|
Name |
Accession |
Description |
Interval |
E-value |
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
35-469 |
0e+00 |
|
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.
Pssm-ID: 293780 [Multi-domain] Cd Length: 383 Bit Score: 598.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDMGWGDLGANWAETKDTT-NLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGG 113
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAILTpNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 114 LPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDmgctdapgynyppcpacpqrdglwrnpgr 193
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 194 dcytdvalplyenlniveqpvnlSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQS-LYRAS 272
Cdd:cd16161 132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRgPYGDA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 273 LREMDSLVGQIKDKVDHV-ARENTLLWFTGDNGPWAQKCELAgsVGPFFGLWQTHQGGSPTKQTTWEGGHRVPALAYWPG 351
Cdd:cd16161 189 LQEMDDLVGQIMDAVKHAgLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 352 RVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGeYGALQTVRLNHYKAF 431
Cdd:cd16161 267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAH 345
|
410 420 430
....*....|....*....|....*....|....*...
gi 1039738450 432 YITGGAKACDGSVGPEQHHVAPLIFNLEDAADEGMPLQ 469
Cdd:cd16161 346 YATGGALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT 383
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-465 |
6.95e-173 |
|
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: 493.23 E-value: 6.95e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGG 113
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 114 LPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDMGCTDAPGYNYPPCPAcpqrdglwrnpgr 193
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 194 dcytdvalPLYENLNIVEQPVNLSGLAQKYAERAVEFIEQAstSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLYRASL 273
Cdd:cd16026 148 --------PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 274 REMDSLVGQIKDKVDHV-ARENTLLWFTGDNGPWAQKCELAGSVGPFfglwqthQGGsptKQTTWEGGHRVPALAYWPGR 352
Cdd:cd16026 218 EELDWSVGRILDALKELgLEENTLVIFTSDNGPWLEYGGHGGSAGPL-------RGG---KGTTWEGGVRVPFIAWWPGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 353 VPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGaageyGALQTVRLNHYKAFY 432
Cdd:cd16026 288 IPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDG-----GDLQAVRSGRWKLHL 362
|
410 420 430
....*....|....*....|....*....|...
gi 1039738450 433 ITGGAKACDGSVGPEQHHVAPLIFNLEDaaDEG 465
Cdd:cd16026 363 PTTYRTGTDPGGLDPTKLEPPLLYDLEE--DPG 393
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
36-522 |
1.14e-114 |
|
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: 347.90 E-value: 1.14e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGGL 114
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGvFYPGSRGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 115 PVNETTLAEVLRQEGYVTAMIGKWHL--GHHGSYHPNFRGFDYYFGIPYSNDMGctdaPGYN---YPPCPACpqrDGLWR 189
Cdd:cd16158 82 PLNETTIAEVLKTVGYQTAMVGKWHLgvGLNGTYLPTHQGFDHYLGIPYSHDQG----PCQNltcFPPNIPC---FGGCD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 190 nPGrdcytDVALPLYENLNIVEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLY 269
Cdd:cd16158 155 -QG-----EVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 270 RASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGPWAQKCELAGSVgpffGLWQTHQGgsptkqTTWEGGHRVPALAY 348
Cdd:cd16158 229 GDALAELDGSVGELLQTLKENGiDNNTLVFFTSDNGPSTMRKSRGGNA----GLLKCGKG------TTYEGGVREPAIAY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 349 WPGRVPANVTStALLSLLDIFPTVIALAGASLpPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGEYGALqTVRLNHY 428
Cdd:cd16158 299 WPGRIKPGVTH-ELASTLDILPTIAKLAGAPL-PNVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVF-AVRWGKY 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 429 KAFYITGGA--------KACDGSvGPEQHHVAPLIFNLEDAADEGMPLQKGsPEYQEVLQQVtRALADVLQDIADDNSSR 500
Cdd:cd16158 376 KAHFYTQGAahsgttpdKDCHPS-AELTSHDPPLLFDLSQDPSENYNLLGL-PEYNQVLKQI-QQVKERFEASMKFGESE 452
|
490 500
....*....|....*....|....*.
gi 1039738450 501 ADYTQDPSVIPCCN----PYQTTCRC 522
Cdd:cd16158 453 INKGEDPALEPCCKpgctPKPSCCQC 478
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
35-487 |
1.69e-110 |
|
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: 335.94 E-value: 1.69e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV---THNFAVTSV 111
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 112 GGLPVNETTLAEVLRQEGYVTAMIGKWHLG-----HHGSYH-PNFRGFDYY-FGIPYSNDMGCtDAPGYNYPpcpacpqr 184
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDFVgTNLPFTNSWAC-DDTGRHVD-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 185 dglWRNPGRdCYtdvalpLYENLNIVEQPVNLSGLAQKYAERAVEFIEqaSTSGRPFLLYVGLAHMHVPLSVTPPLAHPQ 264
Cdd:cd16160 152 ---FPDRSA-CF------LYYNDTIVEQPIQHEHLTETLVGDAKSFIE--DNQENPFFLYFSFPQTHTPLFASKRFKGKS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 265 RQSLYRASLREMDSLVGQIKDK-VDHVARENTLLWFTGDNGPWAQKCELAGSVGPFfglwqthQGGsptKQTTWEGGHRV 343
Cdd:cd16160 220 KRGRYGDNINEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGL-------KGG---KGNSWEGGIRV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 344 PALAYWPGRVPANVtSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHR-VLFHPNSgaageygALQT 422
Cdd:cd16160 290 PFIAYWPGTIKPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDdILYYCCS-------RLMA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 423 VRLNHYKAFYITG--------GAKACDG---------SVGPEQH---HVAPLIFNLEDAADEGMPLQkgSPEYQEVLQQV 482
Cdd:cd16160 362 VRYGSYKIHFKTQplpsqeslDPNCDGGgplsdyivcYDCEDECvtkHNPPLIFDVEKDPGEQYPLQ--PSVYEHMLEAV 439
|
....*
gi 1039738450 483 TRALA 487
Cdd:cd16160 440 EKLIA 444
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-488 |
1.68e-105 |
|
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: 323.65 E-value: 1.68e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG--VTHNFAVTS-- 110
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 111 ----VGGLPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPysndmGCTDAPGYN--YPPCPAcpQR 184
Cdd:cd16157 81 pqniVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAP-----NCHFGPYDNkaYPNIPV--YR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 185 DglWRNPGRdcytdvalpLYENLNIvEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQ 264
Cdd:cd16157 154 D--WEMIGR---------YYEEFKI-DKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 265 RQSLYRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNG-PWAQKCELAGSVGPFFGlwqthqggspTKQTTWEGGHR 342
Cdd:cd16157 222 QRGLYGDAVMELDSSVGKILESLKSLGiENNTFVFFSSDNGaALISAPEQGGSNGPFLC----------GKQTTFEGGMR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 343 VPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSgaageygALQT 422
Cdd:cd16157 292 EPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGD-------ELMA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 423 VRLNHYKAFYIT---------GGAKACDGSVGP-------EQHHVAPLIFNLEDAADEGMPLQKGSPEYQEVLQQVTRAL 486
Cdd:cd16157 365 VRLGQYKAHFWTwsnsweefrKGINFCPGQNVPgvtthnqTDHTKLPLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVV 444
|
..
