|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
29-553 |
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: 770.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 29 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIQNL 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 109 AVPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQCHHPYNYGFDYYYGMPFTLVDSCWPDPSRNTELAFESQ 188
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 189 LWLCVQLVAIAILTLTFGKLSGWVSvpWLLIFSMILFIFLLGYAWFSSHTSPLYWDCLLMRGHEITEQPMKAERAGSIMV 268
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLYLGAVS--KRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 269 KEAISFLERHSKETFLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGG 348
Cdd:cd16159 239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 349 HLEARRGHAQLGGWNGIYKGGKGMGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRD 428
Cdd:cd16159 319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 429 LMPLLQGNVRHSEHEFLFHYCGSYLHAVRWIPKdDSGSVWKAHYVTPVFQpPASGGCYVTSLCRCFGEQVTYHNPPLLFD 508
Cdd:cd16159 399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPR-DGGAVWKAHYFTPNFY-PGTEGCCGTLLCRCFGDSVTHHDPPLLFD 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 319996604 509 LSRDPSESTPLTPATEPlHDFVIKKVANALKEHQETIVPVTYQLS 553
Cdd:cd16159 477 LSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
29-520 |
3.52e-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: 437.77 E-value: 3.52e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 29 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIQNl 108
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 109 avpaGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsrsDQ-CHHPYNYGFDYYYGMPFTlvDSCWPDPSRNTElafes 187
Cdd:cd16026 80 ----GLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYS--NDMWPFPLYRND----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 188 qlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsPLYWDCLLMRGHEITEQPMKAERAGSIM 267
Cdd:cd16026 142 ----------------------------------------------------PPGPLPPLMENEEVIEQPADQSSLTQRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 268 VKEAISFLERHSKETFLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHG 347
Cdd:cd16026 170 TDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 348 GHLE--ARRGHAQL----------GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSG 415
Cdd:cd16026 250 PWLEygGHGGSAGPlrggkgttweGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 416 GSLPQDRVIDGRDLMPLLQGNVRHSEHEFLFHYCGSYLHAVRWIPkddsgsvWKAHYVTPVFQPPASGGCYVTSlcrcfg 495
Cdd:cd16026 313 APLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR-------WKLHLPTTYRTGTDPGGLDPTK------ 379
|
490 500
....*....|....*....|....*
gi 319996604 496 eqvtyHNPPLLFDLSRDPSESTPLT 520
Cdd:cd16026 380 -----LEPPLLYDLEEDPGETYNVA 399
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
29-540 |
1.08e-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: 377.16 E-value: 1.08e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 29 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSsGNRRVIQNL 108
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG-GTRVFLPWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 109 AVpaGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQCHHPYNYGFDYY-YGMPFTLVdscwpdpsrntelafes 187
Cdd:cd16160 80 IG--GLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFDFVgTNLPFTNS----------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 188 qlWLCVqlvaiailtltfgklsgwvsvPWllifsmilfifllGYAWFSSHTSPlywdCLLMRGHEITEQPMKAERAGSIM 267
Cdd:cd16160 141 --WACD---------------------DT-------------GRHVDFPDRSA----CFLYYNDTIVEQPIQHEHLTETL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 268 VKEAISFLERHSKETFLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHG 347
Cdd:cd16160 181 VGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 348 GHLEA----------RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPaGRLIKEPTSLMDILPTVASVSG 415
Cdd:cd16160 261 PHVEYcleggstgglKGGKGNSweGG-----------------IRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTFVDLAG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 416 GSLPQDRVIDGRDLMPLLQGNVRHSEHEFLFHYCgSYLHAVRwipkddSGSvWKAHYVTPVFQ------PPASGGCYVTS 489
Cdd:cd16160 323 GTLPTDRIYDGLSITDLLLGEADSPHDDILYYCC-SRLMAVR------YGS-YKIHFKTQPLPsqesldPNCDGGGPLSD 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 319996604 490 --LCR-CFGEQVTYHNPPLLFDLSRDPSESTPLTPAtepLHDFVIKKVANALKE 540
Cdd:cd16160 395 yiVCYdCEDECVTKHNPPLIFDVEKDPGEQYPLQPS---VYEHMLEAVEKLIAH 445
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
29-520 |
2.44e-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: 302.08 E-value: 2.44e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 29 KPNIVLIMVDDLGIGDLGCYGNDTMR-TPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIqn 107
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 108 lavpAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNcdsrsdQCHHPYNYGFDYYYGMPFtlvdscwpdpSRNTELAFEs 187
Cdd:cd16161 79 ----GGLPLNETTLAEVLRQAGYATGMIGKWHLGQR------EAYLPNSRGFDYYFGIPF----------SHDSSLADR- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 188 qlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgYAWFsshtsplywdcllmrgheiteqpmkaeragsim 267
Cdd:cd16161 138 -------------------------------------------YAQF--------------------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 268 vkeAISFLERHSKET--FLLFFSFLHVHTPLPTTDDF-TGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTS 344
Cdd:cd16161 142 ---ATDFIQRASAKDrpFFLYAALAHVHVPLANLPRFqSPTSGRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTS 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 345 DHGGHLEARRGHAQLGGWNGIYKGGKGMGGWEG---GIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQD 421
Cdd:cd16161 219 DNGPWEVKCELAVGPGTGDWQGNLGGSVAKASTwegGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 422 RVIDGRDLMPLLQGNVRhSEHEFLFHYCGSY-----LHAVRWIPkddsgsvWKAHYVTpvfqppasGGCYVTslCRCFGE 496
Cdd:cd16161 299 RIYDGKDLSPVLFGGSK-TGHRCLFHPNSGAagagaLSAVRCGD-------YKAHYAT--------GGALAC--CGSTGP 360
|
490 500
....*....|....*....|....
gi 319996604 497 QVtYHNPPLLFDLSRDPSESTPLT 520
Cdd:cd16161 361 KL-YHDPPLLFDLEVDPAESFPLT 383
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-517 |
1.46e-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: 301.00 E-value: 1.46e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGM--VSSGNRRVIQN 107
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 108 LAVPA-----GLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDsrsdqcHHPYNYGFDYYYGmpftlvDSCWPDPSRnte 182
Cdd:cd16144 81 TKLIPppsttRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGG------YGPEDQGFDVNIG------GTGNGGPPS--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 183 lafesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllGYAWFSSHTSPLYwdcllmrghEITEQPMKAER 262
Cdd:cd16144 146 -----------------------------------------------YYFPPGKPNPDLE---------DGPEGEYLTDR 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 263 agsiMVKEAISFLERHSKETFLLFFSFLHVHTPLPTTDDF----------TGTSKHG-LYGDNVEEMDSMVGKILDAIDD 331
Cdd:cd16144 170 ----LTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELiekyekkkkgLRKGQKNpVYAAMIESLDESVGRILDALEE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 332 FGLRNNTLVYFTSDHGGHLEA----------RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKE 399
Cdd:cd16144 246 LGLADNTLVIFTSDNGGLSTRggpptsnaplRGGKGSLyeGG-----------------IRVPLIVRWPGVIKPGSVSDV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 400 PTSLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNVRHSEHEFLF----HYCGSYLHAVRWIPKDDsgsvWKAHYvtp 475
Cdd:cd16144 309 PVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFwhfpHYHGQGGRPASAIRKGD----WKLIE--- 381
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 319996604 476 vfqppasggcyvtslcrcFGEQVTYHnpplLFDLSRDPSEST 517
Cdd:cd16144 382 ------------------FYEDGRVE----LYNLKNDIGETN 401
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-519 |
3.86e-96 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 299.10 E-value: 3.86e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 1 MRpRRPLVFMSLVCALLNTCQAhrvhdDKPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSP 80
Cdd:COG3119 1 MK-RLLLLLLALLAAAAAAAAA-----KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 81 SRSAFLTGRYPIRSGMVSSGNRRviqnlavPAGLPLNETTLAALLKKQGYSTGLIGKWHqglncdsrsdqchhpynygfd 160
Cdd:COG3119 75 SRASLLTGRYPHRTGVTDNGEGY-------NGGLPPDEPTLAELLKEAGYRTALFGKWH--------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 161 yyygmpftlvdscwpdpsrntelafesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsp 240
Cdd:COG3119 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 241 LYWDcllmrgHEITEqpmkaeragsimvkEAISFLERHSKET--FLLFFSFLHVHTPLPTTDDF---------------- 302
Cdd:COG3119 127 LYLT------DLLTD--------------KAIDFLERQADKDkpFFLYLAFNAPHAPYQAPEEYldkydgkdiplppnla 186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 303 -------TGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGHLEA---RRGHAQL--GGwngiykggk 370
Cdd:COG3119 187 prdlteeELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEhglRGGKGTLyeGG--------- 257
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 371 gmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNVRHSEHEFLFHYCG 450
Cdd:COG3119 258 --------IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPR 327
