|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
1-502 |
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: 702.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 1 CF-----RTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVVHNLAVPAGLPLNETTFAALLK 75
Cdd:cd16159 19 CFgndtiRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTASSGGLPPNETTFAEVLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 76 KQGYSTGLIGKWHQGLNCDSRSDHCHHPYNYGFDYYYGMPFTLVDSCWPDPSRNTELTFESQLWLCVQLVAIAVLTLTFG 155
Cdd:cd16159 99 QQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPLFPLLTAFVLITALTIFLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 156 KLSGWVSVplLLIFSMILFIFLLGYAWFSSYTSPLYWDCLLMRGHEITEQPMKAERAGSIMVKEAISFLERHRKEPFLLF 235
Cdd:cd16159 179 LYLGAVSK--RFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLTKEAISFLERNKERPFLLV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 236 FSFLHVHIPLPTTDDFIGTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEARRGHAQLGGWNGIY 315
Cdd:cd16159 257 MSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLEEISVGGEYGGGNGGI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 316 KGGKGMGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNARHSEHEFLF 395
Cdd:cd16159 337 YGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLMPLLTGQEKRSPHEFLF 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 396 HYCGSQLHAVRWIPKdDSGAVWKAHYVTPVFQpPEAGGCYVTSLCRCFGEQVTYHNPPLLFDLSRDPSESTPLTPATEPl 475
Cdd:cd16159 417 HYCGAELHAVRYRPR-DGGAVWKAHYFTPNFY-PGTEGCCGTLLCRCFGDSVTHHDPPLLFDLSADPSESNPLDPTDEP- 493
|
490 500
....*....|....*....|....*..
gi 795629712 476 HDFVIKKVADALKEHRETIMPVTYQLS 502
Cdd:cd16159 494 YQEIIKKILEAVAEHQSSIEPVESQLS 520
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
3-469 |
2.55e-133 |
|
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: 393.08 E-value: 2.55e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVSsgnrrVVHNLAVPAGLPLNETTFAALLKKQGYSTG 82
Cdd:cd16026 26 KTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPG-----VVGPPGSKGGLPPDEITIAEVLKKAGYRTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 83 LIGKWHQGlncdsrsDH-CHHPYNYGFDYYYGMPFTlvDSCWPDPSRNTEltfesqlwlcvqlvaiavltltfgklsgwv 161
Cdd:cd16026 101 LVGKWHLG-------HQpEFLPTRHGFDEYFGIPYS--NDMWPFPLYRND------------------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 162 svplllifsmilfifllgyawfssytsPLYWDCLLMRGHEITEQPMKAERAGSIMVKEAISFLERHRKEPFLLFFSFLHV 241
Cdd:cd16026 142 ---------------------------PPGPLPPLMENEEVIEQPADQSSLTQRYTDEAVDFIERNKDQPFFLYLAHTMP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 242 HIPLPTTDDFIGTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLE--ARRGHAQL----------G 309
Cdd:cd16026 195 HVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLEygGHGGSAGPlrggkgttweG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 310 GwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNARHS 389
Cdd:cd16026 275 G-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 390 EHEFLFHYCGSQLHAVRWIPkddsgavWKAHYVTPVFQPPEAGGCYVTSlcrcfgeqvtyHNPPLLFDLSRDPSESTPLT 469
Cdd:cd16026 338 PHPFFYYYDGGDLQAVRSGR-------WKLHLPTTYRTGTDPGGLDPTK-----------LEPPLLYDLEEDPGETYNVA 399
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
7-489 |
1.00e-110 |
|
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: 336.71 E-value: 1.00e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 7 IDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVssGNRRVVHNLAVpAGLPLNETTFAALLKKQGYSTGLIGK 86
Cdd:cd16160 30 IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--GGTRVFLPWDI-GGLPKTEVTMAEALKEAGYTTGMVGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 87 WHQGLNCDSRSDHCHHPYNYGFDYY-YGMPFTLVdscwpdpsrnteltfesqlWLCVQlvaiavltltfgklsgwvsvpl 165
Cdd:cd16160 107 WHLGINENNHSDGAHLPSHHGFDFVgTNLPFTNS-------------------WACDD---------------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 166 llifsmilfifllgyaWFSSYTSPLYWDCLLMRGHEITEQPMKAERAGSIMVKEAISFLERHRKEPFLLFFSFLHVHIPL 245
Cdd:cd16160 146 ----------------TGRHVDFPDRSACFLYYNDTIVEQPIQHEHLTETLVGDAKSFIEDNQENPFFLYFSFPQTHTPL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 246 PTTDDFIGTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEarrgHAQLGGwNGIYKGGKGMGGWE 325
Cdd:cd16160 210 FASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVE----YCLEGG-STGGLKGGKGNSWE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 326 GGIRVPGIVRWPGKVPaGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNARHSEHEFLFHYCgSQLHAV 405
Cdd:cd16160 285 GGIRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDILYYCC-SRLMAV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 406 RWIPkddsgavWKAHYVTPVFQPPEA------GGCYVTS--LCR-CFGEQVTYHNPPLLFDLSRDPSESTPLTPAtepLH 476
Cdd:cd16160 363 RYGS-------YKIHFKTQPLPSQESldpncdGGGPLSDyiVCYdCEDECVTKHNPPLIFDVEKDPGEQYPLQPS---VY 432
|
490
....*....|...
gi 795629712 477 DFVIKKVADALKE 489
Cdd:cd16160 433 EHMLEAVEKLIAH 445
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
4-469 |
7.44e-87 |
|
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: 273.19 E-value: 7.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 4 TPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVVHNLAVPA--GLPLNETTFAALLKKQGYST 81
Cdd:cd16161 28 TPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNG--------VGHNFLPTSvgGLPLNETTLAEVLRQAGYAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 82 GLIGKWHQGLNcdsrsdHCHHPYNYGFDYYYGMPFtlvdscwpdpSRNTELTFEsqlwlcvqlvaiavltltfgklsgwv 161
Cdd:cd16161 100 GMIGKWHLGQR------EAYLPNSRGFDYYFGIPF----------SHDSSLADR-------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 162 svplllifsmilfifllgYAWFssytsplywdcllmrgheiteqpmkaeragsimvkeAISFLERH--RKEPFLLFFSFL 239
Cdd:cd16161 138 ------------------YAQF------------------------------------ATDFIQRAsaKDRPFFLYAALA 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 240 HVHIPLPTTDDF-IGTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEARRGHAQLGGWNGIYKGG 318
Cdd:cd16161 164 HVHVPLANLPRFqSPTSGRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGPWEVKCELAVGPGTGDWQGNLG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 319 KGMGGWEG---GIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNARhSEHEFLF 395
Cdd:cd16161 244 GSVAKASTwegGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSK-TGHRCLF 322
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795629712 396 HYCGS-----QLHAVRWIPkddsgavWKAHYVTpvfqppeaGGCYVTslCRCFGEQVtYHNPPLLFDLSRDPSESTPLT 469
Cdd:cd16161 323 HPNSGaagagALSAVRCGD-------YKAHYAT--------GGALAC--CGSTGPKL-YHDPPLLFDLEVDPAESFPLT 383
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
3-469 |
3.76e-81 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 257.85 E-value: 3.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAASlCSPSRSAFLTGRYPIRSGMVSSGnrrvvhnLA-VPAGLPLNETTFAALLKKQGYST 81
Cdd:cd16142 28 PTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVG-------LPgSPGGLPPWEPTLAELLKDAGYAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 82 GLIGKWHQGlncdsrsDHCHH-PYNYGFDYYYGMPFTLVDScwpdpsrnteltfesqlwlcvqlvaiavltltfgklsgw 160
Cdd:cd16142 100 AQFGKWHLG-------DEDGRlPTDHGFDEFYGNLYHTIDE--------------------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 161 vsvplllifsmilfifllgyawfssytsplywdcllmrghEITEQpmkaeragsimvkeAISFLERHRK--EPFLLFFSF 238
Cdd:cd16142 134 ----------------------------------------EIVDK--------------AIDFIKRNAKadKPFFLYVNF 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 239 LHVHIPLPTTDDFIGTSK-HGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEA--------RRGH---A 306
Cdd:cd16142 160 TKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGPEQDVwpdggytpFRGEkgtT 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 307 QLGGWngiykggkgmggweggiRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLP------QDRVIDGRDLMP 380
Cdd:cd16142 240 WEGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRHIDGVDQSP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 381 LLQGNARHSEHEFLFHYCGSQLHAVRWipKDdsgavWKAHYVTpvfQPPEAGGCYVTSlcrcfgEQVTYhnpPLLFDLSR 460
Cdd:cd16142 303 FLLGKSEKSRRSEFFYFGEGELGAVRW--KN-----WKVHFKA---QEDTGGPTGEPF------YVLTF---PLIFNLRR 363
|
....*....
