|
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: 762.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 29 KPNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVVHNL 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 109 AVPAGLPLNETTFAALLKKQGYSTGLIGKWHQGLNCDSRSDHCHHPYNYGFDYYYGMPFTLVDSCWPDPSRNTELTFESQ 188
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 189 LWLCVQLVAIAVLTLTFGKLSGWVSVplLLIFSMILFIFLLGYAWFSSYTSPLYWDCLLMRGHEITEQPMKAERAGSIMV 268
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLYLGAVSK--RFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 269 KEAISFLERHRKEPFLLFFSFLHVHIPLPTTDDFIGTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGG 348
Cdd:cd16159 239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 349 HLEARRGHAQLGGWNGIYKGGKGMGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRD 428
Cdd:cd16159 319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 429 LMPLLQGNARHSEHEFLFHYCGSQLHAVRWIPKdDSGAVWKAHYVTPVFQpPEAGGCYVTSLCRCFGEQVTYHNPPLLFD 508
Cdd:cd16159 399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPR-DGGAVWKAHYFTPNFY-PGTEGCCGTLLCRCFGDSVTHHDPPLLFD 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2309511980 509 LSRDPSESTPLTPATEPlHDFVIKKVADALKEHRETIMPVTYQLS 553
Cdd:cd16159 477 LSADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
29-520 |
7.02e-154 |
|
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: 447.40 E-value: 7.02e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 29 KPNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSsgnrrVVHNL 108
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPG-----VVGPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 109 AVPAGLPLNETTFAALLKKQGYSTGLIGKWHQGlncdsrsDH-CHHPYNYGFDYYYGMPFTlvDSCWPDPSRNTEltfes 187
Cdd:cd16026 76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYS--NDMWPFPLYRND----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 188 qlwlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssytsPLYWDCLLMRGHEITEQPMKAERAGSIM 267
Cdd:cd16026 142 ----------------------------------------------------PPGPLPPLMENEEVIEQPADQSSLTQRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 268 VKEAISFLERHRKEPFLLFFSFLHVHIPLPTTDDFIGTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHG 347
Cdd:cd16026 170 TDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 348 GHLE--ARRGHAQL----------GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSG 415
Cdd:cd16026 250 PWLEygGHGGSAGPlrggkgttweGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 416 GSLPQDRVIDGRDLMPLLQGNARHSEHEFLFHYCGSQLHAVRWIPkddsgavWKAHYVTPVFQPPEAGGCYVTSlcrcfg 495
Cdd:cd16026 313 APLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR-------WKLHLPTTYRTGTDPGGLDPTK------ 379
|
490 500
....*....|....*....|....*
gi 2309511980 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 |
5.88e-124 |
|
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: 372.53 E-value: 5.88e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 29 KPNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVssGNRRVVHNL 108
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--GGTRVFLPW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 109 AVpAGLPLNETTFAALLKKQGYSTGLIGKWHQGLNCDSRSDHCHHPYNYGFDYY-YGMPFTLVdscwpdpsrnteltfes 187
Cdd:cd16160 79 DI-GGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFDFVgTNLPFTNS----------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 188 qlWLCVQlvaiavltltfgklsgwvsvplllifsmilfifllgyaWFSSYTSPLYWDCLLMRGHEITEQPMKAERAGSIM 267
Cdd:cd16160 141 --WACDD--------------------------------------TGRHVDFPDRSACFLYYNDTIVEQPIQHEHLTETL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 268 VKEAISFLERHRKEPFLLFFSFLHVHIPLPTTDDFIGTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHG 347
Cdd:cd16160 181 VGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 348 GHLEA----------RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPaGRLIKEPTSLMDILPTVASVSG 415
Cdd:cd16160 261 PHVEYcleggstgglKGGKGNSweGG-----------------IRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTFVDLAG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 416 GSLPQDRVIDGRDLMPLLQGNARHSEHEFLFHYCgSQLHAVRWIPkddsgavWKAHYVTPVFQPPEA------GGCYVTS 489
Cdd:cd16160 323 GTLPTDRIYDGLSITDLLLGEADSPHDDILYYCC-SRLMAVRYGS-------YKIHFKTQPLPSQESldpncdGGGPLSD 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2309511980 490 --LCR-CFGEQVTYHNPPLLFDLSRDPSESTPLTPAtepLHDFVIKKVADALKE 540
Cdd:cd16160 395 yiVCYdCEDECVTKHNPPLIFDVEKDPGEQYPLQPS---VYEHMLEAVEKLIAH 445
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
29-520 |
3.18e-98 |
|
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: 304.39 E-value: 3.18e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 29 KPNIVLIMVDDLGIGDLGCYGNDT-IRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVVHN 107
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNaILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNG--------VGHN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 108 LAVPA--GLPLNETTFAALLKKQGYSTGLIGKWHQGLNcdsrsdHCHHPYNYGFDYYYGMPFtlvdscwpdpSRNTELTF 185
Cdd:cd16161 73 FLPTSvgGLPLNETTLAEVLRQAGYATGMIGKWHLGQR------EAYLPNSRGFDYYFGIPF----------SHDSSLAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 186 EsqlwlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgYAWFssytsplywdcllmrgheiteqpmkaerags 265
Cdd:cd16161 137 R--------------------------------------------YAQF------------------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 266 imvkeAISFLERH--RKEPFLLFFSFLHVHIPLPTTDDF-IGTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYF 342
Cdd:cd16161 142 -----ATDFIQRAsaKDRPFFLYAALAHVHVPLANLPRFqSPTSGRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWF 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 343 TSDHGGHLEARRGHAQLGGWNGIYKGGKGMGGWEG---GIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLP 419
Cdd:cd16161 217 TSDNGPWEVKCELAVGPGTGDWQGNLGGSVAKASTwegGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 420 QDRVIDGRDLMPLLQGNARhSEHEFLFHYCGS-----QLHAVRWIPkddsgavWKAHYVTpvfqppeaGGCYVTslCRCF 494
Cdd:cd16161 297 PGRIYDGKDLSPVLFGGSK-TGHRCLFHPNSGaagagALSAVRCGD-------YKAHYAT--------GGALAC--CGST 358
|
490 500
....*....|....*....|....*.
gi 2309511980 495 GEQVtYHNPPLLFDLSRDPSESTPLT 520
Cdd:cd16161 359 GPKL-YHDPPLLFDLEVDPAESFPLT 383
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-544 |
8.66e-98 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 303.34 E-value: 8.66e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 1 MRpRSPLVFMSLVCTFLNTCQAhrvhdDKPNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSP 80
Cdd:COG3119 1 MK-RLLLLLLALLAAAAAAAAA-----KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 81 SRSAFLTGRYPIRSGMVSsgnrrvvHNLAVPAGLPLNETTFAALLKKQGYSTGLIGKWHqglncdsrsdhchhpynygfd 160
Cdd:COG3119 75 SRASLLTGRYPHRTGVTD-------NGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWH--------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 161 yyygmpftlvdscwpdpsrnteltfesqlwlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssytsp 240
Cdd:COG3119 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 241 LYWDcllmrgHEITEqpmkaeragsimvkEAISFLERHRK--EPFLLFFSFLHVHIPLPTTDDFIG-------------- 304
Cdd:COG3119 127 LYLT------DLLTD--------------KAIDFLERQADkdKPFFLYLAFNAPHAPYQAPEEYLDkydgkdiplppnla 186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 305 ---------TSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEA---RRGHAQL--GGwngiykggk 370
Cdd:COG3119 187 prdlteeelRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEhglRGGKGTLyeGG--------- 257
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 371 gmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNARHSEHEFLFHY-C 449
Cdd:COG3119 258 --------IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYpR 327
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 450 GSQLHAVRwipKDDsgavWKAHYVTPVFQPPEaggcyvtslcrcfgeqvtyhnpplLFDLSRDPSESTPL---TPAtepl 526
Cdd:COG3119 328 GGGNRAIR---TGR----WKLIRYYDDDGPWE------------------------LYDLKNDPGETNNLaadYPE---- 372
|
570
....*....|....*...
