|
Name |
Accession |
Description |
Interval |
E-value |
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
27-492 |
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: 293776 [Multi-domain] Cd Length: 466 Bit Score: 956.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 27 PPNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 106
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 107 PQEIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKAKPNIPVYRDWEMVGR 186
Cdd:cd16157 81 PQNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCHFGPYDNKAYPNIPVYRDWEMIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 187 FYEEFPINRKTGEANLTQLYTQEALDFIQTQHARQSPFFLYWAIDATHAPVYASRQFLGTSLRGRYGDAVREIDDSVGKI 266
Cdd:cd16157 161 YYEEFKIDKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 267 LSLLQNLGISKNTFVFFTSDNGAALISAPNEGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTT 346
Cdd:cd16157 241 LESLKSLGIENNTFVFFSSDNGAALISAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 347 SLSLAGLKPPSDRVIDGLDLLPTMLKGQMMDRPIFYYRGNTLMAVTLGQYKAHLWTWTNSWEEFTQGTDFCPGQNVSGVT 426
Cdd:cd16157 321 SLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGDELMAVRLGQYKAHFWTWSNSWEEFRKGINFCPGQNVPGVT 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124007189 427 THTQEEHTELPLIFHLGRDPGERFPLSFHSDEYQDALSRTTQVVQEHQKSLVPGQPQLNVCNQAVM 492
Cdd:cd16157 401 THNQTDHTKLPLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVVQQHQKTLVPGEPQLNVCDLAVM 466
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
27-453 |
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: 542.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 27 PPNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharnayt 106
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVG------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 107 PQEIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKAKPNIPVYRDWEMVGR 186
Cdd:cd16026 74 PPGSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLPPLMENE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 187 FYEEFPINRktgeANLTQLYTQEALDFIQTQhaRQSPFFLYWAIDATHAPVYASRQFLGTSLRGRYGDAVREIDDSVGKI 266
Cdd:cd16026 154 EVIEQPADQ----SSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 267 LSLLQNLGISKNTFVFFTSDNGAALISaPNEGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTT 346
Cdd:cd16026 228 LDALKELGLEENTLVIFTSDNGPWLEY-GGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 347 SLSLAGLKPPSDRVIDGLDLLPTMLKG-QMMDRPIFYYR-GNTLMAVTLGQYKAHLWTWTNSWEEFtqgtdfcpgqnvsg 424
Cdd:cd16026 307 LAALAGAPLPEDRVIDGKDISPLLLGGsKSPPHPFFYYYdGGDLQAVRSGRWKLHLPTTYRTGTDP-------------- 372
|
410 420
....*....|....*....|....*....
gi 124007189 425 vtTHTQEEHTELPLIFHLGRDPGERFPLS 453
Cdd:cd16026 373 --GGLDPTKLEPPLLYDLEEDPGETYNVA 399
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
28-453 |
2.30e-120 |
|
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: 360.98 E-value: 2.30e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTnahaRNAYTP 107
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGG----TRVFLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 QEImGGIPNSEHLLPELLKKAGYTNKIVGKWHLG-----HRPQFH-PLKHGFD----------EWFGSPNCHFGPYDNKA 171
Cdd:cd16160 78 WDI-GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDfvgtnlpftnSWACDDTGRHVDFPDRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 172 KPNIpvYRDWEMVgrfyeEFPINRKtgeaNLTQLYTQEALDFIQTQHARqsPFFLYWAIDATHAPVYASRQFLGTSLRGR 251
Cdd:cd16160 157 ACFL--YYNDTIV-----EQPIQHE----HLTETLVGDAKSFIEDNQEN--PFFLYFSFPQTHTPLFASKRFKGKSKRGR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 252 YGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALiSAPNEGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIaAG 331
Cdd:cd16160 224 YGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHV-EYCLEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTI-KP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 332 QVSHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTMLKG-QMMDRPIFYYRGNTLMAVTLGQYKAHLWTWTNSWEEF 410
Cdd:cd16160 302 RVSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEaDSPHDDILYYCCSRLMAVRYGSYKIHFKTQPLPSQES 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 124007189 411 TqGTDFCPGQNVS-------GVTTHTQEEHteLPLIFHLGRDPGERFPLS 453
Cdd:cd16160 382 L-DPNCDGGGPLSdyivcydCEDECVTKHN--PPLIFDVEKDPGEQYPLQ 428
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
27-484 |
1.07e-117 |
|
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: 356.60 E-value: 1.07e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 27 PPNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 106
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 107 PQEimGGIPNSEHLLPELLKKAGYTNKIVGKWHLG-HRPQ-----FHPLKHGFDEWFGSP-----NCHFGP---YDNKAK 172
Cdd:cd16159 81 ASS--GGLPPNETTFAEVLKQQGYSTALIGKWHLGlHCESrndfcHHPLNHGFDYFYGLPltnlkDCGDGSngeYDLSFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 173 PNIPVYRDWEMVG-----------------------------------------------RFYE--EFPINRKtgeaNLT 203
Cdd:cd16159 159 PLFPLLTAFVLITaltiflllylgavskrffvfllilsllfislfflllitnryfncilmRNHEvvEQPMSLE----NLT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 204 QLYTQEALDFIQTQhaRQSPFFLYWAIDATHAPVYASRQFLGTSLRGRYGDAVREIDDSVGKILSLLQNLGISKNTFVFF 283
Cdd:cd16159 235 QRLTKEAISFLERN--KERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 284 TSDNGAAL--ISAPNE--GGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDR 359
Cdd:cd16159 313 TSDNGGHLeeISVGGEygGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 360 VIDGLDLLPtMLKGQMMDRP---IFYYRGNTLMAVTLGQ------YKAHlWTWTNsweeFTQGTDFCPGQNV-----SGV 425
Cdd:cd16159 393 IIDGRDLMP-LLTGQEKRSPhefLFHYCGAELHAVRYRPrdggavWKAH-YFTPN----FYPGTEGCCGTLLcrcfgDSV 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 124007189 426 TTHtqeehtELPLIFHLGRDPGERFPLSFHSDEYQDALSRTTQVVQEHQKSLVPGQPQL 484
Cdd:cd16159 467 THH------DPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIEPVESQL 519
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-452 |
2.08e-117 |
|
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: 350.68 E-value: 2.08e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNG---EPSRETPNLDRMAAEGMLFPSFYsANPLCSPSRAALLTGRLPIRNGFYTTnaharna 104
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFY-VEPSCTPGRAAFITGRHPIRTGLTTV------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 105 yTPQEIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGspnchfgpydnkakpNIPVYRDWEMV 184
Cdd:cd16142 73 -GLPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYG---------------NLYHTIDEEIV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 185 GRfyeefpinrktgeanltqlytqeALDFIQTQHARQSPFFLYWAIDATHAPVYASRQFLGTSLR-GRYGDAVREIDDSV 263
Cdd:cd16142 137 DK-----------------------AIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSSGkGKYADSMVELDDHV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 264 GKILSLLQNLGISKNTFVFFTSDNGAALISAPneGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDL 343
Cdd:cd16142 194 GQILDALDELGIADNTIVIFTTDNGPEQDVWP--DGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDW 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 344 FTTSLSLAGLKPP------SDRVIDGLDLLPTMLK--GQMMDRPIFYYRGNTLMAVTLGQYKAHL----WTWTNSWEEFT 411
Cdd:cd16142 272 FPTLAALAGAPDPkdkllgKDRHIDGVDQSPFLLGksEKSRRSEFFYFGEGELGAVRWKNWKVHFkaqeDTGGPTGEPFY 351
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 124007189 412 QGTdfcpgqnvsgvtthtqeehteLPLIFHLGRDPGERFPL 452
Cdd:cd16142 352 VLT---------------------FPLIFNLRRDPKERYDV 371
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
27-505 |
2.79e-116 |
|
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: 351.75 E-value: 2.79e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 27 PPNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTtnaharNAYT 106
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYP------GVFY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 107 PQEiMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQ--FHPLKHGFDEWFGSPNCH-FGPYDNKA--KPNIPVY--- 178
Cdd:cd16158 75 PGS-RGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNgtYLPTHQGFDHYLGIPYSHdQGPCQNLTcfPPNIPCFggc 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 179 -RDWEMVGRFYEEFPINRKTGEANLTQLYTQEALDFIQTQHARQSPFFLYWAIDATHAPVYASRQFLGTSLRGRYGDAVR 257
Cdd:cd16158 154 dQGEVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 258 EIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALISApNEGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGqVSHQL 337
Cdd:cd16158 234 ELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRK-SRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPG-VTHEL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 338 GSIMDLFTTSLSLAGLKPPsDRVIDGLDLLPTML-KGQMMDRPIFYY-----RGNTLMAVTLGQYKAHLwtwtnsweeFT 411
Cdd:cd16158 312 ASTLDILPTIAKLAGAPLP-NVTLDGVDMSPILFeQGKSPRQTFFYYptspdPDKGVFAVRWGKYKAHF---------YT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 412 QG---TDFCPGQNVSGVTTHTqeeHTELPLIFHLGRDPGERFPLSfHSDEYQDALSRTTQVVQEHQKSLVPGQPQLNV-C 487
Cdd:cd16158 382 QGaahSGTTPDKDCHPSAELT---SHDPPLLFDLSQDPSENYNLL-GLPEYNQVLKQIQQVKERFEASMKFGESEINKgE 457
|
490
....*....|....*...
