|
Name |
Accession |
Description |
Interval |
E-value |
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
31-496 |
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: 962.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 31 PPNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 110
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 111 PQEIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKVKPNIPVYRDWEMVGR 190
Cdd:cd16157 81 PQNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCHFGPYDNKAYPNIPVYRDWEMIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 191 FYEEFPINLKTGEANLTQLYLQEALDFIRTQHARQSPFFLYWAIDATHAPVYASKQFLGTSLRGRYGDAVREIDDSVGKI 270
Cdd:cd16157 161 YYEEFKIDKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 271 LSLLQNLGISKNTFVFFTSDNGAALISAPKEGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTT 350
Cdd:cd16157 241 LESLKSLGIENNTFVFFSSDNGAALISAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 351 SLSLAGLKPPSDRVIDGLDLLPTMLQGHIIDRPIFYYRGNTLMAVTLGQYKAHLWTWTNSWEEFRQGIDFCPGQNVSGVT 430
Cdd:cd16157 321 SLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGDELMAVRLGQYKAHFWTWSNSWEEFRKGINFCPGQNVPGVT 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 114145565 431 THTQEEHTELPLIFHLGRDPGERFPLRFTSNEYQDALSRTTQVIQQHQKSLVPGQPQLNVCNQAVM 496
Cdd:cd16157 401 THNQTDHTKLPLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVVQQHQKTLVPGEPQLNVCDLAVM 466
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
31-456 |
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: 540.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 31 PPNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharnayt 110
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVG------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 111 PQEIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKVKPNIPVYRDWEMVGR 190
Cdd:cd16026 74 PPGSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLPPLMENE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 191 FYEEFPINLktgeANLTQLYLQEALDFIRTQhaRQSPFFLYWAIDATHAPVYASKQFLGTSLRGRYGDAVREIDDSVGKI 270
Cdd:cd16026 154 EVIEQPADQ----SSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 271 LSLLQNLGISKNTFVFFTSDNGAALISaPKEGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTT 350
Cdd:cd16026 228 LDALKELGLEENTLVIFTSDNGPWLEY-GGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 351 SLSLAGLKPPSDRVIDGLDLLPTMLQGH-IIDRPIFYYR-GNTLMAVTLGQYKAHLWTWTNSWEEFRqgidfcpgqnvsg 428
Cdd:cd16026 307 LAALAGAPLPEDRVIDGKDISPLLLGGSkSPPHPFFYYYdGGDLQAVRSGRWKLHLPTTYRTGTDPG------------- 373
|
410 420
....*....|....*....|....*...
gi 114145565 429 vttHTQEEHTELPLIFHLGRDPGERFPL 456
Cdd:cd16026 374 ---GLDPTKLEPPLLYDLEEDPGETYNV 398
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
32-456 |
1.69e-123 |
|
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: 369.07 E-value: 1.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTnahaRNAYTP 111
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGG----TRVFLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 112 QEImGGIPNSEHLLPELLKKAGYTNKIVGKWHLG-----HRPQFH-PLKHGFD----------EWFGSPNCHFGPYDNKV 175
Cdd:cd16160 78 WDI-GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDfvgtnlpftnSWACDDTGRHVDFPDRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 176 KPNIpvYRDWEMVgrfyeEFPINLKtgeaNLTQLYLQEALDFIRTQHARqsPFFLYWAIDATHAPVYASKQFLGTSLRGR 255
Cdd:cd16160 157 ACFL--YYNDTIV-----EQPIQHE----HLTETLVGDAKSFIEDNQEN--PFFLYFSFPQTHTPLFASKRFKGKSKRGR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 256 YGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALiSAPKEGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIaAG 335
Cdd:cd16160 224 YGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHV-EYCLEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTI-KP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 336 QVSHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTMLQGHIID-RPIFYYRGNTLMAVTLGQYKAHLWTWTNSWEEF 414
Cdd:cd16160 302 RVSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPhDDILYYCCSRLMAVRYGSYKIHFKTQPLPSQES 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 114145565 415 rQGIDFCPGQNVS-------GVTTHTQEEHteLPLIFHLGRDPGERFPL 456
Cdd:cd16160 382 -LDPNCDGGGPLSdyivcydCEDECVTKHN--PPLIFDVEKDPGEQYPL 427
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
32-456 |
1.48e-120 |
|
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: 358.77 E-value: 1.48e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYG---EPSRETPNLDRMAAEGMLFPSFYsANPLCSPSRAALLTGRLPIRNGFYTTnaharna 108
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFY-VEPSCTPGRAAFITGRHPIRTGLTTV------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 109 yTPQEIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGspnchfgpydnkvkpNIPVYRDWEMV 188
Cdd:cd16142 73 -GLPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYG---------------NLYHTIDEEIV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 189 GRfyeefpinlktgeanltqlylqeALDFIRTQHARQSPFFLYWAIDATHAPVYASKQFLGTSLR-GRYGDAVREIDDSV 267
Cdd:cd16142 137 DK-----------------------AIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSSGkGKYADSMVELDDHV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 268 GKILSLLQNLGISKNTFVFFTSDNGAALISAPkeGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDL 347
Cdd:cd16142 194 GQILDALDELGIADNTIVIFTTDNGPEQDVWP--DGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDW 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 348 FTTSLSLAGLKPP------SDRVIDGLDLLPTML--QGHIIDRPIFYYRGNTLMAVTLGQYKAHlwtwtnsweeFRQGID 419
Cdd:cd16142 272 FPTLAALAGAPDPkdkllgKDRHIDGVDQSPFLLgkSEKSRRSEFFYFGEGELGAVRWKNWKVH----------FKAQED 341
|
410 420 430
....*....|....*....|....*....|....*..
gi 114145565 420 FcpgqnvsGVTTHTQEEHTELPLIFHLGRDPGERFPL 456
Cdd:cd16142 342 T-------GGPTGEPFYVLTFPLIFNLRRDPKERYDV 371
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
31-509 |
5.41e-118 |
|
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: 356.37 E-value: 5.41e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 31 PPNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTtnaharNAYT 110
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYP------GVFY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 111 PQEiMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQ--FHPLKHGFDEWFGSPNCH-FGPYDNKV--KPNIPVY--- 182
Cdd:cd16158 75 PGS-RGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNgtYLPTHQGFDHYLGIPYSHdQGPCQNLTcfPPNIPCFggc 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 183 -RDWEMVGRFYEEFPINLKTGEANLTQLYLQEALDFIRTQHARQSPFFLYWAIDATHAPVYASKQFLGTSLRGRYGDAVR 261
Cdd:cd16158 154 dQGEVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 262 EIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALISAPKeGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGqVSHQL 341
Cdd:cd16158 234 ELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRKSR-GGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPG-VTHEL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 342 GSIMDLFTTSLSLAGLKPPsDRVIDGLDLLPTMLQGHIIDRPIFYY------RGNTLMAVTLGQYKAHLWTwtnsweefr 415
Cdd:cd16158 312 ASTLDILPTIAKLAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYyptspdPDKGVFAVRWGKYKAHFYT--------- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 416 QGI---DFCPGQNVSGVTTHTqeeHTELPLIFHLGRDPGERFPLRFTSnEYQDALSRTTQVIQQHQKSLVPGQPQLNV-C 491
Cdd:cd16158 382 QGAahsGTTPDKDCHPSAELT---SHDPPLLFDLSQDPSENYNLLGLP-EYNQVLKQIQQVKERFEASMKFGESEINKgE 457
|
490
....*....|....*...
