266
Cdd:cd16151 145 TTEGDYgPDL-----------------------FADFLIDFIER-NKDQPFFAYypMVLVHdPFVPTPDSPDWDPDDKRK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 267 -----LYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNgpwaqkcelaGSVGPFTGFW--QTRQGGspaKQTTWEG 338
Cdd:cd16151 201 kddpeYFPDMVAYMDKLVGKLVDKLEELgLRENTIIIFTGDN----------GTHRPITSRTngREVRGG---KGKTTDA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 339 GHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGEFGA 418
Cdd:cd16151 268 GTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWYYRNPHKKFG 347
|
410
....*....|....*.
gi 1209857069 419 LQTVRLERYKaFYITG 434
Cdd:cd16151 348 SRFVRTKRYK-LYADG 362
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
36-377 |
5.59e-56 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 189.56 E-value: 5.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrnfaVTSVGGLP 115
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSY----VSTPVGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 116 LNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFG-IPYSHDMGCTDTPGYNHPPcpacpqgdgpsrnlqRD 194
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLYADPPDVPYNCSG---------------GG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 195 CYTDValplyenlniveqpvnlsslaqkYAEKATQFIQRASsgRPFLLYVALAHMHVPLPVTQLPAAP------------ 262
Cdd:pfam00884 142 VSDEA-----------------------LLDEALEFLDNND--KPFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscsee 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 263 RGRSLYGAGLWEMDSLVGQIKDKV-DHTVKENTFLWFTGDNGPwaqkcelagSVGPFTGFWQTRQGGspakqTTWEGGHR 341
Cdd:pfam00884 197 QLLNSYDNTLLYTDDAIGRVLDKLeENGLLDNTLVVYTSDHGE---------SLGEGGGYLHGGKYD-----NAPEGGYR 262
|
330 340 350
....*....|....*....|....*....|....*.
gi 1209857069 342 VPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQA 377
Cdd:pfam00884 263 VPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
34-467 |
6.34e-53 |
|
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: 184.18 E-value: 6.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 34 QKPNFVIILADDMGWGDLGANWAETkDTANLDKMASEGMRFVDFHAAAsTCSPSRASLLTGRLGLRNGVtRNFAVTSVGG 113
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEI-PTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 114 ------LPLNETTLAEVLQQAGYVTGIIGKWHLGHHgsyhpnfrgfDYYFgipySHDmgctdtpgynhppcpacpqgdgp 187
Cdd:cd16025 78 pgyegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------DYYS----TDD----------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 188 srnlqrdcytdvalplyenlniveqpvnlsslaqkYAEKATQFI-QRASSGRPFLLYVALAHMHVPL------------- 253
Cdd:cd16025 121 -----------------------------------LTDKAIEYIdEQKAPDKPFFLYLAFGAPHAPLqapkewidkykgk 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 254 -----------------------PVTQLPAAPRG-----------RSLYG------AGLWE-MDSLVGQIKDKVDHT-VK 291
Cdd:cd16025 166 ydagwdalreerlerqkelglipADTKLTPRPPGvpawdslspeeKKLEArrmevyAAMVEhMDQQIGRLIDYLKELgEL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 292 ENTFLWFTGDNGP-----WAQkcelAGSvGPFTGFwqtrqggspaKQTTWEGGHRVPALAYWPGRV-PVNVTSTALLSVL 365
Cdd:cd16025 246 DNTLIIFLSDNGAsaepgWAN----ASN-TPFRLY----------KQASHEGGIRTPLIVSWPKGIkAKGGIRHQFAHVI 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 366 DIFPTVVALAQASLPQGRR------FDGVDVSEVLFGRSQPG-HRVLFHPNSGAAGefgalqtVRLERYKAFYITGGAra 438
Cdd:cd16025 311 DIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSrRRTQYFELFGNRA-------IRKGGWKAVALHPPP-- 381
|
490 500
....*....|....*....|....*....
gi 1209857069 439 cDGSTGPELqhkfpliFNLEDDTAEAVPL 467
Cdd:cd16025 382 -GWGDQWEL-------YDLAKDPSETHDL 402
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
36-432 |
9.78e-53 |
|
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: 183.09 E-value: 9.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGA--NWAETkdtANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFavTSVGG 113
Cdd:cd16027 1 PNILWIIADDLSPDLGGYggNVVKT---PNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR--SRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAWD----------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 194 dcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQRASSGRPFLLYVALAHMH-----------------VPLPvT 256
Cdd:cd16027 127 -----------------------------YASNAADFLNRAKKGQPFFLWFGFHDPHrpyppgdgeepgydpekVKVP-P 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 257 QLPAAPRGR---SLYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGpwaqkcelagsvGPFTGfwqtrqggspAK 332
Cdd:cd16027 177 YLPDTPEVRedlADYYDEIERLDQQVGEILDELEeDGLLDNTIVIFTSDHG------------MPFPR----------AK 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 333 QTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHRVLF-----H 407
Cdd:cd16027 235 GTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGRDYVFaerdrH 312
|
410 420
....*....|....*....|....*.
