|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
46-570 |
0e+00 |
|
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: 771.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIQNL 125
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 126 AVPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQCHHPYNYGFDYYYGMPFTLVDSCWPDPSRNTELAFESQ 205
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 206 LWLCVQLVAIAILTLTFGKLSGWVSvpWLLIFSMILFIFLLGYAWFSSHTSPLYWDCLLMRGHEITEQPMKAERAGSIMV 285
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLYLGAVS--KRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 286 KEAISFLERHSKETFLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGG 365
Cdd:cd16159 239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 366 HLEARRGHAQLGGWNGIYKGGKGMGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRD 445
Cdd:cd16159 319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 446 LMPLLQGNVRHSEHEFLFHYCGSYLHAVRWIPKdDSGSVWKAHYVTPVFQpPASGGCYVTSLCRCFGEQVTYHNPPLLFD 525
Cdd:cd16159 399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPR-DGGAVWKAHYFTPNFY-PGTEGCCGTLLCRCFGDSVTHHDPPLLFD 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 768032434 526 LSRDPSESTPLTPATEPlHDFVIKKVANALKEHQETIVPVTYQLS 570
Cdd:cd16159 477 LSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
46-537 |
2.94e-150 |
|
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: 438.92 E-value: 2.94e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIQNl 125
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 126 avpaGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsrsDQ-CHHPYNYGFDYYYGMPFTlvDSCWPDPSRNTElafes 204
Cdd:cd16026 80 ----GLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYS--NDMWPFPLYRND----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 205 qlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsPLYWDCLLMRGHEITEQPMKAERAGSIM 284
Cdd:cd16026 142 ----------------------------------------------------PPGPLPPLMENEEVIEQPADQSSLTQRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 285 VKEAISFLERHSKETFLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHG 364
Cdd:cd16026 170 TDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 365 GHLE--ARRGHAQL----------GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSG 432
Cdd:cd16026 250 PWLEygGHGGSAGPlrggkgttweGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 433 GSLPQDRVIDGRDLMPLLQGNVRHSEHEFLFHYCGSYLHAVRWIPkddsgsvWKAHYVTPVFQPPASGGCYVTSlcrcfg 512
Cdd:cd16026 313 APLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR-------WKLHLPTTYRTGTDPGGLDPTK------ 379
|
490 500
....*....|....*....|....*
gi 768032434 513 eqvtyHNPPLLFDLSRDPSESTPLT 537
Cdd:cd16026 380 -----LEPPLLYDLEEDPGETYNVA 399
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
46-557 |
1.40e-125 |
|
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: 377.54 E-value: 1.40e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSsGNRRVIQNL 125
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG-GTRVFLPWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 126 AVpaGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQCHHPYNYGFDYY-YGMPFTLVdscwpdpsrntelafes 204
Cdd:cd16160 80 IG--GLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFDFVgTNLPFTNS----------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 205 qlWLCVqlvaiailtltfgklsgwvsvPWllifsmilfifllGYAWFSSHTSPlywdCLLMRGHEITEQPMKAERAGSIM 284
Cdd:cd16160 141 --WACD---------------------DT-------------GRHVDFPDRSA----CFLYYNDTIVEQPIQHEHLTETL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 285 VKEAISFLERHSKETFLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHG 364
Cdd:cd16160 181 VGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 365 GHLEA----------RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPaGRLIKEPTSLMDILPTVASVSG 432
Cdd:cd16160 261 PHVEYcleggstgglKGGKGNSweGG-----------------IRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTFVDLAG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 433 GSLPQDRVIDGRDLMPLLQGNVRHSEHEFLFHYCgSYLHAVRwipkddSGSvWKAHYVTPVFQ------PPASGGCYVTS 506
Cdd:cd16160 323 GTLPTDRIYDGLSITDLLLGEADSPHDDILYYCC-SRLMAVR------YGS-YKIHFKTQPLPsqesldPNCDGGGPLSD 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 768032434 507 --LCR-CFGEQVTYHNPPLLFDLSRDPSESTPLTPAtepLHDFVIKKVANALKE 557
Cdd:cd16160 395 yiVCYdCEDECVTKHNPPLIFDVEKDPGEQYPLQPS---VYEHMLEAVEKLIAH 445
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
46-537 |
2.45e-97 |
|
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: 302.47 E-value: 2.45e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 46 KPNIVLIMVDDLGIGDLGCYGNDTMR-TPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIqn 124
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 125 lavpAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNcdsrsdQCHHPYNYGFDYYYGMPFtlvdscwpdpSRNTELAFEs 204
Cdd:cd16161 79 ----GGLPLNETTLAEVLRQAGYATGMIGKWHLGQR------EAYLPNSRGFDYYFGIPF----------SHDSSLADR- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 205 qlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgYAWFsshtsplywdcllmrgheiteqpmkaeragsim 284
Cdd:cd16161 138 -------------------------------------------YAQF--------------------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 285 vkeAISFLERHSKET--FLLFFSFLHVHTPLPTTDDF-TGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTS 361
Cdd:cd16161 142 ---ATDFIQRASAKDrpFFLYAALAHVHVPLANLPRFqSPTSGRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTS 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 362 DHGGHLEARRGHAQLGGWNGIYKGGKGMGGWEG---GIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQD 438
Cdd:cd16161 219 DNGPWEVKCELAVGPGTGDWQGNLGGSVAKASTwegGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 439 RVIDGRDLMPLLQGNVRhSEHEFLFHYCGSY-----LHAVRWIPkddsgsvWKAHYVTpvfqppasGGCYVTslCRCFGE 513
Cdd:cd16161 299 RIYDGKDLSPVLFGGSK-TGHRCLFHPNSGAagagaLSAVRCGD-------YKAHYAT--------GGALAC--CGSTGP 360
|
490 500
....*....|....*....|....
gi 768032434 514 QVtYHNPPLLFDLSRDPSESTPLT 537
Cdd:cd16161 361 KL-YHDPPLLFDLEVDPAESFPLT 383
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
47-534 |
1.33e-96 |
|
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: 301.77 E-value: 1.33e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGM--VSSGNRRVIQN 124
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 125 LAVPA-----GLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDsrsdqcHHPYNYGFDYYYGmpftlvDSCWPDPSRnte 199
Cdd:cd16144 81 TKLIPppsttRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGG------YGPEDQGFDVNIG------GTGNGGPPS--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 200 lafesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllGYAWFSSHTSPLYwdcllmrghEITEQPMKAER 279
Cdd:cd16144 146 -----------------------------------------------YYFPPGKPNPDLE---------DGPEGEYLTDR 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 280 agsiMVKEAISFLERHSKETFLLFFSFLHVHTPLPTTDDF----------TGTSKHG-LYGDNVEEMDSMVGKILDAIDD 348
Cdd:cd16144 170 ----LTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELiekyekkkkgLRKGQKNpVYAAMIESLDESVGRILDALEE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 349 FGLRNNTLVYFTSDHGGHLEA----------RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKE 416
Cdd:cd16144 246 LGLADNTLVIFTSDNGGLSTRggpptsnaplRGGKGSLyeGG-----------------IRVPLIVRWPGVIKPGSVSDV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 417 PTSLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNVRHSEHEFLF----HYCGSYLHAVRWIPKDDsgsvWKAHYvtp 492
Cdd:cd16144 309 PVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFwhfpHYHGQGGRPASAIRKGD----WKLIE--- 381
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 768032434 493 vfqppasggcyvtslcrcFGEQVTYHnpplLFDLSRDPSEST 534
Cdd:cd16144 382 ------------------FYEDGRVE----LYNLKNDIGETN 401
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
18-536 |
2.72e-96 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 299.87 E-value: 2.72e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 18 MRpRRPLVFMSLVCALLNTCQAhrvhdDKPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSP 97
Cdd:COG3119 1 MK-RLLLLLLALLAAAAAAAAA-----KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 98 SRSAFLTGRYPIRSGMVSSGNRRviqnlavPAGLPLNETTLAALLKKQGYSTGLIGKWHqglncdsrsdqchhpynygfd 177
Cdd:COG3119 75 SRASLLTGRYPHRTGVTDNGEGY-------NGGLPPDEPTLAELLKEAGYRTALFGKWH--------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 178 yyygmpftlvdscwpdpsrntelafesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsp 257
Cdd:COG3119 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 258 LYWDcllmrgHEITEqpmkaeragsimvkEAISFLERHSKET--FLLFFSFLHVHTPLPTTDDF---------------- 319
Cdd:COG3119 127 LYLT------DLLTD--------------KAIDFLERQADKDkpFFLYLAFNAPHAPYQAPEEYldkydgkdiplppnla 186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 320 -------TGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGHLEA---RRGHAQL--GGwngiykggk 387
Cdd:COG3119 187 prdlteeELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEhglRGGKGTLyeGG--------- 257
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 388 gmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNVRHSEHEFLFHYCG 467
Cdd:COG3119 258 --------IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPR 327
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 468 SY-LHAVRwipKDDsgsvWKahYVTPVFQPPasggcyvtslcrcfgeqvtyhnPPLLFDLSRDPSESTPL 536
