|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
25-458 |
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: 745.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVGVFLFSA 104
Cdd:cd16159 2 PNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHHPLSHGFDYFYGLTMTNLRDCKLGQGSVFLKGTEKSI 184
Cdd:cd16159 82 SSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 185 VTSIQIFGITLLSLATVHFIGFlkVPFQALGYCLLITAILLVVLLFFFYNFRYLNCFLMRNHQIIQQPLSYENLTQRLTK 264
Cdd:cd16159 162 PLLTAFVLITALTIFLLLYLGA--VSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLTK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 265 EAVQFIGRNTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAH 344
Cdd:cd16159 240 EAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 345 VEEISSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDRIIDGHDL 424
Cdd:cd16159 320 LEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDL 399
|
410 420 430
....*....|....*....|....*....|....
gi 1444497660 425 MPLLQGKIIQSKHEFLFHYCNAYLNAVRWHPRNS 458
Cdd:cd16159 400 MPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDG 433
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
25-455 |
1.51e-174 |
|
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: 496.32 E-value: 1.51e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAaysrvGVFLFSA 104
Cdd:cd16026 2 PNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLP-----GVVGPPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndFCHHPLSHGFDYFYGLTMTNLRDCKLGQGsvflkgteksi 184
Cdd:cd16026 77 SKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQ------PEFLPTRHGFDEYFGIPYSNDMWPFPLYR----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 185 vtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffYNFRYLNCFLMRNHQIIQQPLSYENLTQRLTK 264
Cdd:cd16026 140 ------------------------------------------------NDPPGPLPPLMENEEVIEQPADQSSLTQRYTD 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 265 EAVQFIGRNTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAH 344
Cdd:cd16026 172 EAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPW 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 345 VEEISssgevHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDRIIDGHDL 424
Cdd:cd16026 252 LEYGG-----HGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDI 326
|
410 420 430
....*....|....*....|....*....|.
gi 1444497660 425 MPLLQGKIIQSKHEFLFHYCNAYLNAVRWHP 455
Cdd:cd16026 327 SPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR 357
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
25-455 |
6.93e-131 |
|
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: 387.17 E-value: 6.93e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMaaYSRVGVFLFSa 104
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGM--YGGTRVFLPW- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHHPLSHGFDyFYGltmTNLRdcklgqgsvflkgteksi 184
Cdd:cd16160 79 DIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVG---TNLP------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 185 vtsiqiFGITLLSLATVHFIGFlkvPFQALgycllitaillvvllfffynfrylnCFLMRNHQIIQQPLSYENLTQRLTK 264
Cdd:cd16160 137 ------FTNSWACDDTGRHVDF---PDRSA-------------------------CFLYYNDTIVEQPIQHEHLTETLVG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 265 EAVQFIGRNTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAH 344
Cdd:cd16160 183 DAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPH 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 345 VEEISssgevHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYiDEPTSNMDIFPTVIKLAGAQLPCDRIIDGHDL 424
Cdd:cd16160 263 VEYCL-----EGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIKPRVS-HEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSI 336
|
410 420 430
....*....|....*....|....*....|.
gi 1444497660 425 MPLLQGKiIQSKHEFLFHYCNAYLNAVRWHP 455
Cdd:cd16160 337 TDLLLGE-ADSPHDDILYYCCSRLMAVRYGS 366
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
25-443 |
8.81e-108 |
|
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: 326.81 E-value: 8.81e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVGVFLFSA 104
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 -------SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndFCHHPLSHGFDYFYGltmtnlrDCKLGQGSVFl 177
Cdd:cd16144 81 tklipppSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGE------GGYGPEDQGFDVNIG-------GTGNGGPPSY- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 178 kgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllFFFYNFRYLNcflmrnhqiIQQPLSYEN 257
Cdd:cd16144 147 ----------------------------------------------------YFPPGKPNPD---------LEDGPEGEY 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 258 LTQRLTKEAVQFIGRNTDAPFLLILSYLHVHTALYASKNFI-----------GKSKHGLYGDAVEEMDWSVGRILDVLEK 326
Cdd:cd16144 166 LTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELIekyekkkkglrKGQKNPVYAAMIESLDESVGRILDALEE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 327 SNLNNKTLVYFTSDQGAHveeisSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVI 406
Cdd:cd16144 246 LGLADNTLVIFTSDNGGL-----STRGGPPTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFL 320
|
410 420 430
....*....|....*....|....*....|....*...
