|
Name |
Accession |
Description |
Interval |
E-value |
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
35-496 |
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: 642.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 35 KPNFVIILADDMGWGDLGANWAET-KDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGG 113
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNaILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 194 dcytdvalplyenlniveqpvnlSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQLPAAP-RGRSLYGAG 272
Cdd:cd16161 132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPtSGRGPYGDA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 273 LWEMDSLVGQIKDKVDH-TVKENTFLWFTGDNGPWAQKCELAgsVGPFTGFWQTRQGGSPAKQTTWEGGHRVPALAYWPG 351
Cdd:cd16161 189 LQEMDDLVGQIMDAVKHaGLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 352 RVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHReeeagggkeaegaqsplcnalqmhgfl 431
Cdd:cd16161 267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHR--------------------------- 319
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462554007 432 VLFHPNSGAAGeFGALQTVRLERYKAFYITGGARACDGSTGPELQHKFPLIFNLEDDTAEAVPLE 496
Cdd:cd16161 320 CLFHPNSGAAG-AGALSAVRCGDYKAHYATGGALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT 383
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-495 |
0e+00 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293750 [Multi-domain] Cd Length: 399 Bit Score: 516.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRN-FAVTSVGG 113
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDMGCTDTPGYNHPPCPAcpqgdgpsrnlqr 193
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 194 dcytdvalPLYENLNIVEQPVNLSSLAQKYAEKATQFIQRAstSGRPFLLYVALAHMHVPLPVTQLPAAPRGRSLYGAGL 273
Cdd:cd16026 148 --------PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 274 WEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRVPALAYWPGR 352
Cdd:cd16026 218 EELDWSVGRILDALKELgLEENTLVIFTSDNGPWLEYGGHGGSAGPLRG----------GKGTTWEGGVRVPFIAWWPGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 353 VPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHREeeagggkeaegaqsplcnalqmhgflV 432
Cdd:cd16026 288 IPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHP--------------------------F 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462554007 433 LFHPNSgaagefGALQTVRLERYKAFYITGGARACDGSTGPELQHKFPLIFNLEDDTAEAVPL 495
Cdd:cd16026 342 FYYYDG------GDLQAVRSGRWKLHLPTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGETYNV 398
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
35-549 |
1.19e-115 |
|
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.
Pssm-ID: 293777 [Multi-domain] Cd Length: 479 Bit Score: 351.36 E-value: 1.19e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRN-FAVTSVGG 113
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGvFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 114 LPLNETTLAEVLQQAGYVTGIIGKWHL--GHHGSYHPNFRGFDYYFGIPYSHDMG-CTD-TPGYNHPPC-PACPQGDGPs 188
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLgvGLNGTYLPTHQGFDHYLGIPYSHDQGpCQNlTCFPPNIPCfGGCDQGEVP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 189 rnlqrdcytdvaLPLYENLNIVEQPVNLSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQLPAAPRGRSL 268
Cdd:cd16158 160 ------------CPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 269 YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFtgfwqtRQGgspaKQTTWEGGHRVPALA 347
Cdd:cd16158 228 FGDALAELDGSVGELLQTLKENgIDNNTLVFFTSDNGPSTMRKSRGGNAGLL------KCG----KGTTYEGGVREPAIA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 348 YWPGRVPVNVTStALLSVLDIFPTVVALAQASLPQgRRFDGVDVSEVLFGrSQPGHREEeagggkeaegaqsplcnalqm 427
Cdd:cd16158 298 YWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLPN-VTLDGVDMSPILFE-QGKSPRQT--------------------- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 428 hgflVLFHPNSgAAGEFGALqTVRLERYKAFYITGGA--------RACDGSTgPELQHKFPLIFNLEDDTAEAVPLErGG 499
Cdd:cd16158 354 ----FFYYPTS-PDPDKGVF-AVRWGKYKAHFYTQGAahsgttpdKDCHPSA-ELTSHDPPLLFDLSQDPSENYNLL-GL 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2462554007 500 AEYQAVLPEVRKVLADVLQDIANDNiSSADYTQDPSVTPCCN----PYQIACRC 549
Cdd:cd16158 426 PEYNQVLKQIQQVKERFEASMKFGE-SEINKGEDPALEPCCKpgctPKPSCCQC 478
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
35-514 |
2.05e-109 |
|
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its homologous proteins. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293779 [Multi-domain] Cd Length: 445 Bit Score: 334.01 E-value: 2.05e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV---TRNFAVTSV 111
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 112 GGLPLNETTLAEVLQQAGYVTGIIGKWHLG-----HHGSYH-PNFRGFDYY-FGIPYSHDMGCTDTPGYNhppcpacpqg 184
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDFVgTNLPFTNSWACDDTGRHV---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 185 DGPSRNLqrdCYtdvalpLYENLNIVEQPVNLSSLAQKYAEKATQFIQraSTSGRPFLLYVALAHMHVPLPVTQLPAAPR 264
Cdd:cd16160 151 DFPDRSA---CF------LYYNDTIVEQPIQHEHLTETLVGDAKSFIE--DNQENPFFLYFSFPQTHTPLFASKRFKGKS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 265 GRSLYGAGLWEMDSLVGQIKDK-VDHTVKENTFLWFTGDNGPWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRV 343
Cdd:cd16160 220 KRGRYGDNINEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKG----------GKGNSWEGGIRV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 344 PALAYWPGRVPVNVtSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHREeeagggkeaegaqsplcn 423
Cdd:cd16160 290 PFIAYWPGTIKPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDD------------------ 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 424 alqmhgflVLFHPNSgaagefgALQTVRLERYKAFYITG--------GARACDGSTGPEL------------QHKFPLIF 483
Cdd:cd16160 351 --------ILYYCCS-------RLMAVRYGSYKIHFKTQplpsqeslDPNCDGGGPLSDYivcydcedecvtKHNPPLIF 415
|
490 500 510
....*....|....*....|....*....|.
gi 2462554007 484 NLEDDTAEAVPLERGGAEYqaVLPEVRKVLA 514
Cdd:cd16160 416 DVEKDPGEQYPLQPSVYEH--MLEAVEKLIA 444
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-515 |
1.42e-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: 312.09 E-value: 1.42e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG--VTRNFAVTS-- 110
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 111 ----VGGLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHdMGCTDTPGYNHPPcpacpqgdg 186
Cdd:cd16157 81 pqniVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCH-FGPYDNKAYPNIP--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 187 psrnLQRDcyTDVALPLYENLNIvEQPVNLSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQLPAAPRGR 266
Cdd:cd16157 151 ----VYRD--WEMIGRYYEEFKI-DKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 267 SLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNG-PWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRVP 344
Cdd:cd16157 224 GLYGDAVMELDSSVGKILESLKSLgIENNTFVFFSSDNGaALISAPEQGGSNGPFLC----------GKQTTFEGGMREP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 345 ALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFgrsqpghreeeagGGKEAEGAqsplcna 424
Cdd:cd16157 294 AIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLL-------------NGKEKDRP------- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 425 lqmhgflVLFHPNSgaagefgALQTVRLERYKAFYIT---------GGARACDG------STGPELQH-KFPLIFNLEDD 488
Cdd:cd16157 354 -------IFYYRGD-------ELMAVRLGQYKAHFWTwsnsweefrKGINFCPGqnvpgvTTHNQTDHtKLPLLFHLGRD 419
|
490 500
....*....|....*....|....*..