gi 2309511980 527 hdfVIKKVADALKEHRET 544
Cdd:COG3119 373 ---VVAELRALLEAWLKE 387
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-517 |
2.60e-97 |
|
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: 302.93 E-value: 2.60e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGM--VSSGNRRVVHN 107
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 108 LAVPA-----GLPLNETTFAALLKKQGYSTGLIGKWHQGLNcdsrsdHCHHPYNYGFDYYYGmpftlvDSCWPDPSRnte 182
Cdd:cd16144 81 TKLIPppsttRLPLEEVTIAEALKDAGYATAHFGKWHLGGE------GGYGPEDQGFDVNIG------GTGNGGPPS--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 183 ltfesqlwlcvqlvaiavltltfgklsgwvsvplllifsmilfifllGYAWFSSYTSPLYwdcllmrghEITEQPMKAER 262
Cdd:cd16144 146 -----------------------------------------------YYFPPGKPNPDLE---------DGPEGEYLTDR 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 263 agsiMVKEAISFLERHRKEPFLLFFSFLHVHIPLPTTDDFI-----------GTSKHGLYGDNVEEMDSMMGKILDAIDD 331
Cdd:cd16144 170 ----LTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELIekyekkkkglrKGQKNPVYAAMIESLDESVGRILDALEE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 332 FGLRNNTIVYFTSDHGGHLEA----------RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKE 399
Cdd:cd16144 246 LGLADNTLVIFTSDNGGLSTRggpptsnaplRGGKGSLyeGG-----------------IRVPLIVRWPGVIKPGSVSDV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 400 PTSLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNARHSEHEFLF----HYCGSQLHAVRWIPKDDsgavWKAHYvtp 475
Cdd:cd16144 309 PVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFwhfpHYHGQGGRPASAIRKGD----WKLIE--- 381
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2309511980 476 vfqppeaggcyvtslcrcFGEQVTYHnpplLFDLSRDPSEST 517
Cdd:cd16144 382 ------------------FYEDGRVE----LYNLKNDIGETN 401
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-520 |
5.74e-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: 293761 [Multi-domain] Cd Length: 372 Bit Score: 297.91 E-value: 5.74e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIR---TPHIDRLAREGVRLTQHISAASlCSPSRSAFLTGRYPIRSGMVSSGnrrvvh 106
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVG------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 107 nLA-VPAGLPLNETTFAALLKKQGYSTGLIGKWHQGlncdsrsDHCHH-PYNYGFDYYYGMPFTLVDScwpdpsrntelt 184
Cdd:cd16142 74 -LPgSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG-------DEDGRlPTDHGFDEFYGNLYHTIDE------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 185 fesqlwlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssytsplywdcllmrghEITEQpmkaerag 264
Cdd:cd16142 134 -------------------------------------------------------------------EIVDK-------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 265 simvkeAISFLERHRK--EPFLLFFSFLHVHIPLPTTDDFIGTSK-HGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVY 341
Cdd:cd16142 139 ------AIDFIKRNAKadKPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVI 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 342 FTSDHGGHLEA--------RRGH---AQLGGWngiykggkgmggweggiRVPGIVRWPGKVPAGRLIKEPTSLMDILPTV 410
Cdd:cd16142 213 FTTDNGPEQDVwpdggytpFRGEkgtTWEGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTL 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 411 ASVSGGSLP------QDRVIDGRDLMPLLQGNARHSEHEFLFHYCGSQLHAVRWipKDdsgavWKAHYVTpvfQPPEAGG 484
Cdd:cd16142 276 AALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRW--KN-----WKVHFKA---QEDTGGP 345
|
490 500 510
....*....|....*....|....*....|....*.
gi 2309511980 485 CYVTSlcrcfgEQVTYhnpPLLFDLSRDPSESTPLT 520
Cdd:cd16142 346 TGEPF------YVLTF---PLIFNLRRDPKERYDVT 372
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-517 |
3.28e-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: 293762 [Multi-domain] Cd Length: 395 Bit Score: 296.80 E-value: 3.28e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDT-IRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgNRRVVHNL 108
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSkIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSR-----LKGGVLGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 109 AVPAGLPLNETTFAALLKKQGYSTGLIGKWHQGLN---CDSRSDHCHH-------------PYNYGFDYYYGMPftlvds 172
Cdd:cd16143 76 FSPPLIEPDRVTLAKMLKQAGYRTAMVGKWHLGLDwkkKDGKKAATGTgkdvdyskpikggPLDHGFDYYFGIP------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 173 cwpdpsrnteltfesqlwlcvqlvAIAVLTLTFGKlsgwvsvplllifsmilfifllgyawfssytsplywdcllmrghe 252
Cdd:cd16143 150 ------------------------ASEVLPTLTDK--------------------------------------------- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 253 iteqpmkaeragsimvkeAISFLERHRK--EPFLLFFSFLHVHIPLPTTDDFIGTSKHGLYGDNVEEMDSMMGKILDAID 330
Cdd:cd16143 161 ------------------AVEFIDQHAKkdKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALK 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 331 DFGLRNNTIVYFTSDHGGHLEARRGHAQL------------------GGwngiykggkgmggweggIRVPGIVRWPGKVP 392
Cdd:cd16143 223 ELGLAENTLVIFTSDNGPSPYADYKELEKfghdpsgplrgmkadiyeGG-----------------HRVPFIVRWPGKIP 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 393 AGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNARHSEHEFLFHYCGSQLHAVR---W--IPKDDSGaV 467
Cdd:cd16143 286 AGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGSFAIRkgdWklIDGTGSG-G 364
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2309511980 468 WKAHYVTPVFQPPeaggcyvtslcrcfgeqvtyhnPPLLFDLSRDPSEST 517
Cdd:cd16143 365 FSYPRGKEKLGLP----------------------PGQLYNLSTDPGESN 392
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
29-574 |
2.18e-92 |
|
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.
Pssm-ID: 293777 [Multi-domain] Cd Length: 479 Bit Score: 292.43 E-value: 2.18e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 29 KPNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMV-------SSGn 101
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYpgvfypgSRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 102 rrvvhnlavpaGLPLNETTFAALLKKQGYSTGLIGKWHQGLNCDSRsdhcHHPYNYGFDYYYGMPFTLvDSCwpdPsrnt 181
Cdd:cd16158 80 -----------GLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSH-DQG---P---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 182 eltfesqlwlCVQLVAIAVLTLTFGKL-SGWVSVPLLLifsmilfifllgyawfssytsplywdcllmrGHEITEQPMKA 260
Cdd:cd16158 137 ----------CQNLTCFPPNIPCFGGCdQGEVPCPLFY-------------------------------NESIVQQPVDL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 261 ERAGSIMVKEAISFLERHRKE--PFLLFFSFLHVHIPLPTTDDFIGTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNT 338
Cdd:cd16158 176 LTLEERYAKFAKDFIADNAKEgkPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 339 IVYFTSDHGGHL--EARRGHAQL----------GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIkEPTSLMDI 406
Cdd:cd16158 256 LVFFTSDNGPSTmrKSRGGNAGLlkcgkgttyeGG-----------------VREPAIAYWPGRIKPGVTH-ELASTLDI 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 407 LPTVASVSGGSLPqDRVIDGRDLMPLLQGNARHSEHEFLFHYCGSQ----LHAVRWipkddsgAVWKAHYVT---PVFQP 479
Cdd:cd16158 318 LPTIAKLAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDpdkgVFAVRW-------GKYKAHFYTqgaAHSGT 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 480 PEAGGCYVTSLcrcfgeqVTYHNPPLLFDLSRDPSESTPLTPATEplHDFVIKKVaDALKEHRETIMpvTYQLSELNQGR 559
Cdd:cd16158 390 TPDKDCHPSAE-------LTSHDPPLLFDLSQDPSENYNLLGLPE--YNQVLKQI-QQVKERFEASM--KFGESEINKGE 457
|
570 580
....*....|....*....|.
gi 2309511980 560 -MWLKPCC--GVFPF---CLC 574
Cdd:cd16158 458 dPALEPCCkpGCTPKpscCQC 478
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-517 |
2.87e-87 |
|
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: 276.78 E-value: 2.87e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYpirsgmvsSGNRRVVHNLA 109
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLH--------TGHTRVRGNSE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 110 VPAGLPL--NETTFAALLKKQGYSTGLIGKWhqGLNCDSRSDhchHPYNYGFDYYYGmpftlvdscwpdpsrnteltfes 187
Cdd:cd16145 73 PGGQDPLppDDVTLAEVLKKAGYATAAFGKW--GLGGPGTPG---HPTKQGFDYFYG----------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 188 qlWLCvQLVAiavltLTFgklsgwvsvpllliFSMILfifllgyaWFSSYTSPLYWDCLLMRGHEITEQPMKAERAGSIM 267
Cdd:cd16145 125 --YLD-QVHA-----HNY--------------YPEYL--------WRNGEKVPLPNNVIPPLDEGNNAGGGGGTYSHDLF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 268 VKEAISFLERHRKEPFLLFFSFL--HVHIPLPTTD-DFIGTSKHGLYGDN------------VEEMDSMMGKILDAIDDF 332
Cdd:cd16145 175 TDEALDFIRENKDKPFFLYLAYTlpHAPLQVPDDGpYKYKPKDPGIYAYLpwpqpekayaamVTRLDRDVGRILALLKEL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 333 GLRNNTIVYFTSDHGGHLEARRGHAQL-----------------GGwngiykggkgmggweggIRVPGIVRWPGKVPAGR 395
Cdd:cd16145 255 GIDENTLVVFTSDNGPHSEGGSEHDPDffdsngplrgykrslyeGG-----------------IRVPFIARWPGKIPAGS 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 396 LIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNARHSEHEFL---FHYCGSQlHAVRWipkDDsgavWKAhy 472
Cdd:cd16145 318 VSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLyweFYEGGGA-QAVRM---GG----WKA-- 385
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2309511980 473 vtpVFQPPEAGgcyvtslcrcfgeqvtyhnPPLLFDLSRDPSEST 517
Cdd:cd16145 386 ---VRHGKKDG-------------------PFELYDLSTDPGETN 408
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
29-560 |
7.45e-87 |
|
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: 277.43 E-value: 7.45e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 29 KPNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRrvVHNL 108
