|
Name |
Accession |
Description |
Interval |
E-value |
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
35-500 |
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: 601.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 35 KPNFVIILADDMGWGDLGANWAET-KDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGG 113
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNaILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 114 LPLNETTLAEVLQQAGYVTGMIGKWHLGHHGPYHPNFRGFDYYFGIPYSHDmgctdtpgynhppcpacprgdrpsrsler 193
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 194 dcytdvalplyenlniveqpvnlSSLAHKYAEKAIQFIQHASASGRPFLLYMGLAHMHVPISRTQL-SADLRGRRPYGAG 272
Cdd:cd16161 132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRfQSPTSGRGPYGDA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 273 LREMDSLVGQIKDKVDR-TAKENTFLWFTGDNGPWAQKCELAgsVGPFTGLWQTHQGGSPAKQTTWEGGHRVPALAYWPG 351
Cdd:cd16161 189 LQEMDDLVGQIMDAVKHaGLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 352 RVPVNVTSTALLSVLDIFPTVVALAGASLPQDRHFDGLDASEVLFGWSQTGHRepavitlagdlaatvtraqhgscspme 431
Cdd:cd16161 267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHR--------------------------- 319
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953410506 432 tlnhVLFHPNSGAAGeFGALQTVRLGSYKVFYVSGGAKACDGDVGREQHHDPPLIFNLEDDVAEAVPLD 500
Cdd:cd16161 320 ----CLFHPNSGAAG-AGALSAVRCGDYKAHYATGGALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT 383
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-499 |
5.80e-170 |
|
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: 487.46 E-value: 5.80e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGG 113
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 114 LPLNETTLAEVLQQAGYVTGMIGKWHLGHHGPYHPNFRGFDYYFGIPYSHDMGCTDTPGYNHPPCPAcprgdrpsrsler 193
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 194 dcytdvalPLYENLNIVEQPVNLSSLAHKYAEKAIQFIQhaSASGRPFLLYMGLAHMHVPISRTQLSADLRGRRPYGAGL 273
Cdd:cd16026 148 --------PLMENEEVIEQPADQSSLTQRYTDEAVDFIE--RNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 274 REMDSLVGQIKDKVDRT-AKENTFLWFTGDNGPWAQKCELAGSVGPFTGlwqthqggspAKQTTWEGGHRVPALAYWPGR 352
Cdd:cd16026 218 EELDWSVGRILDALKELgLEENTLVIFTSDNGPWLEYGGHGGSAGPLRG----------GKGTTWEGGVRVPFIAWWPGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 353 VPVNVTSTALLSVLDIFPTVVALAGASLPQDRHFDGLDASEVLFGWSQTGHREpavitlagdlaatvtraqhgscspmet 432
Cdd:cd16026 288 IPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHP--------------------------- 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953410506 433 lnhVLFHPNSgaagefGALQTVRLGSYKVFYVSGGAKACDGDVGREQHHDPPLIFNLEDDVAEAVPL 499
Cdd:cd16026 341 ---FFYYYDG------GDLQAVRSGRWKLHLPTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGETYNV 398
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
35-546 |
1.58e-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: 348.67 E-value: 1.58e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGG 113
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGvFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 114 LPLNETTLAEVLQQAGYVTGMIGKWHL--GHHGPYHPNFRGFDYYFGIPYSHDMG-CTDTPGYnhPPCPACPRGDRPSrs 190
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLgvGLNGTYLPTHQGFDHYLGIPYSHDQGpCQNLTCF--PPNIPCFGGCDQG-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 191 lerdcytDVALPLYENLNIVEQPVNLSSLAHKYAEKAIQFIQHASASGRPFLLYMGLAHMHVPISRTQLSADLRGRRPYG 270
Cdd:cd16158 157 -------EVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 271 AGLREMDSLVGQIKDKVDRTA-KENTFLWFTGDNGPWAQKCELAGSvgpfTGLWQTHQGgspakqTTWEGGHRVPALAYW 349
Cdd:cd16158 230 DALAELDGSVGELLQTLKENGiDNNTLVFFTSDNGPSTMRKSRGGN----AGLLKCGKG------TTYEGGVREPAIAYW 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 350 PGRVPVNVTStALLSVLDIFPTVVALAGASLPqDRHFDGLDASEVLFGWSQtghrepavitlagdlaatvtraqhgscSP 429
Cdd:cd16158 300 PGRIKPGVTH-ELASTLDILPTIAKLAGAPLP-NVTLDGVDMSPILFEQGK---------------------------SP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 430 METLnhvLFHPNSgAAGEFGALqTVRLGSYKVFYVSGGA--------KACDGDVGReQHHDPPLIFNLEDDVAEAVPLDR 501
Cdd:cd16158 351 RQTF---FYYPTS-PDPDKGVF-AVRWGKYKAHFYTQGAahsgttpdKDCHPSAEL-TSHDPPLLFDLSQDPSENYNLLG 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1953410506 502 GSaEYQDVLPKVREILADVLLDIA-GDntSRADYTRHPSVTPCCNP 546
Cdd:cd16158 425 LP-EYNQVLKQIQQVKERFEASMKfGE--SEINKGEDPALEPCCKP 467
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
35-518 |
1.86e-109 |
|
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: 334.40 E-value: 1.86e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV---THNFAVTSV 111
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 112 GGLPLNETTLAEVLQQAGYVTGMIGKWHLG-----HHGPYH-PNFRGFDYY-FGIPYSHDMGCTDTPGYNhppcpacprg 184
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDFVgTNLPFTNSWACDDTGRHV---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 185 DRPSRSLerdCYtdvalpLYENLNIVEQPVNLSSLAHKYAEKAIQFIqHASASgRPFLLYMGLAHMHVPI--SRTQLSAD 262
Cdd:cd16160 151 DFPDRSA---CF------LYYNDTIVEQPIQHEHLTETLVGDAKSFI-EDNQE-NPFFLYFSFPQTHTPLfaSKRFKGKS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 263 LRGRrpYGAGLREMDSLVGQIKDK-VDRTAKENTFLWFTGDNGPWAQKCELAGSVGPFTGlwqthqggspAKQTTWEGGH 341
Cdd:cd16160 220 KRGR--YGDNINEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKG----------GKGNSWEGGI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 342 RVPALAYWPGRVPVNVtSTALLSVLDIFPTVVALAGASLPQDRHFDGLDASEVLFGWSQTGHREpavitlagdlaatvtr 421
Cdd:cd16160 288 RVPFIAYWPGTIKPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDD---------------- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 422 aqhgscspmetlnhVLFHPNSgaagefgALQTVRLGSYKVFYVSGG-------AKACDGDVGREQH-------------H 481
Cdd:cd16160 351 --------------ILYYCCS-------RLMAVRYGSYKIHFKTQPlpsqeslDPNCDGGGPLSDYivcydcedecvtkH 409
|
490 500 510
....*....|....*....|....*....|....*..