gi 2462554007 489 TAEAVPLERGGAEYQAVLPEVRKVLAD 515
Cdd:cd16157 420 PGEKYPISFKSAEYKQAMPRISKVVQQ 446
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
35-521 |
3.56e-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: 304.98 E-value: 3.56e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGR------LGLRNGVTRNFAV 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRypirsgMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 109 TSVGGLPLNETTLAEVLQQAGYVTGIIGKWHLGHH------GSYHPNFRGFDYYFGIPYSHDMGCTDTPG--YNHPPCP- 179
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHcesrndFCHHPLNHGFDYFYGLPLTNLKDCGDGSNgeYDLSFDPl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 180 ------ACPQGDGPSRNLQRD-------------CYTDVALP--------------LYENLNIVEQPVNLSSLAQKYAEK 226
Cdd:cd16159 161 fplltaFVLITALTIFLLLYLgavskrffvflliLSLLFISLfflllitnryfnciLMRNHEVVEQPMSLENLTQRLTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 227 ATQFIQRasTSGRPFLLYVALAHMHvplpvTQLPAAP--RGRS---LYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFT 300
Cdd:cd16159 241 AISFLER--NKERPFLLVMSFLHVH-----TALFTSKkfKGRSkhgRYGDNVEEMDWSVGQILDALDELgLKDNTFVYFT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 301 GDNGPWAqkcELAGSVGPFTGFWQTRQGGSpaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASL 380
Cdd:cd16159 314 SDNGGHL---EEISVGGEYGGGNGGIYGGK--KMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 381 PQGRRFDGVDVSEVLFGRSQpghreeeagggkeaegaQSP------LCNAlQMHGflVLFHPNSGAAgefgalqtvrleR 454
Cdd:cd16159 389 PSDRIIDGRDLMPLLTGQEK-----------------RSPheflfhYCGA-ELHA--VRYRPRDGGA------------V 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462554007 455 YKAFYIT-----GGARA-------CDGSTGpeLQHKFPLIFNLEDDTAEAVPLERGGAEYQAVLPEVRKVLADVLQDIA 521
Cdd:cd16159 437 WKAHYFTpnfypGTEGCcgtllcrCFGDSV--THHDPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIE 513
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-488 |
7.33e-90 |
|
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: 280.96 E-value: 7.33e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGAN---WAETKDTANLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTRNFAVTSVG 112
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYgggIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 113 GLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHdmgctdtpgynhppcpacpqgdgpsrnlq 192
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYHT----------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 193 rdcytdvalplyenlniveqpvnlssLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVP-LPVTQLPAAPRGRSLYGA 271
Cdd:cd16142 131 --------------------------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPtLPSPEFEGKSSGKGKYAD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 272 GLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSvGPFTGfwqtrqggspAKQTTWEGGHRVPALAYWP 350
Cdd:cd16142 185 SMVELDDHVGQILDALDELgIADNTIVIFTTDNGPEQDVWPDGGY-TPFRG----------EKGTTWEGGVRVPAIVRWP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 351 GRVPVNVTSTALLSVLDIFPTVVALAQASLP------QGRRFDGVDVSEVLFGRSQPGHREEeagggkeaegaqsplcna 424
Cdd:cd16142 254 GKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSE------------------ 315
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462554007 425 lqmhgflVLFHPNsgaaGEFGAlqtVRLERYKA-FYITGGARAcdGSTGPELQHKFPLIFNLEDD 488
Cdd:cd16142 316 -------FFYFGE----GELGA---VRWKNWKVhFKAQEDTGG--PTGEPFYVLTFPLIFNLRRD 364
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
34-524 |
1.16e-83 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 265.59 E-value: 1.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvTSVGG 113
Cdd:COG3119 22 KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE-GYNGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 114 LPLNETTLAEVLQQAGYVTGIIGKWHLghhgsyhpnfrgfdyyfgipYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:COG3119 101 LPPDEPTLAELLKEAGYRTALFGKWHL--------------------YLTD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 194 dcytdvalplyenlniveqpvnlsslaqKYAEKATQFIQRASTSGRPFLLYVALAHMHVP-----------------LPV 256
Cdd:COG3119 132 ----------------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPyqapeeyldkydgkdipLPP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 257 TQLPAA------PRGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAqkcelagsvgpftGFWQTRQGg 329
Cdd:COG3119 184 NLAPRDlteeelRRARAAYAAMIEEVDDQVGRLLDALEELgLADNTIVVFTSDNGPSL-------------GEHGLRGG- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 330 spaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHREeeag 409
Cdd:COG3119 250 ---KGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDY---- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 410 ggkeaegaqsplcnalqmhgflVLFHpnsgaAGEFGALQTVRLERYKAFYITGGARAcdgstgPELqhkfpliFNLEDDT 489
Cdd:COG3119 321 ----------------------LYWE-----YPRGGGNRAIRTGRWKLIRYYDDDGP------WEL-------YDLKNDP 360
|
490 500 510
....*....|....*....|....*....|....*
gi 2462554007 490 AEAVPLergGAEYqavlPEVRKVLADVLQDIANDN 524
Cdd:COG3119 361 GETNNL---AADY----PEVVAELRALLEAWLKEL 388
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-405 |
3.46e-83 |
|
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: 265.18 E-value: 3.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTG----RLGL---------RNGV 102
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGqypaRLGItdvipgrrgPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 103 TRNFAVTSVGGLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGI-PYSHDMGCTDTPGYNHPPCPAC 181
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIGGtGNGGPPSYYFPPGKPNPDLEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 182 PQGDgpsrnlqrdcytdvalplyenlniveqpvnlsSLAQKYAEKATQFIQRAstSGRPFLLYvaLAH--MHVPLPVTQ- 258
Cdd:cd16144 161 PEGE--------------------------------YLTDRLTDEAIDFIEQN--KDKPFFLY--LSHyaVHTPIQARPe 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 259 -------LPAAPRGR---SLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFtgfwqtRQ 327
Cdd:cd16144 205 liekyekKKKGLRKGqknPVYAAMIESLDESVGRILDALEELgLADNTLVIFTSDNGGLSTRGGPPTSNAPL------RG 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462554007 328 GgspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRE 405
Cdd:cd16144 279 G----KGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRR 352
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-406 |
1.70e-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: 260.21 E-value: 1.70e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETK-DTANLDKMASEGMRFVDFHAAASTCSPSRASLLTG----RLGLRNGVTRNFavts 110
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGrypwRSRLKGGVLGGF---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 111 vgGLPL---NETTLAEVLQQAGYVTGIIGKWHLG-----------HHGSYH-----------PNFRGFDYYFGIPYShdm 165
Cdd:cd16143 77 --SPPLiepDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkaATGTGKdvdyskpikggPLDHGFDYYFGIPAS--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 166 gctdtpgynhppcpacpqgdgpsrnlqrdcytDVaLPLyenlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYV 245
Cdd:cd16143 152 --------------------------------EV-LPT-------------------LTDKAVEFIDQHAKKDKPFFLYF 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 246 ALAHMHVPLpvtqLPAAP-RGRS---LYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGPwaqkcelagsvGPFT 320
Cdd:cd16143 180 ALPAPHTPI----VPSPEfQGKSgagPYGDFVYELDWVVGRILDALKeLGLAENTLVIFTSDNGP-----------SPYA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 321 GFWQT-RQGGSPA------KQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSE 393
Cdd:cd16143 245 DYKELeKFGHDPSgplrgmKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLP 324
|
410
....*....|...