gi 1444497660 407 KLAGAQLPCDRIIDGHDLMPLLQGKIIQSKHEFLF-HY 443
Cdd:cd16144 321 ELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFwHF 358
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-452 |
7.68e-102 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 310.66 E-value: 7.68e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 1 MRLLSFLIICqCAIKSLSSHSASNPNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAF 80
Cdd:COG3119 1 MKRLLLLLLA-LLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 81 LTGRYPIRSGMAaysrvgvFLFSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLgmncessndfchhplshgfdyfygl 160
Cdd:COG3119 80 LTGRYPHRTGVT-------DNGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 161 tmtnlrdcklgqgsvflkgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylnc 240
Cdd:COG3119 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 241 flmrnhqiiqqplsyeNLTQRLTKEAVQFIGRNT--DAPFLLILSYLHVHTALYASKNFIGK------------------ 300
Cdd:COG3119 128 ----------------YLTDLLTDKAIDFLERQAdkDKPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlt 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 301 -----SKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAHVEEisssgevHGgyngiYKGGKSMNWEGGIR 375
Cdd:COG3119 192 eeelrRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGE-------HG-----LRGGKGTLYEGGIR 259
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444497660 376 VPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKIIQSKHEFLFHYCNAYLN-AVR 452
Cdd:COG3119 260 VPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNrAIR 335
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
25-454 |
7.37e-99 |
|
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: 305.91 E-value: 7.37e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMaaYSrvGVFlFSA 104
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGV--YP--GVF-YPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSndfcHHPLSHGFDYFYGltmtnlrdcklgqgsvflkgteksi 184
Cdd:cd16158 77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLG------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 185 vtsiqifgitllslatvhfigflkVPF-QALGYCLLITAILLVVLLFFFYNFRYLNCFLMRNHQIIQQPLSYENLTQRLT 263
Cdd:cd16158 128 ------------------------IPYsHDQGPCQNLTCFPPNIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 264 KEAVQFIGRNT--DAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQ 341
Cdd:cd16158 184 KFAKDFIADNAkeGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDN 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 342 GAhveeiSSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIdEPTSNMDIFPTVIKLAGAQLPcDRIIDG 421
Cdd:cd16158 264 GP-----STMRKSRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLP-NVTLDG 336
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1444497660 422 HDLMPLL--QGKiiqSKHEFLFHY-----CNAYLNAVRWH 454
Cdd:cd16158 337 VDMSPILfeQGK---SPRQTFFYYptspdPDKGVFAVRWG 373
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
25-452 |
3.98e-97 |
|
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: 301.31 E-value: 3.98e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGM---AAYSRVGvFL 101
Cdd:cd16157 2 PNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFyttNAHARNA-YT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 102 FSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCEssndfcHHPLSHGFDYFYGLTmtnlrDCKLGQgsvflkgte 181
Cdd:cd16157 81 PQNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NCHFGP--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 182 ksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllffFYNFRYLNCFLMRNHQIIQQplSYE----- 256
Cdd:cd16157 141 --------------------------------------------------YDNKAYPNIPVYRDWEMIGR--YYEefkid 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 257 ------NLTQRLTKEAVQFIGR--NTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSN 328
Cdd:cd16157 169 kktgesNLTQIYLQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 329 LNNKTLVYFTSDQGAHVeeisSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKL 408
Cdd:cd16157 249 IENNTFVFFSSDNGAAL----ISAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLAL 324
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1444497660 409 AGAQLPCDRIIDGHDLMP-LLQGKIIQSKHeflFHYCNAYLNAVR 452
Cdd:cd16157 325 AGLPIPSDRAIDGIDLLPvLLNGKEKDRPI---FYYRGDELMAVR 366
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
25-454 |
1.57e-95 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 293.67 E-value: 1.57e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYG---NRTLRTPNIDRLAKEGVTLTQHIAaSPLCTPSRAAFLTGRYPIRSGMaaySRVGvfl 101