gi 1953410506 482 DPPLIFNLEDDVAEAVPLdrGSAEYQDVLPKVREILA 518
Cdd:cd16160 410 NPPLIFDVEKDPGEQYPL--QPSVYEHMLEAVEKLIA 444
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-519 |
2.56e-99 |
|
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: 309.01 E-value: 2.56e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG--VTHNFAVTS-- 110
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 111 ----VGGLPLNETTLAEVLQQAGYVTGMIGKWHLGHHGPYHPNFRGFDYYFGIPYSHdMGCTDTPgynhppcpacprgDR 186
Cdd:cd16157 81 pqniVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCH-FGPYDNK-------------AY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 187 PSRSLERDcyTDVALPLYENLNIvEQPVNLSSLAHKYAEKAIQFIQHASASGRPFLLYMGLAHMHVPI--SRTQLSADLR 264
Cdd:cd16157 147 PNIPVYRD--WEMIGRYYEEFKI-DKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVyaSKPFLGTSQR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 265 GRrpYGAGLREMDSLVGQIKDKVDRTA-KENTFLWFTGDNG-PWAQKCELAGSVGPFTGlwqthqggspAKQTTWEGGHR 342
Cdd:cd16157 224 GL--YGDAVMELDSSVGKILESLKSLGiENNTFVFFSSDNGaALISAPEQGGSNGPFLC----------GKQTTFEGGMR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 343 VPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPQDRHFDGLDASEVLFgwsqTGHrepavitlagdlaatvtra 422
Cdd:cd16157 292 EPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLL----NGK------------------- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 423 qhgscspmETLNHVLFHPNSgaagefgALQTVRLGSYKVFY---------VSGGAKACDG-DVG------REQHHDPPLI 486
Cdd:cd16157 349 --------EKDRPIFYYRGD-------ELMAVRLGQYKAHFwtwsnsweeFRKGINFCPGqNVPgvtthnQTDHTKLPLL 413
|
490 500 510
....*....|....*....|....*....|...
gi 1953410506 487 FNLEDDVAEAVPLDRGSAEYQDVLPKVREILAD 519
Cdd:cd16157 414 FHLGRDPGEKYPISFKSAEYKQAMPRISKVVQQ 446
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
35-519 |
6.32e-99 |
|
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: 309.99 E-value: 6.32e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN------FAV 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASShgmrviLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 109 TSVGGLPLNETTLAEVLQQAGYVTGMIGKWHLGHH------GPYHPNFRGFDYYFGIPYSHDMGCTDTPG----YNHPP- 177
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHcesrndFCHHPLNHGFDYFYGLPLTNLKDCGDGSNgeydLSFDPl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 178 -------CPAC-----------PRGDRPSRSLERDCYTDVALP-------------LYENLNIVEQPVNLSSLAHKYAEK 226
Cdd:cd16159 161 fplltafVLITaltiflllylgAVSKRFFVFLLILSLLFISLFflllitnryfnciLMRNHEVVEQPMSLENLTQRLTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 227 AIQFIQhaSASGRPFLLYMGLAHMHVPISRTQLSADLRGRRPYGAGLREMDSLVGQIKDKVDRTA-KENTFLWFTGDNGP 305
Cdd:cd16159 241 AISFLE--RNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGlKDNTFVYFTSDNGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 306 WAqkcELAGSVGPFTGLWQTHQGGSpaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPQDRH 385
Cdd:cd16159 319 HL---EEISVGGEYGGGNGGIYGGK--KMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 386 FDGLDASEVLFGwsQTGHrepavitlagdlaatvtraqhgscSPMETLNH--------VLFHPNSGAAgefgalqtvrlg 457
Cdd:cd16159 394 IDGRDLMPLLTG--QEKR------------------------SPHEFLFHycgaelhaVRYRPRDGGA------------ 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953410506 458 SYKVFYVS----GGAKACDG------DVGREQHHDPPLIFNLEDDVAEAVPLDRGSAEYQDVLPKVREILAD 519
Cdd:cd16159 436 VWKAHYFTpnfyPGTEGCCGtllcrcFGDSVTHHDPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAE 507
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-417 |
1.58e-91 |
|
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: 285.58 E-value: 1.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGAN---WAETKDTANLDKMAAEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHNFAVTSVG 112
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYgggIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 113 GLPLNETTLAEVLQQAGYVTGMIGKWHLGHHgPYH-PNFRGFDYYFGIPYSHDmgctdtpgynhppcpacprgdrpsrsl 191
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGDE-DGRlPTDHGFDEFYGNLYHTI--------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 192 erDCYtdvalplyenlniveqpvnlsslahkYAEKAIQFIQHASASGRPFLLYMGLAHMHVPisrTQLSADLRGRRP--- 268
Cdd:cd16142 132 --DEE--------------------------IVDKAIDFIKRNAKADKPFFLYVNFTKMHFP---TLPSPEFEGKSSgkg 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 269 -YGAGLREMDSLVGQIKDKVDRTA-KENTFLWFTGDNGPWAQKCELAGSvGPFTGlwqthqggspAKQTTWEGGHRVPAL 346
Cdd:cd16142 181 kYADSMVELDDHVGQILDALDELGiADNTIVIFTTDNGPEQDVWPDGGY-TPFRG----------EKGTTWEGGVRVPAI 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953410506 347 AYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLP------QDRHFDGLDASEVLFGWSQTGHREPAVITLAGDLAA 417
Cdd:cd16142 250 VRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGA 326
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-406 |
7.14e-86 |
|
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: 272.88 E-value: 7.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--------- 106
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIpgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 107 ----AVTSVGGLPLNETTLAEVLQQAGYVTGMIGKWHLGHHGPYHPNFRGFDYYFGI-PYSHDMGCTDTPGYNHPPCPAC 181
Cdd:cd16144 81 tkliPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIGGtGNGGPPSYYFPPGKPNPDLEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 182 PRGDRPSRSLerdcytdvalplyenlniveqpvnlsslahkyAEKAIQFIQhaSASGRPFLLYmgLAH--MHVPI-SRTQ 258
Cdd:cd16144 161 PEGEYLTDRL--------------------------------TDEAIDFIE--QNKDKPFFLY--LSHyaVHTPIqARPE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 259 LSADLRGRRP----------YGAGLREMDSLVGQIKDKVDRTA-KENTFLWFTGDNGPWAQKCELAGSVGPFTGlwqthq 327
Cdd:cd16144 205 LIEKYEKKKKglrkgqknpvYAAMIESLDESVGRILDALEELGlADNTLVIFTSDNGGLSTRGGPPTSNAPLRG------ 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953410506 328 ggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPQDRHFDGLDASEVLFGWSQTGHREP 406
Cdd:cd16144 279 ----GKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRA 353
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
34-519 |
3.54e-82 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 262.12 E-value: 3.54e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvTSVGG 113
Cdd:COG3119 22 KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE-GYNGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 114 LPLNETTLAEVLQQAGYVTGMIGKWHLghhgpyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacprgdrpsrsler 193
Cdd:COG3119 101 LPPDEPTLAELLKEAGYRTALFGKWHL----------------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 194 dcYTDvalplyenlniveqpvnlsslaHKYAEKAIQFIQHASASGRPFLLYMGLAHMHVPISRTQLSADL---------- 263
Cdd:COG3119 128 --YLT----------------------DLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplpp 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 264 -------------RGRRPYGAGLREMDSLVGQIKDKVDRT-AKENTFLWFTGDNGPWAQKcelagsvgpftglwQTHQGG 329
Cdd:COG3119 184 nlaprdlteeelrRARAAYAAMIEEVDDQVGRLLDALEELgLADNTIVVFTSDNGPSLGE--------------HGLRGG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 330 spaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPQDrhFDGLDASEVLFGwSQTGHREPAVi 409
Cdd:COG3119 250 ---KGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTG-EKAEWRDYLY- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 410 tlagdlaatvtrAQHGSCSPMetlnhvlfhpnsgaagefgalQTVRLGSYKVFYvsggakacdgdvgREQHHDPPLIFNL 489
Cdd:COG3119 323 ------------WEYPRGGGN---------------------RAIRTGRWKLIR-------------YYDDDGPWELYDL 356
|
490 500 510
....*....|....*....|....*....|
gi 1953410506 490 EDDVAEAVPLdrgSAEYQDVLPKVREILAD 519
Cdd:COG3119 357 KNDPGETNNL---AADYPEVVAELRALLEA 383
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-495 |
2.96e-80 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 257.13 E-value: 2.96e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETK-DTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGL 114
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGG--VLGGFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 115 PL---NETTLAEVLQQAGYVTGMIGKWHLG---------HHGPYH-------------PNFRGFDYYFGIPYShdmgctd 169
Cdd:cd16143 79 PLiepDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkKAATGTgkdvdyskpikggPLDHGFDYYFGIPAS------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 170 tpgynhppcpacprgdrpsrslerdcytDVaLPLyenlniveqpvnlsslahkYAEKAIQFIQHASASGRPFLLYMGLAH 249
Cdd:cd16143 152 ----------------------------EV-LPT-------------------LTDKAVEFIDQHAKKDKPFFLYFALPA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 250 MHVPISRtqlSADLRGRR---PYGAGLREMDSLVGQIKDKVDRTA-KENTFLWFTGDNGP----WAQKCELAG--SVGPF 319
Cdd:cd16143 184 PHTPIVP---SPEFQGKSgagPYGDFVYELDWVVGRILDALKELGlAENTLVIFTSDNGPspyaDYKELEKFGhdPSGPL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 320 TGLwqthqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPQDRHFDGLDASEVLFGWS 399
Cdd:cd16143 261 RGM----------KADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPK 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 400 QTGHREPAVItlagdlaatvtraqhgscspmetlnhvlfHPNSGAagefgalQTVRLGSYKVFYVSGGAKACDGDVGREQ 479
Cdd:cd16143 331 KQEVRESLVH-----------------------------HSGNGS-------FAIRKGDWKLIDGTGSGGFSYPRGKEKL 374
|
490
....*....|....*.