Cdd:COG3119 328 GGgNRAIR---TGR----WK--LIRYYDDDG----------------------PWELYDLKNDPGETNNL 366
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
47-537 |
1.37e-95 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 297.52 E-value: 1.37e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDT---MRTPHIDRLAREGVRLTQHISAASlCSPSRSAFLTGRYPIRSGMVSSGnrrvIQ 123
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIgrgAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVG----LP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 124 NLavPAGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsRSDQcHHPYNYGFDYYYGMPFTLVDScwpdpsrntelafe 203
Cdd:cd16142 76 GS--PGGLPPWEPTLAELLKDAGYATAQFGKWHLG-----DEDG-RLPTDHGFDEFYGNLYHTIDE-------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 204 sqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplywdcllmrghEITEQpmkaeragsi 283
Cdd:cd16142 134 -----------------------------------------------------------------EIVDK---------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 284 mvkeAISFLERHSKET--FLLFFSFLHVHTPLPTTDDFTGTSK-HGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFT 360
Cdd:cd16142 139 ----AIDFIKRNAKADkpFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFT 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 361 SDHGGHLEA--------RRGH---AQLGGWngiykggkgmggweggiRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVAS 429
Cdd:cd16142 215 TDNGPEQDVwpdggytpFRGEkgtTWEGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAA 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 430 VSGGSLP------QDRVIDGRDLMPLLQGNVRHSEHEFLFHYCGSYLHAVRWipKDdsgsvWKAHY-VTPVFQPPASGGC 502
Cdd:cd16142 278 LAGAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRW--KN-----WKVHFkAQEDTGGPTGEPF 350
|
490 500 510
....*....|....*....|....*....|....*
gi 768032434 503 YVTSLcrcfgeqvtyhnpPLLFDLSRDPSESTPLT 537
Cdd:cd16142 351 YVLTF-------------PLIFNLRRDPKERYDVT 372
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
47-534 |
1.00e-94 |
|
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: 296.03 E-value: 1.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDT-MRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGM---VSSGNRrvi 122
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSkIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLkggVLGGFS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 123 qnlavPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQCHH----------------PYNYGFDYYYGMPftl 186
Cdd:cd16143 78 -----PPLIEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIP--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 187 vdscwpdpsrntelafesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplywdcllmr 266
Cdd:cd16143 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 267 gheiteqpmkAERAGSIMVKEAISFLERHSKET--FLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILD 344
Cdd:cd16143 150 ----------ASEVLPTLTDKAVEFIDQHAKKDkpFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILD 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 345 AIDDFGLRNNTLVYFTSDHGGHLEARRGHAQL------------------GGwngiykggkgmggweggIRVPGIVRWPG 406
Cdd:cd16143 220 ALKELGLAENTLVIFTSDNGPSPYADYKELEKfghdpsgplrgmkadiyeGG-----------------HRVPFIVRWPG 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 407 KVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNVRHSEHEFLFHYCGSYLHAVR---W--IPKDDS 481
Cdd:cd16143 283 KIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGSFAIRkgdWklIDGTGS 362
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 768032434 482 GSvWKAHYVTPVFQPPasggcyvtslcrcfgeqvtyhnPPLLFDLSRDPSEST 534
Cdd:cd16143 363 GG-FSYPRGKEKLGLP----------------------PGQLYNLSTDPGESN 392
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
46-591 |
1.06e-92 |
|
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: 293.58 E-value: 1.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMV-------SSGn 118
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYpgvfypgSRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 119 rrviqnlavpaGLPLNETTLAALLKKQGYSTGLIGKWHQGLNcdsrSDQCHHPYNYGFDYYYGMPFTLvDSCwpdPsrnt 198
Cdd:cd16158 80 -----------GLPLNETTIAEVLKTVGYQTAMVGKWHLGVG----LNGTYLPTHQGFDHYLGIPYSH-DQG---P---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 199 elafesqlwlCVQLVAIAILTLTFGKLSGWVSvpwllifsmilfifllgyawfsshTSPLYWDcllmrgHEITEQPMKAE 278
Cdd:cd16158 137 ----------CQNLTCFPPNIPCFGGCDQGEV------------------------PCPLFYN------ESIVQQPVDLL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 279 RAGSIMVKEAISFLERHSKET--FLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTL 356
Cdd:cd16158 177 TLEERYAKFAKDFIADNAKEGkpFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 357 VYFTSDHGGHL--EARRGHAQL----------GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIkEPTSLMDIL 424
Cdd:cd16158 257 VFFTSDNGPSTmrKSRGGNAGLlkcgkgttyeGG-----------------VREPAIAYWPGRIKPGVTH-ELASTLDIL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 425 PTVASVSGGSLPqDRVIDGRDLMPLLQGNVRHSEHEFLFHYCGSY----LHAVRWipkddsgSVWKAHYVT---PVFQPP 497
Cdd:cd16158 319 PTIAKLAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDpdkgVFAVRW-------GKYKAHFYTqgaAHSGTT 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 498 ASGGCYVTSLcrcfgeqVTYHNPPLLFDLSRDPSESTPLTPATEplHDFVIKKVaNALKEHQETivPVTYQLSELNQGR- 576
Cdd:cd16158 391 PDKDCHPSAE-------LTSHDPPLLFDLSQDPSENYNLLGLPE--YNQVLKQI-QQVKERFEA--SMKFGESEINKGEd 458
|
570 580
....*....|....*....|
gi 768032434 577 TWLKPCC--GVFPF---CLC 591
Cdd:cd16158 459 PALEPCCkpGCTPKpscCQC 478
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
46-569 |
1.02e-85 |
|
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: 275.11 E-value: 1.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSG----NRRV 121
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNaharNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 122 IQNLAvpAGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsrSDQCHHPYNYGFDYYYGMPftlvdSCWPDPSRNTELa 201
Cdd:cd16157 81 PQNIV--GGIPDSEILLPELLKKAGYRNKIVGKWHLG------HRPQYHPLKHGFDEWFGAP-----NCHFGPYDNKAY- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 202 fesqlwlcvqlvaiailtltfgklsgwvsvPWLlifsmilfifllgyawfsshtsPLYWDCLlMRGHEITEQPMKAERAG 281
Cdd:cd16157 147 ------------------------------PNI----------------------PVYRDWE-MIGRYYEEFKIDKKTGE 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 282 S----IMVKEAISFLERH--SKETFLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNT 355
Cdd:cd16157 174 SnltqIYLQEALEFIEKQhdAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 356 LVYFTSDHGGhleARRGHAQLGGWNgIYKGGKGMGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSL 435
Cdd:cd16157 254 FVFFSSDNGA---ALISAPEQGGSN-GPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 436 PQDRVIDGRDLMPLLQGNvrHSEHEFLFHYCGSYLHAVRWipkddsgSVWKAHYVTpvFQPPASGGCYVTSLCRcfGEQ- 514
Cdd:cd16157 330 PSDRAIDGIDLLPVLLNG--KEKDRPIFYYRGDELMAVRL-------GQYKAHFWT--WSNSWEEFRKGINFCP--GQNv 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032434 515 --VTYHN------PPLLFDLSRDPSESTPLTPATePLHDFVIKKVANALKEHQETIVPVTYQL 569
Cdd:cd16157 397 pgVTTHNqtdhtkLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQL 458
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
47-534 |
7.27e-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: 293764 [Multi-domain] Cd Length: 415 Bit Score: 266.00 E-value: 7.27e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYpirsgmvsSGNRRVIQNLA 126
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLH--------TGHTRVRGNSE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 127 VPAGLPL--NETTLAALLKKQGYSTGLIGKWhqGLNCDSRSDqchHPYNYGFDYYYGmpftlvdscwpdpsrntelafes 204
Cdd:cd16145 73 PGGQDPLppDDVTLAEVLKKAGYATAAFGKW--GLGGPGTPG---HPTKQGFDYFYG----------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 205 qlWLCvQLVAiailtLTFgklsgwvsvpwlliFSMILfifllgyaWFSSHTSPLYWDCLLMRGHEITEQPMKAERAGSIM 284
Cdd:cd16145 125 --YLD-QVHA-----HNY--------------YPEYL--------WRNGEKVPLPNNVIPPLDEGNNAGGGGGTYSHDLF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 285 VKEAISFLERHSKETFLLFFSFLHVHTPLPTTDD---FTGTSKHGLYGDN------------VEEMDSMVGKILDAIDDF 349
Cdd:cd16145 175 TDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDDgpyKYKPKDPGIYAYLpwpqpekayaamVTRLDRDVGRILALLKEL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 350 GLRNNTLVYFTSDHGGHLEARRGHAQL-----------------GGwngiykggkgmggweggIRVPGIVRWPGKVPAGR 412
Cdd:cd16145 255 GIDENTLVVFTSDNGPHSEGGSEHDPDffdsngplrgykrslyeGG-----------------IRVPFIARWPGKIPAGS 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 413 LIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNVRHSEHEFLF--HYCGSYLHAVRWipkDDsgsvWKAhyv 490
Cdd:cd16145 318 VSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLYweFYEGGGAQAVRM---GG----WKA--- 385
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 768032434 491 tpVFQPPASGgcyvtslcrcfgeqvtyhnPPLLFDLSRDPSEST 534
Cdd:cd16145 386 --VRHGKKDG-------------------PFELYDLSTDPGETN 408
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
47-445 |
3.71e-80 |
|
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: 252.36 E-value: 3.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSsgnrrviqNLA 126
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRG--------NVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 127 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQglncdsrsdqchhpynygfdyyygmpftlvdscwpdpsrntelafesql 206