gi 1039738450 487 AD 488
Cdd:cd16157 445 QQ 446
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
35-494 |
4.83e-104 |
|
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: 321.54 E-value: 4.83e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN------FAV 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASShgmrviLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 109 TSVGGLPVNETTLAEVLRQEGYVTAMIGKWHLGHH------GSYHPNFRGFDYYFGIPYSNDMGCTDAPG--YNYPPCPA 180
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHcesrndFCHHPLNHGFDYFYGLPLTNLKDCGDGSNgeYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 181 CPQRDGL------------------WRnPGRDCYTDVALP-----------------LYENLNIVEQPVNLSGLAQKYAE 225
Cdd:cd16159 161 FPLLTAFvlitaltiflllylgavsKR-FFVFLLILSLLFislfflllitnryfnciLMRNHEVVEQPMSLENLTQRLTK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 226 RAVEFIEQasTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLYRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNG 304
Cdd:cd16159 240 EAISFLER--NKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGlKDNTFVYFTSDNG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 305 PWAqkcELAGSVGPFFGLWQTHQGGSptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNR 384
Cdd:cd16159 318 GHL---EEISVGGEYGGGNGGIYGGK--KMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 385 KFDGRDVSEVLFGKSQMG-HRVLFH------------PNSGAAgeygalqtvrlnHYKAFYIT-----GGAKACDGSVGP 446
Cdd:cd16159 393 IIDGRDLMPLLTGQEKRSpHEFLFHycgaelhavryrPRDGGA------------VWKAHYFTpnfypGTEGCCGTLLCR 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1039738450 447 -----EQHHVAPLIFNLEDAADEGMPLQKGSPEYQEVLQQVTRALADVLQDIA 494
Cdd:cd16159 461 cfgdsVTHHDPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIE 513
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-459 |
6.38e-93 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 287.89 E-value: 6.38e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGAN---WAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHNFAVTSVG 112
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYgggIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 113 GLPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPYSNdmgctdapgynyppcpacpqrdglwrnpg 192
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYHT----------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 193 rdcytdvalplyenlniveqpvnlsgLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAH-PQRQSLYRA 271
Cdd:cd16142 131 --------------------------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGkSSGKGKYAD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 272 SLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGPWAQKCELAGSvGPFFGlwqthqggspTKQTTWEGGHRVPALAYWP 350
Cdd:cd16142 185 SMVELDDHVGQILDALDELGiADNTIVIFTTDNGPEQDVWPDGGY-TPFRG----------EKGTTWEGGVRVPAIVRWP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 351 GRVPANVTSTALLSLLDIFPTVIALAGASLPP------NRKFDGRDVSEVLFGKS-QMGHRVLFHpnsGAAGEYGAlqtV 423
Cdd:cd16142 254 GKIKPGRVSNEIVSHLDWFPTLAALAGAPDPKdkllgkDRHIDGVDQSPFLLGKSeKSRRSEFFY---FGEGELGA---V 327
|
410 420 430
....*....|....*....|....*....|....*.
gi 1039738450 424 RLNHYKAFYITGGAKACDGSVGPEQHHVaPLIFNLE 459
Cdd:cd16142 328 RWKNWKVHFKAQEDTGGPTGEPFYVLTF-PLIFNLR 362
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
13-432 |
2.46e-91 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 284.46 E-value: 2.46e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 13 MAFSGFFYPLVDFSISGKTRAPQPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLL 92
Cdd:COG3119 1 MKRLLLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 93 TGRLGLRNGVTHNFAvTSVGGLPVNETTLAEVLRQEGYVTAMIGKWHLghhgsyhpnfrgfdyyfgipYSNDmgctdapg 172
Cdd:COG3119 81 TGRYPHRTGVTDNGE-GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------YLTD-------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 173 ynyppcpacpqrdglwrnpgrdcytdvalplyenlniveqpvnlsglaqKYAERAVEFIEQASTSGRPFLLYVGLAHMHV 252
Cdd:COG3119 132 -------------------------------------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHA 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 253 PLSVTPPLAHP-----------------------QRQSLYRASLREMDSLVGQIkdkVDHVAR----ENTLLWFTGDNGP 305
Cdd:COG3119 163 PYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVGRL---LDALEElglaDNTIVVFTSDNGP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 306 WaqkcelagsvgpfFGLWqTHQGGsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPnrK 385
Cdd:COG3119 240 S-------------LGEH-GLRGG---KGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPE--D 300
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1039738450 386 FDGRDVSEVLFGKSQMGHRVLFHpnsgAAGEYGALQTVRLNHYKAFY 432
Cdd:COG3119 301 LDGRSLLPLLTGEKAEWRDYLYW----EYPRGGGNRAIRTGRWKLIR 343
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-429 |
7.80e-88 |
|
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: 276.35 E-value: 7.80e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--------- 106
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIpgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 107 ----AVTSVGGLPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGipysndMGCTDAPGYNYPPCPACP 182
Cdd:cd16144 81 tkliPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIG------GTGNGGPPSYYFPPGKPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 183 qrdGLWRNPGRDCYtdvalplyenlniveqpvnlsgLAQKYAERAVEFIEQAstSGRPFLLYvgLAH--MHVPLSVTP-- 258
Cdd:cd16144 155 ---PDLEDGPEGEY----------------------LTDRLTDEAIDFIEQN--KDKPFFLY--LSHyaVHTPIQARPel 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 259 ---------PLAHPQRQSLYRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGPWAQKCELAGSVGPFfglwqthQG 328
Cdd:cd16144 206 iekyekkkkGLRKGQKNPVYAAMIESLDESVGRILDALEELGlADNTLVIFTSDNGGLSTRGGPPTSNAPL-------RG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 329 GsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHR--VL 406
Cdd:cd16144 279 G---KGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRraLF 355
|
410 420
....*....|....*....|....*
gi 1039738450 407 FH-PN-SGAAGEYGAlqTVRLNHYK 429
Cdd:cd16144 356 WHfPHyHGQGGRPAS--AIRKGDWK 378
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-460 |
8.33e-85 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 267.91 E-value: 8.33e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETK-DTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTG----RLGLRNGVTHNFAvTS 110
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGrypwRSRLKGGVLGGFS-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 111 VggLPVNETTLAEVLRQEGYVTAMIGKWHLG-----------HHGSYH-----------PNFRGFDYYFGIPYSNdmgct 168
Cdd:cd16143 80 L--IEPDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkaATGTGKdvdyskpikggPLDHGFDYYFGIPASE----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 169 dapgynyppcpacpqrdglwrnpgrdcytdvALPLyenlniveqpvnlsgLAQKyaerAVEFIEQASTSGRPFLLYVGLA 248
Cdd:cd16143 153 -------------------------------VLPT---------------LTDK----AVEFIDQHAKKDKPFFLYFALP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 249 HMHVPLSVTPPLAHPQRQSLYRASLREMDSLVGQIKDKVD-HVARENTLLWFTGDNGPwaqkcelagSVGPFFGLWQtHQ 327
Cdd:cd16143 183 APHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALKeLGLAENTLVIFTSDNGP---------SPYADYKELE-KF 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 328 GGSPT------KQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQM 401
Cdd:cd16143 253 GHDPSgplrgmKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQ 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738450 402 GHRVLFHPNSGAAGeygalQTVRLNHYKafYITGGAKacDGSVGPEQHHVAPL----IFNLED 460
Cdd:cd16143 333 EVRESLVHHSGNGS-----FAIRKGDWK--LIDGTGS--GGFSYPRGKEKLGLppgqLYNLST 386
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-438 |
2.99e-84 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 267.15 E-value: 2.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGLP 115
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 116 VNETTLAEVLRQEGYVTAMIGKWHLGHHGSY-HPNFRGFDYYFGIpysndMGCTDAPGYnYPPCpacpqrdgLWRNPGRd 194
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYGY-----LDQVHAHNY-YPEY--------LWRNGEK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 195 cytdvaLPLYENLNIVEQPVNLSGLAQK-YAE-----RAVEFIEQAstSGRPFLLYVGL----AHMHVP----------- 253
Cdd:cd16145 146 ------VPLPNNVIPPLDEGNNAGGGGGtYSHdlftdEALDFIREN--KDKPFFLYLAYtlphAPLQVPddgpykykpkd 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 254 LSVTPPLAHPQRQSLYRASLREMDSLVGQIKDKV-DHVARENTLLWFTGDNGP-----WAQKCELAGSVGPFFGLwqthq 327
Cdd:cd16145 218 PGIYAYLPWPQPEKAYAAMVTRLDRDVGRILALLkELGIDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 328 ggsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASlPPNRKfDGRDVSEVLFGKS-QMGHRVL 406
Cdd:cd16145 293 -----KRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAE-PPEDI-DGISLLPTLLGKPqQQQHDYL 365
|
410 420 430
....*....|....*....|....*....|..