gi 1953410506 480 HHDPPLIFNLEDDVAE 495
Cdd:cd16143 375 GLPPGQLYNLSTDPGE 390
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
36-397 |
6.44e-76 |
|
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: 246.31 E-value: 6.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTHnfavTSVGG-- 113
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWH----TILGRer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 114 LPLNETTLAEVLQQAGYVTGMIGKWHLGHHGPYHPNFRGFDYYFGIPYSHDmgcTDTPGY--NHPPCPACPRGDRPSRSl 191
Cdd:cd16146 76 MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGGGI---GQYPDYwgNDYFDDTYYHNGKFVKT- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 192 ERDCyTDValplyenlniveqpvnlsslahkYAEKAIQFIQhaSASGRPFLLYMGLAHMHVPisrtqLSADLRGRRPY-G 270
Cdd:cd16146 152 EGYC-TDV-----------------------FFDEAIDFIE--ENKDKPFFAYLATNAPHGP-----LQVPDKYLDPYkD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 271 AGLRE-----------MDSLVGQIKDKVDRT-AKENTFLWFTGDNGPWaqkcelagsvGPFTGLWQTHQGGSpaKQTTWE 338
Cdd:cd16146 201 MGLDDklaafygmienIDDNVGRLLAKLKELgLEENTIVIFMSDNGPA----------GGVPKRFNAGMRGK--KGSVYE 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953410506 339 GGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPQDRHFDGLDASEVLFG 397
Cdd:cd16146 269 GGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKG 327
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-389 |
5.02e-71 |
|
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: 233.64 E-value: 5.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGLP 115
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 116 LNETTLAEVLQQAGYVTGMIGKWHLG-HHGPYHPNFRGFDYYFGIpYSHdmgctdTPGYNH-PPcpacprgdrpsrSLER 193
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGgPGTPGHPTKQGFDYFYGY-LDQ------VHAHNYyPE------------YLWR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 194 DcytDVALPLYENLNIVEQPVNLSSLAHK-YAE-----KAIQFIQ-HASasgRPFLLYMGL----AHMHVP--------I 254
Cdd:cd16145 142 N---GEKVPLPNNVIPPLDEGNNAGGGGGtYSHdlftdEALDFIReNKD---KPFFLYLAYtlphAPLQVPddgpykykP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 255 SRTQLSADLRGRRP---YGAGLREMDSLVGQIKDKVDRTA-KENTFLWFTGDNGP-----WAQKCELAGSVGPFTGLwqt 325
Cdd:cd16145 216 KDPGIYAYLPWPQPekaYAAMVTRLDRDVGRILALLKELGiDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY--- 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953410506 326 hqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPQDrhFDGL 389
Cdd:cd16145 293 -------KRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGI 347
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
36-390 |
1.24e-68 |
|
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: 221.54 E-value: 1.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGLP 115
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 116 LNETTLAEVLQQAGYVTGMIGKWHlghhgpyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacprgdrpsrslerdc 195
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 196 ytdvalplyenlniveqpvnlsslahkyaEKAIQFIQHASASgRPFLLYMGLAHMHVPISrtqlsadlrgrrpYGAGLRE 275
Cdd:cd16022 103 -----------------------------DEAIDFIERRDKD-KPFFLYVSFNAPHPPFA-------------YYAMVSA 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 276 MDSLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaqkcelaGSVGPFTGLWQthqggspaKQTTWEGGHRVPALAYWPGRVP 354
Cdd:cd16022 140 IDDQIGRILDALEELGLlDNTLIVFTSDHG---------DMLGDHGLRGK--------KGSLYEGGIRVPFIVRWPGKIP 202
|
330 340 350
....*....|....*....|....*....|....*.