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWHD------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 207 wlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplywdcllmrgheiteqpmkaeragsimvk 286
Cdd:cd16022 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 287 EAISFLERHSKET-FLLFFSFLHVHTPLpttddftgtskhgLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGG 365
Cdd:cd16022 104 EAIDFIERRDKDKpFFLYVSFNAPHPPF-------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 366 HLEA---RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrv 440
Cdd:cd16022 171 MLGDhglRGKKGSLyeGG-----------------IRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG-- 231
|
....*
gi 768032434 441 IDGRD 445
Cdd:cd16022 232 LDGRS 236
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
47-534 |
6.07e-71 |
|
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: 234.37 E-value: 6.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQ-HISaaSLCSPSRSAFLTGRYPIRSGMVSSGNRRVIqnl 125
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 126 avpagLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDsrsdqcHHPYNYGFDYYYGmpftlvdscwpdpsrntelafesq 205
Cdd:cd16146 76 -----MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYP------YRPQDRGFDEVLG------------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 206 lwlcvqlvaiailtltFGklSGWVSVPWllifsmilfifllgYAWFSSHTSPLYWdcllmrgHEITEQPMKaeraG---S 282
Cdd:cd16146 121 ----------------HG--GGGIGQYP--------------DYWGNDYFDDTYY-------HNGKFVKTE----GyctD 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 283 IMVKEAISFLERHSKETFLLFFSFLHVHTPLPTTDDF------TGTSKH--GLYGdNVEEMDSMVGKILDAIDDFGLRNN 354
Cdd:cd16146 158 VFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYldpykdMGLDDKlaAFYG-MIENIDDNVGRLLAKLKELGLEEN 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 355 TLVYFTSDHG----------GHLEARRGHAQLGGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDIL 424
Cdd:cd16146 237 TIVIFMSDNGpaggvpkrfnAGMRGKKGSVYEGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDLL 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 425 PTVASVSGGSLPQDRVIDGRDLMPLLQGNVRHSEHEFLFhycgsyLHAVRWIPKDDS---GSVWKAHY--VTPvfqppas 499
Cdd:cd16146 300 PTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLF------THSGRWPPPPKKkrnAAVRTGRWrlVSP------- 366
|
490 500 510
....*....|....*....|....*....|....*
gi 768032434 500 ggcyvtslcrcfgeqvtYHNPPLLFDLSRDPSEST 534
Cdd:cd16146 367 -----------------KGFQPELYDIENDPGEEN 384
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-536 |
2.76e-68 |
|
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: 226.33 E-value: 2.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTqHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrviqnlA 126
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNY-------------V 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 127 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSdqchHPYNYGFDYYYgmpftlvdscwpdpsrntelafesqL 206
Cdd:cd16151 67 VFGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGD----YPHEFGFDEYC-------------------------L 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 207 WlcvQLVaiailtltfgklsgwvsvpwllifsmilfifllGYAWFSSHTSPLYWDCLLMRGHEITEQpmkaERAGSIMVK 286
Cdd:cd16151 118 W---QLT---------------------------------ETGEKYSRPATPTFNIRNGKLLETTEG----DYGPDLFAD 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 287 EAISFLERHSKETFLLFFSFLHVHTPLPTT------DDFTGTSKH--GLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVY 358
Cdd:cd16151 158 FLIDFIERNKDQPFFAYYPMVLVHDPFVPTpdspdwDPDDKRKKDdpEYFPDMVAYMDKLVGKLVDKLEELGLRENTIII 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 359 FTSDHGGHLEARR-----------GHAQLGGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTV 427
Cdd:cd16151 238 FTGDNGTHRPITSrtngrevrggkGKTTDAG-----------------THVPLIVNWPGLIPAGGVSDDLVDFSDFLPTL 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 428 ASVSGGSLPQDRVIDGRDLMPLLQGNVRHSEHEFLFHYcgsylhAVRWIPKDDSGSVWKAHYvtpvfqppasggcyvtsl 507
Cdd:cd16151 301 AELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWY------YRNPHKKFGSRFVRTKRY------------------ 356
|
490 500
....*....|....*....|....*....
gi 768032434 508 crcfgeqvTYHNPPLLFDLSRDPSESTPL 536
Cdd:cd16151 357 --------KLYADGRFFDLREDPLEKNPL 377
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
47-536 |
7.41e-67 |
|
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: 223.20 E-value: 7.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASlCSPSRSAFLTGRYPIRSGMvssgNRRVIQNlA 126
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGM----QHGVILA-G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 127 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsrsdQCHHPY---NYGFDYYYGmpftlvdscwpdpsrntelafe 203
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWEYtptNRGFDSFYG---------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 204 sqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfiFLLGYAWFSSHTSPLYWDC--LLMRGHEITEQPMKAERAG 281
Cdd:cd16029 125 ----------------------------------------YYGGAEDYYTHTSGGANDYgnDDLRDNEEPAWDYNGTYST 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 282 SIMVKEAISFLERHSKET-FLLFFSFLHVHTPLPT----TDDFTGTSKHGLYGD------NVEEMDSMVGKILDAIDDFG 350
Cdd:cd16029 165 DLFTDRAVDIIENHDPSKpLFLYLAFQAVHAPLQVppeyADPYEDKFAHIKDEDrrtyaaMVSALDESVGNVVDALKAKG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 351 LRNNTLVYFTSDHGGHLEA---------RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPG-KVPAGRLIKEPT 418
Cdd:cd16029 245 MLDNTLIVFTSDNGGPTGGgdggsnyplRGGKNTLweGG-----------------VRVPAFVWSPLlPPKRGTVSDGLM 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 419 SLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNVRHSEHEFL----FHYCGSYLHAVRWipKDdsgsvWKahYVTpvf 494
Cdd:cd16029 308 HVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILlnidDITRTTGGAAIRV--GD-----WK--LIV--- 375
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 768032434 495 qppasggcyvtslcrcfGEQvtyhnpplLFDLSRDPSESTPL 536
Cdd:cd16029 376 -----------------GKP--------LFNIENDPCERNDL 392
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-536 |
1.63e-64 |
|
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: 217.05 E-value: 1.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRrviqnl 125
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 126 avpagLPLNETTLAALLKKQGYSTGLIGKWH----QGLNCDSRSDQCHHPYNYGFDYYYGMpftlvdSCWPDpsrntela 201
Cdd:cd16034 75 -----LPPDAPTIADVLKDAGYRTGYIGKWHldgpERNDGRADDYTPPPERRHGFDYWKGY------ECNHD-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 202 fesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfssHTSPLYWDcllmrgheiTEQPMKAERAG 281
Cdd:cd16034 136 ----------------------------------------------------HNNPHYYD---------DDGKRIYIKGY 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 282 S--IMVKEAISFLERHSKET--FLLFFSFLHVHTP------------------LPTTDDFTGTSKHGL-------YGdNV 332
Cdd:cd16034 155 SpdAETDLAIEYLENQADKDkpFALVLSWNPPHDPyttapeeyldmydpkkllLRPNVPEDKKEEAGLredlrgyYA-MI 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 333 EEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGHLEArrgHAQLG---GWNgiykggkgmggweGGIRVPGIVRWPGKVP 409
Cdd:cd16034 234 TALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGS---HGLMNkqvPYE-------------ESIRVPFIIRYPGKIK 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 410 AGRLIKEPTSLMDILPTVASVSGgsLPQDRVIDGRDLMPLLQGNVRHSEHEFLFhYCGSYLHAVRWIPKDDSGSVWKAHY 489
Cdd:cd16034 298 AGRVVDLLINTVDIMPTLLGLCG--LPIPDTVEGRDLSPLLLGGKDDEPDSVLL-QCFVPFGGGSARDGGEWRGVRTDRY 374
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 768032434 490 vtpvfqppasggcyvtSLCRCFGeqvtyhNPPLLFDLSRDPSESTPL 536
Cdd:cd16034 375 ----------------TYVRDKN------GPWLLFDNEKDPYQLNNL 399
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
47-560 |
1.69e-63 |
|
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: 213.52 E-value: 1.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIgDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMvsSGNRRVIQNLa 126
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA--HGLRSRGFPL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 127 vPAGLPlnetTLAALLKKQGYSTGLIGKWHQGlncdsrsdqchHPYNYGFDYYYGMPFTLVDSCWPDPSrntelAFESQL 206
Cdd:cd16027 77 -PDGVK----TLPELLREAGYYTGLIGKTHYN-----------PDAVFPFDDEMRGPDDGGRNAWDYAS-----NAADFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 207 WLCVQlvaiailtltfGKlsgwvsvPWllifsmilfifllgYAWFSSHTSplywdcllmrgHEITEQPMKAEragsimvk 286
Cdd:cd16027 136 NRAKK-----------GQ-------PF--------------FLWFGFHDP-----------HRPYPPGDGEE-------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 287 eaisflERHSKETFLLfFSFLhVHTPlPTTDDFTGtskhglYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGH 366
Cdd:cd16027 165 ------PGYDPEKVKV-PPYL-PDTP-EVREDLAD------YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMP 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 367 LEarRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGR 444
Cdd:cd16027 230 FP--RAKGTLydSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGR 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 445 DLMPLLQGNVRHsEHEFLF---HYCGSYLHAVRWIPKDDsgsvWKahYVtpvfqppasggcyvtslcRCFgeqvtyhNPP 521
Cdd:cd16027 289 SFLPLLKGEKDP-GRDYVFaerDRHDETYDPIRSVRTGR----YK--YI------------------RNY-------MPE 336
|
490 500 510
....*....|....*....|....*....|....*....