gi 124007189 488 NQAVMNWAPPGCEKLGKC 505
Cdd:cd16158 458 DPALEPCCKPGCTPKPSC 475
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
27-452 |
1.90e-111 |
|
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: 335.98 E-value: 1.90e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 27 PPNIVLLLMDDMGWGDLGVNGEPSR-ETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFyTTNAHARNay 105
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAiLTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 106 tpqeiMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHfgpydnkakpnipvyrdwemvg 185
Cdd:cd16161 78 -----VGGLPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSH---------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 186 rfyeefpinrktgEANLTQLYTQEALDFIQTQHARQSPFFLYWAIDATHAPV-YASRQFLGTSLRGRYGDAVREIDDSVG 264
Cdd:cd16161 131 -------------DSSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLaNLPRFQSPTSGRGPYGDALQEMDDLVG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 265 KILSLLQNLGISKNTFVFFTSDNGAALISAPNEGG-------SNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQL 337
Cdd:cd16161 198 QIMDAVKHAGLKDNTLTWFTSDNGPWEVKCELAVGpgtgdwqGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAAL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 338 GSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTMLKGQMMDRPIFYY------RGNTLMAVTLGQYKAHLWTWTNsweeFT 411
Cdd:cd16161 278 VSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHpnsgaaGAGALSAVRCGDYKAHYATGGA----LA 353
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 124007189 412 QGTDFCPgqnvsgvtthtqEEHTELPLIFHLGRDPGERFPL 452
Cdd:cd16161 354 CCGSTGP------------KLYHDPPLLFDLEVDPAESFPL 382
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-408 |
2.70e-110 |
|
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: 334.13 E-value: 2.70e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAY-- 105
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 106 ---TPQEIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSpnCHFGPYDNKAKPNIPVYRDWE 182
Cdd:cd16144 81 tklIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIGG--TGNGGPPSYYFPPGKPNPDLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 183 mvgrfyeefpiNRKTGEaNLTQLYTQEALDFIQTQHarQSPFFLYWAIDATHAPVYASRQFL------GTSLRGRYGDA- 255
Cdd:cd16144 159 -----------DGPEGE-YLTDRLTDEAIDFIEQNK--DKPFFLYLSHYAVHTPIQARPELIekyekkKKGLRKGQKNPv 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 256 ----VREIDDSVGKILSLLQNLGISKNTFVFFTSDNGaALISAPNEGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAG 331
Cdd:cd16144 225 yaamIESLDESVGRILDALEELGLADNTLVIFTSDNG-GLSTRGGPPTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 332 QVSHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTMLKGQMM--DRPIF----YYRGNTLM---AVTLGQYKAHLWT 402
Cdd:cd16144 304 SVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADlpRRALFwhfpHYHGQGGRpasAIRKGDWKLIEFY 383
|
....*.
gi 124007189 403 WTNSWE 408
Cdd:cd16144 384 EDGRVE 389
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
25-477 |
7.14e-104 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 316.82 E-value: 7.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 25 PQPPNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARna 104
Cdd:COG3119 21 AKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYN-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 105 ytpqeimGGIPNSEHLLPELLKKAGYTNKIVGKWHLghrpqfhplkhgfdewfgspnchfgpydnkakpnipvyrdwemv 184
Cdd:COG3119 99 -------GGLPPDEPTLAELLKEAGYRTALFGKWHL-------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 185 grfyeefpinrktgeaNLTQLYTQEALDFIQTQHARQSPFFLYWAIDATHAPVYASRQFLG------------------- 245
Cdd:COG3119 128 ----------------YLTDLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDkydgkdiplppnlaprdlt 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 246 ----TSLRGRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapNEGGSNGpflcGKQTTFEGGMREPAI 321
Cdd:COG3119 192 eeelRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSL----GEHGLRG----GKGTLYEGGIRVPLI 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 322 AWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPTML-KGQMMDRPIF--YYRGNTLMAVTLGQYKA 398
Cdd:COG3119 264 VRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTgEKAEWRDYLYweYPRGGGNRAIRTGRWKL 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124007189 399 HLWTWTNSWEEFtqgtdfcpgqnvsgvtthtqeehtelpliFHLGRDPGERFPLsfhSDEYQDALSRTTQVVQEHQKSL 477
Cdd:COG3119 342 IRYYDDDGPWEL-----------------------------YDLKNDPGETNNL---AADYPEVVAELRALLEAWLKEL 388
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-408 |
5.36e-102 |
|
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: 312.61 E-value: 5.36e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRlpirngfYTTNAHARNAYTP 107
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGL-------HTGHTRVRGNSEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 QEIMgGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQF-HPLKHGFDEWFGSPN---CHFG--PY--DNKAKPNIPvyr 179
Cdd:cd16145 74 GGQD-PLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYGYLDqvhAHNYypEYlwRNGEKVPLP--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 180 dwEMVGRFYEEFPINRKTGEANLTQLYTQEALDFIQTQHARqsPFFLYWAIDATHAPV------YASRQFLGTSLRG--- 250
Cdd:cd16145 150 --NNVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIRENKDK--PFFLYLAYTLPHAPLqvpddgPYKYKPKDPGIYAylp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 251 ------RYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAAlisapNEGG---------SNGPFLCGKQTTFEGG 315
Cdd:cd16145 226 wpqpekAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPH-----SEGGsehdpdffdSNGPLRGYKRSLYEGG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 316 MREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPTML--KGQMMDRPIFY--YRGNTLMAV 391
Cdd:cd16145 301 IRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLgkPQQQQHDYLYWefYEGGGAQAV 378
|
410
....*....|....*...
