|
Name |
Accession |
Description |
Interval |
E-value |
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
35-469 |
0e+00 |
|
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.
Pssm-ID: 293780 [Multi-domain] Cd Length: 383 Bit Score: 641.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 35 KPNFVIILADDIGWGDLGANWAETKDTT-NLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGG 113
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAILTpNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 114 LPLNETTLAEVLQQAGYVTGMIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 194 dcytdvalplyenlniveqpvnlSSLAQKYAEKATQFIQQASTSGRPFLLYVGLAHMHVPLPVTQLPAAPW-GRRLYGAG 272
Cdd:cd16161 132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTsGRGPYGDA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 273 LREMDGLVGQIKDKVDR-TAKENTFLWFTGDNGPWAQKCELAgsVGPFTGLWQTRQGGSPAKQTTWEGGHRVPALAYWPG 351
Cdd:cd16161 189 LQEMDDLVGQIMDAVKHaGLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 352 RVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGeFGALQTVRLERYKAF 431
Cdd:cd16161 267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAH 345
|
410 420 430
....*....|....*....|....*....|....*...
gi 1864488355 432 YITGGARACDGSTGPEMQHKFPLIFNLEDDIAEAMPLE 469
Cdd:cd16161 346 YATGGALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT 383
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-468 |
2.08e-179 |
|
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: 509.80 E-value: 2.08e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGG 113
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 114 LPLNETTLAEVLQQAGYVTGMIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDMGCTDTPGYNHPPCPAcpqgdgpsrnlqr 193
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 194 dcytdvalPLYENLNIVEQPVNLSSLAQKYAEKATQFIQQAstSGRPFLLYVGLAHMHVPLPVTQLPAAPWGRRLYGAGL 273
Cdd:cd16026 148 --------PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 274 REMDGLVGQIKDKVDRT-AKENTFLWFTGDNGPWAQKCELAGSVGPFTGlwqtrqggspAKQTTWEGGHRVPALAYWPGR 352
Cdd:cd16026 218 EELDWSVGRILDALKELgLEENTLVIFTSDNGPWLEYGGHGGSAGPLRG----------GKGTTWEGGVRVPFIAWWPGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 353 VPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQ-PGHRVLFHPNSgaagefGALQTVRLERYKAF 431
Cdd:cd16026 288 IPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKsPPHPFFYYYDG------GDLQAVRSGRWKLH 361
|
410 420 430
....*....|....*....|....*....|....*..
gi 1864488355 432 YITGGARACDGSTGPEMQHKFPLIFNLEDDIAEAMPL 468
Cdd:cd16026 362 LPTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGETYNV 398
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
35-515 |
6.10e-119 |
|
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: 358.68 E-value: 6.10e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGG 113
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGvFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 114 LPLNETTLAEVLQQAGYVTGMIGKWHL--GHHGSYHPNFRGFDYYFGIPYSHDMG-CTD-TPGYNHPPC-PACPQGDGPs 188
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLgvGLNGTYLPTHQGFDHYLGIPYSHDQGpCQNlTCFPPNIPCfGGCDQGEVP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 189 rnlqrdcytdvaLPLYENLNIVEQPVNLSSLAQKYAEKATQFIQQASTSGRPFLLYVGLAHMHVPLPVTQLPAAPWGRRL 268
Cdd:cd16158 160 ------------CPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 269 YGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGPWAQKCELAGSvgpfTGLWQTRQGgspakqTTWEGGHRVPALA 347
Cdd:cd16158 228 FGDALAELDGSVGELLQTLKENGiDNNTLVFFTSDNGPSTMRKSRGGN----AGLLKCGKG------TTYEGGVREPAIA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 348 YWPGRVPVNVTStALLSVLDIFPTVVALAQASLPQgRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGEFGALqTVRLER 427
Cdd:cd16158 298 YWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLPN-VTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVF-AVRWGK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 428 YKAFYITGGA--------RACDGSTgPEMQHKFPLIFNLEDDIAEAMPLErGGTEYRAVLPKVRKVLADILQDI--ANDS 497
Cdd:cd16158 375 YKAHFYTQGAahsgttpdKDCHPSA-ELTSHDPPLLFDLSQDPSENYNLL-GLPEYNQVLKQIQQVKERFEASMkfGESE 452
|
490
....*....|....*...
gi 1864488355 498 ISRADytlDPSVTPCCNP 515
Cdd:cd16158 453 INKGE---DPALEPCCKP 467
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
35-487 |
3.18e-111 |
|
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: 337.86 E-value: 3.18e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV---THNFAVTSV 111
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 112 GGLPLNETTLAEVLQQAGYVTGMIGKWHLG-----HHGSYH-PNFRGFDYY-FGIPYSHDMGCTDTPGYNhppcpacpqg 184
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDFVgTNLPFTNSWACDDTGRHV---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 185 DGPSRNLqrdCYtdvalpLYENLNIVEQPVNLSSLAQKYAEKATQFIQqaSTSGRPFLLYVGLAHMHVPLPVTQLPAAPW 264
Cdd:cd16160 151 DFPDRSA---CF------LYYNDTIVEQPIQHEHLTETLVGDAKSFIE--DNQENPFFLYFSFPQTHTPLFASKRFKGKS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 265 GRRLYGAGLREMDGLVGQIKDK-VDRTAKENTFLWFTGDNGPWAQKCELAGSVGPFTGlwqtrqggspAKQTTWEGGHRV 343
Cdd:cd16160 220 KRGRYGDNINEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKG----------GKGNSWEGGIRV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 344 PALAYWPGRVPVNVtSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQ-PGHRVLFHPNSgaagefgALQT 422
Cdd:cd16160 290 PFIAYWPGTIKPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADsPHDDILYYCCS-------RLMA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 423 VRLERYKAFYITG--------GARACDGSTGPE------------MQHKFPLIFNLEDDIAEAMPLErgGTEYRAVLPKV 482
Cdd:cd16160 362 VRYGSYKIHFKTQplpsqeslDPNCDGGGPLSDyivcydcedecvTKHNPPLIFDVEKDPGEQYPLQ--PSVYEHMLEAV 439
|
....*
gi 1864488355 483 RKVLA 487
Cdd:cd16160 440 EKLIA 444
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-488 |
5.92e-100 |
|
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: 309.40 E-value: 5.92e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG--VTHNFAVTS-- 110
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 111 ----VGGLPLNETTLAEVLQQAGYVTGMIGKWHLGHHGSYHPNFRGFDYYFGIPYSHdMGCTDTPGYNHPPcpacpqgdg 186
Cdd:cd16157 81 pqniVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCH-FGPYDNKAYPNIP--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 187 psrnLQRDcyTDVALPLYENLNIvEQPVNLSSLAQKYAEKATQFIQQASTSGRPFLLYVGLAHMHVPLPVTQLPAAPWGR 266
Cdd:cd16157 151 ----VYRD--WEMIGRYYEEFKI-DKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 267 RLYGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNG-PWAQKCELAGSVGPFTGlwqtrqggspAKQTTWEGGHRVP 344