gi 795629712 461 DPSESTPLT 469
Cdd:cd16142 364 DPKERYDVT 372
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
2-466 |
3.01e-79 |
|
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: 254.78 E-value: 3.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 2 FRTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGM--VSSGNRRVVHNLAVPA-----GLPLNETTFAALL 74
Cdd:cd16144 24 YETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdVIPGRRGPPDNTKLIPppsttRLPLEEVTIAEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 75 KKQGYSTGLIGKWHQGLNcdsrsdHCHHPYNYGFDYYYGmpftlvDSCWPDPSRnteltfesqlwlcvqlvaiavltltf 154
Cdd:cd16144 104 KDAGYATAHFGKWHLGGE------GGYGPEDQGFDVNIG------GTGNGGPPS-------------------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 155 gklsgwvsvplllifsmilfifllGYAWFSSYTSPLYwdcllmrghEITEQPMKAERagsiMVKEAISFLERHRKEPFLL 234
Cdd:cd16144 146 ------------------------YYFPPGKPNPDLE---------DGPEGEYLTDR----LTDEAIDFIEQNKDKPFFL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 235 FFSFLHVHIPLPTTDDFI-----------GTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEA-- 301
Cdd:cd16144 189 YLSHYAVHTPIQARPELIekyekkkkglrKGQKNPVYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRgg 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 302 --------RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDR 371
Cdd:cd16144 269 pptsnaplRGGKGSLyeGG-----------------IRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQ 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 372 VIDGRDLMPLLQGNARHSEHEFLF----HYCGSQLHAVRWIPKDDsgavWKAHYvtpvfqppeaggcyvtslcrcFGEQV 447
Cdd:cd16144 332 HLDGVSLVPLLKGGEADLPRRALFwhfpHYHGQGGRPASAIRKGD----WKLIE---------------------FYEDG 386
|
490
....*....|....*....
gi 795629712 448 TYHnpplLFDLSRDPSEST 466
Cdd:cd16144 387 RVE----LYNLKNDIGETN 401
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
2-466 |
1.08e-78 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 252.51 E-value: 1.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 2 FRTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgNRRVVHNLAVPAGLPLNETTFAALLKKQGYST 81
Cdd:cd16143 25 IPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSR-----LKGGVLGGFSPPLIEPDRVTLAKMLKQAGYRT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 82 GLIGKWHQGLN---CDSRSDHCHH-------------PYNYGFDYYYGMPftlvdscwpdpsrnteltfesqlwlcvqlv 145
Cdd:cd16143 100 AMVGKWHLGLDwkkKDGKKAATGTgkdvdyskpikggPLDHGFDYYFGIP------------------------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 146 AIAVLTLTFGKlsgwvsvplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaeragsimvkeAISFLE 225
Cdd:cd16143 150 ASEVLPTLTDK---------------------------------------------------------------AVEFID 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 226 RHRK--EPFLLFFSFLHVHIPLPTTDDFIGTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEARR 303
Cdd:cd16143 167 QHAKkdKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPYADY 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 304 GHAQL------------------GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGG 365
Cdd:cd16143 247 KELEKfghdpsgplrgmkadiyeGG-----------------HRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQ 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 366 SLPQDRVIDGRDLMPLLQGNARHSEHEFLFHYCGSQLHAVR---W--IPKDDSGaVWKAHYVTPVFQPPeaggcyvtslc 440
Cdd:cd16143 310 KLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGSFAIRkgdWklIDGTGSG-GFSYPRGKEKLGLP----------- 377
|
490 500
....*....|....*....|....*.
gi 795629712 441 rcfgeqvtyhnPPLLFDLSRDPSEST 466
Cdd:cd16143 378 -----------PGQLYNLSTDPGESN 392
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
3-493 |
1.79e-77 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 249.02 E-value: 1.79e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVSsgnrrvvHNLAVPAGLPLNETTFAALLKKQGYSTG 82
Cdd:COG3119 48 KTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD-------NGEGYNGGLPPDEPTLAELLKEAGYRTA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 83 LIGKWHqglncdsrsdhchhpynygfdyyygmpftlvdscwpdpsrnteltfesqlwlcvqlvaiavltltfgklsgwvs 162
Cdd:COG3119 121 LFGKWH-------------------------------------------------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 163 vplllifsmilfifllgyawfssytspLYWDcllmrgHEITEqpmkaeragsimvkEAISFLERHRK--EPFLLFFSFLH 240
Cdd:COG3119 127 ---------------------------LYLT------DLLTD--------------KAIDFLERQADkdKPFFLYLAFNA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 241 VHIPLPTTDDFIG-----------------------TSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGG 297
Cdd:COG3119 160 PHAPYQAPEEYLDkydgkdiplppnlaprdlteeelRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 298 HLEA---RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrv 372
Cdd:COG3119 240 SLGEhglRGGKGTLyeGG-----------------IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED-- 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 373 IDGRDLMPLLQGNARHSEHEFLFHY-CGSQLHAVRwipKDDsgavWKAHYVTPVFQPPEaggcyvtslcrcfgeqvtyhn 451
Cdd:COG3119 301 LDGRSLLPLLTGEKAEWRDYLYWEYpRGGGNRAIR---TGR----WKLIRYYDDDGPWE--------------------- 352
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 795629712 452 pplLFDLSRDPSESTPL---TPAteplhdfVIKKVADALKEHRET 493
Cdd:COG3119 353 ---LYDLKNDPGETNNLaadYPE-------VVAELRALLEAWLKE 387
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
4-523 |
1.81e-76 |
|
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: 249.28 E-value: 1.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 4 TPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMV-------SSGnrrvvhnlavpaGLPLNETTFAALLKK 76
Cdd:cd16158 27 TPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYpgvfypgSRG------------GLPLNETTIAEVLKT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 77 QGYSTGLIGKWHQGLNCDSRsdhcHHPYNYGFDYYYGMPFTLvDSCwpdPsrnteltfesqlwlCVQLVAIAVLTLTFGK 156
Cdd:cd16158 95 VGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSH-DQG---P--------------CQNLTCFPPNIPCFGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 157 L-SGWVSVPLLLifsmilfifllgyawfssytsplywdcllmrGHEITEQPMKAERAGSIMVKEAISFLERHRKE--PFL 233
Cdd:cd16158 153 CdQGEVPCPLFY-------------------------------NESIVQQPVDLLTLEERYAKFAKDFIADNAKEgkPFF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 234 LFFSFLHVHIPLPTTDDFIGTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHL--EARRGHAQL--- 308
Cdd:cd16158 202 LYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrKSRGGNAGLlkc 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 309 -------GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIkEPTSLMDILPTVASVSGGSLPqDRVIDGRDLMPL 381
Cdd:cd16158 282 gkgttyeGG-----------------VREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLP-NVTLDGVDMSPI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 382 LQGNARHSEHEFLFHYCGSQ----LHAVRWipkddsgAVWKAHYVT---PVFQPPEAGGCYVTSLcrcfgeqVTYHNPPL 454
Cdd:cd16158 343 LFEQGKSPRQTFFYYPTSPDpdkgVFAVRW-------GKYKAHFYTqgaAHSGTTPDKDCHPSAE-------LTSHDPPL 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795629712 455 LFDLSRDPSESTPLTPATEplHDFVIKKVaDALKEHRETIMpvTYQLSELNQGR-MWLKPCC--GVFPF---CLC 523
Cdd:cd16158 409 LFDLSQDPSENYNLLGLPE--YNQVLKQI-QQVKERFEASM--KFGESEINKGEdPALEPCCkpGCTPKpscCQC 478
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
4-509 |
1.33e-74 |
|
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: 243.91 E-value: 1.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 4 TPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRrvVHNLAVP----AGLPLNETTFAALLKKQGY 79
Cdd:cd16157 27 TPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAH--ARNAYTPqnivGGIPDSEILLPELLKKAGY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 80 STGLIGKWHQGlncdSRSDHchHPYNYGFDYYYGMPftlvdSCWPDPSRNTELtfesqlwlcvqlvaiavltltfgklsg 159
Cdd:cd16157 105 RNKIVGKWHLG----HRPQY--HPLKHGFDEWFGAP-----NCHFGPYDNKAY--------------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 160 wvsvPLLlifsmilfifllgyawfssytsPLYWDCLlMRGHEITEQPMKAERAGS----IMVKEAISFLERHR--KEPFL 233
Cdd:cd16157 147 ----PNI----------------------PVYRDWE-MIGRYYEEFKIDKKTGESnltqIYLQEALEFIEKQHdaQKPFF 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 234 LFFSFLHVHIPLPTTDDFIGTSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGhleARRGHAQLGGWNg 313
Cdd:cd16157 200 LYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGA---ALISAPEQGGSN- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 314 IYKGGKGMGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNarHSEHEF 393
Cdd:cd16157 276 GPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNG--KEKDRP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 394 LFHYCGSQLHAVRWipkddsgAVWKAHYVTpvFQPPEAGGCYVTSLCRcfGEQ---VTYHN------PPLLFDLSRDPSE 464
Cdd:cd16157 354 IFYYRGDELMAVRL-------GQYKAHFWT--WSNSWEEFRKGINFCP--GQNvpgVTTHNqtdhtkLPLLFHLGRDPGE 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 795629712 465 STPLTPATePLHDFVIKKVADALKEHRETIMPVTYQLSELNQGRM 509
Cdd:cd16157 423 KYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLNVCDLAVM 466
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
2-466 |
8.34e-68 |
|
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: 224.40 E-value: 8.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 2 FRTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYpirsgmvsSGNRRVVHNLAVPAGLPL--NETTFAALLKKQGY 79
Cdd:cd16145 24 IKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLH--------TGHTRVRGNSEPGGQDPLppDDVTLAEVLKKAGY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 80 STGLIGKWhqGLNCDSRSDHchhPYNYGFDYYYGmpftlvdscwpdpsrnteltfesqlWLCvQLVAiavltLTFgklsg 159
Cdd:cd16145 96 ATAAFGKW--GLGGPGTPGH---PTKQGFDYFYG-------------------------YLD-QVHA-----HNY----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 160 wvsvpllliFSMILfifllgyaWFSSYTSPLYWDCLLMRGHEITEQPMKAERAGSIMVKEAISFLERHRKEPFLLFFSFL 239
Cdd:cd16145 135 ---------YPEYL--------WRNGEKVPLPNNVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIRENKDKPFFLYLAYT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 240 --HVHIPLPTTD-DFIGTSKHGLYGDN------------VEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEARRG 304
Cdd:cd16145 198 lpHAPLQVPDDGpYKYKPKDPGIYAYLpwpqpekayaamVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSEGGSE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 305 HAQL-----------------GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSL 367
Cdd:cd16145 278 HDPDffdsngplrgykrslyeGG-----------------IRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEP 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 368 PQDrvIDGRDLMPLLQGNARHSEHEFL---FHYCGSQlHAVRWipkDDsgavWKAhyvtpVFQPPEAGgcyvtslcrcfg 444
Cdd:cd16145 341 PED--IDGISLLPTLLGKPQQQQHDYLyweFYEGGGA-QAVRM---GG----WKA-----VRHGKKDG------------ 393
|
490 500
....*....|....*....|..
