|
Name |
Accession |
Description |
Interval |
E-value |
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
23-479 |
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: 526.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 23 PPNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGArwtggVFSS 102
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGV-----VGPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 103 IAKGGLPENETTFASLLSDVGYSSLAIGKWHVGQQPQFLPTSHGFDEYFGIPYSVDMGNSAWAssGYTKIQVPLPLLHNK 182
Cdd:cd16026 76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLY--RNDPPGPLPPLMENE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 183 TVIEQPVNLNTLEKRYAEKASDFIHKNAaaQKPFLIYLAWSHAHVPDFVTPSMCNSSRRGRFGDAMEEMDSHIGDVMAAL 262
Cdd:cd16026 154 EVIEQPADQSSLTQRYTDEAVDFIERNK--DQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 263 KNAGVDDNTLVFFTSDNGPWLIQRLSGGSQGTFFEGKTTTWEGGVREPAIVRWPGKVAAGSVSREVVATYDIFATIVSLA 342
Cdd:cd16026 232 KELGLEENTLVIFTSDNGPWLEYGGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 343 GAKLPQDRVIDGRDISGVLFRGQKSPHNCLFHYKGTpstglppkpddsqPGLWAVRCGAYKAHYVTSCAVMQNWGDkrcr 422
Cdd:cd16026 312 GAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDG-------------GDLQAVRSGRWKLHLPTTYRTGTDPGG---- 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2003236968 423 sttyswngmkdlaheaafklcretlamdecalllsSSPVLHNPPILYNVEHDPSELY 479
Cdd:cd16026 375 -----------------------------------LDPTKLEPPLLYDLEEDPGETY 396
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
23-536 |
4.02e-161 |
|
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: 468.08 E-value: 4.02e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 23 PPNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIagarwTGGVFSS 102
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGV-----YPGVFYP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 103 IAKGGLPENETTFASLLSDVGYSSLAIGKWH--VGQQPQFLPTSHGFDEYFGIPYSVDMGNSAWASSGYTKIQ------- 173
Cdd:cd16158 76 GSRGGLPLNETTIAEVLKTVGYQTAMVGKWHlgVGLNGTYLPTHQGFDHYLGIPYSHDQGPCQNLTCFPPNIPcfggcdq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 174 --VPLPLLHNKTVIEQPVNLNTLEKRYAEKASDFIHKNAAAQKPFLIYLAWSHAHVPDFVTPSMCNSSRRGRFGDAMEEM 251
Cdd:cd16158 156 geVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 252 DSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLIQRLSGGSQGTFFEGKTTTWEGGVREPAIVRWPGKVAAGsVSREVVAT 331
Cdd:cd16158 236 DGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRKSRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPG-VTHELAST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 332 YDIFATIVSLAGAKLPqDRVIDGRDISGVLFRGQKSPHNCLFHYkgtpstglPPKPDDSQpGLWAVRCGAYKAHYVT-SC 410
Cdd:cd16158 315 LDILPTIAKLAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYY--------PTSPDPDK-GVFAVRWGKYKAHFYTqGA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 411 AVMQNWGDKRCRsttyswngmkdlaheaafklcretlamdecallLSSSPVLHNPPILYNVEHDPSELYQISpKSSEYQA 490
Cdd:cd16158 385 AHSGTTPDKDCH---------------------------------PSAELTSHDPPLLFDLSQDPSENYNLL-GLPEYNQ 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2003236968 491 AMETITQAKKEHEATLTPVPNQIAMGMDNSRRVCCDNNTKP---ACTCN 536
Cdd:cd16158 431 VLKQIQQVKERFEASMKFGESEINKGEDPALEPCCKPGCTPkpsCCQCH 479
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
23-477 |
8.29e-156 |
|
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: 450.77 E-value: 8.29e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 23 PPNFLILFADDMGYGDMSCNGHPS-IATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIagarwtGGVFS 101
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNaILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV------GHNFL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 102 SIAKGGLPENETTFASLLSDVGYSSLAIGKWHVGQQPQFLPTSHGFDEYFGIPYSVDmgnsawassgytkiqvplpllhn 181
Cdd:cd16161 75 PTSVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 182 ktvieqpvnlNTLEKRYAEKASDFIHKNAAAQKPFLIYLAWSHAHVPDFVTPSMCNSSR-RGRFGDAMEEMDSHIGDVMA 260
Cdd:cd16161 132 ----------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSgRGPYGDALQEMDDLVGQIMD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 261 ALKNAGVDDNTLVFFTSDNGPWLIQRLSGGSQGTFFE--------GKTTTWEGGVREPAIVRWPGKVAAGSVSREVVATY 332
Cdd:cd16161 202 AVKHAGLKDNTLTWFTSDNGPWEVKCELAVGPGTGDWqgnlggsvAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 333 DIFATIVSLAGAKLPQDRVIDGRDISGVLFRGQKSPHNCLFHykgtpstglPPKPDDSQPGLWAVRCGAYKAHYVTSCAV 412
Cdd:cd16161 282 DIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFH---------PNSGAAGAGALSAVRCGDYKAHYATGGAL 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2003236968 413 MQnwgdkrCRSTtyswngmkdlaheaafklcretlamdecalllsSSPVLHNPPILYNVEHDPSE 477
Cdd:cd16161 353 AC------CGST---------------------------------GPKLYHDPPLLFDLEVDPAE 378
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
24-483 |
1.10e-138 |
|
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: 409.51 E-value: 1.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGARwtgGVFSSI 103
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGT---RVFLPW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 AKGGLPENETTFASLLSDVGYSSLAIGKWHVGQQPQ------FLPTSHGFDeYFG--IPYsvdmGNSaWASSgYTKIQVP 175
Cdd:cd16160 79 DIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENnhsdgaHLPSHHGFD-FVGtnLPF----TNS-WACD-DTGRHVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 176 LP------LLHNKTVIEQPVNLNTLEKRYAEKASDFIHKNAaaQKPFLIYLAWSHAHVPDFVTPSMCNSSRRGRFGDAME 249
Cdd:cd16160 152 FPdrsacfLYYNDTIVEQPIQHEHLTETLVGDAKSFIEDNQ--ENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNIN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 250 EMDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLIQRLSGGSQGTFFEGKTTTWEGGVREPAIVRWPGKVAAGsVSREVV 329
Cdd:cd16160 230 EMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIKPR-VSHEVV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 330 ATYDIFATIVSLAGAKLPQDRVIDGRDISGVLFRGQKSPHN-CLFHYKGTpstglppkpddsqpgLWAVRCGAYKAHYVT 408
Cdd:cd16160 309 STMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDdILYYCCSR---------------LMAVRYGSYKIHFKT 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2003236968 409 SCAVMQNWGDKRCRsttyswngmkDLAHEAAFKLCREtlAMDECAlllssspVLHNPPILYNVEHDPSELYQISP 483
Cdd:cd16160 374 QPLPSQESLDPNCD----------GGGPLSDYIVCYD--CEDECV-------TKHNPPLIFDVEKDPGEQYPLQP 429
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
23-514 |
1.91e-133 |
|
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: 398.58 E-value: 1.91e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 23 PPNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGARWTGGVFSS 102
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 103 IAKGGLPENETTFASLLSDVGYSSLAIGKWHVG------QQPQFLPTSHGFDEYFGIPY------------SVDMGN--- 161
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGlhcesrNDFCHHPLNHGFDYFYGLPLtnlkdcgdgsngEYDLSFdpl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 162 ----SAWASSGYTKIQVPLPLLH------------------------------------NKTVIEQPVNLNTLEKRYAEK 201
Cdd:cd16159 161 fpllTAFVLITALTIFLLLYLGAvskrffvfllilsllfislfflllitnryfncilmrNHEVVEQPMSLENLTQRLTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 202 ASDFIHKNAaaQKPFLIYLAWSHAHVPDFVTPSMCNSSRRGRFGDAMEEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGP 281
Cdd:cd16159 241 AISFLERNK--ERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 282 WL-----IQRLSGGSQGTFFEGKTTTWEGGVREPAIVRWPGKVAAGSVSREVVATYDIFATIVSLAGAKLPQDRVIDGRD 356
Cdd:cd16159 319 HLeeisvGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 357 ISGVLfRGQK--SPHNCLFHYKGTPSTGLPPKPDDSQpglwAVrcgaYKAHYVTScavmqNW--GDKRCRSTTyswngmk 432
Cdd:cd16159 399 LMPLL-TGQEkrSPHEFLFHYCGAELHAVRYRPRDGG----AV----WKAHYFTP-----NFypGTEGCCGTL------- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 433 dlaheaafkLCRetlamdecalLLSSSPVLHNPPILYNVEHDPSELYQISPKSSEYQAAMETITQAKKEHEATLTPVPNQ 512
Cdd:cd16159 458 ---------LCR----------CFGDSVTHHDPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIEPVESQ 518
|
..