gi 1953410506 355 VNVTSTALLSVLDIFPTVVALAGASLPqdRHFDGLD 390
Cdd:cd16022 203 AGQVSDALVSLLDLLPTLLDLAGIEPP--EGLDGRS 236
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
36-390 |
9.47e-65 |
|
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: 216.65 E-value: 9.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFvDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSV-GGL 114
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVIL-NNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEpYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 115 PLNETTLAEVLQQAGYVTGMIGKWHLGHHGPYH-PNFRGFDYYFGiPYShdmGCTDtpGYNHPPCPACPRGDRPSRSLE- 192
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYTWEYtPTNRGFDSFYG-YYG---GAED--YYTHTSGGANDYGNDDLRDNEe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 193 -----RDCYTdvalplyenlniveqpvnlsslAHKYAEKAIQFIQHASASgRPFLLYMGLAHMHVPISRTQLSADL---- 263
Cdd:cd16029 154 pawdyNGTYS----------------------TDLFTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPyedk 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 264 ------RGRRPYGAGLREMDSLVGQIKDK-VDRTAKENTFLWFTGDNGPWAQKCElAGSVGPFTGlwqthqggspAKQTT 336
Cdd:cd16029 211 fahikdEDRRTYAAMVSALDESVGNVVDAlKAKGMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRG----------GKNTL 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1953410506 337 WEGGHRVPALAYWPGRVPV-NVTSTALLSVLDIFPTVVALAGASLPQDRHFDGLD 390
Cdd:cd16029 280 WEGGVRVPAFVWSPLLPPKrGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVD 334
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-405 |
2.87e-59 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 201.67 E-value: 2.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHnfavtsvGGLP 115
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPL-CTPSRVQLMTGKYNFRNYVVF-------GYLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 116 LNETTLAEVLQQAGYVTGMIGKWHLG---HHGPYHPNFrGFDYYFGIPYSHdmgcTDTPGYNHPPcpacprgdrpsrsLE 192
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGKWQLGggrGDGDYPHEF-GFDEYCLWQLTE----TGEKYSRPAT-------------PT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 193 RDCYTDVALPLYENlniveqpvnlsslahKY-----AEKAIQFIQHASAsgRPFLLY--MGLAH---MHVPISR-TQLSA 261
Cdd:cd16151 135 FNIRNGKLLETTEG---------------DYgpdlfADFLIDFIERNKD--QPFFAYypMVLVHdpfVPTPDSPdWDPDD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 262 DLRGRRP--YGAGLREMDSLVGQIKDKVDRTA-KENTFLWFTGDNgpwaqkcelaGSVGPFTGLW--QTHQGGspaKQTT 336
Cdd:cd16151 198 KRKKDDPeyFPDMVAYMDKLVGKLVDKLEELGlRENTIIIFTGDN----------GTHRPITSRTngREVRGG---KGKT 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953410506 337 WEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPQDRHFDGLDASEVLFGWSQTGHRE 405
Cdd:cd16151 265 TDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRRE 333
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
36-378 |
1.68e-56 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 191.87 E-value: 1.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtSVGGLP 115
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS----TPVGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 116 LNETTLAEVLQQAGYVTGMIGKWHLGHHGPYHPNFRGFDYYFG-IPYSHDMGCTDTPGYNHPPcpacprgdrpsrsleRD 194
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLYADPPDVPYNCSG---------------GG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 195 CYTDValplyenlniveqpvnlsslahkYAEKAIQFIQHASasgRPFLLYMGLAHMHVP-----------ISRTQLSADL 263
Cdd:pfam00884 142 VSDEA-----------------------LLDEALEFLDNND---KPFFLVLHTLGSHGPpyypdrypekyATFKPSSCSE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 264 RG-RRPYGAGLREMDSLVGQIKDKVDRTAK-ENTFLWFTGDNGPwaqkcelagSVGPFTGLWQTHQGGspakqTTWEGGH 341
Cdd:pfam00884 196 EQlLNSYDNTLLYTDDAIGRVLDKLEENGLlDNTLVVYTSDHGE---------SLGEGGGYLHGGKYD-----NAPEGGY 261
|
330 340 350
....*....|....*....|....*....|....*..
gi 1953410506 342 RVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGA 378
Cdd:pfam00884 262 RVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
34-381 |
5.66e-54 |
|
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: 188.04 E-value: 5.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 34 QKPNFVIILADDMGWGDLGANWAETkDTANLDKMAAEGMRFVDFHAAAsTCSPSRASLLTGRLGLRNGV-THNFAVTSVG 112
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEI-PTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQVGMgTMAELATGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 113 G----LPLNETTLAEVLQQAGYVTGMIGKWHLGHHgpyhpnfrgfDYYFgipySHDmgctdtpgynhppcpacprgdrps 188
Cdd:cd16025 79 GyegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------DYYS----TDD------------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 189 rslerdcytdvalplyenlniveqpvnlsslahkYAEKAIQFIQHASASGRPFLLYM--GLAH--MHVP---ISR----- 256
Cdd:cd16025 121 ----------------------------------LTDKAIEYIDEQKAPDKPFFLYLafGAPHapLQAPkewIDKykgky 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 257 ------------------------TQLSADLRGRRP------------------YGAGLREMDSLVGQIKDKVDRTAK-E 293
Cdd:cd16025 167 dagwdalreerlerqkelglipadTKLTPRPPGVPAwdslspeekklearrmevYAAMVEHMDQQIGRLIDYLKELGElD 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 294 NTFLWFTGDNGP-----WAQkcelAGSvGPFTGlwqthqggspAKQTTWEGGHRVPALAYWPGRV-PVNVTSTALLSVLD 367
Cdd:cd16025 247 NTLIIFLSDNGAsaepgWAN----ASN-TPFRL----------YKQASHEGGIRTPLIVSWPKGIkAKGGIRHQFAHVID 311
|
410
....*....|....
gi 1953410506 368 IFPTVVALAGASLP 381
Cdd:cd16025 312 IAPTILELAGVEYP 325
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
36-405 |
2.35e-49 |
|
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: 175.00 E-value: 2.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGA--NWAETkdtANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFavTSVGG 113
Cdd:cd16027 1 PNILWIIADDLSPDLGGYggNVVKT---PNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR--SRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 114 LPLNETTLAEVLQQAGYVTGMIGKWhlghHGPYHPNFRGFDYYFGIPYSHDMgctdtpgynhppcpacprgdrpsrsler 193
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKT----HYNPDAVFPFDDEMRGPDDGGRN---------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 194 dcytdvalplyenlniveqpvnlsslAHKYAEKAIQFIQHAsASGRPFLLYMGLAHMHVPisRTQLSADLRGRRP----- 268
Cdd:cd16027 124 --------------------------AWDYASNAADFLNRA-KKGQPFFLWFGFHDPHRP--YPPGDGEEPGYDPekvkv 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 269 ----------------YGAGLREMDSLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaqkcelagsvGPFTGlwqthqggsp 331
Cdd:cd16027 175 ppylpdtpevredladYYDEIERLDQQVGEILDELEEDGLlDNTIVIFTSDHG------------MPFPR---------- 232
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953410506 332 AKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPQdrHFDGLDASEVLFGWSQTGHRE 405
Cdd:cd16027 233 AKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPE--YLQGRSFLPLLKGEKDPGRDY 304
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-397 |
1.31e-48 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 173.52 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggL 114
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 115 PLNETTLAEVLQQAGYVTGMIGKWHL-GHHGPYH--------PNFR-GFDYYFGipyshdMGCTDtpGYNHPpcpacPRG 184
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGraddytppPERRhGFDYWKG------YECNH--DHNNP-----HYY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 185 DRPSRSLERDCYTDVALplyenlniveqpvnlsslahkyAEKAIQFIQHASASGRPFLLY--MGLAH------------M 250
Cdd:cd16034 143 DDDGKRIYIKGYSPDAE----------------------TDLAIEYLENQADKDKPFALVlsWNPPHdpyttapeeyldM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 251 HVPISRTqLSADLRGRRPYGAGLREM-----------DSLVGQIKDKVDRTA-KENTFLWFTGDNGpwaqkcELAGSvgp 318
Cdd:cd16034 201 YDPKKLL-LRPNVPEDKKEEAGLREDlrgyyamitalDDNIGRLLDALKELGlLENTIVVFTSDHG------DMLGS--- 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953410506 319 ftglwqtHqgGSPAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGasLPQDRHFDGLDASEVLFG 397
Cdd:cd16034 271 -------H--GLMNKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCG--LPIPDTVEGRDLSPLLLG 338
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
34-405 |
2.84e-43 |
|
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: 159.62 E-value: 2.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvGG 113
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG----PL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 114 LPLNETTLAEVLQQAGYVTGMIGKWHLGHHGpYHPNfRGFDYYFGIPyshdmGctdtPGYNHPPCPACPRGDRPSRSLER 193
Cdd:cd16031 77 FDASQPTYPKLLRKAGYQTAFIGKWHLGSGG-DLPP-PGFDYWVSFP-----G----QGSYYDPEFIENGKRVGQKGYVT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 194 DCYTDvalplyenlniveqpvnlsslahkyaeKAIQFIQHASASgRPFLLYMG--LAH---------------MHVPISR 256
Cdd:cd16031 146 DIITD---------------------------KALDFLKERDKD-KPFCLSLSfkAPHrpftpaprhrglyedVTIPEPE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 257 TQLSADLRGR-----------------------------RPYGAGLREMDSLVGQIKDKVDRTAK-ENTFLWFTGDNGpw 306
Cdd:cd16031 198 TFDDDDYAGRpewareqrnrirgvldgrfdtpekyqrymKDYLRTVTGVDDNVGRILDYLEEQGLaDNTIIIYTSDNG-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 307 aqkcelagsvgpFT----GLwqthqGGspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPq 382
Cdd:cd16031 276 ------------FFlgehGL-----FD---KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIP- 334
|
410 420
....*....|....*....|...