gi 124007189 392 TLGQYKA-HLWTWTNSWE 408
Cdd:cd16145 379 RMGGWKAvRHGKKDGPFE 396
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-449 |
1.86e-93 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 289.87 E-value: 1.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSR-ETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIR--NGFYTTNAHARNA 104
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRsrLKGGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 105 ytpqeimggIPNSEHLLPELLKKAGYTNKIVGKWHLG---------HRPQFH-------------PLKHGFDEWFGSPNC 162
Cdd:cd16143 81 ---------IEPDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkKAATGTgkdvdyskpikggPLDHGFDYYFGIPAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 163 HFGPydnkakpnipvyrdwemvgrfyeefpinrktgeanltqLYTQEALDFIQTQHARQSPFFLYWAIDATHAPVYASRQ 242
Cdd:cd16143 152 EVLP--------------------------------------TLTDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 243 FLGTSLRGRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAAL----ISAPNEGG-SNGPFLCGKQTTFEGGMR 317
Cdd:cd16143 194 FQGKSGAGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPyadyKELEKFGHdPSGPLRGMKADIYEGGHR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 318 EPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTML--KGQMMDRPIFYYRGNTLMAVTLGQ 395
Cdd:cd16143 274 VPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLgpKKQEVRESLVHHSGNGSFAIRKGD 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 124007189 396 YKahlwtwtnsweeftqgtdFCPGQNVSGVTTHTQEEHTELPLI--FHLGRDPGER 449
Cdd:cd16143 354 WK------------------LIDGTGSGGFSYPRGKEKLGLPPGqlYNLSTDPGES 391
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
28-436 |
2.07e-91 |
|
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: 285.21 E-value: 2.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYsANPLCSPSRAALLTGRLPIRNGFYTTnaharnaYTP 107
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFH-VSPVCAPTRAALLTGRYPFRTGVWHT-------ILG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 QEIMGGipnSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDnkakpnipvyrDWEMVGRF 187
Cdd:cd16146 73 RERMRL---DETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGGGIGQYP-----------DYWGNDYF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 188 YEEFPIN--RKTGEANLTQLYTQEALDFIQTQHarQSPFFLYWAIDATHAPVYASRQF--------LGTSLRGRYGdAVR 257
Cdd:cd16146 139 DDTYYHNgkFVKTEGYCTDVFFDEAIDFIEENK--DKPFFAYLATNAPHGPLQVPDKYldpykdmgLDDKLAAFYG-MIE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 258 EIDDSVGKILSLLQNLGISKNTFVFFTSDNGAAlisapneGGSNGPFLCG----KQTTFEGGMREPAIAWWPGHIAAGQV 333
Cdd:cd16146 216 NIDDNVGRLLAKLKELGLEENTIVIFMSDNGPA-------GGVPKRFNAGmrgkKGSVYEGGHRVPFFIRWPGKILAGKD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 334 SHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTMLKGQMM--DRPIFYYRGNTLM--------AVTLGQYKAhLWTW 403
Cdd:cd16146 289 VDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPwpERTLFTHSGRWPPppkkkrnaAVRTGRWRL-VSPK 367
|
410 420 430
....*....|....*....|....*....|....*
gi 124007189 404 TNSWEEFTQGTDfcPGQ--NVSgvtthtqEEHTEL 436
Cdd:cd16146 368 GFQPELYDIEND--PGEenDVA-------DEHPEV 393
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
28-397 |
4.54e-88 |
|
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: 275.97 E-value: 4.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSaNPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYtp 107
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYV-QPICTPSRAALMTGRYPIHTGMQHGVILAGEPY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 qeimgGIPNSEHLLPELLKKAGYTNKIVGKWHLGH-RPQFHPLKHGFDEWFGSPNCHFGPYDNKAKPnipvYRDWEMVGR 186
Cdd:cd16029 78 -----GLPLNETLLPQYLKELGYATHLVGKWHLGFyTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGG----ANDYGNDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 187 FYEEFPINRKTGEaNLTQLYTQEALDFIQtQHARQSPFFLYWAIDATHAPVYAS--------RQFLGTSLRGR--YGDAV 256
Cdd:cd16029 149 RDNEEPAWDYNGT-YSTDLFTDRAVDIIE-NHDPSKPLFLYLAFQAVHAPLQVPpeyadpyeDKFAHIKDEDRrtYAAMV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 257 REIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALISapNEGGSNGPFLCGKQTTFEGGMREPAIAWWPG-HIAAGQVSH 335
Cdd:cd16029 227 SALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGG--GDGGSNYPLRGGKNTLWEGGVRVPAFVWSPLlPPKRGTVSD 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124007189 336 QLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTMLKGQMMDR-PIFY-----YRGNTLMAVTLGQYK 397
Cdd:cd16029 305 GLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRtEILLniddiTRTTGGAAIRVGDWK 372
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
28-365 |
8.91e-86 |
|
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: 264.68 E-value: 8.91e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHArnaytp 107
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 qeimGGIPNSEHLLPELLKKAGYTNKIVGKWHlghrpqfhplkhgfdewfgspnchfgpydnkakpnipvyrdwemvgrf 187
Cdd:cd16022 75 ----GGLPPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 188 yeefpinrktgeanltqlytQEALDFIQtQHARQSPFFLYWAIDATHAPVYasrqflgtslrgrYGDAVREIDDSVGKIL 267
Cdd:cd16022 103 --------------------DEAIDFIE-RRDKDKPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRIL 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 268 SLLQNLGISKNTFVFFTSDNGAALisapNEGGSNGpflcGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTS 347
Cdd:cd16022 149 DALEELGLLDNTLIVFTSDHGDML----GDHGLRG----KKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTL 220
|
330
....*....|....*...
gi 124007189 348 LSLAGLKPPSDrvIDGLD 365
Cdd:cd16022 221 LDLAGIEPPEG--LDGRS 236
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
28-353 |
3.00e-84 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 262.74 E-value: 3.00e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTnaharnaytp 107
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 qeIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKakpnipvYRDWEMVGRF 187
Cdd:pfam00884 71 --TPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPP-------DVPYNCSGGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 188 YeefpinrktgeanLTQLYTQEALDFIQTQharQSPFFLYWAIDATHAPVYASRQFLGT------------SLRGRYGDA 255
Cdd:pfam00884 142 V-------------SDEALLDEALEFLDNN---DKPFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscseeQLLNSYDNT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 256 VREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapneGGSNGPFLCGKQ-TTFEGGMREPAIAWWPGHIAAGQVS 334
Cdd:pfam00884 206 LLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESL------GEGGGYLHGGKYdNAPEGGYRVPLLIWSPGGKAKGQKS 279
|
330
....*....|....*....