gi 2003236968 513 IA 514
Cdd:cd16159 519 LS 520
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
23-515 |
4.94e-126 |
|
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: 377.58 E-value: 4.94e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 23 PPNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGI----AGARwtGG 98
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFyttnAHAR--NA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 99 VFSSIAKGGLPENETTFASLLSDVGYSSLAIGKWHVGQQPQFLPTSHGFDEYFGIPysvdmgNSAWASsgYTKIQVP-LP 177
Cdd:cd16157 79 YTPQNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAP------NCHFGP--YDNKAYPnIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 178 LLHNKTVI-----EQPVNLNT----LEKRYAEKASDFIHKNAAAQKPFLIYLAWSHAHVPDFVTPSMCNSSRRGRFGDAM 248
Cdd:cd16157 151 VYRDWEMIgryyeEFKIDKKTgesnLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 249 EEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLIQR-LSGGSQGTFFEGKTTTWEGGVREPAIVRWPGKVAAGSVSRE 327
Cdd:cd16157 231 MELDSSVGKILESLKSLGIENNTFVFFSSDNGAALISApEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 328 VVATYDIFATIVSLAGAKLPQDRVIDGRDISGVLFRGqKSPHNCLFHYKGTPstglppkpddsqpgLWAVRCGAYKAHYv 407
Cdd:cd16157 311 LGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNG-KEKDRPIFYYRGDE--------------LMAVRLGQYKAHF- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 408 tscavmqnwgdkrcrsttYSWNGMKDlaheaAFKlcretLAMDECALLLSSSPVLHN------PPILYNVEHDPSELYQI 481
Cdd:cd16157 375 ------------------WTWSNSWE-----EFR-----KGINFCPGQNVPGVTTHNqtdhtkLPLLFHLGRDPGEKYPI 426
|
490 500 510
....*....|....*....|....*....|....
gi 2003236968 482 SPKSSEYQAAMETITQAKKEHEATLTPVPNQIAM 515
Cdd:cd16157 427 SFKSAEYKQAMPRISKVVQQHQKTLVPGEPQLNV 460
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-406 |
3.46e-124 |
|
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: 369.55 E-value: 3.46e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGH---PSIATPNLDKLAAEGMRLTQWYSGfHVCSPSRASMLTGRLPIRSGIAGARWTGgvf 100
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGgigRGAPTPNIDRLAKEGLRFTSFYVE-PSCTPGRAAFITGRHPIRTGLTTVGLPG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 101 ssiAKGGLPENETTFASLLSDVGYSSLAIGKWHVGQQPQFLPTSHGFDEYFGIPYSvdmgnsawassgytkiqvplpllh 180
Cdd:cd16142 77 ---SPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYH------------------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 181 nktvieqpvnlnTLEKRYAEKASDFIHKNAAAQKPFLIYLAWSHAHVPDFVTP-SMCNSSRRGRFGDAMEEMDSHIGDVM 259
Cdd:cd16142 130 ------------TIDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPeFEGKSSGKGKYADSMVELDDHVGQIL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 260 AALKNAGVDDNTLVFFTSDNGPWLIQRLSGGSqgTFFEG-KTTTWEGGVREPAIVRWPGKVAAGSVSREVVATYDIFATI 338
Cdd:cd16142 198 DALDELGIADNTIVIFTTDNGPEQDVWPDGGY--TPFRGeKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTL 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2003236968 339 VSLAGAKLP------QDRVIDGRDISGVLF-RGQKSPHNCLFHYkgtpstglppkpDDSQPGlwAVRCGAYKAHY 406
Cdd:cd16142 276 AALAGAPDPkdkllgKDRHIDGVDQSPFLLgKSEKSRRSEFFYF------------GEGELG--AVRWKNWKVHF 336
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-406 |
5.78e-106 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 323.37 E-value: 5.78e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 1 MYWQIQTLLLLLSFSCVGATTKPPNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASML 80
Cdd:COG3119 1 MKRLLLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 81 TGRLPIRSGIAGarwtggvFSSIAKGGLPENETTFASLLSDVGYSSLAIGKWHVgqqpqflptshgfdeyfgipYSVDmg 160
Cdd:COG3119 81 TGRYPHRTGVTD-------NGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------YLTD-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 161 nsawassgytkiqvplpllhnktvieqpvnlntlekRYAEKASDFIHKNAAAQKPFLIYLAWSHAHVP------------ 228
Cdd:COG3119 132 ------------------------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPyqapeeyldkyd 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 229 --DFVTPSMCNS---------SRRGRFGDAMEEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLiqrlsgGSQGtFFE 297
Cdd:COG3119 176 gkDIPLPPNLAPrdlteeelrRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSL------GEHG-LRG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 298 GKTTTWEGGVREPAIVRWPGKVAAGSVSREVVATYDIFATIVSLAGAKLPQDrvIDGRDISGVLFRGQKSPHNCLFHYkg 377
Cdd:COG3119 249 GKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWE-- 324
|
410 420
....*....|....*....|....*....
gi 2003236968 378 tpstglppkpDDSQPGLWAVRCGAYKAHY 406
Cdd:COG3119 325 ----------YPRGGGNRAIRTGRWKLIR 343
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-406 |
1.01e-98 |
|
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: 306.01 E-value: 1.01e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSG----IAGARWTGGV 99
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGitdvIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 100 FSSIA---KGGLPENETTFASLLSDVGYSSLAIGKWHVGQQPQFLPTSHGFDEYFGipysvdMGNSAWASSGYTKIQVPL 176
Cdd:cd16144 81 TKLIPppsTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIG------GTGNGGPPSYYFPPGKPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 177 PLLHNKTVIEQPVNlntlekRYAEKASDFIHKNaaAQKPFLIYLaWSHA-HVP-----DFV------TPSMCNSSRRGRF 244
Cdd:cd16144 155 PDLEDGPEGEYLTD------RLTDEAIDFIEQN--KDKPFFLYL-SHYAvHTPiqarpELIekyekkKKGLRKGQKNPVY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 245 GdAM-EEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLIQRLSGGSQGTFFEGKTTTWEGGVREPAIVRWPGKVAAGS 323
Cdd:cd16144 226 A-AMiESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 324 VSREVVATYDIFATIVSLAGAKLPQDRVIDGRDISGVLFRG-QKSPHNCLF-HY------KGTPSTglppkpddsqpglw 395
Cdd:cd16144 305 VSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGeADLPRRALFwHFphyhgqGGRPAS-------------- 370
|
410
....*....|.
gi 2003236968 396 AVRCGAYKAHY 406
Cdd:cd16144 371 AIRKGDWKLIE 381
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-369 |
5.83e-98 |
|
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: 302.97 E-value: 5.83e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSC-NGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGARWTGGVFSS 102
Cdd:cd16143 1 PNIVIILADDLGYGDISCyNPDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 103 IakgglPENETTFASLLSDVGYSSLAIGKWHVG-------QQPQFL---------------PTSHGFDEYFGIPYSvdmg 160
Cdd:cd16143 81 I-----EPDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdGKKAATgtgkdvdyskpikggPLDHGFDYYFGIPAS---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 161 nsawassgytkiQVpLPLLHNKTVieqpvnlntlekryaekasDFIHKNAAAQKPFLIYLAWSHAHVPDFVTPSMCNSSR 240
Cdd:cd16143 152 ------------EV-LPTLTDKAV-------------------EFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQGKSG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 241 RGRFGDAMEEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGP------WLIQRLSGGSQGTFFEGKTTTWEGGVREPAIVR 314
Cdd:cd16143 200 AGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPspyadyKELEKFGHDPSGPLRGMKADIYEGGHRVPFIVR 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2003236968 315 WPGKVAAGSVSREVVATYDIFATIVSLAGAKLPQDRVIDGRDISGVLfRGQKSPH 369
Cdd:cd16143 280 WPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPAL-LGPKKQE 333
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-404 |
1.37e-89 |
|
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: 282.18 E-value: 1.37e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGARWTGGVFSsi 103
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 akggLPENETTFASLLSDVGYSSLAIGKWHVGQQPQF-LPTSHGFDEYFGI-----------PYSVDMGNsawassgytk 171
Cdd:cd16145 79 ----LPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYGYldqvhahnyypEYLWRNGE---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 172 iQVPLPllhNKTVIEQPVNLNTLEKR--YAE-----KASDFIHKNAAaqKPFLIYLAWS--HA--HVPDFVTPSM----- 235
Cdd:cd16145 145 -KVPLP---NNVIPPLDEGNNAGGGGgtYSHdlftdEALDFIRENKD--KPFFLYLAYTlpHAplQVPDDGPYKYkpkdp 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 236 -CNSSRRGRFGDA-----MEEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGPwliqRLSGGSQ--GTFFE-------GKT 300
Cdd:cd16145 219 gIYAYLPWPQPEKayaamVTRLDRDVGRILALLKELGIDENTLVVFTSDNGP----HSEGGSEhdPDFFDsngplrgYKR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 301 TTWEGGVREPAIVRWPGKVAAGSVSREVVATYDIFATIVSLAGAKLPQDrvIDGRDISGVLF-RGQKSPHNCL---FHYK 376
Cdd:cd16145 295 SLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLgKPQQQQHDYLyweFYEG 372
|
410 420
....*....|....*....|....*...