gi 1953410506 383 dRHFDGLDASEVLFGWSQTGHRE 405
Cdd:cd16031 335 -EDMQGRSLLPLLEGEKPVDWRK 356
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-384 |
5.95e-42 |
|
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: 151.24 E-value: 5.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV-----THNFAVTS 110
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 111 VG-GLPLNETTLAEVLQQAGYVTGMIGKWHLGhhgpyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacprgdrpsr 189
Cdd:cd16149 81 KPeGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 190 slerdcytdvalplyenlniveqpvnlsslahkyaEKAIQFIQHASASGRPFLLYMGLAHMHVPISrtqlsadlrgrrpY 269
Cdd:cd16149 113 -----------------------------------DDAADFLRRRAEAEKPFFLSVNYTAPHSPWG-------------Y 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 270 GAGLREMDSLVGQIKDKVDRTA-KENTFLWFTGDNGpwaqkcelagsvgpFT----GLWQTHQGGSPakQTTWEGGHRVP 344
Cdd:cd16149 145 FAAVTGVDRNVGRLLDELEELGlTENTLVIFTSDNG--------------FNmghhGIWGKGNGTFP--LNMYDNSVKVP 208
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1953410506 345 ALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPQDR 384
Cdd:cd16149 209 FIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADP 248
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-404 |
2.88e-40 |
|
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: 150.19 E-value: 2.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWgDLGANWAETKD---TANLDKMAAEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVThnfavtSVG 112
Cdd:cd16154 1 PNILLIIADDQGL-DSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVL------AVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 113 G-LPLNETTL--AEVLQQ--AGYVTGMIGKWHLGHHGPYHPNFRGFDYYFGIpyshdmgctdTPGynhppcpacprgdrp 187
Cdd:cd16154 73 DeLLLSEETLlqLLIKDAttAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGI----------LGG--------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 188 srslerdcytdvALPLYENLNIVEQPVNLSSlaHKYA-----EKAIQFIQHASasgRPFLLYMGLAHMHVPI-------- 254
Cdd:cd16154 128 ------------GVQDYYNWNLTNNGQTTNS--TEYAttkltNLAIDWIDQQT---KPWFLWLAYNAPHTPFhlppaelh 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 255 SRTQL--SADLRG-RRP-YGAGLREMDSLVGQIKDKVDRTAKENTFLWFTGDNG-PwaqkcelagsvGPFTGLWQTHQGg 329
Cdd:cd16154 191 SRSLLgdSADIEAnPRPyYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGtP-----------GQVVDLPYTRNH- 258
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953410506 330 spAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPQdrHFDGLDASEVLFGWSQTGHR 404
Cdd:cd16154 259 --AKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNASTRQ 329
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
35-388 |
7.61e-37 |
|
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: 141.15 E-value: 7.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 35 KPNFVIILADDMGWgDLGANWAETKdTANLdkMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtSVGGL 114
Cdd:cd16147 1 RPNIVLILTDDQDV-ELGSMDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSP--PGGGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 115 P------LNETTLAEVLQQAGYVTGMIGK----WHLGHHGPYHPnfRGFDYYFGIPyshdmgcTDTPGYNHppCPACPRG 184
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYVP--PGWDEWDGLV-------GNSTYYNY--TLSNGGN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 185 DRPSRSLERDCYTDValplyenlniveqpvnlsslahkYAEKAIQFIQHASASGRPFLLYMG--LAHMH-VPISRTQ-LS 260
Cdd:cd16147 144 GKHGVSYPGDYLTDV-----------------------IANKALDFLRRAAADDKPFFLVVAppAPHGPfTPAPRYAnLF 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 261 ADLRGRRPYGAG-----------------------------------LREMDSLVGQIKDKVDRTAK-ENTFLWFTGDNG 304
Cdd:cd16147 201 PNVTAPPRPPPNnpdvsdkphwlrrlpplnptqiayidelyrkrlrtLQSVDDLVERLVNTLEATGQlDNTYIIYTSDNG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 305 pwaqkcelagsvgpftglwqTHQGG---SPAKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDIFPTVVALAGASLP 381
Cdd:cd16147 281 --------------------YHLGQhrlPPGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPP 339
|
....*..
gi 1953410506 382 qdRHFDG 388
Cdd:cd16147 340 --SDMDG 344
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-388 |
6.30e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 136.20 E-value: 6.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--AVTSVGG 113
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 114 LPLNETTLAEVLQQAGYVTGMIGKWHLGHHgpYHPNFRGFDYYFgipyshdmgctdtpgynhppcpacprgdrpsrsler 193
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVGPE--ETPLDYGFDEYL------------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 194 dcytdvalplyenlniveqPVNlSSLAHKYAEKAIQFIQHASASGRPFLLYMGLAHMHVP-------------------- 253
Cdd:cd16033 123 -------------------PVE-TTIEYFLADRAIEMLEELAADDKPFFLRVNFWGPHDPyippepyldmydpediplpe 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 254 -----------ISR------TQLSADLRGRRP----YGAGLREMDSLVGQIKDKVDRT-AKENTFLWFTGDNGpwaqkcE 311
Cdd:cd16033 183 sfaddfedkpyIYRrerkrwGVDTEDEEDWKEiiahYWGYITLIDDAIGRILDALEELgLADDTLVIFTSDHG------D 256
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953410506 312 LAGSvgpfTGLWQthQGGSPAKQTtweggHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPQDrhFDG 388
Cdd:cd16033 257 ALGA----HRLWD--KGPFMYEET-----YRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK--VDG 320
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-395 |
1.02e-31 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 126.14 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAAST----CSPSRASLLTGRlglrngvtHNFAVT 109
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGR--------TLFHAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 110 SVGG--LPLNETTLAEVLQQAGYVTGMIGKWHLGhhgpyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacprgdrp 187
Cdd:cd16155 73 EGGKaaIPSDDKTWPETFKKAGYRTFATGKWHNG---------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 188 srslerdcytdvalplyenlniveqpvnlsslahkYAEKAIQFIQHASASGRPFLLYMGLAHMHVPISRTQ--------- 258
Cdd:cd16155 107 -----------------------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPeyldmyppe 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 259 ---LSADLRGRRPYGAGLR-----------------------------EMDSLVGQIKDKVDRTAK-ENTFLWFTGDNGp 305
Cdd:cd16155 152 tipLPENFLPQHPFDNGEGtvrdeqlapfprtpeavrqhlaeyyamitHLDAQIGRILDALEASGElDNTIIVFTSDHG- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 306 waqkceLA-GSvgpfTGLwqthQGgspaKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDIFPTVVALAGASLPQdr 384
Cdd:cd16155 231 ------LAvGS----HGL----MG----KQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPE-- 289
|
410
....*....|.