gi 795629712 445 eqvtyhnPPLLFDLSRDPSEST 466
Cdd:cd16145 394 -------PFELYDLSTDPGETN 408
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
2-377 |
9.87e-63 |
|
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: 205.36 E-value: 9.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 2 FRTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVVHNLAVPAGLPLNETTFAALLKKQGYST 81
Cdd:cd16022 24 IKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVGNGGGLPPDEPTLAELLKEAGYRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 82 GLIGKWHQglncdsrsdhchhpynygfdyyygmpftlvdscwpdpsrnteltfesqlwlcvqlvaiavltltfgklsgwv 161
Cdd:cd16022 96 ALIGKWHD------------------------------------------------------------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 162 svplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaeragsimvkEAISFLERHRKE-PFLLFFSFLH 240
Cdd:cd16022 104 ---------------------------------------------------------EAIDFIERRDKDkPFFLYVSFNA 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 241 VHIPLpttddfigtskhgLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEA---RRGHAQL--GGwngiy 315
Cdd:cd16022 127 PHPPF-------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDhglRGKKGSLyeGG----- 188
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795629712 316 kggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRD 377
Cdd:cd16022 189 ------------IRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
3-466 |
1.15e-59 |
|
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: 202.78 E-value: 1.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQ-HISaaSLCSPSRSAFLTGRYPIRSGMVSSGNRRvvHNLAvpaglpLNETTFAALLKKQGYST 81
Cdd:cd16146 25 KTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGR--ERMR------LDETTLAEVFKDAGYRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 82 GLIGKWHQGLNcdsrsdHCHHPYNYGFDYYYGmpftlvdscwpdpsrnteltfesqlwlcvqlvaiavltltFGklSGWV 161
Cdd:cd16146 95 GIFGKWHLGDN------YPYRPQDRGFDEVLG----------------------------------------HG--GGGI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 162 SVPlllifsmilfifllGYAWFSSYTSPLYWdcllmrgHEITEQPMKaeraG---SIMVKEAISFLERHRKEPFLLFFSF 238
Cdd:cd16146 127 GQY--------------PDYWGNDYFDDTYY-------HNGKFVKTE----GyctDVFFDEAIDFIEENKDKPFFAYLAT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 239 LHVHIPL--PT--TDDFIGTSKH----GLYGdNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHG----------GHLE 300
Cdd:cd16146 182 NAPHGPLqvPDkyLDPYKDMGLDdklaAFYG-MIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGpaggvpkrfnAGMR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 301 ARRGHAQLGGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRDLMP 380
Cdd:cd16146 261 GKKGSVYEGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLP 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 381 LLQGNARHSEHEFLFhycgsqLHAVRWIPKDDS---GAVWKAHY--VTPVFQPPEaggcyvtslcrcfgeqvtyhnpplL 455
Cdd:cd16146 324 LLKGESDPWPERTLF------THSGRWPPPPKKkrnAAVRTGRWrlVSPKGFQPE------------------------L 373
|
490
....*....|.
gi 795629712 456 FDLSRDPSEST 466
Cdd:cd16146 374 YDIENDPGEEN 384
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
2-468 |
5.39e-57 |
|
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: 194.74 E-value: 5.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 2 FRTPHIDRLAREGVQLTqHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVVHNLAVPaglplNETTFAALLKKQGYST 81
Cdd:cd16151 24 YKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNY--------VVFGYLDP-----KQKTFGHLLKDAGYAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 82 GLIGKWHQGLNcDSRSDHCHHpynYGFDYYYgmpftlvdscwpdpsrnteltfesqLWlcvqlvaiavlTLTFGKLSGWv 161
Cdd:cd16151 90 AIAGKWQLGGG-RGDGDYPHE---FGFDEYC-------------------------LW-----------QLTETGEKYS- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 162 svplllifSMILFIFLLGYAWFSSYTSPLYwdcllmrgheiteqpmkaeraGS-IMVKEAISFLERHRKEPFLLFFSFLH 240
Cdd:cd16151 129 --------RPATPTFNIRNGKLLETTEGDY---------------------GPdLFADFLIDFIERNKDQPFFAYYPMVL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 241 VHIPLPTT------DDFIGTSKH--GLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEARR--------- 303
Cdd:cd16151 180 VHDPFVPTpdspdwDPDDKRKKDdpEYFPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSrtngrevrg 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 304 --GHAQLGGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRDLMPL 381
Cdd:cd16151 260 gkGKTTDAG-----------------THVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQ 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 382 LQGNARHSEHEFLFHYcgsqlhAVRWIPKDDSGAVWKAHYvtpvfqppeaggcyvtslcrcfgeqvTYHNPPLLFDLSRD 461
Cdd:cd16151 323 LLGKTGSPRREWIYWY------YRNPHKKFGSRFVRTKRY--------------------------KLYADGRFFDLRED 370
|
....*..
gi 795629712 462 PSESTPL 468
Cdd:cd16151 371 PLEKNPL 377
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-468 |
1.15e-55 |
|
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: 192.01 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 4 TPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRrvvhnlavpagLPLNETTFAALLKKQGYSTGL 83
Cdd:cd16034 27 TPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----------LPPDAPTIADVLKDAGYRTGY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 84 IGKWH----QGLNCDSRSDHCHHPYNYGFDYYYGMpftlvdSCWPDpsrnteltfesqlwlcvqlvaiavltltfgklsg 159
Cdd:cd16034 96 IGKWHldgpERNDGRADDYTPPPERRHGFDYWKGY------ECNHD---------------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 160 wvsvplllifsmilfifllgyawfssYTSPLYWDcllmrgheiTEQPMKAERAGS--IMVKEAISFLERHRKE--PFLLF 235
Cdd:cd16034 136 --------------------------HNNPHYYD---------DDGKRIYIKGYSpdAETDLAIEYLENQADKdkPFALV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 236 FS------------------FLHVHIPLPTTDDFIGTSKHGL-------YGdNVEEMDSMMGKILDAIDDFGLRNNTIVY 290
Cdd:cd16034 181 LSwnpphdpyttapeeyldmYDPKKLLLRPNVPEDKKEEAGLredlrgyYA-MITALDDNIGRLLDALKELGLLENTIVV 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 291 FTSDHGGHLEArrgHAQLG---GWNgiykggkgmggweGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGgsL 367
Cdd:cd16034 260 FTSDHGDMLGS---HGLMNkqvPYE-------------ESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCG--L 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 368 PQDRVIDGRDLMPLLQGNARHSEHEFLFhYCGSQLHAVRWIPKDDSGAVWKAHYvtpvfqppeaggcyvtSLCRCFGeqv 447
Cdd:cd16034 322 PIPDTVEGRDLSPLLLGGKDDEPDSVLL-QCFVPFGGGSARDGGEWRGVRTDRY----------------TYVRDKN--- 381
|
490 500
....*....|....*....|.
gi 795629712 448 tyhNPPLLFDLSRDPSESTPL 468
Cdd:cd16034 382 ---GPWLLFDNEKDPYQLNNL 399
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
4-468 |
6.02e-53 |
|
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: 184.68 E-value: 6.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 4 TPHIDRLAREGVQLTQHISAASlCSPSRSAFLTGRYPIRSGMvssgNRRVVHNlAVPAGLPLNETTFAALLKKQGYSTGL 83
Cdd:cd16029 26 TPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGM----QHGVILA-GEPYGLPLNETLLPQYLKELGYATHL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 84 IGKWHQGlncdsrsdHCHHPY---NYGFDYYYGmpftlvdscwpdpsrnteltfesqlwlcvqlvaiavltltfgklsgw 160
Cdd:cd16029 100 VGKWHLG--------FYTWEYtptNRGFDSFYG----------------------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 161 vsvplllifsmilfiFLLGYAWFSSYTSPLYWDC--LLMRGHEITEQPMKAERAGSIMVKEAISFLERHRK-EPFLLFFS 237
Cdd:cd16029 125 ---------------YYGGAEDYYTHTSGGANDYgnDDLRDNEEPAWDYNGTYSTDLFTDRAVDIIENHDPsKPLFLYLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 238 FLHVHIPLPT----TDDFIGTSKHGLYGD------NVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEA------ 301
Cdd:cd16029 190 FQAVHAPLQVppeyADPYEDKFAHIKDEDrrtyaaMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGgdggsn 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 302 ---RRGHAQL--GGwngiykggkgmggweggIRVPGIVRWPG-KVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDG 375
Cdd:cd16029 270 yplRGGKNTLweGG-----------------VRVPAFVWSPLlPPKRGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 376 RDLMPLLQGNARHSEHEFL----FHYCGSQLHAVRWipKDdsgavWKahYVTpvfqppeaggcyvtslcrcfGEQvtyhn 451
Cdd:cd16029 333 VDQWDALSGGAPSPRTEILlnidDITRTTGGAAIRV--GD-----WK--LIV--------------------GKP----- 378
|
490
....*....|....*..