gi 2003236968 377 GTPStglppkpddsqpglwAVRCGAYKA 404
Cdd:cd16145 373 GGAQ---------------AVRMGGWKA 385
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
24-356 |
3.71e-85 |
|
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: 264.30 E-value: 3.71e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGARWTGgvfssi 103
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 akGGLPENETTFASLLSDVGYSSLAIGKWHvgqqpqflptshgfdeyfgipysvdmgnsawassgytkiqvplpllhnkt 183
Cdd:cd16022 75 --GGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 184 vieqpvnlntlekryaEKASDFIhKNAAAQKPFLIYLAWSHAHVPdFVTPSMCnssrrgrfgdamEEMDSHIGDVMAALK 263
Cdd:cd16022 103 ----------------DEAIDFI-ERRDKDKPFFLYVSFNAPHPP-FAYYAMV------------SAIDDQIGRILDALE 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 264 NAGVDDNTLVFFTSDNGPWLiqrlsgGSQGTFFeGKTTTWEGGVREPAIVRWPGKVAAGSVSREVVATYDIFATIVSLAG 343
Cdd:cd16022 153 ELGLLDNTLIVFTSDHGDML------GDHGLRG-KKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAG 225
|
330
....*....|...
gi 2003236968 344 AKLPQDrvIDGRD 356
Cdd:cd16022 226 IEPPEG--LDGRS 236
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
24-403 |
5.28e-82 |
|
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: 262.10 E-value: 5.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQwysgFHV---CSPSRASMLTGRLPIRSGiagarwtggVF 100
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTN----FHVspvCAPTRAALLTGRYPFRTG---------VW 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 101 SSIAKGG-LPENETTFASLLSDVGYSSLAIGKWHVGQQPQFLPTSHGFDEYFG------IPYSVDMGNSAWASSgytkiq 173
Cdd:cd16146 68 HTILGRErMRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGhggggiGQYPDYWGNDYFDDT------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 174 vplpLLHNKTVIEQpvnlntleKRYA-----EKASDFIHKNAaaQKPFLIYLAWSHAHVPDFVTPSM--------CNSSR 240
Cdd:cd16146 142 ----YYHNGKFVKT--------EGYCtdvffDEAIDFIEENK--DKPFFAYLATNAPHGPLQVPDKYldpykdmgLDDKL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 241 RGRFGdaM-EEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGPW--LIQRLSGGSQGTffegKTTTWEGGVREPAIVRWPG 317
Cdd:cd16146 208 AAFYG--MiENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAggVPKRFNAGMRGK----KGSVYEGGHRVPFFIRWPG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 318 KVAAGSVSREVVATYDIFATIVSLAGAKLPQDRVIDGRDISGVLFRG-QKSPHNCLFHYKGtpstglPPKPDDSQPGLWA 396
Cdd:cd16146 282 KILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGEsDPWPERTLFTHSG------RWPPPPKKKRNAA 355
|
....*..
gi 2003236968 397 VRCGAYK 403
Cdd:cd16146 356 VRTGRWR 362
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
24-403 |
2.38e-78 |
|
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: 252.09 E-value: 2.38e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSgFHVCSPSRASMLTGRLPIRSGIagarwTGGVFSSI 103
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYV-QPICTPSRAALMTGRYPIHTGM-----QHGVILAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 AKGGLPENETTFASLLSDVGYSSLAIGKWHVGQ-QPQFLPTSHGFDEYFGipY---SVDMgnsaWASSGYTKIQVPLPLL 179
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLGFyTWEYTPTNRGFDSFYG--YyggAEDY----YTHTSGGANDYGNDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 180 HNKTVIEQPVNLNTLEKRYAEKASDFIHkNAAAQKPFLIYLAWSHAHVPDFVTPSM-----------CNSSRRgRFGDAM 248
Cdd:cd16029 149 RDNEEPAWDYNGTYSTDLFTDRAVDIIE-NHDPSKPLFLYLAFQAVHAPLQVPPEYadpyedkfahiKDEDRR-TYAAMV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 249 EEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLIQRlSGGSQGTFFEGKTTTWEGGVREPAIVRWPG-KVAAGSVSRE 327
Cdd:cd16029 227 SALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGG-DGGSNYPLRGGKNTLWEGGVRVPAFVWSPLlPPKRGTVSDG 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2003236968 328 VVATYDIFATIVSLAGAKLPQDRVIDGRDISGVLFRGQKSPHNCLFHYKGtpstglppkPDDSQPGLWAVRCGAYK 403
Cdd:cd16029 306 LMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNID---------DITRTTGGAAIRVGDWK 372
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
24-373 |
8.14e-73 |
|
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: 237.02 E-value: 8.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYgDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGARWTGGVfssi 103
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFP---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 akggLPENETTFASLLSDVGYSSLAIGKWHVGQQPQFlptsHGFDEYFGIPysvDMGNSAWassgytkiqvplpllhnkt 183
Cdd:cd16027 76 ----LPDGVKTLPELLREAGYYTGLIGKTHYNPDAVF----PFDDEMRGPD---DGGRNAW------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 184 vieqpvnlntlekRYAEKASDFIhKNAAAQKPFLIYLAWSHAH-------------------VPDFV--TPSMcnssRR- 241
Cdd:cd16027 126 -------------DYASNAADFL-NRAKKGQPFFLWFGFHDPHrpyppgdgeepgydpekvkVPPYLpdTPEV----REd 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 242 -GRFGDAMEEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGpwliqrlsggsqGTFFEGKTTTWEGGVREPAIVRWPGKVA 320
Cdd:cd16027 188 lADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG------------MPFPRAKGTLYDSGLRVPLIVRWPGKIK 255
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2003236968 321 AGSVSREVVATYDIFATIVSLAGAKLPQDrvIDGRDISGVLFRGQKSPHNCLF 373
Cdd:cd16027 256 PGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGRDYVF 306
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
24-344 |
5.23e-66 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 216.91 E-value: 5.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGiagarwtggvFSSI 103
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFG----------SYVS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 AKGGLPENETTFASLLSDVGYSSLAIGKWHVGQQPQFLPTSHGFDEYFG-IPYSVDMGNsawassgytkiqvplpllhNK 182
Cdd:pfam00884 71 TPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLYAD-------------------PP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 183 TVIEQPVNLNTLEKRYAEKASDFIHKNaaaQKPFLIYLAWSHAHVPDFV-----------TPSMC-NSSRRGRFGDAMEE 250
Cdd:pfam00884 132 DVPYNCSGGGVSDEALLDEALEFLDNN---DKPFFLVLHTLGSHGPPYYpdrypekyatfKPSSCsEEQLLNSYDNTLLY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 251 MDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLiqrlsGGSQGTFFEGKT-TTWEGGVREPAIVRWPGKVAAGSVSREVV 329
Cdd:pfam00884 209 TDDAIGRVLDKLEENGLLDNTLVVYTSDHGESL-----GEGGGYLHGGKYdNAPEGGYRVPLLIWSPGGKAKGQKSEALV 283
|
330
....*....|....*
gi 2003236968 330 ATYDIFATIVSLAGA 344
Cdd:pfam00884 284 SHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-403 |
3.38e-65 |
|
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: 217.08 E-value: 3.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSgFHVCSPSRASMLTGRLPIRSGIAGarwtggvfssi 103
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRNYVVF----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 akGGLPENETTFASLLSDVGYSSLAIGKWHVGQQPQFL--PTSHGFDEYfgipysvdmgnSAWASSGYTKiqvplPLLHN 181
Cdd:cd16151 69 --GYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGdyPHEFGFDEY-----------CLWQLTETGE-----KYSRP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 182 KTVIEQPVNLNTLEKR--------YAEKASDFIHKNaaAQKPFLIYLA-----WSHAHVPDFVT---PSMCNSSRRGRFG 245
Cdd:cd16151 131 ATPTFNIRNGKLLETTegdygpdlFADFLIDFIERN--KDQPFFAYYPmvlvhDPFVPTPDSPDwdpDDKRKKDDPEYFP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 246 DAMEEMDSHIGDVMAALKNAGVDDNTLVFFTSDNG--PWLIQRLSGGS-QGtffeGKTTTWEGGVREPAIVRWPGKVAAG 322
Cdd:cd16151 209 DMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGthRPITSRTNGREvRG----GKGKTTDAGTHVPLIVNWPGLIPAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 323 SVSREVVATYDIFATIVSLAGAKLPQDRVIDGRDISGVLfRGQK-SPHNCLFHYkgtpSTGLPPKPDDSQPglwaVRCGA 401
Cdd:cd16151 285 GVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQL-LGKTgSPRREWIYW----YYRNPHKKFGSRF----VRTKR 355
|
..