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAH--ARNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 109 AVP----AGLPLNETTFAALLKKQGYSTGLIGKWHQGlncdSRSDHchHPYNYGFDYYYGMPftlvdSCWPDPSRNTELt 184
Cdd:cd16157 79 YTPqnivGGIPDSEILLPELLKKAGYRNKIVGKWHLG----HRPQY--HPLKHGFDEWFGAP-----NCHFGPYDNKAY- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 185 fesqlwlcvqlvaiavltltfgklsgwvsvPLLlifsmilfifllgyawfssytsPLYWDCLlMRGHEITEQPMKAERAG 264
Cdd:cd16157 147 ------------------------------PNI----------------------PVYRDWE-MIGRYYEEFKIDKKTGE 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 265 S----IMVKEAISFLERHR--KEPFLLFFSFLHVHIPLPTTDDFIGTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNT 338
Cdd:cd16157 174 SnltqIYLQEALEFIEKQHdaQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 339 IVYFTSDHGGhleARRGHAQLGGWNgIYKGGKGMGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSL 418
Cdd:cd16157 254 FVFFSSDNGA---ALISAPEQGGSN-GPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 419 PQDRVIDGRDLMPLLQGNarHSEHEFLFHYCGSQLHAVRWipkddsgAVWKAHYVTpvFQPPEAGGCYVTSLCRcfGEQ- 497
Cdd:cd16157 330 PSDRAIDGIDLLPVLLNG--KEKDRPIFYYRGDELMAVRL-------GQYKAHFWT--WSNSWEEFRKGINFCP--GQNv 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2309511980 498 --VTYHN------PPLLFDLSRDPSESTPLTPATePLHDFVIKKVADALKEHRETIMPVTYQLSELNQGRM 560
Cdd:cd16157 397 pgVTTHNqtdhtkLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLNVCDLAVM 466
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
30-428 |
5.42e-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: 251.59 E-value: 5.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVVHNLA 109
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 110 VPAGLPLNETTFAALLKKQGYSTGLIGKWHQglncdsrsdhchhpynygfdyyygmpftlvdscwpdpsrnteltfesql 189
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWHD------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 190 wlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaeragsimvk 269
Cdd:cd16022 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 270 EAISFLERHRKE-PFLLFFSFLHVHIPLpttddfigtskhgLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGG 348
Cdd:cd16022 104 EAIDFIERRDKDkPFFLYVSFNAPHPPF-------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 349 HLEA---RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrv 423
Cdd:cd16022 171 MLGDhglRGKKGSLyeGG-----------------IRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG-- 231
|
....*
gi 2309511980 424 IDGRD 428
Cdd:cd16022 232 LDGRS 236
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
30-517 |
4.98e-75 |
|
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293765 [Multi-domain] Cd Length: 409 Bit Score: 244.77 E-value: 4.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQ-HISaaSLCSPSRSAFLTGRYPIRSGMVSSGNRRvvHNL 108
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGR--ERM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 109 AvpaglpLNETTFAALLKKQGYSTGLIGKWHQGLNcdsrsdHCHHPYNYGFDYYYGmpftlvdscwpdpsrnteltfesq 188
Cdd:cd16146 77 R------LDETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLG------------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 189 lwlcvqlvaiavltltFGklSGWVSVPlllifsmilfifllGYAWFSSYTSPLYWdcllmrgHEITEQPMKaeraG---S 265
Cdd:cd16146 121 ----------------HG--GGGIGQY--------------PDYWGNDYFDDTYY-------HNGKFVKTE----GyctD 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 266 IMVKEAISFLERHRKEPFLLFFSFLHVHIPL--PT--TDDFIGTSKH----GLYGdNVEEMDSMMGKILDAIDDFGLRNN 337
Cdd:cd16146 158 VFFDEAIDFIEENKDKPFFAYLATNAPHGPLqvPDkyLDPYKDMGLDdklaAFYG-MIENIDDNVGRLLAKLKELGLEEN 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 338 TIVYFTSDHG----------GHLEARRGHAQLGGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDIL 407
Cdd:cd16146 237 TIVIFMSDNGpaggvpkrfnAGMRGKKGSVYEGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDLL 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 408 PTVASVSGGSLPQDRVIDGRDLMPLLQGNARHSEHEFLFhycgsqLHAVRWIPKDDS---GAVWKAHY--VTPVFQPPEa 482
Cdd:cd16146 300 PTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLF------THSGRWPPPPKKkrnAAVRTGRWrlVSPKGFQPE- 372
|
490 500 510
....*....|....*....|....*....|....*
gi 2309511980 483 ggcyvtslcrcfgeqvtyhnpplLFDLSRDPSEST 517
Cdd:cd16146 373 -----------------------LYDIENDPGEEN 384
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-519 |
1.31e-71 |
|
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: 234.80 E-value: 1.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTqHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVVHNLA 109
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNY--------VVFGYL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 110 VPaglplNETTFAALLKKQGYSTGLIGKWHQGLNCDSRSdhchHPYNYGFDYYYgmpftlvdscwpdpsrnteltfesqL 189
Cdd:cd16151 72 DP-----KQKTFGHLLKDAGYATAIAGKWQLGGGRGDGD----YPHEFGFDEYC-------------------------L 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 190 WlcvqlvaiavlTLTFGKLSGWvsvplllifSMILFIFLLGYAWFSSYTSPLYwdcllmrgheiteqpmkaeraGS-IMV 268
Cdd:cd16151 118 W-----------QLTETGEKYS---------RPATPTFNIRNGKLLETTEGDY---------------------GPdLFA 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 269 KEAISFLERHRKEPFLLFFSFLHVHIPLPTT------DDFIGTSKH--GLYGDNVEEMDSMMGKILDAIDDFGLRNNTIV 340
Cdd:cd16151 157 DFLIDFIERNKDQPFFAYYPMVLVHDPFVPTpdspdwDPDDKRKKDdpEYFPDMVAYMDKLVGKLVDKLEELGLRENTII 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 341 YFTSDHGGHLEARR-----------GHAQLGGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPT 409
Cdd:cd16151 237 IFTGDNGTHRPITSrtngrevrggkGKTTDAG-----------------THVPLIVNWPGLIPAGGVSDDLVDFSDFLPT 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 410 VASVSGGSLPQDRVIDGRDLMPLLQGNARHSEHEFLFHYcgsqlhAVRWIPKDDSGAVWKAHYvtpvfqppeaggcyvts 489
Cdd:cd16151 300 LAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWY------YRNPHKKFGSRFVRTKRY----------------- 356
|
490 500 510
....*....|....*....|....*....|
gi 2309511980 490 lcrcfgeqvTYHNPPLLFDLSRDPSESTPL 519
Cdd:cd16151 357 ---------KLYADGRFFDLREDPLEKNPL 377
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-519 |
8.18e-67 |
|
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: 222.83 E-value: 8.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 29 KPNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRrvvhnl 108
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 109 avpagLPLNETTFAALLKKQGYSTGLIGKWH----QGLNCDSRSDHCHHPYNYGFDYYYGMpftlvdSCWPDpsrntelt 184
Cdd:cd16034 75 -----LPPDAPTIADVLKDAGYRTGYIGKWHldgpERNDGRADDYTPPPERRHGFDYWKGY------ECNHD-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 185 fesqlwlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssYTSPLYWDcllmrgheiTEQPMKAERAG 264
Cdd:cd16034 136 ----------------------------------------------------HNNPHYYD---------DDGKRIYIKGY 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 265 S--IMVKEAISFLERHRKE--PFLLFFS------------------FLHVHIPLPTTDDFIGTSKHGL-------YGdNV 315
Cdd:cd16034 155 SpdAETDLAIEYLENQADKdkPFALVLSwnpphdpyttapeeyldmYDPKKLLLRPNVPEDKKEEAGLredlrgyYA-MI 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 316 EEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEArrgHAQLG---GWNgiykggkgmggweGGIRVPGIVRWPGKVP 392
Cdd:cd16034 234 TALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGS---HGLMNkqvPYE-------------ESIRVPFIIRYPGKIK 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 393 AGRLIKEPTSLMDILPTVASVSGgsLPQDRVIDGRDLMPLLQGNARHSEHEFLFhYCGSQLHAVRWIPKDDSGAVWKAHY 472
Cdd:cd16034 298 AGRVVDLLINTVDIMPTLLGLCG--LPIPDTVEGRDLSPLLLGGKDDEPDSVLL-QCFVPFGGGSARDGGEWRGVRTDRY 374
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2309511980 473 vtpvfqppeaggcyvtSLCRCFGeqvtyhNPPLLFDLSRDPSESTPL 519
Cdd:cd16034 375 ----------------TYVRDKN------GPWLLFDNEKDPYQLNNL 399
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
30-519 |
9.33e-65 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 217.03 E-value: 9.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASlCSPSRSAFLTGRYPIRSGMvssgNRRVVHNlA 109
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGM----QHGVILA-G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 110 VPAGLPLNETTFAALLKKQGYSTGLIGKWHQGlncdsrsdHCHHPY---NYGFDYYYGmpftlvdscwpdpsrnteltfe 186
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWEYtptNRGFDSFYG---------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 187 sqlwlcvqlvaiavltltfgklsgwvsvplllifsmilfiFLLGYAWFSSYTSPLYWDC--LLMRGHEITEQPMKAERAG 264
Cdd:cd16029 125 ----------------------------------------YYGGAEDYYTHTSGGANDYgnDDLRDNEEPAWDYNGTYST 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 265 SIMVKEAISFLERHRK-EPFLLFFSFLHVHIPLPT----TDDFIGTSKHGLYGD------NVEEMDSMMGKILDAIDDFG 333
Cdd:cd16029 165 DLFTDRAVDIIENHDPsKPLFLYLAFQAVHAPLQVppeyADPYEDKFAHIKDEDrrtyaaMVSALDESVGNVVDALKAKG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 334 LRNNTIVYFTSDHGGHLEA---------RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPG-KVPAGRLIKEPT 401
Cdd:cd16029 245 MLDNTLIVFTSDNGGPTGGgdggsnyplRGGKNTLweGG-----------------VRVPAFVWSPLlPPKRGTVSDGLM 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 402 SLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNARHSEHEFL----FHYCGSQLHAVRWipKDdsgavWKahYVTpvf 477
Cdd:cd16029 308 HVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILlnidDITRTTGGAAIRV--GD-----WK--LIV--- 375
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2309511980 478 qppeaggcyvtslcrcfGEQvtyhnpplLFDLSRDPSESTPL 519
Cdd:cd16029 376 -----------------GKP--------LFNIENDPCERNDL 392
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
30-543 |
1.42e-63 |
|
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.