gi 124007189 335 HQLGSIMDLFTTSLSLAGL 353
Cdd:pfam00884 280 EALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-390 |
8.03e-75 |
|
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: 241.35 E-value: 8.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYsANPLCSPSRAALLTGRLPIRNG--FYTTNAharnay 105
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYvvFGYLDP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 106 tpqeimggipnSEHLLPELLKKAGYTNKIVGKWHLGHRPQF--HPLKHGFDEWfgspnCHFGPYDNKAKPNIPVYRDWEM 183
Cdd:cd16151 74 -----------KQKTFGHLLKDAGYATAIAGKWQLGGGRGDgdYPHEFGFDEY-----CLWQLTETGEKYSRPATPTFNI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 184 vgrfyeefpINRKTGEANLTQ----LYTQEALDFIQTQHARqsPFFLYWAIDATHAPV----------YASRQFlgTSLR 249
Cdd:cd16151 138 ---------RNGKLLETTEGDygpdLFADFLIDFIERNKDQ--PFFAYYPMVLVHDPFvptpdspdwdPDDKRK--KDDP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 250 GRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNG--AALISAPNEGGSNGpflcGKQTTFEGGMREPAIAWWPGH 327
Cdd:cd16151 205 EYFPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGthRPITSRTNGREVRG----GKGKTTDAGTHVPLIVNWPGL 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124007189 328 IAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTML--KGQMMDRPIFYYRGNTLMA 390
Cdd:cd16151 281 IPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLgkTGSPRREWIYWYYRNPHKK 345
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
26-417 |
5.08e-73 |
|
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: 237.34 E-value: 5.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 26 QPPNIVLLLMDDMGWGDLGVNGEPSReTPNLDRMAAEGMLFPSFYsANPLCSPSRAALLTGRLPIRNGF--YTTNAHARN 103
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEIP-TPNLDALAAEGLRFTNFH-TTALCSPTRAALLTGRNHHQVGMgtMAELATGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 104 AYTpqeimGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHrPQFHplkhgfdewfgspnchfgpydnkakpnipvyrdwem 183
Cdd:cd16025 79 GYE-----GYLPDSAATIAEVLKDAGYHTYMSGKWHLGP-DDYY------------------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 184 vgrfyeefpinrktgeanLTQLYTQEALDFIQTQHARQSPFFLYWAIDATHAPVYASRQFLgTSLRGRYG---DAVRE-- 258
Cdd:cd16025 117 ------------------STDDLTDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWI-DKYKGKYDagwDALREer 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 259 --------------------------------------------------IDDSVGKILSLLQNLGISKNTFVFFTSDNG 288
Cdd:cd16025 178 lerqkelglipadtkltprppgvpawdslspeekklearrmevyaamvehMDQQIGRLIDYLKELGELDNTLIIFLSDNG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 289 AaliSApnEGG----SNGPFLCGKQTTFEGGMREPAIAWWPGHIAA-GQVSHQLGSIMDLFTTSLSLAGLKPPSDRV--- 360
Cdd:cd16025 258 A---SA--EPGwanaSNTPFRLYKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvp 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124007189 361 ---IDGLDLLPTmLKGQM--MDRPIFYYR--GNTlmAVTLGQYKA---H-LWTWTNSWEEFTQGTDFC 417
Cdd:cd16025 333 qlpLDGVSLLPT-LDGAAapSRRRTQYFElfGNR--AIRKGGWKAvalHpPPGWGDQWELYDLAKDPS 397
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
28-378 |
2.09e-68 |
|
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: 224.31 E-value: 2.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSReTPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAYTP 107
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVK-TPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNG--AHGLRSRGFPLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 QEImggipnseHLLPELLKKAGYTNKIVGKWHlghrpqfhplkHGFDEwfgspncHFGPYDNKAKPNIPVYRDWEMVGRF 187
Cdd:cd16027 78 DGV--------KTLPELLREAGYYTGLIGKTH-----------YNPDA-------VFPFDDEMRGPDDGGRNAWDYASNA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 188 YeefpinrktgeanltqlytqealDFIQTQHARQsPFFLYWAIDATHAP-VYASRQFLGTSLR----------------- 249
Cdd:cd16027 132 A-----------------------DFLNRAKKGQ-PFFLWFGFHDPHRPyPPGDGEEPGYDPEkvkvppylpdtpevred 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 250 -GRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapneggsngPFlcGKQTTFEGGMREPAIAWWPGHI 328
Cdd:cd16027 188 lADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPF-----------PR--AKGTLYDSGLRVPLIVRWPGKI 254
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 124007189 329 AAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPTMLKGQMMDR 378
Cdd:cd16027 255 KPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGR 302
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
26-384 |
9.20e-68 |
|
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: 224.33 E-value: 9.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 26 QPPNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGfYTTNAHarnay 105
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHG-VTDNNG----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 106 tpqeimGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPlkHGFDEWFGSPnchfGPYDNKAKPNIpvyrdwEMVG 185
Cdd:cd16031 75 ------PLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPP--PGFDYWVSFP----GQGSYYDPEFI------ENGK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 186 RFYEEFPInrktgeanlTQLYTQEALDFIQTQHARQsPFFLYWAIDATHAPVYASRQFLGT------------------- 246
Cdd:cd16031 137 RVGQKGYV---------TDIITDKALDFLKERDKDK-PFCLSLSFKAPHRPFTPAPRHRGLyedvtipepetfddddyag 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 247 ----------SLRGRYGD-----------------AVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapnegG 299
Cdd:cd16031 207 rpewareqrnRIRGVLDGrfdtpekyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL-------G 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 300 SNGpfLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPtMLKGQMMD-- 377
Cdd:cd16031 280 EHG--LFDKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLP-LLEGEKPVdw 354
|
....*..
gi 124007189 378 RPIFYYR 384
Cdd:cd16031 355 RKEFYYE 361
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-374 |
4.02e-64 |
|
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: 213.97 E-value: 4.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHarnaytp 107
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 qeimggIPNSEHLLPELLKKAGYTNKIVGKWHL-GHRPQFH---------PLKHGFDEWFGSPNC--HFGPYDNKAKPNI 175
Cdd:cd16034 75 ------LPPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGraddytpppERRHGFDYWKGYECNhdHNNPHYYDDDGKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 176 PVYRDWEMvgrFYEefpinrktgeanltqlyTQEALDFIQTQHARQSPFFLYWAIDATHAPVYASRQ------------- 242
Cdd:cd16034 149 IYIKGYSP---DAE-----------------TDLAIEYLENQADKDKPFALVLSWNPPHDPYTTAPEeyldmydpkklll 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 243 ------------FLGTSLRGRYGdAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapnegGSNGpfLCGKQT 310
Cdd:cd16034 209 rpnvpedkkeeaGLREDLRGYYA-MITALDDNIGRLLDALKELGLLENTIVVFTSDHGDML-------GSHG--LMNKQV 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124007189 311 TFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPTMLKGQ 374
Cdd:cd16034 279 PYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGK 340
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-368 |
3.08e-53 |
|
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: 180.51 E-value: 3.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNG---FYTTNAHARnA 104
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGihdWIVEGSHGK-T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 105 YTPQEIMGGIPnsehLLPELLKKAGYTNKIVGKWHLGhrpqfhplkhgfdewfgspnchfgpydnkakpnipvyrdwemv 184
Cdd:cd16149 80 KKPEGYLEGQT----TLPEVLQDAGYRCGLSGKWHLG------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 185 grfyeefpinrktgeanltqlytQEALDFIQTQHARQSPFFLYWAIDATHAPvyasrqflgtslrGRYGDAVREIDDSVG 264
Cdd:cd16149 113 -----------------------DDAADFLRRRAEAEKPFFLSVNYTAPHSP-------------WGYFAAVTGVDRNVG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 265 KILSLLQNLGISKNTFVFFTSDNGAALisapnegGSNGPFlcGK------QTTFEGGMREPAIAWWPGHIAAGQVSHQLG 338
Cdd:cd16149 157 RLLDELEELGLTENTLVIFTSDNGFNM-------GHHGIW--GKgngtfpLNMYDNSVKVPFIIRWPGVVPAGRVVDSLV 227
|
330 340 350
....*....|....*....|....*....|
gi 124007189 339 SIMDLFTTSLSLAGLKPPSDRVIDGLDLLP 368
Cdd:cd16149 228 SAYDFFPTLLELAGVDPPADPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-397 |
1.80e-51 |
|
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: 178.12 E-value: 1.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTtNAHArnaytp 107
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWD-NADP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 qeIMGGIPNSEHLLPEllkkAGYTNKIVGKWHLGHRPQFHplkhGFDewfgspnchfgpYDnkakpnipvyrdwEMVgrf 187
Cdd:cd16037 74 --YDGDVPSWGHALRA----AGYETVLIGKLHFRGEDQRH----GFR------------YD-------------RDV--- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 188 yeefpinrktgeanltqlyTQEALDFIQTQHARQSPFFLYWAIDATHAPVYASRQFLG----TSLRGRYGdAVREIDDSV 263
Cdd:cd16037 116 -------------------TEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDlyvrRARAAYYG-LVEFLDENI 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 264 GKILSLLQNLGISKNTFVFFTSDNGAALisapnegGSNGpfLCGKQTTFEGGMREPAIAWWPGhIAAGQVSHQLGSIMDL 343
Cdd:cd16037 176 GRVLDALEELGLLDNTLIIYTSDHGDML-------GERG--LWGKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDL 245
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 124007189 344 FTTSLSLAGLKPPSDRviDGLDLLPTMLKGQMMDRPIF--YYRGNTLMA---VTLGQYK 397
Cdd:cd16037 246 APTILEAAGAPPPPDL--DGRSLLPLAEGPDDPDRVVFseYHAHGSPSGafmLRKGRWK 302
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-368 |
1.21e-49 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 175.87 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTtnaharNAYTP 107
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLN------NVENA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 QEIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGhrPQFHPLKHGFDEWFgsPNCHFGPYDnkakpnipvyrdwemvgrf 187
Cdd:cd16033 75 GAYSRGLPPGVETFSEDLREAGYRNGYVGKWHVG--PEETPLDYGFDEYL--PVETTIEYF------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 188 yeefpinrktgeanltqlYTQEALDFIQTQHARQSPFFLYWAIDATHAPVYASRQFLG---------------------- 245
Cdd:cd16033 132 ------------------LADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDmydpediplpesfaddfedkpy 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 246 ----TSLRG---------------RYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALISapnEGGSN-GPFL 305
Cdd:cd16033 194 iyrrERKRWgvdtedeedwkeiiaHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGA---HRLWDkGPFM 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124007189 306 cgkqttFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLP 368
Cdd:cd16033 271 ------YEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK--VDGRSLLP 325
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
28-351 |
2.71e-48 |
|
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: 166.83 E-value: 2.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFpSFYSANPLCS--PSRAALLTGRLPIRNGFYTTNAHARnay 105
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATF-NFRSVSPPTSsaPNHAALLTGAYPTLHGYTGNGSADP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 106 TPQEIMGGIPNSEHLLPELLKKAGYTNKIVGkwhlghrpqfhplkhgfdewfgspnchfgpydnkakpnipvyrdwemvg 185
Cdd:cd00016 77 ELPSRAAGKDEDGPTIPELLKQAGYRTGVIG------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 186 rfyeefpinrktgeanltqlytqeALDFIQtQHARQSPFFLYWAIDATHAPVYASRqflgtSLRGRYGDAVREIDDSVGK 265
Cdd:cd00016 108 ------------------------LLKAID-ETSKEKPFVLFLHFDGPDGPGHAYG-----PNTPEYYDAVEEIDERIGK 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 266 ILSLLQNLGISKNTFVFFTSDNGAALisapnEGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIaAGQVSHQLGSIMDLFT 345
Cdd:cd00016 158 VLDALKKAGDADDTVIIVTADHGGID-----KGHGGDPKADGKADKSHTGMRVPFIAYGPGVK-KGGVKHELISQYDIAP 231
|
....*.