Cdd:cd16157 224 GLYGDAVMELDSSVGKILESLKSLGiENNTFVFFSSDNGaALISAPEQGGSNGPFLC----------GKQTTFEGGMREP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 345 ALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSgaagefgALQTVR 424
Cdd:cd16157 294 AIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGD-------ELMAVR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 425 LERYKAFYIT---------GGARACDG------STGPEMQH-KFPLIFNLEDDIAEAMPLERGGTEYRAVLPKVRKVLAD 488
Cdd:cd16157 367 LGQYKAHFWTwsnsweefrKGINFCPGqnvpgvTTHNQTDHtKLPLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVVQQ 446
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
35-507 |
1.14e-97 |
|
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: 305.37 E-value: 1.14e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN------FAV 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASShgmrviLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 109 TSVGGLPLNETTLAEVLQQAGYVTGMIGKWHLGHH------GSYHPNFRGFDYYFGIPYSHDMGCTDTPG--YNHPPCPA 180
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHcesrndFCHHPLNHGFDYFYGLPLTNLKDCGDGSNgeYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 181 CPQgdgpSRNLQRDCYTDVALPLY--------------------------------------ENLNIVEQPVNLSSLAQK 222
Cdd:cd16159 161 FPL----LTAFVLITALTIFLLLYlgavskrffvfllilsllfislfflllitnryfncilmRNHEVVEQPMSLENLTQR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 223 YAEKATQFIQQasTSGRPFLLYVGLAHMHVPLPVTQLPAAPWGRRLYGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTG 301
Cdd:cd16159 237 LTKEAISFLER--NKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGlKDNTFVYFTS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 302 DNGPWAqkcELAGSVGPFTGLWQTRQGGSpaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLP 381
Cdd:cd16159 315 DNGGHL---EEISVGGEYGGGNGGIYGGK--KMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 382 QGRRFDGVDVSEVLFGRSQ-PGHRVLFH------------PNSGAAgefgalqtvrleRYKAFYIT-----GGARA---- 439
Cdd:cd16159 390 SDRIIDGRDLMPLLTGQEKrSPHEFLFHycgaelhavryrPRDGGA------------VWKAHYFTpnfypGTEGCcgtl 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864488355 440 ---CDGSTGpeMQHKFPLIFNLEDDIAEAMPLERGGTEYRAVLPKVRKVLADilqdiANDSISRADYTLDP 507
Cdd:cd16159 458 lcrCFGDSV--THHDPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAE-----HQSSIEPVESQLSF 521
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-468 |
9.25e-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: 282.50 E-value: 9.25e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGAN---WAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHNFAVTSVG 112
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYgggIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 113 GLPLNETTLAEVLQQAGYVTGMIGKWHLGHHGSYHPNFRGFDYYFGIPYSHdmgctdtpgynhppcpacpqgdgpsrnlq 192
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYHT----------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 193 rdcytdvalplyenlniveqpvnlssLAQKYAEKATQFIQQASTSGRPFLLYVGLAHMHVP-LPVTQLPAAPWGRRLYGA 271
Cdd:cd16142 131 --------------------------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPtLPSPEFEGKSSGKGKYAD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 272 GLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGPWAQKCELAGSvGPFTGlwqtrqggspAKQTTWEGGHRVPALAYWP 350
Cdd:cd16142 185 SMVELDDHVGQILDALDELGiADNTIVIFTTDNGPEQDVWPDGGY-TPFRG----------EKGTTWEGGVRVPAIVRWP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 351 GRVPVNVTSTALLSVLDIFPTVVALAQASLP------QGRRFDGVDVSEVLFGRS-QPGHRVLFHpnsGAAGEFGAlqtV 423
Cdd:cd16142 254 GKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSeKSRRSEFFY---FGEGELGA---V 327
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1864488355 424 RLERYKA-FYITGGARAcdGSTGPEMQHKFPLIFNLEDDIAEAMPL 468
Cdd:cd16142 328 RWKNWKVhFKAQEDTGG--PTGEPFYVLTFPLIFNLRRDPKERYDV 371
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
28-464 |
1.97e-88 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 277.14 E-value: 1.97e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 28 SGKARGQKPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFA 107
Cdd:COG3119 16 AAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 108 vTSVGGLPLNETTLAEVLQQAGYVTGMIGKWHLghhgsyhpnfrgfdyyfgipYSHDmgctdtpgynhppcpacpqgdgp 187
Cdd:COG3119 96 -GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------YLTD----------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 188 srnlqrdcytdvalplyenlniveqpvnlsslaqKYAEKATQFIQQASTSGRPFLLYVGLAHMHVP-------------- 253
Cdd:COG3119 132 ----------------------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPyqapeeyldkydgk 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 254 ---LPVTQLPAAPW------GRRLYGAGLREMDGLVGQIKDKVDRT-AKENTFLWFTGDNGPWAqkcelagsvgpftGLW 323
Cdd:COG3119 178 dipLPPNLAPRDLTeeelrrARAAYAAMIEEVDDQVGRLLDALEELgLADNTIVVFTSDNGPSL-------------GEH 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 324 QTRQGgspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGH 403
Cdd:COG3119 245 GLRGG----KGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWR 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864488355 404 RVLFHpnsgAAGEFGALQTVRLERYKAFYitggaraCDGSTGPEMqhkfplIFNLEDDIAE 464
Cdd:COG3119 319 DYLYW----EYPRGGGNRAIRTGRWKLIR-------YYDDDGPWE------LYDLKNDPGE 362
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-465 |
8.38e-84 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 265.95 E-value: 8.38e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--------- 106
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIpgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 107 ----AVTSVGGLPLNETTLAEVLQQAGYVTGMIGKWHLGHHGSYHPNFRGFDYYFGI-PYSHDMGCTDTPGYNHPPCPAC 181
Cdd:cd16144 81 tkliPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIGGtGNGGPPSYYFPPGKPNPDLEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 182 PQGDgpsrnlqrdcytdvalplyenlniveqpvnlsSLAQKYAEKATQFIQQAstSGRPFLLYvgLAH--MHVPLPVTQ- 258
Cdd:cd16144 161 PEGE--------------------------------YLTDRLTDEAIDFIEQN--KDKPFFLY--LSHyaVHTPIQARPe 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 259 -------LPAAPWGRR---LYGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGPWAQKCELAGSVGPFtglwqtRQ 327
Cdd:cd16144 205 liekyekKKKGLRKGQknpVYAAMIESLDESVGRILDALEELGlADNTLVIFTSDNGGLSTRGGPPTSNAPL------RG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 328 GgspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHR--V 405
Cdd:cd16144 279 G----KGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRraL 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864488355 406 LFH-PN-SGAAGEFGAlqTVRLERYK--AFYITGgaracdgstgpemqhKFPLiFNLEDDIAEA 465
Cdd:cd16144 355 FWHfPHyHGQGGRPAS--AIRKGDWKliEFYEDG---------------RVEL-YNLKNDIGET 400
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-464 |