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYV-EPSCTPGRAAFITGRHPIRTGL---TTVG--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 102 FSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCEssndfcHHPLSHGFDYFYGltmtnlrdcklgqgsvflkgte 181
Cdd:cd16142 74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDG------RLPTDHGFDEFYG---------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 182 ksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfFFYNFrylncflmrnhqiiqqplsyenLTQR 261
Cdd:cd16142 126 -------------------------------------------------NLYHT----------------------IDEE 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 262 LTKEAVQFIGRN--TDAPFLLILSYLHVHTALYASKNFIGKSK-HGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFT 338
Cdd:cd16142 135 IVDKAIDFIKRNakADKPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFT 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 339 SDQGAHVEEISSSGevhggyNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLP---- 414
Cdd:cd16142 215 TDNGPEQDVWPDGG------YTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkl 288
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1444497660 415 --CDRIIDGHDLMPLLQGKIIQSKHEFLFHYCNAYLNAVRWH 454
Cdd:cd16142 289 lgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWK 330
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
25-442 |
1.93e-94 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 291.80 E-value: 1.93e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYG-NRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSgmaaYSRVGVFLFS 103
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRS----RLKGGVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 104 ASSGgLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHH----------------PLSHGFDYFYGLTMTNLRD 167
Cdd:cd16143 77 SPPL-IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIPASEVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 168 cklgqgsvflkgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhq 247
Cdd:cd16143 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 248 iiqqplsyenltqRLTKEAVQFIGRN--TDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLE 325
Cdd:cd16143 156 -------------TLTDKAVEFIDQHakKDKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALK 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 326 KSNLNNKTLVYFTSDQGAHVEEISSSGEVHGGY-NGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPT 404
Cdd:cd16143 223 ELGLAENTLVIFTSDNGPSPYADYKELEKFGHDpSGPLRGMKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFAT 302
|
410 420 430
....*....|....*....|....*....|....*...
gi 1444497660 405 VIKLAGAQLPCDRIIDGHDLMPLLQGKIIQSKHEFLFH 442
Cdd:cd16143 303 LAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH 340
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
25-442 |
5.63e-90 |
|
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: 280.12 E-value: 5.63e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLR-TPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAaysrvGVFLfS 103
Cdd:cd16161 2 PNFLLLFADDLGWGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVG-----HNFL-P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 104 ASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNcESsndfcHHPLSHGFDYFYGLtmtnlrdcklgqgsvflkgteks 183
Cdd:cd16161 76 TSVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQR-EA-----YLPNSRGFDYYFGI----------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 184 ivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiqqPLSYE-NLTQRL 262
Cdd:cd16161 127 --------------------------------------------------------------------PFSHDsSLADRY 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 263 TKEAVQFIGRNTDA--PFLLILSYLHVHTAL-YASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTS 339
Cdd:cd16161 139 AQFATDFIQRASAKdrPFFLYAALAHVHVPLaNLPRFQSPTSGRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTS 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 340 DQGAHVEEISSSGEVHGGY---NGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCD 416
Cdd:cd16161 219 DNGPWEVKCELAVGPGTGDwqgNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPG 298
|
410 420
....*....|....*....|....*.
gi 1444497660 417 RIIDGHDLMPLLQGKiIQSKHEFLFH 442
Cdd:cd16161 299 RIYDGKDLSPVLFGG-SKTGHRCLFH 323
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
25-455 |
4.27e-89 |
|
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: 278.66 E-value: 4.27e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQ-HiaASPLCTPSRAAFLTGRYPIRSGmaaysrvgvfLFS 103
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfH--VSPVCAPTRAALLTGRYPFRTG----------VWH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 104 ASSGG--LPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndFCHHPLSHGFDYFYGltmtnlrdckLGQGSVflkgte 181