Pssm-ID: 293751 [Multi-domain] Cd Length: 373 Bit Score: 213.52 E-value: 1.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIgDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMvsSGNRRvvHNLA 109
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA--HGLRS--RGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 110 VPAGLPlnetTFAALLKKQGYSTGLIGKWHQGlncdsrsdhchHPYNYGFDYYYGMPFTLVDSCWPDPSRnteltfesql 189
Cdd:cd16027 76 LPDGVK----TLPELLREAGYYTGLIGKTHYN-----------PDAVFPFDDEMRGPDDGGRNAWDYASN---------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 190 wlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaeragsimvk 269
Cdd:cd16027 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 270 eAISFLERHRKE-PFLLFFSFLHVHIPLPTTDDFIGTSK-------------------HGLYGDNVEEMDSMMGKILDAI 329
Cdd:cd16027 131 -AADFLNRAKKGqPFFLWFGFHDPHRPYPPGDGEEPGYDpekvkvppylpdtpevredLADYYDEIERLDQQVGEILDEL 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 330 DDFGLRNNTIVYFTSDHGGHLEarRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDIL 407
Cdd:cd16027 210 EEDGLLDNTIVIFTSDHGMPFP--RAKGTLydSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLA 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 408 PTVASVSGGSLPQDrvIDGRDLMPLLQGNARHsEHEFLF---HYCGSQLHAVRWIPKDDsgavWKahYVtpvfqppeagg 484
Cdd:cd16027 271 PTLLDLAGIEPPEY--LQGRSFLPLLKGEKDP-GRDYVFaerDRHDETYDPIRSVRTGR----YK--YI----------- 330
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2309511980 485 cyvtslcRCFgeqvtyhNPPLLFDLSRDPSESTPLtpATEPLHDFVIKKVADALKEHRE 543
Cdd:cd16027 331 -------RNY-------MPEELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
30-415 |
3.01e-59 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 199.57 E-value: 3.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSgnrrvvhnla 109
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 110 VPAGLPLNETTFAALLKKQGYSTGLIGKWHQGLNcdSRSDhchhPYNYGFDYYYGmpftlvdscwpdpsrnteltfesql 189
Cdd:pfam00884 71 TPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWY--NNQS----PCNLGFDKFFG------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 190 wlcvqlvaiavltltfgklsgwvsvplllifsmilfiFLLGYAWFS-SYTSPLYWDcllmrGHEITEQpmkaeragsIMV 268
Cdd:pfam00884 120 -------------------------------------RNTGSDLYAdPPDVPYNCS-----GGGVSDE---------ALL 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 269 KEAISFLERHrKEPFLLFFSFLHVHIPLPTTDDFIGTSK------------HGLYGDNVEEMDSMMGKILDAIDDFGLRN 336
Cdd:pfam00884 149 DEALEFLDNN-DKPFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLLD 227
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2309511980 337 NTIVYFTSDHGGHLEARRGHAQLGGWNgiykggkgmGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSG 415
Cdd:pfam00884 228 NTLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
28-540 |
9.22e-58 |
|
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: 199.68 E-value: 9.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 28 DKPNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGnrrvvhn 107
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNN------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 108 lavPAGLPLNETTFAALLKKQGYSTGLIGKWHQGLNCDSRSDhchhpynyGFDYYYGMPftlvdscwpdpsrnteltfes 187
Cdd:cd16031 74 ---GPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--------GFDYWVSFP--------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 188 qlwlcvqlvaiavltltfgklsgwvsvplllifsmilfifllGYAWfssytsplYWDCLLMRGHEITEQPMKAERagsIM 267
Cdd:cd16031 122 ------------------------------------------GQGS--------YYDPEFIENGKRVGQKGYVTD---II 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 268 VKEAISFLERHRKE-PFLLFFSFLHVH-----------------IPLPTT---DDFIGTSK------------------- 307
Cdd:cd16031 149 TDKALDFLKERDKDkPFCLSLSFKAPHrpftpaprhrglyedvtIPEPETfddDDYAGRPEwareqrnrirgvldgrfdt 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 308 HGLYGDNVE-------EMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLearrGHAQLGG-WNgiykggkgmgGWEGGI 379
Cdd:cd16031 229 PEKYQRYMKdylrtvtGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL----GEHGLFDkRL----------MYEESI 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 380 RVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNARHS-EHEFLFHYCGSQLHAvrW 458
Cdd:cd16031 295 RVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEYYEEPNFH--N 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 459 IPKddSGAV----WK-AHYvtpvfqppeaggcyvtslcrcfgeqvtYHNPPL--LFDLSRDPSESTPLtpATEPLHDFVI 531
Cdd:cd16031 371 VPT--HEGVrterYKyIYY---------------------------YGVWDEeeLYDLKKDPLELNNL--ANDPEYAEVL 419
|
....*....
gi 2309511980 532 KKVADALKE 540
Cdd:cd16031 420 KELRKRLEE 428
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
28-519 |
1.02e-53 |
|
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293749 [Multi-domain] Cd Length: 402 Bit Score: 188.04 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 28 DKPNIVLIMVDDLGIGDLGCYGNDtIRTPHIDRLAREGVRLTQ-HisAASLCSPSRSAFLTGRYPIRSGMvssGNrrVVH 106
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM---GT--MAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 107 NLAVPAG----LPLNETTFAALLKKQGYSTGLIGKWHQGLNcdsrsdhchhpynygfDYYYgmpftlvdscwpdpsrnTE 182
Cdd:cd16025 73 LATGKPGyegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------------DYYS-----------------TD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 183 Ltfesqlwlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaer 262
Cdd:cd16025 120 D------------------------------------------------------------------------------- 120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 263 agsiMVKEAISFLERHRKE--PFLLFFSFLHVHIPLPTTDDFIgtSKH----------------------GLYGDN---- 314
Cdd:cd16025 121 ----LTDKAIEYIDEQKAPdkPFFLYLAFGAPHAPLQAPKEWI--DKYkgkydagwdalreerlerqkelGLIPADtklt 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 315 ------------------------------VEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGhlEARRGHAQ------ 358
Cdd:cd16025 195 prppgvpawdslspeekklearrmevyaamVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGA--SAEPGWANasntpf 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 359 --------LGGwngiykggkgmggweggIRVPGIVRWP-GKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRV------ 423
Cdd:cd16025 273 rlykqashEGG-----------------IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlp 335
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 424 IDGRDLMPLLQGNARHSEHEFLFHycgsQLHAVRWIPKDDsgavWKAhyvtpvfqppeaggcyvtslcrcfgeqVTYHNP 503
Cdd:cd16025 336 LDGVSLLPTLDGAAAPSRRRTQYF----ELFGNRAIRKGG----WKA---------------------------VALHPP 380
|
570 580
....*....|....*....|..