3.20e-81 |
|
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: 258.67 E-value: 3.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETK-DTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGL 114
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGG--VLGGFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 115 PL---NETTLAEVLQQAGYVTGMIGKWHLG-----------HHGSYH-----------PNFRGFDYYFGIPYShdmgctd 169
Cdd:cd16143 79 PLiepDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkaATGTGKdvdyskpikggPLDHGFDYYFGIPAS------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 170 tpgynhppcpacpqgdgpsrnlqrdcytDVaLPLyenlniveqpvnlsslaqkYAEKATQFIQQASTSGRPFLLYVGLAH 249
Cdd:cd16143 152 ----------------------------EV-LPT-------------------LTDKAVEFIDQHAKKDKPFFLYFALPA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 250 MHVPLpvtqLPAAPW-GRrlYGAGLR-----EMDGLVGQIKDKVDRTA-KENTFLWFTGDNGP----WAQKCELAG--SV 316
Cdd:cd16143 184 PHTPI----VPSPEFqGK--SGAGPYgdfvyELDWVVGRILDALKELGlAENTLVIFTSDNGPspyaDYKELEKFGhdPS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 317 GPFTGLwqtrqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLF 396
Cdd:cd16143 258 GPLRGM----------KADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALL 327
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864488355 397 GRSQPGHRV-LFHpnSGAAGEFgalqTVR-----LERYKAFYITGGARACDGSTGPEMQhkfplIFNLEDDIAE 464
Cdd:cd16143 328 GPKKQEVREsLVH--HSGNGSF----AIRkgdwkLIDGTGSGGFSYPRGKEKLGLPPGQ-----LYNLSTDPGE 390
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-464 |
7.01e-78 |
|
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: 250.59 E-value: 7.01e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGLP 115
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 116 LNETTLAEVLQQAGYVTGMIGKWHLGHHGSY-HPNFRGFDYYFGIpYSHdmgctdTPGYNHPPcpacPQGDgpsRNLQRd 194
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYGY-LDQ------VHAHNYYP----EYLW---RNGEK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 195 cytdvaLPLYENLNIVEQPVNLSSLAQK-YAE-----KATQFIQQAstSGRPFLLYVGLAHMHVPLPVTQLPAA------ 262
Cdd:cd16145 146 ------VPLPNNVIPPLDEGNNAGGGGGtYSHdlftdEALDFIREN--KDKPFFLYLAYTLPHAPLQVPDDGPYkykpkd 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 263 -------PW--GRRLYGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGP-----WAQKCELAGSVGPFTGLwqtrq 327
Cdd:cd16145 218 pgiyaylPWpqPEKAYAAMVTRLDRDVGRILALLKELGiDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 328 ggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPG-HRVL 406
Cdd:cd16145 293 -----KRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPE--DIDGISLLPTLLGKPQQQqHDYL 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1864488355 407 FHpnsgAAGEFGALQTVRLERYKAFYItggaracDGSTGPEMqhkfplIFNLEDDIAE 464
Cdd:cd16145 366 YW----EFYEGGGAQAVRMGGWKAVRH-------GKKDGPFE------LYDLSTDPGE 406
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
36-407 |
3.20e-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: 245.92 E-value: 3.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTHnfavTSVGG-- 113
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWH----TILGRer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 114 LPLNETTLAEVLQQAGYVTGMIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgcTDTPGYnhppcpacpqgdgpsrnLQR 193
Cdd:cd16146 76 MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGGGI---GQYPDY-----------------WGN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 194 DCYTDValpLYENlNIVEQpvnlsslAQKYA-----EKATQFIQQASTsgRPFLLYVGLAHMHVPLpvtQLPAAPWGrRL 268
Cdd:cd16146 136 DYFDDT---YYHN-GKFVK-------TEGYCtdvffDEAIDFIEENKD--KPFFAYLATNAPHGPL---QVPDKYLD-PY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 269 YGAGLRE-----------MDGLVGQIKDKVDRT-AKENTFLWFTGDNGPWaqkcelAGSVGPFTGLWQtrqgGSpaKQTT 336
Cdd:cd16146 199 KDMGLDDklaafygmienIDDNVGRLLAKLKELgLEENTIVIFMSDNGPA------GGVPKRFNAGMR----GK--KGSV 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864488355 337 WEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQP-GHRVLF 407
Cdd:cd16146 267 YEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPwPERTLF 338
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
36-470 |
1.65e-68 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 225.51 E-value: 1.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFvDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSV-GGL 114
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVIL-NNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEpYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 115 PLNETTLAEVLQQAGYVTGMIGKWHLGHHGSYH-PNFRGFDYYFGiPYShdmGCTDtpGYNHPPCPACP------QGDGP 187
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYTWEYtPTNRGFDSFYG-YYG---GAED--YYTHTSGGANDygnddlRDNEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 188 SRNLQRDCY-TDValplyenlniveqpvnlsslaqkYAEKATQFIQQASTSgRPFLLYVGLAHMHVPLPVTQLPAAPW-- 264
Cdd:cd16029 154 PAWDYNGTYsTDL-----------------------FTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYed 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 265 --------GRRLYGAGLREMDGLVGQIKDK-VDRTAKENTFLWFTGDNGPWAQKCElAGSVGPFTGlwqtrqggspAKQT 335
Cdd:cd16029 210 kfahikdeDRRTYAAMVSALDESVGNVVDAlKAKGMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRG----------GKNT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 336 TWEGGHRVPALAYWPGRVPV-NVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHR-VLFHPNSGA 413
Cdd:cd16029 279 LWEGGVRVPAFVWSPLLPPKrGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTeILLNIDDIT 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1864488355 414 AGEFGAlqTVRLERYKafYITGgaracdgstgpemqhkFPLiFNLEDDiaeamPLER 470
Cdd:cd16029 359 RTTGGA--AIRVGDWK--LIVG----------------KPL-FNIEND-----PCER 389
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
36-390 |
7.60e-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: 218.46 E-value: 7.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGLP 115
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 116 LNETTLAEVLQQAGYVTGMIGKWHlghhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsrnlqrdc 195
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 196 ytdvalplyenlniveqpvnlsslaqkyaEKATQFIQQASTSgRPFLLYVGLAHMHVPLpvtqlpaapwgrrLYGAGLRE 275
Cdd:cd16022 103 -----------------------------DEAIDFIERRDKD-KPFFLYVSFNAPHPPF-------------AYYAMVSA 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 276 MDGLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaqkcelaGSVGPFTGLWQtrqggspaKQTTWEGGHRVPALAYWPGRVP 354
Cdd:cd16022 140 IDDQIGRILDALEELGLlDNTLIVFTSDHG---------DMLGDHGLRGK--------KGSLYEGGIRVPFIVRWPGKIP 202
|
330 340 350
....*....|....*....|....*....|....*.