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 451 SY-LHAVRwipKDDsgsvWKahYVTPVFQPPasggcyvtslcrcfgeqvtyhnPPLLFDLSRDPSESTPL 519
Cdd:COG3119 328 GGgNRAIR---TGR----WK--LIRYYDDDG----------------------PWELYDLKNDPGETNNL 366
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-520 |
1.77e-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: 296.75 E-value: 1.77e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDT---MRTPHIDRLAREGVRLTQHISAASlCSPSRSAFLTGRYPIRSGMVSSGnrrvIQ 106
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIgrgAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVG----LP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 107 NLavPAGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsRSDQcHHPYNYGFDYYYGMPFTLVDScwpdpsrntelafe 186
Cdd:cd16142 76 GS--PGGLPPWEPTLAELLKDAGYATAQFGKWHLG-----DEDG-RLPTDHGFDEFYGNLYHTIDE-------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 187 sqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplywdcllmrghEITEQpmkaeragsi 266
Cdd:cd16142 134 -----------------------------------------------------------------EIVDK---------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 267 mvkeAISFLERHSKET--FLLFFSFLHVHTPLPTTDDFTGTSK-HGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFT 343
Cdd:cd16142 139 ----AIDFIKRNAKADkpFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFT 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 344 SDHGGHLEA--------RRGH---AQLGGWngiykggkgmggweggiRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVAS 412
Cdd:cd16142 215 TDNGPEQDVwpdggytpFRGEkgtTWEGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAA 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 413 VSGGSLP------QDRVIDGRDLMPLLQGNVRHSEHEFLFHYCGSYLHAVRWipKDdsgsvWKAHY-VTPVFQPPASGGC 485
Cdd:cd16142 278 LAGAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRW--KN-----WKVHFkAQEDTGGPTGEPF 350
|
490 500 510
....*....|....*....|....*....|....*
gi 319996604 486 YVTSLcrcfgeqvtyhnpPLLFDLSRDPSESTPLT 520
Cdd:cd16142 351 YVLTF-------------PLIFNLRRDPKERYDVT 372
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-517 |
1.02e-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: 295.65 E-value: 1.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDT-MRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGM---VSSGNRrvi 105
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSkIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLkggVLGGFS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 106 qnlavPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQCHH----------------PYNYGFDYYYGMPftl 169
Cdd:cd16143 78 -----PPLIEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIP--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 170 vdscwpdpsrntelafesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplywdcllmr 249
Cdd:cd16143 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 250 gheiteqpmkAERAGSIMVKEAISFLERHSKET--FLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILD 327
Cdd:cd16143 150 ----------ASEVLPTLTDKAVEFIDQHAKKDkpFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILD 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 328 AIDDFGLRNNTLVYFTSDHGGHLEARRGHAQL------------------GGwngiykggkgmggweggIRVPGIVRWPG 389
Cdd:cd16143 220 ALKELGLAENTLVIFTSDNGPSPYADYKELEKfghdpsgplrgmkadiyeGG-----------------HRVPFIVRWPG 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 390 KVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNVRHSEHEFLFHYCGSYLHAVR---W--IPKDDS 464
Cdd:cd16143 283 KIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGSFAIRkgdWklIDGTGS 362
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 319996604 465 GSvWKAHYVTPVFQPPasggcyvtslcrcfgeqvtyhnPPLLFDLSRDPSEST 517
Cdd:cd16143 363 GG-FSYPRGKEKLGLP----------------------PGQLYNLSTDPGESN 392
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
29-574 |
6.33e-93 |
|
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: 6.33e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 29 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMV-------SSGn 101
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYpgvfypgSRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 102 rrviqnlavpaGLPLNETTLAALLKKQGYSTGLIGKWHQGLNcdsrSDQCHHPYNYGFDYYYGMPFTLvDSCwpdPsrnt 181
Cdd:cd16158 80 -----------GLPLNETTIAEVLKTVGYQTAMVGKWHLGVG----LNGTYLPTHQGFDHYLGIPYSH-DQG---P---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 182 elafesqlwlCVQLVAIAILTLTFGKLSGWVSvpwllifsmilfifllgyawfsshTSPLYWDcllmrgHEITEQPMKAE 261
Cdd:cd16158 137 ----------CQNLTCFPPNIPCFGGCDQGEV------------------------PCPLFYN------ESIVQQPVDLL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 262 RAGSIMVKEAISFLERHSKET--FLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTL 339
Cdd:cd16158 177 TLEERYAKFAKDFIADNAKEGkpFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 340 VYFTSDHGGHL--EARRGHAQL----------GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIkEPTSLMDIL 407
Cdd:cd16158 257 VFFTSDNGPSTmrKSRGGNAGLlkcgkgttyeGG-----------------VREPAIAYWPGRIKPGVTH-ELASTLDIL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 408 PTVASVSGGSLPqDRVIDGRDLMPLLQGNVRHSEHEFLFHYCGSY----LHAVRWipkddsgSVWKAHYVT---PVFQPP 480
Cdd:cd16158 319 PTIAKLAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDpdkgVFAVRW-------GKYKAHFYTqgaAHSGTT 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 481 ASGGCYVTSLcrcfgeqVTYHNPPLLFDLSRDPSESTPLTPATEplHDFVIKKVaNALKEHQETivPVTYQLSELNQGR- 559
Cdd:cd16158 391 PDKDCHPSAE-------LTSHDPPLLFDLSQDPSENYNLLGLPE--YNQVLKQI-QQVKERFEA--SMKFGESEINKGEd 458
|
570 580
....*....|....*....|
gi 319996604 560 TWLKPCC--GVFPF---CLC 574
Cdd:cd16158 459 PALEPCCkpGCTPKpscCQC 478
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
29-552 |
7.40e-86 |
|
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: 274.73 E-value: 7.40e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 29 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSG----NRRV 104
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNaharNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 105 IQNLAvpAGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsrSDQCHHPYNYGFDYYYGMPftlvdSCWPDPSRNTELa 184
Cdd:cd16157 81 PQNIV--GGIPDSEILLPELLKKAGYRNKIVGKWHLG------HRPQYHPLKHGFDEWFGAP-----NCHFGPYDNKAY- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 185 fesqlwlcvqlvaiailtltfgklsgwvsvPWLlifsmilfifllgyawfsshtsPLYWDCLlMRGHEITEQPMKAERAG 264
Cdd:cd16157 147 ------------------------------PNI----------------------PVYRDWE-MIGRYYEEFKIDKKTGE 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 265 S----IMVKEAISFLERH--SKETFLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNT 338
Cdd:cd16157 174 SnltqIYLQEALEFIEKQhdAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 339 LVYFTSDHGGhleARRGHAQLGGWNgIYKGGKGMGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSL 418
Cdd:cd16157 254 FVFFSSDNGA---ALISAPEQGGSN-GPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 419 PQDRVIDGRDLMPLLQGNvrHSEHEFLFHYCGSYLHAVRWipkddsgSVWKAHYVTpvFQPPASGGCYVTSLCRcfGEQ- 497
Cdd:cd16157 330 PSDRAIDGIDLLPVLLNG--KEKDRPIFYYRGDELMAVRL-------GQYKAHFWT--WSNSWEEFRKGINFCP--GQNv 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 319996604 498 --VTYHN------PPLLFDLSRDPSESTPLTPATePLHDFVIKKVANALKEHQETIVPVTYQL 552
Cdd:cd16157 397 pgVTTHNqtdhtkLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQL 458
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-517 |
1.01e-82 |
|
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: 264.84 E-value: 1.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYpirsgmvsSGNRRVIQNLA 109
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLH--------TGHTRVRGNSE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 110 VPAGLPL--NETTLAALLKKQGYSTGLIGKWhqGLNCDSRSDqchHPYNYGFDYYYGmpftlvdscwpdpsrntelafes 187
Cdd:cd16145 73 PGGQDPLppDDVTLAEVLKKAGYATAAFGKW--GLGGPGTPG---HPTKQGFDYFYG----------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 188 qlWLCvQLVAiailtLTFgklsgwvsvpwlliFSMILfifllgyaWFSSHTSPLYWDCLLMRGHEITEQPMKAERAGSIM 267
Cdd:cd16145 125 --YLD-QVHA-----HNY--------------YPEYL--------WRNGEKVPLPNNVIPPLDEGNNAGGGGGTYSHDLF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 268 VKEAISFLERHSKETFLLFFSFLHVHTPLPTTDD---FTGTSKHGLYGDN------------VEEMDSMVGKILDAIDDF 332
Cdd:cd16145 175 TDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDDgpyKYKPKDPGIYAYLpwpqpekayaamVTRLDRDVGRILALLKEL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 333 GLRNNTLVYFTSDHGGHLEARRGHAQL-----------------GGwngiykggkgmggweggIRVPGIVRWPGKVPAGR 395
Cdd:cd16145 255 GIDENTLVVFTSDNGPHSEGGSEHDPDffdsngplrgykrslyeGG-----------------IRVPFIARWPGKIPAGS 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 396 LIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNVRHSEHEFLF--HYCGSYLHAVRWipkDDsgsvWKAhyv 473
Cdd:cd16145 318 VSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLYweFYEGGGAQAVRM---GG----WKA--- 385
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 319996604 474 tpVFQPPASGgcyvtslcrcfgeqvtyhnPPLLFDLSRDPSEST 517
Cdd:cd16145 386 --VRHGKKDG-------------------PFELYDLSTDPGETN 408
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
30-428 |
4.28e-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: 251.97 E-value: 4.28e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSsgnrrviqNLA 109
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRG--------NVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 110 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQglncdsrsdqchhpynygfdyyygmpftlvdscwpdpsrntelafesql 189