gi 2462554007 394 VLFGRSQPGHREE 406
Cdd:cd16143 325 ALLGPKKQEVRES 337
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-491 |
1.19e-76 |
|
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: 248.28 E-value: 1.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGGLP 115
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 116 LNETTLAEVLQQAGYVTGIIGKWHLGHHGSY-HPNFRGFDYYFGIpYSHdmgctdTPGYNHPPcpacPQGDgpsRNLQRd 194
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYGY-LDQ------VHAHNYYP----EYLW---RNGEK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 195 cytdvaLPLYENLNIVEQPVNLSSLAQK-YAE-----KATQFIQRAstSGRPFLLYVALAHMHVPLPVTQLPAA---PRG 265
Cdd:cd16145 146 ------VPLPNNVIPPLDEGNNAGGGGGtYSHdlftdEALDFIREN--KDKPFFLYLAYTLPHAPLQVPDDGPYkykPKD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 266 RSLYGAGLWE------------MDSLVGQIKDKV-DHTVKENTFLWFTGDNGP-----WAQKCELAGSVGPFTGFwqtrq 327
Cdd:cd16145 218 PGIYAYLPWPqpekayaamvtrLDRDVGRILALLkELGIDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 328 ggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPghreee 407
Cdd:cd16145 293 -----KRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPE--DIDGISLLPTLLGKPQQ------ 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 408 agggkeaegaqsplcnalQMHGFLVL-FHpnsgaagEFGALQTVRLERYKAFYItggaracDGSTGP-ELqhkfpliFNL 485
Cdd:cd16145 360 ------------------QQHDYLYWeFY-------EGGGAQAVRMGGWKAVRH-------GKKDGPfEL-------YDL 400
|
....*.
gi 2462554007 486 EDDTAE 491
Cdd:cd16145 401 STDPGE 406
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
36-401 |
2.90e-75 |
|
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: 244.38 E-value: 2.90e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTRnfavTSVGG-- 113
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWH----TILGRer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgcTDTPGYnhppcpacpqgdgpsrnLQR 193
Cdd:cd16146 76 MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGGGI---GQYPDY-----------------WGN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 194 DCYTDValpLYENlNIVEQpvnlsslAQKYA-----EKATQFIQRASTsgRPFLLYVALAHMHVPLPVTQLPAAP----- 263
Cdd:cd16146 136 DYFDDT---YYHN-GKFVK-------TEGYCtdvffDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPykdmg 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 264 --RGRSLYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGPWaqkcelAGSVGPFTGFWQtrqgGSpaKQTTWEGG 340
Cdd:cd16146 203 ldDKLAAFYGMIENIDDNVGRLLAKLKeLGLEENTIVIFMSDNGPA------GGVPKRFNAGMR----GK--KGSVYEGG 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462554007 341 HRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQP 401
Cdd:cd16146 271 HRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDP 331
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
36-390 |
3.03e-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: 220.00 E-value: 3.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNfaVTSVGGLP 115
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 116 LNETTLAEVLQQAGYVTGIIGKWHlghhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsrnlqrdc 195
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 196 ytdvalplyenlniveqpvnlsslaqkyaEKATQFIQRASTSgRPFLLYVALAHMHVPLpvtqlpaaprgrsLYGAGLWE 275
Cdd:cd16022 103 -----------------------------DEAIDFIERRDKD-KPFFLYVSFNAPHPPF-------------AYYAMVSA 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 276 MDSLVGQIKDKVDHT-VKENTFLWFTGDNgpwaqkcelagsvGPFTGFWQTRQGgspaKQTTWEGGHRVPALAYWPGRVP 354
Cdd:cd16022 140 IDDQIGRILDALEELgLLDNTLIVFTSDH-------------GDMLGDHGLRGK----KGSLYEGGIRVPFIVRWPGKIP 202
|
330 340 350
....*....|....*....|....*....|....*.