gi 2309511980 504 PL------LFDLSRDPSESTPL 519
Cdd:cd16025 381 PGwgdqweLYDLAKDPSETHDL 402
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
440-574 |
9.86e-53 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 175.96 E-value: 9.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 440 SEHEFLFHYCGSQLHAVRWIPkddsgavWKAHYVTPVFQPPEAGGCYVTslcrcfGEQVTYHNPPLLFDLSRDPSESTPL 519
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP-------YKAHFFTPSFDPPGAEGCYGS------KVPVTHHDPPLLFDLERDPSEKYPL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2309511980 520 TPATePLHDFVIKKVADALKEHRETIMPVTYQLSELNQG-RMWLKPCCGVFPFCLC 574
Cdd:pfam14707 68 SPDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLwDPWLQPCCPTFPACTC 122
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-437 |
5.47e-50 |
|
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: 178.18 E-value: 5.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRrvvhNLA 109
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVEN----AGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 110 VPAGLPLNETTFAALLKKQGYSTGLIGKWHQGLNCDsrsdhchhPYNYGFDYYygmpftlvdscwpdpsrNTELTFESql 189
Cdd:cd16033 77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEET--------PLDYGFDEY-----------------LPVETTIE-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 190 wlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssytsplYWdcllmrgheiteqpmkaeragsiMVK 269
Cdd:cd16033 130 ----------------------------------------------------YF-----------------------LAD 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 270 EAISFLERHRK--EPFLLFFSFLHVH-----------------IPLPTT--DDFIG-------TSKH-GLYGDN------ 314
Cdd:cd16033 135 RAIEMLEELAAddKPFFLRVNFWGPHdpyippepyldmydpedIPLPESfaDDFEDkpyiyrrERKRwGVDTEDeedwke 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 315 --------VEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEARRGHAQlgGWNGIYKGGkgmggweggiRVPGIVR 386
Cdd:cd16033 215 iiahywgyITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDK--GPFMYEETY----------RIPLIIK 282
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2309511980 387 WPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNA 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 |
8.48e-48 |
|
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: 169.68 E-value: 8.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNrrvvhnlA 109
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-------E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 110 VPAGLPlnetTFAALLKKQGYSTGLIGKWH-----QglncdsrsdhcHHpynyGFDYyygmpftlvdscwpdpsrNTELT 184
Cdd:cd16032 74 FPADIP----TFAHYLRAAGYRTALSGKMHfvgpdQ-----------LH----GFDY------------------DEEVA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 185 FESQLWLcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssytsplyWDclLMRgheiteqpmkaerag 264
Cdd:cd16032 117 FKAVQKL---------------------------------------------------YD--LAR--------------- 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 265 simvkeaisfleRHRKEPFLLFFSFLHVHIPLPTTDDF----IGTSKHGLYGdNVEEMDSMMGKILDAIDDFGLRNNTIV 340
Cdd:cd16032 129 ------------GEDGRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIV 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 341 YFTSDHGGHLEARrghaqlGGWngiykggKGMGGWEGGIRVPGIVRWPGKvPAGRLIKEPTSLMDILPTVASVSGGSLPQ 420
Cdd:cd16032 196 IFTSDHGDMLGER------GLW-------YKMSFFEGSARVPLIISAPGR-FAPRRVAEPVSLVDLLPTLVDLAGGGTAP 261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 421 DRV-IDGRDLMPLLQGNARHSEHEFLFHYCGSQLHA-VRWIPKDDsgavWKahYVtpvfqppeaggcyvtslcrcfgeqV 498
Cdd:cd16032 262 HVPpLDGRSLLPLLEGGDSGGEDEVISEYLAEGAVApCVMIRRGR----WK--FI------------------------Y 311
|
490
....*....|....*
gi 2309511980 499 TYHNPPLLFDLSRDP 513
Cdd:cd16032 312 CPGDPDQLFDLEADP 326
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
29-524 |
9.69e-48 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 173.70 E-value: 9.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 29 KPNIVLIMVDDLGiGD-LGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNrrvvhn 107
Cdd:PRK13759 6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGD------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 108 lavpaGLPLN-ETTFAALLKKQGYSTGLIGK--WHQglncdSRSDHchhpynyGFDYyygmpfTLVDSCWPDPSRNTELT 184
Cdd:PRK13759 79 -----VVPWNyKNTLPQEFRDAGYYTQCIGKmhVFP-----QRNLL-------GFHN------VLLHDGYLHSGRNEDKS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 185 FESQ-----LWLCVQLVAIAVLTLTFGklsgwvsvplllifsmilfifllgyawfssytsplyWDCllmrgHEITEQPM- 258
Cdd:PRK13759 136 QFDFvsdylAWLREKAPGKDPDLTDIG------------------------------------WDC-----NSWVARPWd 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 259 KAER--AGSIMVKEAISFLERH-RKEPFLLFFSFLHVHIPL-------------PTTDDFIG------------TSKHGL 310
Cdd:PRK13759 175 LEERlhPTNWVGSESIEFLRRRdPTKPFFLKMSFARPHSPYdppkryfdmykdaDIPDPHIGdweyaedqdpegGSIDAL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 311 YGD---------------NVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDH----GGHLEARRGHAQLGGwngiykggkg 371
Cdd:PRK13759 255 RGNlgeeyarraraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHgdmlGDHYLFRKGYPYEGS---------- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 372 mggweggIRVPGIVRWPG---KVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNAR------HSEH 442
Cdd:PRK13759 325 -------AHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYEgwrpylHGEH 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 443 EflfhYCGSQLHavrWIPKDDSGAVWKAHYVTpvfqppeaggcyvtslcrcfgEQvtyhnpplLFDLSRDPSESTPLTPA 522
Cdd:PRK13759 396 A----LGYSSDN---YLTDGKWKYIWFSQTGE---------------------EQ--------LFDLKKDPHELHNLSPS 439
|
..
gi 2309511980 523 TE 524
Cdd:PRK13759 440 EK 441
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
28-467 |
1.91e-46 |
|
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: 169.29 E-value: 1.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 28 DKPNIVLIMVDDLGiGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSG-NRRVVH 106
Cdd:cd16030 1 KKPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNsYFRKVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 107 NlavpaglplNETTFAALLKKQGYSTGLIGK-WHQGLNCDsrsdhchHPYNYGFDYYYGMPftlvdSCWPDPSRNTELTF 185
Cdd:cd16030 80 P---------DAVTLPQYFKENGYTTAGVGKiFHPGIPDG-------DDDPASWDEPPNPP-----GPEKYPPGKLCPGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 186 ESQLWLCvqlvaiavltltfgklsgwvsvplllifsmilfiflLGYAWfssytsplywdcllmrghEITEQPMKAERAGS 265
Cdd:cd16030 139 KGGKGGG------------------------------------GGPAW------------------EAADVPDEAYPDGK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 266 ImVKEAISFLERHRK--EPFLLFFSFLHVHIP-------------------------------------LPTTDDFIGTS 306
Cdd:cd16030 165 V-ADEAIEQLRKLKDsdKPFFLAVGFYKPHLPfvapkkyfdlyplesiplpnpfdpidlpevawndlddLPKYGDIPALN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 307 KHGLYGD---------------NVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLearrG-HAQLG---GWNgiyk 367
Cdd:cd16030 244 PGDPKGPlpdeqarelrqayyaSVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHL----GeHGHWGkhtLFE---- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 368 ggkgmggweGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGgsLPQDRVIDGRDLMPLLQG-NARHSEHEFL- 445
Cdd:cd16030 316 ---------EATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNpSAKWKDAAFSq 384
|
490 500 510
....*....|....*....|....*....|
gi 2309511980 446 FHYCGSQLHAVR--------WIPKDDSGAV 467
Cdd:cd16030 385 YPRPSIMGYSIRteryryteWVDFDKVGAE 414
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-513 |
1.93e-46 |
|
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: 165.79 E-value: 1.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrvVHNLA 109
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETG---------VWDNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 110 VPagLPLNETTFAALLKKQGYSTGLIGKWHQGLNCDsrsdhchhpyNYGFDYyygmpftlvdscwpdpsrnteltfesql 189
Cdd:cd16037 72 DP--YDGDVPSWGHALRAAGYETVLIGKLHFRGEDQ----------RHGFRY---------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 190 wlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaERAgsiMVK 269
Cdd:cd16037 112 -----------------------------------------------------------------------DRD---VTE 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 270 EAISFLERH--RKEPFLLFFSFLHVHIPLPTTDDF----IGTSKHGLYGdNVEEMDSMMGKILDAIDDFGLRNNTIVYFT 343
Cdd:cd16037 118 AAVDWLREEaaDDKPWFLFVGFVAPHFPLIAPQEFydlyVRRARAAYYG-LVEFLDENIGRVLDALEELGLLDNTLIIYT 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 344 SDHGGHLEARrghaqlGGWNgiykggkGMGGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRv 423
Cdd:cd16037 197 SDHGDMLGER------GLWG-------KSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL- 261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 424 iDGRDLMPLLQGNARHSEHEFLFHYCGSQLHAVRWIPKDDsgavWKAHYvtpvfqppeaggcyvtslcrcfgeqvtYHN- 502
Cdd:cd16037 262 -DGRSLLPLAEGPDDPDRVVFSEYHAHGSPSGAFMLRKGR----WKYIY---------------------------YVGy 309
|
490
....*....|.
gi 2309511980 503 PPLLFDLSRDP 513
Cdd:cd16037 310 PPQLFDLENDP 320
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-431 |
2.71e-45 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 161.18 E-value: 2.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLgIGD-LGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIrsgmvssgnrrvvHNL 108
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPF-------------YHG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 109 AVPAGLPLNETTFAALLKKQGYSTGLIgkwhqglncdsrSDHCHHPYNYGFDyyygmpftlvdscwpdpsrnteLTFESq 188
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFD----------------------RGFDT- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 189 lwlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssytsplYWDCLLMRGHEITEQPMKAERagsiMV 268
Cdd:cd16148 112 -----------------------------------------------------FEDFRGQEGDPGEEGDERAER----VT 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 269 KEAISFLERHRK-EPFllffsFLHVHIPLPttddfigtskHGLYG-DN-VEEMDSMMGKILDAIDDFGLRNNTIVYFTSD 345
Cdd:cd16148 135 DRALEWLDRNADdDPF-----FLFLHYFDP----------HEPYLyDAeVRYVDEQIGRLLDKLKELGLLEDTLVIVTSD 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 346 HGGHL-EarrgHAQLGGWNgiykggkgMGGWEGGIRVPGIVRWPGKVPAGRlIKEPTSLMDILPTVASVSGGSLPQDrvI 424
Cdd:cd16148 200 HGEEFgE----HGLYWGHG--------SNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--S 264
|
....*..