gi 1953410506 385 HFDGLDASEVL 395
Cdd:cd16155 290 SVEGKSLLPVI 300
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
436-553 |
1.21e-31 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 118.57 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 436 VLFHpNSGAAgefgaLQTVRLGSYKVFYV-----SGGAKACDGDVGREQHHDPPLIFNLEDDVAEAVPLDRGSAEYQDVL 510
Cdd:pfam14707 5 FLFH-YCGAA-----LHAVRWGPYKAHFFtpsfdPPGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYPEVL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1953410506 511 PKVREILADVLLDI--AGDNTSRADYTRHPSVTPCCnPHHVACRC 553
Cdd:pfam14707 79 AEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-390 |
4.99e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 116.11 E-value: 4.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILAD----DMgwgdLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHnfavtsv 111
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWG------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 112 GGLPLNETTLAEVLQQAGYVTGMIGKW-HLGHHGPYHpnfRGFDYYFGIPYSHdmgctdtpgynhppcpacprGDRPSRS 190
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAVSSNpHLFGGPGFD---RGFDTFEDFRGQE--------------------GDPGEEG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 191 LERdcytdvalplyenlniveqpvnlsslAHKYAEKAIQFIQHAsASGRPFLLYMglaHM---HVPisrtqlsadlrgrR 267
Cdd:cd16148 127 DER--------------------------AERVTDRALEWLDRN-ADDDPFFLFL---HYfdpHEP-------------Y 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 268 PYGAGLREMDSLVGQIKDKVDRT-AKENTFLWFTGDNGpwaqkcELAGSvgpfTGLWQTHQggspakQTTWEGGHRVPAL 346
Cdd:cd16148 164 LYDAEVRYVDEQIGRLLDKLKELgLLEDTLVIVTSDHG------EEFGE----HGLYWGHG------SNLYDEQLHVPLI 227
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1953410506 347 AYWPGRVPVNVTStALLSVLDIFPTVVALAGASLPQDrhFDGLD 390
Cdd:cd16148 228 IRWPGKEPGKRVD-ALVSHIDIAPTLLDLLGVEPPDY--SDGRS 268
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
36-492 |
1.13e-28 |
|
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: 116.52 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-----EFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 116 LNETTLAEVLQQAGYVTGMIGKWHLGhhGP--YHpnfrGFDYyfgipyshdmgctdtpgynhppcpacprgDRpsrsler 193
Cdd:cd16032 76 ADIPTFAHYLRAAGYRTALSGKMHFV--GPdqLH----GFDY-----------------------------DE------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 194 dcytDVALplyenlniveqpvnlsslahkyaeKAIQFI-QHA-SASGRPFLLYMGLAHMHVPISRTQLSADL---RGRRP 268
Cdd:cd16032 114 ----EVAF------------------------KAVQKLyDLArGEDGRPFFLTVSFTHPHDPYVIPQEYWDLyvrRARRA 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 269 YGAGLREMDSLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaqkcELAGSvgpfTGLWQthqggspaKQTTWEGGHRVPALA 347
Cdd:cd16032 166 YYGMVSYVDDKVGQLLDTLERTGLaDDTIVIFTSDHG------DMLGE----RGLWY--------KMSFFEGSARVPLII 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 348 YWPGR-VPVNVTstALLSVLDIFPTVVALAGASLPQDR-HFDGLDASEVLFGwSQTGHREPAVITLAGDlaatvtraqhG 425
Cdd:cd16032 228 SAPGRfAPRRVA--EPVSLVDLLPTLVDLAGGGTAPHVpPLDGRSLLPLLEG-GDSGGEDEVISEYLAE----------G 294
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953410506 426 SCSPMetlnhvlfhpnsgaagefgalQTVRLGSYKVFYVsggakacdgdvgreqHHDPPLIFNLEDD 492
Cdd:cd16032 295 AVAPC---------------------VMIRRGRWKFIYC---------------PGDPDQLFDLEAD 325
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-388 |
1.16e-28 |
|
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: 116.10 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggLP 115
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP-----YD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 116 LNETTLAEVLQQAGYVTGMIGKWHLGHHGPYHpnfrGFDYyfgipyshdmgctdtpgynhppcpacprgdrpsrslERDC 195
Cdd:cd16037 76 GDVPSWGHALRAAGYETVLIGKLHFRGEDQRH----GFRY------------------------------------DRDV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 196 ytdvalplyenlniveqpvnlsslahkyAEKAIQFIQHASASGRPFLLYMGLAHMHVPISRTQLSADL---RGRRPYGAG 272
Cdd:cd16037 116 ----------------------------TEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLyvrRARAAYYGL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 273 LREMDSLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaqkcELAGSvgpfTGLWQthqggspaKQTTWEGGHRVPALAYWPG 351
Cdd:cd16037 168 VEFLDENIGRVLDALEELGLlDNTLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMIISGPG 229
|
330 340 350
....*....|....*....|....*....|....*..
gi 1953410506 352 RVPVNVTSTAlLSVLDIFPTVVALAGAslPQDRHFDG 388
Cdd:cd16037 230 IPAGKRVKTP-VSLVDLAPTILEAAGA--PPPPDLDG 263
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
34-410 |
1.27e-28 |
|
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: 118.44 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 34 QKPNFVIILADDM----GWgdLGANWAETkdtANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVtHNFAVT 109
Cdd:cd16030 1 KKPNVLFIAVDDLrpwlGC--YGGHPAKT---PNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGV-YDNNSY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 110 SVGGLPlNETTLAEVLQQAGYVTGMIGKwhlghhgPYHPNFRGFDYYfgiPYSHDMGCTDTPGYNHPPCPACPRGDRPSr 189
Cdd:cd16030 75 FRKVAP-DAVTLPQYFKENGYTTAGVGK-------IFHPGIPDGDDD---PASWDEPPNPPGPEKYPPGKLCPGKKGGK- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 190 slerdcyTDVALPLYENLNIVEqpvnlSSLA-HKYAEKAIQFIQHASASGRPFLLYMGLAHMHVP------------ISR 256
Cdd:cd16030 143 -------GGGGGPAWEAADVPD-----EAYPdGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPfvapkkyfdlypLES 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 257 TQLSA----------------DLRG------------------------RRPYGAGLREMDSLVGQIKDKVDRTA-KENT 295
Cdd:cd16030 211 IPLPNpfdpidlpevawndldDLPKygdipalnpgdpkgplpdeqarelRQAYYASVSYVDAQVGRVLDALEELGlADNT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 296 FLWFTGDNGpWaqkcelagSVGPfTGLWqthqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVAL 375
Cdd:cd16030 291 IVVLWSDHG-W--------HLGE-HGHW--------GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAEL 352
|
410 420 430
....*....|....*....|....*....|....*
gi 1953410506 376 AGasLPQDRHFDGLDASEVLFGWSQTgHREPAVIT 410
Cdd:cd16030 353 AG--LPAPPCLEGKSLVPLLKNPSAK-WKDAAFSQ 384
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
31-521 |
1.66e-28 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 119.00 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 31 TRGQKPNFVIILADDMGwGD-LGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNGV 102
Cdd:PRK13759 2 VQTKKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 103 THNFavtsvgglplnETTLAEVLQQAGYVTGMIGKWHlghhgpYHP--NFRGFDYYFgipySHDmGCTDTPGYNHPPCPA 180