gi 795629712 452 pplLFDLSRDPSESTPL 468
Cdd:cd16029 379 ---LFNIENDPCERNDL 392
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
389-523 |
7.23e-53 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 175.19 E-value: 7.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 389 SEHEFLFHYCGSQLHAVRWIPkddsgavWKAHYVTPVFQPPEAGGCYVTslcrcfGEQVTYHNPPLLFDLSRDPSESTPL 468
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP-------YKAHFFTPSFDPPGAEGCYGS------KVPVTHHDPPLLFDLERDPSEKYPL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 795629712 469 TPATePLHDFVIKKVADALKEHRETIMPVTYQLSELNQG-RMWLKPCCGVFPFCLC 523
Cdd:pfam14707 68 SPDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLwDPWLQPCCPTFPACTC 122
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
3-492 |
1.08e-50 |
|
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.
Pssm-ID: 293751 [Multi-domain] Cd Length: 373 Bit Score: 178.09 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMvsSGNRRvvHNLAVPAGLPlnetTFAALLKKQGYSTG 82
Cdd:cd16027 24 KTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA--HGLRS--RGFPLPDGVK----TLPELLREAGYYTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 83 LIGKWHQGlncdsrsdhchHPYNYGFDYYYGMPFTLVDSCWPDPSRnteltfesqlwlcvqlvaiavltltfgklsgwvs 162
Cdd:cd16027 96 LIGKTHYN-----------PDAVFPFDDEMRGPDDGGRNAWDYASN---------------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 163 vplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaeragsimvkeAISFLERHRKE-PFLLFFSFLHV 241
Cdd:cd16027 131 ---------------------------------------------------------AADFLNRAKKGqPFFLWFGFHDP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 242 HIPLPTTDDFIGTSK-------------------HGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEar 302
Cdd:cd16027 154 HRPYPPGDGEEPGYDpekvkvppylpdtpevredLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP-- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 303 RGHAQL--GGwngiykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMP 380
Cdd:cd16027 232 RAKGTLydSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLP 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 381 LLQGNARHsEHEFLF---HYCGSQLHAVRWIPKDDsgavWKahYVtpvfqppeaggcyvtslcRCFgeqvtyhNPPLLFD 457
Cdd:cd16027 293 LLKGEKDP-GRDYVFaerDRHDETYDPIRSVRTGR----YK--YI------------------RNY-------MPEELYD 340
|
490 500 510
....*....|....*....|....*....|....*
gi 795629712 458 LSRDPSESTPLtpATEPLHDFVIKKVADALKEHRE 492
Cdd:cd16027 341 LKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
4-364 |
1.48e-47 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 167.21 E-value: 1.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 4 TPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSgnrrvvhnlaVPAGLPLNETTFAALLKKQGYSTGL 83
Cdd:pfam00884 26 TPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS----------TPVGLPRTEPSLPDLLKRAGYNTGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 84 IGKWHQGLNcdSRSDhchhPYNYGFDYYYGmpftlvdscwpdpsrnteltfesqlwlcvqlvaiavltltfgklsgwvsv 163
Cdd:pfam00884 96 IGKWHLGWY--NNQS----PCNLGFDKFFG-------------------------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 164 plllifsmilfiFLLGYAWFS-SYTSPLYWDcllmrGHEITEQpmkaeragsIMVKEAISFLERHrKEPFLLFFSFLHVH 242
Cdd:pfam00884 120 ------------RNTGSDLYAdPPDVPYNCS-----GGGVSDE---------ALLDEALEFLDNN-DKPFFLVLHTLGSH 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 243 IPLPTTDDFIGTSK------------HGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEARRGHAQLGG 310
Cdd:pfam00884 173 GPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGK 252
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 795629712 311 WNGIYKGGkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSG 364
Cdd:pfam00884 253 YDNAPEGG---------YRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
3-489 |
3.54e-43 |
|
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: 159.23 E-value: 3.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGnrrvvhnlavPAGLPLNETTFAALLKKQGYSTG 82
Cdd:cd16031 27 KTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNN----------GPLFDASQPTYPKLLRKAGYQTA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 83 LIGKWHQGLNCDSRSDhchhpynyGFDYYYGMPftlvdscwpdpsrnteltfesqlwlcvqlvaiavltltfgklsgwvs 162
Cdd:cd16031 97 FIGKWHLGSGGDLPPP--------GFDYWVSFP----------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 163 vplllifsmilfifllGYAWfssytsplYWDCLLMRGHEITEQPMKAERagsIMVKEAISFLERHRKE-PFLLFFSFLHV 241
Cdd:cd16031 122 ----------------GQGS--------YYDPEFIENGKRVGQKGYVTD---IITDKALDFLKERDKDkPFCLSLSFKAP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 242 H-----------------IPLPTT---DDFIGTSK-------------------HGLYGDNVE-------EMDSMMGKIL 275
Cdd:cd16031 175 HrpftpaprhrglyedvtIPEPETfddDDYAGRPEwareqrnrirgvldgrfdtPEKYQRYMKdylrtvtGVDDNVGRIL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 276 DAIDDFGLRNNTIVYFTSDHGGHLearrGHAQLGG-WNgiykggkgmgGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMD 354
Cdd:cd16031 255 DYLEEQGLADNTIIIYTSDNGFFL----GEHGLFDkRL----------MYEESIRVPLIIRDPRLIKAGTVVDALVLNID 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 355 ILPTVASVSGGSLPQDrvIDGRDLMPLLQGNARHS-EHEFLFHYCGSQLHAvrWIPKddSGAV----WK-AHYvtpvfqp 428
Cdd:cd16031 321 FAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEYYEEPNFH--NVPT--HEGVrterYKyIYY------- 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795629712 429 peaggcyvtslcrcfgeqvtYHNPPL--LFDLSRDPSESTPLtpATEPLHDFVIKKVADALKE 489
Cdd:cd16031 388 --------------------YGVWDEeeLYDLKKDPLELNNL--ANDPEYAEVLKELRKRLEE 428
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-386 |
4.04e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 153.15 E-value: 4.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRrvvhNLAVPAGLPLNETTFAALLKKQGYSTG 82
Cdd:cd16033 25 KTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVEN----AGAYSRGLPPGVETFSEDLREAGYRNG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 83 LIGKWHQGLNCDsrsdhchhPYNYGFDYYygmpftlvdscwpdpsrNTELTFESqlwlcvqlvaiavltltfgklsgwvs 162
Cdd:cd16033 101 YVGKWHVGPEET--------PLDYGFDEY-----------------LPVETTIE-------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 163 vplllifsmilfifllgyawfssytsplYWdcllmrgheiteqpmkaeragsiMVKEAISFLERHRK--EPFLLFFSFLH 240
Cdd:cd16033 130 ----------------------------YF-----------------------LADRAIEMLEELAAddKPFFLRVNFWG 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 241 VH-----------------IPLPTT--DDFIG-------TSKH-GLYGDN--------------VEEMDSMMGKILDAID 279
Cdd:cd16033 159 PHdpyippepyldmydpedIPLPESfaDDFEDkpyiyrrERKRwGVDTEDeedwkeiiahywgyITLIDDAIGRILDALE 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 280 DFGLRNNTIVYFTSDHGGHLEARRGHAQlgGWNGIYKGGkgmggweggiRVPGIVRWPGKVPAGRLIKEPTSLMDILPTV 359
Cdd:cd16033 239 ELGLADDTLVIFTSDHGDALGAHRLWDK--GPFMYEETY----------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPTI 306
|
410 420
....*....|....*....|....*..