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWHD------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 190 wlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplywdcllmrgheiteqpmkaeragsimvk 269
Cdd:cd16022 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 270 EAISFLERHSKET-FLLFFSFLHVHTPLpttddftgtskhgLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGG 348
Cdd:cd16022 104 EAIDFIERRDKDKpFFLYVSFNAPHPPF-------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 349 HLEA---RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrv 423
Cdd:cd16022 171 MLGDhglRGKKGSLyeGG-----------------IRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG-- 231
|
....*
gi 319996604 424 IDGRD 428
Cdd:cd16022 232 LDGRS 236
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
30-517 |
6.63e-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: 233.98 E-value: 6.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQ-HISaaSLCSPSRSAFLTGRYPIRSGMVSSGNRRVIqnl 108
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 109 avpagLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDsrsdqcHHPYNYGFDYYYGmpftlvdscwpdpsrntelafesq 188
Cdd:cd16146 76 -----MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYP------YRPQDRGFDEVLG------------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 189 lwlcvqlvaiailtltFGklSGWVSVPWllifsmilfifllgYAWFSSHTSPLYWdcllmrgHEITEQPMKaeraG---S 265
Cdd:cd16146 121 ----------------HG--GGGIGQYP--------------DYWGNDYFDDTYY-------HNGKFVKTE----GyctD 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 266 IMVKEAISFLERHSKETFLLFFSFLHVHTPLPTTDDF------TGTSKH--GLYGdNVEEMDSMVGKILDAIDDFGLRNN 337
Cdd:cd16146 158 VFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYldpykdMGLDDKlaAFYG-MIENIDDNVGRLLAKLKELGLEEN 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 338 TLVYFTSDHG----------GHLEARRGHAQLGGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDIL 407
Cdd:cd16146 237 TIVIFMSDNGpaggvpkrfnAGMRGKKGSVYEGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDLL 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 408 PTVASVSGGSLPQDRVIDGRDLMPLLQGNVRHSEHEFLFhycgsyLHAVRWIPKDDS---GSVWKAHY--VTPvfqppas 482
Cdd:cd16146 300 PTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLF------THSGRWPPPPKKkrnAAVRTGRWrlVSP------- 366
|
490 500 510
....*....|....*....|....*....|....*
gi 319996604 483 ggcyvtslcrcfgeqvtYHNPPLLFDLSRDPSEST 517
Cdd:cd16146 367 -----------------KGFQPELYDIENDPGEEN 384
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-519 |
2.53e-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: 225.94 E-value: 2.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTqHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrviqnlA 109
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNY-------------V 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 110 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSdqchHPYNYGFDYYYgmpftlvdscwpdpsrntelafesqL 189
Cdd:cd16151 67 VFGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGD----YPHEFGFDEYC-------------------------L 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 190 WlcvQLVaiailtltfgklsgwvsvpwllifsmilfifllGYAWFSSHTSPLYWDCLLMRGHEITEQpmkaERAGSIMVK 269
Cdd:cd16151 118 W---QLT---------------------------------ETGEKYSRPATPTFNIRNGKLLETTEG----DYGPDLFAD 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 270 EAISFLERHSKETFLLFFSFLHVHTPLPTT------DDFTGTSKH--GLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVY 341
Cdd:cd16151 158 FLIDFIERNKDQPFFAYYPMVLVHDPFVPTpdspdwDPDDKRKKDdpEYFPDMVAYMDKLVGKLVDKLEELGLRENTIII 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 342 FTSDHGGHLEARR-----------GHAQLGGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTV 410
Cdd:cd16151 238 FTGDNGTHRPITSrtngrevrggkGKTTDAG-----------------THVPLIVNWPGLIPAGGVSDDLVDFSDFLPTL 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 411 ASVSGGSLPQDRVIDGRDLMPLLQGNVRHSEHEFLFHYcgsylhAVRWIPKDDSGSVWKAHYvtpvfqppasggcyvtsl 490
Cdd:cd16151 301 AELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWY------YRNPHKKFGSRFVRTKRY------------------ 356
|
490 500
....*....|....*....|....*....
gi 319996604 491 crcfgeqvTYHNPPLLFDLSRDPSESTPL 519
Cdd:cd16151 357 --------KLYADGRFFDLREDPLEKNPL 377
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
30-519 |
1.36e-66 |
|
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: 222.04 E-value: 1.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASlCSPSRSAFLTGRYPIRSGMvssgNRRVIQNlA 109
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGM----QHGVILA-G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 110 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsrsdQCHHPY---NYGFDYYYGmpftlvdscwpdpsrntelafe 186
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWEYtptNRGFDSFYG---------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 187 sqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfiFLLGYAWFSSHTSPLYWDC--LLMRGHEITEQPMKAERAG 264
Cdd:cd16029 125 ----------------------------------------YYGGAEDYYTHTSGGANDYgnDDLRDNEEPAWDYNGTYST 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 265 SIMVKEAISFLERHSKET-FLLFFSFLHVHTPLPT----TDDFTGTSKHGLYGD------NVEEMDSMVGKILDAIDDFG 333
Cdd:cd16029 165 DLFTDRAVDIIENHDPSKpLFLYLAFQAVHAPLQVppeyADPYEDKFAHIKDEDrrtyaaMVSALDESVGNVVDALKAKG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 334 LRNNTLVYFTSDHGGHLEA---------RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPG-KVPAGRLIKEPT 401
Cdd:cd16029 245 MLDNTLIVFTSDNGGPTGGgdggsnyplRGGKNTLweGG-----------------VRVPAFVWSPLlPPKRGTVSDGLM 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 402 SLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNVRHSEHEFL----FHYCGSYLHAVRWipKDdsgsvWKahYVTpvf 477
Cdd:cd16029 308 HVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILlnidDITRTTGGAAIRV--GD-----WK--LIV--- 375
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 319996604 478 qppasggcyvtslcrcfGEQvtyhnpplLFDLSRDPSESTPL 519
Cdd:cd16029 376 -----------------GKP--------LFNIENDPCERNDL 392
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-519 |
1.90e-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: 216.67 E-value: 1.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 29 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRrviqnl 108
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 109 avpagLPLNETTLAALLKKQGYSTGLIGKWH----QGLNCDSRSDQCHHPYNYGFDYYYGMpftlvdSCWPDpsrntela 184
Cdd:cd16034 75 -----LPPDAPTIADVLKDAGYRTGYIGKWHldgpERNDGRADDYTPPPERRHGFDYWKGY------ECNHD-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 185 fesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfssHTSPLYWDcllmrgheiTEQPMKAERAG 264
Cdd:cd16034 136 ----------------------------------------------------HNNPHYYD---------DDGKRIYIKGY 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 265 S--IMVKEAISFLERHSKET--FLLFFSFLHVHTP------------------LPTTDDFTGTSKHGL-------YGdNV 315
Cdd:cd16034 155 SpdAETDLAIEYLENQADKDkpFALVLSWNPPHDPyttapeeyldmydpkkllLRPNVPEDKKEEAGLredlrgyYA-MI 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 316 EEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGHLEArrgHAQLG---GWNgiykggkgmggweGGIRVPGIVRWPGKVP 392
Cdd:cd16034 234 TALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGS---HGLMNkqvPYE-------------ESIRVPFIIRYPGKIK 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 393 AGRLIKEPTSLMDILPTVASVSGgsLPQDRVIDGRDLMPLLQGNVRHSEHEFLFhYCGSYLHAVRWIPKDDSGSVWKAHY 472
Cdd:cd16034 298 AGRVVDLLINTVDIMPTLLGLCG--LPIPDTVEGRDLSPLLLGGKDDEPDSVLL-QCFVPFGGGSARDGGEWRGVRTDRY 374
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 319996604 473 vtpvfqppasggcyvtSLCRCFGeqvtyhNPPLLFDLSRDPSESTPL 519
Cdd:cd16034 375 ----------------TYVRDKN------GPWLLFDNEKDPYQLNNL 399
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
30-543 |
2.50e-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: 212.75 E-value: 2.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIgDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMvsSGNRRVIQNLa 109
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA--HGLRSRGFPL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 110 vPAGLPlnetTLAALLKKQGYSTGLIGKWHQGlncdsrsdqchHPYNYGFDYYYGMPFTLVDSCWPDPSrntelAFESQL 189
Cdd:cd16027 77 -PDGVK----TLPELLREAGYYTGLIGKTHYN-----------PDAVFPFDDEMRGPDDGGRNAWDYAS-----NAADFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 190 WLCVQlvaiailtltfGKlsgwvsvPWllifsmilfifllgYAWFSSHTSplywdcllmrgHEITEQPMKAEragsimvk 269
Cdd:cd16027 136 NRAKK-----------GQ-------PF--------------FLWFGFHDP-----------HRPYPPGDGEE-------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 270 eaisflERHSKETFLLfFSFLhVHTPlPTTDDFTGtskhglYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGH 349
Cdd:cd16027 165 ------PGYDPEKVKV-PPYL-PDTP-EVREDLAD------YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMP 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 350 LEarRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGR 427
Cdd:cd16027 230 FP--RAKGTLydSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGR 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 428 DLMPLLQGNVRHsEHEFLF---HYCGSYLHAVRWIPKDDsgsvWKahYVtpvfqppasggcyvtslcRCFgeqvtyhNPP 504
Cdd:cd16027 289 SFLPLLKGEKDP-GRDYVFaerDRHDETYDPIRSVRTGR----YK--YI------------------RNY-------MPE 336
|
490 500 510
....*....|....*....|....*....|....*....