gi 114145565 492 NQAVMNWAPPGCEKLGKC 509
Cdd:cd16158 458 DPALEPCCKPGCTPKPSC 475
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
31-488 |
1.82e-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: 356.21 E-value: 1.82e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 31 PPNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 110
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 111 PQEimGGIPNSEHLLPELLKKAGYTNKIVGKWHLG-HRPQ-----FHPLKHGFDEWFGSP-----NCHFGP---YDNKVK 176
Cdd:cd16159 81 ASS--GGLPPNETTFAEVLKQQGYSTALIGKWHLGlHCESrndfcHHPLNHGFDYFYGLPltnlkDCGDGSngeYDLSFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 177 PNIPVYRDWEMVG-----------------------------------------------RFYE--EFPINLKtgeaNLT 207
Cdd:cd16159 159 PLFPLLTAFVLITaltiflllylgavskrffvfllilsllfislfflllitnryfncilmRNHEvvEQPMSLE----NLT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 208 QLYLQEALDFIRTQhaRQSPFFLYWAIDATHAPVYASKQFLGTSLRGRYGDAVREIDDSVGKILSLLQNLGISKNTFVFF 287
Cdd:cd16159 235 QRLTKEAISFLERN--KERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 288 TSDNGAAL--ISAPKE--GGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDR 363
Cdd:cd16159 313 TSDNGGHLeeISVGGEygGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 364 VIDGLDLLPtMLQGHIIDRP---IFYYRGNTLMAVTLGQ------YKAHlWTWTNsweeFRQGIDFCPGQNV-----SGV 429
Cdd:cd16159 393 IIDGRDLMP-LLTGQEKRSPhefLFHYCGAELHAVRYRPrdggavWKAH-YFTPN----FYPGTEGCCGTLLcrcfgDSV 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 114145565 430 TTHtqeehtELPLIFHLGRDPGERFPLRFTSNEYQDALSRTTQVIQQHQKSLVPGQPQL 488
Cdd:cd16159 467 THH------DPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIEPVESQL 519
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
32-412 |
4.86e-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: 333.74 E-value: 4.86e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAY-- 109
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 110 ---TPQEIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSpnCHFGPYDNKVKPNIPVYRDWE 186
Cdd:cd16144 81 tklIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIGG--TGNGGPPSYYFPPGKPNPDLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 187 mvgrfyeefpiNLKTGEaNLTQLYLQEALDFIRTQHarQSPFFLYWAIDATHAPVYASKQFL------GTSLRGRYGDA- 259
Cdd:cd16144 159 -----------DGPEGE-YLTDRLTDEAIDFIEQNK--DKPFFLYLSHYAVHTPIQARPELIekyekkKKGLRKGQKNPv 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 260 ----VREIDDSVGKILSLLQNLGISKNTFVFFTSDNGaALISAPKEGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAG 335
Cdd:cd16144 225 yaamIESLDESVGRILDALEELGLADNTLVIFTSDNG-GLSTRGGPPTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 336 QVSHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTMLQGHII--DRPIF----YYRGNTLM---AVTLGQYKAHLWT 406
Cdd:cd16144 304 SVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADlpRRALFwhfpHYHGQGGRpasAIRKGDWKLIEFY 383
|
....*.
gi 114145565 407 WTNSWE 412
Cdd:cd16144 384 EDGRVE 389
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
31-456 |
1.66e-108 |
|
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: 328.66 E-value: 1.66e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 31 PPNIVLLLMDDMGWGDLGVYGEPSR-ETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFyTTNAHARNay 109
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAiLTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 110 tpqeiMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHfgpydnkvkpnipvyrdwemvg 189
Cdd:cd16161 78 -----VGGLPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSH---------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 190 rfyeefpinlktgEANLTQLYLQEALDFIRTQHARQSPFFLYWAIDATHAPV-YASKQFLGTSLRGRYGDAVREIDDSVG 268
Cdd:cd16161 131 -------------DSSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLaNLPRFQSPTSGRGPYGDALQEMDDLVG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 269 KILSLLQNLGISKNTFVFFTSDNGAALISAPKEGG-------SNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQL 341
Cdd:cd16161 198 QIMDAVKHAGLKDNTLTWFTSDNGPWEVKCELAVGpgtgdwqGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAAL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 342 GSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTMLQGHIIDRPIFYY------RGNTLMAVTLGQYKAHLWTwtnsweefr 415
Cdd:cd16161 278 VSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHpnsgaaGAGALSAVRCGDYKAHYAT--------- 348
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 114145565 416 QGI-----DFCPgqnvsgvtthtqEEHTELPLIFHLGRDPGERFPL 456
Cdd:cd16161 349 GGAlaccgSTGP------------KLYHDPPLLFDLEVDPAESFPL 382
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
9-481 |
6.70e-106 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 322.21 E-value: 6.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 9 RAQQLLLPVLSALglLAAGAPQPPNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALL 88
Cdd:COG3119 3 RLLLLLLALLAAA--AAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 89 TGRLPIRNGFYTTNAHARnaytpqeimGGIPNSEHLLPELLKKAGYTNKIVGKWHLghrpqfhplkhgfdewfgspnchf 168
Cdd:COG3119 81 TGRYPHRTGVTDNGEGYN---------GGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 169 gpydnkvkpnipvyrdwemvgrfyeefpinlktgeaNLTQLYLQEALDFIRTQHARQSPFFLYWAIDATHAPVYASKQFL 248
Cdd:COG3119 128 ------------------------------------YLTDLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 249 G-----------------------TSLRGRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapkegGSN 305
Cdd:COG3119 172 DkydgkdiplppnlaprdlteeelRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSL-------GEH 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 306 GpFLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPTMLQGHIIDRPIF 385
Cdd:COG3119 245 G-LRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYL 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 386 YY---RGNTLMAVTLGQYKAHLWTWTNSWEEFrqgidfcpgqnvsgvtthtqeehtelpliFHLGRDPGERFPLrftSNE 462
Cdd:COG3119 322 YWeypRGGGNRAIRTGRWKLIRYYDDDGPWEL-----------------------------YDLKNDPGETNNL---AAD 369
|
490
....*....|....*....
gi 114145565 463 YQDALSRTTQVIQQHQKSL 481
Cdd:COG3119 370 YPEVVAELRALLEAWLKEL 388
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
32-412 |
1.04e-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: 314.53 E-value: 1.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRlpirngfYTTNAHARNAYTP 111
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGL-------HTGHTRVRGNSEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 112 QEIMgGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQF-HPLKHGFDEWFGSPN---CHFG--PY--DNKVKPNIPvyr 183
Cdd:cd16145 74 GGQD-PLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYGYLDqvhAHNYypEYlwRNGEKVPLP--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 184 dwEMVGRFYEEFPINLKTGEANLTQLYLQEALDFIRTQHARqsPFFLYWAIDATHAPV------YASKQFLGTSLRG--- 254
Cdd:cd16145 150 --NNVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIRENKDK--PFFLYLAYTLPHAPLqvpddgPYKYKPKDPGIYAylp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 255 ------RYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAAlisapKEGG---------SNGPFLCGKQTTFEGG 319
Cdd:cd16145 226 wpqpekAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPH-----SEGGsehdpdffdSNGPLRGYKRSLYEGG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 320 MREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPTML-----QGHiidRPIFY--YRGNTL 392
Cdd:cd16145 301 IRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLgkpqqQQH---DYLYWefYEGGGA 375
|
410 420
....*....|....*....|.