gi 2309511980 425 DGRDLMP 431
Cdd:cd16148 265 DGRSLLP 271
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
30-542 |
6.11e-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: 165.12 E-value: 6.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIrsgmvssgNRRVVHNlA 109
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLM--------NHRSVWN-G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 110 VPagLPLNETTFAALLKKQGYSTGLIGKWHQGLncDSRSDHCHHPYN-------YGFDYYYGMPFTlvdscwpdPSRNTE 182
Cdd:cd16028 72 TP--LDARHLTLALELRKAGYDPALFGYTDTSP--DPRGLAPLDPRLlsyelamPGFDPVDRLDEY--------PAEDSD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 183 LTFesqlwlcvqlvaIAVLTLTFgkLSGWVSVPLLLIFSmilFI-----FLLGYAWFSSYTSplywdcllmrgheitEQP 257
Cdd:cd16028 140 TAF------------LTDRAIEY--LDERQDEPWFLHLS---YIrphppFVAPAPYHALYDP---------------ADV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 258 MKAERAGSIMVKEAI-SFLERHRKEPFLLFFSFLH---VHIPLPTTDDFIGTSkHGLygdnVEEMDSMMGKILDAIDDFG 333
Cdd:cd16028 188 PPPIRAESLAAEAAQhPLLAAFLERIESLSFSPGAanaADLDDEEVAQMRATY-LGL----IAEVDDHLGRLFDYLKETG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 334 LRNNTIVYFTSDHGGHLearrG-HAQLG--GWNGIYKggkgmggweggiRVPGIVRWPG---KVPAGRLIKEPTSLMDIL 407
Cdd:cd16028 263 QWDDTLIVFTSDHGEQL----GdHWLWGkdGFFDQAY------------RVPLIVRDPRreaDATRGQVVDAFTESVDVM 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 408 PTVASVSGGslPQDRVIDGRDLMPLLQGNarhseheflfhycgsqlhavrwIPKD-DSGAVWKAHYVTPVFQPPEAG--- 483
Cdd:cd16028 327 PTILDWLGG--EIPHQCDGRSLLPLLAGA----------------------QPSDwRDAVHYEYDFRDVSTRRPQEAlgl 382
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2309511980 484 ---GCyvtSLCRCFGEQVTY-HN---PPLLFDLSRDPSESTPLtpATEPLHDFVIKKVADALKEHR 542
Cdd:cd16028 383 spdEC---SLAVIRDERWKYvHFaalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKLLSWR 443
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-431 |
3.29e-42 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 152.39 E-value: 3.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSG----MVSSGNRRVV 105
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGihdwIVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 106 HNLAVPAGlplnETTFAALLKKQGYSTGLIGKWHQGlncdsrsdhchhpynygfdyyygmpftlvdscwpdpsrnteltf 185
Cdd:cd16149 81 KPEGYLEG----QTTLPEVLQDAGYRCGLSGKWHLG-------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 186 esqlwlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaerags 265
Cdd:cd16149 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 266 imvKEAISFLERH--RKEPFLLFFSFLHVHiplpttddfigtSKHGlYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFT 343
Cdd:cd16149 113 ---DDAADFLRRRaeAEKPFFLSVNYTAPH------------SPWG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFT 176
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 344 SDHG---GH---LEARRGHAQLGGWNgiykggkgmggweGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGS 417
Cdd:cd16149 177 SDNGfnmGHhgiWGKGNGTFPLNMYD-------------NSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVD 243
|
410
....*....|....
gi 2309511980 418 LPQDRVIDGRDLMP 431
Cdd:cd16149 244 PPADPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-539 |
7.18e-42 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 155.03 E-value: 7.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 29 KPNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQ-HI----SAAsLCSPSRSAFLTGRYpirsgmvssgnrr 103
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRT------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 104 vVHNL--AVPAGLPLNETTFAALLKKQGYSTGLIGKWHQGLnCDSRSDHCHHpYNYGFDyyygmPFtlvdscwpdpsrnt 181
Cdd:cd16155 68 -LFHApeGGKAAIPSDDKTWPETFKKAGYRTFATGKWHNGF-ADAAIEFLEE-YKDGDK-----PF-------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 182 eltfesqlwlcvqlvaiavltltfgklsgwvsvplllifsmilFIFLlgyawfsSYTSPlywdcllmrgHEITEQPMKAE 261
Cdd:cd16155 126 -------------------------------------------FMYV-------AFTAP----------HDPRQAPPEYL 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 262 R---AGSIMVKEaiSFLERH--RKEPFLLFFSFLHvhiPLPTTDDFIgtSKH-GLYGDNVEEMDSMMGKILDAIDDFGLR 335
Cdd:cd16155 146 DmypPETIPLPE--NFLPQHpfDNGEGTVRDEQLA---PFPRTPEAV--RQHlAEYYAMITHLDAQIGRILDALEASGEL 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 336 NNTIVYFTSDHG---GHlearrgHAQLGGWNgiykggkgmgGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVAS 412
Cdd:cd16155 219 DNTIIVFTSDHGlavGS------HGLMGKQN----------LYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCE 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 413 VSGGSLPQDrvIDGRDLMPLLQGNARhSEHEFLF-HYCGSQlhavRWIPKDDsgavWKAHYVTPvfqppeaggcyvtslc 491
Cdd:cd16155 282 LAGIEIPES--VEGKSLLPVIRGEKK-AVRDTLYgAYRDGQ----RAIRDDR----WKLIIYVP---------------- 334
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2309511980 492 rcfGEQVTyhnppLLFDLSRDPSESTPLtpATEPLHDFVIKKVADALK 539
Cdd:cd16155 335 ---GVKRT-----QLFDLKKDPDELNNL--ADEPEYQERLKKLLAELK 372
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-541 |
2.13e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 133.89 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 29 KPNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVVHNl 108
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETG--------CFRN- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 109 AVPagLPLNETTFAALLKKQGYSTGLIGKWHqglncdsrsdhchhpynygfdyyygmpftlvdscwpdpsrnteltfesq 188
Cdd:cd16152 72 GIP--LPADEKTLAHYFRDAGYETGYVGKWH------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 189 lwlcvqlvaiavltltfgklsgwvsvplllifsmilfifLLGYawfssytsplywdcllmRGHEITEQpmkaeragsimv 268
Cdd:cd16152 101 ---------------------------------------LAGY-----------------RVDALTDF------------ 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 269 keAISFL-ERHRKEPFLLFFSFLHVH----------------------IPlPTTDDFIGTSKHGL---YGdNVEEMDSMM 322
Cdd:cd16152 113 --AIDYLdNRQKDKPFFLFLSYLEPHhqndrdryvapegsaerfanfwVP-PDLAALPGDWAEELpdyLG-CCERLDENV 188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 323 GKILDAIDDFGLRNNTIVYFTSDHGGHLEARRG------HaqlggwngiykggkgmggwEGGIRVPGIVRWPGkVPAGRL 396
Cdd:cd16152 189 GRIRDALKELGLYDNTIIVFTSDHGCHFRTRNAeykrscH-------------------ESSIRVPLVIYGPG-FNGGGR 248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 397 IKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNARHSEHEFLFHYCGSQL-HAVRwipkddsGAVWKahYVtp 475
Cdd:cd16152 249 VEELVSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNEVFIQISESQVgRAIR-------TDRWK--YS-- 315
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2309511980 476 VFQPPEAGGCYVTSLcrcfgeqvTYHnPPLLFDLSRDPSESTPLtpATEPLHdfviKKVADALKEH 541
Cdd:cd16152 316 VAAPDKDGWKDSGSD--------VYV-EDYLYDLEADPYELVNL--IGRPEY----REVAAELRER 366
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
29-427 |
7.32e-34 |
|
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: 133.06 E-value: 7.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 29 KPNIVLIMVDDLgigDLGcYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPirsgmvssGNRRVVHNL 108
Cdd:cd16147 1 RPNIVLILTDDQ---DVE-LGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYA--------HNHGVTNNS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 109 AVPAGLP------LNETTFAALLKKQGYSTGLIGKWhqgLN-CDSRSDHCHHPynYGFDYYYGMpftlvdscwPDPSRNT 181
Cdd:cd16147 69 PPGGGYPkfwqngLERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVP--PGWDEWDGL---------VGNSTYY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 182 EltfesqlwlcvqlvaiavLTLTFGKLSGwvsvplllifsmilfiflLGYAWFSSYTSPLYwdcllmrgheiteqpmkAE 261
Cdd:cd16147 135 N------------------YTLSNGGNGK------------------HGVSYPGDYLTDVI-----------------AN 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 262 RagsimvkeAISFLERHRK--EPFLLFFSFLHVHIPL-----------------PTTDDFIGTS--KHGL---------- 310
Cdd:cd16147 162 K--------ALDFLRRAAAddKPFFLVVAPPAPHGPFtpapryanlfpnvtappRPPPNNPDVSdkPHWLrrlpplnptq 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 311 --YGDNV--------EEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLearrG-HAQLGGwngiykggkGMGGWEGGI 379
Cdd:cd16147 234 iaYIDELyrkrlrtlQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHL----GqHRLPPG---------KRTPYEEDI 300
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2309511980 380 RVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGR 427
Cdd:cd16147 301 RVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
30-433 |
2.31e-32 |
|
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: 130.19 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSgnrrvvhNLA 109
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTN-------CMA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 110 vpagLPLNETTFAALLKKQGYSTGLIGKWHqglnCDSrSDH-----ChhPYNYGFDYYYGMpftlvdscwpdpsRN--TE 182
Cdd:cd16156 74 ----LGDNVKTIGQRLSDNGIHTAYIGKWH----LDG-GDYfgngiC--PQGWDPDYWYDM-------------RNylDE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 183 LTFESQlwlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgYAWFSSYTSplywdcllMRGHEITEQPMKAER 262
Cdd:cd16156 130 LTEEER------------------------------------------RKSRRGLTS--------LEAEGIKEEFTYGHR 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 263 agsiMVKEAISFLERHRKEPFLLFFSFLHVH----IPLPTTD---DFIGTSKHGLYgDNVEE------------------ 317
Cdd:cd16156 160 ----CTNRALDFIEKHKDEDFFLVVSYDEPHhpflCPKPYASmykDFEFPKGENAY-DDLENkplhqrlwagakphedgd 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 318 ---------------MDSMMGKILDAIDDfgLRNNTIVYFTSDHGGHLEARRGHAQlggwngiykggkGMGGWEGGIRVP 382