Cdd:cd16146 69 TILGRerMRLDETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLG----------HGGGGI------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 182 ksivtsIQIFGitllslatvhfigflkvpfqalgycllitaillvvllffFYNFRYLNCFLMRNHQIIQqplsYEN-LTQ 260
Cdd:cd16146 127 ------GQYPD---------------------------------------YWGNDYFDDTYYHNGKFVK----TEGyCTD 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 261 RLTKEAVQFIGRNTDAPFLLILSYLHVHTALYA----SKNFIGKSKH----GLYGdAVEEMDWSVGRILDVLEKSNLNNK 332
Cdd:cd16146 158 VFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVpdkyLDPYKDMGLDdklaAFYG-MIENIDDNVGRLLAKLKELGLEEN 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 333 TLVYFTSDQGahveeisSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQ 412
Cdd:cd16146 237 TIVIFMSDNG-------PAGGVPKRFNAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVK 309
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1444497660 413 LPCDRIIDGHDLMPLLQGKIIQSKHEFLF-HYCNAYLNAVRWHP 455
Cdd:cd16146 310 LPEGIKLDGRSLLPLLKGESDPWPERTLFtHSGRWPPPPKKKRN 353
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
25-441 |
7.51e-86 |
|
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: 270.23 E-value: 7.51e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVGVFLfsa 104
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 ssgGLPSEEITFSKLLKQRGYSTALIGKWHLGmnCESSNDfchHPLSHGFDYFYGltmtnlrdcklgqgsvFLKgteksi 184
Cdd:cd16145 78 ---PLPPDDVTLAEVLKKAGYATAAFGKWGLG--GPGTPG---HPTKQGFDYFYG----------------YLD------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 185 vtsiQIFGitllslatvHFigflkvpfqalgycllitaillvvllFFFYnfrylncFLMRNHQIIQQPLSYENL------ 258
Cdd:cd16145 128 ----QVHA---------HN--------------------------YYPE-------YLWRNGEKVPLPNNVIPPldegnn 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 259 ---------TQRLTKEAVQFIGRNTDAPFLLILSYL---------HVHTALYASKNFIGKSKHGL------YGDAVEEMD 314
Cdd:cd16145 162 agggggtysHDLFTDEALDFIRENKDKPFFLYLAYTlphaplqvpDDGPYKYKPKDPGIYAYLPWpqpekaYAAMVTRLD 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 315 WSVGRILDVLEKSNLNNKTLVYFTSDQGAHVE-EISSSGEVHGGyNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYID 393
Cdd:cd16145 242 RDVGRILALLKELGIDENTLVVFTSDNGPHSEgGSEHDPDFFDS-NGPLRGYKRSLYEGGIRVPFIARWPGKIPAGSVSD 320
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1444497660 394 EPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKIIQSKHEFLF 441
Cdd:cd16145 321 HPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLY 366
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
25-423 |
1.49e-78 |
|
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: 245.04 E-value: 1.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPirsgmaaySRVGVFLFSA 104
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYP--------HRHGVRGNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHlgmncessndfchhplshgfdyfygltmtnlrdcklgqgsvflkgteksi 184
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 185 vtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiqqplsyenltqrltK 264
Cdd:cd16022 103 -------------------------------------------------------------------------------D 103
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 265 EAVQFIGRN-TDAPFLLILSYLHVHTALYasknfigkskhglYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGA 343
Cdd:cd16022 104 EAIDFIERRdKDKPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 344 HVEEisssgevHGGyngiyKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPcdRIIDGHD 423
Cdd:cd16022 171 MLGD-------HGL-----RGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPP--EGLDGRS 236
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
25-443 |
4.23e-75 |
|
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: 241.69 E-value: 4.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAAsPLCTPSRAAFLTGRYPIRSGMaaYSRVgvfLFSA 104
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGM--QHGV---ILAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMnceSSNDFChhPLSHGFDYFYGltmtnlrdcklgqgsvFLKGTEksi 184
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLGF---YTWEYT--PTNRGFDSFYG----------------YYGGAE--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 185 vtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfFFYNFR------YLNCFLMRNHQIiqqPLSYEN- 257
Cdd:cd16029 131 ----------------------------------------------DYYTHTsggandYGNDDLRDNEEP---AWDYNGt 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 258 -LTQRLTKEAVQFIGR-NTDAPFLLILSYLHVHTALYASKNFI----GKSKHGLYGD------AVEEMDWSVGRILDVLE 325