gi 795629712 360 ASVSGGSLPQDrvIDGRDLMPLLQGNA 386
Cdd:cd16033 307 LDLAGVDVPPK--VDGRSLLPLLRGEQ 331
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
3-462 |
3.29e-38 |
|
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: 142.72 E-value: 3.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNrrvvhnlAVPAGLPlnetTFAALLKKQGYSTG 82
Cdd:cd16032 25 KTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-------EFPADIP----TFAHYLRAAGYRTA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 83 LIGKWH-----QglncdsrsdhcHHpynyGFDYyygmpftlvdscwpdpsrNTELTFESQLWLcvqlvaiavltltfgkl 157
Cdd:cd16032 94 LSGKMHfvgpdQ-----------LH----GFDY------------------DEEVAFKAVQKL----------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 158 sgwvsvplllifsmilfifllgyawfssytsplyWDclLMRgheiteqpmkaeragsimvkeaisfleRHRKEPFLLFFS 237
Cdd:cd16032 124 ----------------------------------YD--LAR---------------------------GEDGRPFFLTVS 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 238 FLHVHIPLPTTDDF----IGTSKHGLYGdNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEARrghaqlGGWng 313
Cdd:cd16032 141 FTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGER------GLW-- 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 314 iykggKGMGGWEGGIRVPGIVRWPGKvPAGRLIKEPTSLMDILPTVASVSGGSLPQDRV-IDGRDLMPLLQGNARHSEHE 392
Cdd:cd16032 212 -----YKMSFFEGSARVPLIISAPGR-FAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpLDGRSLLPLLEGGDSGGEDE 285
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 795629712 393 FLFHYCGSQLHA-VRWIPKDDsgavWKahYVtpvfqppeaggcyvtslcrcfgeqVTYHNPPLLFDLSRDP 462
Cdd:cd16032 286 VISEYLAEGAVApCVMIRRGR----WK--FI------------------------YCPGDPDQLFDLEADP 326
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-462 |
1.98e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 140.37 E-value: 1.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrvVHNLAVPagLPLNETTFAALLKKQGYSTG 82
Cdd:cd16037 25 RTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETG---------VWDNADP--YDGDVPSWGHALRAAGYETV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 83 LIGKWHQGLNCDsrsdhchhpyNYGFDYyygmpftlvdscwpdpsrnteltfesqlwlcvqlvaiavltltfgklsgwvs 162
Cdd:cd16037 94 LIGKLHFRGEDQ----------RHGFRY---------------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 163 vplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaERAgsiMVKEAISFLERH--RKEPFLLFFSFLH 240
Cdd:cd16037 112 -----------------------------------------------DRD---VTEAAVDWLREEaaDDKPWFLFVGFVA 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 241 VHIPLPTTDDF----IGTSKHGLYGdNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEARrghaqlGGWNgiyk 316
Cdd:cd16037 142 PHFPLIAPQEFydlyVRRARAAYYG-LVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGER------GLWG---- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 317 ggkGMGGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRviDGRDLMPLLQGNARHSEHEFLFH 396
Cdd:cd16037 211 ---KSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL--DGRSLLPLAEGPDDPDRVVFSEY 284
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795629712 397 YCGSQLHAVRWIPKDDsgavWKAHYvtpvfqppeaggcyvtslcrcfgeqvtYHN-PPLLFDLSRDP 462
Cdd:cd16037 285 HAHGSPSGAFMLRKGR----WKYIY---------------------------YVGyPPQLFDLENDP 320
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
1-468 |
4.01e-37 |
|
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: 141.81 E-value: 4.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 1 CF----RTPHIDRLAREGVQLTQ-HisAASLCSPSRSAFLTGRYPIRSGMvssGNrrVVHNLAVPAG----LPLNETTFA 71
Cdd:cd16025 20 CFggeiPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM---GT--MAELATGKPGyegyLPDSAATIA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 72 ALLKKQGYSTGLIGKWHQGLNcdsrsdhchhpynygfDYYYgmpftlvdscwpdpsrnTELtfesqlwlcvqlvaiavlt 151
Cdd:cd16025 93 EVLKDAGYHTYMSGKWHLGPD----------------DYYS-----------------TDD------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 152 ltfgklsgwvsvplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaeragsiMVKEAISFLERHRKE- 230
Cdd:cd16025 121 ----------------------------------------------------------------LTDKAIEYIDEQKAPd 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 231 -PFLLFFSFLHVHIPLPTTDDFIgtSKH----------------------GLYGDN------------------------ 263
Cdd:cd16025 137 kPFFLYLAFGAPHAPLQAPKEWI--DKYkgkydagwdalreerlerqkelGLIPADtkltprppgvpawdslspeekkle 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 264 ----------VEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGhlEARRGHAQ--------------LGGwngiykggk 319
Cdd:cd16025 215 arrmevyaamVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGA--SAEPGWANasntpfrlykqashEGG--------- 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 320 gmggweggIRVPGIVRWP-GKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRV------IDGRDLMPLLQGNARHSEHE 392
Cdd:cd16025 284 --------IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRR 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 393 FLFHycgsQLHAVRWIPKDDsgavWKAhyvtpvfqppeaggcyvtslcrcfgeqVTYHNPPL------LFDLSRDPSEST 466
Cdd:cd16025 356 TQYF----ELFGNRAIRKGG----WKA---------------------------VALHPPPGwgdqweLYDLAKDPSETH 400
|
..
gi 795629712 467 PL 468
Cdd:cd16025 401 DL 402
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-380 |
4.44e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 138.06 E-value: 4.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 4 TPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIrsgmvssgnrrvvHNLAVPAGLPLNETTFAALLKKQGYSTGL 83
Cdd:cd16148 26 TPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPF-------------YHGVWGGPLEPDDPTLAEILRKAGYYTAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 84 IgkwhqglncdsrSDHCHHPYNYGFDyyygmpftlvdscwpdpsrnteLTFESqlwlcvqlvaiavltltfgklsgwvsv 163
Cdd:cd16148 93 V------------SSNPHLFGGPGFD----------------------RGFDT--------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 164 plllifsmilfifllgyawfssytsplYWDCLLMRGHEITEQPMKAERagsiMVKEAISFLERHRK-EPFllffsFLHVH 242
Cdd:cd16148 112 ---------------------------FEDFRGQEGDPGEEGDERAER----VTDRALEWLDRNADdDPF-----FLFLH 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 243 IPLPttddfigtskHGLYG-DN-VEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHL-EarrgHAQLGGWNgiykggk 319
Cdd:cd16148 156 YFDP----------HEPYLyDAeVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFgE----HGLYWGHG------- 214
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 795629712 320 gMGGWEGGIRVPGIVRWPGKVPAGRlIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMP 380
Cdd:cd16148 215 -SNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SDGRSLLP 271
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
1-491 |
1.34e-36 |
|
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: 141.24 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 1 CFRTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIrsgmvssgNRRVVHNlAVPagLPLNETTFAALLKKQGYS 80
Cdd:cd16028 23 LVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLM--------NHRSVWN-GTP--LDARHLTLALELRKAGYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 81 TGLIGKWHQGLncDSRSDHCHHPYN-------YGFDYYYGMPFTlvdscwpdPSRNTELTFesqlwlcvqlvaIAVLTLT 153
Cdd:cd16028 92 PALFGYTDTSP--DPRGLAPLDPRLlsyelamPGFDPVDRLDEY--------PAEDSDTAF------------LTDRAIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 154 FgkLSGWVSVPLLLIFSmilFI-----FLLGYAWFSSYTSplywdcllmrgheitEQPMKAERAGSIMVKEAI-SFLERH 227
Cdd:cd16028 150 Y--LDERQDEPWFLHLS---YIrphppFVAPAPYHALYDP---------------ADVPPPIRAESLAAEAAQhPLLAAF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 228 RKEPFLLFFSFLH---VHIPLPTTDDFIGTSkHGLygdnVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLearrG 304
Cdd:cd16028 210 LERIESLSFSPGAanaADLDDEEVAQMRATY-LGL----IAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQL----G 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 305 -HAQLG--GWNGIYKggkgmggweggiRVPGIVRWPG---KVPAGRLIKEPTSLMDILPTVASVSGGslPQDRVIDGRDL 378
Cdd:cd16028 281 dHWLWGkdGFFDQAY------------RVPLIVRDPRreaDATRGQVVDAFTESVDVMPTILDWLGG--EIPHQCDGRSL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 379 MPLLQGNarhseheflfhycgsqlhavrwIPKD-DSGAVWKAHYVTPVFQPPEAG------GCyvtSLCRCFGEQVTY-H 450
Cdd:cd16028 347 LPLLAGA----------------------QPSDwRDAVHYEYDFRDVSTRRPQEAlglspdEC---SLAVIRDERWKYvH 401
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 795629712 451 N---PPLLFDLSRDPSESTPLtpATEPLHDFVIKKVADALKEHR 491
Cdd:cd16028 402 FaalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKLLSWR 443
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
3-473 |
3.64e-36 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 140.57 E-value: 3.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNrrvvhnlavpaGLPLN-ETTFAALLKKQGYST 81
Cdd:PRK13759 31 ETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGD-----------VVPWNyKNTLPQEFRDAGYYT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 82 GLIGK--WHQglncdSRSDHchhpynyGFDYyygmpfTLVDSCWPDPSRNTELTFESQ-----LWLCVQLVAIAVLTLTF 154
Cdd:PRK13759 100 QCIGKmhVFP-----QRNLL-------GFHN------VLLHDGYLHSGRNEDKSQFDFvsdylAWLREKAPGKDPDLTDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 155 GklsgwvsvplllifsmilfifllgyawfssytsplyWDCllmrgHEITEQPM-KAER--AGSIMVKEAISFLERH-RKE 230
Cdd:PRK13759 162 G------------------------------------WDC-----NSWVARPWdLEERlhPTNWVGSESIEFLRRRdPTK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 231 PFLLFFSFLHVHIPL-------------PTTDDFIG------------TSKHGLYGD---------------NVEEMDSM 270
Cdd:PRK13759 201 PFFLKMSFARPHSPYdppkryfdmykdaDIPDPHIGdweyaedqdpegGSIDALRGNlgeeyarraraayygLITHIDHQ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 271 MGKILDAIDDFGLRNNTIVYFTSDH----GGHLEARRGHAQLGgwngiykggkgmggwegGIRVPGIVRWPG---KVPAG 343
Cdd:PRK13759 281 IGRFLQALKEFGLLDNTIILFVSDHgdmlGDHYLFRKGYPYEG-----------------SAHIPFIIYDPGgllAGNRG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 344 RLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNAR------HSEHEflfhYCGSQLHavrWIPKDDSGAVW 417
Cdd:PRK13759 344 TVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYEgwrpylHGEHA----LGYSSDN---YLTDGKWKYIW 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 795629712 418 KAHYVTpvfqppeaggcyvtslcrcfgEQvtyhnpplLFDLSRDPSESTPLTPATE 473
Cdd:PRK13759 415 FSQTGE---------------------EQ--------LFDLKKDPHELHNLSPSEK 441
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
3-416 |
1.35e-34 |
|
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: 135.39 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSG-NRRVVHNlavpaglplNETTFAALLKKQGYST 81
Cdd:cd16030 26 KTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNsYFRKVAP---------DAVTLPQYFKENGYTT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 82 GLIGK-WHQGLNCDsrsdhchHPYNYGFDYYYGMPftlvdSCWPDPSRNTELTFESQLWLCvqlvaiavltltfgklsgw 160
Cdd:cd16030 97 AGVGKiFHPGIPDG-------DDDPASWDEPPNPP-----GPEKYPPGKLCPGKKGGKGGG------------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 161 vsvplllifsmilfiflLGYAWfssytsplywdcllmrghEITEQPMKAERAGSImVKEAISFLERHRK--EPFLLFFSF 238
Cdd:cd16030 146 -----------------GGPAW------------------EAADVPDEAYPDGKV-ADEAIEQLRKLKDsdKPFFLAVGF 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 239 LHVHIP-------------------------------------LPTTDDFIGTSKHGLYGD---------------NVEE 266
Cdd:cd16030 190 YKPHLPfvapkkyfdlyplesiplpnpfdpidlpevawndlddLPKYGDIPALNPGDPKGPlpdeqarelrqayyaSVSY 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 267 MDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLearrG-HAQLG---GWNgiykggkgmggweGGIRVPGIVRWPGKVPA 342
Cdd:cd16030 270 VDAQVGRVLDALEELGLADNTIVVLWSDHGWHL----GeHGHWGkhtLFE-------------EATRVPLIIRAPGVTKP 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 343 GRLIKEPTSLMDILPTVASVSGgsLPQDRVIDGRDLMPLLQG-NARHSEHEFL-FHYCGSQLHAVR--------WIPKDD 412
Cdd:cd16030 333 GKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNpSAKWKDAAFSqYPRPSIMGYSIRteryryteWVDFDK 410
|
....