gi 124007189 346 TSLSLA 351
Cdd:cd00016 232 TLADLL 237
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-463 |
7.69e-45 |
|
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: 161.96 E-value: 7.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANP----LCSPSRAALLTGrlpiRNGFYTTNAHARN 103
Cdd:cd16155 3 PNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGwsgaVCVPSRAMLMTG----RTLFHAPEGGKAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 104 aytpqeimggIPNSEHLLPELLKKAGYTNKIVGKWHLGhrpqfhplkhgfdewfgspnchfgpydnkakpnipvyrdwem 183
Cdd:cd16155 79 ----------IPSDDKTWPETFKKAGYRTFATGKWHNG------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 184 vgrfyeefpinrktgeanltqlYTQEALDFIQTQHARQSPFFLYWAIDATHAPVYA---------------------SRQ 242
Cdd:cd16155 107 ----------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAppeyldmyppetiplpenflpQHP 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 243 FLGTSLRG---------RYGDAVRE-----------IDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapnegGSNG 302
Cdd:cd16155 165 FDNGEGTVrdeqlapfpRTPEAVRQhlaeyyamithLDAQIGRILDALEASGELDNTIIVFTSDHGLAV-------GSHG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 303 pfLCGKQTTFEGGMREPAIAWWPGhIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPtMLKGQ---MMDRP 379
Cdd:cd16155 238 --LMGKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES--VEGKSLLP-VIRGEkkaVRDTL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 380 IFYYRGNTLMAVTlGQYKAHLWTwtnsweeftqgtdfcPGQNvsgvtthtqeeHTELpliFHLGRDPGERFPLSfHSDEY 459
Cdd:cd16155 312 YGAYRDGQRAIRD-DRWKLIIYV---------------PGVK-----------RTQL---FDLKKDPDELNNLA-DEPEY 360
|
....
gi 124007189 460 QDAL 463
Cdd:cd16155 361 QERL 364
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
27-410 |
7.37e-42 |
|
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: 154.25 E-value: 7.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 27 PPNIVLLLMDDMGWGDLGVNGEPsretPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFyTTNAHARNAYT 106
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMP----KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGV-TNNSPPGGGYP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 107 PQEIMGGIPNSehlLPELLKKAGYTNKIVGK----WHLGHRPQFHPLkhGFDEWFGSpnchFGPYdnkakpnipVYRDWE 182
Cdd:cd16147 76 KFWQNGLERST---LPVWLQEAGYRTAYAGKylngYGVPGGVSYVPP--GWDEWDGL----VGNS---------TYYNYT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 183 MVGRFYEEFPINRKtgEANLTQLYTQEALDFIQTQHARQSPFFLYWAIDATHAPV-----YASRqFLGTSLRGR------ 251
Cdd:cd16147 138 LSNGGNGKHGVSYP--GDYLTDVIANKALDFLRRAAADDKPFFLVVAPPAPHGPFtpaprYANL-FPNVTAPPRpppnnp 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 252 ---------------------YGD--------AVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapnegGSNG 302
Cdd:cd16147 215 dvsdkphwlrrlpplnptqiaYIDelyrkrlrTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHL-------GQHR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 303 -PFlcGKQTTFEGGMREPAIAWWPGhIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGldllptmlkgqmmdRPIF 381
Cdd:cd16147 288 lPP--GKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDG--------------RSCG 348
|
410 420 430
....*....|....*....|....*....|.
gi 124007189 382 YYRGNTLMAV-TLGQYKAHLWT-WTNSWEEF 410
Cdd:cd16147 349 DSNNNTYKCVrTVDDTYNLLYFeWCTGFREL 379
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
26-370 |
1.04e-41 |
|
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: 154.65 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 26 QPPNIVLLLMDDMG-WgdLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARna 104
Cdd:cd16030 1 KKPNVLFIAVDDLRpW--LGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 105 ytpqEIMGGIPnsehLLPELLKKAGYTNKIVGK-WHlGHRPQFHPLKHGFDEWFGSPncHFGPYDNKAKPNIPVYRDWEM 183
Cdd:cd16030 77 ----KVAPDAV----TLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPP--GPEKYPPGKLCPGKKGGKGGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 184 VGRFYEEFPInrkTGEANLTQLYTQEALDFIQTQHARQSPFFL----------------YW------------AIDATHA 235
Cdd:cd16030 146 GGPAWEAADV---PDEAYPDGKVADEAIEQLRKLKDSDKPFFLavgfykphlpfvapkkYFdlyplesiplpnPFDPIDL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 236 PVYASRQFlgTSLRGRYGD--------------------------AVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGA 289
Cdd:cd16030 223 PEVAWNDL--DDLPKYGDIpalnpgdpkgplpdeqarelrqayyaSVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 290 ALisapnegGSNGPFlcGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPT 369
Cdd:cd16030 301 HL-------GEHGHW--GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPPC--LEGKSLVPL 369
|
.
gi 124007189 370 M 370
Cdd:cd16030 370 L 370
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-368 |
8.90e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 148.08 E-value: 8.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMD----DMgwgdLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYttnaharn 103
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 104 aytpqeiMGGIPNSEHLLPELLKKAGYTNKIVGKW-HLGHRPQFHplkHGFDEWfgspncHFGPYDNKAKPNIPVYRDwe 182
Cdd:cd16148 69 -------GGPLEPDDPTLAEILRKAGYYTAAVSSNpHLFGGPGFD---RGFDTF------EDFRGQEGDPGEEGDERA-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 183 mvgrfyeefpinRKTgeanltqlyTQEALDFIQtQHARQSPFFLYWAIDATHAPvYasrqflgtslrgRYGDAVREIDDS 262
Cdd:cd16148 131 ------------ERV---------TDRALEWLD-RNADDDPFFLFLHYFDPHEP-Y------------LYDAEVRYVDEQ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 263 VGKILSLLQNLGISKNTFVFFTSDNGAALisapNEGGSNGpflcGKQTTF-EGGMREPAIAWWPGHIAAGQVSHQLGSIm 341
Cdd:cd16148 176 IGRLLDKLKELGLLEDTLVIVTSDHGEEF----GEHGLYW----GHGSNLyDEQLHVPLIIRWPGKEPGKRVDALVSHI- 246
|
330 340
....*....|....*....|....*..