gi 1864488355 355 VNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVD 390
Cdd:cd16022 203 AGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-468 |
5.04e-62 |
|
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: 207.84 E-value: 5.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHnfavtsvGGLP 115
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPL-CTPSRVQLMTGKYNFRNYVVF-------GYLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 116 LNETTLAEVLQQAGYVTGMIGKWHLG---HHGSYHPNFrGFDYY--FGipyshdmGCTDTPGYNHPPCPACPQGDGPSRN 190
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGKWQLGggrGDGDYPHEF-GFDEYclWQ-------LTETGEKYSRPATPTFNIRNGKLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 191 LQRDCY-TDValplyenlniveqpvnlsslaqkYAEKATQFIQQAstSGRPFLLY--VGLAH-MHVPLPVTQLPAAPWGR 266
Cdd:cd16151 145 TTEGDYgPDL-----------------------FADFLIDFIERN--KDQPFFAYypMVLVHdPFVPTPDSPDWDPDDKR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 267 -----RLYGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNgpwaqkcelaGSVGPFTGLW--QTRQGGspaKQTTWE 338
Cdd:cd16151 200 kkddpEYFPDMVAYMDKLVGKLVDKLEELGlRENTIIIFTGDN----------GTHRPITSRTngREVRGG---KGKTTD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 339 GGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGEFG 418
Cdd:cd16151 267 AGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWYYRNPHKKF 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1864488355 419 ALQTVRLERYKaFYITGgaracdgstgpemqhKFpliFNLEDDIAEAMPL 468
Cdd:cd16151 347 GSRFVRTKRYK-LYADG---------------RF---FDLREDPLEKNPL 377
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
36-378 |
4.21e-56 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 189.94 E-value: 4.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtSVGGLP 115
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS----TPVGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 116 LNETTLAEVLQQAGYVTGMIGKWHLGHHGSYHPNFRGFDYYFG-IPYSHDMGCTDTPGYNHPPcpacpqgdgpsrnlqRD 194
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLYADPPDVPYNCSG---------------GG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 195 CYTDValplyenlniveqpvnlsslaqkYAEKATQFIQQAStsgRPFLLYVGLAHMHVPLPVTQLPAAPWG--------- 265
Cdd:pfam00884 142 VSDEA-----------------------LLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscse 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 266 ---RRLYGAGLREMDGLVGQIKDKVDRTAK-ENTFLWFTGDNGPwaqkcelagSVGPFTGLWQTRQGGspakqTTWEGGH 341
Cdd:pfam00884 196 eqlLNSYDNTLLYTDDAIGRVLDKLEENGLlDNTLVVYTSDHGE---------SLGEGGGYLHGGKYD-----NAPEGGY 261
|
330 340 350
....*....|....*....|....*....|....*..
gi 1864488355 342 RVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQA 378
Cdd:pfam00884 262 RVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
34-465 |
5.88e-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: 187.27 E-value: 5.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 34 QKPNFVIILADDIGWGDLGANWAETkDTTNLDKMASEGMRFVDFHAAAsTCSPSRASLLTGRLGLRNGV-THNFAVTSVG 112
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEI-PTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQVGMgTMAELATGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 113 G----LPLNETTLAEVLQQAGYVTGMIGKWHLGHHgsyhpnfrgfDYYFgipySHDmgctdtpgynhppcpacpqgdgps 188
Cdd:cd16025 79 GyegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------DYYS----TDD------------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 189 rnlqrdcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQQASTSGRPFLLYVGLAHMHVPL-------------- 254
Cdd:cd16025 121 ----------------------------------LTDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLqapkewidkykgky 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 255 ----------------------PVTQLPA-----APW-----------GRR--LYGAGLREMDGLVGQIKDKVDRTAK-E 293
Cdd:cd16025 167 dagwdalreerlerqkelglipADTKLTPrppgvPAWdslspeekkleARRmeVYAAMVEHMDQQIGRLIDYLKELGElD 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 294 NTFLWFTGDNGP-----WAQkcelAGSvGPFTGlwqtrqggspAKQTTWEGGHRVPALAYWPGRV-PVNVTSTALLSVLD 367
Cdd:cd16025 247 NTLIIFLSDNGAsaepgWAN----ASN-TPFRL----------YKQASHEGGIRTPLIVSWPKGIkAKGGIRHQFAHVID 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 368 IFPTVVALAQASLPQGRR------FDGVDVSEVLFGRSQPG-HRVLFHPNSGAAGefgalqtVRLERYKAFYITGGarac 440
Cdd:cd16025 312 IAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSrRRTQYFELFGNRA-------IRKGGWKAVALHPP---- 380
|
490 500
....*....|....*....|....*
gi 1864488355 441 dGSTGPEMQhkfplIFNLEDDIAEA 465
Cdd:cd16025 381 -PGWGDQWE-----LYDLAKDPSET 399
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
36-433 |
1.91e-51 |
|
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: 179.63 E-value: 1.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGA--NWAETkdtTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFavTSVGG 113
Cdd:cd16027 1 PNILWIIADDLSPDLGGYggNVVKT---PNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR--SRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 114 LPLNETTLAEVLQQAGYVTGMIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAWD----------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 194 dcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQQAStSGRPFLLYVGLAHMH-----------------VPLPv 256
Cdd:cd16027 127 -----------------------------YASNAADFLNRAK-KGQPFFLWFGFHDPHrpyppgdgeepgydpekVKVP- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 257 TQLPAAPWGRR---LYGAGLREMDGLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaqkcelagsvGPFTGlwqtrqggspA 332
Cdd:cd16027 176 PYLPDTPEVREdlaDYYDEIERLDQQVGEILDELEEDGLlDNTIVIFTSDHG------------MPFPR----------A 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 333 KQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHRVLF----- 407
Cdd:cd16027 234 KGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGRDYVFaerdr 311
|
410 420
....*....|....*....|....*..
gi 1864488355 408 HpnsgaaGEFGALQ-TVRLERYKafYI 433
Cdd:cd16027 312 H------DETYDPIrSVRTGRYK--YI 330
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-461 |
8.13e-49 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 173.14 E-value: 8.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggL 114
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 115 PLNETTLAEVLQQAGYVTGMIGKWHL-GHHGSYH--------PNFR-GFDYYFGipyshdMGCTDtpGYNHPPCpacpQG 184
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGraddytppPERRhGFDYWKG------YECNH--DHNNPHY----YD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 185 DGPSRNlQRDCYTDVALplyenlniveqpvnlsslaqkyAEKATQFIQQASTSGRPFLLYV--GLAHM---HVP------ 253
Cdd:cd16034 144 DDGKRI-YIKGYSPDAE----------------------TDLAIEYLENQADKDKPFALVLswNPPHDpytTAPeeyldm 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 254 -----------LPVTQLPAAPWGR--RLYGAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGpwaqkcELAGSVGPF 319
Cdd:cd16034 201 ydpkklllrpnVPEDKKEEAGLREdlRGYYAMITALDDNIGRLLDALKELGlLENTIVVFTSDHG------DMLGSHGLM 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 320 tglwqtrqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRS 399
Cdd:cd16034 275 ------------NKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGK 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864488355 400 QPGHR----VLFHPNSG-AAGEFGALQTVRLERYKafYitggarACDGSTGpemqhkfPLIFNLEDD 461
Cdd:cd16034 341 DDEPDsvllQCFVPFGGgSARDGGEWRGVRTDRYT--Y------VRDKNGP-------WLLFDNEKD 392
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-388 |
1.10e-44 |
|
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: 158.17 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV-----THNFAVTS 110
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 111 VG-GLPLNETTLAEVLQQAGYVTGMIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd16149 81 KPeGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 190 nlqrdcytdvalplyenlniveqpvnlsslaqkyaEKATQFIQQASTSGRPFLLYVGlahmhvplpvTQLPAAPWGrrlY 269