gi 114145565 393 MAVTLGQYKA-HLWTWTNSWE 412
Cdd:cd16145 376 QAVRMGGWKAvRHGKKDGPFE 396
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
32-453 |
4.50e-95 |
|
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: 294.49 E-value: 4.50e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSR-ETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIR--NGFYTTNAHARNA 108
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRsrLKGGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 109 ytpqeimggIPNSEHLLPELLKKAGYTNKIVGKWHLG---------HRPQFH-------------PLKHGFDEWFGSPNC 166
Cdd:cd16143 81 ---------IEPDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkKAATGTgkdvdyskpikggPLDHGFDYYFGIPAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 167 HFGPYdnkvkpnipvyrdwemvgrfyeefpinlktgeanLTQlylqEALDFIRTQHARQSPFFLYWAIDATHAPVYASKQ 246
Cdd:cd16143 152 EVLPT----------------------------------LTD----KAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 247 FLGTSLRGRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAAL----ISAPKEGG-SNGPFLCGKQTTFEGGMR 321
Cdd:cd16143 194 FQGKSGAGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPyadyKELEKFGHdPSGPLRGMKADIYEGGHR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 322 EPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTML--QGHIIDRPIFYYRGNTLMAVTLGQ 399
Cdd:cd16143 274 VPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLgpKKQEVRESLVHHSGNGSFAIRKGD 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 114145565 400 YKahlwtwtnsweefrqgidFCPGQNVSGVTTHTQEEHTELPLI--FHLGRDPGER 453
Cdd:cd16143 354 WK------------------LIDGTGSGGFSYPRGKEKLGLPPGqlYNLSTDPGES 391
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
32-440 |
2.39e-89 |
|
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: 279.82 E-value: 2.39e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYsANPLCSPSRAALLTGRLPIRNGFYTTnaharnaYTP 111
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFH-VSPVCAPTRAALLTGRYPFRTGVWHT-------ILG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 112 QEIMGGipnSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDnkvkpnipvyrDWEMVGRF 191
Cdd:cd16146 73 RERMRL---DETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGGGIGQYP-----------DYWGNDYF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 192 YEEFPIN--LKTGEANLTQLYLQEALDFIRTQHarQSPFFLYWAIDATHAPVYASKQF--------LGTSLRGRYGdAVR 261
Cdd:cd16146 139 DDTYYHNgkFVKTEGYCTDVFFDEAIDFIEENK--DKPFFAYLATNAPHGPLQVPDKYldpykdmgLDDKLAAFYG-MIE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 262 EIDDSVGKILSLLQNLGISKNTFVFFTSDNGAAlisapkeGGSNGPFLCG----KQTTFEGGMREPAIAWWPGHIAAGQV 337
Cdd:cd16146 216 NIDDNVGRLLAKLKELGLEENTIVIFMSDNGPA-------GGVPKRFNAGmrgkKGSVYEGGHRVPFFIRWPGKILAGKD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 338 SHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTMLQG--HIIDRPIFYYRGNTLM--------AVTLGQYKAhLWTW 407
Cdd:cd16146 289 VDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGEsdPWPERTLFTHSGRWPPppkkkrnaAVRTGRWRL-VSPK 367
|
410 420 430
....*....|....*....|....*....|....*
gi 114145565 408 TNSWEEFRQGIDfcPGQ--NVSgvtthtqEEHTEL 440
Cdd:cd16146 368 GFQPELYDIEND--PGEenDVA-------DEHPEV 393
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
32-401 |
1.92e-87 |
|
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: 274.43 E-value: 1.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSaNPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYtp 111
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYV-QPICTPSRAALMTGRYPIHTGMQHGVILAGEPY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 112 qeimgGIPNSEHLLPELLKKAGYTNKIVGKWHLGH-RPQFHPLKHGFDEWFGspncHFGPYDNKVKPNIPVYRDWEMVGR 190
Cdd:cd16029 78 -----GLPLNETLLPQYLKELGYATHLVGKWHLGFyTWEYTPTNRGFDSFYG----YYGGAEDYYTHTSGGANDYGNDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 191 FYEEFPINLKTGEaNLTQLYLQEALDFIRtQHARQSPFFLYWAIDATHAPVYASKQFL--------GTSLRGR--YGDAV 260
Cdd:cd16029 149 RDNEEPAWDYNGT-YSTDLFTDRAVDIIE-NHDPSKPLFLYLAFQAVHAPLQVPPEYAdpyedkfaHIKDEDRrtYAAMV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 261 REIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALISApkEGGSNGPFLCGKQTTFEGGMREPAIAWWPG-HIAAGQVSH 339
Cdd:cd16029 227 SALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGG--DGGSNYPLRGGKNTLWEGGVRVPAFVWSPLlPPKRGTVSD 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114145565 340 QLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTMLQG---------HIIDrpiFYYRGNTLMAVTLGQYK 401
Cdd:cd16029 305 GLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGapsprteilLNID---DITRTTGGAAIRVGDWK 372
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
32-369 |
3.05e-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: 265.84 E-value: 3.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHArnaytp 111
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 112 qeimGGIPNSEHLLPELLKKAGYTNKIVGKWHlghrpqfhplkhgfdewfgspnchfgpydnkvkpnipvyrdwemvgrf 191
Cdd:cd16022 75 ----GGLPPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 192 yeefpinlktgeanltqlylQEALDFIRtQHARQSPFFLYWAIDATHAPVYaskqflgtslrgrYGDAVREIDDSVGKIL 271
Cdd:cd16022 103 --------------------DEAIDFIE-RRDKDKPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRIL 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 272 SLLQNLGISKNTFVFFTSDNGAALisapKEGGSNGpflcGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTS 351
Cdd:cd16022 149 DALEELGLLDNTLIVFTSDHGDML----GDHGLRG----KKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTL 220
|
330
....*....|....*...
gi 114145565 352 LSLAGLKPPSDrvIDGLD 369
Cdd:cd16022 221 LDLAGIEPPEG--LDGRS 236
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
32-357 |
3.47e-85 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 265.44 E-value: 3.47e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTnaharnaytp 111
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 112 qeIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKvkpnipvYRDWEMVGRF 191
Cdd:pfam00884 71 --TPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPP-------DVPYNCSGGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 192 YeefpinlktgeanLTQLYLQEALDFIRTQharQSPFFLYWAIDATHAPVYASKQFLGT------------SLRGRYGDA 259
Cdd:pfam00884 142 V-------------SDEALLDEALEFLDNN---DKPFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscseeQLLNSYDNT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 260 VREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapkeGGSNGPFLCGKQ-TTFEGGMREPAIAWWPGHIAAGQVS 338
Cdd:pfam00884 206 LLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESL------GEGGGYLHGGKYdNAPEGGYRVPLLIWSPGGKAKGQKS 279
|
330
....*....|....*....