gi 124007189 342 DLFTTSLSLAGLKPPSDrvIDGLDLLP 368
Cdd:cd16148 247 DIAPTLLDLLGVEPPDY--SDGRSLLP 271
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
28-473 |
3.90e-40 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 151.36 E-value: 3.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTp 107
Cdd:PRK13759 7 PNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVPWNYK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 qeimggipnseHLLPELLKKAGYTNKIVGKWHlghrpqFHP--LKHGFDE-WFGSPNCHFGPYDNKAKPN-IPVYRDW-- 181
Cdd:PRK13759 86 -----------NTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHNvLLHDGYLHSGRNEDKSQFDfVSDYLAWlr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 182 -EMVGRFYEEFPI--NRKTGEA-------NL--TQLYTQEALDFIQTQHARQsPFFLYWAIDATHAP---------VYAS 240
Cdd:PRK13759 149 eKAPGKDPDLTDIgwDCNSWVArpwdleeRLhpTNWVGSESIEFLRRRDPTK-PFFLKMSFARPHSPydppkryfdMYKD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 241 RQFLG-------------------TSLRGRYGDA------------VREIDDSVGKILSLLQNLGISKNTFVFFTSDNGA 289
Cdd:PRK13759 228 ADIPDphigdweyaedqdpeggsiDALRGNLGEEyarraraayyglITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 290 ALisapnegGSNGPFLcgKQTTFEGGMREPAIAWWPGHI---AAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDL 366
Cdd:PRK13759 308 ML-------GDHYLFR--KGYPYEGSAHIPFIIYDPGGLlagNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 367 LPtMLKGQmmdrpifyyrgntlmavtlgqykahlwtwTNSWEEFTQGTDFCPGQNVSGVTT-------HTQEEHTELpli 439
Cdd:PRK13759 377 KN-LIFGQ-----------------------------YEGWRPYLHGEHALGYSSDNYLTDgkwkyiwFSQTGEEQL--- 423
|
490 500 510
....*....|....*....|....*....|....
gi 124007189 440 FHLGRDPGERFPLSfHSDEYQDALSRTTQVVQEH 473
Cdd:PRK13759 424 FDLKKDPHELHNLS-PSEKYQPRLREMRKKLVDH 456
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
378-506 |
1.02e-39 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 140.14 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 378 RPIFYYRGNTLMAVTLGQYKAHLWTwtNSWeeFTQGTDFCPGQNVsgvtthtQEEHTELPLIFHLGRDPGERFPLSFHSD 457
Cdd:pfam14707 4 EFLFHYCGAALHAVRWGPYKAHFFT--PSF--DPPGAEGCYGSKV-------PVTHHDPPLLFDLERDPSEKYPLSPDSP 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 124007189 458 EYQDALSRTTQVVQEHQKSLVPGQPQLNVCNQAVMNWAPPGCEKLGKCL 506
Cdd:pfam14707 73 EYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACT 121
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
28-379 |
1.10e-37 |
|
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: 141.18 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYtTNAharnaytp 107
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAY-DNA-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 QEIMGGIPNSEHllpeLLKKAGYTNKIVGKWHL-GhrPQFHplkHGFDewfgspnchfgpYDnkakpnipvyrdwEMVgr 186
Cdd:cd16032 72 AEFPADIPTFAH----YLRAAGYRTALSGKMHFvG--PDQL---HGFD------------YD-------------EEV-- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 187 fyeEFPINRKtgeanltqLYtqealdfiqtQHARQS---PFFLYWAIDATHAPvYASRQ-----FLGTSLRGRYGdAVRE 258
Cdd:cd16032 116 ---AFKAVQK--------LY----------DLARGEdgrPFFLTVSFTHPHDP-YVIPQeywdlYVRRARRAYYG-MVSY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 259 IDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapnegGSNGpfLCGKQTTFEGGMREPAIAWWPGHIAAGQVShQLG 338
Cdd:cd16032 173 VDDKVGQLLDTLERTGLADDTIVIFTSDHGDML-------GERG--LWYKMSFFEGSARVPLIISAPGRFAPRRVA-EPV 242
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 124007189 339 SIMDLFTTSLSLAGLKPPSDRV-IDGLDLLPtMLKGQMMDRP 379
Cdd:cd16032 243 SLVDLLPTLVDLAGGGTAPHVPpLDGRSLLP-LLEGGDSGGE 283
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-368 |
1.04e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 136.97 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 27 PPNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYttnahaRNAyt 106
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCF------RNG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 107 pqeimGGIPNSEHLLPELLKKAGYTNKIVGKWHL-GHRPQFhplkhgfdewfgspnchfgpydnkakpnipvyrdwemvg 185
Cdd:cd16152 73 -----IPLPADEKTLAHYFRDAGYETGYVGKWHLaGYRVDA--------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 186 rfyeefpinrktgeanLTQLytqeALDFIQtQHARQSPFFLYWA---------IDATHAPV-YASR---QFLGTSLRGRY 252
Cdd:cd16152 109 ----------------LTDF----AIDYLD-NRQKDKPFFLFLSylephhqndRDRYVAPEgSAERfanFWVPPDLAALP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 253 GDA----------VREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALISAPNEggsngpflcGKQTTFEGGMREPAIA 322
Cdd:cd16152 168 GDWaeelpdylgcCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCHFRTRNAE---------YKRSCHESSIRVPLVI 238
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 124007189 323 WWPGhIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLP 368
Cdd:cd16152 239 YGPG-FNGGGRVEELVSLIDLPPTLLDAAGIDVPEE--MQGRSLLP 281
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-415 |
2.66e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 132.86 E-value: 2.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSR--ETPNLDRMAAEGMLFPSFYsANPLCSPSRAALLTGRLPIRNGFYTTNaharnay 105
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFDNLW-ATPACSPTRATILTGKYGFRTGVLAVP------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 106 tpqeimGGIPNSEHLLPELLKK----AGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSPNchfgpydnkakPNIPVYRDW 181
Cdd:cd16154 73 ------DELLLSEETLLQLLIKdattAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGILG-----------GGVQDYYNW 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 182 EMVgrfyeefpINRKTGEAN--LTQLYTQEALDFIQTQHarqSPFFLYWAIDATHAPVYA------SRQFLGTSL----- 248
Cdd:cd16154 136 NLT--------NNGQTTNSTeyATTKLTNLAIDWIDQQT---KPWFLWLAYNAPHTPFHLppaelhSRSLLGDSAdiean 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 249 -RGRYGDAVREIDDSVGKIL-SLLQNlgISKNTFVFFTSDNG---AALISAPNEGGSngpflcgKQTTFEGGMREPAIAW 323
Cdd:cd16154 205 pRPYYLAAIEAMDTEIGRLLaSIDEE--ERENTIIIFIGDNGtpgQVVDLPYTRNHA-------KGSLYEGGINVPLIVS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 324 WPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSdrVIDGLDLLPTmLKGQMMDRPIFYY----RGNTLMAVTLGQYKah 399
Cdd:cd16154 276 GAGVERANERESALVNATDLYATIAELAGVDAAE--IHDSVSFKPL-LSDVNASTRQYNYteyeSPTTTGWATRNQYY-- 350
|
410
....*....|....*.