gi 2462554007 355 VNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVD 390
Cdd:cd16022 203 AGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
36-406 |
1.49e-65 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 218.19 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFvDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSV-GGL 114
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVIL-NNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEpYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 115 PLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYH-PNFRGFDYYFGiPYShdmGCTDtpGYNHPPCPACP------QGDGP 187
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYTWEYtPTNRGFDSFYG-YYG---GAED--YYTHTSGGANDygnddlRDNEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 188 SRNLQRDCY-TDValplyenlniveqpvnlsslaqkYAEKATQFIQRASTSgRPFLLYVALAHMHVPLPVTQLPAAP--- 263
Cdd:cd16029 154 PAWDYNGTYsTDL-----------------------FTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPyed 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 264 -------RGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCElAGSVGPFTGfwqtrqggspAKQT 335
Cdd:cd16029 210 kfahikdEDRRTYAAMVSALDESVGNVVDALKAKgMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRG----------GKNT 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462554007 336 TWEGGHRVPALAYWPGRVPV-NVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSqPGHREE 406
Cdd:cd16029 279 LWEGGVRVPAFVWSPLLPPKrGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGA-PSPRTE 349
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-405 |
6.92e-60 |
|
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: 202.83 E-value: 6.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTRnfavtsvGGLP 115
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPL-CTPSRVQLMTGKYNFRNYVVF-------GYLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 116 LNETTLAEVLQQAGYVTGIIGKWHLG---HHGSYHPNFrGFDYY--FGipyshdmGCTDTPGYNHPPCPACPQGDGPSRN 190
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGKWQLGggrGDGDYPHEF-GFDEYclWQ-------LTETGEKYSRPATPTFNIRNGKLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 191 LQRDCY-TDValplyenlniveqpvnlsslaqkYAEKATQFIQRAstSGRPFLLY--VALAH-MHVPLPVTQLPAAPRGR 266
Cdd:cd16151 145 TTEGDYgPDL-----------------------FADFLIDFIERN--KDQPFFAYypMVLVHdPFVPTPDSPDWDPDDKR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 267 S-----LYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNgpwaqkcelaGSVGPFTGFW--QTRQGGspaKQTTWE 338
Cdd:cd16151 200 KkddpeYFPDMVAYMDKLVGKLVDKLEELgLRENTIIIFTGDN----------GTHRPITSRTngREVRGG---KGKTTD 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462554007 339 GGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRE 405
Cdd:cd16151 267 AGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRRE 333
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
36-378 |
5.26e-56 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 190.33 E-value: 5.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrnfaVTSVGGLP 115
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSY----VSTPVGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 116 LNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFG-IPYSHDMGCTDTPGYNHPPcpacpqgdgpsrnlqRD 194
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLYADPPDVPYNCSG---------------GG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 195 CYTDValplyenlniveqpvnlsslaqkYAEKATQFIQRAStsgRPFLLYVALAHMHVPLPVTQLPAAP----------- 263
Cdd:pfam00884 142 VSDEA-----------------------LLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscse 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 264 -RGRSLYGAGLWEMDSLVGQIKDKV-DHTVKENTFLWFTGDNGPwaqkcelagSVGPFTGFWQTRQGGspakqTTWEGGH 341
Cdd:pfam00884 196 eQLLNSYDNTLLYTDDAIGRVLDKLeENGLLDNTLVVYTSDHGE---------SLGEGGGYLHGGKYD-----NAPEGGY 261
|
330 340 350
....*....|....*....|....*....|....*..
gi 2462554007 342 RVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQA 378
Cdd:pfam00884 262 RVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
34-406 |
1.66e-53 |
|
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: 186.49 E-value: 1.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 34 QKPNFVIILADDMGWGDLGANWAETkDTANLDKMASEGMRFVDFHAAAsTCSPSRASLLTGRLGLRNGVtRNFAVTSVGG 113
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEI-PTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 114 ------LPLNETTLAEVLQQAGYVTGIIGKWHLGHHgsyhpnfrgfDYYFgipySHDmgctdtpgynhppcpacpqgdgp 187
Cdd:cd16025 78 pgyegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------DYYS----TDD----------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 188 srnlqrdcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYVALAHMHVPL------------- 254
Cdd:cd16025 121 -----------------------------------LTDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLqapkewidkykgk 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 255 -----------------------PVTQLPAAPRG-----------RSLYG------AGLWE-MDSLVGQIKDKVDHT-VK 292
Cdd:cd16025 166 ydagwdalreerlerqkelglipADTKLTPRPPGvpawdslspeeKKLEArrmevyAAMVEhMDQQIGRLIDYLKELgEL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 293 ENTFLWFTGDNGP-----WAQkcelAGSvGPFTGFwqtrqggspaKQTTWEGGHRVPALAYWPGRV-PVNVTSTALLSVL 366
Cdd:cd16025 246 DNTLIIFLSDNGAsaepgWAN----ASN-TPFRLY----------KQASHEGGIRTPLIVSWPKGIkAKGGIRHQFAHVI 310
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2462554007 367 DIFPTVVALAQASLPQGRR------FDGVDVSEVLFGRSQPGHREE 406
Cdd:cd16025 311 DIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRT 356
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
36-405 |
2.47e-50 |
|
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: 177.32 E-value: 2.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGA--NWAETkdtANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFavTSVGG 113
Cdd:cd16027 1 PNILWIIADDLSPDLGGYggNVVKT---PNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR--SRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 193
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAWD----------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 194 dcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQRAStSGRPFLLYVALAHMH-----------------VPLPv 256
Cdd:cd16027 127 -----------------------------YASNAADFLNRAK-KGQPFFLWFGFHDPHrpyppgdgeepgydpekVKVP- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 257 TQLPAAPRGR---SLYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGpwaqkcelagsvGPFTGfwqtrqggspA 332
Cdd:cd16027 176 PYLPDTPEVRedlADYYDEIERLDQQVGEILDELEeDGLLDNTIVIFTSDHG------------MPFPR----------A 233
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462554007 333 KQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHRE 405
Cdd:cd16027 234 KGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGRDY 304
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-488 |
1.12e-47 |
|
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: 170.83 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVtsvggL 114
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 115 PLNETTLAEVLQQAGYVTGIIGKWHL-GHHGSYH--------PNFR-GFDYYFGipyshdMGCTDtpGYNHPPCpacpQG 184
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGraddytppPERRhGFDYWKG------YECNH--DHNNPHY----YD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 185 DGPSRNlQRDCYTDVALplyenlniveqpvnlsslaqkyAEKATQFIQRASTSGRPFLLYVALAHMHVP----------- 253
Cdd:cd16034 144 DDGKRI-YIKGYSPDAE----------------------TDLAIEYLENQADKDKPFALVLSWNPPHDPyttapeeyldm 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 254 -----------LPVTQLPAAPRGRSL---YGA--GLwemDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSV 316
Cdd:cd16034 201 ydpkklllrpnVPEDKKEEAGLREDLrgyYAMitAL---DDNIGRLLDALKELgLLENTIVVFTSDHG------DMLGSH 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 317 GPFtgfwqtrqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLF 396
Cdd:cd16034 272 GLM------------NKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 397 GRSQPGHREEeagggkeaegaqsplcnalqmhgFLVLFHPNSG-AAGEFGALQTVRLERYKafYitggarACDGSTGpel 475
Cdd:cd16034 338 GGKDDEPDSV-----------------------LLQCFVPFGGgSARDGGEWRGVRTDRYT--Y------VRDKNGP--- 383
|
490
....*....|...