gi 2003236968 402 YK 403
Cdd:cd16151 356 YK 357
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
22-368 |
1.53e-63 |
|
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: 213.46 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 22 KPPNFLILFADDMGYGDMSCNGHPsIATPNLDKLAAEGMRLTQwysgFHV---CSPSRASMLTGRLPIRSGIAGARWTGG 98
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTN----FHTtalCSPTRAALLTGRNHHQVGMGTMAELAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 99 VFSSIaKGGLPENETTFASLLSDVGYSSLAIGKWHVgqqpqflptshGFDEYfgipYSVDMgnsawassgytkiqvplpl 178
Cdd:cd16025 76 GKPGY-EGYLPDSAATIAEVLKDAGYHTYMSGKWHL-----------GPDDY----YSTDD------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 179 lhnktvieqpvnlntlekrYAEKASDFIHKNAAAQKPFLIYLAWS--HA--HVPD-----FvtpsmcnssrRGRFGD--- 246
Cdd:cd16025 121 -------------------LTDKAIEYIDEQKAPDKPFFLYLAFGapHAplQAPKewidkY----------KGKYDAgwd 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 247 ---------------------------------------------------AM-EEMDSHIGDVMAALKNAGVDDNTLVF 274
Cdd:cd16025 172 alreerlerqkelglipadtkltprppgvpawdslspeekklearrmevyaAMvEHMDQQIGRLIDYLKELGELDNTLII 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 275 FTSDNGPwliqrlSGGS-----QGT-FFEGKTTTWEGGVREPAIVRWP-GKVAAGSVSREVVATYDIFATIVSLAGAKLP 347
Cdd:cd16025 252 FLSDNGA------SAEPgwanaSNTpFRLYKQASHEGGIRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYP 325
|
410 420
....*....|....*....|....*...
gi 2003236968 348 QdrVIDGRD---ISGV----LFRGQKSP 368
Cdd:cd16025 326 K--TVNGVPqlpLDGVsllpTLDGAAAP 351
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-368 |
1.48e-59 |
|
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: 202.80 E-value: 1.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGARWTggvfssi 103
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 akggLPENETTFASLLSDVGYSSLAIGKWHVGQQPQFLPTS----------HGFDEYFGipysvdMGNSAWassgytkiq 173
Cdd:cd16034 75 ----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRAddytppperrHGFDYWKG------YECNHD--------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 174 vplpllHNKTvieqPVNLNTLEKRY---------AEKASDFIHKNAAAQKPFLIYLAWSHAHVPDFVTPSM--------- 235
Cdd:cd16034 136 ------HNNP----HYYDDDGKRIYikgyspdaeTDLAIEYLENQADKDKPFALVLSWNPPHDPYTTAPEEyldmydpkk 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 236 --------CNSSRRGRFGDAM-------EEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLiqrlsgGSQGTFfeGKT 300
Cdd:cd16034 206 lllrpnvpEDKKEEAGLREDLrgyyamiTALDDNIGRLLDALKELGLLENTIVVFTSDHGDML------GSHGLM--NKQ 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2003236968 301 TTWEGGVREPAIVRWPGKVAAGSVSREVVATYDIFATIVSLAGAKLPQDrvIDGRDISGVLFRGQKSP 368
Cdd:cd16034 278 VPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDE 343
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
22-368 |
1.70e-58 |
|
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: 200.83 E-value: 1.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 22 KPPNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGarwtggvfs 101
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTD--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 102 sIAKGGLPENETTFASLLSDVGYSSLAIGKWHVGQQPQFLPTshGFDEYFGIPysvdmgnsawassGYTKIQVPLPLLHN 181
Cdd:cd16031 72 -NNGPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--GFDYWVSFP-------------GQGSYYDPEFIENG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 182 KTVIEQPvnLNTLEkrYAEKASDFIhKNAAAQKPFLIYLA-------WS----HAHV--------------------PDF 230
Cdd:cd16031 136 KRVGQKG--YVTDI--ITDKALDFL-KERDKDKPFCLSLSfkaphrpFTpaprHRGLyedvtipepetfddddyagrPEW 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 231 VTPSMCNSSRRGRFGDAMEE---------------MDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLiqrlsgGSQGtf 295
Cdd:cd16031 211 AREQRNRIRGVLDGRFDTPEkyqrymkdylrtvtgVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL------GEHG-- 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2003236968 296 FEGKTTTWEGGVREPAIVRWPGKVAAGSVSREVVATYDIFATIVSLAGAKLPQDrvIDGRDISGvLFRGQKSP 368
Cdd:cd16031 283 LFDKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLP-LLEGEKPV 352
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-358 |
6.82e-55 |
|
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: 185.91 E-value: 6.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGarWTGGVFSSI 103
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHD--WIVEGSHGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 AKGGLP--ENETTFASLLSDVGYSSLAIGKWHVGqqpqflptshgfdeyfgipysvdmgnsawassgytkiqvplpllhn 181
Cdd:cd16149 79 TKKPEGylEGQTTLPEVLQDAGYRCGLSGKWHLG---------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 182 ktvieqpvnlntlekryaEKASDFIHKNAAAQKPFLIYLAWSHAHvpdfvtpsmcnsSRRGRFGdAMEEMDSHIGDVMAA 261
Cdd:cd16149 113 ------------------DDAADFLRRRAEAEKPFFLSVNYTAPH------------SPWGYFA-AVTGVDRNVGRLLDE 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 262 LKNAGVDDNTLVFFTSDNGpwliqrLSGGSQGTFFEGKTTT----WEGGVREPAIVRWPGKVAAGSVSREVVATYDIFAT 337
Cdd:cd16149 162 LEELGLTENTLVIFTSDNG------FNMGHHGIWGKGNGTFplnmYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPT 235
|
330 340
....*....|....*....|.
gi 2003236968 338 IVSLAGAKLPQDRVIDGRDIS 358
Cdd:cd16149 236 LLELAGVDPPADPRLPGRSFA 256
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-378 |
6.89e-52 |
|
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: 181.61 E-value: 6.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWY--SGFH--VCSPSRASMLTGRlpirsgiagarwtgGV 99
Cdd:cd16155 3 PNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYnmGGWSgaVCVPSRAMLMTGR--------------TL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 100 FSS--IAKGGLPENETTFASLLSDVGYSSLAIGKWHVGqqpqflptshgfdeyfgipysvdmgnsawassgytkiqvplp 177
Cdd:cd16155 69 FHApeGGKAAIPSDDKTWPETFKKAGYRTFATGKWHNG------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 178 llhnktvieqpvnlntlekrYAEKASDFIHKNAAAQKPFLIYLAWSHAHVP-----------DFVTPSMCNS-------- 238
Cdd:cd16155 107 --------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHDPrqappeyldmyPPETIPLPENflpqhpfd 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 239 --SRRGRF-----------------GD--AM-EEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGpwliqrLSGGSQGTFf 296
Cdd:cd16155 167 ngEGTVRDeqlapfprtpeavrqhlAEyyAMiTHLDAQIGRILDALEASGELDNTIIVFTSDHG------LAVGSHGLM- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 297 eGKTTTWEGGVREPAIVRWPGkVAAGSVSREVVATYDIFATIVSLAGAKLPQDrvIDGRDISGVLfRGQKSPHNC--LFH 374
Cdd:cd16155 240 -GKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES--VEGKSLLPVI-RGEKKAVRDtlYGA 314
|
....