gi 124007189 400 lwtwtnSWEEFTQGTD 415
Cdd:cd16154 351 ------KLIESENGQE 360
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-366 |
1.07e-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: 126.34 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEP------SR----ETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTt 97
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNAhtgkseSRlgyvESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 98 naharNAYTPQEIMGGIPnsehLLPELLKKAGYTNKIVGKWHLGhrpqfhplkhgfdewfgspnchfgpydnkakpnipv 177
Cdd:cd16153 81 -----FEAAHPALDHGLP----TFPEVLKKAGYQTASFGKSHLE------------------------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 178 yrdwemvgrfyeefPINRKTGEANltQLYTQEALDFIQTQHARQsPFFLYWAIDATHAPVYASRQFLGtslRGRYGDAVR 257
Cdd:cd16153 116 --------------AFQRYLKNAN--QSYKSFWGKIAKGADSDK-PFFVRLSFLQPHTPVLPPKEFRD---RFDYYAFCA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 258 EIDDSVGKILSLLQNLGISK---NTFVFFTSDNGAALisapnegGSNGpfLCGKQTTFEGGMREPAIAWWPGHIA--AGQ 332
Cdd:cd16153 176 YGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHL-------GEQG--ILAKFTFWPQSHRVPLIVVSSDKLKapAGK 246
|
330 340 350
....*....|....*....|....*....|....
gi 124007189 333 VSHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDL 366
Cdd:cd16153 247 VRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
28-381 |
2.64e-26 |
|
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: 111.71 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTN-AHARNAYT 106
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCmALGDNVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 107 pqeiMGgipnsehllpELLKKAGYTNKIVGKWHL-GHrpqfhplkhgfdEWFGSPNCHFGpYDnkakpniPVYrdWEMVG 185
Cdd:cd16156 81 ----IG----------QRLSDNGIHTAYIGKWHLdGG------------DYFGNGICPQG-WD-------PDY--WYDMR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 186 RFYEEFPINRKTGEAN-LTQLY--------------TQEALDFIQtQHARQsPFFLYWAIDATHAP---------VYASR 241
Cdd:cd16156 125 NYLDELTEEERRKSRRgLTSLEaegikeeftyghrcTNRALDFIE-KHKDE-DFFLVVSYDEPHHPflcpkpyasMYKDF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 242 QF-LGTSL---------------RGRYGDAVRE--------------IDDSVGKILSLLQNLGisKNTFVFFTSDNGAAL 291
Cdd:cd16156 203 EFpKGENAyddlenkplhqrlwaGAKPHEDGDKgtikhplyfgcnsfVDYEIGRVLDAADEIA--EDAWVIYTSDHGDML 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 292 isapnegGSNGPFLCGKqTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPsdRVIDGLDLLPTML 371
Cdd:cd16156 281 -------GAHKLWAKGP-AVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQP--KVLEGESILATIE 350
|
410
....*....|.
gi 124007189 372 KGQM-MDRPIF 381
Cdd:cd16156 351 DPEIpENRGVF 361
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
31-375 |
1.20e-22 |
|
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: 100.41 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 31 VLLLMDDMGWGD-LGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGfyttnaHARNAyTPqe 109
Cdd:cd16028 3 VLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHR------SVWNG-TP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 110 imggIPNSEHLLPELLKKAGYTNKIVGKWH----LGHRPQFHPLKH-------GFDewfgsPNCHFGPYD---------- 168
Cdd:cd16028 74 ----LDARHLTLALELRKAGYDPALFGYTDtspdPRGLAPLDPRLLsyelampGFD-----PVDRLDEYPaedsdtaflt 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 169 NKAKPNIPVYRD--WEMVGRFYEEF-------PINRKTGEANLTQLYTQEALDFIQTQHarqsPFFLYW-------AIDA 232
Cdd:cd16028 145 DRAIEYLDERQDepWFLHLSYIRPHppfvapaPYHALYDPADVPPPIRAESLAAEAAQH----PLLAAFlerieslSFSP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 233 THAPVYASRQFLGTSLRGRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapnegGSNgpFLCGKQTTF 312
Cdd:cd16028 221 GAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQL-------GDH--WLWGKDGFF 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124007189 313 EGGMREPAIAWWPG---HIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPtMLKGQM 375
Cdd:cd16028 292 DQAYRVPLIVRDPRreaDATRGQVVDAFTESVDVMPTILDWLGGEIPHQ--CDGRSLLP-LLAGAQ 354
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-356 |
4.54e-22 |
|
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: 98.46 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARnaytP 107
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLR----P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 QEimggiPNsehlLPELLKKAGYTNKIVGKWHLghrpqfhpLKHGFDewfgspnchFGPYdnkakpnipVYRDWEMVgrf 187
Cdd:cd16150 77 DE-----PN----LLKTLKDAGYHVAWAGKNDD--------LPGEFA---------AEAY---------CDSDEACV--- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 188 yeefpinrktgeanltqlytQEALDFIqTQHARQSPFFLYWAIDATHAPV-----YASR------------------QFL 244
Cdd:cd16150 119 --------------------RTAIDWL-RNRRPDKPFCLYLPLIFPHPPYgveepWFSMidreklpprrppglrakgKPS 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 245 GTSLRGRYG------DAVREI-----------DDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapnegGSNGpfLCG 307
Cdd:cd16150 178 MLEGIEKQGldrwseERWRELratylgmvsrlDHQFGRLLEALKETGLYDDTAVFFFSDHGDYT-------GDYG--LVE 248
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 124007189 308 K-QTTFEGGM-REPAIAWWPGhIAAGQVSHQLGSIMDLFTTSLSLAGLKPP 356
Cdd:cd16150 249 KwPNTFEDCLtRVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAGIPLS 298
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-371 |
4.99e-20 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 90.73 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNG-FYTTNAHARNAYT 106
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGvTDTLGSPMQPLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 107 PQeimggIPNSEHllpeLLKKAGYTNKIVGKWHLGhrpqfhplkhgfdewfGSPNchfGPYDnkakpnipvyRDwemvgr 186
Cdd:cd16035 81 PD-----VPTLGH----MLRAAGYYTAYKGKWHLS----------------GAAG---GGYK----------RD------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 187 fyeefpinrktgeanltQLYTQEALDFIQTQHAR---QSPFFL-----------YWAIDAThAPVYaSRQFlgtslrgrY 252
Cdd:cd16035 117 -----------------PGIAAQAVEWLRERGAKnadGKPWFLvvslvnphdimFPPDDEE-RWRR-FRNF--------Y 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 253 GDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGaalisapnE-GGSNGpflcGKQ---TTFEGGMREPAIAWWPGHI 328
Cdd:cd16035 170 YNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG--------EmGGAHG----LRGkgfNAYEEALHVPLIISHPDLF 237
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 124007189 329 AAGQVSHQLGSIMDLFTTSLSLAGLKPPSDRVID----GLDLLPTML 371
Cdd:cd16035 238 GTGQTTDALTSHIDLLPTLLGLAGVDAEARATEApplpGRDLSPLLT 284
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
28-352 |
1.78e-16 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 79.65 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDdmGWGDLGVNGEPSRE--TPNLDRMAAEGMLFPSFYSANPLCSPSRA--ALLTGRLPIRNGFYTTNAHARN 103
Cdd:cd16015 1 PNVIVILLE--SFSDPYIDKDVGGEdlTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 104 AYtpqeimggipNSehlLPELLKKAGYTNKIVgkwHLGH-----RPQFHPlKHGFDEWFGspnCHFGPYDNKAKPNIPVY 178
Cdd:cd16015 79 PL----------PS---LPSILKEQGYETIFI---HGGDasfynRDSVYP-NLGFDEFYD---LEDFPDDEKETNGWGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 179 rDWEMVGRFYEEFpinrktgeanltqlytqealdfiqtQHARQSPFFLY---------WAIDATHAPVYASRQFLGTSLr 249
Cdd:cd16015 139 -DESLFDQALEEL-------------------------EELKKKPFFIFlvtmsnhgpYDLPEEKKDEPLKVEEDKTEL- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 250 GRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALISAPNEGGSNgpflcgkqttFEGGMREPAIAWWPGhIA 329
Cdd:cd16015 192 ENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDED----------PLDLYRTPLLIYSPG-LK 260
|
330 340
....*....|....*....|...