Cdd:cd16156 235 kgtikhplyfgcnsfVDYEIGRVLDAADE--IAEDAWVIYTSDHGDMLGAHKLWAK------------GPAVYDEITNIP 300
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2309511980 383 GIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGgsLPQDRVIDGRDLMPLL 433
Cdd:cd16156 301 LIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATI 349
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-448 |
3.65e-31 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 123.47 E-value: 3.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDD--------LGIGDLGCygndtirtPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVssgn 101
Cdd:cd16035 1 PNILLILTDQerypppwpAGWAALNL--------PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 102 rrvvHNLAVPAGLPLNET--TFAALLKKQGYSTGLIGKWHqgLncdsrSDHCHHPYNYgfdyyygmpftlvdscwpDPsr 179
Cdd:cd16035 69 ----DTLGSPMQPLLSPDvpTLGHMLRAAGYYTAYKGKWH--L-----SGAAGGGYKR------------------DP-- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 180 nteltfesqlwlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssytsplywdcllmrghEITEQpmk 259
Cdd:cd16035 118 ------------------------------------------------------------------------GIAAQ--- 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 260 aeragsimvkeAISFLERHRK-----EPFLLFFSFL--H-VHIPLPTTDDFIgtSKHGLYGDNVEEMDSMMGKILDAIDD 331
Cdd:cd16035 123 -----------AVEWLRERGAknadgKPWFLVVSLVnpHdIMFPPDDEERWR--RFRNFYYNLIRDVDRQIGRVLDALDA 189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 332 FGLRNNTIVYFTSDHGGHLEARRGHAQLGgwngiykggkgmGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVA 411
Cdd:cd16035 190 SGLADNTIVVFTSDHGEMGGAHGLRGKGF------------NAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLL 257
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2309511980 412 SVSGGSLPQDRVID----GRDLMPLLQGNARHS-EHEFLFHY 448
Cdd:cd16035 258 GLAGVDAEARATEApplpGRDLSPLLTDADADAvRDGILFTY 299
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-429 |
9.58e-31 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 121.33 E-value: 9.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 29 KPNIVLIMVDDLGIGDLGCYGN----------DTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVs 98
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 99 sGNRRvVHNlAVPAGLPlnetTFAALLKKQGYSTGLIGKwhqglncdsrsdhchhpynygfdyyygmpftlvdscwpdps 178
Cdd:cd16153 80 -GFEA-AHP-ALDHGLP----TFPEVLKKAGYQTASFGK----------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 179 rnteltfesqlwlcvqlvaiavltltfgklsgwvsvplllifsmilfiflLGYAWFSSYtsplywdcllmrgheiTEQPM 258
Cdd:cd16153 112 --------------------------------------------------SHLEAFQRY----------------LKNAN 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 259 KAERAGSIMVKEAISflerhRKEPFLLFFSFLHVHIP-LPTTD-----DFIGTSKHGlygdnveemDSMMGKILDAIDDF 332
Cdd:cd16153 126 QSYKSFWGKIAKGAD-----SDKPFFVRLSFLQPHTPvLPPKEfrdrfDYYAFCAYG---------DAQVGRAVEAFKAY 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 333 GL---RNNTIVYFTSDHGGHLEARRGHAQLGGWNgiykggkgmggweGGIRVPGIVRWPGK--VPAGRLIKEPTSLMDIL 407
Cdd:cd16153 192 SLkqdRDYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QSHRVPLIVVSSDKlkAPAGKVRHDFVEFVDLA 258
|
410 420
....*....|....*....|..
gi 2309511980 408 PTVASVSGGSLPQDRVIDGRDL 429
Cdd:cd16153 259 PTLLAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-515 |
3.73e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 123.11 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnRRVVHNLa 109
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG------HRTLHHL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 110 vpagLPLNETTFAALLKKQGYSTGLIGKWHqglncdsrsdhchhpynygfdyyygmpftlvdsCWPDPsrnteltfesql 189
Cdd:cd16150 74 ----LRPDEPNLLKTLKDAGYHVAWAGKND---------------------------------DLPGE------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 190 wlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyAWFSSYTSplyWDCLlmrgheiteqpmkaeragsiMVK 269
Cdd:cd16150 105 ------------------------------------------FAAEAYCD---SDEA--------------------CVR 119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 270 EAISFLERHR-KEPFLLFFSFLHVHIPLPTTDDF--------------------------IGTSKHGLYGDN-------- 314
Cdd:cd16150 120 TAIDWLRNRRpDKPFCLYLPLIFPHPPYGVEEPWfsmidreklpprrppglrakgkpsmlEGIEKQGLDRWSeerwrelr 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 315 ------VEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLearrG-HAQLGGWngiykggkGMGGWEGGIRVPGIVRw 387
Cdd:cd16150 200 atylgmVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYT----GdYGLVEKW--------PNTFEDCLTRVPLIIK- 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 388 PGKVPAGRLIKEPTSLMDILPTVASVSGgsLPQDRVIDGRDLMPLLQG------NARHSEHEFLFHycGSQLHAVRWIPK 461
Cdd:cd16150 267 PPGGPAGGVSDALVELVDIPPTLLDLAG--IPLSHTHFGRSLLPVLAGeteehrDAVFSEGGRLHG--EEQAMEGGHGPY 342
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2309511980 462 DDsgavwKAHYVTPVFQPPEAGGCYVtslCRcfGEQVTY----HNPPLLFDLSRDPSE 515
Cdd:cd16150 343 DL-----KWPRLLQQEEPPEHTKAVM---IR--TRRYKYvyrlYEPDELYDLEADPLE 390
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
30-411 |
3.76e-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: 118.29 E-value: 3.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCYGNDTIRTPHIDRLAREGVRL-TQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVVHNl 108
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 109 AVPAGLPLNETTFAALLKKQGYSTGLIGkwhqglncdsrsdhchhpynygfdyyygmpftlvdscwpdpsrnteltfesq 188
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG---------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 189 lwlcvqlvaiavltltfgklsgwvsvplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaeragsimv 268
Cdd:cd00016 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 269 keAISFLERHRKE-PFLLFFSFLHVHIPLPTTDdfigtSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHG 347
Cdd:cd00016 108 --LLKAIDETSKEkPFVLFLHFDGPDGPGHAYG-----PNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHG 180
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2309511980 348 GHLEarrGHAQLGGwngiykGGKGMGGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVA 411
Cdd:cd00016 181 GIDK---GHGGDPK------ADGKADKSHTGMRVPFIAYGPG-VKKGGVKHELISQYDIAPTLA 234
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-435 |
7.60e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 109.36 E-value: 7.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGIGDLGCY--GNDTIRTPHIDRLAREGVRLTqHISAASLCSPSRSAFLTGRYPIRSGMvssgnrrvvhn 107
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYslSSDLPVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGV----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 108 LAVPAGLPLNETTFAALLKKQ----GYSTGLIGKWHQGlNCDSrsdhchHPYNYG-FDYYYGMPFTLVDSCWPDPSRNTE 182
Cdd:cd16154 69 LAVPDELLLSEETLLQLLIKDattaGYSSAVIGKWHLG-GNDN------SPNNPGgIPYYAGILGGGVQDYYNWNLTNNG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 183 LTFESQLWLCVQLVAIAVltltfgklsgwvsvplllifsmilfifllgyAWFSSYTSPLY-Wdcllmrgheiteqpmkae 261
Cdd:cd16154 142 QTTNSTEYATTKLTNLAI-------------------------------DWIDQQTKPWFlW------------------ 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 262 ragsimvkeaISFLERHrkEPFLLFFSFLHVHIPLPTTDDfIGTSKHGLYGDNVEEMDSMMGKILDAIDDfGLRNNTIVY 341
Cdd:cd16154 173 ----------LAYNAPH--TPFHLPPAELHSRSLLGDSAD-IEANPRPYYLAAIEAMDTEIGRLLASIDE-EERENTIII 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 342 FTSDHGGHLEAR-----RGHAQ----LGGwngiykggkgmggweggIRVPGIVRWPGkvpAGRLIKEPTSLM---DILPT 409
Cdd:cd16154 239 FIGDNGTPGQVVdlpytRNHAKgslyEGG-----------------INVPLIVSGAG---VERANERESALVnatDLYAT 298
|
410 420
....*....|....*....|....*.
gi 2309511980 410 VASVSGGSLPQdrVIDGRDLMPLLQG 435
Cdd:cd16154 299 IAELAGVDAAE--IHDSVSFKPLLSD 322
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
30-514 |
7.60e-21 |
|
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: 94.53 E-value: 7.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDDLGiGDLGCY-GNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPirsGMVSSGNRRvvhnl 108
Cdd:cd16171 1 PNVVMVMSDSFD-GRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT---HLTESWNNY----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 109 avpAGLPLNETTFAALLKKQGYSTGLIGKwhqglnCDSRSDHcHHPYNYGFDYYYGMPFTLVDSCWPdpsrnteltfesq 188
Cdd:cd16171 72 ---KGLDPNYPTWMDRLEKHGYHTQKYGK------LDYTSGH-HSVSNRVEAWTRDVPFLLRQEGRP------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 189 lwlCVQLVAIAvlTLTFGKLSGWVSVplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaERAGSIMV 268
Cdd:cd16171 129 ---TVNLVGDR--STVRVMLKDWQNT----------------------------------------------DKAVHWIR 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 269 KEAISFlerhrKEPFLLFfsfLHVHIPLPTTDDFIGTSKHGL------YGDNVEEMDSMMGKILDAIDDFGLRNNTIVYF 342
Cdd:cd16171 158 KEAPNL-----TQPFALY---LGLNLPHPYPSPSMGENFGSIrnirafYYAMCAETDAMLGEIISALKDTGLLDKTYVFF 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 343 TSDHGghlEARRGHAQLggwngiykggKGMGGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDr 422
Cdd:cd16171 230 TSDHG---ELAMEHRQF----------YKMSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN- 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 423 vIDGRDLMPLLQGNARHSEHEFLFH-------YCGSQLHAVRWIPKDDSgavWKahYVTpvfqppeaggcYVTslcrcfG 495
Cdd:cd16171 295 -LSGYSLLPLLSESSIKESPSRVPHpdwvlseFHGCNVNASTYMLRTNS---WK--YIA-----------YAD------G 351
|
490
....*....|....*....