gi 114145565 339 HQLGSIMDLFTTSLSLAGL 357
Cdd:pfam00884 280 EALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-394 |
7.93e-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: 7.93e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYsANPLCSPSRAALLTGRLPIRNG--FYTTNAharnay 109
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYvvFGYLDP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 110 tpqeimggipnSEHLLPELLKKAGYTNKIVGKWHLGHRPQF--HPLKHGFDEWfgspnCHFGPYDNKVKPNIPVYRDWEM 187
Cdd:cd16151 74 -----------KQKTFGHLLKDAGYATAIAGKWQLGGGRGDgdYPHEFGFDEY-----CLWQLTETGEKYSRPATPTFNI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 188 vgrfyeefpINLKTGEANLTQ----LYLQEALDFIRTQHARqsPFFLYWAIDATHAPV----------YASKQFlgTSLR 253
Cdd:cd16151 138 ---------RNGKLLETTEGDygpdLFADFLIDFIERNKDQ--PFFAYYPMVLVHDPFvptpdspdwdPDDKRK--KDDP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 254 GRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNG-AALISAPKEGGS-NGpflcGKQTTFEGGMREPAIAWWPGH 331
Cdd:cd16151 205 EYFPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGtHRPITSRTNGREvRG----GKGKTTDAGTHVPLIVNWPGL 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114145565 332 IAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTML--QGHIIDRPIFYYRGNTLMA 394
Cdd:cd16151 281 IPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLgkTGSPRREWIYWYYRNPHKK 345
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
30-412 |
1.16e-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: 238.88 E-value: 1.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 30 QPPNIVLLLMDDMGWGDLGVYGEPSReTPNLDRMAAEGMLFPSFYsANPLCSPSRAALLTGRLPIRNGF--YTTNAHARN 107
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEIP-TPNLDALAAEGLRFTNFH-TTALCSPTRAALLTGRNHHQVGMgtMAELATGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 108 AYTpqeimGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHrPQFHplkhgfdewfgspnchfgpydnkvkpnipvyrdwem 187
Cdd:cd16025 79 GYE-----GYLPDSAATIAEVLKDAGYHTYMSGKWHLGP-DDYY------------------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 188 vgrfyeefpinlktgeanLTQLYLQEALDFIRTQHARQSPFFLYWAIDATHAPVYASKQFLgTSLRGRYG---DAVRE-- 262
Cdd:cd16025 117 ------------------STDDLTDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWI-DKYKGKYDagwDALREer 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 263 --------------------------------------------------IDDSVGKILSLLQNLGISKNTFVFFTSDNG 292
Cdd:cd16025 178 lerqkelglipadtkltprppgvpawdslspeekklearrmevyaamvehMDQQIGRLIDYLKELGELDNTLIIFLSDNG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 293 AaliSApkEGG----SNGPFLCGKQTTFEGGMREPAIAWWPGHIAA-GQVSHQLGSIMDLFTTSLSLAGLKPPSDRV--- 364
Cdd:cd16025 258 A---SA--EPGwanaSNTPFRLYKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvp 332
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 114145565 365 ---IDGLDLLPTmLQG---HIIDRPIFYYR-GNTlmAVTLGQYKA---H-LWTWTNSWE 412
Cdd:cd16025 333 qlpLDGVSLLPT-LDGaaaPSRRRTQYFELfGNR--AIRKGGWKAvalHpPPGWGDQWE 388
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
32-372 |
6.91e-70 |
|
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: 228.16 E-value: 6.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWgDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAYTP 111
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNG--AHGLRSRGFPLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 112 QEImggipnseHLLPELLKKAGYTNKIVGKWHlghrpqfhplkHGFDEwfgspncHFGPYDNKVKPNIPVYRDWEMVGRF 191
Cdd:cd16027 78 DGV--------KTLPELLREAGYYTGLIGKTH-----------YNPDA-------VFPFDDEMRGPDDGGRNAWDYASNA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 192 YeefpinlktgeanltqlylqealDFIRTQHARQsPFFLYWAIDATHAP-VYASKQFLGTSLR----------------- 253
Cdd:cd16027 132 A-----------------------DFLNRAKKGQ-PFFLWFGFHDPHRPyPPGDGEEPGYDPEkvkvppylpdtpevred 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 254 -GRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapkeggsngPFlcGKQTTFEGGMREPAIAWWPGHI 332
Cdd:cd16027 188 lADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPF-----------PR--AKGTLYDSGLRVPLIVRWPGKI 254
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 114145565 333 AAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLP 372
Cdd:cd16027 255 KPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLP 292
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
30-388 |
8.96e-69 |
|
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: 227.03 E-value: 8.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 30 QPPNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGfYTTNAHarnay 109
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHG-VTDNNG----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 110 tpqeimGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPlkHGFDEWFGSP-NCHFGPYDNKvkpnipvyrdwEMV 188
Cdd:cd16031 75 ------PLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPP--PGFDYWVSFPgQGSYYDPEFI-----------ENG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 189 GRFYEEFPInlktgeanlTQLYLQEALDFIRTQHARQsPFFLYWAIDATHAP---------VYASKQF------------ 247
Cdd:cd16031 136 KRVGQKGYV---------TDIITDKALDFLKERDKDK-PFCLSLSFKAPHRPftpaprhrgLYEDVTIpepetfddddya 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 248 -----LGTSLRGRYGD--------------------AVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapkeg 302
Cdd:cd16031 206 grpewAREQRNRIRGVldgrfdtpekyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 303 GSNGpfLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPtMLQGHIID- 381
Cdd:cd16031 279 GEHG--LFDKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLP-LLEGEKPVd 353
|
....*...
gi 114145565 382 -RPIFYYR 388
Cdd:cd16031 354 wRKEFYYE 361
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-377 |
2.73e-63 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 211.66 E-value: 2.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHarnaytp 111
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 112 qeimggIPNSEHLLPELLKKAGYTNKIVGKWHL-GHRPQFH---------PLKHGFDEWFGSPNC--HFGPYDNKVKPNI 179
Cdd:cd16034 75 ------LPPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGraddytpppERRHGFDYWKGYECNhdHNNPHYYDDDGKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 180 PVYRDWEmvgrfyeefPInlktGEANLtqlylqeALDFIRTQHARQSPFFLYWAIDATHAPV----------YASKQ--- 246
Cdd:cd16034 149 IYIKGYS---------PD----AETDL-------AIEYLENQADKDKPFALVLSWNPPHDPYttapeeyldmYDPKKlll 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 247 ------------FLGTSLRGRYGdAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapkegGSNGpfLCGKQT 314
Cdd:cd16034 209 rpnvpedkkeeaGLREDLRGYYA-MITALDDNIGRLLDALKELGLLENTIVVFTSDHGDML-------GSHG--LMNKQV 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114145565 315 TFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPTMLQG 377
Cdd:cd16034 279 PYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGG 339
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-372 |
3.95e-55 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 185.91 E-value: 3.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNG---FYTTNAHARnA 108
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGihdWIVEGSHGK-T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 109 YTPQEIMGGIPnsehLLPELLKKAGYTNKIVGKWHLGhrpqfhplkhgfdewfgspnchfgpydnkvkpnipvyrdwemv 188
Cdd:cd16149 80 KKPEGYLEGQT----TLPEVLQDAGYRCGLSGKWHLG------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 189 grfyeefpinlktgeanltqlylQEALDFIRTQHARQSPFFLYWAIDATHAP--VYAskqflgtslrgrygdAVREIDDS 266
Cdd:cd16149 113 -----------------------DDAADFLRRRAEAEKPFFLSVNYTAPHSPwgYFA---------------AVTGVDRN 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 267 VGKILSLLQNLGISKNTFVFFTSDNGAALISAPKEGGSNGPFlcgKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMD 346
Cdd:cd16149 155 VGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKGNGTF---PLNMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYD 231
|
330 340
....*....|....*....|....*.
gi 114145565 347 LFTTSLSLAGLKPPSDRVIDGLDLLP 372
Cdd:cd16149 232 FFPTLLELAGVDPPADPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-401 |
2.77e-52 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 180.43 E-value: 2.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTtNAHArnaytp 111
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWD-NADP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 112 qeIMGGIPNSEHLLPEllkkAGYTNKIVGKWHLGHRPQFHplkhGFDewfgspnchfgpYDNKVkpnipvyrdwemvgrf 191
Cdd:cd16037 74 --YDGDVPSWGHALRA----AGYETVLIGKLHFRGEDQRH----GFR------------YDRDV---------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 192 yeefpinlktgeanltqlyLQEALDFIRTQHARQSPFFLYWAIDATHAPVYASKQFLG----TSLRGRYGdAVREIDDSV 267
Cdd:cd16037 116 -------------------TEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDlyvrRARAAYYG-LVEFLDENI 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 268 GKILSLLQNLGISKNTFVFFTSDNGAALisapkegGSNGpfLCGKQTTFEGGMREPAIAWWPGhIAAGQVSHQLGSIMDL 347
Cdd:cd16037 176 GRVLDALEELGLLDNTLIIYTSDHGDML-------GERG--LWGKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDL 245
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 114145565 348 FTTSLSLAGLKPPSDRviDGLDLLPTMLQGHIIDRPIF--YYRGNTLMA---VTLGQYK 401
Cdd:cd16037 246 APTILEAAGAPPPPDL--DGRSLLPLAEGPDDPDRVVFseYHAHGSPSGafmLRKGRWK 302
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-401 |
1.91e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 180.88 E-value: 1.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTtnaharNAYTP 111
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLN------NVENA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 112 QEIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGhrPQFHPLKHGFDEWFgsPNCHFGPYDnkvkpnipvyrdwemvgrf 191
Cdd:cd16033 75 GAYSRGLPPGVETFSEDLREAGYRNGYVGKWHVG--PEETPLDYGFDEYL--PVETTIEYF------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 192 yeefpinlktgeanltqlYLQEALDFIRTQHARQSPFFLYWAIDATHAPVYASKQFLG---------------------- 249
Cdd:cd16033 132 ------------------LADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDmydpediplpesfaddfedkpy 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 250 ----TSLRG---------------RYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALISapkEGGSN-GPFL 309
Cdd:cd16033 194 iyrrERKRWgvdtedeedwkeiiaHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGA---HRLWDkGPFM 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 310 cgkqttFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPTMLQGHIIDRPI----- 384
Cdd:cd16033 271 ------YEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK--VDGRSLLPLLRGEQPEDWRDevvte 342
|
410
....*....|....*....