gi 795629712 413 SGAV 416
Cdd:cd16030 411 VGAE 414
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-380 |
9.82e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 120.04 E-value: 9.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSG----MVSSGNRRVVHNLAVPAGlplnETTFAALLKKQG 78
Cdd:cd16149 25 VTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGihdwIVEGSHGKTKKPEGYLEG----QTTLPEVLQDAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 79 YSTGLIGKWHQGlncdsrsdhchhpynygfdyyygmpftlvdscwpdpsrnteltfesqlwlcvqlvaiavltltfgkls 158
Cdd:cd16149 101 YRCGLSGKWHLG-------------------------------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 159 gwvsvplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaeragsimvKEAISFLERH--RKEPFLLFF 236
Cdd:cd16149 113 -----------------------------------------------------------DDAADFLRRRaeAEKPFFLSV 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 237 SFLHVHiplpttddfigtSKHGlYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHG---GH---LEARRGHAQLGG 310
Cdd:cd16149 134 NYTAPH------------SPWG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGfnmGHhgiWGKGNGTFPLNM 200
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 311 WNGIykggkgmggweggIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRDLMP 380
Cdd:cd16149 201 YDNS-------------VKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-488 |
1.44e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 122.67 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQ-HI----SAAsLCSPSRSAFLTGRYpirsgmvssgnrrvVHNL--AVPAGLPLNETTFAALLK 75
Cdd:cd16155 27 QTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRT--------------LFHApeGGKAAIPSDDKTWPETFK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 76 KQGYSTGLIGKWHQGLnCDSRSDHCHHpYNYGFDyyygmPFtlvdscwpdpsrnteltfesqlwlcvqlvaiavltltfg 155
Cdd:cd16155 92 KAGYRTFATGKWHNGF-ADAAIEFLEE-YKDGDK-----PF--------------------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 156 klsgwvsvplllifsmilFIFLlgyawfsSYTSPlywdcllmrgHEITEQPMKAER---AGSIMVKEaiSFLERH--RKE 230
Cdd:cd16155 126 ------------------FMYV-------AFTAP----------HDPRQAPPEYLDmypPETIPLPE--NFLPQHpfDNG 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 231 PFLLFFSFLHvhiPLPTTDDFIgtSKH-GLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHG---GHlearrgHA 306
Cdd:cd16155 169 EGTVRDEQLA---PFPRTPEAV--RQHlAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGlavGS------HG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 307 QLGGWNgiykggkgmgGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDrvIDGRDLMPLLQGNA 386
Cdd:cd16155 238 LMGKQN----------LYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES--VEGKSLLPVIRGEK 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 387 RhSEHEFLF-HYCGSQlhavRWIPKDDsgavWKAHYVTPvfqppeaggcyvtslcrcfGEQVTyhnppLLFDLSRDPSES 465
Cdd:cd16155 305 K-AVRDTLYgAYRDGQ----RAIRDDR----WKLIIYVP-------------------GVKRT-----QLFDLKKDPDEL 351
|
490 500
....*....|....*....|...
gi 795629712 466 TPLtpATEPLHDFVIKKVADALK 488
Cdd:cd16155 352 NNL--ADEPEYQERLKKLLAELK 372
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
5-397 |
5.04e-29 |
|
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: 116.92 E-value: 5.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 5 PHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVssgnrrvvHNLAVPAGLPLNET--TFAALLKKQGYSTG 82
Cdd:cd16035 27 PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT--------DTLGSPMQPLLSPDvpTLGHMLRAAGYYTA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 83 LIGKWHqgLncdsrSDHCHHPYNYgfdyyygmpftlvdscwpDPsrnteltfesqlwlcvqlvaiavltltfgklsgwvs 162
Cdd:cd16035 99 YKGKWH--L-----SGAAGGGYKR------------------DP------------------------------------ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 163 vplllifsmilfifllgyawfssytsplywdcllmrghEITEQpmkaeragsimvkeAISFLERHRK-----EPFLLFFS 237
Cdd:cd16035 118 --------------------------------------GIAAQ--------------AVEWLRERGAknadgKPWFLVVS 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 238 FL--H-VHIPLPTTDDFIgtSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEARRGHAQLGgwngi 314
Cdd:cd16035 146 LVnpHdIMFPPDDEERWR--RFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGF----- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 315 ykggkgmGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVID----GRDLMPLLQGNARHS- 389
Cdd:cd16035 219 -------NAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATEApplpGRDLSPLLTDADADAv 291
|
....*...
gi 795629712 390 EHEFLFHY 397
Cdd:cd16035 292 RDGILFTY 299
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-490 |
1.64e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 116.94 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 4 TPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnrrVVHNlAVPagLPLNETTFAALLKKQGYSTGL 83
Cdd:cd16152 27 TPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETG--------CFRN-GIP--LPADEKTLAHYFRDAGYETGY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 84 IGKWHqglncdsrsdhchhpynygfdyyygmpftlvdscwpdpsrnteltfesqlwlcvqlvaiavltltfgklsgwvsv 163
Cdd:cd16152 96 VGKWH--------------------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 164 plllifsmilfifLLGYawfssytsplywdcllmRGHEITEQpmkaeragsimvkeAISFL-ERHRKEPFLLFFSFLHVH 242
Cdd:cd16152 101 -------------LAGY-----------------RVDALTDF--------------AIDYLdNRQKDKPFFLFLSYLEPH 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 243 ----------------------IPlPTTDDFIGTSKHGL---YGdNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGG 297
Cdd:cd16152 137 hqndrdryvapegsaerfanfwVP-PDLAALPGDWAEELpdyLG-CCERLDENVGRIRDALKELGLYDNTIIVFTSDHGC 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 298 HLEARRG------HaqlggwngiykggkgmggwEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDr 371
Cdd:cd16152 215 HFRTRNAeykrscH-------------------ESSIRVPLVIYGPG-FNGGGRVEELVSLIDLPPTLLDAAGIDVPEE- 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 372 vIDGRDLMPLLQGNARHSEHEFLFHYCGSQL-HAVRwipkddsGAVWKahYVtpVFQPPEAGGCYVTSLcrcfgeqvTYH 450
Cdd:cd16152 274 -MQGRSLLPLVDGKVEDWRNEVFIQISESQVgRAIR-------TDRWK--YS--VAAPDKDGWKDSGSD--------VYV 333
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 795629712 451 nPPLLFDLSRDPSESTPLtpATEPLHdfviKKVADALKEH 490
Cdd:cd16152 334 -EDYLYDLEADPYELVNL--IGRPEY----REVAAELRER 366
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
5-376 |
1.72e-27 |
|
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: 114.18 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 5 PHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPirsgmvssGNRRVVHNLAVPAGLP------LNETTFAALLKKQG 78
Cdd:cd16147 24 KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYA--------HNHGVTNNSPPGGGYPkfwqngLERSTLPVWLQEAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 79 YSTGLIGKWhqgLN-CDSRSDHCHHPYnyGFDYYYGMPftlvdscwpDPSRNTELTfesqlwlcvqlvaiavltLTFGKL 157
Cdd:cd16147 96 YRTAYAGKY---LNgYGVPGGVSYVPP--GWDEWDGLV---------GNSTYYNYT------------------LSNGGN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 158 SGwvsvplllifsmilfiflLGYAWFSSYTSPLYwdcllmrgheiteqpmkAERAgsimvkeaISFLERHRK--EPFLLF 235
Cdd:cd16147 144 GK------------------HGVSYPGDYLTDVI-----------------ANKA--------LDFLRRAAAddKPFFLV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 236 FSFLHVHIPL-----------------PTTDDFIGTS--KHGL------------YGDNV--------EEMDSMMGKILD 276
Cdd:cd16147 181 VAPPAPHGPFtpapryanlfpnvtappRPPPNNPDVSdkPHWLrrlpplnptqiaYIDELyrkrlrtlQSVDDLVERLVN 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 277 AIDDFGLRNNTIVYFTSDHGGHLearrG-HAQLGGwngiykggkGMGGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDI 355
Cdd:cd16147 261 TLEATGQLDNTYIIYTSDNGYHL----GqHRLPPG---------KRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDL 326
|
410 420
....*....|....*....|.