gi 768032434 522 LLFDLSRDPSESTPLtpATEPLHDFVIKKVANALKEHQE 560
Cdd:cd16027 337 ELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
47-432 |
2.59e-59 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 199.96 E-value: 2.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSgnrrviqnla 126
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 127 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNcdSRSDqchhPYNYGFDYYYGmpftlvdscwpdpsrntelafesql 206
Cdd:pfam00884 71 TPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWY--NNQS----PCNLGFDKFFG------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 207 wlcvqlvaiailtltfgklsgwvsvpwllifsmilfiFLLGYAWFSSHTSPLYWdcllMRGHEITEQpmkaeragsIMVK 286
Cdd:pfam00884 120 -------------------------------------RNTGSDLYADPPDVPYN----CSGGGVSDE---------ALLD 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 287 EAISFLERHSKEtFLLFFSFLHVHTPLPTTDDFTGTSK------------HGLYGDNVEEMDSMVGKILDAIDDFGLRNN 354
Cdd:pfam00884 150 EALEFLDNNDKP-FFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLLDN 228
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032434 355 TLVYFTSDHGGHLEARRGHAQLGGWNgiykggkgmGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSG 432
Cdd:pfam00884 229 TLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
45-557 |
1.66e-54 |
|
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: 191.20 E-value: 1.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 45 DKPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGnrrviqn 124
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNN------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 125 lavPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDqchhpynyGFDYYYGmpftlvdscwpdpsrntelaFES 204
Cdd:cd16031 74 ---GPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--------GFDYWVS--------------------FPG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 205 QlwlcvqlvaIAILTLTFGKLSGWVSVPWllifsmilfifllgyawfssHTSplywdcllmrgHEITEQpmkaeragsim 284
Cdd:cd16031 123 Q---------GSYYDPEFIENGKRVGQKG--------------------YVT-----------DIITDK----------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 285 vkeAISFLERHSKET-FLLFFSFLHVHT-----------------PLPTT---DDFTGTSK------------------- 324
Cdd:cd16031 152 ---ALDFLKERDKDKpFCLSLSFKAPHRpftpaprhrglyedvtiPEPETfddDDYAGRPEwareqrnrirgvldgrfdt 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 325 HGLYGDNVE-------EMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGHLearrGHAQLGG-WNgiykggkgmgGWEGGI 396
Cdd:cd16031 229 PEKYQRYMKdylrtvtGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL----GEHGLFDkRL----------MYEESI 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 397 RVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNVRHS-EHEFLFHYcgSYLHAVRW 475
Cdd:cd16031 295 RVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEY--YEEPNFHN 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 476 IPK------DDsgsvWK-AHYvtpvfqppasggcyvtslcrcfgeqvtYHNPPL--LFDLSRDPSESTPLtpATEPLHDF 546
Cdd:cd16031 371 VPThegvrtER----YKyIYY---------------------------YGVWDEeeLYDLKKDPLELNNL--ANDPEYAE 417
|
570
....*....|.
gi 768032434 547 VIKKVANALKE 557
Cdd:cd16031 418 VLKELRKRLEE 428
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
457-591 |
5.84e-54 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 179.43 E-value: 5.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 457 SEHEFLFHYCGSYLHAVRWIPkddsgsvWKAHYVTPVFQPPASGGCYVTslcrcfGEQVTYHNPPLLFDLSRDPSESTPL 536
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP-------YKAHFFTPSFDPPGAEGCYGS------KVPVTHHDPPLLFDLERDPSEKYPL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 768032434 537 TPATePLHDFVIKKVANALKEHQETIVPVTYQLSELNQG-RTWLKPCCGVFPFCLC 591
Cdd:pfam14707 68 SPDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLwDPWLQPCCPTFPACTC 122
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
45-536 |
1.76e-49 |
|
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: 176.86 E-value: 1.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 45 DKPNIVLIMVDDLGIGDLGCYGNDtMRTPHIDRLAREGVRLTQ-HisAASLCSPSRSAFLTGRYPIRSGMvssGNrrvIQ 123
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM---GT---MA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 124 NLAVPAG-----LPLNETTLAALLKKQGYSTGLIGKWHQGLNcdsrsdqchhpynygfDYYygmpftlvdscwpdpsrnt 198
Cdd:cd16025 72 ELATGKPgyegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------------DYY------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 199 elafesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfSSHTsplywdcllmrgheiteqpmkae 278
Cdd:cd16025 117 -----------------------------------------------------STDD----------------------- 120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 279 ragsiMVKEAISFLERHSKET--FLLFFSFLHVHTPL----PTTDDFTGTSKHG----------------LYGDN----- 331
Cdd:cd16025 121 -----LTDKAIEYIDEQKAPDkpFFLYLAFGAPHAPLqapkEWIDKYKGKYDAGwdalreerlerqkelgLIPADtkltp 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 332 -----------------------------VEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGhlEARRGHAQ------- 375
Cdd:cd16025 196 rppgvpawdslspeekklearrmevyaamVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGA--SAEPGWANasntpfr 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 376 -------LGGwngiykggkgmggweggIRVPGIVRWP-GKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRV------I 441
Cdd:cd16025 274 lykqashEGG-----------------IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpL 336
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 442 DGRDLMPLLQGNVRHSEHEFL-FHYCGSylHAVRwipKDDsgsvWKAhyvtpvfqppasggcyvtslcrcfgeqVTYHNP 520
Cdd:cd16025 337 DGVSLLPTLDGAAAPSRRRTQyFELFGN--RAIR---KGG----WKA---------------------------VALHPP 380
|
570 580
....*....|....*....|..