gi 114145565 385 FYYRGNTLM--AVTLGQYK 401
Cdd:cd16033 343 YNGHEFYLPqrMVRTDRYK 361
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
32-355 |
2.68e-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: 167.21 E-value: 2.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFpSFYSANPLCS--PSRAALLTGRLPIRNGFYTTNAHARnay 109
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATF-NFRSVSPPTSsaPNHAALLTGAYPTLHGYTGNGSADP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 110 TPQEIMGGIPNSEHLLPELLKKAGYTNKIVGkwhlghrpqfhplkhgfdewfgspnchfgpydnkvkpnipvyrdwemvg 189
Cdd:cd00016 77 ELPSRAAGKDEDGPTIPELLKQAGYRTGVIG------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 190 rfyeefpinlktgeanltqlylqeALDFIrTQHARQSPFFLYWAIDATHAPVYASkqflgTSLRGRYGDAVREIDDSVGK 269
Cdd:cd00016 108 ------------------------LLKAI-DETSKEKPFVLFLHFDGPDGPGHAY-----GPNTPEYYDAVEEIDERIGK 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 270 ILSLLQNLGISKNTFVFFTSDNGAALisapkEGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIaAGQVSHQLGSIMDLFT 349
Cdd:cd00016 158 VLDALKKAGDADDTVIIVTADHGGID-----KGHGGDPKADGKADKSHTGMRVPFIAYGPGVK-KGGVKHELISQYDIAP 231
|
....*.
gi 114145565 350 TSLSLA 355
Cdd:cd00016 232 TLADLL 237
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-467 |
5.30e-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: 162.35 E-value: 5.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANP----LCSPSRAALLTGrlpiRNGFYTTNAHARN 107
Cdd:cd16155 3 PNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGwsgaVCVPSRAMLMTG----RTLFHAPEGGKAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 108 aytpqeimggIPNSEHLLPELLKKAGYTNKIVGKWHLGHrpqfhplkhgfdewfgspnchfgpydnkvkpnipvyrdwem 187
Cdd:cd16155 79 ----------IPSDDKTWPETFKKAGYRTFATGKWHNGF----------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 188 vgrfyeefpinlktgeANltqlylqEALDFIRTQHARQSPFFLYWAIDATHAPVYASKQFLgtslrGRYG---------- 257
Cdd:cd16155 108 ----------------AD-------AAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYL-----DMYPpetiplpenf 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 258 -------------------------DAVRE-----------IDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapke 301
Cdd:cd16155 160 lpqhpfdngegtvrdeqlapfprtpEAVRQhlaeyyamithLDAQIGRILDALEASGELDNTIIVFTSDHGLAV------ 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 302 gGSNGpfLCGKQTTFEGGMREPAIAWWPGhIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPtMLQG---H 378
Cdd:cd16155 234 -GSHG--LMGKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES--VEGKSLLP-VIRGekkA 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 379 IIDRPIFYYRGNTLMAVTlGQYKahlwtwtnsweefrqGIDFCPGQNvsgvtthtqeeHTELpliFHLGRDPGERFPLrF 458
Cdd:cd16155 307 VRDTLYGAYRDGQRAIRD-DRWK---------------LIIYVPGVK-----------RTQL---FDLKKDPDELNNL-A 355
|
....*....
gi 114145565 459 TSNEYQDAL 467
Cdd:cd16155 356 DEPEYQERL 364
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
30-397 |
2.16e-43 |
|
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: 159.66 E-value: 2.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 30 QPPNIVLLLMDDMG-WgdLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARna 108
Cdd:cd16030 1 KKPNVLFIAVDDLRpW--LGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 109 ytpqEIMGGIPnsehLLPELLKKAGYTNKIVGK-WHlGHRPQFHPLKHGFDEWFGSPncHFGPYDNKVKPNIPVYRDWEM 187
Cdd:cd16030 77 ----KVAPDAV----TLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPP--GPEKYPPGKLCPGKKGGKGGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 188 VGRFYEEFPInlkTGEANLTQLYLQEALDFIRTQHARQSPFFL----------------YW------------AIDATHA 239
Cdd:cd16030 146 GGPAWEAADV---PDEAYPDGKVADEAIEQLRKLKDSDKPFFLavgfykphlpfvapkkYFdlyplesiplpnPFDPIDL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 240 PVYASKQFlgTSLRGRYGD--------------------------AVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGA 293
Cdd:cd16030 223 PEVAWNDL--DDLPKYGDIpalnpgdpkgplpdeqarelrqayyaSVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 294 ALisapkegGSNGPFlcGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPT 373
Cdd:cd16030 301 HL-------GEHGHW--GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPPC--LEGKSLVPL 369
|
410 420
....*....|....*....|....*.
gi 114145565 374 MLQ-GHIIDRPIF-YYRGNTLMAVTL 397
Cdd:cd16030 370 LKNpSAKWKDAAFsQYPRPSIMGYSI 395
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
31-414 |
2.60e-41 |
|
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: 152.70 E-value: 2.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 31 PPNIVLLLMDDMGWGDLGVYGEPsretPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFyTTNAHARNAYT 110
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMP----KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGV-TNNSPPGGGYP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 111 PQEIMGGIPNSehlLPELLKKAGYTNKIVGK----WHLGHRPQFHPLkhGFDEWFGSpnchFGPYdnkvkpnipVYRDWE 186
Cdd:cd16147 76 KFWQNGLERST---LPVWLQEAGYRTAYAGKylngYGVPGGVSYVPP--GWDEWDGL----VGNS---------TYYNYT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 187 MVGRFYEEFPINLKtgEANLTQLYLQEALDFIRTQHARQSPFFLYWAIDATHAPVYASKQ----FLGTSLRGR------- 255
Cdd:cd16147 138 LSNGGNGKHGVSYP--GDYLTDVIANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRyanlFPNVTAPPRpppnnpd 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 256 --------------------YGD--------AVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapkegGSNG- 306
Cdd:cd16147 216 vsdkphwlrrlpplnptqiaYIDelyrkrlrTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHL-------GQHRl 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 307 PFlcGKQTTFEGGMREPAIAWWPGhIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGldllptmlqghiidRPIFY 386
Cdd:cd16147 289 PP--GKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDG--------------RSCGD 349
|
410 420 430
....*....|....*....|....*....|
gi 114145565 387 YRGNTLMAV-TLGQYKAHLWT-WTNSWEEF 414
Cdd:cd16147 350 SNNNTYKCVrTVDDTYNLLYFeWCTGFREL 379
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-372 |
9.44e-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: 9.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMD----DMgwgdLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYttnaharn 107
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 108 aytpqeiMGGIPNSEHLLPELLKKAGYTNKIVGKW-HLGHRPQFHplkHGFDEWfgspncHFGPYDNKVKPNIPVYRDWE 186
Cdd:cd16148 69 -------GGPLEPDDPTLAEILRKAGYYTAAVSSNpHLFGGPGFD---RGFDTF------EDFRGQEGDPGEEGDERAER 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 187 MVgrfyeefpinlktgeanltqlylQEALDFIRtQHARQSPFFLYWAIDATHAPvYaskqflgtslrgRYGDAVREIDDS 266
Cdd:cd16148 133 VT-----------------------DRALEWLD-RNADDDPFFLFLHYFDPHEP-Y------------LYDAEVRYVDEQ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 267 VGKILSLLQNLGISKNTFVFFTSDNGAALisapkegGSNGpFLCGKQTTF-EGGMREPAIAWWPGHIAAGQVSHQLGSIm 345
Cdd:cd16148 176 IGRLLDKLKELGLLEDTLVIVTSDHGEEF-------GEHG-LYWGHGSNLyDEQLHVPLIIRWPGKEPGKRVDALVSHI- 246
|
330 340
....*....|....*....|....*..