gi 795629712 356 LPTVASVSGGSLPQDrvIDGR 376
Cdd:cd16147 327 APTILDLAGAPPPSD--MDGR 345
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
4-382 |
4.53e-24 |
|
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: 105.16 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 4 TPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSgnrrvvhNLAvpagLPLNETTFAALLKKQGYSTGL 83
Cdd:cd16156 26 TPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTN-------CMA----LGDNVKTIGQRLSDNGIHTAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 84 IGKWHqglnCDSrSDH-----ChhPYNYGFDYYYGMpftlvdscwpdpsRN--TELTFESQlwlcvqlvaiavltltfgk 156
Cdd:cd16156 95 IGKWH----LDG-GDYfgngiC--PQGWDPDYWYDM-------------RNylDELTEEER------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 157 lsgwvsvplllifsmilfifllgYAWFSSYTSplywdcllMRGHEITEQPMKAERagsiMVKEAISFLERHRKEPFLLFF 236
Cdd:cd16156 136 -----------------------RKSRRGLTS--------LEAEGIKEEFTYGHR----CTNRALDFIEKHKDEDFFLVV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 237 SFLHVH----IPLPTTD---DFIGTSKHGLYgDNVEE---------------------------------MDSMMGKILD 276
Cdd:cd16156 181 SYDEPHhpflCPKPYASmykDFEFPKGENAY-DDLENkplhqrlwagakphedgdkgtikhplyfgcnsfVDYEIGRVLD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 277 AIDDfgLRNNTIVYFTSDHGGHLEARRGHAQlggwngiykggkGMGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDIL 356
Cdd:cd16156 260 AADE--IAEDAWVIYTSDHGDMLGAHKLWAK------------GPAVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLA 325
|
410 420
....*....|....*....|....*.
gi 795629712 357 PTVASVSGgsLPQDRVIDGRDLMPLL 382
Cdd:cd16156 326 PTILDYAG--IPQPKVLEGESILATI 349
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-378 |
5.52e-23 |
|
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: 98.99 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGMVssGNRRVvHNlAVPAGLPlnetTFAALLKKQGYSTG 82
Cdd:cd16153 36 ESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY--GFEAA-HP-ALDHGLP----TFPEVLKKAGYQTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 83 LIGKwhqglncdsrsdhchhpynygfdyyygmpftlvdscwpdpsrnteltfesqlwlcvqlvaiavltltfgklsgwvs 162
Cdd:cd16153 108 SFGK---------------------------------------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 163 vplllifsmilfiflLGYAWFSSYTsplywdcllmrgheitEQPMKAERAGSIMVKEAISflerhRKEPFLLFFSFLHVH 242
Cdd:cd16153 112 ---------------SHLEAFQRYL----------------KNANQSYKSFWGKIAKGAD-----SDKPFFVRLSFLQPH 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 243 IP-LPTTD-----DFIGTSKHGlygdnveemDSMMGKILDAIDDFGL---RNNTIVYFTSDHGGHLEARRGHAQLGGWNg 313
Cdd:cd16153 156 TPvLPPKEfrdrfDYYAFCAYG---------DAQVGRAVEAFKAYSLkqdRDYTIVYVTGDHGWHLGEQGILAKFTFWP- 225
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795629712 314 iykggkgmggweGGIRVPGIVRWPGK--VPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRDL 378
Cdd:cd16153 226 ------------QSHRVPLIVVSSDKlkAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL 280
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
211-360 |
1.43e-21 |
|
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: 93.64 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 211 RAGSIMVKEAISFLERHRkePFLLFFSFLHVHIPLPTTDdfigtSKHGLYGDNVEEMDSMMGKILDAIDDFGLRNNTIVY 290
Cdd:cd00016 102 RTGVIGLLKAIDETSKEK--PFVLFLHFDGPDGPGHAYG-----PNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVII 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 291 FTSDHGGHLEarrGHAQLGGwngiykGGKGMGGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVA 360
Cdd:cd00016 175 VTADHGGIDK---GHGGDPK------ADGKADKSHTGMRVPFIAYGPG-VKKGGVKHELISQYDIAPTLA 234
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-464 |
1.03e-20 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 94.61 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSGmvssgnRRVVHNLavpagLPLNETTFAALLKKQGYSTG 82
Cdd:cd16150 25 VTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG------HRTLHHL-----LRPDEPNLLKTLKDAGYHVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 83 LIGKWHqglncdsrsdhchhpynygfdyyygmpftlvdsCWPDPsrnteltfesqlwlcvqlvaiavltltfgklsgwvs 162
Cdd:cd16150 94 WAGKND---------------------------------DLPGE------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 163 vplllifsmilfifllgyAWFSSYTSplyWDCLlmrgheiteqpmkaeragsiMVKEAISFLERHR-KEPFLLFFSFLHV 241
Cdd:cd16150 105 ------------------FAAEAYCD---SDEA--------------------CVRTAIDWLRNRRpDKPFCLYLPLIFP 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 242 HIPLPTTDDF--------------------------IGTSKHGLYGDN--------------VEEMDSMMGKILDAIDDF 281
Cdd:cd16150 144 HPPYGVEEPWfsmidreklpprrppglrakgkpsmlEGIEKQGLDRWSeerwrelratylgmVSRLDHQFGRLLEALKET 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 282 GLRNNTIVYFTSDHGGHLearrG-HAQLGGWngiykggkGMGGWEGGIRVPGIVRwPGKVPAGRLIKEPTSLMDILPTVA 360
Cdd:cd16150 224 GLYDDTAVFFFSDHGDYT----GdYGLVEKW--------PNTFEDCLTRVPLIIK-PPGGPAGGVSDALVELVDIPPTLL 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 361 SVSGgsLPQDRVIDGRDLMPLLQG------NARHSEHEFLFHycGSQLHAVRWIPKDDsgavwKAHYVTPVFQPPEAGGC 434
Cdd:cd16150 291 DLAG--IPLSHTHFGRSLLPVLAGeteehrDAVFSEGGRLHG--EEQAMEGGHGPYDL-----KWPRLLQQEEPPEHTKA 361
|
490 500 510
....*....|....*....|....*....|....
gi 795629712 435 YVtslCRcfGEQVTY----HNPPLLFDLSRDPSE 464
Cdd:cd16150 362 VM---IR--TRRYKYvyrlYEPDELYDLEADPLE 390
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-384 |
3.24e-19 |
|
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: 89.33 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 4 TPHIDRLAREGVQLTqHISAASLCSPSRSAFLTGRYPIRSGMvssgnrrvvhnLAVPAGLPLNETTFAALLKKQ----GY 79
Cdd:cd16154 28 TPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGV-----------LAVPDELLLSEETLLQLLIKDattaGY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 80 STGLIGKWHQGlNCDSrsdhchHPYNYG-FDYYYGMPFTLVDSCWPDPSRNTELTFESQLWLCVQLVAIAVltltfgkls 158
Cdd:cd16154 96 SSAVIGKWHLG-GNDN------SPNNPGgIPYYAGILGGGVQDYYNWNLTNNGQTTNSTEYATTKLTNLAI--------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 159 gwvsvplllifsmilfifllgyAWFSSYTSPLY-WdcllmrgheiteqpmkaeragsimvkeaISFLERHrkEPFLLFFS 237
Cdd:cd16154 160 ----------------------DWIDQQTKPWFlW----------------------------LAYNAPH--TPFHLPPA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 238 FLHVHIPLPTTDDfIGTSKHGLYGDNVEEMDSMMGKILDAIDDfGLRNNTIVYFTSDHGGHLEAR-----RGHAQ----L 308
Cdd:cd16154 188 ELHSRSLLGDSAD-IEANPRPYYLAAIEAMDTEIGRLLASIDE-EERENTIIIFIGDNGTPGQVVdlpytRNHAKgslyE 265
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795629712 309 GGwngiykggkgmggweggIRVPGIVRWPGkvpAGRLIKEPTSLM---DILPTVASVSGGSLPQdrVIDGRDLMPLLQG 384
Cdd:cd16154 266 GG-----------------INVPLIVSGAG---VERANERESALVnatDLYATIAELAGVDAAE--IHDSVSFKPLLSD 322
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
218-463 |
5.38e-17 |
|
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: 82.59 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 218 KEAISFlerhrKEPFLLFfsfLHVHIPLPTTDDFIGTSKHGL------YGDNVEEMDSMMGKILDAIDDFGLRNNTIVYF 291
Cdd:cd16171 158 KEAPNL-----TQPFALY---LGLNLPHPYPSPSMGENFGSIrnirafYYAMCAETDAMLGEIISALKDTGLLDKTYVFF 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 292 TSDHGghlEARRGHAQLggwngiykggKGMGGWEGGIRVPGIVRWPGkVPAGRLIKEPTSLMDILPTVASVSGGSLPQDr 371
Cdd:cd16171 230 TSDHG---ELAMEHRQF----------YKMSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 372 vIDGRDLMPLLQGNARHSEHEFLFH-------YCGSQLHAVRWIPKDDSgavWKahYVTpvfqppeaggcYVTslcrcfG 444
Cdd:cd16171 295 -LSGYSLLPLLSESSIKESPSRVPHpdwvlseFHGCNVNASTYMLRTNS---WK--YIA-----------YAD------G 351
|
250
....*....|....*....