gi 768032434 521 PL------LFDLSRDPSESTPL 536
Cdd:cd16025 381 PGwgdqweLYDLAKDPSETHDL 402
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
46-541 |
2.47e-48 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 176.01 E-value: 2.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 46 KPNIVLIMVDDLGiGD-LGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNrrviqn 124
Cdd:PRK13759 6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGD------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 125 lavpaGLPLN-ETTLAALLKKQGYSTGLIGKWHqglncdsrsdqcHHPYN--YGFDYyygmpfTLVDSCWPDPSRN---T 198
Cdd:PRK13759 79 -----VVPWNyKNTLPQEFRDAGYYTQCIGKMH------------VFPQRnlLGFHN------VLLHDGYLHSGRNedkS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 199 ELAFESQ--LWLCVQLVAI-AILTLTFGKLSGWVSVPWLLifsmilfifllgyawfSSHTSPLYWdcllmrgheiteqpm 275
Cdd:PRK13759 136 QFDFVSDylAWLREKAPGKdPDLTDIGWDCNSWVARPWDL----------------EERLHPTNW--------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 276 kaeragsiMVKEAISFLERHSK-ETFLLFFSFLHVHTPL-----------------PTTDDF--------TGTSKHGLYG 329
Cdd:PRK13759 185 --------VGSESIEFLRRRDPtKPFFLKMSFARPHSPYdppkryfdmykdadipdPHIGDWeyaedqdpEGGSIDALRG 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 330 D---------------NVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDH----GGHLEARRGHAQLGgwngiykggkgmg 390
Cdd:PRK13759 257 NlgeeyarraraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHgdmlGDHYLFRKGYPYEG------------- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 391 gwegGIRVPGIVRWPG---KVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGN---VR---HSEHEf 461
Cdd:PRK13759 324 ----SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQyegWRpylHGEHA- 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 462 lfhYCGSYLHavrWIPKDDSGSVWKAHYVTpvfqppasggcyvtslcrcfgEQvtyhnpplLFDLSRDPSESTPLTPATE 541
Cdd:PRK13759 397 ---LGYSSDN---YLTDGKWKYIWFSQTGE---------------------EQ--------LFDLKKDPHELHNLSPSEK 441
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-454 |
1.48e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 172.02 E-value: 1.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRrviqNLA 126
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVEN----AGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 127 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDsrsdqchhPYNYGFDYYygmpftlvdscwpdpsrNTELAFESql 206
Cdd:cd16033 77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEET--------PLDYGFDEY-----------------LPVETTIE-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 207 wlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplYWdcllmrgheiteqpmkaeragsiMVK 286
Cdd:cd16033 130 ----------------------------------------------------YF-----------------------LAD 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 287 EAISFLERHSK--ETFLLFFSFLHVHTP-----------------LPTT--DDFTG-------TSKH-GLYGDN------ 331
Cdd:cd16033 135 RAIEMLEELAAddKPFFLRVNFWGPHDPyippepyldmydpedipLPESfaDDFEDkpyiyrrERKRwGVDTEDeedwke 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 332 --------VEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGHLEARRGHAQlgGWNGIYKGGkgmggweggiRVPGIVR 403
Cdd:cd16033 215 iiahywgyITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDK--GPFMYEETY----------RIPLIIK 282
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 768032434 404 WPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNV 454
Cdd:cd16033 283 WPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK--VDGRSLLPLLRGEQ 331
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
47-530 |
1.35e-46 |
|
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: 166.99 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMvssgnrrvIQNLA 126
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA--------YDNAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 127 -VPAGLPlnetTLAALLKKQGYSTGLIGKWH-QGlncdsrSDQCHhpynyGFDYyygmpftlvdscwpdpsrNTELAFES 204
Cdd:cd16032 73 eFPADIP----TFAHYLRAAGYRTALSGKMHfVG------PDQLH-----GFDY------------------DEEVAFKA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 205 QLWLcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplyWDclLMRGHEitEQPmkaeragsim 284
Cdd:cd16032 120 VQKL---------------------------------------------------YD--LARGED--GRP---------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 285 vkeaisflerhsketFLLFFSFLHVHTPLPTTDDF----TGTSKHGLYGdNVEEMDSMVGKILDAIDDFGLRNNTLVYFT 360
Cdd:cd16032 135 ---------------FFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFT 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 361 SDHGGHLEARrghaqlGGWngiykggKGMGGWEGGIRVPGIVRWPGKvPAGRLIKEPTSLMDILPTVASVSGGSLPQDRV 440
Cdd:cd16032 199 SDHGDMLGER------GLW-------YKMSFFEGSARVPLIISAPGR-FAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVP 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 441 -IDGRDLMPLLQGNVRHSEHEFLFHYCGSYLHA-VRWIPKDDsgsvWKahYVtpvfqppasggcyvtslcrcfgeqVTYH 518
Cdd:cd16032 265 pLDGRSLLPLLEGGDSGGEDEVISEYLAEGAVApCVMIRRGR----WK--FI------------------------YCPG 314
|
490
....*....|..
gi 768032434 519 NPPLLFDLSRDP 530
Cdd:cd16032 315 DPDQLFDLEADP 326
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
47-558 |
1.47e-45 |
|
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: 167.44 E-value: 1.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIrsgmvssgNRRVIQNlA 126
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLM--------NHRSVWN-G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 127 VPagLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQchHPYN-------YGFDYYYGMPFTlvdscwpdPSRNTE 199
Cdd:cd16028 72 TP--LDARHLTLALELRKAGYDPALFGYTDTSPDPRGLAPL--DPRLlsyelamPGFDPVDRLDEY--------PAEDSD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 200 LAFesqlwlcvqlvaIAILTLTFgkLSGWVSVPWLLIFSmilFI-----FLLGYAWFSSHTSplywdcllmrgheitEQP 274
Cdd:cd16028 140 TAF------------LTDRAIEY--LDERQDEPWFLHLS---YIrphppFVAPAPYHALYDP---------------ADV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 275 MKAERAGSIMVKEAI-SFLERHSKETFLLffSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRN 353
Cdd:cd16028 188 PPPIRAESLAAEAAQhPLLAAFLERIESL--SFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 354 NTLVYFTSDHGGHLearrG-HAQLG--GWNGIYKggkgmggweggiRVPGIVRWPG---KVPAGRLIKEPTSLMDILPTV 427
Cdd:cd16028 266 DTLIVFTSDHGEQL----GdHWLWGkdGFFDQAY------------RVPLIVRDPRreaDATRGQVVDAFTESVDVMPTI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 428 ASVSGGslPQDRVIDGRDLMPLLQG-------NVRHSEHEFlfhYCGSYLHAVR-----------WIPKDDSgsvWKahY 489
Cdd:cd16028 330 LDWLGG--EIPHQCDGRSLLPLLAGaqpsdwrDAVHYEYDF---RDVSTRRPQEalglspdecslAVIRDER---WK--Y 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032434 490 VTpvfqppasggcyVTSLcrcfgeqvtyhnPPLLFDLSRDPSESTPLtpATEPLHDFVIKKVANALKEH 558
Cdd:cd16028 400 VH------------FAAL------------PPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKLLSW 442
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
45-484 |
2.34e-45 |
|
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: 166.59 E-value: 2.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 45 DKPNIVLIMVDDLGiGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVIQN 124
Cdd:cd16030 1 KKPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTG--------VYDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 125 LAVPAGLPLNETTLAALLKKQGYSTGLIGK-WHQGLNCDsrsdqchHPYNYGFDYYYGMPftlvdSCWPDPSRNTELAFE 203
Cdd:cd16030 72 NSYFRKVAPDAVTLPQYFKENGYTTAGVGKiFHPGIPDG-------DDDPASWDEPPNPP-----GPEKYPPGKLCPGKK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 204 SQLWLCVQLV-------------------AIAILTltfgKLSGwVSVPWllifsmilfiFL-LGYawFSSHTsPL----- 258
Cdd:cd16030 140 GGKGGGGGPAweaadvpdeaypdgkvadeAIEQLR----KLKD-SDKPF----------FLaVGF--YKPHL-PFvapkk 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 259 YWDcllMrgHEITEQPMKAERAGSIMVKEAISFLERHSKETFLLFFSFLHVHTPLPttDDFTGTSKHGLYGdNVEEMDSM 338
Cdd:cd16030 202 YFD---L--YPLESIPLPNPFDPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLP--DEQARELRQAYYA-SVSYVDAQ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 339 VGKILDAIDDFGLRNNTLVYFTSDHGGHLearrG-HAQLG---GWNgiykggkgmggweGGIRVPGIVRWPGKVPAGRLI 414
Cdd:cd16030 274 VGRVLDALEELGLADNTIVVLWSDHGWHL----GeHGHWGkhtLFE-------------EATRVPLIIRAPGVTKPGKVT 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 415 KEPTSLMDILPTVASVSGgsLPQDRVIDGRDLMPLLQG-NVRHSEHEFL-FHYCGSYLHAVR--------WIPKDDSGSV 484
Cdd:cd16030 337 DALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNpSAKWKDAAFSqYPRPSIMGYSIRteryryteWVDFDKVGAE 414
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-448 |
3.54e-45 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 161.18 E-value: 3.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLgIGD-LGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrviqnl 125
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 126 AVPAGLPLNETTLAALLKKQGYSTGLIgkwhqglncdsrSDQCHHPYNYGFDYYYgmpFTlvdscwpdpsrntelafesq 205
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFDRGF---DT-------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 206 lwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplYWDCLLMRGHEITEQPMKAERagsiMV 285
Cdd:cd16148 112 -----------------------------------------------------FEDFRGQEGDPGEEGDERAER----VT 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 286 KEAISFLERHSKETflLFFSFLH---VHTPLpttddftgtskhgLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSD 362
Cdd:cd16148 135 DRALEWLDRNADDD--PFFLFLHyfdPHEPY-------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSD 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 363 HGGHL-EarrgHAQLGGWNgiykggkgMGGWEGGIRVPGIVRWPGKVPAGRlIKEPTSLMDILPTVASVSGGSLPQDrvI 441
Cdd:cd16148 200 HGEEFgE----HGLYWGHG--------SNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--S 264
|
....*..