gi 319996604 505 LLFDLSRDPSESTPLtpATEPLHDFVIKKVANALKEHQE 543
Cdd:cd16027 337 ELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
30-415 |
3.49e-59 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 199.57 E-value: 3.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSgnrrviqnla 109
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 110 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNcdSRSDqchhPYNYGFDYYYGmpftlvdscwpdpsrntelafesql 189
Cdd:pfam00884 71 TPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWY--NNQS----PCNLGFDKFFG------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 190 wlcvqlvaiailtltfgklsgwvsvpwllifsmilfiFLLGYAWFSSHTSPLYWdcllMRGHEITEQpmkaeragsIMVK 269
Cdd:pfam00884 120 -------------------------------------RNTGSDLYADPPDVPYN----CSGGGVSDE---------ALLD 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 270 EAISFLERHSKEtFLLFFSFLHVHTPLPTTDDFTGTSK------------HGLYGDNVEEMDSMVGKILDAIDDFGLRNN 337
Cdd:pfam00884 150 EALEFLDNNDKP-FFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLLDN 228
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319996604 338 TLVYFTSDHGGHLEARRGHAQLGGWNgiykggkgmGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSG 415
Cdd:pfam00884 229 TLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
28-540 |
2.34e-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: 190.43 E-value: 2.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 28 DKPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGnrrviqn 107
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNN------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 108 lavPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDqchhpynyGFDYYYGmpftlvdscwpdpsrntelaFES 187
Cdd:cd16031 74 ---GPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--------GFDYWVS--------------------FPG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 188 QlwlcvqlvaIAILTLTFGKLSGWVSVPWllifsmilfifllgyawfssHTSplywdcllmrgHEITEQpmkaeragsim 267
Cdd:cd16031 123 Q---------GSYYDPEFIENGKRVGQKG--------------------YVT-----------DIITDK----------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 268 vkeAISFLERHSKET-FLLFFSFLHVHT-----------------PLPTT---DDFTGTSK------------------- 307
Cdd:cd16031 152 ---ALDFLKERDKDKpFCLSLSFKAPHRpftpaprhrglyedvtiPEPETfddDDYAGRPEwareqrnrirgvldgrfdt 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 308 HGLYGDNVE-------EMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGHLearrGHAQLGG-WNgiykggkgmgGWEGGI 379
Cdd:cd16031 229 PEKYQRYMKdylrtvtGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL----GEHGLFDkRL----------MYEESI 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 380 RVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNVRHS-EHEFLFHYcgsYLHavrw 458
Cdd:cd16031 295 RVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEY---YEE---- 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 459 ipkddsgsvWKAHYVTPVFqppasgGCyVTS---LCRCFGEQVTYHnpplLFDLSRDPSESTPLtpATEPLHDFVIKKVA 535
Cdd:cd16031 366 ---------PNFHNVPTHE------GV-RTErykYIYYYGVWDEEE----LYDLKKDPLELNNL--ANDPEYAEVLKELR 423
|
....*
gi 319996604 536 NALKE 540
Cdd:cd16031 424 KRLEE 428
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
440-574 |
5.08e-54 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 179.43 E-value: 5.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 440 SEHEFLFHYCGSYLHAVRWIPkddsgsvWKAHYVTPVFQPPASGGCYVTslcrcfGEQVTYHNPPLLFDLSRDPSESTPL 519
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP-------YKAHFFTPSFDPPGAEGCYGS------KVPVTHHDPPLLFDLERDPSEKYPL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 319996604 520 TPATePLHDFVIKKVANALKEHQETIVPVTYQLSELNQG-RTWLKPCCGVFPFCLC 574
Cdd:pfam14707 68 SPDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLwDPWLQPCCPTFPACTC 122
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
28-519 |
1.73e-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: 176.48 E-value: 1.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 28 DKPNIVLIMVDDLGIGDLGCYGNDtMRTPHIDRLAREGVRLTQ-HisAASLCSPSRSAFLTGRYPIRSGMvssGNrrvIQ 106
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM---GT---MA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 107 NLAVPAG-----LPLNETTLAALLKKQGYSTGLIGKWHQGLNcdsrsdqchhpynygfDYYygmpftlvdscwpdpsrnt 181
Cdd:cd16025 72 ELATGKPgyegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------------DYY------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 182 elafesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfSSHTsplywdcllmrgheiteqpmkae 261
Cdd:cd16025 117 -----------------------------------------------------STDD----------------------- 120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 262 ragsiMVKEAISFLERHSKET--FLLFFSFLHVHTPL----PTTDDFTGTSKHG----------------LYGDN----- 314
Cdd:cd16025 121 -----LTDKAIEYIDEQKAPDkpFFLYLAFGAPHAPLqapkEWIDKYKGKYDAGwdalreerlerqkelgLIPADtkltp 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 315 -----------------------------VEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGhlEARRGHAQ------- 358
Cdd:cd16025 196 rppgvpawdslspeekklearrmevyaamVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGA--SAEPGWANasntpfr 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 359 -------LGGwngiykggkgmggweggIRVPGIVRWP-GKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRV------I 424
Cdd:cd16025 274 lykqashEGG-----------------IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpL 336
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 425 DGRDLMPLLQGNVRHSEHEFL-FHYCGSylHAVRwipKDDsgsvWKAhyvtpvfqppasggcyvtslcrcfgeqVTYHNP 503
Cdd:cd16025 337 DGVSLLPTLDGAAAPSRRRTQyFELFGN--RAIR---KGG----WKA---------------------------VALHPP 380
|
570 580
....*....|....*....|..