gi 1209857069 408 pnsgaaGEFGALQ-TVRLERYKafYI 432
Cdd:cd16027 313 ------DETYDPIrSVRTGRYK--YI 330
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-460 |
1.38e-48 |
|
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: 172.75 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVtsvggL 114
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 115 PLNETTLAEVLQQAGYVTGIIGKWHL-GHHGSYH--------PNFR-GFDYYFGipyshdMGCTDtpGYNHPPCpacpQG 184
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGraddytppPERRhGFDYWKG------YECNH--DHNNPHY----YD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 185 DGPSRNlQRDCYTDVALplyenlniveqpvnlsslaqkyAEKATQFI-QRASSGRPFLLYVALAHMHVP----------- 252
Cdd:cd16034 144 DDGKRI-YIKGYSPDAE----------------------TDLAIEYLeNQADKDKPFALVLSWNPPHDPyttapeeyldm 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 253 -----------LPVTQLPAAPRGRSL---YGA--GLwemDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSV 315
Cdd:cd16034 201 ydpkklllrpnVPEDKKEEAGLREDLrgyYAMitAL---DDNIGRLLDALKELgLLENTIVVFTSDHG------DMLGSH 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 316 GPFtgfwqtrqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLF 395
Cdd:cd16034 272 GLM------------NKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLL 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 396 GRSQPGHR----VLFHPNSG-AAGEFGALQTVRLERYKafYitggarACDGSTGpelqhkfPLIFNLEDD 460
Cdd:cd16034 338 GGKDDEPDsvllQCFVPFGGgSARDGGEWRGVRTDRYT--Y------VRDKNGP-------WLLFDNEKD 392
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
34-483 |
7.84e-46 |
|
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: 166.17 E-value: 7.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvGG 113
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG----PL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGsYHPNfRGFDYYFGIPyshdmgctdtpgynhppcpacPQGDgpsrnlqr 193
Cdd:cd16031 77 FDASQPTYPKLLRKAGYQTAFIGKWHLGSGG-DLPP-PGFDYWVSFP---------------------GQGS-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 194 dcYTDvaLPLYENLNIVEQPVNLSSLaqkYAEKATQFIQRASSGRPFLLYV-----------ALAHMHV------PLPVT 256
Cdd:cd16031 126 --YYD--PEFIENGKRVGQKGYVTDI---ITDKALDFLKERDKDKPFCLSLsfkaphrpftpAPRHRGLyedvtiPEPET 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 257 QLPA--APRGRSL---------------------------YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwa 306
Cdd:cd16031 199 FDDDdyAGRPEWAreqrnrirgvldgrfdtpekyqrymkdYLRTVTGVDDNVGRILDYLEEQgLADNTIIIYTSDNG--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 307 qkcELAGSVGpFTGfwqtrqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPqgRRFD 386
Cdd:cd16031 276 ---FFLGEHG-LFD-----------KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIP--EDMQ 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 387 GVDVSEVLFGRSQPGHR------VLFHPNS-GAAGEFGalqtVRLERYKAFYITGGARAcdgstgPELqhkfpliFNLED 459
Cdd:cd16031 339 GRSLLPLLEGEKPVDWRkefyyeYYEEPNFhNVPTHEG----VRTERYKYIYYYGVWDE------EEL-------YDLKK 401
|
490 500
....*....|....*....|....*...