Cdd:PRK13759 81 PWNY-----------KNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHNVL----LHD-GYLHSGRNEDKSQFD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 181 CP-------RGDRPSRSLER-----DCYTDVALP--LYENLNiveqPVNLSslahkyAEKAIQFIQHASaSGRPFLLYMG 246
Cdd:PRK13759 139 FVsdylawlREKAPGKDPDLtdigwDCNSWVARPwdLEERLH----PTNWV------GSESIEFLRRRD-PTKPFFLKMS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 247 LAHMHVPI--------------------------------------SRTQLSADL--RGRRPYGAGLREMDSLVGQIKDK 286
Cdd:PRK13759 208 FARPHSPYdppkryfdmykdadipdphigdweyaedqdpeggsidaLRGNLGEEYarRARAAYYGLITHIDHQIGRFLQA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 287 V-DRTAKENTFLWFTGDNGpwaqkcELAGSvgpfTGLWQthqggspaKQTTWEGGHRVPALAYWPG---RVPVNVTSTAL 362
Cdd:PRK13759 288 LkEFGLLDNTIILFVSDHG------DMLGD----HYLFR--------KGYPYEGSAHIPFIIYDPGgllAGNRGTVIDQV 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 363 LSVLDIFPTVVALAGASLPQDrhFDGLDASEVLFGwSQTGHREpavitlagdlaatVTRAQHGSCspmetlnhvlfhpns 442
Cdd:PRK13759 350 VELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFG-QYEGWRP-------------YLHGEHALG--------------- 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953410506 443 gaageFGALQTVRLGSYKVFYVSGgakacdgdVGREQhhdpplIFNLEDDVAEAVPLdRGSAEYQDVLPKVREILADVL 521
Cdd:PRK13759 399 -----YSSDNYLTDGKWKYIWFSQ--------TGEEQ------LFDLKKDPHELHNL-SPSEKYQPRLREMRKKLVDHL 457
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-390 |
1.14e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 109.77 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 35 KPNFVIILADDMGWGDLGA-NWAETKD---------TANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTH 104
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCyNNAHTGKsesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 105 NFAVTSVGGLPLneTTLAEVLQQAGYVTGMIGKwhlGHHGPYhpnfrgfdyyfgipyshdmgcTDtpgynhppcpacprg 184
Cdd:cd16153 81 FEAAHPALDHGL--PTFPEVLKKAGYQTASFGK---SHLEAF---------------------QR--------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 185 drpsrslerdcYTDVALPLYEnlniveqpvnlsSLAHKYAEKAiqfiqhasASGRPFLLYMGLAHMHVPIsrtQLSADLR 264
Cdd:cd16153 120 -----------YLKNANQSYK------------SFWGKIAKGA--------DSDKPFFVRLSFLQPHTPV---LPPKEFR 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 265 GRRPYGAGLREMDSLVGQIKDKVDR----TAKENTFLWFTGDNGpwaqkcelagsvgpftglWQTHQGGSPAKQTTWEGG 340
Cdd:cd16153 166 DRFDYYAFCAYGDAQVGRAVEAFKAyslkQDRDYTIVYVTGDHG------------------WHLGEQGILAKFTFWPQS 227
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1953410506 341 HRVPALAYWPGR--VPVNVTSTALLSVLDIFPTVVALAGASLPQDRHFDGLD 390
Cdd:cd16153 228 HRVPLIVVSSDKlkAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRD 279
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-384 |
7.59e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 108.06 E-value: 7.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDM-GWGDLGANWAETKDTAnLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGL 114
Cdd:cd16035 1 PNILLILTDQErYPPPWPAGWAALNLPA-RERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 115 PLNETTLAEVLQQAGYVTGMIGKWHLGHHGpyhpnfRGfdyyfgipyshdmgctdtpGYNHPPcpacprgdrpsrslerd 194
Cdd:cd16035 80 SPDVPTLGHMLRAAGYYTAYKGKWHLSGAA------GG-------------------GYKRDP----------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 195 cytdvalplyenlniveqpvnlsslahKYAEKAIQFIQHASAS---GRPFLLYMGLA--H--MHVPISRTQLsadLRGRR 267
Cdd:cd16035 118 ---------------------------GIAAQAVEWLRERGAKnadGKPWFLVVSLVnpHdiMFPPDDEERW---RRFRN 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 268 PYGAGLREMDSLVGQIKDKVDRTA-KENTFLWFTGDNGpwaqkcELAGSVGpftGLwqtHQGGSPAKQTTwegghRVPAL 346
Cdd:cd16035 168 FYYNLIRDVDRQIGRVLDALDASGlADNTIVVFTSDHG------EMGGAHG---LR---GKGFNAYEEAL-----HVPLI 230
|
330 340 350
....*....|....*....|....*....|....*...
gi 1953410506 347 AYWPGRVPVNVTSTALLSVLDIFPTVVALAGASLPQDR 384
Cdd:cd16035 231 ISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARA 268
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
36-376 |
5.10e-25 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 103.65 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCS-PSRASLLTGRLGLRNGVTHNFAVT----- 109
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSaPNHAALLTGAYPTLHGYTGNGSADpelps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 110 SVGGLPLNETTLAEVLQQAGYVTGMIGkwhlghhgpyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacprgdrpsr 189
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 190 slerdcytdvalplyenlniveqpvnlsslahkyAEKAIQFIqhasASGRPFLLYMGLAHMHVPisrtqLSADLRGRRPY 269
Cdd:cd00016 108 ----------------------------------LLKAIDET----SKEKPFVLFLHFDGPDGP-----GHAYGPNTPEY 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 270 GAGLREMDSLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaqkcelagsvGPFTGLwqTHQGGSPAKQTTWEGGHRVPALAY 348
Cdd:cd00016 145 YDAVEEIDERIGKVLDALKKAGDaDDTVIIVTADHG------------GIDKGH--GGDPKADGKADKSHTGMRVPFIAY 210
|
330 340
....*....|....*....|....*...
gi 1953410506 349 WPGrVPVNVTSTALLSVLDIFPTVVALA 376
Cdd:cd00016 211 GPG-VKKGGVKHELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-140 |
1.22e-20 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 93.83 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtsVGGL 114
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPL 75
|
90 100
....*....|....*....|....*.
gi 1953410506 115 PLNETTLAEVLQQAGYVTGMIGKWHL 140
Cdd:cd16152 76 PADEKTLAHYFRDAGYETGYVGKWHL 101
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
36-388 |
1.84e-18 |
|
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: 88.21 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG-VTHNFAVTSvggl 114
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGsWTNCMALGD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 115 plNETTLAEVLQQAGYVTGMIGKWHLGhhgpyhpnfrGFDYY-FGIpyshdmgctdtpgynhppcpaCPRGDRPSRSLER 193
Cdd:cd16156 77 --NVKTIGQRLSDNGIHTAYIGKWHLD----------GGDYFgNGI---------------------CPQGWDPDYWYDM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 194 DCYTD-----------VALPLYENLNIVEQpvnlSSLAHKYAEKAIQFI-QHASasgRPFLL------------------ 243
Cdd:cd16156 124 RNYLDelteeerrksrRGLTSLEAEGIKEE----FTYGHRCTNRALDFIeKHKD---EDFFLvvsydephhpflcpkpya 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 244 --------------YMGLAH---MHVPISRTQLS---ADLRGRRPYGAGLRE-MDSLVGQIKDKVDRTAkENTFLWFTGD 302
Cdd:cd16156 197 smykdfefpkgenaYDDLENkplHQRLWAGAKPHedgDKGTIKHPLYFGCNSfVDYEIGRVLDAADEIA-EDAWVIYTSD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 303 NGpwaqkcELAGSvgpfTGLWqthqGGSPAkqtTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAGasLPQ 382
Cdd:cd16156 276 HG------DMLGA----HKLW----AKGPA---VYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQ 336
|
....*.