gi 1039738450 407 FHpnsgAAGEYGALQTVRLNHYKAFYITGGAK 438
Cdd:cd16145 366 YW----EFYEGGGAQAVRMGGWKAVRHGKKDG 393
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
36-429 |
2.57e-81 |
|
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: 259.40 E-value: 2.57e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTHnfavTSVGG-- 113
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWH----TILGRer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 114 LPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIpysndmgctdapgynyppcpacpqRDGLWRNPGR 193
Cdd:cd16146 76 MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGH------------------------GGGGIGQYPD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 194 DCYTDVALPLYENLNIVEQpvnlsglAQKYA-----ERAVEFIEQASTsgRPFLLYVGLAHMHVPLSVTPPLAHPQRQSL 268
Cdd:cd16146 132 YWGNDYFDDTYYHNGKFVK-------TEGYCtdvffDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPYKDMG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 269 YRASLRE-------MDSLVGQIKDKVDHV-ARENTLLWFTGDNGPWaqkcelagsvGPFFGLWQTHQGGspTKQTTWEGG 340
Cdd:cd16146 203 LDDKLAAfygmienIDDNVGRLLAKLKELgLEENTIVIFMSDNGPA----------GGVPKRFNAGMRG--KKGSVYEGG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 341 HRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQM-GHRVLF--HPNSGAAGEY 417
Cdd:cd16146 271 HRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPwPERTLFthSGRWPPPPKK 350
|
410
....*....|..
gi 1039738450 418 GALQTVRLNHYK 429
Cdd:cd16146 351 KRNAAVRTGRWR 362
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
36-390 |
3.24e-74 |
|
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: 234.64 E-value: 3.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGLP 115
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 116 VNETTLAEVLRQEGYVTAMIGKWHlghhgsyhpnfrgfdyyfgipysndmgctdapgynyppcpacpqrdglwrnpgrdc 195
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 196 ytdvalplyenlniveqpvnlsglaqkyaERAVEFIEQASTSgRPFLLYVGLAHMHvplsvtPPLAhpqrqslYRASLRE 275
Cdd:cd16022 103 -----------------------------DEAIDFIERRDKD-KPFFLYVSFNAPH------PPFA-------YYAMVSA 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 276 MDSLVGQIKDKVD-HVARENTLLWFTGDNGpwaqkcelaGSVGPFFGLWQthqggsptKQTTWEGGHRVPALAYWPGRVP 354
Cdd:cd16022 140 IDDQIGRILDALEeLGLLDNTLIVFTSDHG---------DMLGDHGLRGK--------KGSLYEGGIRVPFIVRWPGKIP 202
|
330 340 350
....*....|....*....|....*....|....*.
gi 1039738450 355 ANVTSTALLSLLDIFPTVIALAGASLPpnRKFDGRD 390
Cdd:cd16022 203 AGQVSDALVSLLDLLPTLLDLAGIEPP--EGLDGRS 236
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
36-435 |
1.00e-68 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 225.89 E-value: 1.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFvDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSV-GGL 114
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVIL-NNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEpYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 115 PVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYH-PNFRGFDYYFGiPYSndmGCTDapGYNYPPCPACP-QRDGLWRN-- 190
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYTWEYtPTNRGFDSFYG-YYG---GAED--YYTHTSGGANDyGNDDLRDNee 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 191 ---PGRDCY-TDValplyenlniveqpvnlsglaqkYAERAVEFIEQASTSgRPFLLYVGLAHMHVPLSVTPPLA----- 261
Cdd:cd16029 154 pawDYNGTYsTDL-----------------------FTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYAdpyed 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 262 ------HPQRQsLYRASLREMDSLVGQIKDKVDHVAR-ENTLLWFTGDNGPWAQKCElAGSVGPFFGlwqthqggspTKQ 334
Cdd:cd16029 210 kfahikDEDRR-TYAAMVSALDESVGNVVDALKAKGMlDNTLIVFTSDNGGPTGGGD-GGSNYPLRG----------GKN 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 335 TTWEGGHRVPALAYWPGRVP-ANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHR-VLFHPNSG 412
Cdd:cd16029 278 TLWEGGVRVPAFVWSPLLPPkRGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTeILLNIDDI 357
|
410 420
....*....|....*....|...
gi 1039738450 413 AAGEYGAlqTVRLNHYKafYITG 435
Cdd:cd16029 358 TRTTGGA--AIRVGDWK--LIVG 376
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-435 |
5.04e-66 |
|
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: 218.24 E-value: 5.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHnfavtsvGGLP 115
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPL-CTPSRVQLMTGKYNFRNYVVF-------GYLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 116 VNETTLAEVLRQEGYVTAMIGKWHLG---HHGSYHPNFrGFDYY--FGIPYSNDmgctDAPGYNYPpCPACPQRDGLWRN 190
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGKWQLGggrGDGDYPHEF-GFDEYclWQLTETGE----KYSRPATP-TFNIRNGKLLETT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 191 PGR---DCYTDVALplyenlniveqpvnlsglaqkyaeravEFIEQAStsGRPFLLYVGLAHMHVPLSVTPPLAHP---- 263
Cdd:cd16151 147 EGDygpDLFADFLI---------------------------DFIERNK--DQPFFAYYPMVLVHDPFVPTPDSPDWdpdd 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 264 ----QRQSLYRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkcelagSVGPFFGLW--QTHQGGsptKQTT 336
Cdd:cd16151 198 krkkDDPEYFPDMVAYMDKLVGKLVDKLEELGlRENTIIIFTGDNG----------THRPITSRTngREVRGG---KGKT 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 337 WEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGE 416
Cdd:cd16151 265 TDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWYYRNPHK 344
|
410
....*....|....*....
gi 1039738450 417 YGALQTVRLNHYKaFYITG 435
Cdd:cd16151 345 KFGSRFVRTKRYK-LYADG 362
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
36-407 |
1.15e-57 |
|
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: 196.19 E-value: 1.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGA--NWAETkdtTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFavTSVGG 113
Cdd:cd16027 1 PNILWIIADDLSPDLGGYggNVVKT---PNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR--SRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 114 LPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDmgctdapgynyppcpacpqrdglwrnpgr 193
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAWD----------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 194 dcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQAStSGRPFLLYVGLAHMHV-------------PLSVTPPL 260
Cdd:cd16027 127 -----------------------------YASNAADFLNRAK-KGQPFFLWFGFHDPHRpyppgdgeepgydPEKVKVPP 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 261 AHPQ----RQSL--YRASLREMDSLVGQIKDKVD-HVARENTLLWFTGDNGpwaqkcelagsvGPFFGlwqthqggspTK 333
Cdd:cd16027 177 YLPDtpevREDLadYYDEIERLDQQVGEILDELEeDGLLDNTIVIFTSDHG------------MPFPR----------AK 234
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738450 334 QTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNrkFDGRDVSEVLFGKSQMGHRVLF 407
Cdd:cd16027 235 GTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGRDYVF 306
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
36-378 |
1.27e-56 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 191.10 E-value: 1.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtSVGGLP 115
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS----TPVGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 116 VNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFG-IPYSNDMGctdapgynyppcpACPQRDGLWRNPGrd 194
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLYA-------------DPPDVPYNCSGGG-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 195 CYTDValplyenlniveqpvnlsglaqkYAERAVEFIEQAStsgRPFLLYVGLAHMHVPLSVTP----------PLAHPQ 264
Cdd:pfam00884 142 VSDEA-----------------------LLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDrypekyatfkPSSCSE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 265 RQSL--YRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGPwaqkcelagSVGPFfglwQTHQGGSPTKQTtWEGGH 341
Cdd:pfam00884 196 EQLLnsYDNTLLYTDDAIGRVLDKLEENGlLDNTLVVYTSDHGE---------SLGEG----GGYLHGGKYDNA-PEGGY 261
|
330 340 350
....*....|....*....|....*....|....*..