gi 114145565 346 DLFTTSLSLAGLKPPSDrvIDGLDLLP 372
Cdd:cd16148 247 DIAPTLLDLLGVEPPDY--SDGRSLLP 271
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
382-510 |
5.39e-39 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 138.21 E-value: 5.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 382 RPIFYYRGNTLMAVTLGQYKAHLWTwtNSWeeFRQGIDFCPGQNVsgvtthtQEEHTELPLIFHLGRDPGERFPLRFTSN 461
Cdd:pfam14707 4 EFLFHYCGAALHAVRWGPYKAHFFT--PSF--DPPGAEGCYGSKV-------PVTHHDPPLLFDLERDPSEKYPLSPDSP 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 114145565 462 EYQDALSRTTQVIQQHQKSLVPGQPQLNVCNQAVMNWAPPGCEKLGKCL 510
Cdd:pfam14707 73 EYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACT 121
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
32-383 |
7.95e-39 |
|
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: 144.26 E-value: 7.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYtTNAharnaytp 111
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAY-DNA-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 112 QEIMGGIPNSEHllpeLLKKAGYTNKIVGKWHL-GhrPQFHplkHGFDewfgspnchfgpYDNKVkpnipVYRdwemvgr 190
Cdd:cd16032 72 AEFPADIPTFAH----YLRAAGYRTALSGKMHFvG--PDQL---HGFD------------YDEEV-----AFK------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 191 fyeefpinlktgeanltqlylqeALDFIRtQHARQS---PFFLYWAIDATHAPVYASKQFLG----TSLRGRYGdAVREI 263
Cdd:cd16032 119 -----------------------AVQKLY-DLARGEdgrPFFLTVSFTHPHDPYVIPQEYWDlyvrRARRAYYG-MVSYV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 264 DDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapkegGSNGpfLCGKQTTFEGGMREPAIAWWPGHIAAGQVShQLGS 343
Cdd:cd16032 174 DDKVGQLLDTLERTGLADDTIVIFTSDHGDML-------GERG--LWYKMSFFEGSARVPLIISAPGRFAPRRVA-EPVS 243
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 114145565 344 IMDLFTTSLSLAGLKPPSDRV-IDGLDLLPtMLQGHIIDRP 383
Cdd:cd16032 244 LVDLLPTLVDLAGGGTAPHVPpLDGRSLLP-LLEGGDSGGE 283
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-383 |
2.93e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 143.91 E-value: 2.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 31 PPNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYttnahaRNAyt 110
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCF------RNG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 111 pqeimGGIPNSEHLLPELLKKAGYTNKIVGKWHL-GHRPQFhplkhgfdewfgspnchfgpydnkvkpnipvyrdwemvg 189
Cdd:cd16152 73 -----IPLPADEKTLAHYFRDAGYETGYVGKWHLaGYRVDA--------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 190 rfyeefpinlktgeanLTQLylqeALDFIRtQHARQSPFFLYWA---------IDATHAPVYASKQFLGTS----LRGRY 256
Cdd:cd16152 109 ----------------LTDF----AIDYLD-NRQKDKPFFLFLSylephhqndRDRYVAPEGSAERFANFWvppdLAALP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 257 GDA----------VREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALISAPKEggsngpflcGKQTTFEGGMREPAIA 326
Cdd:cd16152 168 GDWaeelpdylgcCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCHFRTRNAE---------YKRSCHESSIRVPLVI 238
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 114145565 327 WWPGhIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPtMLQGHIIDRP 383
Cdd:cd16152 239 YGPG-FNGGGRVEELVSLIDLPPTLLDAAGIDVPEE--MQGRSLLP-LVDGKVEDWR 291
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
28-477 |
1.91e-37 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 144.04 E-value: 1.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 28 APQPPNIVLLLMDDMGwGD-LGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHAR 106
Cdd:PRK13759 3 QTKKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 107 NAYTpqeimggipnseHLLPELLKKAGYTNKIVGKWHlghrpqFHP--LKHGFDE-WFGSPNCHFG-PYDNKVKPNIPVY 182
Cdd:PRK13759 82 WNYK------------NTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHNvLLHDGYLHSGrNEDKSQFDFVSDY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 183 RDW---EMVGRFYEEFPINLK---------TGEANL--TQLYLQEALDFIRTQHARQsPFFLYWAIDATHAPVYASKQFL 248
Cdd:PRK13759 144 LAWlreKAPGKDPDLTDIGWDcnswvarpwDLEERLhpTNWVGSESIEFLRRRDPTK-PFFLKMSFARPHSPYDPPKRYF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 249 G----------------------------TSLRGRYGDA------------VREIDDSVGKILSLLQNLGISKNTFVFFT 288
Cdd:PRK13759 223 DmykdadipdphigdweyaedqdpeggsiDALRGNLGEEyarraraayyglITHIDHQIGRFLQALKEFGLLDNTIILFV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 289 SDNGAALisapkegGSNGPFLcgKQTTFEGGMREPAIAWWPGHI---AAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvI 365
Cdd:PRK13759 303 SDHGDML-------GDHYLFR--KGYPYEGSAHIPFIIYDPGGLlagNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--V 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 366 DGLDLLPtmlqghiidrpifyyrgntlmaVTLGQYKAhlwtwtnsWEEFRQGIDFCPGQNVSGVTT-------HTQEEHT 438
Cdd:PRK13759 372 DGRSLKN----------------------LIFGQYEG--------WRPYLHGEHALGYSSDNYLTDgkwkyiwFSQTGEE 421
|
490 500 510
....*....|....*....|....*....|....*....
gi 114145565 439 ELpliFHLGRDPGERFPLrFTSNEYQDALSRTTQVIQQH 477
Cdd:PRK13759 422 QL---FDLKKDPHELHNL-SPSEKYQPRLREMRKKLVDH 456
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-370 |
2.34e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 133.65 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEP------SR----ETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTt 101
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNAhtgkseSRlgyvESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 102 naharNAYTPQEIMGGIPnsehLLPELLKKAGYTNKIVGKWHLGhrpqfhplkhGFDEWFGSPNCHFGPYDNKVKPNIpv 181
Cdd:cd16153 81 -----FEAAHPALDHGLP----TFPEVLKKAGYQTASFGKSHLE----------AFQRYLKNANQSYKSFWGKIAKGA-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 182 yrdwemvgrfyeefpinlktgeanltqlylqealdfirtqhARQSPFFLYWAIDATHAPVYASKQFLGtslRGRYGDAVR 261
Cdd:cd16153 140 -----------------------------------------DSDKPFFVRLSFLQPHTPVLPPKEFRD---RFDYYAFCA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 262 EIDDSVGKILSLLQNLGISK---NTFVFFTSDNGAALisapkegGSNGpfLCGKQTTFEGGMREPAIAWWPGHIA--AGQ 336
Cdd:cd16153 176 YGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHL-------GEQG--ILAKFTFWPQSHRVPLIVVSSDKLKapAGK 246
|
330 340 350
....*....|....*....|....*....|....