Cdd:cd16149 113 -----------------------------------DDAADFLRRRAEAEKPFFLSVN----------YTAPHSPWG---Y 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 270 GAGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGpwaqkcelagsvgpFT----GLWQTRQGGSPakQTTWEGGHRVP 344
Cdd:cd16149 145 FAAVTGVDRNVGRLLDELEELGlTENTLVIFTSDNG--------------FNmghhGIWGKGNGTFP--LNMYDNSVKVP 208
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1864488355 345 ALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDG 388
Cdd:cd16149 209 FIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPG 252
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
34-433 |
1.15e-42 |
|
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: 157.31 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 34 QKPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvGG 113
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG----PL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 114 LPLNETTLAEVLQQAGYVTGMIGKWHLGHHGsYHPNfRGFDYYFGIPyshdmgctdtpgynhppcpacPQGDgpsrnlqr 193
Cdd:cd16031 77 FDASQPTYPKLLRKAGYQTAFIGKWHLGSGG-DLPP-PGFDYWVSFP---------------------GQGS-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 194 dcYTDvaLPLYENLNIVEQPVNLSSLaqkYAEKATQFIQQAStSGRPFLLYVG--LAH---------------MHVPLPV 256
Cdd:cd16031 126 --YYD--PEFIENGKRVGQKGYVTDI---ITDKALDFLKERD-KDKPFCLSLSfkAPHrpftpaprhrglyedVTIPEPE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 257 TQLPA-----APWGR------------------------RLYGAGLREMDGLVGQIKDKVDRTAK-ENTFLWFTGDNGpw 306
Cdd:cd16031 198 TFDDDdyagrPEWAReqrnrirgvldgrfdtpekyqrymKDYLRTVTGVDDNVGRILDYLEEQGLaDNTIIIYTSDNG-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 307 aqkcelagsvgpFT----GLwqtrqGGspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPq 382
Cdd:cd16031 276 ------------FFlgehGL-----FD---KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIP- 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1864488355 383 gRRFDGVDVSEVLFGRSQPGHR------VLFHPNS-GAAGEFGalqtVRLERYKafYI 433
Cdd:cd16031 335 -EDMQGRSLLPLLEGEKPVDWRkefyyeYYEEPNFhNVPTHEG----VRTERYK--YI 385
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-464 |
4.29e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 143.64 E-value: 4.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWgDLGANWAETKD---TTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVThnfavtSVG 112
Cdd:cd16154 1 PNILLIIADDQGL-DSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVL------AVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 113 G-LPLNETTL--AEVLQQ--AGYVTGMIGKWHLGHHGSYHPNFRGFDYYFGIpyshdmgctdTPGynhppcpacpqgdgp 187
Cdd:cd16154 73 DeLLLSEETLlqLLIKDAttAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGI----------LGG--------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 188 srnlqrdcytdvALPLYENLNIVEQPVNLSS---LAQKYAEKATQFIQQASTsgrPFLLYVGLAHMHVP--LPVTQL--- 259
Cdd:cd16154 128 ------------GVQDYYNWNLTNNGQTTNSteyATTKLTNLAIDWIDQQTK---PWFLWLAYNAPHTPfhLPPAELhsr 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 260 ---------PAAPwgRRLYGAGLREMDGLVGQIKDKVDRTAKENTFLWFTGDNG-PwaqkcelagsvGPFTGLWQTRQGg 329
Cdd:cd16154 193 sllgdsadiEANP--RPYYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGtP-----------GQVVDLPYTRNH- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 330 spAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPGHRVLFHP 409
Cdd:cd16154 259 --AKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNASTRQYNYTE 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1864488355 410 NSGAAGEFGAlqtVRLERYKAFYITGGARAcdgstgpemqhkfplIFNLEDDIAE 464
Cdd:cd16154 335 YESPTTTGWA---TRNQYYKLIESENGQEE---------------LYDLINDPSE 371
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
35-388 |
1.23e-35 |
|
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: 137.30 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 35 KPNFVIILADDIGWgDLGANWAETKdTTNLdkMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtSVGGL 114
Cdd:cd16147 1 RPNIVLILTDDQDV-ELGSMDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSP--PGGGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 115 P------LNETTLAEVLQQAGYVTGMIGK----WHLGHHGSYHPnfRGFDYYFGI-------PYSHDMGCTDTPGYNHPp 177
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYVP--PGWDEWDGLvgnstyyNYTLSNGGNGKHGVSYP- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 178 cpacpqgdgpsrnlqRDCYTDValplyenlniveqpvnlsslaqkYAEKATQFIQQASTSGRPFLLYVG----------- 246
Cdd:cd16147 152 ---------------GDYLTDV-----------------------IANKALDFLRRAAADDKPFFLVVAppaphgpftpa 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 247 --LAHMHVPLPVTQLPA---------APWGRRLYGAG-----------------LREMDGLVGQIKDKVDRTAK-ENTFL 297
Cdd:cd16147 194 prYANLFPNVTAPPRPPpnnpdvsdkPHWLRRLPPLNptqiayidelyrkrlrtLQSVDDLVERLVNTLEATGQlDNTYI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 298 WFTGDNGPWaqkcelagsvgpftgLWQTRQGgsPAKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDIFPTVVALAQ 377
Cdd:cd16147 274 IYTSDNGYH---------------LGQHRLP--PGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAG 335
|
410
....*....|.
gi 1864488355 378 ASLPqgRRFDG 388
Cdd:cd16147 336 APPP--SDMDG 344
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-432 |
8.26e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 132.34 E-value: 8.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--AVTSVGG 113
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 114 LPLNETTLAEVLQQAGYVTGMIGKWHLGHHGSyhPNFRGFDYYFgiPYSHDMgctdtPGYnhppcpacpqgdgpsrnlqr 193
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVGPEET--PLDYGFDEYL--PVETTI-----EYF-------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 194 dcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQQASTSGRPFLLYVGLAHMH-----------------VPLP- 255
Cdd:cd16033 132 -----------------------------LADRAIEMLEELAADDKPFFLRVNFWGPHdpyippepyldmydpedIPLPe 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 256 -----------VTQLPAAPWG------------RRLYGAGLREMDGLVGQIKDKVDRT-AKENTFLWFTGDNGpwaqkcE 311
Cdd:cd16033 183 sfaddfedkpyIYRRERKRWGvdtedeedwkeiIAHYWGYITLIDDAIGRILDALEELgLADDTLVIFTSDHG------D 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 312 LAGSvgpfTGLWqtRQGGSPAKQTtweggHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDV 391
Cdd:cd16033 257 ALGA----HRLW--DKGPFMYEET-----YRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVP--PKVDGRSL 323
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1864488355 392 SEVLFGRSQPGHR--VL--FHPNsgaagEFGALQT-VRLERYKAFY 432
Cdd:cd16033 324 LPLLRGEQPEDWRdeVVteYNGH-----EFYLPQRmVRTDRYKYVF 364
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-469 |
9.47e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 131.53 E-value: 9.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 34 QKPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAST----CSPSRASLLTGRlglrngvtHNFAVT 109
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGR--------TLFHAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 110 SVGG--LPLNETTLAEVLQQAGYVTGMIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgp 187
Cdd:cd16155 73 EGGKaaIPSDDKTWPETFKKAGYRTFATGKWHNG---------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 188 srnlqrdcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQQASTSGRPFLLYVGLAHMH---------------- 251
Cdd:cd16155 107 -----------------------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHdprqappeyldmyppe 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 252 -VPLPVTQLPA---------------APWGRRL---------YGAGLREMDGLVGQIKDKVDRTAK-ENTFLWFTGDNGp 305
Cdd:cd16155 152 tIPLPENFLPQhpfdngegtvrdeqlAPFPRTPeavrqhlaeYYAMITHLDAQIGRILDALEASGElDNTIIVFTSDHG- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 306 waqkceLA-GSvgpfTGLwqtrQGgspaKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDIFPTVVALAQASLPQGr 384
Cdd:cd16155 231 ------LAvGS----HGL----MG----KQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES- 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 385 rFDGVDVSEVLFGRSQPGHRVLFhpnsgaaGEFGALQ-TVRLERYKAFYITGGAracdgstgpemqhKFPLIFNLEDDia 463
Cdd:cd16155 291 -VEGKSLLPVIRGEKKAVRDTLY-------GAYRDGQrAIRDDRWKLIIYVPGV-------------KRTQLFDLKKD-- 347
|
....*.