gi 1039738450 342 RVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGA 378
Cdd:pfam00884 262 RVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
35-408 |
6.55e-55 |
|
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: 189.58 E-value: 6.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDMGWGDLGANWAETkDTTNLDKMASEGMRFVDFHAAAsTCSPSRASLLTGRLGLRNGV-THNFAVTSVGG 113
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGEI-PTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQVGMgTMAELATGKPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 114 ----LPVNETTLAEVLRQEGYVTAMIGKWHLGHHgsyhpnfrgfDYYFgipysndmgcTDApgynyppcpacpqrdglwr 189
Cdd:cd16025 80 yegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------DYYS----------TDD------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 190 npgrdcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYV--GLAH--MHVP------------ 253
Cdd:cd16025 121 ---------------------------------LTDKAIEYIDEQKAPDKPFFLYLafGAPHapLQAPkewidkykgkyd 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 254 -------------------------LSVTPPLAHP-------------QRQSLYRASLREMDSLVGQIkdkVDHVAR--- 292
Cdd:cd16025 168 agwdalreerlerqkelglipadtkLTPRPPGVPAwdslspeekkleaRRMEVYAAMVEHMDQQIGRL---IDYLKElge 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 293 -ENTLLWFTGDNGP-----WAQkcelAGSvGPFFGlwqthqggspTKQTTWEGGHRVPALAYWPGRVPA-NVTSTALLSL 365
Cdd:cd16025 245 lDNTLIIFLSDNGAsaepgWAN----ASN-TPFRL----------YKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHV 309
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 366 LDIFPTVIALAGASLP------PNRKFDGRDVSEVLFGKSQ-----------MGHRVLFH 408
Cdd:cd16025 310 IDIAPTILELAGVEYPktvngvPQLPLDGVSLLPTLDGAAApsrrrtqyfelFGNRAIRK 369
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-424 |
7.27e-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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 178.92 E-value: 7.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggL 114
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 115 PVNETTLAEVLRQEGYVTAMIGKWHL-GHHGSYH--------PNFR-GFDYYFGipysndMGCTDapGYNYPPcpacpqr 184
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGraddytppPERRhGFDYWKG------YECNH--DHNNPH------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 185 dgLWRNPGRDCYTDVALPLYEnlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYV--GLAH------------M 250
Cdd:cd16034 141 --YYDDDGKRIYIKGYSPDAE------------------TDLAIEYLENQADKDKPFALVLswNPPHdpyttapeeyldM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 251 HVPLSVT----PPLAHPQRQSL------YRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkcELAGSvgpf 319
Cdd:cd16034 201 YDPKKLLlrpnVPEDKKEEAGLredlrgYYAMITALDDNIGRLLDALKELGlLENTIVVFTSDHG------DMLGS---- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 320 fglwqtHqgGSPTKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGasLPPNRKFDGRDVSEVLFGKS 399
Cdd:cd16034 271 ------H--GLMNKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCG--LPIPDTVEGRDLSPLLLGGK 340
|
410 420 430
....*....|....*....|....*....|...
gi 1039738450 400 QMGHR----VLFHPNSGAA----GEYGALQTVR 424
Cdd:cd16034 341 DDEPDsvllQCFVPFGGGSardgGEWRGVRTDR 373
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
35-486 |
6.40e-48 |
|
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: 171.56 E-value: 6.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvGGL 114
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG----PLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 115 PVNETTLAEVLRQEGYVTAMIGKWHLGHHGsYHPNfRGFDYYFGIPysndmgctdAPGYNYPPcpacpqrdglwrnpgrd 194
Cdd:cd16031 78 DASQPTYPKLLRKAGYQTAFIGKWHLGSGG-DLPP-PGFDYWVSFP---------GQGSYYDP----------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 195 cytdvalPLYENLNIVEQPVNLSGLaqkYAERAVEFIEQAStSGRPFLLYVG--LAH---------------MHVPLSVT 257
Cdd:cd16031 130 -------EFIENGKRVGQKGYVTDI---ITDKALDFLKERD-KDKPFCLSLSfkAPHrpftpaprhrglyedVTIPEPET 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 258 ---------PPLAHPQRQSL--------------------YRASLREMDSLVGQIKDKVD-HVARENTLLWFTGDNGpwa 307
Cdd:cd16031 199 fddddyagrPEWAREQRNRIrgvldgrfdtpekyqrymkdYLRTVTGVDDNVGRILDYLEeQGLADNTIIIYTSDNG--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 308 qkcelagsvgpFF----GLwqthqGGsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPN 383
Cdd:cd16031 276 -----------FFlgehGL-----FD---KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 384 rkFDGRDVSEVLFGKSQMGHR------VLFHPNSGAAGEYGALQTVRlnhYKAFYITGGAKAcdgsvgpEQhhvaplIFN 457
Cdd:cd16031 337 --MQGRSLLPLLEGEKPVDWRkefyyeYYEEPNFHNVPTHEGVRTER---YKYIYYYGVWDE-------EE------LYD 398
|
490 500 510
....*....|....*....|....*....|...
gi 1039738450 458 LEdaADegmPLQK----GSPEYQEVLQQVTRAL 486
Cdd:cd16031 399 LK--KD---PLELnnlaNDPEYAEVLKELRKRL 426
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-393 |
2.50e-46 |
|
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: 162.41 E-value: 2.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV-----THNFAVTS 110
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 111 VG-GLPVNETTLAEVLRQEGYVTAMIGKWHLGhhgsyhpnfrgfdyyfgipysndmgctdapgynyppcpacpqrdglwr 189
Cdd:cd16149 81 KPeGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 190 npgrdcytdvalplyenlniveqpvnlsglaqkyaERAVEFIEQASTSGRPFLLYVGLAHMHVPLSvtpplahpqrqslY 269
Cdd:cd16149 113 -----------------------------------DDAADFLRRRAEAEKPFFLSVNYTAPHSPWG-------------Y 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 270 RASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkcelagsvgpfF-----GLWqtHQGGSPTKQTTWEGGHRV 343
Cdd:cd16149 145 FAAVTGVDRNVGRLLDELEELGlTENTLVIFTSDNG---------------FnmghhGIW--GKGNGTFPLNMYDNSVKV 207
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1039738450 344 PALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSE 393
Cdd:cd16149 208 PFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPGRSFAD 257
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
35-389 |
8.69e-40 |
|
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: 148.85 E-value: 8.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDMGWgDLGANWAETKdTTNLdkMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtSVGGL 114
Cdd:cd16147 1 RPNIVLILTDDQDV-ELGSMDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSP--PGGGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 115 PV------NETTLAEVLRQEGYVTAMIGK----WHLGHHGSYHPnfRGFDYYFGI-------PYSNDMGCTDAPGYNYPp 177
Cdd:cd16147 75 PKfwqnglERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYVP--PGWDEWDGLvgnstyyNYTLSNGGNGKHGVSYP- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 178 cpacpqrdglwrnpgRDCYTDValplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYVG---------LA 248
Cdd:cd16147 152 ---------------GDYLTDV-----------------------IANKALDFLRRAAADDKPFFLVVAppaphgpftPA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 249 HMHVPLSVTPPLAHP---------------------------QRQSLYRA---SLREMDSLVGQIKDKVDHVAR-ENTLL 297
Cdd:cd16147 194 PRYANLFPNVTAPPRpppnnpdvsdkphwlrrlpplnptqiaYIDELYRKrlrTLQSVDDLVERLVNTLEATGQlDNTYI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 298 WFTGDNG-PWAQkcelagsvgpfFGLWqthqggsPTKQTTWEGGHRVPALAYWPGrVPANVTSTALLSLLDIFPTVIALA 376
Cdd:cd16147 274 IYTSDNGyHLGQ-----------HRLP-------PGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLA 334
|
410
....*....|...