gi 1209857069 460 DtaeavPLER----GGAEYQAVLPEVRK 483
Cdd:cd16031 402 D-----PLELnnlaNDPEYAEVLKELRK 424
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-387 |
4.27e-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: 148.54 E-value: 4.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV-----TRNFAVTS 110
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 111 VG-GLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd16149 81 KPeGYLEGQTTLPEVLQDAGYRCGLSGKWHLGDDA--------------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 190 nlqrdcytdvalplyenlniveqpvnlsslaqkyaekATQFIQRASSGRPFLLYVAlahmhvplpvTQLPAAPRGrslYG 269
Cdd:cd16149 116 -------------------------------------ADFLRRRAEAEKPFFLSVN----------YTAPHSPWG---YF 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 270 AGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcelagsvgpFT----GFWQTRQGGSPakQTTWEGGHRVPA 344
Cdd:cd16149 146 AAVTGVDRNVGRLLDELEELgLTENTLVIFTSDNG--------------FNmghhGIWGKGNGTFP--LNMYDNSVKVPF 209
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1209857069 345 LAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDG 387
Cdd:cd16149 210 IIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPG 252
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-438 |
3.91e-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: 143.64 E-value: 3.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWgDLGANWAETKD---TANLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTrnfavtSVG 112
Cdd:cd16154 1 PNILLIIADDQGL-DSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVL------AVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 113 G-LPLNETTL--AEVLQQ--AGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIpyshdMGctdtpgynhppcpacpqGDGP 187
Cdd:cd16154 73 DeLLLSEETLlqLLIKDAttAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGI-----LG-----------------GGVQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 188 SrnlqrdcYTDVALplyeNLNIVEQPVN------LSSLAQKYAEKATQfiqrassgrPFLLYVALAHMHVPLpvtQLPAA 261
Cdd:cd16154 131 D-------YYNWNL----TNNGQTTNSTeyattkLTNLAIDWIDQQTK---------PWFLWLAYNAPHTPF---HLPPA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 262 ---PRG------------RSLYGAGLWEMDSLVGQIKDKVDHTVKENTFLWFTGDNG-PwaqkcelagsvGPFTGFWQTR 325
Cdd:cd16154 188 elhSRSllgdsadieanpRPYYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGtP-----------GQVVDLPYTR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 326 QGgspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPGHRVL 405
Cdd:cd16154 257 NH---AKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNASTRQYN 331
|
410 420 430
....*....|....*....|....*....|...
gi 1209857069 406 FHPNSGAAGEFGAlqtVRLERYKAFYITGGARA 438
Cdd:cd16154 332 YTEYESPTTTGWA---TRNQYYKLIESENGQEE 361
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
31-491 |
5.78e-35 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 137.11 E-value: 5.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 31 TRGQKPNFVIILADDMGwGD-LGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNGV 102
Cdd:PRK13759 2 VQTKKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 103 TRNFavtsvgglplnETTLAEVLQQAGYVTGIIGKWHlghhgsYHP--NFRGFD--------YYFGIPYSH---DMgCTD 169
Cdd:PRK13759 81 PWNY-----------KNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHnvllhdgyLHSGRNEDKsqfDF-VSD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 170 --------TPGYNhppcpACPQGDGpsrnlqRDCYTDVALP--LYENLNiveqPVNLSslaqkyAEKATQFIQRASSGRP 239
Cdd:PRK13759 143 ylawlrekAPGKD-----PDLTDIG------WDCNSWVARPwdLEERLH----PTNWV------GSESIEFLRRRDPTKP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 240 FLLYVALAHMHVPL--PV--------TQLPAAPRGRSLYGAGLW----EMDSLVGQIKDK---------------VDH-- 288
Cdd:PRK13759 202 FFLKMSFARPHSPYdpPKryfdmykdADIPDPHIGDWEYAEDQDpeggSIDALRGNLGEEyarraraayyglithIDHqi 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 289 -----TVKE-----NTFLWFTGDNGpwaqkcELAGSVGPFTgfwqtrqggspaKQTTWEGGHRVPALAYWPG---RVPVN 355
Cdd:PRK13759 282 grflqALKEfglldNTIILFVSDHG------DMLGDHYLFR------------KGYPYEGSAHIPFIIYDPGgllAGNRG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 356 VTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGrSQPGHRVLFHpnsgaaGEFGALqtvrlerYKAF-YITG 434
Cdd:PRK13759 344 TVIDQVVELRDIMPTLLDLAGGTIP--DDVDGRSLKNLIFG-QYEGWRPYLH------GEHALG-------YSSDnYLTD 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1209857069 435 GaracdgstgpelQHKF--------PLIFNLEDDTAEAVPLErGGAEYQAVLPEVRKVLADVLQD 491
Cdd:PRK13759 408 G------------KWKYiwfsqtgeEQLFDLKKDPHELHNLS-PSEKYQPRLREMRKKLVDHLRG 459
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-490 |
3.05e-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: 133.50 E-value: 3.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNF--AVTSVGG 113
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSyhPNFRGFDYYFgiPYSH-------DMGC--------TDTP-----GY 173
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVGPEET--PLDYGFDEYL--PVETtieyflaDRAIemleelaaDDKPfflrvNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 174 NHPPCPACPqgdgPSRNLqrDCYTDVALPLYENLNiveqpvnlSSLAQK---YAEKATQFIQRASSG---RPfllyvALA 247
Cdd:cd16033 157 WGPHDPYIP----PEPYL--DMYDPEDIPLPESFA--------DDFEDKpyiYRRERKRWGVDTEDEedwKE-----IIA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 248 HmhvplpvtqlpaaprgrslYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGPFTgfwqtrQ 326
Cdd:cd16033 218 H-------------------YWGYITLIDDAIGRILDALEELgLADDTLVIFTSDHG------DALGAHRLWD------K 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 327 GGSPAKQTtweggHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGRSQPGHR--V 404
Cdd:cd16033 267 GPFMYEET-----YRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVP--PKVDGRSLLPLLRGEQPEDWRdeV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 405 L--FHPNsgaagEFGALQT-VRLERYKafYItggaraCDGSTGPELqhkfpliFNLEDDTAEAVPLeRGGAEYQAVLPEV 481
Cdd:cd16033 340 VteYNGH-----EFYLPQRmVRTDRYK--YV------FNGFDIDEL-------YDLESDPYELNNL-IDDPEYEEILREM 398
|
....*....