gi 2309511980 496 EQVtyhnPPLLFDLSRDPS 514
Cdd:cd16171 352 NSV----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 2309511980 29 KPNIVLIMVDDLG---IGDLGcYGNDTirTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSG--MVSSGNRR 103
Cdd:COG1368 234 KPNVVVILLESFSdffIGALG-NGKDV--TPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGspYKRPGQNN 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 104 VvhnlavpaglplneTTFAALLKKQGYSTgligkwhqglncdsrsdHCHHPYNYGFD----YYYGMPF-TLVD-SCWPDP 177
Cdd:COG1368 311 F--------------PSLPSILKKQGYET-----------------SFFHGGDGSFWnrdsFYKNLGFdEFYDrEDFDDP 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 178 SRNteltfesqlwlcvqlvaiavltltfgklsGWVsvplllifsmilfifllgyawfssytsplYWDcllmrgheiteqp 257
Cdd:COG1368 360 FDG-----------------------------GWG-----------------------------VSD------------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 258 mkaeragSIMVKEAISFLERHrKEPFLLFFSFLHVHIP--LPTTDDFIGTSKHGLYGDN---VEEMDSMMGKILDAIDDF 332
Cdd:COG1368 369 -------EDLFDKALEELEKL-KKPFFAFLITLSNHGPytLPEEDKKIPDYGKTTLNNYlnaVRYADQALGEFIEKLKKS 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 333 GLRNNTIVYFTSDHGGHLEARRghaqlggwngiykggkGMGGWEGGIRVPGIVrWPGKVPAGRLIKEPTSLMDILPTVAS 412
Cdd:COG1368 441 GWYDNTIFVIYGDHGPRSPGKT----------------DYENPLERYRVPLLI-YSPGLKKPKVIDTVGSQIDIAPTLLD 503
|
410
....*....|....*...
gi 2309511980 413 VSGGSLPQDRVIdGRDLM 430
Cdd:COG1368 504 LLGIDYPSYYAF-GRDLL 520
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
30-415 |
4.52e-10 |
|
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: 60.77 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 30 PNIVLIMVDdlGIGD--LGCYGNDTIRTPHIDRLAREGVRLTQHISAASLCSPSRS--AFLTGRYPIRSGMVSSgNRRVV 105
Cdd:cd16015 1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSY-TLYKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 106 HNLavpaglplneTTFAALLKKQGYSTGLIgkwhqglncdsrsdHCHHPYNY---------GFDYYYGMpftlvdSCWPD 176
Cdd:cd16015 78 NPL----------PSLPSILKEQGYETIFI--------------HGGDASFYnrdsvypnlGFDEFYDL------EDFPD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 177 PSRNTeltfesqlwlcvqlvaiavltltfgklSGWVsvplllifsmilfifllgyawfssytsplYWDcllmrgheiteq 256
Cdd:cd16015 128 DEKET---------------------------NGWG-----------------------------VSD------------ 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 257 pmkaeragSIMVKEAISFLERHRKEPFLLFFSFLHVHIPLPTTDDFIGTSKHGLYGDN--------VEEMDSMMGKILDA 328
Cdd:cd16015 140 --------ESLFDQALEELEELKKKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTelenylnaIHYTDKALGEFIEK 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 329 IDDFGLRNNTIVYFTSDHGGHLEarrghaqlggwngiYKGGKGMGGWEGGIRVPGIVRWPGKVPAGRlIKEPTSLMDILP 408
Cdd:cd16015 212 LKKSGLYENTIIVIYGDHLPSLG--------------SDYDETDEDPLDLYRTPLLIYSPGLKKPKK-IDRVGSQIDIAP 276
|
....*..
gi 2309511980 409 TVASVSG 415
Cdd:cd16015 277 TLLDLLG 283
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
234-409 |
1.90e-09 |
|
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: 60.30 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 234 FSS--YTSPLYWDCLLmrgHEITEQPMKAERAG----SIMVKEAISFL-ERHRKEPFllfFSFL-------------HVH 293
Cdd:COG3083 330 FSSagFNSPLFRQTIF---SDVSLPRLHTPGGPaqrdRQITAQWLQWLdQRDSDRPW---FSYLfldaphaysfpadYPK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 294 IPLPTTD-DFIGTSKHG-------LYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHL----EARRGHAqlGG 361
Cdd:COG3083 404 PFQPSEDcNYLALDNESdptpfknRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnengQNYWGHN--SN 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2309511980 362 WNgiykggkgmggwEGGIRVPGIVRWPGKVPagRLIKEPTSLMDILPT 409
Cdd:COG3083 482 FS------------RYQLQVPLVIHWPGTPP--QVISKLTSHLDIVPT 515
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
1-347 |
1.50e-08 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 57.07 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 1 MRPRSPLVFMSLVCTFLNTCQAHRvhddkpNIVLIMVDDLGIGDLgcygnDTIRTPHIDRLAREGVRLTQHISAA-SLCS 79
Cdd:COG1524 1 MKRGLSLLLASLLAAAAAAAPPAK------KVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 80 PSRSAFLTGRYPIRSGMVSSG------NRRVVHNLAVPAGLPLNE----TTFAALLKKQGYSTGLIGKWHQGlncDSRSD 149
Cdd:COG1524 70 PAHTTLLTGLYPGEHGIVGNGwydpelGRVVNSLSWVEDGFGSNSllpvPTIFERARAAGLTTAAVFWPSFE---GSGLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 150 HCHHPYNY-GFDYYYGMPFTlvdscwpdpsrnteltfesqlwlcvqlvaiavltltfgklsgwvsvplllifsmilfifl 228
Cdd:COG1524 147 DAARPYPYdGRKPLLGNPAA------------------------------------------------------------ 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 229 lgyawfssytsplywdcllmrgheiteqpmkaeraGSIMVKEAISFLERHRkePFLLFFSFLHVhiplpttdDFIGtSKH 308
Cdd:COG1524 167 -----------------------------------DRWIAAAALELLREGR--PDLLLVYLPDL--------DYAG-HRY 200
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2309511980 309 GLYGDN----VEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHG 347
Cdd:COG1524 201 GPDSPEyraaLREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
274-353 |
8.81e-05 |
|
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: 45.41 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 274 FLERHRKEP-FLLFFSFLHVHiplpttDDFIGTSKhglygdnveeMDSMMGKILDAIDDFGLRNNTIVYFTSDHG----- 347
Cdd:pfam02995 284 FLPRYRDSPfFGFFWSNSLSH------DDFNYASA----------LDEDFLKYLKKLHKRGLLDNTIVIFMSDHGlrfgk 347
|
90
....*....|..
gi 2309511980 348 ------GHLEAR 353
Cdd:pfam02995 348 lrrtsqGMLEER 359
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
33-347 |
1.78e-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: 43.95 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 33 VLIMVDDLGIGDLgcygNDTIRTPHIDRLAREGVRLTQHISAA-SLCSPSRSAFLTGRYPIRSGMVS------SGNRRVV 105
Cdd:pfam01663 2 LVISLDGFRADYL----DRFELTPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVGntfydpKTGEYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 106 HNLAVP-AGLPLNETTFAALLKKQGYSTGLIGkWhqglncdSRSDHCHHPYNYGFDYYYGMPFtlvdscwpdpsrNTELT 184
Cdd:pfam01663 78 FVISDPeDPRWWQGEPIWDTAAKAGVRAAALF-W-------PGSEVDYSTYYGTPPRYLKDDY------------NNSVP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 185 FEsqlwlcvqlvaiavltltfGKLSGWVSvplllifsmilfifllgYAWFSSytsplywdcllmrgheiteqpmkaerag 264
Cdd:pfam01663 138 FE-------------------DRVDTAVL-----------------QTWLDL---------------------------- 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511980 265 simvkeaiSFLERHRKEPFLLFFSFLHVhiplpttdDFIGtSKHGLYGDNVEEM----DSMMGKILDAIDDFGLRNNTIV 340
Cdd:pfam01663 154 --------PFADVAAERPDLLLVYLEEP--------DYAG-HRYGPDSPEVEDAlrrvDRAIGDLLEALDERGLFEDTNV 216
|
....*..
gi 2309511980 341 YFTSDHG 347
Cdd:pfam01663 217 IVVSDHG 223
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
307-347 |
4.12e-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: 39.49 E-value: 4.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2309511980 307 KHGLYGDNV----EEMDSMMGKILDAIDDFGLRNNTIVYFTSDHG 347
Cdd:cd16018 173 KYGPDSPEVnealKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG 217
|
|
| AP-SPAP |
cd16016 |
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
301-349 |
8.45e-03 |
|
SPAP is a subclass of alkaline phosphatase (AP); 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. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.
Pssm-ID: 293740 [Multi-domain] Cd Length: 457 Bit Score: 39.05 E-value: 8.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2309511980 301 DFIGTSkhglYGDNVEEM-------DSMMGKILDAIDDFGLRNNTIVYFTSDHGGH 349
Cdd:cd16016 218 DYIGHA----FGPNSVEMedtylrlDRDLARLLDALDKKVGKGNYLVFLTADHGAA 269
|
|
| |