gi 319996604 504 PL------LFDLSRDPSESTPL 519
Cdd:cd16025 381 PGwgdqweLYDLAKDPSETHDL 402
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
29-524 |
3.20e-48 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 175.24 E-value: 3.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 29 KPNIVLIMVDDLGiGD-LGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNrrviqn 107
Cdd:PRK13759 6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGD------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 108 lavpaGLPLN-ETTLAALLKKQGYSTGLIGKWHqglncdsrsdqcHHPYN--YGFDYyygmpfTLVDSCWPDPSRN---T 181
Cdd:PRK13759 79 -----VVPWNyKNTLPQEFRDAGYYTQCIGKMH------------VFPQRnlLGFHN------VLLHDGYLHSGRNedkS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 182 ELAFESQ--LWLCVQLVAI-AILTLTFGKLSGWVSVPWLLifsmilfifllgyawfSSHTSPLYWdcllmrgheiteqpm 258
Cdd:PRK13759 136 QFDFVSDylAWLREKAPGKdPDLTDIGWDCNSWVARPWDL----------------EERLHPTNW--------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 259 kaeragsiMVKEAISFLERHSK-ETFLLFFSFLHVHTPL-----------------PTTDDF--------TGTSKHGLYG 312
Cdd:PRK13759 185 --------VGSESIEFLRRRDPtKPFFLKMSFARPHSPYdppkryfdmykdadipdPHIGDWeyaedqdpEGGSIDALRG 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 313 D---------------NVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDH----GGHLEARRGHAQLGgwngiykggkgmg 373
Cdd:PRK13759 257 NlgeeyarraraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHgdmlGDHYLFRKGYPYEG------------- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 374 gwegGIRVPGIVRWPG---KVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGN---VR---HSEHEf 444
Cdd:PRK13759 324 ----SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQyegWRpylHGEHA- 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 445 lfhYCGSYLHavrWIPKDDSGSVWKAHYVTpvfqppasggcyvtslcrcfgEQvtyhnpplLFDLSRDPSESTPLTPATE 524
Cdd:PRK13759 397 ---LGYSSDN---YLTDGKWKYIWFSQTGE---------------------EQ--------LFDLKKDPHELHNLSPSEK 441
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-437 |
1.83e-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: 171.25 E-value: 1.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRrviqNLA 109
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVEN----AGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 110 VPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDsrsdqchhPYNYGFDYYygmpftlvdscwpdpsrNTELAFESql 189
Cdd:cd16033 77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEET--------PLDYGFDEY-----------------LPVETTIE-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 190 wlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplYWdcllmrgheiteqpmkaeragsiMVK 269
Cdd:cd16033 130 ----------------------------------------------------YF-----------------------LAD 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 270 EAISFLERHSK--ETFLLFFSFLHVHTP-----------------LPTT--DDFTG-------TSKH-GLYGDN------ 314
Cdd:cd16033 135 RAIEMLEELAAddKPFFLRVNFWGPHDPyippepyldmydpedipLPESfaDDFEDkpyiyrrERKRwGVDTEDeedwke 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 315 --------VEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGHLEARRGHAQlgGWNGIYKGGkgmggweggiRVPGIVR 386
Cdd:cd16033 215 iiahywgyITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDK--GPFMYEETY----------RIPLIIK 282
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 319996604 387 WPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNV 437
Cdd:cd16033 283 WPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK--VDGRSLLPLLRGEQ 331
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
30-513 |
1.61e-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: 166.21 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNrrviqnlA 109
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-------E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 110 VPAGLPlnetTLAALLKKQGYSTGLIGKWH-QGlncdsrSDQCHhpynyGFDYyygmpftlvdscwpdpsrNTELAFESQ 188
Cdd:cd16032 74 FPADIP----TFAHYLRAAGYRTALSGKMHfVG------PDQLH-----GFDY------------------DEEVAFKAV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 189 LWLcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplyWDclLMRGHEitEQPmkaeragsimv 268
Cdd:cd16032 121 QKL---------------------------------------------------YD--LARGED--GRP----------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 269 keaisflerhsketFLLFFSFLHVHTPLPTTDDF----TGTSKHGLYGdNVEEMDSMVGKILDAIDDFGLRNNTLVYFTS 344
Cdd:cd16032 135 --------------FFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTS 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 345 DHGGHLEARrghaqlGGWngiykggKGMGGWEGGIRVPGIVRWPGKvPAGRLIKEPTSLMDILPTVASVSGGSLPQDRV- 423
Cdd:cd16032 200 DHGDMLGER------GLW-------YKMSFFEGSARVPLIISAPGR-FAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPp 265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 424 IDGRDLMPLLQGNVRHSEHEFLFHYCGSYLHA-VRWIPKDDsgsvWKahYVtpvfqppasggcyvtslcrcfgeqVTYHN 502
Cdd:cd16032 266 LDGRSLLPLLEGGDSGGEDEVISEYLAEGAVApCVMIRRGR----WK--FI------------------------YCPGD 315
|
490
....*....|.
gi 319996604 503 PPLLFDLSRDP 513
Cdd:cd16032 316 PDQLFDLEADP 326
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
30-541 |
2.43e-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: 166.28 E-value: 2.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIrsgmvssgNRRVIQNlA 109
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLM--------NHRSVWN-G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 110 VPagLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQchHPYN-------YGFDYYYGMPFTlvdscwpdPSRNTE 182
Cdd:cd16028 72 TP--LDARHLTLALELRKAGYDPALFGYTDTSPDPRGLAPL--DPRLlsyelamPGFDPVDRLDEY--------PAEDSD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 183 LAFesqlwlcvqlvaIAILTLTFgkLSGWVSVPWLLIFSmilFI-----FLLGYAWFSSHTSplywdcllmrgheitEQP 257
Cdd:cd16028 140 TAF------------LTDRAIEY--LDERQDEPWFLHLS---YIrphppFVAPAPYHALYDP---------------ADV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 258 MKAERAGSIMVKEAI-SFLERHSKETFLLffSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRN 336
Cdd:cd16028 188 PPPIRAESLAAEAAQhPLLAAFLERIESL--SFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 337 NTLVYFTSDHGGHLearrG-HAQLG--GWNGIYKggkgmggweggiRVPGIVRWPG---KVPAGRLIKEPTSLMDILPTV 410
Cdd:cd16028 266 DTLIVFTSDHGEQL----GdHWLWGkdGFFDQAY------------RVPLIVRDPRreaDATRGQVVDAFTESVDVMPTI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 411 ASVSGGslPQDRVIDGRDLMPLLQG-------NVRHSEHEFlfhYCGSYLHAVR-----------WIPKDDSgsvWKahY 472
Cdd:cd16028 330 LDWLGG--EIPHQCDGRSLLPLLAGaqpsdwrDAVHYEYDF---RDVSTRRPQEalglspdecslAVIRDER---WK--Y 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319996604 473 VTpvfqppasggcyVTSLcrcfgeqvtyhnPPLLFDLSRDPSESTPLtpATEPLHDFVIKKVANALKEH 541
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 ... |
28-467 |
3.09e-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: 165.82 E-value: 3.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 28 DKPNIVLIMVDDLGiGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVIQN 107
Cdd:cd16030 1 KKPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTG--------VYDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 108 LAVPAGLPLNETTLAALLKKQGYSTGLIGK-WHQGLNCDsrsdqchHPYNYGFDYYYGMPftlvdSCWPDPSRNTELAFE 186
Cdd:cd16030 72 NSYFRKVAPDAVTLPQYFKENGYTTAGVGKiFHPGIPDG-------DDDPASWDEPPNPP-----GPEKYPPGKLCPGKK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 187 SQLWLCVQLV-------------------AIAILTltfgKLSGwVSVPWllifsmilfiFL-LGYawFSSHTsPL----- 241
Cdd:cd16030 140 GGKGGGGGPAweaadvpdeaypdgkvadeAIEQLR----KLKD-SDKPF----------FLaVGF--YKPHL-PFvapkk 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 242 YWDcllMrgHEITEQPMKAERAGSIMVKEAISFLERHSKETFLLFFSFLHVHTPLPttDDFTGTSKHGLYGdNVEEMDSM 321
Cdd:cd16030 202 YFD---L--YPLESIPLPNPFDPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLP--DEQARELRQAYYA-SVSYVDAQ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 322 VGKILDAIDDFGLRNNTLVYFTSDHGGHLearrG-HAQLG---GWNgiykggkgmggweGGIRVPGIVRWPGKVPAGRLI 397
Cdd:cd16030 274 VGRVLDALEELGLADNTIVVLWSDHGWHL----GeHGHWGkhtLFE-------------EATRVPLIIRAPGVTKPGKVT 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 398 KEPTSLMDILPTVASVSGgsLPQDRVIDGRDLMPLLQG-NVRHSEHEFL-FHYCGSYLHAVR--------WIPKDDSGSV 467
Cdd:cd16030 337 DALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNpSAKWKDAAFSqYPRPSIMGYSIRteryryteWVDFDKVGAE 414
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-431 |
8.08e-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: 160.02 E-value: 8.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLgIGD-LGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrviqnl 108
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 109 AVPAGLPLNETTLAALLKKQGYSTGLIgkwhqglncdsrSDQCHHPYNYGFDYYYgmpFTlvdscwpdpsrntelafesq 188
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFDRGF---DT-------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 189 lwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplYWDCLLMRGHEITEQPMKAERagsiMV 268
Cdd:cd16148 112 -----------------------------------------------------FEDFRGQEGDPGEEGDERAER----VT 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 269 KEAISFLERHSKETflLFFSFLH---VHTPLpttddftgtskhgLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSD 345
Cdd:cd16148 135 DRALEWLDRNADDD--PFFLFLHyfdPHEPY-------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSD 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 346 HGGHL-EarrgHAQLGGWNgiykggkgMGGWEGGIRVPGIVRWPGKVPAGRlIKEPTSLMDILPTVASVSGGSLPQDrvI 424
Cdd:cd16148 200 HGEEFgE----HGLYWGHG--------SNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--S 264
|
....*..
gi 319996604 425 DGRDLMP 431
Cdd:cd16148 265 DGRSLLP 271
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-513 |
7.04e-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: 156.16 E-value: 7.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrvIQNLA 109
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETG---------VWDNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 110 VPagLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsRSDQCHhpynyGFDYyygmpftlvdscwpdpsrntelafesql 189
Cdd:cd16037 72 DP--YDGDVPSWGHALRAAGYETVLIGKLHFR-----GEDQRH-----GFRY---------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 190 wlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplywdcllmrgheiteqpmkaERAgsiMVK 269
Cdd:cd16037 112 -----------------------------------------------------------------------DRD---VTE 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 270 EAISFLERH--SKETFLLFFSFLHVHTPLPTTDDF----TGTSKHGLYGdNVEEMDSMVGKILDAIDDFGLRNNTLVYFT 343
Cdd:cd16037 118 AAVDWLREEaaDDKPWFLFVGFVAPHFPLIAPQEFydlyVRRARAAYYG-LVEFLDENIGRVLDALEELGLLDNTLIIYT 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 344 SDHGGHLEARrghaqlGGWNgiykggkGMGGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRv 423
Cdd:cd16037 197 SDHGDMLGER------GLWG-------KSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL- 261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 424 iDGRDLMPLLQGNVRH-----SEheflFHYCGSYlHAVRWIPKDDsgsvWKAHYvtpvfqppasggcyvtslcrcfgeqv 498
Cdd:cd16037 262 -DGRSLLPLAEGPDDPdrvvfSE----YHAHGSP-SGAFMLRKGR----WKYIY-------------------------- 305
|
490
....*....|....*.