gi 2462554007 476 qhkfPLIFNLEDD 488
Cdd:cd16034 384 ----WLLFDNEKD 392
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
34-406 |
4.30e-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: 156.15 E-value: 4.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvGG 113
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG----PL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGsYHPNfRGFDYYFGIPyshdmgctdtpgynhppcpacPQGDgpsrnlqr 193
Cdd:cd16031 77 FDASQPTYPKLLRKAGYQTAFIGKWHLGSGG-DLPP-PGFDYWVSFP---------------------GQGS-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 194 dcYTDvaLPLYENLNIVEQPVNLSSLaqkYAEKATQFIQRAStSGRPFLLYV-----------ALAHMHV------PLPV 256
Cdd:cd16031 126 --YYD--PEFIENGKRVGQKGYVTDI---ITDKALDFLKERD-KDKPFCLSLsfkaphrpftpAPRHRGLyedvtiPEPE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 257 TQLPA--APRGRSL---------------------------YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpw 306
Cdd:cd16031 198 TFDDDdyAGRPEWAreqrnrirgvldgrfdtpekyqrymkdYLRTVTGVDDNVGRILDYLEEQgLADNTIIIYTSDNG-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 307 aqkcELAGSVGpFTGfwqtrqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPqgRRF 386
Cdd:cd16031 276 ----FFLGEHG-LFD-----------KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIP--EDM 337
|
410 420
....*....|....*....|
gi 2462554007 387 DGVDVSEVLFGRSQPGHREE 406
Cdd:cd16031 338 QGRSLLPLLEGEKPVDWRKE 357
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-388 |
1.16e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 150.47 E-value: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV-----TRNFAVTS 110
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 111 VG-GLPLNETTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd16149 81 KPeGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 190 nlqrdcytdvalplyenlniveqpvnlsslaqkyaEKATQFIQRASTSGRPFLLYVAlahmhvplpvTQLPAAPRGrslY 269
Cdd:cd16149 113 -----------------------------------DDAADFLRRRAEAEKPFFLSVN----------YTAPHSPWG---Y 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 270 GAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcelagsvgpFT----GFWQTRQGGSPakQTTWEGGHRVP 344
Cdd:cd16149 145 FAAVTGVDRNVGRLLDELEELgLTENTLVIFTSDNG--------------FNmghhGIWGKGNGTFP--LNMYDNSVKVP 208
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2462554007 345 ALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDG 388
Cdd:cd16149 209 FIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPG 252
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-404 |
1.68e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 142.10 E-value: 1.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWgDLGANWAETKD---TANLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTrnfavtSVG 112
Cdd:cd16154 1 PNILLIIADDQGL-DSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVL------AVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 113 G-LPLNETTL--AEVLQQ--AGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIpyshdMGctdtpgynhppcpacpqGDGP 187
Cdd:cd16154 73 DeLLLSEETLlqLLIKDAttAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGI-----LG-----------------GGVQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 188 SrnlqrdcYTDVALplyeNLNIVEQPVN------LSSLAQKYAEKATQfiqrastsgrPFLLYVALAHMHVPLpvtQLPA 261
Cdd:cd16154 131 D-------YYNWNL----TNNGQTTNSTeyattkLTNLAIDWIDQQTK----------PWFLWLAYNAPHTPF---HLPP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 262 A---PRG------------RSLYGAGLWEMDSLVGQIKDKVDHTVKENTFLWFTGDNG-PwaqkcelagsvGPFTGFWQT 325
Cdd:cd16154 187 AelhSRSllgdsadieanpRPYYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGtP-----------GQVVDLPYT 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462554007 326 RQGgspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPGHR 404
Cdd:cd16154 256 RNH---AKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNASTRQ 329
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
35-388 |
2.49e-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: 136.91 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 35 KPNFVIILADDMGWgDLGANWAETKdTANLdkMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtSVGGL 114
Cdd:cd16147 1 RPNIVLILTDDQDV-ELGSMDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSP--PGGGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 115 P------LNETTLAEVLQQAGYVTGIIGK----WHLGHHGSYHPnfRGFDYYFGI-------PYSHDMGCTDTPGYNHPp 177
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYVP--PGWDEWDGLvgnstyyNYTLSNGGNGKHGVSYP- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 178 cpacpqgdgpsrnlqRDCYTDValplyenlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYVA----------- 246
Cdd:cd16147 152 ---------------GDYLTDV-----------------------IANKALDFLRRAAADDKPFFLVVAppaphgpftpa 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 247 --LAHMHVPLPVT------------------QLPAAP-----------RGRslygaglWE----MDSLVGQIKDKVDHT- 290
Cdd:cd16147 194 prYANLFPNVTAPprpppnnpdvsdkphwlrRLPPLNptqiayidelyRKR-------LRtlqsVDDLVERLVNTLEATg 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 291 VKENTFLWFTGDNgpwaqkcelagsvgpftGFW--QTRQGgsPAKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDI 368
Cdd:cd16147 267 QLDNTYIIYTSDN-----------------GYHlgQHRLP--PGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDL 326
|
410 420
....*....|....*....|
gi 2462554007 369 FPTVVALAQASLPqgRRFDG 388
Cdd:cd16147 327 APTILDLAGAPPP--SDMDG 344
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-406 |
2.34e-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: 134.27 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNF--AVTSVGG 113
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 114 LPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSyhPNFRGFDYYFgiPYSH-------DMGC--------TDTP-----GY 173
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVGPEET--PLDYGFDEYL--PVETtieyflaDRAIemleelaaDDKPfflrvNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 174 NHPPCPACPqgdgPSRNLqrDCYTDVALPLYENLNiveqpvnlSSLAQK---YAEKATQFIQRASTSG--RPfllyvALA 248
Cdd:cd16033 157 WGPHDPYIP----PEPYL--DMYDPEDIPLPESFA--------DDFEDKpyiYRRERKRWGVDTEDEEdwKE-----IIA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 249 HmhvplpvtqlpaaprgrslYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGPFTgfwqtrQ 327
Cdd:cd16033 218 H-------------------YWGYITLIDDAIGRILDALEELgLADDTLVIFTSDHG------DALGAHRLWD------K 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462554007 328 GGSPAKQTtweggHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGRSQPGHREE 406
Cdd:cd16033 267 GPFMYEET-----YRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVP--PKVDGRSLLPLLRGEQPEDWRDE 338
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
432-549 |
1.63e-30 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 115.49 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 432 VLFHpNSGAAgefgaLQTVRLERYKAFYITG-----GARACDGSTGPELQHKFPLIFNLEDDTAEAVPLERGGAEYQAVL 506
Cdd:pfam14707 5 FLFH-YCGAA-----LHAVRWGPYKAHFFTPsfdppGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYPEVL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462554007 507 PEVRKVLADVLQDI--ANDNISSADYTQDPSVTPCCnPYQIACRC 549
Cdd:pfam14707 79 AEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-395 |
5.09e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 121.13 E-value: 5.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAAST----CSPSRASLLTGRLGLRNGVTRNFAvt 109
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFHAPEGGKAA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 110 svggLPLNETTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd16155 79 ----IPSDDKTWPETFKKAGYRTFATGKWHNG------------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 190 nlqrdcytdvalplyenlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYVALAHMH-----------------V 252
Cdd:cd16155 107 ---------------------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHdprqappeyldmyppetI 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 253 PLPVTQLPAAP------------------------RGRSLYGAGLWEMDSLVGQIKDKVDHTVK-ENTFLWFTGDNGpwa 307
Cdd:cd16155 154 PLPENFLPQHPfdngegtvrdeqlapfprtpeavrQHLAEYYAMITHLDAQIGRILDALEASGElDNTIIVFTSDHG--- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 308 qkceLAgsVGpftgfwqtrQGGSPAKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFD 387
Cdd:cd16155 231 ----LA--VG---------SHGLMGKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES--VE 292
|
....*...