gi 124007189 330 AGQVSHQLGSIMDLFTTSLSLAG 352
Cdd:cd16015 261 KPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
28-446 |
1.61e-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: 77.97 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGrlpirngFYTTNAHARNAYTp 107
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG-------LFTHLTESWNNYK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 108 qeimgGIPNSEHLLPELLKKAGYTNKIVGKwhLGHRPQFHPLKHGFDEWfgspnchfgpydnkakpnipvYRDWEMVGRf 187
Cdd:cd16171 73 -----GLDPNYPTWMDRLEKHGYHTQKYGK--LDYTSGHHSVSNRVEAW---------------------TRDVPFLLR- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 188 YEEFPINRKTGEANLTQLY------TQEALDFIQTQHARQS-PFFLYWAIDATHA-PVYASRQFLGT--SLRGRYGDAVR 257
Cdd:cd16171 124 QEGRPTVNLVGDRSTVRVMlkdwqnTDKAVHWIRKEAPNLTqPFALYLGLNLPHPyPSPSMGENFGSirNIRAFYYAMCA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 258 EIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALIsapneggSNGPFLcgKQTTFEGGMREPAIAWWPGhIAAGQVSHQL 337
Cdd:cd16171 204 ETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAM-------EHRQFY--KMSMYEGSSHVPLLIMGPG-IKAGQQVSDV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 338 GSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPTMLKGQMMDRPIFYYRGNTLMA------VTLGQYKahlwTWTNSWEEFT 411
Cdd:cd16171 274 VSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLLSESSIKESPSRVPHPDWVLSefhgcnVNASTYM----LRTNSWKYIA 347
|
410 420 430
....*....|....*....|....*....|....*
gi 124007189 412 qgtdFCPGQNVSgvtthtqeehtelPLIFHLGRDP 446
Cdd:cd16171 348 ----YADGNSVP-------------PQLFDLSKDP 365
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
26-367 |
4.56e-15 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 77.77 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 26 QPPNIVLLLMDDMGW---GDLGVNGEPsreTPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGrLPIRNGFYTTNAHAR 102
Cdd:COG1368 233 KKPNVVVILLESFSDffiGALGNGKDV---TPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTG-LPPLPGGSPYKRPGQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 103 NAYtpqeimggipNSehlLPELLKKAGYTNKIV--GKWHLGHRPQFHPlKHGFDEWFGSPNchfgpYDNKAKPNIPVYrD 180
Cdd:COG1368 309 NNF----------PS---LPSILKKQGYETSFFhgGDGSFWNRDSFYK-NLGFDEFYDRED-----FDDPFDGGWGVS-D 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 181 WEMvgrfyeefpinrktgeanltqlyTQEALDFIQTQharQSPFFLY---------WAIDATHAPVYAsrqfLGTSLRGR 251
Cdd:COG1368 369 EDL-----------------------FDKALEELEKL---KKPFFAFlitlsnhgpYTLPEEDKKIPD----YGKTTLNN 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 252 YGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapnEGGSNGPFLCGKQTTfeggmrePAIaWWPGHIAAG 331
Cdd:COG1368 419 YLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRS-----PGKTDYENPLERYRV-------PLL-IYSPGLKKP 485
|
330 340 350
....*....|....*....|....*....|....*.
gi 124007189 332 QVSHQLGSIMDLFTTSLSLAGLKPPSDRVIdGLDLL 367
Cdd:COG1368 486 KVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
31-293 |
1.17e-10 |
|
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: 62.82 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 31 VLLLMDDMGWGDLgvngEPSRETPNLDRMAAEG----MLFPSFysaNPLCSPSRAALLTGRLPIRNGFYttnaharnayt 106
Cdd:pfam01663 2 LVISLDGFRADYL----DRFELTPNLAALAKEGvsapNLTPVF---PTLTFPNHYTLVTGLYPGSHGIV----------- 63
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 107 pqeimggipNSEHLLPELLKKAGY--TNKIVGKWHLGHRPQFHPLKHGFdewfgSPNCHFGPYDNKAKPNIPVYRDWEMV 184
Cdd:pfam01663 64 ---------GNTFYDPKTGEYLVFviSDPEDPRWWQGEPIWDTAAKAGV-----RAAALFWPGSEVDYSTYYGTPPRYLK 129
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 185 GRFYEEFPINRKTGEANLTQLYTQEALDfiqtqHARQSPFFLYW---AIDAT-HAPVYASRQFLgtslrgrygDAVREID 260
Cdd:pfam01663 130 DDYNNSVPFEDRVDTAVLQTWLDLPFAD-----VAAERPDLLLVyleEPDYAgHRYGPDSPEVE---------DALRRVD 195
|
250 260 270
....*....|....*....|....*....|...
gi 124007189 261 DSVGKILSLLQNLGISKNTFVFFTSDNGAALIS 293
Cdd:pfam01663 196 RAIGDLLEALDERGLFEDTNVIVVSDHGMTPVS 228
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|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
25-288 |
5.46e-10 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 61.30 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 25 PQPPNIVLLLMDDMGWGDLGvngepSRETPNLDRMAAEGMLFPSFYSANPlcS---PSRAALLTGRLPIR-----NGFYT 96
Cdd:COG1524 21 PPAKKVVLILVDGLRADLLE-----RAHAPNLAALAARGVYARPLTSVFP--SttaPAHTTLLTGLYPGEhgivgNGWYD 93
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 97 TNAHARNAYTPQEIMGGIPNSEHLLP---ELLKKAGYTNKIVGKWHLGHRPQFHplkhgfdewfgspnchfgpydnkakP 173
Cdd:COG1524 94 PELGRVVNSLSWVEDGFGSNSLLPVPtifERARAAGLTTAAVFWPSFEGSGLID-------------------------A 148
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 174 NIPVYRDwemvGRFYeefpinrKTGEANLTQLYTQEALDFIQTQHarqsP--FFLYW-AIDAT-Hapvyasrqflgtslr 249
Cdd:COG1524 149 ARPYPYD----GRKP-------LLGNPAADRWIAAAALELLREGR----PdlLLVYLpDLDYAgH--------------- 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 124007189 250 gRYG-------DAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNG 288
Cdd:COG1524 199 -RYGpdspeyrAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
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| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
28-288 |
5.46e-06 |
|
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: 47.96 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 28 PNIVLLLMDDMGWGDLgvngEPSRETPNLDRMAAEGMLFPSFYSANP-LCSPSRAALLTGRLPIR-----NGFY--TTNA 99
Cdd:cd16018 1 PPLIVISIDGFRWDYL----DRAGLTPNLKRLAEEGVRAKYVKPVFPtLTFPNHYSIVTGLYPEShgivgNYFYdpKTNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 100 --HARNAYTPQEIMGGIPnsehlLPELLKKAGYTnkiVGKWHlghrpqfhplkhgfdeWFGSPNCHFGPYdnkakpNIPV 177
Cdd:cd16018 77 efSDSDWVWDPWWIGGEP-----IWVTAEKAGLK---TASYF----------------WPGSEVAIIGYN------PTPI 126
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124007189 178 YRDWeMVGRFYEEFPinrktgeanltqlyTQEALDFIQTQHARQSPFFLYW---AIDAT-HapvyasrqflgtslrgRYG 253
Cdd:cd16018 127 PLGG-YWQPYNDSFP--------------FEERVDTILEWLDLERPDLILLyfeEPDSAgH----------------KYG 175
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 124007189 254 -------DAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNG 288
Cdd:cd16018 176 pdspevnEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG 217
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