gi 768032434 442 DGRDLMP 448
Cdd:cd16148 265 DGRSLLP 271
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-530 |
5.58e-43 |
|
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: 156.93 E-value: 5.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrvIQNLA 126
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETG---------VWDNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 127 VPagLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsRSDQCHhpynyGFDYyygmpftlvdscwpdpsrntelafesql 206
Cdd:cd16037 72 DP--YDGDVPSWGHALRAAGYETVLIGKLHFR-----GEDQRH-----GFRY---------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 207 wlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplywdcllmrgheiteqpmkaERAgsiMVK 286
Cdd:cd16037 112 -----------------------------------------------------------------------DRD---VTE 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 287 EAISFLERH--SKETFLLFFSFLHVHTPLPTTDDF----TGTSKHGLYGdNVEEMDSMVGKILDAIDDFGLRNNTLVYFT 360
Cdd:cd16037 118 AAVDWLREEaaDDKPWFLFVGFVAPHFPLIAPQEFydlyVRRARAAYYG-LVEFLDENIGRVLDALEELGLLDNTLIIYT 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 361 SDHGGHLEARrghaqlGGWNgiykggkGMGGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRv 440
Cdd:cd16037 197 SDHGDMLGER------GLWG-------KSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL- 261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 441 iDGRDLMPLLQGNVRH-----SEheflFHYCGSYlHAVRWIPKDDsgsvWKAHYvtpvfqppasggcyvtslcrcfgeqv 515
Cdd:cd16037 262 -DGRSLLPLAEGPDDPdrvvfSE----YHAHGSP-SGAFMLRKGR----WKYIY-------------------------- 305
|
490
....*....|....*.
gi 768032434 516 tYHN-PPLLFDLSRDP 530
Cdd:cd16037 306 -YVGyPPQLFDLENDP 320
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-448 |
9.81e-42 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 151.24 E-value: 9.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGM---VSSGNrrvIQ 123
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwIVEGS---HG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 124 NLAVPAGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsrsdqchhpynygfdyyygmpftlvdscwpdpsrntelafe 203
Cdd:cd16149 78 KTKKPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG--------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 204 sqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplywdcllmrgheiteqpmkaeragsi 283
Cdd:cd16149 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 284 mVKEAISFLERHSKET-FLLFFSFLHVHTPlpttddftgtskHGlYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSD 362
Cdd:cd16149 113 -DDAADFLRRRAEAEKpFFLSVNYTAPHSP------------WG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSD 178
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 363 HG---GH---LEARRGHAQLGGWNgiykggkgmggweGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLP 436
Cdd:cd16149 179 NGfnmGHhgiWGKGNGTFPLNMYD-------------NSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPP 245
|
410
....*....|..
gi 768032434 437 QDRVIDGRDLMP 448
Cdd:cd16149 246 ADPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-556 |
2.18e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 145.40 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQ-HI----SAAsLCSPSRSAFLTGRYPIRSGMvssgnrr 120
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 121 viqnlAVPAGLPLNETTLAALLKKQGYSTGLIGKWHQglncdsrsdqchhpynygfdyyygmpftlvdscwpdpsrntel 200
Cdd:cd16155 74 -----GGKAAIPSDDKTWPETFKKAGYRTFATGKWHN------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 201 afesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllGYAwfsshtsplywdcllmrgheiteqpmkaera 280
Cdd:cd16155 106 ----------------------------------------------GFA------------------------------- 108
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 281 gsimvKEAISFLERHSKET--FLLFFSFLHVHTPLPTTDDFtgtskHGLYG----------------DN----------- 331
Cdd:cd16155 109 -----DAAIEFLEEYKDGDkpFFMYVAFTAPHDPRQAPPEY-----LDMYPpetiplpenflpqhpfDNgegtvrdeqla 178
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 332 -------------------VEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHG---GHlearrgHAQLGGWNgiykggkgm 389
Cdd:cd16155 179 pfprtpeavrqhlaeyyamITHLDAQIGRILDALEASGELDNTIIVFTSDHGlavGS------HGLMGKQN--------- 243
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 390 gGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNVRhSEHEFLFhycGSY 469
Cdd:cd16155 244 -LYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES--VEGKSLLPVIRGEKK-AVRDTLY---GAY 315
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 470 LHAVRWIPKDDsgsvWKAHYVTPvfqppasggcyvtslcrcfGEQVTyhnppLLFDLSRDPSESTPLtpATEPLHDFVIK 549
Cdd:cd16155 316 RDGQRAIRDDR----WKLIIYVP-------------------GVKRT-----QLFDLKKDPDELNNL--ADEPEYQERLK 365
|
....*..
gi 768032434 550 KVANALK 556
Cdd:cd16155 366 KLLAELK 372
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-558 |
1.19e-33 |
|
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: 131.97 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVIQNl 125
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETG--------CFRN- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 126 AVPagLPLNETTLAALLKKQGYSTGLIGKWHqglncdsrsdqchhpynygfdyyygmpftlvdscwpdpsrntelafesq 205
Cdd:cd16152 72 GIP--LPADEKTLAHYFRDAGYETGYVGKWH------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 206 lwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifLLGYawfsshtsplywdcllmRGHEITEQpmkaeragsimv 285
Cdd:cd16152 101 ---------------------------------------LAGY-----------------RVDALTDF------------ 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 286 keAISFLERHSKET-FLLFFSFLHVH----------------------TPlPTTDDFTGTSKHGL---YGdNVEEMDSMV 339
Cdd:cd16152 113 --AIDYLDNRQKDKpFFLFLSYLEPHhqndrdryvapegsaerfanfwVP-PDLAALPGDWAEELpdyLG-CCERLDENV 188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 340 GKILDAIDDFGLRNNTLVYFTSDHGGHLEARRG------HaqlggwngiykggkgmggwEGGIRVPGIVRWPGkVPAGRL 413
Cdd:cd16152 189 GRIRDALKELGLYDNTIIVFTSDHGCHFRTRNAeykrscH-------------------ESSIRVPLVIYGPG-FNGGGR 248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 414 IKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNVRHSEHEFLFHYCGSylHAVRWIPKDDsgsvWKahYVtpV 493
Cdd:cd16152 249 VEELVSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNEVFIQISES--QVGRAIRTDR----WK--YS--V 316
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032434 494 FQPPASGGCYVTSLcrcfgeqvTYHnPPLLFDLSRDPSESTPLtpATEPLHdfviKKVANALKEH 558
Cdd:cd16152 317 AAPDKDGWKDSGSD--------VYV-EDYLYDLEADPYELVNL--IGRPEY----REVAAELRER 366
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
46-444 |
1.40e-33 |
|
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: 132.29 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 46 KPNIVLIMVDDLgigDLGCYGNDTMRtPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPirsgmvssGNRRVIQNL 125
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYA--------HNHGVTNNS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 126 AVPAGLP------LNETTLAALLKKQGYSTGLIGKWhqgLN-CDSRSDQCHHPynYGFDYYYGMpftlvdscwPDPSRNT 198
Cdd:cd16147 69 PPGGGYPkfwqngLERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVP--PGWDEWDGL---------VGNSTYY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 199 ElafesqlwlcvqlvaiaiLTLTFGKLSGwvsvpwllifsmilfifllGYAWFSShtspLYWDCLLmrgheiteqpmkAE 278
Cdd:cd16147 135 N------------------YTLSNGGNGK-------------------HGVSYPG----DYLTDVI------------AN 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 279 RagsimvkeAISFLERHSKET--FLLFFSFLHVHTPL----PTTDDFTGTS---------------KHGL---------- 327
Cdd:cd16147 162 K--------ALDFLRRAAADDkpFFLVVAPPAPHGPFtpapRYANLFPNVTapprpppnnpdvsdkPHWLrrlpplnptq 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 328 --YGDNV--------EEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGHLearrG-HAQLGGwngiykggkGMGGWEGGI 396
Cdd:cd16147 234 iaYIDELyrkrlrtlQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHL----GqHRLPPG---------KRTPYEEDI 300
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 768032434 397 RVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGR 444
Cdd:cd16147 301 RVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
47-450 |
1.72e-33 |
|
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: 133.66 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSgnrrviqNLA 126
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTN-------CMA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 127 vpagLPLNETTLAALLKKQGYSTGLIGKWHqgLNcdsrsdqchhpynyGFDYY-YGMpftlvdsCwPDpsrntelafesq 205
Cdd:cd16156 74 ----LGDNVKTIGQRLSDNGIHTAYIGKWH--LD--------------GGDYFgNGI-------C-PQ------------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 206 lwlcvqlvaiailtltfgklsGWVSVPWlliFSMILFIFLLG----YAWFSSHTSplywdcllMRGHEITEQPMKAERag 281
Cdd:cd16156 114 ---------------------GWDPDYW---YDMRNYLDELTeeerRKSRRGLTS--------LEAEGIKEEFTYGHR-- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 282 siMVKEAISFLERHSKETFLLFFSFLHVHTPL----PTTD---DF--------------------------------TGT 322