gi 1864488355 464 eamPLE 469
Cdd:cd16155 348 ---PDE 350
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
402-522 |
2.09e-30 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 114.72 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 402 GHRVLFHpNSGAAgefgaLQTVRLERYKAFYITG-----GARACDGSTGPEMQHKFPLIFNLEDDIAEAMPLERGGTEYR 476
Cdd:pfam14707 2 PHEFLFH-YCGAA-----LHAVRWGPYKAHFFTPsfdppGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYP 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1864488355 477 AVLPKVRKVLADILQDI--ANDSISRADYTLDPSVTPCCnPYHIACRC 522
Cdd:pfam14707 76 EVLAEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
34-428 |
6.33e-29 |
|
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: 118.83 E-value: 6.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 34 QKPNFVIILADD----IGWgdLGANWAETKdttNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVtHNFAVT 109
Cdd:cd16030 1 KKPNVLFIAVDDlrpwLGC--YGGHPAKTP---NIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGV-YDNNSY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 110 SVGGLPlNETTLAEVLQQAGYVTGMIGK-WHlGHHGSYHPNFRGFDYYFGIP--------YSHDMGCTDTPGYNHPPCPA 180
Cdd:cd16030 75 FRKVAP-DAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPPgpekyppgKLCPGKKGGKGGGGGPAWEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 181 CPQGDGPsrnlqrdcYTDvalplyenlniveqpvnlsslaQKYAEKATQFIQQASTSGRPFLLYVGLAHMHVPLPVTQ-- 258
Cdd:cd16030 153 ADVPDEA--------YPD----------------------GKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKky 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 259 -------------------LPAAPWG-------------------------------RRLYGAGLREMDGLVGQIKDKVD 288
Cdd:cd16030 203 fdlyplesiplpnpfdpidLPEVAWNdlddlpkygdipalnpgdpkgplpdeqarelRQAYYASVSYVDAQVGRVLDALE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 289 RTA-KENTFLWFTGDNGpWaqkcelagSVGPfTGLWqtrqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLD 367
Cdd:cd16030 283 ELGlADNTIVVLWSDHG-W--------HLGE-HGHW--------GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVD 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864488355 368 IFPTVVALAQasLPQGRRFDGVDVSEVLFGRSQPGHRVLF--HPNSGAAGEfgalqTVRLERY 428
Cdd:cd16030 345 IYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKDAAFsqYPRPSIMGY-----SIRTERY 400
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
31-492 |
2.90e-28 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 117.85 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 31 ARGQKPNFVIILADDigW-GD-LGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNG 101
Cdd:PRK13759 2 VQTKKPNIILIMVDQ--MrGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 102 VTHNFavtsvgglplnETTLAEVLQQAGYVTGMIGKWHlghhgsYHP--NFRGFD--------YYFGIPYSHDMG--CTD 169
Cdd:PRK13759 80 VPWNY-----------KNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHnvllhdgyLHSGRNEDKSQFdfVSD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 170 --------TPGYNhppcpACPQGDGpsrnlqRDCYTDVALP--LYENLNiveqPVNLSslaqkyAEKATQFIQQAStSGR 239
Cdd:PRK13759 143 ylawlrekAPGKD-----PDLTDIG------WDCNSWVARPwdLEERLH----PTNWV------GSESIEFLRRRD-PTK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 240 PFLLYVGLAHMHVPL------------------------------PVTQLPAAPWG----------RRLYGAGLREMDGL 279
Cdd:PRK13759 201 PFFLKMSFARPHSPYdppkryfdmykdadipdphigdweyaedqdPEGGSIDALRGnlgeeyarraRAAYYGLITHIDHQ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 280 VGQIKDKV-DRTAKENTFLWFTGDNGpwaqkcELAGSvgpfTGLWQtrqggspaKQTTWEGGHRVPALAYWPG---RVPV 355
Cdd:PRK13759 281 IGRFLQALkEFGLLDNTIILFVSDHG------DMLGD----HYLFR--------KGYPYEGSAHIPFIIYDPGgllAGNR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 356 NVTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGrSQPGHRVLFHpnsgaaGEFGALqtvrlerYKAF-YIT 434
Cdd:PRK13759 343 GTVIDQVVELRDIMPTLLDLAGGTIP--DDVDGRSLKNLIFG-QYEGWRPYLH------GEHALG-------YSSDnYLT 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864488355 435 GGaracdgstgpemQHKF--------PLIFNLEDDIAEAMPLErGGTEYRAVLPKVRKVLADILQD 492
Cdd:PRK13759 407 DG------------KWKYiwfsqtgeEQLFDLKKDPHELHNLS-PSEKYQPRLREMRKKLVDHLRG 459
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-405 |
8.38e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 113.07 E-value: 8.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILAD-DIGWGDLGANWAETKdTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGL 114
Cdd:cd16035 1 PNILLILTDqERYPPPWPAGWAALN-LPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 115 PLNETTLAEVLQQAGYVTGMIGKWHLGHHGsyhpnfRGfdyyfgipyshdmgctdtpGYNHPPcpacpqgdgpsrnlqrd 194
Cdd:cd16035 80 SPDVPTLGHMLRAAGYYTAYKGKWHLSGAA------GG-------------------GYKRDP----------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 195 cytdvalplyenlniveqpvnlsslaqKYAEKATQFIQQASTS---GRPFLLYVGLAHMH-VPLPVTQLPAAPWGRRLYG 270
Cdd:cd16035 118 ---------------------------GIAAQAVEWLRERGAKnadGKPWFLVVSLVNPHdIMFPPDDEERWRRFRNFYY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 271 AGLREMDGLVGQIKDKVDRTA-KENTFLWFTGDNGpwaqkcELAGSVGpftGLwqtRQGGSPAKQTTwegghRVPALAYW 349
Cdd:cd16035 171 NLIRDVDRQIGRVLDALDASGlADNTIVVFTSDHG------EMGGAHG---LR---GKGFNAYEEAL-----HVPLIISH 233
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 350 PGRVPVNVTSTALLSVLDIFPTVVALAQASLPQ----GRRFDGVDVSEVLfgRSQPGHRV 405
Cdd:cd16035 234 PDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEArateAPPLPGRDLSPLL--TDADADAV 291
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-393 |
1.01e-27 |
|
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: 112.47 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 35 KPNFVIILADDIGWGDLGA-NWAETKD---------TTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTH 104
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCyNNAHTGKsesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 105 NFAVTSVGGLPLneTTLAEVLQQAGYVTGMIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqg 184
Cdd:cd16153 81 FEAAHPALDHGL--PTFPEVLKKAGYQTASFGKSHLE------------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 185 dgpsrNLQRdcYTDVALPLYENLNIVEqpvnlsslaqkyaekatqfIQQASTSGrPFLLYVGLAHMHVPLpvtqLPAAPW 264