gi 1209857069 482 RKVLADVLQ 490
Cdd:cd16033 399 RTRLYEWME 407
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
35-387 |
2.33e-33 |
|
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: 130.75 E-value: 2.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 35 KPNFVIILADDMGWgDLGANWAETKdTANLdkMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtSVGGL 114
Cdd:cd16147 1 RPNIVLILTDDQDV-ELGSMDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSP--PGGGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 115 P------LNETTLAEVLQQAGYVTGIIGK----WHLGHHGSYHPnfRGFDYYFGI-------PYSHDMGCTDTPGYNHPp 177
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYVP--PGWDEWDGLvgnstyyNYTLSNGGNGKHGVSYP- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 178 cpacpqgdgpsrnlqRDCYTDValplyenlniveqpvnlsslaqkYAEKATQFIQRAS-SGRPFLLYVA----------- 245
Cdd:cd16147 152 ---------------GDYLTDV-----------------------IANKALDFLRRAAaDDKPFFLVVAppaphgpftpa 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 246 --LAHMHVPLPVT------------------QLPAAP-----------RGRslygaglWE----MDSLVGQIKDKVDHT- 289
Cdd:cd16147 194 prYANLFPNVTAPprpppnnpdvsdkphwlrRLPPLNptqiayidelyRKR-------LRtlqsVDDLVERLVNTLEATg 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 290 VKENTFLWFTGDNgpwaqkcelagsvgpftGFW--QTRQGgsPAKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDI 367
Cdd:cd16147 267 QLDNTYIIYTSDN-----------------GYHlgQHRLP--PGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDL 326
|
410 420
....*....|....*....|
gi 1209857069 368 FPTVVALAQASLPqgRRFDG 387
Cdd:cd16147 327 APTILDLAGAPPP--SDMDG 344
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
401-521 |
1.34e-32 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 120.88 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 401 GHRVLFHpNSGAAgefgaLQTVRLERYKAFYITG-----GARACDGSTGPELQHKFPLIFNLEDDTAEAVPLERGGAEYQ 475
Cdd:pfam14707 2 PHEFLFH-YCGAA-----LHAVRWGPYKAHFFTPsfdppGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYP 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1209857069 476 AVLPEVRKVLADVLQDI--ANDNISSADYTQDPSVTPCCnPYQIACRC 521
Cdd:pfam14707 76 EVLAEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-485 |
2.02e-31 |
|
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: 124.98 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAAST----CSPSRASLLTGRLGLRNGVTRNFAvt 109
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFHAPEGGKAA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 110 svggLPLNETTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd16155 79 ----IPSDDKTWPETFKKAGYRTFATGKWHNG------------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 190 nlqrdcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQRASSG-RPFLLYVALAHMH-----------------V 251
Cdd:cd16155 107 ---------------------------------FADAAIEFLEEYKDGdKPFFMYVAFTAPHdprqappeyldmyppetI 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 252 PLPVTQLPAAP------------------------RGRSLYGAGLWEMDSLVGQIKDKVDHTVK-ENTFLWFTGDNGpwa 306
Cdd:cd16155 154 PLPENFLPQHPfdngegtvrdeqlapfprtpeavrQHLAEYYAMITHLDAQIGRILDALEASGElDNTIIVFTSDHG--- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 307 qkceLAgsVGpftgfwqtrQGGSPAKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFD 386
Cdd:cd16155 231 ----LA--VG---------SHGLMGKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES--VE 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 387 GVDVSEVLFGRSQPGHRVLFhpnsgaaGEFGALQ-TVRLERYKAFYITGGAracdgstgpelqhKFPLIFNLEDDTAEAV 465
Cdd:cd16155 293 GKSLLPVIRGEKKAVRDTLY-------GAYRDGQrAIRDDRWKLIIYVPGV-------------KRTQLFDLKKDPDELN 352
|
490 500
....*....|....*....|
gi 1209857069 466 PLErGGAEYQAVLPEVRKVL 485
Cdd:cd16155 353 NLA-DEPEYQERLKKLLAEL 371
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-389 |
7.41e-30 |
|
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: 118.03 E-value: 7.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILAD----DMgwgdLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrnfavtsV 111
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW-------G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 112 GGLPLNETTLAEVLQQAGYVTGIIGKWhlgHHGSYHPNF-RGFDYYFGIPYSHdmgcTDTPGYNHPPCPACpqgdgpsrn 190
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAVSSN---PHLFGGPGFdRGFDTFEDFRGQE----GDPGEEGDERAERV--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 191 lqrdcyTDVALplyenlniveqpvnlsslaqkyaekatQFIQRASSGRPFLLYValaHMHvplpvtqlpaAPRGRSLYGA 270