gi 319996604 499 tYHN-PPLLFDLSRDP 513
Cdd:cd16037 306 -YVGyPPQLFDLENDP 320
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-431 |
1.21e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 150.85 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGM---VSSGNrrvIQ 106
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwIVEGS---HG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 107 NLAVPAGLPLNETTLAALLKKQGYSTGLIGKWHQGlncdsrsdqchhpynygfdyyygmpftlvdscwpdpsrntelafe 186
Cdd:cd16149 78 KTKKPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG--------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 187 sqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplywdcllmrgheiteqpmkaeragsi 266
Cdd:cd16149 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 267 mVKEAISFLERHSKET-FLLFFSFLHVHTPlpttddftgtskHGlYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSD 345
Cdd:cd16149 113 -DDAADFLRRRAEAEKpFFLSVNYTAPHSP------------WG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSD 178
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 346 HG---GH---LEARRGHAQLGGWNgiykggkgmggweGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLP 419
Cdd:cd16149 179 NGfnmGHhgiWGKGNGTFPLNMYD-------------NSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPP 245
|
410
....*....|..
gi 319996604 420 QDRVIDGRDLMP 431
Cdd:cd16149 246 ADPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-539 |
2.15e-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: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 29 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQ-HI----SAAsLCSPSRSAFLTGRYPIRSGMvssgnrr 103
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 104 viqnlAVPAGLPLNETTLAALLKKQGYSTGLIGKWHQglncdsrsdqchhpynygfdyyygmpftlvdscwpdpsrntel 183
Cdd:cd16155 74 -----GGKAAIPSDDKTWPETFKKAGYRTFATGKWHN------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 184 afesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllGYAwfsshtsplywdcllmrgheiteqpmkaera 263
Cdd:cd16155 106 ----------------------------------------------GFA------------------------------- 108
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 264 gsimvKEAISFLERHSKET--FLLFFSFLHVHTPLPTTDDFtgtskHGLYG----------------DN----------- 314
Cdd:cd16155 109 -----DAAIEFLEEYKDGDkpFFMYVAFTAPHDPRQAPPEY-----LDMYPpetiplpenflpqhpfDNgegtvrdeqla 178
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 315 -------------------VEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHG---GHlearrgHAQLGGWNgiykggkgm 372
Cdd:cd16155 179 pfprtpeavrqhlaeyyamITHLDAQIGRILDALEASGELDNTIIVFTSDHGlavGS------HGLMGKQN--------- 243
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 373 gGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNVRhSEHEFLFhycGSY 452
Cdd:cd16155 244 -LYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES--VEGKSLLPVIRGEKK-AVRDTLY---GAY 315
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 453 LHAVRWIPKDDsgsvWKAHYVTPvfqppasggcyvtslcrcfGEQVTyhnppLLFDLSRDPSESTPLtpATEPLHDFVIK 532
Cdd:cd16155 316 RDGQRAIRDDR----WKLIIYVP-------------------GVKRT-----QLFDLKKDPDELNNL--ADEPEYQERLK 365
|
....*..
gi 319996604 533 KVANALK 539
Cdd:cd16155 366 KLLAELK 372
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-541 |
1.36e-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: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 29 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVIQNl 108
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETG--------CFRN- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 109 AVPagLPLNETTLAALLKKQGYSTGLIGKWHqglncdsrsdqchhpynygfdyyygmpftlvdscwpdpsrntelafesq 188
Cdd:cd16152 72 GIP--LPADEKTLAHYFRDAGYETGYVGKWH------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 189 lwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifLLGYawfsshtsplywdcllmRGHEITEQpmkaeragsimv 268
Cdd:cd16152 101 ---------------------------------------LAGY-----------------RVDALTDF------------ 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 269 keAISFLERHSKET-FLLFFSFLHVH----------------------TPlPTTDDFTGTSKHGL---YGdNVEEMDSMV 322
Cdd:cd16152 113 --AIDYLDNRQKDKpFFLFLSYLEPHhqndrdryvapegsaerfanfwVP-PDLAALPGDWAEELpdyLG-CCERLDENV 188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 323 GKILDAIDDFGLRNNTLVYFTSDHGGHLEARRG------HaqlggwngiykggkgmggwEGGIRVPGIVRWPGkVPAGRL 396
Cdd:cd16152 189 GRIRDALKELGLYDNTIIVFTSDHGCHFRTRNAeykrscH-------------------ESSIRVPLVIYGPG-FNGGGR 248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 397 IKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNVRHSEHEFLFHYCGSylHAVRWIPKDDsgsvWKahYVtpV 476
Cdd:cd16152 249 VEELVSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNEVFIQISES--QVGRAIRTDR----WK--YS--V 316
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 319996604 477 FQPPASGGCYVTSLcrcfgeqvTYHnPPLLFDLSRDPSESTPLtpATEPLHdfviKKVANALKEH 541
Cdd:cd16152 317 AAPDKDGWKDSGSD--------VYV-EDYLYDLEADPYELVNL--IGRPEY----REVAAELRER 366
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
30-433 |
1.96e-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: 133.28 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSgnrrviqNLA 109
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTN-------CMA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 110 vpagLPLNETTLAALLKKQGYSTGLIGKWHqgLNcdsrsdqchhpynyGFDYY-YGMpftlvdsCwPDpsrntelafesq 188
Cdd:cd16156 74 ----LGDNVKTIGQRLSDNGIHTAYIGKWH--LD--------------GGDYFgNGI-------C-PQ------------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 189 lwlcvqlvaiailtltfgklsGWVSVPWlliFSMILFIFLLG----YAWFSSHTSplywdcllMRGHEITEQPMKAERag 264
Cdd:cd16156 114 ---------------------GWDPDYW---YDMRNYLDELTeeerRKSRRGLTS--------LEAEGIKEEFTYGHR-- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 265 siMVKEAISFLERHSKETFLLFFSFLHVHTPL----PTTD---DF--------------------------------TGT 305
Cdd:cd16156 160 --CTNRALDFIEKHKDEDFFLVVSYDEPHHPFlcpkPYASmykDFefpkgenayddlenkplhqrlwagakphedgdKGT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 306 SKHGLY-GDNvEEMDSMVGKILDAIDDfgLRNNTLVYFTSDHGGHLEARRGHAQlggwngiykggkGMGGWEGGIRVPGI 384
Cdd:cd16156 238 IKHPLYfGCN-SFVDYEIGRVLDAADE--IAEDAWVIYTSDHGDMLGAHKLWAK------------GPAVYDEITNIPLI 302
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 319996604 385 VRWPGKVPAGRLIKEPTSLMDILPTVASVSGgsLPQDRVIDGRDLMPLL 433
Cdd:cd16156 303 IRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATI 349
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
29-427 |
2.09e-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: 131.90 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 29 KPNIVLIMVDDLgigDLGCYGNDTMRtPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPirsgmvssGNRRVIQNL 108
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYA--------HNHGVTNNS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 109 AVPAGLP------LNETTLAALLKKQGYSTGLIGKWhqgLN-CDSRSDQCHHPynYGFDYYYGMpftlvdscwPDPSRNT 181
Cdd:cd16147 69 PPGGGYPkfwqngLERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVP--PGWDEWDGL---------VGNSTYY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 182 ElafesqlwlcvqlvaiaiLTLTFGKLSGwvsvpwllifsmilfifllGYAWFSShtspLYWDCLLmrgheiteqpmkAE 261
Cdd:cd16147 135 N------------------YTLSNGGNGK-------------------HGVSYPG----DYLTDVI------------AN 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 262 RagsimvkeAISFLERHSKET--FLLFFSFLHVHTPL----PTTDDFTGTS---------------KHGL---------- 310
Cdd:cd16147 162 K--------ALDFLRRAAADDkpFFLVVAPPAPHGPFtpapRYANLFPNVTapprpppnnpdvsdkPHWLrrlpplnptq 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 311 --YGDNV--------EEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGHLearrG-HAQLGGwngiykggkGMGGWEGGI 379
Cdd:cd16147 234 iaYIDELyrkrlrtlQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHL----GqHRLPPG---------KRTPYEEDI 300
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 319996604 380 RVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGR 427
Cdd:cd16147 301 RVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
30-411 |
1.68e-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: 119.45 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRL-TQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIQNl 108