gi 1039738450 377 GASLPPNrkFDGR 389
Cdd:cd16147 335 GAPPPSD--MDGR 345
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-389 |
1.05e-39 |
|
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: 148.91 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--AVTSVGG 113
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 114 LPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSyhPNFRGFDYYFGIpysndmgctdapgynyppcpacpqrdglwrNPGR 193
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVGPEET--PLDYGFDEYLPV------------------------------ETTI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 194 DCYTdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYVGL-------------AHMHVPLSVTPP- 259
Cdd:cd16033 129 EYFL--------------------------ADRAIEMLEELAADDKPFFLRVNFwgphdpyippepyLDMYDPEDIPLPe 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 260 -LAHP-------QRQSLYRASLRE-------------------MDSLVGQIKDKVDHV-ARENTLLWFTGDNGpwaqkcE 311
Cdd:cd16033 183 sFADDfedkpyiYRRERKRWGVDTedeedwkeiiahywgyitlIDDAIGRILDALEELgLADDTLVIFTSDHG------D 256
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738450 312 LAGSvgpfFGLWQThqgGSPTKQTTweggHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGAslPPNRKFDGR 389
Cdd:cd16033 257 ALGA----HRLWDK---GPFMYEET----YRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGV--DVPPKVDGR 321
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-381 |
1.14e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 145.19 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWgDLGANWAETKD---TTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVThnfavtSVG 112
Cdd:cd16154 1 PNILLIIADDQGL-DSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVL------AVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 113 G-LPVNETTLAEVLRQE----GYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIpysndmgctdapgynyppcpacpqrdgl 187
Cdd:cd16154 73 DeLLLSEETLLQLLIKDattaGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGI---------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 188 wrNPGrdcytdvALPLYENLNIVEQPVNLSglAQKYA-----ERAVEFIEQASTsgrPFLLYVGLAHMHVPLSVTPPLAH 262
Cdd:cd16154 125 --LGG-------GVQDYYNWNLTNNGQTTN--STEYAttkltNLAIDWIDQQTK---PWFLWLAYNAPHTPFHLPPAELH 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 263 PQRQS------------LYRASLREMDSLVGQIKDKVDHVARENTLLWFTGDNG-PwaqkcelaGSVGPffgLWQTHQGg 329
Cdd:cd16154 191 SRSLLgdsadieanprpYYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGtP--------GQVVD---LPYTRNH- 258
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039738450 330 spTKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLP 381
Cdd:cd16154 259 --AKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAA 308
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-460 |
2.34e-37 |
|
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: 139.99 E-value: 2.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggLP 115
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP-----YD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 116 VNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHpnfrGFDYyfgipysndmgctdapgynyppcpacpqrdglwrnpgrdc 195
Cdd:cd16037 76 GDVPSWGHALRAAGYETVLIGKLHFRGEDQRH----GFRY---------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 196 ytdvalplyenlnivEQPVnlsglaqkyAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAhpqrqSLYRASLR- 274
Cdd:cd16037 112 ---------------DRDV---------TEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFY-----DLYVRRARa 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 275 -------EMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkcELAGSvgpfFGLWQthqggsptKQTTWEGGHRVPAL 346
Cdd:cd16037 163 ayyglveFLDENIGRVLDALEELGlLDNTLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMI 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 347 AYWPGrVPANVTSTALLSLLDIFPTVIALAGASLPPNRkfDGRDVSEVLFGKSQMGHRVL--FHpnsgAAGEYGALQTVR 424
Cdd:cd16037 225 ISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL--DGRSLLPLAEGPDDPDRVVFseYH----AHGSPSGAFMLR 297
|
410 420 430
....*....|....*....|....*....|....*...
gi 1039738450 425 LNHYKafYItggakacdgsvgpeqHHV--APLIFNLED 460
Cdd:cd16037 298 KGRWK--YI---------------YYVgyPPQLFDLEN 318
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-390 |
3.17e-37 |
|
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: 138.45 E-value: 3.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILAD----DMgwgdLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHnfavtsv 111
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWG------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 112 GGLPVNETTLAEVLRQEGYVTAMIGKWhlgHHGSYHPNF-RGFDYYFgipysndmgctdapgynyppcpacPQRDGLWRN 190
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAVSSN---PHLFGGPGFdRGFDTFE------------------------DFRGQEGDP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 191 PGRDCYTdvalplyenlniveqpvnlsglAQKYAERAVEFIEQASTSgRPFLLYVglaHM---HVPlsvtpplahpqrqS 267
Cdd:cd16148 123 GEEGDER----------------------AERVTDRALEWLDRNADD-DPFFLFL---HYfdpHEP-------------Y 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 268 LYRASLREMDSLVGQIKDKVD-HVARENTLLWFTGDNGpwaqkcELagsvgpFF--GLWQTHqGGSPTKQTTwegghRVP 344
Cdd:cd16148 164 LYDAEVRYVDEQIGRLLDKLKeLGLLEDTLVIVTSDHG------EE------FGehGLYWGH-GSNLYDEQL-----HVP 225
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1039738450 345 ALAYWPGRVPANVTStALLSLLDIFPTVIALAGasLPPNRKFDGRD 390
Cdd:cd16148 226 LIIRWPGKEPGKRVD-ALVSHIDIAPTLLDLLG--VEPPDYSDGRS 268
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-486 |
1.31e-36 |
|
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: 139.24 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAST----CSPSRASLLTGRlglrngvtHNFAVTS 110
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGR--------TLFHAPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 111 VGG--LPVNETTLAEVLRQEGYVTAMIGKWHLGhhgsyhpnfrgfdyyfgipysndmgctdapgynyppcpacpqrdglw 188
Cdd:cd16155 74 GGKaaIPSDDKTWPETFKKAGYRTFATGKWHNG----------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 189 rnpgrdcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPL-------- 260
Cdd:cd16155 107 ----------------------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYldmyppet 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 261 ---------AHP------------------------QRQSLYRASLREMDSLVGQIKDKVDHVAR-ENTLLWFTGDNGpw 306
Cdd:cd16155 153 iplpenflpQHPfdngegtvrdeqlapfprtpeavrQHLAEYYAMITHLDAQIGRILDALEASGElDNTIIVFTSDHG-- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 307 aqkceLA-GSvgpfFGLwqthQGgsptKQTTWEGGHRVPALAYWPGrVPANVTSTALLSLLDIFPTVIALAGASLPPnrK 385
Cdd:cd16155 231 -----LAvGS----HGL----MG----KQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPE--S 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 386 FDGRDVSEVLFGKSQMGHRVLFhpnsgaaGEYGALQ-TVRLNHYKAFYITGGAKacdgsvgpeqhhvAPLIFNLEDAADE 464
Cdd:cd16155 291 VEGKSLLPVIRGEKKAVRDTLY-------GAYRDGQrAIRDDRWKLIIYVPGVK-------------RTQLFDLKKDPDE 350
|
490 500
....*....|....*....|..