gi 2003236968 375 YKGT 378
Cdd:cd16155 315 YRDG 318
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-355 |
2.05e-50 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 178.57 E-value: 2.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGI-AGARWTGGVFss 102
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVlNNVENAGAYS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 103 iakGGLPENETTFASLLSDVGYSSLAIGKWHVGqqPQFLPTSHGFDEYFgipysvdmgnsawassgytkiqvplpllhnk 182
Cdd:cd16033 79 ---RGLPPGVETFSEDLREAGYRNGYVGKWHVG--PEETPLDYGFDEYL------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 183 tvieqPVNlNTLEKRYAEKASDFIHKNAAAQKPFLIYLAWSHAHVPDFVT---------------PSMC----------- 236
Cdd:cd16033 123 -----PVE-TTIEYFLADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPepyldmydpediplpESFAddfedkpyiyr 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 237 NSSRRGRFGDAMEE---------------MDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLiqrlsgGSQGTFFEGkTT 301
Cdd:cd16033 197 RERKRWGVDTEDEEdwkeiiahywgyitlIDDAIGRILDALEELGLADDTLVIFTSDHGDAL------GAHRLWDKG-PF 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2003236968 302 TWEGGVREPAIVRWPGKVAAGSVSREVVATYDIFATIVSLAGAKLPQDrvIDGR 355
Cdd:cd16033 270 MYEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK--VDGR 321
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-406 |
8.51e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 169.26 E-value: 8.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIagarWTGGvfssi 103
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGV----WDNA----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 akGGLPENETTFASLLSDVGYSSLAIGKWHVGQQPQFlptsHGFDeyfgipysvdmgnsawassgytkiqvplpllhnkt 183
Cdd:cd16037 72 --DPYDGDVPSWGHALRAAGYETVLIGKLHFRGEDQR----HGFR----------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 184 vieqpvnlntLEKRYAEKASDFIHKNAAAQKPFLIYLAWSHAHVPdFVTP----SM-CNSSRRGRFGdAMEEMDSHIGDV 258
Cdd:cd16037 111 ----------YDRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFP-LIAPqefyDLyVRRARAAYYG-LVEFLDENIGRV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 259 MAALKNAGVDDNTLVFFTSDNGPWLiqrlsgGSQGTFfeGKTTTWEGGVREPAIVRWPGkVAAGSVSREVVATYDIFATI 338
Cdd:cd16037 179 LDALEELGLLDNTLIIYTSDHGDML------GERGLW--GKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTI 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 339 VSLAGAKLPQDRviDGRDISGVLFRGQKSPHN--CLFHYKGTPStglppkpddsqpGLWAVRCGAYKAHY 406
Cdd:cd16037 250 LEAAGAPPPPDL--DGRSLLPLAEGPDDPDRVvfSEYHAHGSPS------------GAFMLRKGRWKYIY 305
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
24-373 |
1.68e-40 |
|
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: 149.65 E-value: 1.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSgiagarwtgGVFSSI 103
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRI---------GAYDNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 AKggLPENETTFASLLSDVGYSSLAIGKWH-VGqqPQFLptsHGFD-----EYFGIPYSVDMGnsawassgytkiqvplp 177
Cdd:cd16032 72 AE--FPADIPTFAHYLRAAGYRTALSGKMHfVG--PDQL---HGFDydeevAFKAVQKLYDLA----------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 178 llhnktvieqpvnlntlekRYAEKasdfihknaaaqKPFLIYLAWSHAHVPDFVTPSMCN----SSRRGRFGdAMEEMDS 253
Cdd:cd16032 128 -------------------RGEDG------------RPFFLTVSFTHPHDPYVIPQEYWDlyvrRARRAYYG-MVSYVDD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 254 HIGDVMAALKNAGVDDNTLVFFTSDNGPWLiqrlsgGSQGTFFegKTTTWEGGVREPAIVRWPGKVAAGSVSrEVVATYD 333
Cdd:cd16032 176 KVGQLLDTLERTGLADDTIVIFTSDHGDML------GERGLWY--KMSFFEGSARVPLIISAPGRFAPRRVA-EPVSLVD 246
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2003236968 334 IFATIVSLAGAKLPQDRV-IDGRDISGVLFRGQKSPHNCLF 373
Cdd:cd16032 247 LLPTLVDLAGGGTAPHVPpLDGRSLLPLLEGGDSGGEDEVI 287
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
22-361 |
2.97e-39 |
|
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: 148.87 E-value: 2.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 22 KPPNFLILFADDMGYgDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGarwtggvFS 101
Cdd:cd16030 1 KKPNVLFIAVDDLRP-WLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYD-------NN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 102 SIAKGGLPeNETTFASLLSDVGYSSLAIGK-WHVGqQPQFLPTSHGFDEYFGIPYSvdMGNSAWASSGYTKIQVPLPLLH 180
Cdd:cd16030 73 SYFRKVAP-DAVTLPQYFKENGYTTAGVGKiFHPG-IPDGDDDPASWDEPPNPPGP--EKYPPGKLCPGKKGGKGGGGGP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 181 NKTVIEQPvnlntlEKRY-----AEKASDFIHKNAAAQKPFLIylawshA------HVPdFVTP------------SMCN 237
Cdd:cd16030 149 AWEAADVP------DEAYpdgkvADEAIEQLRKLKDSDKPFFL------AvgfykpHLP-FVAPkkyfdlyplesiPLPN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 238 SSRR--------------GRFGDAMEE---------------------------MDSHIGDVMAALKNAGVDDNTLVFFT 276
Cdd:cd16030 216 PFDPidlpevawndlddlPKYGDIPALnpgdpkgplpdeqarelrqayyasvsyVDAQVGRVLDALEELGLADNTIVVLW 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 277 SDNGpWLIqrlsgGSQGTFfeGKTTTWEGGVREPAIVRWPGKVAAGSVSREVVATYDIFATIVSLAGakLPQDRVIDGRD 356
Cdd:cd16030 296 SDHG-WHL-----GEHGHW--GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKS 365
|
....*
gi 2003236968 357 ISGVL 361
Cdd:cd16030 366 LVPLL 370
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
18-357 |
2.28e-37 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 144.43 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 18 GATTKPPNFLILFADDMgYGD-MSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGarwt 96
Cdd:PRK13759 1 MVQTKKPNIILIMVDQM-RGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVG---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 97 ggvfssIAKGGLPENETTFASLLSDVGYSSLAIGKWHVGQQPQFlptsHGF------DEYFGIPYSVDMGNSAWASS--G 168
Cdd:PRK13759 76 ------YGDVVPWNYKNTLPQEFRDAGYYTQCIGKMHVFPQRNL----LGFhnvllhDGYLHSGRNEDKSQFDFVSDylA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 169 YTKIQVPlplLHNKTVIEQPVNLNTLEKR---YAEK----------ASDFIHkNAAAQKPFLIYLAWSHAHVP------- 228
Cdd:PRK13759 146 WLREKAP---GKDPDLTDIGWDCNSWVARpwdLEERlhptnwvgseSIEFLR-RRDPTKPFFLKMSFARPHSPydppkry 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 229 -------DFVTPSMCN--------------SSRRGRFGDA------------MEEMDSHIGDVMAALKNAGVDDNTLVFF 275
Cdd:PRK13759 222 fdmykdaDIPDPHIGDweyaedqdpeggsiDALRGNLGEEyarraraayyglITHIDHQIGRFLQALKEFGLLDNTIILF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 276 TSDNGPWLiqrlsgGSQGTFfeGKTTTWEGGVREPAIVRWPG---KVAAGSVSREVVATYDIFATIVSLAGAKLPQDrvI 352
Cdd:PRK13759 302 VSDHGDML------GDHYLF--RKGYPYEGSAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--V 371
|
....*
gi 2003236968 353 DGRDI 357
Cdd:PRK13759 372 DGRSL 376
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
23-355 |
1.23e-36 |
|