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 109 AVPAGLPLNETTLAALLKKQGYSTGLIGkwhqglncdsrsdqchhpynygfdyyygmpftlvdscwpdpsrntelafesq 188
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG---------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 189 lwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifllgyawfsshtsplywdcllmrgheiteqpmkaeragsimv 268
Cdd:cd00016 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 269 keAISFLERHSKE-TFLLFFSFLHVHTPlpttdDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHG 347
Cdd:cd00016 108 --LLKAIDETSKEkPFVLFLHFDGPDGP-----GHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHG 180
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319996604 348 GHLEarrGHAQLGGwngiykGGKGMGGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVA 411
Cdd:cd00016 181 GIDK---GHGGDPK------ADGKADKSHTGMRVPFIAYGPG-VKKGGVKHELISQYDIAPTLA 234
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-448 |
4.01e-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: 120.39 E-value: 4.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDD--------LGIGDLGCygndtmrtPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMvssgn 101
Cdd:cd16035 1 PNILLILTDQerypppwpAGWAALNL--------PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGV----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 102 rrvIQNLAVPAGLPLNET--TLAALLKKQGYSTGLIGKWHqglncdsrsdqchhpynygfdyyygmpftlvdscwpdpsr 179
Cdd:cd16035 68 ---TDTLGSPMQPLLSPDvpTLGHMLRAAGYYTAYKGKWH---------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 180 ntelafesqlwlcvqlvaiailtltfgklsgwvsvpwllifsmilfifLLGYAWFSSHTSPLywdcllmrgheITEQpmk 259
Cdd:cd16035 105 ------------------------------------------------LSGAAGGGYKRDPG-----------IAAQ--- 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 260 aeragsimvkeAISFLERHSKET-----FLLFFSFL--H-VHTPLPTTDDFTgtSKHGLYGDNVEEMDSMVGKILDAIDD 331
Cdd:cd16035 123 -----------AVEWLRERGAKNadgkpWFLVVSLVnpHdIMFPPDDEERWR--RFRNFYYNLIRDVDRQIGRVLDALDA 189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 332 FGLRNNTLVYFTSDHGGHLEARRGHAQLGgwngiykggkgmGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVA 411
Cdd:cd16035 190 SGLADNTIVVFTSDHGEMGGAHGLRGKGF------------NAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLL 257
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 319996604 412 SVSGGSLPQDRVID----GRDLMPLLQGNVRHS-EHEFLFHY 448
Cdd:cd16035 258 GLAGVDAEARATEApplpGRDLSPLLTDADADAvRDGILFTY 299
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-429 |
8.37e-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: 118.63 E-value: 8.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 29 KPNIVLIMVDDLGIGDLGCYGN----------DTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVs 98
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 99 sGNRRVIQNLavPAGLPlnetTLAALLKKQGYSTGLIGKWHQGlncdsrsdqchhpynygfdyyygmPFTLVdscwpdpS 178
Cdd:cd16153 80 -GFEAAHPAL--DHGLP----TFPEVLKKAGYQTASFGKSHLE------------------------AFQRY-------L 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 179 RNTELAFESqlwlcvqlvaiailtltfgklsgwvsvPWLLIFSMIlfifllgyawfsshtsplywdcllmrgheiteqpm 258
Cdd:cd16153 122 KNANQSYKS---------------------------FWGKIAKGA----------------------------------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 259 kaeragsimvkeaisflerHSKETFLLFFSFLHVHTP-LPTTD-----DFTGTSKHGlygdnveemDSMVGKILDAIDDF 332
Cdd:cd16153 140 -------------------DSDKPFFVRLSFLQPHTPvLPPKEfrdrfDYYAFCAYG---------DAQVGRAVEAFKAY 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 333 GL---RNNTLVYFTSDHGGHLEARRGHAQLGGWNgiykggkgmggweGGIRVPGIVRWPGK--VPAGRLIKEPTSLMDIL 407
Cdd:cd16153 192 SLkqdRDYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QSHRVPLIVVSSDKlkAPAGKVRHDFVEFVDLA 258
|
410 420
....*....|....*....|..
gi 319996604 408 PTVASVSGGSLPQDRVIDGRDL 429
Cdd:cd16153 259 PTLLAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-435 |
1.36e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 115.41 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnRRVIQNLa 109
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG------HRTLHHL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 110 vpagLPLNETTLAALLKKQGYSTGLIGKwhqglNCDSRSDqchhpynygfdyyygmpFTLVDSCWPDpsrntelafesql 189
Cdd:cd16150 74 ----LRPDEPNLLKTLKDAGYHVAWAGK-----NDDLPGE-----------------FAAEAYCDSD------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 190 WLCVQlVAIAILTLTFGKlsgwvsVPWLlifsmiLFIFLLG----YA----WFSSHTSplywDCLLMRgheITEQPMKAE 261
Cdd:cd16150 115 EACVR-TAIDWLRNRRPD------KPFC------LYLPLIFphppYGveepWFSMIDR----EKLPPR---RPPGLRAKG 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 262 RAgSIMVKEAISFLERHSKETFllffsflhvhtplpttDDFTGTskhglYGDNVEEMDSMVGKILDAIDDFGLRNNTLVY 341
Cdd:cd16150 175 KP-SMLEGIEKQGLDRWSEERW----------------RELRAT-----YLGMVSRLDHQFGRLLEALKETGLYDDTAVF 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 342 FTSDHGGHLearrG-HAQLGGWngiykggkGMGGWEGGIRVPGIVRwPGKVPAGRLIKEPTSLMDILPTVASVSGgsLPQ 420
Cdd:cd16150 233 FFSDHGDYT----GdYGLVEKW--------PNTFEDCLTRVPLIIK-PPGGPAGGVSDALVELVDIPPTLLDLAG--IPL 297
|
410
....*....|....*
gi 319996604 421 DRVIDGRDLMPLLQG 435
Cdd:cd16150 298 SHTHFGRSLLPVLAG 312
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-435 |
2.40e-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: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGIGDLGCY--GNDTMRTPHIDRLAREGVRLTqHISAASLCSPSRSAFLTGRYPIRSGMvssgnrrviqn 107
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYslSSDLPVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGV----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 108 LAVPAGLPLNETTLAALLKKQ----GYSTGLIGKWHQGlNCDSrsdqchHPYNYG-FDYYYGMPFTLVDSCWPDPSRNTE 182
Cdd:cd16154 69 LAVPDELLLSEETLLQLLIKDattaGYSSAVIGKWHLG-GNDN------SPNNPGgIPYYAGILGGGVQDYYNWNLTNNG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 183 LAFESQLWLCVQLVAIAIltltfgklsGWV---SVPWLLIfsmilfiflLGYawfsshTSPlywdcllmrgHEiteqPMK 259
Cdd:cd16154 142 QTTNSTEYATTKLTNLAI---------DWIdqqTKPWFLW---------LAY------NAP----------HT----PFH 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 260 AERAGsimvkeaisflerhsketfllffsfLHVHTPLPTTDDFtGTSKHGLYGDNVEEMDSMVGKILDAIDDfGLRNNTL 339
Cdd:cd16154 184 LPPAE-------------------------LHSRSLLGDSADI-EANPRPYYLAAIEAMDTEIGRLLASIDE-EERENTI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 340 VYFTSDHGGHLEAR-----RGHAQ----LGGwngiykggkgmggweggIRVPGIVRWPGkvpAGRLIKEPTSLM---DIL 407
Cdd:cd16154 237 IIFIGDNGTPGQVVdlpytRNHAKgslyEGG-----------------INVPLIVSGAG---VERANERESALVnatDLY 296
|
410 420
....*....|....*....|....*...
gi 319996604 408 PTVASVSGGSLPQdrVIDGRDLMPLLQG 435
Cdd:cd16154 297 ATIAELAGVDAAE--IHDSVSFKPLLSD 322
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
30-514 |
2.52e-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: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDDLGiGDLGCY-GNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPirsgmvssgnrRVIQNL 108
Cdd:cd16171 1 PNVVMVMSDSFD-GRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT-----------HLTESW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 109 AVPAGLPLNETTLAALLKKQGYSTGLIGKwhqglnCDSRSDQcHHPYNYGFDYYYGMPFTLVDSCWPdpsrntelafesq 188
Cdd:cd16171 69 NNYKGLDPNYPTWMDRLEKHGYHTQKYGK------LDYTSGH-HSVSNRVEAWTRDVPFLLRQEGRP------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 189 lwlCVQLVAIAilTLTFGKLSGWVSVpwllifsmilfifllgyawfsshtsplywdcllmrgheiteqpmkaERAGSIMV 268
Cdd:cd16171 129 ---TVNLVGDR--STVRVMLKDWQNT----------------------------------------------DKAVHWIR 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 269 KEAISFlerhsKETFLLFFSfLHVHTPLPTT---DDFTGTSK-HGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTS 344
Cdd:cd16171 158 KEAPNL-----TQPFALYLG-LNLPHPYPSPsmgENFGSIRNiRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTS 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 345 DHGghlEARRGHAQLggwngiykggKGMGGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvI 424
Cdd:cd16171 232 DHG---ELAMEHRQF----------YKMSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--L 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 425 DGRDLMPLLQGNVRHSEHEFLFH-------YCGSYLHAVRWIPKDDSgsvWKahYVTpvfqppasggcYVTslcrcfGEQ 497
Cdd:cd16171 296 SGYSLLPLLSESSIKESPSRVPHpdwvlseFHGCNVNASTYMLRTNS---WK--YIA-----------YAD------GNS 353
|
490
....*....|....*..