gi 2462554007 388 GVDVSEVL 395
Cdd:cd16155 293 GKSLLPVI 300
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
31-406 |
1.57e-29 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 121.70 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 31 TRGQKPNFVIILADDMGwGD-LGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNGV 102
Cdd:PRK13759 2 VQTKKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 103 TRNFavtsvgglplnETTLAEVLQQAGYVTGIIGKWHlghhgsYHP--NFRGFD--------YYFGIPYSH---DMgCTD 169
Cdd:PRK13759 81 PWNY-----------KNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHnvllhdgyLHSGRNEDKsqfDF-VSD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 170 --------TPGYNhppcpACPQGDGpsrnlqRDCYTDVALP--LYENLNiveqPVNLSslaqkyAEKATQFIQRAStSGR 239
Cdd:PRK13759 143 ylawlrekAPGKD-----PDLTDIG------WDCNSWVARPwdLEERLH----PTNWV------GSESIEFLRRRD-PTK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 240 PFLLYVALAHMHVPL--PV--------TQLPAAPRGRSLYGAGLW----EMDSLVGQIKDK---------------VDH- 289
Cdd:PRK13759 201 PFFLKMSFARPHSPYdpPKryfdmykdADIPDPHIGDWEYAEDQDpeggSIDALRGNLGEEyarraraayyglithIDHq 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 290 ------TVKE-----NTFLWFTGDNGpwaqkcELAGSVGPFTgfwqtrqggspaKQTTWEGGHRVPALAYWPG---RVPV 355
Cdd:PRK13759 281 igrflqALKEfglldNTIILFVSDHG------DMLGDHYLFR------------KGYPYEGSAHIPFIIYDPGgllAGNR 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2462554007 356 NVTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGrSQPGHREE 406
Cdd:PRK13759 343 GTVIDQVVELRDIMPTLLDLAGGTIP--DDVDGRSLKNLIFG-QYEGWRPY 390
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-390 |
1.88e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 114.18 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILAD----DMgwgdLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrnfavtsV 111
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW-------G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 112 GGLPLNETTLAEVLQQAGYVTGIIGKWhlgHHGSYHPNF-RGFDYYFGIPYSHdmgcTDTPGYNHPPCPACpqgdgpsrn 190
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAVSSN---PHLFGGPGFdRGFDTFEDFRGQE----GDPGEEGDERAERV--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 191 lqrdcyTDVALplyenlniveqpvnlsslaqkyaekatQFIQRASTSgRPFLLYValaHMHvplpvtqlpaAPRGRSLYG 270
Cdd:cd16148 134 ------TDRAL---------------------------EWLDRNADD-DPFFLFL---HYF----------DPHEPYLYD 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 271 AGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGpwaqkcELAGSVGPFTGFWqtrqggspakQTTWEGGHRVPALAYW 349
Cdd:cd16148 167 AEVRYVDEQIGRLLDKLKeLGLLEDTLVIVTSDHG------EEFGEHGLYWGHG----------SNLYDEQLHVPLIIRW 230
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2462554007 350 PGRVPVNVTStALLSVLDIFPTVVALAQASLPqgRRFDGVD 390
Cdd:cd16148 231 PGKEPGKRVD-ALVSHIDIAPTLLDLLGVEPP--DYSDGRS 268
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-408 |
6.36e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 111.15 E-value: 6.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDM-GWGDLGANWAETKDTAnLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGGL 114
Cdd:cd16035 1 PNILLILTDQErYPPPWPAGWAALNLPA-RERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 115 PLNETTLAEVLQQAGYVTGIIGKWHLGHHGsyhpnfRGfdyyfgipyshdmgctdtpGYNHppcpacpqgDGpsrnlqrd 194
Cdd:cd16035 80 SPDVPTLGHMLRAAGYYTAYKGKWHLSGAA------GG-------------------GYKR---------DP-------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 195 cytdvalplyenlniveqpvnlsslaqKYAEKATQFIQRASTS---GRPFLLYVALAHMH-VPLPVTQLPAAPRGRSLYG 270
Cdd:cd16035 118 ---------------------------GIAAQAVEWLRERGAKnadGKPWFLVVSLVNPHdIMFPPDDEERWRRFRNFYY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 271 AGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGpftgfwQTRQGGSPAKQTTwegghRVPALAYW 349
Cdd:cd16035 171 NLIRDVDRQIGRVLDALDASgLADNTIVVFTSDHG------EMGGAHG------LRGKGFNAYEEAL-----HVPLIISH 233
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462554007 350 PGRVPVNVTSTALLSVLDIFPTVVALAQASLPQ----GRRFDGVDVSEVLfgRSQPGHREEEA 408
Cdd:cd16035 234 PDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEArateAPPLPGRDLSPLL--TDADADAVRDG 294
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-390 |
3.27e-25 |
|
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: 106.09 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVtsvggLP 115
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP-----YD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 116 LNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHpnfrGFDYyfgipyshDMGCTDTpgynhppcpacpqgdgpsrnlqrdc 195
Cdd:cd16037 76 GDVPSWGHALRAAGYETVLIGKLHFRGEDQRH----GFRY--------DRDVTEA------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 196 ytdvalplyenlniveqpvnlsslaqkyaekATQFIQRASTSGRPFLLYVALAHMHVPLPVTQ---LPAAPRGRSLYGAG 272
Cdd:cd16037 119 -------------------------------AVDWLREEAADDKPWFLFVGFVAPHFPLIAPQefyDLYVRRARAAYYGL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 273 LWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSvgpfTGFWQtrqggspaKQTTWEGGHRVPALAYWPG 351
Cdd:cd16037 168 VEFLDENIGRVLDALEELgLLDNTLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMIISGPG 229
|
330 340 350
....*....|....*....|....*....|....*....
gi 2462554007 352 RVPVNVTSTAlLSVLDIFPTVVALAQASLPqgRRFDGVD 390
Cdd:cd16037 230 IPAGKRVKTP-VSLVDLAPTILEAAGAPPP--PDLDGRS 265
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
36-422 |
4.24e-25 |
|
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: 106.12 E-value: 4.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvgGLP 115
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-----EFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 116 LNETTLAEVLQQAGYVTGIIGKWHL-G---HHGsyhpnfrgFDYyfgipyshdmgctdtpgynhppcpacpqgdgpsrnl 191
Cdd:cd16032 76 ADIPTFAHYLRAAGYRTALSGKMHFvGpdqLHG--------FDY------------------------------------ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 192 qrDcyTDVALplyenlniveqpvnlsslaqkyaeKATQFI-QRA-STSGRPFLLYVALAHMHVPLPVTQ------LPAAp 263
Cdd:cd16032 112 --D--EEVAF------------------------KAVQKLyDLArGEDGRPFFLTVSFTHPHDPYVIPQeywdlyVRRA- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 264 RgRSLYGAGLWeMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSvgpfTGFWQtrqggspaKQTTWEGGHR 342
Cdd:cd16032 163 R-RAYYGMVSY-VDDKVGQLLDTLERTgLADDTIVIFTSDHG------DMLGE----RGLWY--------KMSFFEGSAR 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 343 VPALAYWPGR-VPVNVTstALLSVLDIFPTVVALAQASLPQGR-RFDGVDVSEVLFGRSQPGHReeEAGGGKEAEGAQSP 420
Cdd:cd16032 223 VPLIISAPGRfAPRRVA--EPVSLVDLLPTLVDLAGGGTAPHVpPLDGRSLLPLLEGGDSGGED--EVISEYLAEGAVAP 298
|
..