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: 140.38 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 23 PPNFLILFADDMGYGDMSCNGHPSIAtpnlDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGARWTGGVFSS 102
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTK----KLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPPGGGYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 103 IAKGGLpeNETTFASLLSDVGYSSLAIGKWHVGQQPQFLPTSH--GFDEYFGIPysvdmGNSawassGYTKIQVPLPLLH 180
Cdd:cd16147 77 FWQNGL--ERSTLPVWLQEAGYRTAYAGKYLNGYGVPGGVSYVppGWDEWDGLV-----GNS-----TYYNYTLSNGGNG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 181 NKTVIEQPVNLNTLekrYAEKASDFIHKNAAAQKPFLIYLAW-----------SHAHVPDFVTPSMCNSS---------- 239
Cdd:cd16147 145 KHGVSYPGDYLTDV---IANKALDFLRRAAADDKPFFLVVAPpaphgpftpapRYANLFPNVTAPPRPPPnnpdvsdkph 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 240 ---RRGR-FGDAMEEMDSH--------------IGDVMAALKNAGVDDNTLVFFTSDNGPWLIQ-RLSGgsqgtffeGKT 300
Cdd:cd16147 222 wlrRLPPlNPTQIAYIDELyrkrlrtlqsvddlVERLVNTLEATGQLDNTYIIYTSDNGYHLGQhRLPP--------GKR 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2003236968 301 TTWEGGVREPAIVRWPGkVAAGSVSREVVATYDIFATIVSLAGAKLPQDrvIDGR 355
Cdd:cd16147 294 TPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
24-342 |
2.70e-33 |
|
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: 127.15 E-value: 2.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGmrltqWYSGFHVCS------PSRASMLTGRLPIRSGIAGARWTG 97
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEG-----ATFNFRSVSpptssaPNHAALLTGAYPTLHGYTGNGSAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 98 GVFSSIAkGGLPENETTFASLLSDVGYSSLAIGkwhvgqqpqflptshgfdeyfgipysvdmgnsawassgytkiqvplp 177
Cdd:cd00016 76 PELPSRA-AGKDEDGPTIPELLKQAGYRTGVIG----------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 178 llhnktvIEQPVNLNTLEKryaekasdfihknaaaqkPFLIYLAWSHAHVPDFVTpsmcnSSRRGRFGDAMEEMDSHIGD 257
Cdd:cd00016 108 -------LLKAIDETSKEK------------------PFVLFLHFDGPDGPGHAY-----GPNTPEYYDAVEEIDERIGK 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 258 VMAALKNAGVDDNTLVFFTSDNGpwliqrlsGGSQG----TFFEGKTTTWEGGVREPAIVRWPGkVAAGSVSREVVATYD 333
Cdd:cd00016 158 VLDALKKAGDADDTVIIVTADHG--------GIDKGhggdPKADGKADKSHTGMRVPFIAYGPG-VKKGGVKHELISQYD 228
|
....*....
gi 2003236968 334 IFATIVSLA 342
Cdd:cd00016 229 IAPTLADLL 237
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-356 |
5.28e-33 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 127.28 E-value: 5.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFAD----DMgygdMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGarwtggv 99
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWG------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 100 fssiakGGLPENETTFASLLSDVGYSSLAIGKW-HVGQQPQFlptSHGFDEY-FGIPYSVDMGNSAWASSgytkiqvplp 177
Cdd:cd16148 70 ------GPLEPDDPTLAEILRKAGYYTAAVSSNpHLFGGPGF---DRGFDTFeDFRGQEGDPGEEGDERA---------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 178 llhnktvieqpvnlntleKRYAEKASDFIHKNAAAqKPFLIYL-AWShAHVPDfvtpsmcnssrrgRFGDAMEEMDSHIG 256
Cdd:cd16148 131 ------------------ERVTDRALEWLDRNADD-DPFFLFLhYFD-PHEPY-------------LYDAEVRYVDEQIG 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 257 DVMAALKNAGVDDNTLVFFTSD-------NGPWliqrlsGGSQGTFFEGKTttweggvREPAIVRWPGKVAAGSVSrEVV 329
Cdd:cd16148 178 RLLDKLKELGLLEDTLVIVTSDhgeefgeHGLY------WGHGSNLYDEQL-------HVPLIIRWPGKEPGKRVD-ALV 243
|
330 340
....*....|....*....|....*..
gi 2003236968 330 ATYDIFATIVSLAGAKLPQDrvIDGRD 356
Cdd:cd16148 244 SHIDIAPTLLDLLGVEPPDY--SDGRS 268
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-348 |
3.14e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 127.47 E-value: 3.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMG------YGDMScnGHPsiATPNLDKLAAEGMRLTQWYSgFHVCSPSRASMLTGRLPIRSGIagaRWTG 97
Cdd:cd16154 1 PNILLIIADDQGldssaqYSLSS--DLP--VTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGKYGFRTGV---LAVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 98 GVFSSiakgglpENETTFASLLSD---VGYSSLAIGKWHVGQQPQFLPTSHGFDEYFGI-PYSVDmGNSAWassgytkiq 173
Cdd:cd16154 73 DELLL-------SEETLLQLLIKDattAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGIlGGGVQ-DYYNW--------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 174 vplpllhNKTVIEQPVNLNTlekrYA-----EKASDFIHKNAaaqKPFLIYLAWSHAHVP------DFVTPSMCNSS--- 239
Cdd:cd16154 136 -------NLTNNGQTTNSTE----YAttkltNLAIDWIDQQT---KPWFLWLAYNAPHTPfhlppaELHSRSLLGDSadi 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 240 ---RRGRFGDAMEEMDSHIGDVMAALKNAgVDDNTLVFFTSDNG-PWLIQRLSGGSQGTffegKTTTWEGGVREPAIVRW 315
Cdd:cd16154 202 eanPRPYYLAAIEAMDTEIGRLLASIDEE-ERENTIIIFIGDNGtPGQVVDLPYTRNHA----KGSLYEGGINVPLIVSG 276
|
330 340 350
....*....|....*....|....*....|...
gi 2003236968 316 PGKVAAGSVSREVVATYDIFATIVSLAGAKLPQ 348
Cdd:cd16154 277 AGVERANERESALVNATDLYATIAELAGVDAAE 309
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-357 |
3.72e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 125.18 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHP----------SIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIAGA 93
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNAhtgksesrlgYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 94 RWtggvfssiAKGGLPENETTFASLLSDVGYSSLAIGKWHVGQQPQFLptshgfdeyfgipysvdmgnsawassgytkiq 173
Cdd:cd16153 82 EA--------AHPALDHGLPTFPEVLKKAGYQTASFGKSHLEAFQRYL-------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 174 vplpllhnktvieqpVNLNTLEKRYAEKasdfIHKNAAAQKPFLIYLAWSHAHvpdfvTPSMCNSSRRGRF--------G 245
Cdd:cd16153 122 ---------------KNANQSYKSFWGK----IAKGADSDKPFFVRLSFLQPH-----TPVLPPKEFRDRFdyyafcayG 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 246 DAMeemdshIGDVMAALKNAGVD---DNTLVFFTSDNGPWLiqrlsgGSQGTffEGKTTTWEGGVREPAIVRWPGK--VA 320
Cdd:cd16153 178 DAQ------VGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHL------GEQGI--LAKFTFWPQSHRVPLIVVSSDKlkAP 243
|
330 340 350
....*....|....*....|....*....|....*..
gi 2003236968 321 AGSVSREVVATYDIFATIVSLAGAKLPQDRVIDGRDI 357
Cdd:cd16153 244 AGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL 280
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
367-535 |
1.30e-31 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 118.57 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 367 SPHNCLFHYKGTPstglppkpddsqpgLWAVRCGAYKAHYVTSCAVMQNWGDkrCRSTtyswngmkdlaheaafKLCRET 446
Cdd:pfam14707 1 SPHEFLFHYCGAA--------------LHAVRWGPYKAHFFTPSFDPPGAEG--CYGS----------------KVPVTH 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 447 lamdecalllssspvlHNPPILYNVEHDPSELYQISPKSSEYQAAMETITQAKKEHEATLTPVPNQIAMG---MDNSRRV 523
Cdd:pfam14707 49 ----------------HDPPLLFDLERDPSEKYPLSPDSPEYPEVLAEIKAAVEEHKATLVPVPNQLSKGnylWDPWLQP 112
|
170
....*....|..