Cdd:cd16148 134 ------TDRAL---------------------------EWLDRNADDDPFFLFL---HYF----------DPHEPYLYDA 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 271 GLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGpwaqkcELAGSVGPFTGFWqtrqggspakQTTWEGGHRVPALAYWP 349
Cdd:cd16148 168 EVRYVDEQIGRLLDKLKeLGLLEDTLVIVTSDHG------EEFGEHGLYWGHG----------SNLYDEQLHVPLIIRWP 231
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1209857069 350 GRVPVNVTStALLSVLDIFPTVVALAQASLPqgRRFDGVD 389
Cdd:cd16148 232 GKEPGKRVD-ALVSHIDIAPTLLDLLGVEPP--DYSDGRS 268
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-460 |
1.61e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 109.94 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVtsvggLP 115
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP-----YD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 116 LNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHpnfrGFDYyfgipyshDMGCTDTpgynhppcpacpqgdgpsrnlqrdc 195
Cdd:cd16037 76 GDVPSWGHALRAAGYETVLIGKLHFRGEDQRH----GFRY--------DRDVTEA------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 196 ytdvalplyenlniveqpvnlsslAQKYAEKatqfiqRASSGRPFLLYVALAHMHVPLPVTQ---LPAAPRGRSLYGAGL 272
Cdd:cd16037 119 ------------------------AVDWLRE------EAADDKPWFLFVGFVAPHFPLIAPQefyDLYVRRARAAYYGLV 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 273 WEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSvgpfTGFWQtrqggspaKQTTWEGGHRVPALAYWPGR 351
Cdd:cd16037 169 EFLDENIGRVLDALEELgLLDNTLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMIISGPGI 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 352 VPVNVTSTAlLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGRSQPGHRVL--FHPNSGAAGEFgalqTVRLERYKA 429
Cdd:cd16037 231 PAGKRVKTP-VSLVDLAPTILEAAGAPPP--PDLDGRSLLPLAEGPDDPDRVVFseYHAHGSPSGAF----MLRKGRWKY 303
|
410 420 430
....*....|....*....|....*....|.
gi 1209857069 430 FYITGGAracdgstgPELqhkfpliFNLEDD 460
Cdd:cd16037 304 IYYVGYP--------PQL-------FDLEND 319
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-404 |
2.56e-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: 108.83 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDM-GWGDLGANWAETKDTAnLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGGL 114
Cdd:cd16035 1 PNILLILTDQErYPPPWPAGWAALNLPA-RERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 115 PLNETTLAEVLQQAGYVTGIIGKWHLGHHGsyhpnfRGfdyyfgipyshdmgctdtpGYNHPPcpacpqgdgpsrnlqrd 194
Cdd:cd16035 80 SPDVPTLGHMLRAAGYYTAYKGKWHLSGAA------GG-------------------GYKRDP----------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 195 cytdvalplyenlniveqpvnlsslaqKYAEKATQFIQ----RASSGRPFLLYVALAHMH-VPLPVTQLPAAPRGRSLYG 269
Cdd:cd16035 118 ---------------------------GIAAQAVEWLRergaKNADGKPWFLVVSLVNPHdIMFPPDDEERWRRFRNFYY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 270 AGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGpftgfwQTRQGGSPAKQTTwegghRVPALAYW 348
Cdd:cd16035 171 NLIRDVDRQIGRVLDALDASgLADNTIVVFTSDHG------EMGGAHG------LRGKGFNAYEEAL-----HVPLIISH 233
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 349 PGRVPVNVTSTALLSVLDIFPTVVALAQASLPQ----GRRFDGVDVSEVLfgRSQPGHRV 404
Cdd:cd16035 234 PDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEArateAPPLPGRDLSPLL--TDADADAV 291
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
36-460 |
3.31e-26 |
|
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: 109.21 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvgGLP 115
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-----EFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 116 LNETTLAEVLQQAGYVTGIIGKWHlghhgsyhpnFRGFDYYFGipYSHDmgctdtpgynhppcpacpqgdgpsrnlqrdc 195
Cdd:cd16032 76 ADIPTFAHYLRAAGYRTALSGKMH----------FVGPDQLHG--FDYD------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 196 yTDVALplyenlniveqpvnlsslaqkyaeKATQFI---QRASSGRPFLLYVALAHMHVPLPVTQ------LPAApRgRS 266
Cdd:cd16032 113 -EEVAF------------------------KAVQKLydlARGEDGRPFFLTVSFTHPHDPYVIPQeywdlyVRRA-R-RA 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 267 LYGAGLWeMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSvgpfTGFWQtrqggspaKQTTWEGGHRVPAL 345
Cdd:cd16032 166 YYGMVSY-VDDKVGQLLDTLERTgLADDTIVIFTSDHG------DMLGE----RGLWY--------KMSFFEGSARVPLI 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 346 AYWPGR-VPVNVtsTALLSVLDIFPTVVALAQASLPQGR-RFDGVDVSEVLFGRSQPGHRVLFHPNSGaAGEFGALQTVR 423
Cdd:cd16032 227 ISAPGRfAPRRV--AEPVSLVDLLPTLVDLAGGGTAPHVpPLDGRSLLPLLEGGDSGGEDEVISEYLA-EGAVAPCVMIR 303
|
410 420 430
....*....|....*....|....*....|....*..