Cdd:cd16156 160 --CTNRALDFIEKHKDEDFFLVVSYDEPHHPFlcpkPYASmykDFefpkgenayddlenkplhqrlwagakphedgdKGT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 323 SKHGLY-GDNvEEMDSMVGKILDAIDDfgLRNNTLVYFTSDHGGHLEARRGHAQlggwngiykggkGMGGWEGGIRVPGI 401
Cdd:cd16156 238 IKHPLYfGCN-SFVDYEIGRVLDAADE--IAEDAWVIYTSDHGDMLGAHKLWAK------------GPAVYDEITNIPLI 302
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 768032434 402 VRWPGKVPAGRLIKEPTSLMDILPTVASVSGgsLPQDRVIDGRDLMPLL 450
Cdd:cd16156 303 IRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATI 349
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
47-428 |
1.28e-30 |
|
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: 119.83 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRL-TQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIQNl 125
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 126 AVPAGLPLNETTLAALLKKQGYSTGLIGkwhqglncdsrsdqchhpynygfdyyygmpftlvdscwpdpsrntelafesq 205
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG---------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 206 lwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplywdcllmrgheiteqpmkaeragsimv 285
Cdd:cd00016 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 286 keAISFLERHSKE-TFLLFFSFLHVHTPlpttdDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHG 364
Cdd:cd00016 108 --LLKAIDETSKEkPFVLFLHFDGPDGP-----GHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHG 180
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032434 365 GHLEarrGHAQLGGwngiykGGKGMGGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVA 428
Cdd:cd00016 181 GIDK---GHGGDPK------ADGKADKSHTGMRVPFIAYGPG-VKKGGVKHELISQYDIAPTLA 234
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-465 |
2.46e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 121.16 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDD--------LGIGDLGCygndtmrtPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMvssgn 118
Cdd:cd16035 1 PNILLILTDQerypppwpAGWAALNL--------PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGV----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 119 rrvIQNLAVPAGLPLNET--TLAALLKKQGYSTGLIGKWHqglncdsrsdqchhpynygfdyyygmpftlvdscwpdpsr 196
Cdd:cd16035 68 ---TDTLGSPMQPLLSPDvpTLGHMLRAAGYYTAYKGKWH---------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 197 ntelafesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifLLGYAWFSSHTSPLywdcllmrgheITEQpmk 276
Cdd:cd16035 105 ------------------------------------------------LSGAAGGGYKRDPG-----------IAAQ--- 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 277 aeragsimvkeAISFLERHSKET-----FLLFFSFL--H-VHTPLPTTDDFTgtSKHGLYGDNVEEMDSMVGKILDAIDD 348
Cdd:cd16035 123 -----------AVEWLRERGAKNadgkpWFLVVSLVnpHdIMFPPDDEERWR--RFRNFYYNLIRDVDRQIGRVLDALDA 189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 349 FGLRNNTLVYFTSDHGGHLEARRGHAQLGgwngiykggkgmGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVA 428
Cdd:cd16035 190 SGLADNTIVVFTSDHGEMGGAHGLRGKGF------------NAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLL 257
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 768032434 429 SVSGGSLPQDRVID----GRDLMPLLQGNVRHS-EHEFLFHY 465
Cdd:cd16035 258 GLAGVDAEARATEApplpGRDLSPLLTDADADAvRDGILFTY 299
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-446 |
6.81e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 119.02 E-value: 6.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 46 KPNIVLIMVDDLGIGDLGCYGN----------DTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVs 115
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 116 sGNRRVIQNLavPAGLPlnetTLAALLKKQGYSTGLIGKWHQGlncdsrsdqchhpynygfdyyygmPFTLVdscwpdpS 195
Cdd:cd16153 80 -GFEAAHPAL--DHGLP----TFPEVLKKAGYQTASFGKSHLE------------------------AFQRY-------L 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 196 RNTELAFESqlwlcvqlvaiailtltfgklsgwvsvPWLLIFSMIlfifllgyawfsshtsplywdcllmrgheiteqpm 275
Cdd:cd16153 122 KNANQSYKS---------------------------FWGKIAKGA----------------------------------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 276 kaeragsimvkeaisflerHSKETFLLFFSFLHVHTP-LPTTD-----DFTGTSKHGlygdnveemDSMVGKILDAIDDF 349
Cdd:cd16153 140 -------------------DSDKPFFVRLSFLQPHTPvLPPKEfrdrfDYYAFCAYG---------DAQVGRAVEAFKAY 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 350 GL---RNNTLVYFTSDHGGHLEARRGHAQLGGWNgiykggkgmggweGGIRVPGIVRWPGK--VPAGRLIKEPTSLMDIL 424
Cdd:cd16153 192 SLkqdRDYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QSHRVPLIVVSSDKlkAPAGKVRHDFVEFVDLA 258
|
410 420
....*....|....*....|..
gi 768032434 425 PTVASVSGGSLPQDRVIDGRDL 446
Cdd:cd16153 259 PTLLAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-452 |
1.25e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 115.79 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnRRVIQNLa 126
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG------HRTLHHL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 127 vpagLPLNETTLAALLKKQGYSTGLIGKwhqglNCDSRSDqchhpynygfdyyygmpFTLVDSCWPDpsrntelafesql 206
Cdd:cd16150 74 ----LRPDEPNLLKTLKDAGYHVAWAGK-----NDDLPGE-----------------FAAEAYCDSD------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 207 WLCVQlVAIAILTLTFGKlsgwvsVPWLlifsmiLFIFLLG----YA----WFSSHTSplywDCLLMRgheITEQPMKAE 278
Cdd:cd16150 115 EACVR-TAIDWLRNRRPD------KPFC------LYLPLIFphppYGveepWFSMIDR----EKLPPR---RPPGLRAKG 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 279 RAgSIMVKEAISFLERHSKETFllffsflhvhtplpttDDFTGTskhglYGDNVEEMDSMVGKILDAIDDFGLRNNTLVY 358
Cdd:cd16150 175 KP-SMLEGIEKQGLDRWSEERW----------------RELRAT-----YLGMVSRLDHQFGRLLEALKETGLYDDTAVF 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 359 FTSDHGGHLearrG-HAQLGGWngiykggkGMGGWEGGIRVPGIVRwPGKVPAGRLIKEPTSLMDILPTVASVSGgsLPQ 437
Cdd:cd16150 233 FFSDHGDYT----GdYGLVEKW--------PNTFEDCLTRVPLIIK-PPGGPAGGVSDALVELVDIPPTLLDLAG--IPL 297
|
410
....*....|....*
gi 768032434 438 DRVIDGRDLMPLLQG 452
Cdd:cd16150 298 SHTHFGRSLLPVLAG 312
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-452 |
2.60e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 110.90 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGIGDLGCY--GNDTMRTPHIDRLAREGVRLTqHISAASLCSPSRSAFLTGRYPIRSGMvssgnrrviqn 124
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYslSSDLPVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGV----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 125 LAVPAGLPLNETTLAALLKKQ----GYSTGLIGKWHQGlNCDSrsdqchHPYNYG-FDYYYGMPFTLVDSCWPDPSRNTE 199
Cdd:cd16154 69 LAVPDELLLSEETLLQLLIKDattaGYSSAVIGKWHLG-GNDN------SPNNPGgIPYYAGILGGGVQDYYNWNLTNNG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 200 LAFESQLWLCVQLVAIAIltltfgklsGWV---SVPWLLIfsmilfiflLGYawfsshTSPlywdcllmrgHEiteqPMK 276
Cdd:cd16154 142 QTTNSTEYATTKLTNLAI---------DWIdqqTKPWFLW---------LAY------NAP----------HT----PFH 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 277 AERAGsimvkeaisflerhsketfllffsfLHVHTPLPTTDDFtGTSKHGLYGDNVEEMDSMVGKILDAIDDfGLRNNTL 356
Cdd:cd16154 184 LPPAE-------------------------LHSRSLLGDSADI-EANPRPYYLAAIEAMDTEIGRLLASIDE-EERENTI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 357 VYFTSDHGGHLEAR-----RGHAQ----LGGwngiykggkgmggweggIRVPGIVRWPGkvpAGRLIKEPTSLM---DIL 424
Cdd:cd16154 237 IIFIGDNGTPGQVVdlpytRNHAKgslyEGG-----------------INVPLIVSGAG---VERANERESALVnatDLY 296
|
410 420
....*....|....*....|....*...
gi 768032434 425 PTVASVSGGSLPQdrVIDGRDLMPLLQG 452
Cdd:cd16154 297 ATIAELAGVDAAE--IHDSVSFKPLLSD 322
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
47-531 |
2.42e-16 |
|
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: 81.05 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDDLGiGDLGCY-GNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPirsgmvssgnrRVIQNL 125
Cdd:cd16171 1 PNVVMVMSDSFD-GRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT-----------HLTESW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 126 AVPAGLPLNETTLAALLKKQGYSTGLIGKwhqglnCDSRSDQcHHPYNYGFDYYYGMPFTLVDSCWPdpsrntelafesq 205
Cdd:cd16171 69 NNYKGLDPNYPTWMDRLEKHGYHTQKYGK------LDYTSGH-HSVSNRVEAWTRDVPFLLRQEGRP------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 206 lwlCVQLVAIAilTLTFGKLSGWVSVpwllifsmilfifllgyawfsshtsplywdcllmrgheiteqpmkaERAGSIMV 285
Cdd:cd16171 129 ---TVNLVGDR--STVRVMLKDWQNT----------------------------------------------DKAVHWIR 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 286 KEAISFlerhsKETFLLFFSfLHVHTPLPTT---DDFTGTSK-HGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTS 361
Cdd:cd16171 158 KEAPNL-----TQPFALYLG-LNLPHPYPSPsmgENFGSIRNiRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTS 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 362 DHGghlEARRGHAQLggwngiykggKGMGGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvI 441
Cdd:cd16171 232 DHG---ELAMEHRQF----------YKMSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--L 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 442 DGRDLMPLLQGNVRHSEHEFLFH-------YCGSYLHAVRWIPKDDSgsvWKahYVTpvfqppasggcYVTslcrcfGEQ 514
Cdd:cd16171 296 SGYSLLPLLSESSIKESPSRVPHpdwvlseFHGCNVNASTYMLRTNS---WK--YIA-----------YAD------GNS 353
|
490
....*....|....*..