gi 2003236968 524 CCdnNTKPACTC 535
Cdd:pfam14707 113 CC--PTFPACTC 122
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-347 |
1.56e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 126.58 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPirsGIAGARWTGGVfssi 103
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYP---HVNGHRTLHHL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 akggLPENETTFASLLSDVGYSSLAIGKWHVgqqpqfLPTSHGFDEYfgipysvdmGNSAWAssgytkiqvplpllhnkt 183
Cdd:cd16150 74 ----LRPDEPNLLKTLKDAGYHVAWAGKNDD------LPGEFAAEAY---------CDSDEA------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 184 vieqpvnlntlekrYAEKASDFIhKNAAAQKPFLIYLAWSHAHVPDFVT-------------------------PSMCNS 238
Cdd:cd16150 117 --------------CVRTAIDWL-RNRRPDKPFCLYLPLIFPHPPYGVEepwfsmidreklpprrppglrakgkPSMLEG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 239 SRRGRFGDAMEE---------------MDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLiqrlsggsqGTFfeGKTTTW 303
Cdd:cd16150 182 IEKQGLDRWSEErwrelratylgmvsrLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYT---------GDY--GLVEKW 250
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2003236968 304 EGG-----VREPAIVRwPGKVAAGSVSREVVATYDIFATIVSLAGAKLP 347
Cdd:cd16150 251 PNTfedclTRVPLIIK-PPGGPAGGVSDALVELVDIPPTLLDLAGIPLS 298
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-373 |
5.63e-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: 293771 [Multi-domain] Cd Length: 373 Bit Score: 123.88 E-value: 5.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 23 PPNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIagarWTGGVfss 102
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC----FRNGI--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 103 iakgGLPENETTFASLLSDVGYSSLAIGKWHVGQqpqflptshgfdeyfgipYSVDmgnsawASSGYtkiqvplpllhnk 182
Cdd:cd16152 74 ----PLPADEKTLAHYFRDAGYETGYVGKWHLAG------------------YRVD------ALTDF------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 183 tvieqpvnlntlekryaekASDFIHkNAAAQKPFLIYLAwshahvpdFVTPSMCNSSRR--------GRF---------- 244
Cdd:cd16152 113 -------------------AIDYLD-NRQKDKPFFLFLS--------YLEPHHQNDRDRyvapegsaERFanfwvppdla 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 245 ---GDAMEE----------MDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLIQRLSggsqgtffEGKTTTWEGGVREPA 311
Cdd:cd16152 165 alpGDWAEElpdylgccerLDENVGRIRDALKELGLYDNTIIVFTSDHGCHFRTRNA--------EYKRSCHESSIRVPL 236
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2003236968 312 IVRWPGkVAAGSVSREVVATYDIFATIVSLAGAKLPQDrvIDGRDISGVLFRGQKSPHNCLF 373
Cdd:cd16152 237 VIYGPG-FNGGGRVEELVSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNEVF 295
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
40-407 |
1.16e-30 |
|
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: 124.68 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 40 SCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGiagarwtggvfsSIAKGG-LPENETTFASL 118
Cdd:cd16028 17 SCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHR------------SVWNGTpLDARHLTLALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 119 LSDVGYSSLAIGKWHVGQQPQFLPTSH-----------GFDEYFGIP-YSVDMGNSAW------------------ASSG 168
Cdd:cd16028 85 LRKAGYDPALFGYTDTSPDPRGLAPLDprllsyelampGFDPVDRLDeYPAEDSDTAFltdraieylderqdepwfLHLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 169 YTK----IQVPLPL--LHNKTVIEQPVNLNTLEKRyaekasdfihknaAAQKPFliyLAWSHAHVPD--FVTPSMCNSSR 240
Cdd:cd16028 165 YIRphppFVAPAPYhaLYDPADVPPPIRAESLAAE-------------AAQHPL---LAAFLERIESlsFSPGAANAADL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 241 RGRFGDAM--------EEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLiqrlsgGSQGTFfeGKTTTWEGGVREPAI 312
Cdd:cd16028 229 DDEEVAQMratylgliAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQL------GDHWLW--GKDGFFDQAYRVPLI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 313 VRWPGKVA---AGSVSREVVATYDIFATIVSLAGakLPQDRVIDGRDISGVLFRGQKSPHNCLFHYK---GTPSTGLPPK 386
Cdd:cd16028 301 VRDPRREAdatRGQVVDAFTESVDVMPTILDWLG--GEIPHQCDGRSLLPLLAGAQPSDWRDAVHYEydfRDVSTRRPQE 378
|
410 420
....*....|....*....|....
gi 2003236968 387 P---DDSQPGLWAVRCGAYKahYV 407
Cdd:cd16028 379 AlglSPDECSLAVIRDERWK--YV 400
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
24-373 |
2.06e-25 |
|
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: 109.39 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGIagarWTGGVfssi 103
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----WTNCM---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 akgGLPENETTFASLLSDVGYSSLAIGKWHV--------GQQPQflptshGFDEyfgiPYSVDMGNsawassgYtkiqvp 175
Cdd:cd16156 73 ---ALGDNVKTIGQRLSDNGIHTAYIGKWHLdggdyfgnGICPQ------GWDP----DYWYDMRN-------Y------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 176 LPLLHNKTVIEQPVNLNTLEK-----------RYAEKASDFIHKNaaAQKPFLIYLAWSHAHVP------------DFVT 232
Cdd:cd16156 127 LDELTEEERRKSRRGLTSLEAegikeeftyghRCTNRALDFIEKH--KDEDFFLVVSYDEPHHPflcpkpyasmykDFEF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 233 PSMCN----------------SSRRGRFGDAMEE-----------MDSHIGDVMAALKNAGvdDNTLVFFTSDNGPWLiq 285
Cdd:cd16156 205 PKGENayddlenkplhqrlwaGAKPHEDGDKGTIkhplyfgcnsfVDYEIGRVLDAADEIA--EDAWVIYTSDHGDML-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 286 rlsgGSQGTFFEGkTTTWEGGVREPAIVRWPGKVAAGSVSREVVATYDIFATIVSLAGakLPQDRVIDGRDISGVLFRGQ 365
Cdd:cd16156 281 ----GAHKLWAKG-PAVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATIEDPE 353
|
....*...
gi 2003236968 366 KSPHNCLF 373
Cdd:cd16156 354 IPENRGVF 361
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-361 |
2.12e-21 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 94.97 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMGYGDMSCNGHPSIATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMLTGRLPIRSGiagarwtggVFSSI 103
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTG---------VTDTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 104 AKGGLPENETTF---ASLLSDVGYSSLAIGKWHVgqqpqflptshgfdeyfgipysvdmgnSAWASSGYTKiqvplpllh 180
Cdd:cd16035 72 GSPMQPLLSPDVptlGHMLRAAGYYTAYKGKWHL---------------------------SGAAGGGYKR--------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 181 nktvieqpvnlntlEKRYAEKASDFIHK---NAAAQKPFLiyLAWShahvpdFV-------TPSMCNSSRRGR--FGDAM 248
Cdd:cd16035 116 --------------DPGIAAQAVEWLRErgaKNADGKPWF--LVVS------LVnphdimfPPDDEERWRRFRnfYYNLI 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 249 EEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLiqrLSGGSQGTFFegktTTWEGGVREPAIVRWPGKVAAGSVSREV 328
Cdd:cd16035 174 RDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMG---GAHGLRGKGF----NAYEEALHVPLIISHPDLFGTGQTTDAL 246
|
330 340 350
....*....|....*....|....*....|....*..
gi 2003236968 329 VATYDIFATIVSLAGAKLPQDRVID----GRDISGVL 361
Cdd:cd16035 247 TSHIDLLPTLLGLAGVDAEARATEApplpGRDLSPLL 283
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
24-348 |
3.96e-15 |
|
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: 77.20 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 24 PNFLILFADDMgygDMSCNGHPS---IATPNLDKLAAEGMRLTQWYSGFHVCSPSRASMltgrlpirsgiagarWTGgVF 100
Cdd:cd16171 1 PNVVMVMSDSF---DGRLTFRPGnqvVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAM---------------WSG-LF 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 101 SSIAKG-----GLPENETTFASLLSDVGYSSLAIGKWhvgqqpqflptshgfdEYFGIPYSVDMGNSAWASS-GYTKIQV 174
Cdd:cd16171 62 THLTESwnnykGLDPNYPTWMDRLEKHGYHTQKYGKL----------------DYTSGHHSVSNRVEAWTRDvPFLLRQE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 175 PLP---LLHNKTVieqpVNLNTLEKRYAEKASDFIHKNAAA-QKPFLIYLAWSHAHvpDFVTPSM---CNSSRRGR-FGD 246
Cdd:cd16171 126 GRPtvnLVGDRST----VRVMLKDWQNTDKAVHWIRKEAPNlTQPFALYLGLNLPH--PYPSPSMgenFGSIRNIRaFYY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 247 AM-EEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGPWLIQRLSggsqgtFFegKTTTWEGGVREPAIVRWPGkVAAGSVS 325
Cdd:cd16171 200 AMcAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQ------FY--KMSMYEGSSHVPLLIMGPG-IKAGQQV 270
|
330 340
....*....|....*....|...