gi 1209857069 424 LERYKAFYITGgaracDGstgpelqhkfPLIFNLEDD 460
Cdd:cd16032 304 RGRWKFIYCPG-----DP----------DQLFDLEAD 325
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-392 |
3.51e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 105.15 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 35 KPNFVIILADDMGWGDLGA-NWAETKD---------TANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTR 104
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCyNNAHTGKsesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 105 NFAVTSVGGLPLneTTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqg 184
Cdd:cd16153 81 FEAAHPALDHGL--PTFPEVLKKAGYQTASFGKSHLE------------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 185 dgpsrNLQRdcYTDVALPLYENLNIVEqpvnlsslaqkyaekatqfIQRASSGRPFLLYVALAHMHVP-LPvtqlPAAPR 263
Cdd:cd16153 116 -----AFQR--YLKNANQSYKSFWGKI-------------------AKGADSDKPFFVRLSFLQPHTPvLP----PKEFR 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 264 GRSLYGAGLWEMDSLVGQIKDKVD----HTVKENTFLWFTGDNGpwaqkcelagsvgpftgfWQTRQGGSPAKQTTWEGG 339
Cdd:cd16153 166 DRFDYYAFCAYGDAQVGRAVEAFKayslKQDRDYTIVYVTGDHG------------------WHLGEQGILAKFTFWPQS 227
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1209857069 340 HRVPALAYWPGR--VPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSE 392
Cdd:cd16153 228 HRVPLIVVSSDKlkAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
36-375 |
5.05e-25 |
|
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: 103.65 E-value: 5.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCS-PSRASLLTGRLGLRNGVTRNFAVT----- 109
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSaPNHAALLTGAYPTLHGYTGNGSADpelps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 110 SVGGLPLNETTLAEVLQQAGYVTGIIGKWhlghhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIGLL--------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 190 nlqrdcytdvalplyenlniveqpvnlsslaqkyaekatQFIQRASSGRPFLLYVALAHMHVPL--PVTQLPaaprgrsL 267
Cdd:cd00016 110 ---------------------------------------KAIDETSKEKPFVLFLHFDGPDGPGhaYGPNTP-------E 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 268 YGAGLWEMDSLVGQIKDKV-DHTVKENTFLWFTGDNGpwaqkcelAGSVGPftgfwqTRQGGSPAKQTTWEGGHRVPALA 346
Cdd:cd00016 144 YYDAVEEIDERIGKVLDALkKAGDADDTVIIVTADHG--------GIDKGH------GGDPKADGKADKSHTGMRVPFIA 209
|
330 340
....*....|....*....|....*....