gi 2462554007 421 LC 422
Cdd:cd16032 299 CV 300
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
34-395 |
1.22e-24 |
|
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: 106.50 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 34 QKPNFVIILADDM----GWgdLGANWAETkdtANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrNFAVT 109
Cdd:cd16030 1 KKPNVLFIAVDDLrpwlGC--YGGHPAKT---PNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVY-DNNSY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 110 SVGGLPlNETTLAEVLQQAGYVTGIIGK-WHlGHHGSYHPNFRGFDYYFGIP--------YSHDMGCTDTPGYNHPPCPA 180
Cdd:cd16030 75 FRKVAP-DAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPPgpekyppgKLCPGKKGGKGGGGGPAWEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 181 CPQGDGPsrnlqrdcYTDvalplyenlniveqpvnlsslaQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQ-- 258
Cdd:cd16030 153 ADVPDEA--------YPD----------------------GKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKky 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 259 ------------------------------LPAAPRGRSLYG--------AGLWE------------MDSLVGQIKDKVD 288
Cdd:cd16030 203 fdlyplesiplpnpfdpidlpevawndlddLPKYGDIPALNPgdpkgplpDEQARelrqayyasvsyVDAQVGRVLDALE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 289 -HTVKENTFLWFTGDNGpWA--QKcelagsvgpftGFWqtrqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSV 365
Cdd:cd16030 283 eLGLADNTIVVLWSDHG-WHlgEH-----------GHW--------GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVEL 342
|
410 420 430
....*....|....*....|....*....|
gi 2462554007 366 LDIFPTVVALAQasLPQGRRFDGVDVSEVL 395
Cdd:cd16030 343 VDIYPTLAELAG--LPAPPCLEGKSLVPLL 370
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-393 |
1.57e-24 |
|
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: 103.61 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 35 KPNFVIILADDMGWGDLGA-NWAETKD---------TANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTR 104
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCyNNAHTGKsesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 105 NFAVTSVGGLPLneTTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqg 184
Cdd:cd16153 81 FEAAHPALDHGL--PTFPEVLKKAGYQTASFGKSHLE------------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 185 dgpsrNLQRdcYTDVALPLYENLNIVEqpvnlsslaqkyaekatqfIQRASTSGrPFLLYVALAHMHVP-LPvtqlPAAP 263
Cdd:cd16153 116 -----AFQR--YLKNANQSYKSFWGKI-------------------AKGADSDK-PFFVRLSFLQPHTPvLP----PKEF 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 264 RGRSLYGAGLWEMDSLVGQIKDKVD----HTVKENTFLWFTGDNGpwaqkcelagsvgpftgfWQTRQGGSPAKQTTWEG 339
Cdd:cd16153 165 RDRFDYYAFCAYGDAQVGRAVEAFKayslKQDRDYTIVYVTGDHG------------------WHLGEQGILAKFTFWPQ 226
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462554007 340 GHRVPALAYWPGR--VPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSE 393
Cdd:cd16153 227 SHRVPLIVVSSDKlkAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
36-376 |
1.18e-23 |
|
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: 99.80 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCS-PSRASLLTGRLGLRNGVTRNFAVT----- 109
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSaPNHAALLTGAYPTLHGYTGNGSADpelps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 110 SVGGLPLNETTLAEVLQQAGYVTGIIGKWhlghhgsyhpnfrgfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsr 189
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIGLL--------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 190 nlqrdcytdvalplyenlniveqpvnlsslaqkyaekatQFIQRaSTSGRPFLLYVALAHMHVPL--PVTQLPaaprgrs 267
Cdd:cd00016 110 ---------------------------------------KAIDE-TSKEKPFVLFLHFDGPDGPGhaYGPNTP------- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 268 LYGAGLWEMDSLVGQIKDKV-DHTVKENTFLWFTGDNGpwaqkcelAGSVGPftgfwqTRQGGSPAKQTTWEGGHRVPAL 346
Cdd:cd00016 143 EYYDAVEEIDERIGKVLDALkKAGDADDTVIIVTADHG--------GIDKGH------GGDPKADGKADKSHTGMRVPFI 208
|
330 340 350
....*....|....*....|....*....|
gi 2462554007 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 |
1.05e-20 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 93.83 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNfavtsVGGL 114
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPL 75
|
90 100
....*....|....*....|....*.
gi 2462554007 115 PLNETTLAEVLQQAGYVTGIIGKWHL 140
Cdd:cd16152 76 PADEKTLAHYFRDAGYETGYVGKWHL 101
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
36-405 |
6.33e-18 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293775 [Multi-domain] Cd Length: 468 Bit Score: 86.67 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGvtrnfAVTSVGGLP 115
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNG-----SWTNCMALG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 116 LNETTLAEVLQQAGYVTGIIGKWHLGhhgsyhpnfrGFDYY-FGIpyshdmgctdtpgynhppcpaCPQGDGPSRNLQRD 194
Cdd:cd16156 76 DNVKTIGQRLSDNGIHTAYIGKWHLD----------GGDYFgNGI---------------------CPQGWDPDYWYDMR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 195 CYTD-----------VALPLYENLNIVEQpvnlSSLAQKYAEKATQFIQraSTSGRPFLLYVALAHMHVPL--------- 254
Cdd:cd16156 125 NYLDelteeerrksrRGLTSLEAEGIKEE----FTYGHRCTNRALDFIE--KHKDEDFFLVVSYDEPHHPFlcpkpyasm 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 255 --------------------PVTQLPAAPRGRSLYGAGLWEM----------DSLVGQIKDKVDHTVkENTFLWFTGDNG 304
Cdd:cd16156 199 ykdfefpkgenayddlenkpLHQRLWAGAKPHEDGDKGTIKHplyfgcnsfvDYEIGRVLDAADEIA-EDAWVIYTSDHG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 305 pwaqkcELAGSvgpftgfwQTRQGGSPAkqtTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQasLPQGR 384
Cdd:cd16156 278 ------DMLGA--------HKLWAKGPA---VYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPK 338
|
410 420
....*....|....*....|.