gi 1039738450 465 GMPLQkGSPEYQEVLQQVTRAL 486
Cdd:cd16155 351 LNNLA-DEPEYQERLKKLLAEL 371
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
35-492 |
2.94e-36 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 140.57 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDMGwGD-LGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNGVTHNF 106
Cdd:PRK13759 6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDVVPWNY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 107 avtsvgglpvnETTLAEVLRQEGYVTAMIGKWHlghhgsYHP--NFRGFDYYF---GIPYSN--------DMgCTD---- 169
Cdd:PRK13759 85 -----------KNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHNVLlhdGYLHSGrnedksqfDF-VSDylaw 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 170 ----APGYNyppcpacPQRDGLwrnpGRDCYTDVALP--LYENLNiveqPVNLSGlaqkyaERAVEFIEQAStSGRPFLL 243
Cdd:PRK13759 147 lrekAPGKD-------PDLTDI----GWDCNSWVARPwdLEERLH----PTNWVG------SESIEFLRRRD-PTKPFFL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 244 YVGLAHMHVPLSvtPPLA------------------------HPQRQSL------------------YRASLREMDSLVG 281
Cdd:PRK13759 205 KMSFARPHSPYD--PPKRyfdmykdadipdphigdweyaedqDPEGGSIdalrgnlgeeyarraraaYYGLITHIDHQIG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 282 QIKDKVDHVA-RENTLLWFTGDNGpwaqkcELAGSvgpfFGLWQthqggsptKQTTWEGGHRVPALAYWPG---RVPANV 357
Cdd:PRK13759 283 RFLQALKEFGlLDNTIILFVSDHG------DMLGD----HYLFR--------KGYPYEGSAHIPFIIYDPGgllAGNRGT 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 358 TSTALLSLLDIFPTVIALAGASLPPNrkFDGRDVSEVLFGKSQmGHRVLFHpnsgaaGEYGalqtvrlNHYKAF-YITGG 436
Cdd:PRK13759 345 VIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYE-GWRPYLH------GEHA-------LGYSSDnYLTDG 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738450 437 A-KACDGSV-GPEQhhvaplIFNLEDAADEGMPLQkGSPEYQEVLQQVTRALADVLQD 492
Cdd:PRK13759 409 KwKYIWFSQtGEEQ------LFDLKKDPHELHNLS-PSEKYQPRLREMRKKLVDHLRG 459
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
35-395 |
2.95e-34 |
|
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: 134.24 E-value: 2.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDM----GWgdLGANWAETKdttNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVtHNFAVTS 110
Cdd:cd16030 2 KPNVLFIAVDDLrpwlGC--YGGHPAKTP---NIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGV-YDNNSYF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 111 VGGLPvNETTLAEVLRQEGYVTAMIGK-WHlGHHGSYHPNFRGFDYYFGIPysndmgctdAPGYNYPPCPACPQRDGLWR 189
Cdd:cd16030 76 RKVAP-DAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPP---------GPEKYPPGKLCPGKKGGKGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 190 NPGRDC---------YTDvalplyenlniveqpvnlsglaQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSV---- 256
Cdd:cd16030 145 GGGPAWeaadvpdeaYPD----------------------GKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVApkky 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 257 ---------------------------------------------TPPLAHPQRQSL---YRASLREMDSLVGQIKDKVD 288
Cdd:cd16030 203 fdlyplesiplpnpfdpidlpevawndlddlpkygdipalnpgdpKGPLPDEQARELrqaYYASVSYVDAQVGRVLDALE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 289 -HVARENTLLWFTGDNGpWA--QKcelagsvgpffGLWQthqggsptKQTTWEGGHRVPALAYWPGRVPANVTSTALLSL 365
Cdd:cd16030 283 eLGLADNTIVVLWSDHG-WHlgEH-----------GHWG--------KHTLFEEATRVPLIIRAPGVTKPGKVTDALVEL 342
|
410 420 430
....*....|....*....|....*....|
gi 1039738450 366 LDIFPTVIALAGasLPPNRKFDGRDVSEVL 395
Cdd:cd16030 343 VDIYPTLAELAG--LPAPPCLEGKSLVPLL 370
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
402-522 |
5.24e-33 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 122.04 E-value: 5.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 402 GHRVLFHpNSGAAgeygaLQTVRLNHYKAFYITG-----GAKACDGSVGPEQHHVAPLIFNLEDAADEGMPLQKGSPEYQ 476
Cdd:pfam14707 2 PHEFLFH-YCGAA-----LHAVRWGPYKAHFFTPsfdppGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYP 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1039738450 477 EVLQQVTRALADVLQDI--ADDNSSRADYTQDPSVIPCCnPYQTTCRC 522
Cdd:pfam14707 76 EVLAEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-408 |
1.33e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 121.16 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDM-GWGDLGANWAETKdTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGL 114
Cdd:cd16035 1 PNILLILTDQErYPPPWPAGWAALN-LPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 115 PVNETTLAEVLRQEGYVTAMIGKWHLGHHGsyhpnfrgfdyyfgipysndmgctdapgynyppcPACPQRDGLwrnpgrd 194
Cdd:cd16035 80 SPDVPTLGHMLRAAGYYTAYKGKWHLSGAA----------------------------------GGGYKRDPG------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 195 cytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTS---GRPFLLYVGLAHMH-VPLSVTPPLAHPQRQSLYR 270
Cdd:cd16035 119 ----------------------------IAAQAVEWLRERGAKnadGKPWFLVVSLVNPHdIMFPPDDEERWRRFRNFYY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 271 ASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkcELAGSVGpffGLwqtHQGGSPTKQTTwegghRVPALAYW 349
Cdd:cd16035 171 NLIRDVDRQIGRVLDALDASGlADNTIVVFTSDHG------EMGGAHG---LR---GKGFNAYEEAL-----HVPLIISH 233
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738450 350 PGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRK----FDGRDVSEVLFGKS--QMGHRVLFH 408
Cdd:cd16035 234 PDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATeappLPGRDLSPLLTDADadAVRDGILFT 298
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-393 |
1.09e-29 |
|
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: 117.86 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDMGWGDLGA-NWAETKD---------TTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTH 104
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCyNNAHTGKsesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 105 NFAVTSVG--GLPvnetTLAEVLRQEGYVTAMIGKWHLghhgsyhpnfrgfdyyfgipysndmgctdapgynyppcpacp 182
Cdd:cd16153 81 FEAAHPALdhGLP----TFPEVLKKAGYQTASFGKSHL------------------------------------------ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 183 qrdglwrnpgrdcytdvalplyenlnivEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPlsVTPPLAH 262
Cdd:cd16153 115 ----------------------------EAFQRYLKNANQSYKSFWGKIAKGADSDKPFFVRLSFLQPHTP--VLPPKEF 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 263 PQRqSLYRASLREMDSLVGQIKDKVD----HVARENTLLWFTGDNGpwaqkcelagsvgpffglWQTHQGGSPTKQTTWE 338
Cdd:cd16153 165 RDR-FDYYAFCAYGDAQVGRAVEAFKayslKQDRDYTIVYVTGDHG------------------WHLGEQGILAKFTFWP 225
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738450 339 GGHRVPALAYWPGR--VPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSE 393
Cdd:cd16153 226 QSHRVPLIVVSSDKlkAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
36-460 |
1.92e-29 |
|
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: 118.45 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-----EFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 116 VNETTLAEVLRQEGYVTAMIGKWHL-G---HHGsyhpnfrgFDYyfgipysNDmgctdapgynyppcpacpqrdglwrnp 191
Cdd:cd16032 76 ADIPTFAHYLRAAGYRTALSGKMHFvGpdqLHG--------FDY-------DE--------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 192 grdcytDVALplyenlniveqpvnlsglaqkyaeRAVEFIEQASTS--GRPFLLYVGLAHMHVPLSVTPPL----AHPQR 265
Cdd:cd16032 114 ------EVAF------------------------KAVQKLYDLARGedGRPFFLTVSFTHPHDPYVIPQEYwdlyVRRAR 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 266 QSLYrASLREMDSLVGQIKDKVDHV-ARENTLLWFTGDNGpwaqkcELAGSVGpffgLWQthqggsptKQTTWEGGHRVP 344
Cdd:cd16032 164 RAYY-GMVSYVDDKVGQLLDTLERTgLADDTIVIFTSDHG------DMLGERG----LWY--------KMSFFEGSARVP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 345 ALAYWPG-----RVPANVtstallSLLDIFPTVIALAGASLPPNR-KFDGRDVSEVLFGKSQMGHRVLFhpnsgaaGEYG 418
Cdd:cd16032 225 LIISAPGrfaprRVAEPV------SLVDLLPTLVDLAGGGTAPHVpPLDGRSLLPLLEGGDSGGEDEVI-------SEYL 291
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1039738450 419 A------LQTVRLNHYKAFYItggakacdgsvgpeqHHVAPLIFNLED 460
Cdd:cd16032 292 AegavapCVMIRRGRWKFIYC---------------PGDPDQLFDLEA 324
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
36-376 |
1.18e-25 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 105.20 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCS-PSRASLLTGRLGLRNGVTHNFAVT----- 109
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSaPNHAALLTGAYPTLHGYTGNGSADpelps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 110 SVGGLPVNETTLAEVLRQEGYVTAMIGkwhlghhgsyhpnfrgfdyyfgipysndmgctdapgynyppcpacpqrdglwr 189
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 190 npgrdcytdvalplyenlniveqpvnlsglaqkyaerAVEFIEQaSTSGRPFLLYVGLAHMHVPLSvtpplAHPQRQSLY 269
Cdd:cd00016 108 -------------------------------------LLKAIDE-TSKEKPFVLFLHFDGPDGPGH-----AYGPNTPEY 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 270 RASLREMDSLVGQIKDKVD--HVArENTLLWFTGDNGpwaqkcelagsvGPFFGLwqTHQGGSPTKQTTWEGGHRVPALA 347
Cdd:cd00016 145 YDAVEEIDERIGKVLDALKkaGDA-DDTVIIVTADHG------------GIDKGH--GGDPKADGKADKSHTGMRVPFIA 209
|
330 340
....*....|....*....|....*....