gi 1209857069 347 YWPGrVPVNVTSTALLSVLDIFPTVVALA 375
Cdd:cd00016 210 YGPG-VKKGGVKHELISQYDIAPTLADLL 237
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
34-427 |
1.20e-23 |
|
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: 103.42 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 34 QKPNFVIILADDM----GWgdLGANWAETkdtANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrNFAVT 109
Cdd:cd16030 1 KKPNVLFIAVDDLrpwlGC--YGGHPAKT---PNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVY-DNNSY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 110 SVGGLPlNETTLAEVLQQAGYVTGIIGK-WHlGHHGSYHPNFRGFDYYFGIP--------YSHDMGCTDTPGYNHPPCPA 180
Cdd:cd16030 75 FRKVAP-DAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPPgpekyppgKLCPGKKGGKGGGGGPAWEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 181 CPQGDGPsrnlqrdcYTDvalplyenlniveqpvnlsslaQKYAEKATQFIQRAS-SGRPFLLYVALAHMHVPLPVTQ-- 257
Cdd:cd16030 153 ADVPDEA--------YPD----------------------GKVADEAIEQLRKLKdSDKPFFLAVGFYKPHLPFVAPKky 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 258 ------------------------------LPAAPRGRSLYG--------AGLWE------------MDSLVGQIKDKVD 287
Cdd:cd16030 203 fdlyplesiplpnpfdpidlpevawndlddLPKYGDIPALNPgdpkgplpDEQARelrqayyasvsyVDAQVGRVLDALE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 288 -HTVKENTFLWFTGDNGpWA--QKcelagsvgpftGFWqtrqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSV 364
Cdd:cd16030 283 eLGLADNTIVVLWSDHG-WHlgEH-----------GHW--------GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVEL 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1209857069 365 LDIFPTVVALAQasLPQGRRFDGVDVSEVLFGRSQPGHRVLF--HPNSGAAGEfgalqTVRLERY 427
Cdd:cd16030 343 VDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKDAAFsqYPRPSIMGY-----SIRTERY 400
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-140 |
1.09e-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: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNfavtsVGGL 114
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPL 75
|
90 100
....*....|....*....|....*.
gi 1209857069 115 PLNETTLAEVLQQAGYVTGIIGKWHL 140
Cdd:cd16152 76 PADEKTLAHYFRDAGYETGYVGKWHL 101
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
36-428 |
8.48e-20 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293775 [Multi-domain] Cd Length: 468 Bit Score: 92.06 E-value: 8.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGvtrnfAVTSVGGLP 115
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNG-----SWTNCMALG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 116 LNETTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrGFDYY-FGIpyshdmgctdtpgynhppcpaCPQGDGPSRNLQRD 194
Cdd:cd16156 76 DNVKTIGQRLSDNGIHTAYIGKWHLD----------GGDYFgNGI---------------------CPQGWDPDYWYDMR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 195 CYTD-----------VALPLYENLNIVEQpvnlSSLAQKYAEKATQFIQRASSgRPFLLYVALAHMHVPL---------- 253
Cdd:cd16156 125 NYLDelteeerrksrRGLTSLEAEGIKEE----FTYGHRCTNRALDFIEKHKD-EDFFLVVSYDEPHHPFlcpkpyasmy 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 254 -------------------PVTQLPAAPRGRSLYGAGLWEM----------DSLVGQIKDKVDHTVkENTFLWFTGDNGp 304
Cdd:cd16156 200 kdfefpkgenayddlenkpLHQRLWAGAKPHEDGDKGTIKHplyfgcnsfvDYEIGRVLDAADEIA-EDAWVIYTSDHG- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 305 waqkcELAGSvgpftgfwQTRQGGSPAkqtTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQasLPQGRR 384
Cdd:cd16156 278 -----DMLGA--------HKLWAKGPA---VYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKV 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1209857069 385 FDGVDVSEVLFGRSQPGHRVLF---------HPNsgaageFGALQTVRL---ERYK 428
Cdd:cd16156 340 LEGESILATIEDPEIPENRGVFvefgryevdHDG------FGGFQPVRCvvdGRYK 389
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-398 |
1.07e-15 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 79.20 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGR----LGLRngvtrnfavTSV 111
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWyphvNGHR---------TLH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 112 GGLPLNETTLAEVLQQAGYVTGIIGKWHLghhgsyhpnfrgfdyyfgIPYSHDMGCTDTPGYnhppcpacpqgdgpsrnl 191
Cdd:cd16150 72 HLLRPDEPNLLKTLKDAGYHVAWAGKNDD------------------LPGEFAAEAYCDSDE------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 192 qrdcytdvalplyenlniveqpvnlsslaqKYAEKATQFIQRASSGRPFLLYVALAHMHVP---------------LPVT 256
Cdd:cd16150 116 ------------------------------ACVRTAIDWLRNRRPDKPFCLYLPLIFPHPPygveepwfsmidrekLPPR 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 257 --------QLPAAPRGRSLYGAGLW-----------------EMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAqkce 310
Cdd:cd16150 166 rppglrakGKPSMLEGIEKQGLDRWseerwrelratylgmvsRLDHQFGRLLEALKETgLYDDTAVFFFSDHGDYT---- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 311 lagsvGPFtGFWQTRQGGSPAKQTtwegghRVPALAYWPGRVPVNVTStALLSVLDIFPTVVALAqaslpqgrrfdGVDV 390
Cdd:cd16150 242 -----GDY-GLVEKWPNTFEDCLT------RVPLIIKPPGGPAGGVSD-ALVELVDIPPTLLDLA-----------GIPL 297
|
....*...