Cdd:cd16153 116 -----AFQR--YLKNANQSYKSFWGKI-------------------AKGADSDK-PFFVRLSFLQPHTPV----LPPKEF 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 265 GRRL-YGAGLREMDGLVGQIKDKVDR----TAKENTFLWFTGDNGpwaqkcelagsvgpftglWQTRQGGSPAKQTTWEG 339
Cdd:cd16153 165 RDRFdYYAFCAYGDAQVGRAVEAFKAyslkQDRDYTIVYVTGDHG------------------WHLGEQGILAKFTFWPQ 226
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1864488355 340 GHRVPALAYWPGR--VPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSE 393
Cdd:cd16153 227 SHRVPLIVVSSDKlkAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-461 |
1.32e-27 |
|
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: 113.02 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggLP 115
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP-----YD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 116 LNETTLAEVLQQAGYVTGMIGKWHLGHHGSYHpnfrGFDYyfgipyshDMGCTDTpgynhppcpacpqgdgpsrnlqrdc 195
Cdd:cd16037 76 GDVPSWGHALRAAGYETVLIGKLHFRGEDQRH----GFRY--------DRDVTEA------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 196 ytdvalplyenlniveqpvnlsslaqkyaekATQFIQQASTSGRPFLLYVGLAHMHVPLPVTQ-------LPAapwgRRL 268
Cdd:cd16037 119 -------------------------------AVDWLREEAADDKPWFLFVGFVAPHFPLIAPQefydlyvRRA----RAA 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 269 YGAGLREMDGLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaqkcELAGSvgpfTGLWQtrqggspaKQTTWEGGHRVPALA 347
Cdd:cd16037 164 YYGLVEFLDENIGRVLDALEELGLlDNTLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMII 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 348 YWPGRVPVNVTSTAlLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGRSQPGHRVL--FHPNSGAAGEFgalqTVRL 425
Cdd:cd16037 226 SGPGIPAGKRVKTP-VSLVDLAPTILEAAGAPPP--PDLDGRSLLPLAEGPDDPDRVVFseYHAHGSPSGAF----MLRK 298
|
410 420 430
....*....|....*....|....*....|....*.
gi 1864488355 426 ERYKAFYITGGAracdgstgpemqhkfPLIFNLEDD 461
Cdd:cd16037 299 GRWKYIYYVGYP---------------PQLFDLEND 319
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-390 |
3.06e-27 |
|
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: 110.72 E-value: 3.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILAD----DIgwgdLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHnfavtsv 111
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWG------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 112 GGLPLNETTLAEVLQQAGYVTGMIGKWhlgHHGSYHPNF-RGFDYYFGIPYSHdmgcTDTPGYNHPPCPACpqgdgpsrn 190
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAVSSN---PHLFGGPGFdRGFDTFEDFRGQE----GDPGEEGDERAERV--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 191 lqrdcyTDVALplyenlniveqpvnlsslaqkyaekatQFIQQASTSgRPFLLYVglaHM---HvplpvtqlpaAPWgrr 267
Cdd:cd16148 134 ------TDRAL---------------------------EWLDRNADD-DPFFLFL---HYfdpH----------EPY--- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 268 LYGAGLREMDGLVGQIKDKVDRT-AKENTFLWFTGDNGpwaqkcELAGSVGPFTGlwqtrqGGSPAkqttWEGGHRVPAL 346
Cdd:cd16148 164 LYDAEVRYVDEQIGRLLDKLKELgLLEDTLVIVTSDHG------EEFGEHGLYWG------HGSNL----YDEQLHVPLI 227
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1864488355 347 AYWPGRVPVNVTStALLSVLDIFPTVVALAQASLPqgRRFDGVD 390
Cdd:cd16148 228 IRWPGKEPGKRVD-ALVSHIDIAPTLLDLLGVEPP--DYSDGRS 268
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
36-461 |
7.08e-27 |
|
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: 111.13 E-value: 7.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-----EFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 116 LNETTLAEVLQQAGYVTGMIGKWHlghhgsyhpnFRGFDYYFGipYSHDmgctdtpgynhppcpacpqgdgpsrnlqrdc 195
Cdd:cd16032 76 ADIPTFAHYLRAAGYRTALSGKMH----------FVGPDQLHG--FDYD------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 196 yTDVALplyenlniveqpvnlsslaqkyaeKATQFIQQASTS--GRPFLLYVGLAHMHVPLPVTQ------LPAApwgRR 267
Cdd:cd16032 113 -EEVAF------------------------KAVQKLYDLARGedGRPFFLTVSFTHPHDPYVIPQeywdlyVRRA---RR 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 268 LYGAGLREMDGLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaqkcELAGSvgpfTGLWQtrqggspaKQTTWEGGHRVPAL 346
Cdd:cd16032 165 AYYGMVSYVDDKVGQLLDTLERTGLaDDTIVIFTSDHG------DMLGE----RGLWY--------KMSFFEGSARVPLI 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 347 AYWPGR-VPVNVTstALLSVLDIFPTVVALAQASLPQGR-RFDGVDVSEVLFGRSQPGHRVLFHPNSGaAGEFGALQTVR 424
Cdd:cd16032 227 ISAPGRfAPRRVA--EPVSLVDLLPTLVDLAGGGTAPHVpPLDGRSLLPLLEGGDSGGEDEVISEYLA-EGAVAPCVMIR 303
|
410 420 430
....*....|....*....|....*....|....*..
gi 1864488355 425 LERYKAFYITGgaracDGstgpemqhkfPLIFNLEDD 461
Cdd:cd16032 304 RGRWKFIYCPG-----DP----------DQLFDLEAD 325
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
36-376 |
2.97e-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: 104.04 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCS-PSRASLLTGRLGLRNGVTHNFAVT----- 109
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSaPNHAALLTGAYPTLHGYTGNGSADpelps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 110 SVGGLPLNETTLAEVLQQAGYVTGMIGKWhlghhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIGLL--------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 190 nlqrdcytdvalplyenlniveqpvnlsslaqkyaekatQFIQQaSTSGRPFLLYVGLAHMHVPL--PVTQLPaapwgrr 267
Cdd:cd00016 110 ---------------------------------------KAIDE-TSKEKPFVLFLHFDGPDGPGhaYGPNTP------- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 268 LYGAGLREMDGLVGQIKDKVDRTAK-ENTFLWFTGDNGpwaqkcelagsvGPFTGLwqTRQGGSPAKQTTWEGGHRVPAL 346
Cdd:cd00016 143 EYYDAVEEIDERIGKVLDALKKAGDaDDTVIIVTADHG------------GIDKGH--GGDPKADGKADKSHTGMRVPFI 208
|
330 340 350
....*....|....*....|....*....|
gi 1864488355 347 AYWPGrVPVNVTSTALLSVLDIFPTVVALA 376
Cdd:cd00016 209 AYGPG-VKKGGVKHELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-140 |
2.68e-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: 92.68 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 35 KPNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtsVGGL 114
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPL 75
|
90 100
....*....|....*....|....*.