gi 2003236968 326 REVVATYDIFATIVSLAGAKLPQ 348
Cdd:cd16171 271 SDVVSLVDIYPTMLDIAGVPQPQ 293
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
49-343 |
1.22e-12 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 68.48 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 49 TPNLDKLAAEGmrltqWYSGfHVCSPSRA--------SMLTGRLPIRSGiagarwtGGVFSSIAKGGLPenetTFASLLS 120
Cdd:cd16015 26 TPNLNKLAKEG-----LYFG-NFYSPGFGggtangefEVLTGLPPLPLG-------SGSYTLYKLNPLP----SLPSILK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 121 DVGYSSLAIgkwHVGQ-----QPQFLPtSHGFDEYFGIPysvDMGNSAWASSGytkiqvplPLLHNKTVIEQpvnlntLE 195
Cdd:cd16015 89 EQGYETIFI---HGGDasfynRDSVYP-NLGFDEFYDLE---DFPDDEKETNG--------WGVSDESLFDQ------AL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 196 KRYAEKAsdfihknaaaQKPFLIYLAWSHAHVPDFVTPSMCNSSRRGRFGD--------AMEEMDSHIGDVMAALKNAGV 267
Cdd:cd16015 148 EELEELK----------KKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKtelenylnAIHYTDKALGEFIEKLKKSGL 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2003236968 268 DDNTLVFFTSDNGPWLiqrlsggsqGTFFEGKTTTWEGGVREPAIVRWPGKVAAGSVSReVVATYDIFATIVSLAG 343
Cdd:cd16015 218 YENTIIVIYGDHLPSL---------GSDYDETDEDPLDLYRTPLLIYSPGLKKPKKIDR-VGSQIDIAPTLLDLLG 283
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
8-280 |
1.36e-12 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 69.39 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 8 LLLLLSFSCVGATTKPPNFLILFADDMGYGDMScnghpSIATPNLDKLAAEGMRLTQWYSGFH-VCSPSRASMLTGRLPI 86
Cdd:COG1524 8 LLASLLAAAAAAAPPAKKVVLILVDGLRADLLE-----RAHAPNLAALAARGVYARPLTSVFPsTTAPAHTTLLTGLYPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 87 RSGIAG----ARWTGGVFSSIAKGGLPE------NETTFASLLSDVGYSSLAIGKWHVgqqpqflptshgfdeyfgipys 156
Cdd:COG1524 83 EHGIVGngwyDPELGRVVNSLSWVEDGFgsnsllPVPTIFERARAAGLTTAAVFWPSF---------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 157 vdmgnsawASSGYTKIQVPLPLLHNKTVIEQPvnlnTLEKRYAEKASDFIHKNaaaqKPFLIYLAWS------HAHVPDf 230
Cdd:COG1524 141 --------EGSGLIDAARPYPYDGRKPLLGNP----AADRWIAAAALELLREG----RPDLLLVYLPdldyagHRYGPD- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2003236968 231 vtpsmcnsSRRGRfgDAMEEMDSHIGDVMAALKNAGVDDNTLVFFTSDNG 280
Cdd:COG1524 204 --------SPEYR--AALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
19-357 |
5.47e-11 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 65.06 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 19 ATTKPPN-FLIL---FADDMgygdMSCNGHPSIATPNLDKLAAEGMRLTQWYSgfHVCSPSRA--SMLTGRLPIRSGIag 92
Cdd:COG1368 230 GPAKKPNvVVILlesFSDFF----IGALGNGKDVTPFLDSLAKESLYFGNFYS--QGGRTSRGefAVLTGLPPLPGGS-- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 93 arwtggVFSSIAKGGLPenetTFASLLSDVGYSSLAI--GK---WHVGqqpQFLPtSHGFDEYFGIPYSVDMGNSAWass 167
Cdd:COG1368 302 ------PYKRPGQNNFP----SLPSILKKQGYETSFFhgGDgsfWNRD---SFYK-NLGFDEFYDREDFDDPFDGGW--- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 168 GYtkiqvplpllHNKTVIEQPvnLNTLEKryaekasdfihknaaAQKPFLIYLAWSHAHVPdFVTPSmcNSSRRGRFGD- 246
Cdd:COG1368 365 GV----------SDEDLFDKA--LEELEK---------------LKKPFFAFLITLSNHGP-YTLPE--EDKKIPDYGKt 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 247 -------AMEEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGPwliqRLSGGSQGTFFEGKTTTweggvrePAIVrWPGKV 319
Cdd:COG1368 415 tlnnylnAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGP----RSPGKTDYENPLERYRV-------PLLI-YSPGL 482
|
330 340 350
....*....|....*....|....*....|....*...
gi 2003236968 320 AAGSVSREVVATYDIFATIVSLAGAKLPQDRVIdGRDI 357
Cdd:COG1368 483 KKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDL 519
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
49-280 |
3.41e-09 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 58.59 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 49 TPNLDKLAAEGMRLTQWYSGF-HVCSPSRASMLTGRLPIRSGIAGARW----TGGVFS-SIAKGGLPE---NETTFASLL 119
Cdd:pfam01663 20 TPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVGNTFydpkTGEYLVfVISDPEDPRwwqGEPIWDTAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 120 SDvGYSSLAIgkwhvgqqpqFLPTShgfdeyfGIPYSVDMGNSAWASSGYTKIQVPLPLLHNKTVIEQPVNLNTlekrya 199
Cdd:pfam01663 100 KA-GVRAAAL----------FWPGS-------EVDYSTYYGTPPRYLKDDYNNSVPFEDRVDTAVLQTWLDLPF------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 200 ekasdfihKNAAAQKPFLIYLAWS------HAHVPDfvtpSMcnssrrgRFGDAMEEMDSHIGDVMAALKNAGVDDNTLV 273
Cdd:pfam01663 156 --------ADVAAERPDLLLVYLEepdyagHRYGPD----SP-------EVEDALRRVDRAIGDLLEALDERGLFEDTNV 216
|
....*..
gi 2003236968 274 FFTSDNG 280
Cdd:pfam01663 217 IVVSDHG 223
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
12-338 |
3.55e-06 |
|
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: 49.90 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 12 LSFScvgATTKPPNFLILFADDMGYGDMScnghpSIATPNLDKLAAEGMRLTQWYSGfhvcspsrasmltgrlpirsgia 91
Cdd:COG3083 236 LQFS---DPAKPPNILLIVVDSLRADMLD-----PEVMPNLYAFAQRSLRFTNHYSS----------------------- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 92 GARWTGGVFSSIAkgGLPENETTfaSLLSDvGYSSLAIgkwHVGQQpqflptsHGFDeyFGIPYSVDMGNSAWASSGYTK 171
Cdd:COG3083 285 GNSTRAGLFGLFY--GLPGNYWD--SILAE-RTPPVLI---DALQQ-------QGYQ--FGLFSSAGFNSPLFRQTIFSD 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 172 iqVPLPLLHNKTVIEQPVNLNTlekryaEKASDFIhKNAAAQKPFLIYLAWSHAH--------VPDFVTPSMCNSSRRGR 243
Cdd:COG3083 348 --VSLPRLHTPGGPAQRDRQIT------AQWLQWL-DQRDSDRPWFSYLFLDAPHaysfpadyPKPFQPSEDCNYLALDN 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003236968 244 FGD----------AMEEMDSHIGDVMAALKNAGVDDNTLVFFTSDNGPwliqrlsggsqgTFFEGKTTTWEGG------- 306
Cdd:COG3083 419 ESDptpfknryrnAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGE------------EFNENGQNYWGHNsnfsryq 486
|
330 340 350
....*....|....*....|....*....|..
gi 2003236968 307 VREPAIVRWPGKvAAGSVSReVVATYDIFATI 338
Cdd:COG3083 487 LQVPLVIHWPGT-PPQVISK-LTSHLDIVPTL 516
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
246-280 |
2.39e-03 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 39.88 E-value: 2.39e-03
10 20 30
....*....|....*....|....*....|....*
gi 2003236968 246 DAMEEMDSHIGDVMAALKNAGVDDNTLVFFTSDNG 280
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG 217
|
|
| |