gi 768032434 515 VtyhnPPLLFDLSRDPS 531
Cdd:cd16171 354 V----PPQLFDLSKDPD 366
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
46-447 |
2.03e-11 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 66.60 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 46 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSG--MVSSGNRRViq 123
Cdd:COG1368 234 KPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGspYKRPGQNNF-- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 124 nlavpaglplneTTLAALLKKQGYSTgligkwhqglncdsrsdQCHHPYNYGFD----YYYGMPF-TLVD-SCWPDPSRN 197
Cdd:COG1368 312 ------------PSLPSILKKQGYET-----------------SFFHGGDGSFWnrdsFYKNLGFdEFYDrEDFDDPFDG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 198 telafesqlwlcvqlvaiailtltfgklsGWvsvpwllifsmilfifllGyawfsshtsplYWDcllmrgheiteqpmka 277
Cdd:COG1368 363 -----------------------------GW------------------G-----------VSD---------------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 278 eragSIMVKEAISFLERHSKETFLLFFSfLHVHTPLPTTDDF-----TGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLR 352
Cdd:COG1368 369 ----EDLFDKALEELEKLKKPFFAFLIT-LSNHGPYTLPEEDkkipdYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWY 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 353 NNTLVYFTSDHGGHLEARRghaqlggwngiykggkGMGGWEGGIRVPGIVrWPGKVPAGRLIKEPTSLMDILPTVASVSG 432
Cdd:COG1368 444 DNTIFVIYGDHGPRSPGKT----------------DYENPLERYRVPLLI-YSPGLKKPKVIDTVGSQIDIAPTLLDLLG 506
|
410
....*....|....*
gi 768032434 433 GSLPQDRVIdGRDLM 447
Cdd:COG1368 507 IDYPSYYAF-GRDLL 520
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
251-426 |
3.03e-10 |
|
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: 63.00 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 251 FSSH--TSPLYWDCLLmrgHEITEQPMKAERAG----SIMVKEAISFLERHSKETflLFFSFL---HVHT---------- 311
Cdd:COG3083 330 FSSAgfNSPLFRQTIF---SDVSLPRLHTPGGPaqrdRQITAQWLQWLDQRDSDR--PWFSYLfldAPHAysfpadypkp 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 312 --------PLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGHL----EARRGHAqlGGW 379
Cdd:COG3083 405 fqpsedcnYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnengQNYWGHN--SNF 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 768032434 380 NGIYkggkgmggweggIRVPGIVRWPGKVPagRLIKEPTSLMDILPT 426
Cdd:COG3083 483 SRYQ------------LQVPLVIHWPGTPP--QVISKLTSHLDIVPT 515
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
18-364 |
2.03e-09 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 59.76 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 18 MRPRRPLVFMSLVCALLNTCQAHRvhddkpNIVLIMVDDLGIGDLgcygnDTMRTPHIDRLAREGVRLTQHISAA-SLCS 96
Cdd:COG1524 1 MKRGLSLLLASLLAAAAAAAPPAK------KVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 97 PSRSAFLTGRYPIRSGMVSSG-----NRRVIQNLAVPAGLP-----LNETTLAALLKKQGYSTGLIGKWHQGlncDSRSD 166
Cdd:COG1524 70 PAHTTLLTGLYPGEHGIVGNGwydpeLGRVVNSLSWVEDGFgsnslLPVPTIFERARAAGLTTAAVFWPSFE---GSGLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 167 QCHHPYNY-GFDYYYGMPFTlvDscwpdpsrntelafesqlwlcVQLVAIAILTLTfgklsgwvsvpwllifsmilfifl 245
Cdd:COG1524 147 DAARPYPYdGRKPLLGNPAA--D---------------------RWIAAAALELLR------------------------ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 246 lgyawfsshtsplywdcllmrgheiTEQPmkaeragsimvkeaisflerhsketfllffSFLHVHtpLPTTDDfTGtSKH 325
Cdd:COG1524 180 -------------------------EGRP------------------------------DLLLVY--LPDLDY-AG-HRY 200
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 768032434 326 GLYGDN----VEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHG 364
Cdd:COG1524 201 GPDSPEyraaLREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
47-432 |
1.13e-08 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 56.54 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 47 PNIVLIMVDdlGIGD--LGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRS--AFLTGRYPIRSGMVSsgNRRVI 122
Cdd:cd16015 1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGS--YTLYK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 123 QNLAvpaglplneTTLAALLKKQGYSTGLIgkwhqglncdsrsdqchHPY------------NYGFDYYYGMpftlvdSC 190
Cdd:cd16015 77 LNPL---------PSLPSILKEQGYETIFI-----------------HGGdasfynrdsvypNLGFDEFYDL------ED 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 191 WPDPSRNTelafesqlwlcvqlvaiailtltfgklSGWvsvpwllifsmilfifllgyawfsshtspLYWDcllmrghei 270
Cdd:cd16015 125 FPDDEKET---------------------------NGW-----------------------------GVSD--------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 271 teqpmkaeragSIMVKEAISFLERHSKETFLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDN--------VEEMDSMVGKI 342
Cdd:cd16015 140 -----------ESLFDQALEELEELKKKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTelenylnaIHYTDKALGEF 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 343 LDAIDDFGLRNNTLVYFTSDHGGHLEarrghaqlggwngiYKGGKGMGGWEGGIRVPGIVRWPGKVPAGRlIKEPTSLMD 422
Cdd:cd16015 209 IEKLKKSGLYENTIIVIYGDHLPSLG--------------SDYDETDEDPLDLYRTPLLIYSPGLKKPKK-IDRVGSQID 273
|
410
....*....|
gi 768032434 423 ILPTVASVSG 432
Cdd:cd16015 274 IAPTLLDLLG 283
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
50-364 |
1.09e-04 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 44.72 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 50 VLIMVDDLGIGDLgcygNDTMRTPHIDRLAREGVRLTQHISAA-SLCSPSRSAFLTGRYPIRSGMVssGNR--------- 119
Cdd:pfam01663 2 LVISLDGFRADYL----DRFELTPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIV--GNTfydpktgey 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 120 --RVIQNLAVPAglPLNETTLAALLKKQGYSTGLIGkWhqglncdSRSDQCHHPYNYGFDYYYGMPFtlvdscwpdpsrN 197
Cdd:pfam01663 76 lvFVISDPEDPR--WWQGEPIWDTAAKAGVRAAALF-W-------PGSEVDYSTYYGTPPRYLKDDY------------N 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 198 TELAFEsqlwlcvqlvaiailtltfGKLSGWVSVPWLlifsmilfifllgyawfsshtsplywdcllmrgheiteqpmka 277
Cdd:pfam01663 134 NSVPFE-------------------DRVDTAVLQTWL------------------------------------------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 278 eragsimvkeAISFLERHSKETFLLFFSFLHVhtplpttdDFTGtSKHGLYGDNVEEM----DSMVGKILDAIDDFGLRN 353
Cdd:pfam01663 152 ----------DLPFADVAAERPDLLLVYLEEP--------DYAG-HRYGPDSPEVEDAlrrvDRAIGDLLEALDERGLFE 212
|
330
....*....|.
gi 768032434 354 NTLVYFTSDHG 364
Cdd:pfam01663 213 DTNVIVVSDHG 223
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
291-370 |
3.16e-04 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 43.49 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032434 291 FLERHSKETFllfFSFLHVHTPlpTTDDFTGTSKhglygdnveeMDSMVGKILDAIDDFGLRNNTLVYFTSDHG------ 364
Cdd:pfam02995 284 FLPRYRDSPF---FGFFWSNSL--SHDDFNYASA----------LDEDFLKYLKKLHKRGLLDNTIVIFMSDHGlrfgkl 348
|
90
....*....|.
gi 768032434 365 -----GHLEAR 370
Cdd:pfam02995 349 rrtsqGMLEER 359
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
304-364 |
2.06e-03 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 40.26 E-value: 2.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032434 304 FSFLHVHTPlpttdDFTGtskHGlYGDN-------VEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHG 364
Cdd:cd16018 159 LILLYFEEP-----DSAG---HK-YGPDspevneaLKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG 217
|
|
| |