gi 114145565 337 VSHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDL 370
Cdd:cd16153 247 VRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-401 |
5.75e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 134.78 E-value: 5.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSR--ETPNLDRMAAEGMLFPSFYsANPLCSPSRAALLTGRLPIRNGFYTTNaharnay 109
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFDNLW-ATPACSPTRATILTGKYGFRTGVLAVP------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 110 tpqeimGGIPNSEHLLPELLKK----AGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSpnchfgpydnkVKPNIPVYRDW 185
Cdd:cd16154 73 ------DELLLSEETLLQLLIKdattAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGI-----------LGGGVQDYYNW 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 186 EMVgrfyeefpINLKTGEAN------LTQLylqeALDFIRTQHarqSPFFLYWAIDATHAPVYA------SKQFLGTSL- 252
Cdd:cd16154 136 NLT--------NNGQTTNSTeyattkLTNL----AIDWIDQQT---KPWFLWLAYNAPHTPFHLppaelhSRSLLGDSAd 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 253 -----RGRYGDAVREIDDSVGKIL-SLLQNlgISKNTFVFFTSDNGAALISAPKEGGSNGpflcGKQTTFEGGMREPAIA 326
Cdd:cd16154 201 ieanpRPYYLAAIEAMDTEIGRLLaSIDEE--ERENTIIIFIGDNGTPGQVVDLPYTRNH----AKGSLYEGGINVPLIV 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114145565 327 WWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSdrVIDGLDLLPTMLQGHIIDRPI---FYYRGNTLMAVTLGQYK 401
Cdd:cd16154 275 SGAGVERANERESALVNATDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNASTRQYnytEYESPTTTGWATRNQYY 350
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
32-385 |
7.35e-27 |
|
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: 113.25 E-value: 7.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTN-AHARNAYT 110
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCmALGDNVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 111 pqeiMGgipnsehllpELLKKAGYTNKIVGKWHL-GHrpqfhplkhgfdEWFGSPNCHFGpYDnkvkpniPVYrdWEMVG 189
Cdd:cd16156 81 ----IG----------QRLSDNGIHTAYIGKWHLdGG------------DYFGNGICPQG-WD-------PDY--WYDMR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 190 RFYEEFP---INLKTGEANLTQLY------------LQEALDFIRtQHARQsPFFLYWAIDATHAPV-----YAS--KQF 247
Cdd:cd16156 125 NYLDELTeeeRRKSRRGLTSLEAEgikeeftyghrcTNRALDFIE-KHKDE-DFFLVVSYDEPHHPFlcpkpYASmyKDF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 248 ---LGTSL---------------RGRYGDAVRE--------------IDDSVGKILSLLQNLGisKNTFVFFTSDNGAAL 295
Cdd:cd16156 203 efpKGENAyddlenkplhqrlwaGAKPHEDGDKgtikhplyfgcnsfVDYEIGRVLDAADEIA--EDAWVIYTSDHGDML 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 296 isapkegGSNGPFLCGKqTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPsdRVIDGLDLLPTML 375
Cdd:cd16156 281 -------GAHKLWAKGP-AVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQP--KVLEGESILATIE 350
|
410
....*....|.
gi 114145565 376 QGHI-IDRPIF 385
Cdd:cd16156 351 DPEIpENRGVF 361
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
35-379 |
3.26e-23 |
|
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: 102.34 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 35 VLLLMDDMGWGD-LGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGfyttnaHARNAyTPqe 113
Cdd:cd16028 3 VLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHR------SVWNG-TP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 114 imggIPNSEHLLPELLKKAGYTNKIVGKWH----LGHRPQFHPLKH-------GFDewfgsPNCHFGPY----------- 171
Cdd:cd16028 74 ----LDARHLTLALELRKAGYDPALFGYTDtspdPRGLAPLDPRLLsyelampGFD-----PVDRLDEYpaedsdtaflt 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 172 -----DNKVKPNipvyRDWEMVGRFYEEFPINLKTGEANLtqLY-LQEALDFIR----TQHARQSPFFLYW-------AI 234
Cdd:cd16028 145 draieYLDERQD----EPWFLHLSYIRPHPPFVAPAPYHA--LYdPADVPPPIRaeslAAEAAQHPLLAAFlerieslSF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 235 DATHAPVYASKQFLGTSLRGRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapkegGSNgpFLCGKQT 314
Cdd:cd16028 219 SPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQL-------GDH--WLWGKDG 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114145565 315 TFEGGMREPAIAWWPG---HIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPtMLQGHI 379
Cdd:cd16028 290 FFDQAYRVPLIVRDPRreaDATRGQVVDAFTESVDVMPTILDWLGGEIPHQ--CDGRSLLP-LLAGAQ 354
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-360 |
7.56e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 100.77 E-value: 7.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARnaytP 111
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLR----P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 112 QEimggiPNsehlLPELLKKAGYTNKIVGKWHLghrpqfhpLKHGFDewfgspnchFGPYdnkvkpnipVYRDWEMVgrf 191
Cdd:cd16150 77 DE-----PN----LLKTLKDAGYHVAWAGKNDD--------LPGEFA---------AEAY---------CDSDEACV--- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 192 yeefpinlktgeanltqlylQEALDFIRtQHARQSPFFLYWAIDATHAPV-----YAS------------------KQFL 248
Cdd:cd16150 119 --------------------RTAIDWLR-NRRPDKPFCLYLPLIFPHPPYgveepWFSmidreklpprrppglrakGKPS 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 249 GTSLRGRYG------DAVREI-----------DDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapkegGSNGpfLCG 311
Cdd:cd16150 178 MLEGIEKQGldrwseERWRELratylgmvsrlDHQFGRLLEALKETGLYDDTAVFFFSDHGDYT-------GDYG--LVE 248
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 114145565 312 K-QTTFEGGM-REPAIAWWPGhIAAGQVSHQLGSIMDLFTTSLSLAGLKPP 360
Cdd:cd16150 249 KwPNTFEDCLtRVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAGIPLS 298
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-377 |
7.55e-19 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 87.26 E-value: 7.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNG-FYTTNAHARNAYT 110
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGvTDTLGSPMQPLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 111 PQeimggIPNSEHllpeLLKKAGYTNKIVGKWHLGhrpqfhplkhgfdewfGSPNchfGPYDnkvkpnipvyRDwemvgr 190
Cdd:cd16035 81 PD-----VPTLGH----MLRAAGYYTAYKGKWHLS----------------GAAG---GGYK----------RD------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 191 fyeefpinlktgeanltQLYLQEALDFIRTQHAR---QSPFFL-----------YWAIDAThAPVYaskqflgtsLRGRY 256
Cdd:cd16035 117 -----------------PGIAAQAVEWLRERGAKnadGKPWFLvvslvnphdimFPPDDEE-RWRR---------FRNFY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 257 GDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGaalisapkE-GGSNGpflcGKQ---TTFEGGMREPAIAWWPGHI 332
Cdd:cd16035 170 YNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG--------EmGGAHG----LRGkgfNAYEEALHVPLIISHPDLF 237
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 114145565 333 AAGQVSHQLGSIMDLFTTSLSLAGLKPPSDRVID----GLDLLPTMLQG 377
Cdd:cd16035 238 GTGQTTDALTSHIDLLPTLLGLAGVDAEARATEApplpGRDLSPLLTDA 286
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
32-450 |
6.63e-17 |
|
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: 82.20 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGwGDLGVYGEPSR-ETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGrlpirngFYTTNAHARNAYT 110
Cdd:cd16171 1 PNVVMVMSDSFD-GRLTFRPGNQVvDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG-------LFTHLTESWNNYK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 111 pqeimgGIPNSEHLLPELLKKAGYTNKIVGKwhLGHRPQFHPLKHGFDEWfgspnchfgpydnkvkpnipvYRDWEMVGR 190
Cdd:cd16171 73 ------GLDPNYPTWMDRLEKHGYHTQKYGK--LDYTSGHHSVSNRVEAW---------------------TRDVPFLLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 191 fYEEFPINLKTGEANLTQLYLQE------ALDFIRTQHARQS-PFFLYWAIDATH---APvYASKQFLGT-SLRGRYGDA 259
Cdd:cd16171 124 -QEGRPTVNLVGDRSTVRVMLKDwqntdkAVHWIRKEAPNLTqPFALYLGLNLPHpypSP-SMGENFGSIrNIRAFYYAM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 260 VREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALISAPKeggsngpFLcgKQTTFEGGMREPAIAWWPGhIAAGQVSH 339
Cdd:cd16171 202 CAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQ-------FY--KMSMYEGSSHVPLLIMGPG-IKAGQQVS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 340 QLGSIMDLFTTSLSLAGLKPPSDrvIDGLDLLPTMLQGHIIDRPIFYYRGNTLMA------VTLGQYKahlwTWTNSWEE 413
Cdd:cd16171 272 DVVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLLSESSIKESPSRVPHPDWVLSefhgcnVNASTYM----LRTNSWKY 345
|
410 420 430
....*....|....*....|....*....|....*..