gi 1039738450 348 YWPGrVPANVTSTALLSLLDIFPTVIALA 376
Cdd:cd00016 210 YGPG-VKKGGVKHELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
36-424 |
1.27e-23 |
|
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: 103.62 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG-VTHNFAVTSvggl 114
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGsWTNCMALGD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 115 pvNETTLAEVLRQEGYVTAMIGKWHLGhhgsyhpnfrGFDYY-FGI-P------YSNDMGC-----TDapgynyppcpac 181
Cdd:cd16156 77 --NVKTIGQRLSDNGIHTAYIGKWHLD----------GGDYFgNGIcPqgwdpdYWYDMRNyldelTE------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 182 pQRDGLWRNPgrdcytdvaLPLYENLNIVEQPVnlsgLAQKYAERAVEFIEQASTsgRPFLLYVGLAHMHVPLSVTPPLA 261
Cdd:cd16156 133 -EERRKSRRG---------LTSLEAEGIKEEFT----YGHRCTNRALDFIEKHKD--EDFFLVVSYDEPHHPFLCPKPYA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 262 ---------------------------------HPQRQS------LYRASLREMDSLVGQIKDKVDHVArENTLLWFTGD 302
Cdd:cd16156 197 smykdfefpkgenayddlenkplhqrlwagakpHEDGDKgtikhpLYFGCNSFVDYEIGRVLDAADEIA-EDAWVIYTSD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 303 NGpwaqkcELAGSvgpfFGLWQthQGGSPTKQTTwegghRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPP 382
Cdd:cd16156 276 HG------DMLGA----HKLWA--KGPAVYDEIT-----NIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPK 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1039738450 383 nrKFDGRDVSEVLFGKSQMGHRVLF---------HPNsgaageYGALQTVR 424
Cdd:cd16156 339 --VLEGESILATIEDPEIPENRGVFvefgryevdHDG------FGGFQPVR 381
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-398 |
8.45e-21 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 94.22 E-value: 8.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 35 QPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtsVGGL 114
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 115 PVNETTLAEVLRQEGYVTAMIGKWHLGhhgsyhpnfrgfdyyfgipysndmgctdapGYnyppcpacpqrdglwrnpgR- 193
Cdd:cd16152 76 PADEKTLAHYFRDAGYETGYVGKWHLA------------------------------GY-------------------Rv 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 194 DCYTDvalplyenlniveqpvnlsglaqkyaeRAVEFIEQASTSgRPFLLYVGLAHMH---------VPLS--------V 256
Cdd:cd16152 107 DALTD---------------------------FAIDYLDNRQKD-KPFFLFLSYLEPHhqndrdryvAPEGsaerfanfW 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 257 TPPLAHPQ----RQSL--YRASLREMDSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkCelagsvgpffglwqtHQGG 329
Cdd:cd16152 159 VPPDLAALpgdwAEELpdYLGCCERLDENVGRIRDALKELGlYDNTIIVFTSDHG-----C---------------HFRT 218
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738450 330 SPT--KQTTWEGGHRVPALAYWPG-----RVPANVtstallSLLDIFPTVIALAGASLPPnrKFDGRDVSEVLFGK 398
Cdd:cd16152 219 RNAeyKRSCHESSIRVPLVIYGPGfngggRVEELV------SLIDLPPTLLDAAGIDVPE--EMQGRSLLPLVDGK 286
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
36-389 |
8.65e-20 |
|
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: 91.94 E-value: 8.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT-----PLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 116 VNETTLAEVLRQEGYVTAMIGKWHlghhgsYHPNFRGFDyyfgipySND----MGCTDAPGYNyPPCPACPQRDGLwrnp 191
Cdd:cd16028 76 ARHLTLALELRKAGYDPALFGYTD------TSPDPRGLA-------PLDprllSYELAMPGFD-PVDRLDEYPAED---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 192 grdcyTDVALplyenlniveqpvnlsglaqkYAERAVEFIEqaSTSGRPFLLYVGLAHMHVPL-------------SVTP 258
Cdd:cd16028 138 -----SDTAF---------------------LTDRAIEYLD--ERQDEPWFLHLSYIRPHPPFvapapyhalydpaDVPP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 259 PLAHPQRQS------LYRASLREMDSL------------------------VGQIKDKVDHVAR-----------ENTLL 297
Cdd:cd16028 190 PIRAESLAAeaaqhpLLAAFLERIESLsfspgaanaadlddeevaqmratyLGLIAEVDDHLGRlfdylketgqwDDTLI 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 298 WFTGDNGpwaqkcELAGsvgpffglwQTHQGGsptKQTTWEGGHRVPALAYWPGRvPANVTS----TALLSLLDIFPTVI 373
Cdd:cd16028 270 VFTSDHG------EQLG---------DHWLWG---KDGFFDQAYRVPLIVRDPRR-EADATRgqvvDAFTESVDVMPTIL 330
|
410
....*....|....*.