gi 2462554007 385 RFDGVDVSEVLFGRSQPGHRE 405
Cdd:cd16156 339 VLEGESILATIEDPEIPENRG 359
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-399 |
1.95e-14 |
|
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: 75.35 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGR----LGLRngvtrnfavTSV 111
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWyphvNGHR---------TLH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 112 GGLPLNETTLAEVLQQAGYVTGIIGKWHLghhgsyhpnfrgfdyyfgIPYSHDMGCTDTPGYnhppcpacpqgdgpsrnl 191
Cdd:cd16150 72 HLLRPDEPNLLKTLKDAGYHVAWAGKNDD------------------LPGEFAAEAYCDSDE------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 192 qrdcytdvalplyenlniveqpvnlsslaqKYAEKATQFIQRASTsGRPFLLYVALAHMHVP---------------LPV 256
Cdd:cd16150 116 ------------------------------ACVRTAIDWLRNRRP-DKPFCLYLPLIFPHPPygveepwfsmidrekLPP 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 257 T--------QLPAAPRGRSLYGAGLW-----------------EMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAqkc 310
Cdd:cd16150 165 RrppglrakGKPSMLEGIEKQGLDRWseerwrelratylgmvsRLDHQFGRLLEALKETgLYDDTAVFFFSDHGDYT--- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 311 elagsvGPFtGFWQTRQGGSPAKQTtwegghRVPALAYWPGRVPVNVTStALLSVLDIFPTVVALAqaslpqgrrfdGVD 390
Cdd:cd16150 242 ------GDY-GLVEKWPNTFEDCLT------RVPLIIKPPGGPAGGVSD-ALVELVDIPPTLLDLA-----------GIP 296
|
....*....
gi 2462554007 391 VSEVLFGRS 399
Cdd:cd16150 297 LSHTHFGRS 305
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
36-157 |
5.58e-14 |
|
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: 74.22 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvgGLP 115
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT-----PLD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462554007 116 LNETTLAEVLQQAGYVTGIIGKWHL-----GHH------GSYHPNFRGFDYYF 157
Cdd:cd16028 76 ARHLTLALELRKAGYDPALFGYTDTspdprGLApldprlLSYELAMPGFDPVD 128
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
36-383 |
1.63e-13 |
|
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: 72.19 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGrlgLRNGVTRNFavTSVGGLP 115
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG---LFTHLTESW--NNYKGLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 116 LNETTLAEVLQQAGYVTGIIGK--WHLGHHGSYHpnfRGFDYYFGIPYShdmgctdtpgynhppcpaCPQGDGPSRNLQR 193
Cdd:cd16171 76 PNYPTWMDRLEKHGYHTQKYGKldYTSGHHSVSN---RVEAWTRDVPFL------------------LRQEGRPTVNLVG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 194 DCYTDvalplyenlniveqpvNLSSLAQKYAEKATQFIQRASTS-GRPFLLYVALAHMHvPLPVTQLPAAPRG----RSL 268
Cdd:cd16171 135 DRSTV----------------RVMLKDWQNTDKAVHWIRKEAPNlTQPFALYLGLNLPH-PYPSPSMGENFGSirniRAF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 269 YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAgsvgpftgfWQTRQGgspAKQTTWEGGHRVPALA 347
Cdd:cd16171 198 YYAMCAETDAMLGEIISALKDTgLLDKTYVFFTSDHG------ELA---------MEHRQF---YKMSMYEGSSHVPLLI 259
|
330 340 350
....*....|....*....|....*....|....*.
gi 2462554007 348 YWPGrVPVNVTSTALLSVLDIFPTVVALAQASLPQG 383
Cdd:cd16171 260 MGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN 294
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
28-161 |
1.10e-05 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 48.11 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 28 SGKTRGQKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVtrnfA 107
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGS----P 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 108 VTSVGGLPLNetTLAEVLQQAGYVTGIIgkwHlGHHGS------YHPNFrGFDYYFGIPY 161
Cdd:COG1368 303 YKRPGQNNFP--SLPSILKKQGYETSFF---H-GGDGSfwnrdsFYKNL-GFDEFYDRED 355
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
14-162 |
1.02e-03 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 41.66 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 14 SFSGFLYPLVDFCISGKTRGQKPnFVIILADDMGWGDLGANwaetkDTANLDKMASEGMRFVDFHAA--ASTCsPSRASL 91
Cdd:COG1524 3 RGLSLLLASLLAAAAAAAPPAKK-VVLILVDGLRADLLERA-----HAPNLAALAARGVYARPLTSVfpSTTA-PAHTTL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 92 LTGRLGLRNGVTRNF--------AVTSVGGLP--------LNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPN----FR 151
Cdd:COG1524 76 LTGLYPGEHGIVGNGwydpelgrVVNSLSWVEdgfgsnslLPVPTIFERARAAGLTTAAVFWPSFEGSGLIDAArpypYD 155
|
170
....*....|.
gi 2462554007 152 GFDYYFGIPYS 162
Cdd:COG1524 156 GRKPLLGNPAA 166
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
20-371 |
2.33e-03 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 40.66 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 20 YPLVDfcISGKTRGQKPNFVIILADDMGWGDLGAnwaetKDTANLDKMASEGMRFVDfHAAASTCSPsrasllTGRLGLR 99
Cdd:COG3083 231 YPLHP--LQFSDPAKPPNILLIVVDSLRADMLDP-----EVMPNLYAFAQRSLRFTN-HYSSGNSTR------AGLFGLF 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 100 NGVTRNFAvTSVgglpLNETT---LAEVLQQAGYVTGIigkwhlghhgsyhpnfrgfdyyfgipYSHDmgctdtpGYNHP 176
Cdd:COG3083 297 YGLPGNYW-DSI----LAERTppvLIDALQQQGYQFGL--------------------------FSSA-------GFNSP 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 177 PcpacpqgdgpsrnLQRDCYTDVALPLYENLNIVEQPvnlsslAQKYAEKATQFIQRAStSGRPFLLYVALAHMH----- 251
Cdd:COG3083 339 L-------------FRQTIFSDVSLPRLHTPGGPAQR------DRQITAQWLQWLDQRD-SDRPWFSYLFLDAPHaysfp 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554007 252 -------------VPLPVTQLPAAPRGRSLYGAGLWEMDSLVGQIKDKVDHTVK-ENTFLWFTGDNGPwaqkcelagsvg 317
Cdd:COG3083 399 adypkpfqpsedcNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLlENTIVIITADHGE------------ 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462554007 318 PF----TGFWQTRQGGSPAkQTtwegghRVPALAYWPGRVPVNVTStaLLSVLDIFPT 371
Cdd:COG3083 467 EFnengQNYWGHNSNFSRY-QL------QVPLVIHWPGTPPQVISK--LTSHLDIVPT 515
|
|
| |