gi 319996604 498 VtyhnPPLLFDLSRDPS 514
Cdd:cd16171 354 V----PPQLFDLSKDPD 366
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
29-430 |
3.00e-11 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 66.22 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 29 KPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSG--MVSSGNRRViq 106
Cdd:COG1368 234 KPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGspYKRPGQNNF-- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 107 nlavpaglplneTTLAALLKKQGYSTgligkwhqglncdsrsdQCHHPYNYGFD----YYYGMPF-TLVD-SCWPDPSRN 180
Cdd:COG1368 312 ------------PSLPSILKKQGYET-----------------SFFHGGDGSFWnrdsFYKNLGFdEFYDrEDFDDPFDG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 181 telafesqlwlcvqlvaiailtltfgklsGWVsvpwllifsmilfifllgyawfsshtsplYWDcllmrgheiteqpmka 260
Cdd:COG1368 363 -----------------------------GWG-----------------------------VSD---------------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 261 eragSIMVKEAISFLERHSKETFLLFFSfLHVHTPLPTTDDF-----TGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLR 335
Cdd:COG1368 369 ----EDLFDKALEELEKLKKPFFAFLIT-LSNHGPYTLPEEDkkipdYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWY 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 336 NNTLVYFTSDHGGHLEARRghaqlggwngiykggkGMGGWEGGIRVPGIVrWPGKVPAGRLIKEPTSLMDILPTVASVSG 415
Cdd:COG1368 444 DNTIFVIYGDHGPRSPGKT----------------DYENPLERYRVPLLI-YSPGLKKPKVIDTVGSQIDIAPTLLDLLG 506
|
410
....*....|....*
gi 319996604 416 GSLPQDRVIdGRDLM 430
Cdd:COG1368 507 IDYPSYYAF-GRDLL 520
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
234-409 |
3.47e-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: 62.62 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 234 FSSH--TSPLYWDCLLmrgHEITEQPMKAERAG----SIMVKEAISFLERHSKETflLFFSFL---HVHT---------- 294
Cdd:COG3083 330 FSSAgfNSPLFRQTIF---SDVSLPRLHTPGGPaqrdRQITAQWLQWLDQRDSDR--PWFSYLfldAPHAysfpadypkp 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 295 --------PLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGHL----EARRGHAqlGGW 362
Cdd:COG3083 405 fqpsedcnYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnengQNYWGHN--SNF 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 319996604 363 NGIYkggkgmggweggIRVPGIVRWPGKVPagRLIKEPTSLMDILPT 409
Cdd:COG3083 483 SRYQ------------LQVPLVIHWPGTPP--QVISKLTSHLDIVPT 515
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
1-347 |
3.44e-09 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 58.99 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 1 MRPRRPLVFMSLVCALLNTCQAHRvhddkpNIVLIMVDDLGIGDLgcygnDTMRTPHIDRLAREGVRLTQHISAA-SLCS 79
Cdd:COG1524 1 MKRGLSLLLASLLAAAAAAAPPAK------KVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 80 PSRSAFLTGRYPIRSGMVSSG-----NRRVIQNLAVPAGLP-----LNETTLAALLKKQGYSTGLIGKWHQGlncDSRSD 149
Cdd:COG1524 70 PAHTTLLTGLYPGEHGIVGNGwydpeLGRVVNSLSWVEDGFgsnslLPVPTIFERARAAGLTTAAVFWPSFE---GSGLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 150 QCHHPYNY-GFDYYYGMPFTlvDscwpdpsrntelafesqlwlcVQLVAIAILTLTfgklsgwvsvpwllifsmilfifl 228
Cdd:COG1524 147 DAARPYPYdGRKPLLGNPAA--D---------------------RWIAAAALELLR------------------------ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 229 lgyawfsshtsplywdcllmrgheiTEQPmkaeragsimvkeaisflerhsketfllffSFLHVHtpLPTTDDfTGtSKH 308
Cdd:COG1524 180 -------------------------EGRP------------------------------DLLLVY--LPDLDY-AG-HRY 200
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 319996604 309 GLYGDN----VEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHG 347
Cdd:COG1524 201 GPDSPEyraaLREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
30-415 |
1.08e-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: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 30 PNIVLIMVDdlGIGD--LGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRS--AFLTGRYPIRSGMVSsgNRRVI 105
Cdd:cd16015 1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGS--YTLYK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 106 QNLAvpaglplneTTLAALLKKQGYSTGLIgkwhqglncdsrsdqchHPY------------NYGFDYYYGMpftlvdSC 173
Cdd:cd16015 77 LNPL---------PSLPSILKEQGYETIFI-----------------HGGdasfynrdsvypNLGFDEFYDL------ED 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 174 WPDPSRNTelafesqlwlcvqlvaiailtltfgklSGWvsvpwllifsmilfifllgyawfsshtspLYWDcllmrghei 253
Cdd:cd16015 125 FPDDEKET---------------------------NGW-----------------------------GVSD--------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 254 teqpmkaeragSIMVKEAISFLERHSKETFLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDN--------VEEMDSMVGKI 325
Cdd:cd16015 140 -----------ESLFDQALEELEELKKKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTelenylnaIHYTDKALGEF 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 326 LDAIDDFGLRNNTLVYFTSDHGGHLEarrghaqlggwngiYKGGKGMGGWEGGIRVPGIVRWPGKVPAGRlIKEPTSLMD 405
Cdd:cd16015 209 IEKLKKSGLYENTIIVIYGDHLPSLG--------------SDYDETDEDPLDLYRTPLLIYSPGLKKPKK-IDRVGSQID 273
|
410
....*....|
gi 319996604 406 ILPTVASVSG 415
Cdd:cd16015 274 IAPTLLDLLG 283
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
33-347 |
1.50e-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: 44.33 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 33 VLIMVDDLGIGDLgcygNDTMRTPHIDRLAREGVRLTQHISAA-SLCSPSRSAFLTGRYPIRSGMVssGNR--------- 102
Cdd:pfam01663 2 LVISLDGFRADYL----DRFELTPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIV--GNTfydpktgey 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 103 --RVIQNLAVPAglPLNETTLAALLKKQGYSTGLIGkWhqglncdSRSDQCHHPYNYGFDYYYGMPFtlvdscwpdpsrN 180
Cdd:pfam01663 76 lvFVISDPEDPR--WWQGEPIWDTAAKAGVRAAALF-W-------PGSEVDYSTYYGTPPRYLKDDY------------N 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 181 TELAFEsqlwlcvqlvaiailtltfGKLSGWVSVPWLlifsmilfifllgyawfsshtsplywdcllmrgheiteqpmka 260
Cdd:pfam01663 134 NSVPFE-------------------DRVDTAVLQTWL------------------------------------------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 261 eragsimvkeAISFLERHSKETFLLFFSFLHVhtplpttdDFTGtSKHGLYGDNVEEM----DSMVGKILDAIDDFGLRN 336
Cdd:pfam01663 152 ----------DLPFADVAAERPDLLLVYLEEP--------DYAG-HRYGPDSPEVEDAlrrvDRAIGDLLEALDERGLFE 212
|
330
....*....|.
gi 319996604 337 NTLVYFTSDHG 347
Cdd:pfam01663 213 DTNVIVVSDHG 223
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
274-353 |
3.12e-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: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319996604 274 FLERHSKETFllfFSFLHVHTPlpTTDDFTGTSKhglygdnveeMDSMVGKILDAIDDFGLRNNTLVYFTSDHG------ 347
Cdd:pfam02995 284 FLPRYRDSPF---FGFFWSNSL--SHDDFNYASA----------LDEDFLKYLKKLHKRGLLDNTIVIFMSDHGlrfgkl 348
|
90
....*....|.
gi 319996604 348 -----GHLEAR 353
Cdd:pfam02995 349 rrtsqGMLEER 359
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
287-347 |
2.25e-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: 2.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319996604 287 FSFLHVHTPlpttdDFTGtskHGlYGDN-------VEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHG 347
Cdd:cd16018 159 LILLYFEEP-----DSAG---HK-YGPDspevneaLKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG 217
|
|
| |