gi 1039738450 374 ALAGASLPPnrKFDGR 389
Cdd:cd16028 331 DWLGGEIPH--QCDGR 344
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-399 |
2.75e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 89.99 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGR----LGLRNgvTHNFavtsv 111
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWyphvNGHRT--LHHL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 112 ggLPVNETTLAEVLRQEGYVTAMIGKwhlghhgsyhpnfrgfdyyfgipysNDmgCTDAPgynyppcpacpqrdglwRNP 191
Cdd:cd16150 74 --LRPDEPNLLKTLKDAGYHVAWAGK-------------------------ND--DLPGE-----------------FAA 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 192 GRDCYTDVAlplyenlniveqpvnlsglaqkYAERAVEFIEQASTsGRPFLLYVGLAHMHVPLSVTPP------------ 259
Cdd:cd16150 108 EAYCDSDEA----------------------CVRTAIDWLRNRRP-DKPFCLYLPLIFPHPPYGVEEPwfsmidreklpp 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 260 --------------LAHPQRQSLYRAS---LREM-----------DSLVGQIKDKVDHVA-RENTLLWFTGDNGpwaqkc 310
Cdd:cd16150 165 rrppglrakgkpsmLEGIEKQGLDRWSeerWRELratylgmvsrlDHQFGRLLEALKETGlYDDTAVFFFSDHG------ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 311 ELAGSvgpfFGLWQTHQGGSPTKQTtwegghRVPALAYWPGrVPANVTSTALLSLLDIFPTVIALAGASLPPNRkfdgrd 390
Cdd:cd16150 239 DYTGD----YGLVEKWPNTFEDCLT------RVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAGIPLSHTH------ 301
|
....*....
gi 1039738450 391 vsevlFGKS 399
Cdd:cd16150 302 -----FGRS 305
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
36-463 |
1.06e-15 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 78.74 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGrlgLRNGVTHNFavTSVGGLP 115
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG---LFTHLTESW--NNYKGLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 116 VNETTLAEVLRQEGYVTAMIGK--WHLGHHGsyhpnfrgfdyyfgipYSNDMgctDAPGYNYPpcpacpqrdGLWRNPGR 193
Cdd:cd16171 76 PNYPTWMDRLEKHGYHTQKYGKldYTSGHHS----------------VSNRV---EAWTRDVP---------FLLRQEGR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 194 DCytdvalplyENLNIVEQPVNLSGLAQKYAERAVEFIEQASTS-GRPFLLYVGLAhmhvplsvtppLAHPQR------- 265
Cdd:cd16171 128 PT---------VNLVGDRSTVRVMLKDWQNTDKAVHWIRKEAPNlTQPFALYLGLN-----------LPHPYPspsmgen 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 266 -------QSLYRASLREMDSLVGQIKDKV-DHVARENTLLWFTGDNGpwaqkcELAGSVGPFFglwqthqggsptKQTTW 337
Cdd:cd16171 188 fgsirniRAFYYAMCAETDAMLGEIISALkDTGLLDKTYVFFTSDHG------ELAMEHRQFY------------KMSMY 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 338 EGGHRVPALAYWPGrVPANVTSTALLSLLDIFPTVIALAGASLPPNrkFDGRDVSEVLFGKS-QMGHRVLFHPNSGAAGE 416
Cdd:cd16171 250 EGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLLSESSiKESPSRVPHPDWVLSEF 326
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1039738450 417 YG-----ALQTVRLNHYKafYITGGakacDGSvgpeqhHVAPLIFNLEDAAD 463
Cdd:cd16171 327 HGcnvnaSTYMLRTNSWK--YIAYA----DGN------SVPPQLFDLSKDPD 366
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
28-391 |
1.45e-13 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 73.15 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 28 SGKTRAPQPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVthnfA 107
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGS----P 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 108 VTSVGGLPVNetTLAEVLRQEGYVTAMIgkwHlGHHGS------YHPNFrGFDYYFGIpysNDMGctdapgynyppcpac 181
Cdd:COG1368 303 YKRPGQNNFP--SLPSILKKQGYETSFF---H-GGDGSfwnrdsFYKNL-GFDEFYDR---EDFD--------------- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 182 PQRDGLWRnpgrdcYTDvaLPLYEnlniveqpvnlsglaqkyaeravEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLA 261
Cdd:COG1368 358 DPFDGGWG------VSD--EDLFD-----------------------KALEELEKLKKPFFAFLITLSNHGPYTLPEEDK 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 262 H-----PQRQSLYRASLREMDSLVGQIKDKVDHVAR-ENTLLWFTGDngpwaqkcelagsvgpffglwqtHQGGSPTKQT 335
Cdd:COG1368 407 KipdygKTTLNNYLNAVRYADQALGEFIEKLKKSGWyDNTIFVIYGD-----------------------HGPRSPGKTD 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738450 336 TWE--GGHRVPALAYWPGRVPANVTSTaLLSLLDIFPTVIALAGASLPPNRKFdGRDV 391
Cdd:COG1368 464 YENplERYRVPLLIYSPGLKKPKVIDT-VGSQIDIAPTLLDLLGIDYPSYYAF-GRDL 519
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
13-304 |
6.33e-08 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 54.75 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 13 MAFSGFFYPLVDFSISGKTRAPQPNIVIILADDMGWGDLGANwaetkDTTNLDKMASEGMRFVDFHAA--ASTCsPSRAS 90
Cdd:COG1524 1 MKRGLSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLLERA-----HAPNLAALAARGVYARPLTSVfpSTTA-PAHTT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 91 LLTGRLGLRNGVTHNFAVTSVGGLPVNE----------------TTLAEVLRQEGYVTAMIGKWHLGHHGSYHPN----F 150
Cdd:COG1524 75 LLTGLYPGEHGIVGNGWYDPELGRVVNSlswvedgfgsnsllpvPTIFERARAAGLTTAAVFWPSFEGSGLIDAArpypY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 151 RGFDYYFGIPYSNdmgctdapgynyppcpacpqrdglwrnpgrdcytdvalplyenlniveqpvnlsglaqkyaERAVEF 230
Cdd:COG1524 155 DGRKPLLGNPAAD-------------------------------------------------------------RWIAAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 231 IEQASTSGRPFLLYVGL------AHMHVPLSvtpplahPQrqslYRASLREMDSLVGQIKDKVD-HVARENTLLWFTGDN 303
Cdd:COG1524 174 ALELLREGRPDLLLVYLpdldyaGHRYGPDS-------PE----YRAALREVDAALGRLLDALKaRGLYEGTLVIVTADH 242
|
.
gi 1039738450 304 G 304
Cdd:COG1524 243 G 243
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
36-377 |
1.48e-07 |
|
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: 53.07 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 36 PNIVIILADdmGWGDLGANW-AETKDTT-NLDKMASEGMRFVDFHAAASTCSPSRA--SLLTGRLGLRNGvthnfAVTSV 111
Cdd:cd16015 1 PNVIVILLE--SFSDPYIDKdVGGEDLTpNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLG-----SGSYT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 112 GGLPVNETTLAEVLRQEGYVTAMIgkwHlGHHGS------YHPNFrGFDYYFGIpysNDMGCTDapgynyppcpacPQRD 185
Cdd:cd16015 74 LYKLNPLPSLPSILKEQGYETIFI---H-GGDASfynrdsVYPNL-GFDEFYDL---EDFPDDE------------KETN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 186 GLWrnpgrdcYTDVALplyenlniveqpvnlsglaqkyAERAVEFIEqaSTSGRPFLLYVGLAHMHVPLSV--------T 257
Cdd:cd16015 134 GWG-------VSDESL----------------------FDQALEELE--ELKKKPFFIFLVTMSNHGPYDLpeekkdepL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738450 258 PPLAHPQRQSLYRASLREMDSLVGQIKDKVDHV-ARENTLLWFTGDngpwaqkcelagsvgpffglwqtHQGGSPTKQTT 336
Cdd:cd16015 183 KVEEDKTELENYLNAIHYTDKALGEFIEKLKKSgLYENTIIVIYGD-----------------------HLPSLGSDYDE 239
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1039738450 337 WEGG----HRVPALAYWPGRVPANVTSTaLLSLLDIFPTVIALAG 377
Cdd:cd16015 240 TDEDpldlYRTPLLIYSPGLKKPKKIDR-VGSQIDIAPTLLDLLG 283
|
|
| |