gi 1864488355 115 PLNETTLAEVLQQAGYVTGMIGKWHL 140
Cdd:cd16152 76 PADEKTLAHYFRDAGYETGYVGKWHL 101
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
36-429 |
4.90e-20 |
|
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: 92.83 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG-VTHNFAVTSvggl 114
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGsWTNCMALGD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 115 plNETTLAEVLQQAGYVTGMIGKWHLGhhgsyhpnfrGFDYY-FGIpyshdmgctdtpgynhppcpaCPQGDGPSRNLQR 193
Cdd:cd16156 77 --NVKTIGQRLSDNGIHTAYIGKWHLD----------GGDYFgNGI---------------------CPQGWDPDYWYDM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 194 DCYTD-----------VALPLYENLNIVEQpvnlSSLAQKYAEKATQFIQQASTsgRPFLLYVGLAHMHVP--------- 253
Cdd:cd16156 124 RNYLDelteeerrksrRGLTSLEAEGIKEE----FTYGHRCTNRALDFIEKHKD--EDFFLVVSYDEPHHPflcpkpyas 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 254 ------LPVTQ-----LPAAPWGRRLYGAGLREMDG-------------------LVGQIKDKVDRTAkENTFLWFTGDN 303
Cdd:cd16156 198 mykdfeFPKGEnayddLENKPLHQRLWAGAKPHEDGdkgtikhplyfgcnsfvdyEIGRVLDAADEIA-EDAWVIYTSDH 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 304 GpwaqkcELAGSvgpfTGLWqtrqGGSPAkqtTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQasLPQG 383
Cdd:cd16156 277 G------DMLGA----HKLW----AKGPA---VYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQP 337
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1864488355 384 RRFDGVDVSEVLFGRSQPGHRVLF---------HPNsgaageFGALQTVRL---ERYK 429
Cdd:cd16156 338 KVLEGESILATIEDPEIPENRGVFvefgryevdHDG------FGGFQPVRCvvdGRYK 389
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-399 |
2.68e-15 |
|
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: 78.05 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGR----LGLRNgvTHNFavtsv 111
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWyphvNGHRT--LHHL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 112 ggLPLNETTLAEVLQQAGYVTGMIGKWHLghhgsyhpnfrgfdyyfgIPYSHDMGCTDTPGYnhppcpacpqgdgpsrnl 191
Cdd:cd16150 74 --LRPDEPNLLKTLKDAGYHVAWAGKNDD------------------LPGEFAAEAYCDSDE------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 192 qrdcytdvalplyenlniveqpvnlsslaqKYAEKATQFIQQASTsGRPFLLYVGLAHMHVP---------------LPV 256
Cdd:cd16150 116 ------------------------------ACVRTAIDWLRNRRP-DKPFCLYLPLIFPHPPygveepwfsmidrekLPP 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 257 TQLPAAPWGRRLYGAGLRE-------------------------MDGLVGQIKDKVDRTA-KENTFLWFTGDNGPWAqkc 310
Cdd:cd16150 165 RRPPGLRAKGKPSMLEGIEkqgldrwseerwrelratylgmvsrLDHQFGRLLEALKETGlYDDTAVFFFSDHGDYT--- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 311 elagsvGPFtGLWQTRQGGSPAKQTtwegghRVPALAYWPGRVPVNVTStALLSVLDIFPTVVALAqaslpqgrrfdGVD 390
Cdd:cd16150 242 ------GDY-GLVEKWPNTFEDCLT------RVPLIIKPPGGPAGGVSD-ALVELVDIPPTLLDLA-----------GIP 296
|
....*....
gi 1864488355 391 VSEVLFGRS 399
Cdd:cd16150 297 LSHTHFGRS 305
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
36-383 |
4.13e-14 |
|
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: 73.73 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGrlgLRNGVTHNFavTSVGGLP 115
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG---LFTHLTESW--NNYKGLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 116 LNETTLAEVLQQAGYVTGMIGK--WHLGHHGSYHpnfRGFDYYFGIPYShdmgctdtpgynhppcpaCPQGDGPSRNLQR 193
Cdd:cd16171 76 PNYPTWMDRLEKHGYHTQKYGKldYTSGHHSVSN---RVEAWTRDVPFL------------------LRQEGRPTVNLVG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 194 DCYTDvalplyenlniveqpvNLSSLAQKYAEKATQFIQQASTS-GRPFLLYVGLAHMHvPLPVTQLPAAPWG----RRL 268
Cdd:cd16171 135 DRSTV----------------RVMLKDWQNTDKAVHWIRKEAPNlTQPFALYLGLNLPH-PYPSPSMGENFGSirniRAF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 269 YGAGLREMDGLVGQIKDKVDRTAKEN-TFLWFTGDNGpwaqkcELAgsvgpftglWQTRQGgspAKQTTWEGGHRVPALA 347
Cdd:cd16171 198 YYAMCAETDAMLGEIISALKDTGLLDkTYVFFTSDHG------ELA---------MEHRQF---YKMSMYEGSSHVPLLI 259
|
330 340 350
....*....|....*....|....*....|....*.
gi 1864488355 348 YWPGrVPVNVTSTALLSVLDIFPTVVALAQASLPQG 383
Cdd:cd16171 260 MGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN 294
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
36-157 |
2.07e-13 |
|
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: 72.29 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 36 PNFVIILADDIGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT-----PLD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1864488355 116 LNETTLAEVLQQAGYVTGMIGKWHL-----GHH------GSYHPNFRGFDYYF 157
Cdd:cd16028 76 ARHLTLALELRKAGYDPALFGYTDTspdprGLApldprlLSYELAMPGFDPVD 128
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
28-161 |
7.85e-06 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 48.50 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 28 SGKARGQKPNFVIIL-----ADDIGWGDLGANWaetkdTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV 102
Cdd:COG1368 227 NPFGPAKKPNVVVILlesfsDFFIGALGNGKDV-----TPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGS 301
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864488355 103 thnfAVTSVGGLPLNetTLAEVLQQAGYVTGMIgkwHlGHHGS------YHPNFrGFDYYFGIPY 161
Cdd:COG1368 302 ----PYKRPGQNNFP--SLPSILKKQGYETSFF---H-GGDGSfwnrdsFYKNL-GFDEFYDRED 355
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
14-162 |
6.76e-05 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 45.12 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 14 SFSGFLYPLVDFCFSGKARGQKPnFVIILADdigwGdLGANWAETKDTTNLDKMASEGMRFVDFHAA--ASTCsPSRASL 91
Cdd:COG1524 3 RGLSLLLASLLAAAAAAAPPAKK-VVLILVD----G-LRADLLERAHAPNLAALAARGVYARPLTSVfpSTTA-PAHTTL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864488355 92 LTGRLGLRNGVTHNF--------AVTSVGGLP--------LNETTLAEVLQQAGYVTGMIGKWHLGHHGSYHPN----FR 151
Cdd:COG1524 76 LTGLYPGEHGIVGNGwydpelgrVVNSLSWVEdgfgsnslLPVPTIFERARAAGLTTAAVFWPSFEGSGLIDAArpypYD 155
|
170
....*....|.
gi 1864488355 152 GFDYYFGIPYS 162
Cdd:COG1524 156 GRKPLLGNPAA 166
|
|
| |