gi 1953410506 383 DRHFDG 388
Cdd:cd16156 337 PKVLEG 342
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
36-388 |
3.86e-17 |
|
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: 83.85 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT-----PLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 116 LNETTLAEVLQQAGYVTGMIGKWH----LGHHGPYHPNFR-------GFDYYF---GIPYSH-------DMGCTDTPGYN 174
Cdd:cd16028 76 ARHLTLALELRKAGYDPALFGYTDtspdPRGLAPLDPRLLsyelampGFDPVDrldEYPAEDsdtafltDRAIEYLDERQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 175 -------------HPP--CPAcprgdrPSRSLerdcYTDVALPLyenlniveqPVNLSSLAhkyAEKAiqfiQHasasgr 239
Cdd:cd16028 156 depwflhlsyirpHPPfvAPA------PYHAL----YDPADVPP---------PIRAESLA---AEAA----QH------ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 240 PFLLYM------GLAHMHVPISRTQLSADLRGRRPYGAGL-REMDSLVGQIKDKVDRTAKE-NTFLWFTGDNGpwaqkcE 311
Cdd:cd16028 204 PLLAAFleriesLSFSPGAANAADLDDEEVAQMRATYLGLiAEVDDHLGRLFDYLKETGQWdDTLIVFTSDHG------E 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 312 LAGsvgpftglwQTHQGGspaKQTTWEGGHRVPALAYWPGRvPVNVTS----TALLSVLDIFPTVVALAGasLPQDRHFD 387
Cdd:cd16028 278 QLG---------DHWLWG---KDGFFDQAYRVPLIVRDPRR-EADATRgqvvDAFTESVDVMPTILDWLG--GEIPHQCD 342
|
.
gi 1953410506 388 G 388
Cdd:cd16028 343 G 343
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-386 |
6.54e-17 |
|
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: 83.05 E-value: 6.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGR----LGLRNgvTHNFavtsv 111
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWyphvNGHRT--LHHL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 112 ggLPLNETTLAEVLQQAGYVTGMIGKWHlghhgpyhpnfrgfdyyfgipyshdmgctDTPGynhppcpacprgdrpSRSL 191
Cdd:cd16150 74 --LRPDEPNLLKTLKDAGYHVAWAGKND-----------------------------DLPG---------------EFAA 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 192 ERDCYTDVAlplyenlniveqpvnlsslahkYAEKAIQFIQHASAsGRPFLLYMGLAHMHVP----------ISRTQL-- 259
Cdd:cd16150 108 EAYCDSDEA----------------------CVRTAIDWLRNRRP-DKPFCLYLPLIFPHPPygveepwfsmIDREKLpp 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 260 -----------SADLRGRRPYG------AGLREM-----------DSLVGQIKDKVDRTA-KENTFLWFTGDNGPWAqkc 310
Cdd:cd16150 165 rrppglrakgkPSMLEGIEKQGldrwseERWRELratylgmvsrlDHQFGRLLEALKETGlYDDTAVFFFSDHGDYT--- 241
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953410506 311 elagsvGPFtGLWQTHQGGSPAKQTtwegghRVPALAYWPGRVPVNVTStALLSVLDIFPTVVALAGASLPQDrHF 386
Cdd:cd16150 242 ------GDY-GLVEKWPNTFEDCLT------RVPLIIKPPGGPAGGVSD-ALVELVDIPPTLLDLAGIPLSHT-HF 302
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
36-382 |
5.88e-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: 76.43 E-value: 5.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGrlgLRNGVTHNFavTSVGGLP 115
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG---LFTHLTESW--NNYKGLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 116 LNETTLAEVLQQAGYVTGMIGK--WHLGHHGPYHpnfRGFDYYFGIPYshdmgctdTPGYNHPPCPACPRGDRPSRSLER 193
Cdd:cd16171 76 PNYPTWMDRLEKHGYHTQKYGKldYTSGHHSVSN---RVEAWTRDVPF--------LLRQEGRPTVNLVGDRSTVRVMLK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 194 DCytdvalplyenlniveqpvnlsslahKYAEKAIQFIQHASAS-GRPFLLYMGLAHMH---VPISRTQLSADLRGRRPY 269
Cdd:cd16171 145 DW--------------------------QNTDKAVHWIRKEAPNlTQPFALYLGLNLPHpypSPSMGENFGSIRNIRAFY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 270 GAGLREMDSLVGQIKDKVDRTAKEN-TFLWFTGDNGpwaqkcELAGSVGPFTglwqthqggspaKQTTWEGGHRVPALAY 348
Cdd:cd16171 199 YAMCAETDAMLGEIISALKDTGLLDkTYVFFTSDHG------ELAMEHRQFY------------KMSMYEGSSHVPLLIM 260
|
330 340 350
....*....|....*....|....*....|....
gi 1953410506 349 WPGrVPVNVTSTALLSVLDIFPTVVALAGASLPQ 382
Cdd:cd16171 261 GPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
27-386 |
1.25e-06 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 51.19 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 27 PSGETRGQKPNFVIILADDMGWGDLGANWAETKDTANLDKMAAEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVthnf 106
Cdd:COG1368 226 PNPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGS---- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 107 AVTSVGGLPLNetTLAEVLQQAGYVTGMIgkwhlghHGpYHPNFR---------GFDYYFGI-----PYSHDMGCTDtpg 172
Cdd:COG1368 302 PYKRPGQNNFP--SLPSILKKQGYETSFF-------HG-GDGSFWnrdsfyknlGFDEFYDRedfddPFDGGWGVSD--- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 173 ynhppcpacprgdrpsrslerdcytdvaLPLYEnlniveqpvnlsslahkyaekaiQFIQHASASGRPFLLYMgL---AH 249
Cdd:COG1368 369 ----------------------------EDLFD-----------------------KALEELEKLKKPFFAFL-ItlsNH 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 250 M--HVPISRTQLSADLRGR-RPYGAGLREMDSLVGQIKDKVD-RTAKENTFLWFTGDngpwaqkcelagsvgpftglwqt 325
Cdd:COG1368 397 GpyTLPEEDKKIPDYGKTTlNNYLNAVRYADQALGEFIEKLKkSGWYDNTIFVIYGD----------------------- 453
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953410506 326 HQGGSPAKQTTWE--GGHRVPALAYWPGRVPVNVTSTaLLSVLDIFPTVVALAGASLPQDRHF 386
Cdd:COG1368 454 HGPRSPGKTDYENplERYRVPLLIYSPGLKKPKVIDT-VGSQIDIAPTLLDLLGIDYPSYYAF 515
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
14-162 |
5.58e-04 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 42.43 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 14 TFLGCLYPLVDFCPSGeTRGQKPNFVIILADDMGWGDLGANwaetkDTANLDKMAAEGMRFVDFHAA--ASTCsPSRASL 91
Cdd:COG1524 3 RGLSLLLASLLAAAAA-AAPPAKKVVLILVDGLRADLLERA-----HAPNLAALAARGVYARPLTSVfpSTTA-PAHTTL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953410506 92 LTGRLGLRNGVTHNF--------AVTSVGGLP--------LNETTLAEVLQQAGYVTGMIGKWHLGHHGPYHPN----FR 151
Cdd:COG1524 76 LTGLYPGEHGIVGNGwydpelgrVVNSLSWVEdgfgsnslLPVPTIFERARAAGLTTAAVFWPSFEGSGLIDAArpypYD 155
|
170
....*....|.
gi 1953410506 152 GFDYYFGIPYS 162
Cdd:COG1524 156 GRKPLLGNPAA 166
|
|
| |