gi 795629712 445 EQVtyhnPPLLFDLSRDPS 463
Cdd:cd16171 352 NSV----PPQLFDLSKDPD 366
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
183-358 |
2.09e-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: 59.92 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 183 FSS--YTSPLYWDCLLmrgHEITEQPMKAERAG----SIMVKEAISFL-ERHRKEPFllfFSFL-------------HVH 242
Cdd:COG3083 330 FSSagFNSPLFRQTIF---SDVSLPRLHTPGGPaqrdRQITAQWLQWLdQRDSDRPW---FSYLfldaphaysfpadYPK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 243 IPLPTTD-DFIGTSKHG-------LYGDNVEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHL----EARRGHAqlGG 310
Cdd:COG3083 404 PFQPSEDcNYLALDNESdptpfknRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnengQNYWGHN--SN 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 795629712 311 WNgiykggkgmggwEGGIRVPGIVRWPGKVPagRLIKEPTSLMDILPT 358
Cdd:COG3083 482 FS------------RYQLQVPLVIHWPGTPP--QVISKLTSHLDIVPT 515
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
4-379 |
3.25e-08 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 56.20 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 4 TPHIDRLAREGVQLTQHISAASLCSPSRSAFLTGRYPIRSG--MVSSGNRRVvhnlavpaglplneTTFAALLKKQGYST 81
Cdd:COG1368 260 TPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGspYKRPGQNNF--------------PSLPSILKKQGYET 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 82 gligkwhqglncdsrsdHCHHPYNYGFD----YYYGMPF-TLVD-SCWPDPSRNteltfesqlwlcvqlvaiavltltfg 155
Cdd:COG1368 326 -----------------SFFHGGDGSFWnrdsFYKNLGFdEFYDrEDFDDPFDG-------------------------- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 156 klsGWVsvplllifsmilfifllgyawfssytsplYWDcllmrgheiteqpmkaeragSIMVKEAISFLERHrKEPFLLF 235
Cdd:COG1368 363 ---GWG-----------------------------VSD--------------------EDLFDKALEELEKL-KKPFFAF 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 236 FSFLHVHIP--LPTTDDFIGTSKHGLYGDN---VEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEARRghaqlgg 310
Cdd:COG1368 390 LITLSNHGPytLPEEDKKIPDYGKTTLNNYlnaVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKT------- 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795629712 311 wngiykggkGMGGWEGGIRVPGIVrWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIdGRDLM 379
Cdd:COG1368 463 ---------DYENPLERYRVPLLI-YSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
4-364 |
6.68e-08 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 54.23 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 4 TPHIDRLAREGVQLTQHISAASLCSPSRS--AFLTGRYPIRSGMVSSgNRRVVHNLavpaglplneTTFAALLKKQGYST 81
Cdd:cd16015 26 TPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSY-TLYKLNPL----------PSLPSILKEQGYET 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 82 GLIgkwhqglncdsrsdHCHHPYNY---------GFDYYYGMpftlvdSCWPDPSRNTeltfesqlwlcvqlvaiavltl 152
Cdd:cd16015 95 IFI--------------HGGDASFYnrdsvypnlGFDEFYDL------EDFPDDEKET---------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 153 tfgklSGWVsvplllifsmilfifllgyawfssytsplYWDcllmrgheiteqpmkaeragSIMVKEAISFLERHRKEPF 232
Cdd:cd16015 133 -----NGWG-----------------------------VSD--------------------ESLFDQALEELEELKKKPF 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 233 LLFFSFLHVHIPLPTTDDFIGTSKHGLYGDN--------VEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHGGHLEarrg 304
Cdd:cd16015 159 FIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTelenylnaIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLG---- 234
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 305 haqlggwngiYKGGKGMGGWEGGIRVPGIVRWPGKVPAGRlIKEPTSLMDILPTVASVSG 364
Cdd:cd16015 235 ----------SDYDETDEDPLDLYRTPLLIYSPGLKKPKK-IDRVGSQIDIAPTLLDLLG 283
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
2-296 |
9.51e-07 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 50.90 E-value: 9.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 2 FRTPHIDRLAREGVQLTQHISAA-SLCSPSRSAFLTGRYPIRSGMVSSG------NRRVVHNLAVPAGLPLNE----TTF 70
Cdd:COG1524 42 AHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGLYPGEHGIVGNGwydpelGRVVNSLSWVEDGFGSNSllpvPTI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 71 AALLKKQGYSTGLIGKWHQGlncDSRSDHCHHPYNY-GFDYYYGMPFTlvdscwpdpsrnteltfesqlwlcvqlvaiav 149
Cdd:COG1524 122 FERARAAGLTTAAVFWPSFE---GSGLIDAARPYPYdGRKPLLGNPAA-------------------------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 150 ltltfgklsgwvsvplllifsmilfifllgyawfssytsplywdcllmrgheiteqpmkaeraGSIMVKEAISFLERHRk 229
Cdd:COG1524 167 ---------------------------------------------------------------DRWIAAAALELLREGR- 182
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 795629712 230 ePFLLFFSFLHVhiplpttdDFIGtSKHGLYGDN----VEEMDSMMGKILDAIDDFGLRNNTIVYFTSDHG 296
Cdd:COG1524 183 -PDLLLVYLPDL--------DYAG-HRYGPDSPEyraaLREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
223-302 |
7.69e-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: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 223 FLERHRKEP-FLLFFSFLHVHiplpttDDFIGTSKhglygdnveeMDSMMGKILDAIDDFGLRNNTIVYFTSDHG----- 296
Cdd:pfam02995 284 FLPRYRDSPfFGFFWSNSLSH------DDFNYASA----------LDEDFLKYLKKLHKRGLLDNTIVIFMSDHGlrfgk 347
|
90
....*....|..
gi 795629712 297 ------GHLEAR 302
Cdd:pfam02995 348 lrrtsqGMLEER 359
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
3-296 |
5.22e-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: 42.41 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 3 RTPHIDRLAREGVQLTQHISAA-SLCSPSRSAFLTGRYPIRSGMVS------SGNRRVVHNLAVP-AGLPLNETTFAALL 74
Cdd:pfam01663 19 LTPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVGntfydpKTGEYLVFVISDPeDPRWWQGEPIWDTA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 75 KKQGYSTGLIGkWhqglncdSRSDHCHHPYNYGFDYYYGMPFtlvdscwpdpsrNTELTFEsqlwlcvqlvaiavltltf 154
Cdd:pfam01663 99 AKAGVRAAALF-W-------PGSEVDYSTYYGTPPRYLKDDY------------NNSVPFE------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795629712 155 GKLSGWVSvplllifsmilfifllgYAWFSSytsplywdcllmrgheiteqpmkaeragsimvkeaiSFLERHRKEPFLL 234
Cdd:pfam01663 140 DRVDTAVL-----------------QTWLDL------------------------------------PFADVAAERPDLL 166
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795629712 235 FFSFLHVhiplpttdDFIGtSKHGLYGDNVEEM----DSMMGKILDAIDDFGLRNNTIVYFTSDHG 296
Cdd:pfam01663 167 LVYLEEP--------DYAG-HRYGPDSPEVEDAlrrvDRAIGDLLEALDERGLFEDTNVIVVSDHG 223
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
256-296 |
3.33e-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: 3.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 795629712 256 KHGLYGDNV----EEMDSMMGKILDAIDDFGLRNNTIVYFTSDHG 296
Cdd:cd16018 173 KYGPDSPEVnealKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG 217
|
|
| AP-SPAP |
cd16016 |
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
250-298 |
7.50e-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: 7.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 795629712 250 DFIGTSkhglYGDNVEEM-------DSMMGKILDAIDDFGLRNNTIVYFTSDHGGH 298
Cdd:cd16016 218 DYIGHA----FGPNSVEMedtylrlDRDLARLLDALDKKVGKGNYLVFLTADHGAA 269
|
|
| |