gi 114145565 414 frqgIDFCPGQNVSgvtthtqeehtelPLIFHLGRDP 450
Cdd:cd16171 346 ----IAYADGNSVP-------------PQLFDLSKDP 365
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
32-356 |
1.89e-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: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDdmGWGDLGVYGEPSRE--TPNLDRMAAEGMLFPSFYSANPLCSPSRA--ALLTGRLPIRNGFYTTNAHARN 107
Cdd:cd16015 1 PNVIVILLE--SFSDPYIDKDVGGEdlTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 108 AYtpqeimggipNSehlLPELLKKAGYTNKIVgkwHLGH-----RPQFHPlKHGFDEWFGspnCHFGPYDNKVKPNIPVY 182
Cdd:cd16015 79 PL----------PS---LPSILKEQGYETIFI---HGGDasfynRDSVYP-NLGFDEFYD---LEDFPDDEKETNGWGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 183 rDWEMVGRFYEEFpinlktgeanltqlylqealdfirtQHARQSPFFLY---------WAIDATHAPVYASKQFLGTSLr 253
Cdd:cd16015 139 -DESLFDQALEEL-------------------------EELKKKPFFIFlvtmsnhgpYDLPEEKKDEPLKVEEDKTEL- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 254 GRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALISAPKEGGSNgpflcgkqttFEGGMREPAIAWWPGhIA 333
Cdd:cd16015 192 ENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDED----------PLDLYRTPLLIYSPG-LK 260
|
330 340
....*....|....*....|...
gi 114145565 334 AGQVSHQLGSIMDLFTTSLSLAG 356
Cdd:cd16015 261 KPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
25-371 |
1.37e-15 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 79.70 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 25 AAGAPQPPNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGrLPIRNGFYTTNAH 104
Cdd:COG1368 228 PFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTG-LPPLPGGSPYKRP 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 105 ARNAYtpqeimggipNSehlLPELLKKAGYTNKIV--GKWHLGHRPQFHPlKHGFDEWFGSPNchfgpYDNKVKPNIPVY 182
Cdd:COG1368 307 GQNNF----------PS---LPSILKKQGYETSFFhgGDGSFWNRDSFYK-NLGFDEFYDRED-----FDDPFDGGWGVS 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 183 rDWEMvgrfyeefpinlktgeanltqlyLQEALDFIRTQharQSPFFLY---------WAIDATHAPVYAskqfLGTSLR 253
Cdd:COG1368 368 -DEDL-----------------------FDKALEELEKL---KKPFFAFlitlsnhgpYTLPEEDKKIPD----YGKTTL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 254 GRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALisapkEGGSNGPFLCGKQTTfeggmrePAIaWWPGHIA 333
Cdd:COG1368 417 NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRS-----PGKTDYENPLERYRV-------PLL-IYSPGLK 483
|
330 340 350
....*....|....*....|....*....|....*...
gi 114145565 334 AGQVSHQLGSIMDLFTTSLSLAGLKPPSDRVIdGLDLL 371
Cdd:COG1368 484 KPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
13-292 |
7.82e-12 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 66.70 E-value: 7.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 13 LLLPvlSALGLLAAGAPQPPNIVLLLMDDMGWGDLGvygepSRETPNLDRMAAEGMLFPSFYSANPlcS---PSRAALLT 89
Cdd:COG1524 7 LLLA--SLLAAAAAAAPPAKKVVLILVDGLRADLLE-----RAHAPNLAALAARGVYARPLTSVFP--SttaPAHTTLLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 90 GRLPIR-----NGFYTTNAHARNAYTPQEIMGGIPNSEHLLP---ELLKKAGYTNKIVGKWHLGHRPQFHplkHGFDEWF 161
Cdd:COG1524 78 GLYPGEhgivgNGWYDPELGRVVNSLSWVEDGFGSNSLLPVPtifERARAAGLTTAAVFWPSFEGSGLID---AARPYPY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 162 GSPNCHFGPYDNKVKpnipVYRDWEMVgrfyeefpinLKTGEANLTQLYLQEaLDFIRTQHARQSPfflywaidathapv 241
Cdd:COG1524 155 DGRKPLLGNPAADRW----IAAAALEL----------LREGRPDLLLVYLPD-LDYAGHRYGPDSP-------------- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 114145565 242 yaskqflgtslrgRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNG 292
Cdd:COG1524 206 -------------EYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
35-297 |
7.34e-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: 60.51 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 35 VLLLMDDMGWGDLgvygEPSRETPNLDRMAAEG----MLFPSFysaNPLCSPSRAALLTGRLPIRNGFYttnaharnayt 110
Cdd:pfam01663 2 LVISLDGFRADYL----DRFELTPNLAALAKEGvsapNLTPVF---PTLTFPNHYTLVTGLYPGSHGIV----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 111 pqeimggipNSEHLLPELLKKAGY--TNKIVGKWHLGHRPQFHPLKHGFdewfgSPNCHFGPYDNKVKPNIPVYRDWEMV 188
Cdd:pfam01663 64 ---------GNTFYDPKTGEYLVFviSDPEDPRWWQGEPIWDTAAKAGV-----RAAALFWPGSEVDYSTYYGTPPRYLK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 189 GRFYEEFPinlktGEANLTQLYLQEALDFIRTQHARQSPFFLYW---AIDAT-HAPVYASKQFLgtslrgrygDAVREID 264
Cdd:pfam01663 130 DDYNNSVP-----FEDRVDTAVLQTWLDLPFADVAAERPDLLLVyleEPDYAgHRYGPDSPEVE---------DALRRVD 195
|
250 260 270
....*....|....*....|....*....|...
gi 114145565 265 DSVGKILSLLQNLGISKNTFVFFTSDNGAALIS 297
Cdd:pfam01663 196 RAIGDLLEALDERGLFEDTNVIVVSDHGMTPVS 228
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
32-292 |
9.94e-07 |
|
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: 50.28 E-value: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 32 PNIVLLLMDDMGWGDLgvygEPSRETPNLDRMAAEGMLFPSFYSANP-LCSPSRAALLTGRLPIR-----NGFY--TTNA 103
Cdd:cd16018 1 PPLIVISIDGFRWDYL----DRAGLTPNLKRLAEEGVRAKYVKPVFPtLTFPNHYSIVTGLYPEShgivgNYFYdpKTNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 104 --HARNAYTPQEIMGGIPnsehlLPELLKKAGYTnkiVGKWHlghrpqfhplkhgfdeWFGSPNCHFGPYdnkvkpNIPV 181
Cdd:cd16018 77 efSDSDWVWDPWWIGGEP-----IWVTAEKAGLK---TASYF----------------WPGSEVAIIGYN------PTPI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145565 182 YRDWeMVGRFYEEFPInlktgeanltqlylQEALDFIRTQHARQSPFFLYW---AIDAT---HAPVyaSKQFLgtslrgr 255
Cdd:cd16018 127 PLGG-YWQPYNDSFPF--------------EERVDTILEWLDLERPDLILLyfeEPDSAghkYGPD--SPEVN------- 182
|
250 260 270
....*....|....*....|....*....|....*..
gi 114145565 256 ygDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNG 292
Cdd:cd16018 183 --EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG 217
|
|
| |