gi 1209857069 391 SEVLFGRS 398
Cdd:cd16150 298 SHTHFGRS 305
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
36-157 |
5.69e-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: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvgGLP 115
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT-----PLD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1209857069 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 ... |
36-382 |
3.99e-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: 70.65 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGrlgLRNGVTRNFavTSVGGLP 115
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG---LFTHLTESW--NNYKGLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 116 LNETTLAEVLQQAGYVTGIIGK--WHLGHHGSYHpnfRGFDYYFGIPYShdmgctdtpgynhppcpaCPQGDGPSRNLQR 193
Cdd:cd16171 76 PNYPTWMDRLEKHGYHTQKYGKldYTSGHHSVSN---RVEAWTRDVPFL------------------LRQEGRPTVNLVG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 194 DCYTDvalplyenlniveqpvNLSSLAQKYAEKATQFIQRASSG--RPFLLYVALAHMHvPLPVTQLPAAPRG----RSL 267
Cdd:cd16171 135 DRSTV----------------RVMLKDWQNTDKAVHWIRKEAPNltQPFALYLGLNLPH-PYPSPSMGENFGSirniRAF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 268 YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAgsvgpftgfWQTRQGgspAKQTTWEGGHRVPALA 346
Cdd:cd16171 198 YYAMCAETDAMLGEIISALKDTgLLDKTYVFFTSDHG------ELA---------MEHRQF---YKMSMYEGSSHVPLLI 259
|
330 340 350
....*....|....*....|....*....|....*.
gi 1209857069 347 YWPGrVPVNVTSTALLSVLDIFPTVVALAQASLPQG 382
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 1209857069 28 SGKTRGQKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVtrnfA 107
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGS----P 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 108 VTSVGGLPLNetTLAEVLQQAGYVTGIIgkwHlGHHGS------YHPNFrGFDYYFGIPY 161
Cdd:COG1368 303 YKRPGQNNFP--SLPSILKKQGYETSFF---H-GGDGSfwnrdsFYKNL-GFDEFYDRED 355
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
20-370 |
1.43e-04 |
|
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: 44.51 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 20 YPLVDfcISGKTRGQKPNFVIILADDMGWGDLGAnwaetKDTANLDKMASEGMRFVDfHAAASTCSPsrasllTGRLGLR 99
Cdd:COG3083 231 YPLHP--LQFSDPAKPPNILLIVVDSLRADMLDP-----EVMPNLYAFAQRSLRFTN-HYSSGNSTR------AGLFGLF 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 100 NGVTRNFAvTSVgglpLNETT---LAEVLQQAGYVTGIigkwhlghhgsyhpnfrgfdyyfgipYSHDmgctdtpGYNHP 176
Cdd:COG3083 297 YGLPGNYW-DSI----LAERTppvLIDALQQQGYQFGL--------------------------FSSA-------GFNSP 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 177 PcpacpqgdgpsrnLQRDCYTDVALPLYENLNIVEQPvnlsslAQKYAEKATQFIQRASSGRPFLLYVALAHMH------ 250
Cdd:COG3083 339 L-------------FRQTIFSDVSLPRLHTPGGPAQR------DRQITAQWLQWLDQRDSDRPWFSYLFLDAPHaysfpa 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 251 ------------VPLPVTQLPAAPRGRSLYGAGLWEMDSLVGQIKDKVDHTVK-ENTFLWFTGDNGPwaqkcelagsvgP 317
Cdd:COG3083 400 dypkpfqpsedcNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLlENTIVIITADHGE------------E 467
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1209857069 318 F----TGFWQTRQGGSPAkQTtwegghRVPALAYWPGRVPVNVTStaLLSVLDIFPT 370
Cdd:COG3083 468 FnengQNYWGHNSNFSRY-QL------QVPLVIHWPGTPPQVISK--LTSHLDIVPT 515
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
14-162 |
1.16e-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: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 14 SFSGFLYPLVDFCISGKTRGQKPnFVIILADDMGWGDLGANwaetkDTANLDKMASEGMRFVDFHAA--ASTCsPSRASL 91
Cdd:COG1524 3 RGLSLLLASLLAAAAAAAPPAKK-VVLILVDGLRADLLERA-----HAPNLAALAARGVYARPLTSVfpSTTA-PAHTTL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857069 92 LTGRLGLRNGVTRNF--------AVTSVGGLP--------LNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPN----FR 151
Cdd:COG1524 76 LTGLYPGEHGIVGNGwydpelgrVVNSLSWVEdgfgsnslLPVPTIFERARAAGLTTAAVFWPSFEGSGLIDAArpypYD 155
|
170
....*....|.
gi 1209857069 152 GFDYYFGIPYS 162
Cdd:COG1524 156 GRKPLLGNPAA 166
|
|
| |