Cdd:cd16029 162 ySTDLFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLQVPPEYAdpyeDKFAHIKDEDrrtyaaMVSALDESVGNVVDALK 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 326 KSNLNNKTLVYFTSDQGAHVeeisssGEVHGGYNGIYKGGKSMNWEGGIRVPGlLLWPGVI--QAGTYIDEPTSNMDIFP 403
Cdd:cd16029 242 AKGMLDNTLIVFTSDNGGPT------GGGDGGSNYPLRGGKNTLWEGGVRVPA-FVWSPLLppKRGTVSDGLMHVTDWLP 314
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1444497660 404 TVIKLAGAQLPCDRIIDGHDLMPLLQGKIIQSKHEFLFHY 443
Cdd:cd16029 315 TLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNI 354
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-443 |
8.31e-69 |
|
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: 224.79 E-value: 8.31e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTqHIAASPLCTPSRAAFLTGRYPIRSGMaaysrvgVFlfsa 104
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYV-------VF---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 ssGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNdfchHPLSHGFDYFYGLTMTNLRDCKLGQGSV-FLKGTEKS 183
Cdd:cd16151 69 --GYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGD----YPHEFGFDEYCLWQLTETGEKYSRPATPtFNIRNGKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 184 IVTSIQIFGITLLSlatvhfigflkvpfqalgycllitaillvvllfffynfRYLNcflmrnhqiiqqplsyenltqrlt 263
Cdd:cd16151 143 LETTEGDYGPDLFA--------------------------------------DFLI------------------------ 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 264 keavQFIGRNTDAPFLLILSYLHVHT----------ALYASKNFIGKSKHglYGDAVEEMDWSVGRILDVLEKSNLNNKT 333
Cdd:cd16151 161 ----DFIERNKDQPFFAYYPMVLVHDpfvptpdspdWDPDDKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 334 LVYFTSDQGAHveeisssGEVHGGYNG-IYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQ 412
Cdd:cd16151 235 IIIFTGDNGTH-------RPITSRTNGrEVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAP 307
|
410 420 430
....*....|....*....|....*....|.
gi 1444497660 413 LPCDRIIDGHDLMPLLQGKIIQSKHEFLFHY 443
Cdd:cd16151 308 LPEDYPLDGRSFAPQLLGKTGSPRREWIYWY 338
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
25-411 |
1.80e-67 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 218.83 E-value: 1.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVgvflfsa 104
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPV------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 ssgGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSndfchhPLSHGFDYFYGL--TMTNLRDCKlgqgsvflkgtek 182
Cdd:pfam00884 74 ---GLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFGRntGSDLYADPP------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 183 sivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllFFFYNFRYLNCflmrnhqiiqqplsyenLTQRL 262
Cdd:pfam00884 132 -----------------------------------------------DVPYNCSGGGV-----------------SDEAL 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 263 TKEAVQFIGRNTDaPFLLILSYLHVHTALYASKNFIGKSK------------HGLYGDAVEEMDWSVGRILDVLEKSNLN 330
Cdd:pfam00884 148 LDEALEFLDNNDK-PFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLL 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 331 NKTLVYFTSDQGAHVEEisssgevhggYNGIYKGGKSMN-WEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLA 409
Cdd:pfam00884 227 DNTLVVYTSDHGESLGE----------GGGYLHGGKYDNaPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLA 296
|
..
gi 1444497660 410 GA 411
Cdd:pfam00884 297 GI 298
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-441 |
3.49e-66 |
|
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: 218.59 E-value: 3.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVgvflfsa 104
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 ssggLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHH----PLSHGFDYFYGltmtnlrdcklgqgsvflkgt 180
Cdd:cd16034 75 ----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKG--------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 181 eksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllFFFYNfRYLNCFLMRNHQIIQQPLSYEnlTQ 260
Cdd:cd16034 130 -------------------------------------------------YECNH-DHNNPHYYDDDGKRIYIKGYS--PD 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 261 RLTKEAVQFIGR--NTDAPFLLILSYLHVHT----------ALYASKN---------------FIGKSKHGLYGdAVEEM 313
Cdd:cd16034 158 AETDLAIEYLENqaDKDKPFALVLSWNPPHDpyttapeeylDMYDPKKlllrpnvpedkkeeaGLREDLRGYYA-MITAL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 314 DWSVGRILDVLEKSNLNNKTLVYFTSDqgaHveeisssGEVHGGYNGIYKGgksmNW-EGGIRVPGLLLWPGVIQAGTYI 392
Cdd:cd16034 237 DDNIGRLLDALKELGLLENTIVVFTSD---H-------GDMLGSHGLMNKQ----VPyEESIRVPFIIRYPGKIKAGRVV 302
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1444497660 393 DEPTSNMDIFPTVIKLAGaqLPCDRIIDGHDLMPLLQGKIIQSKHEFLF 441
Cdd:cd16034 303 DLLINTVDIMPTLLGLCG--LPIPDTVEGRDLSPLLLGGKDDEPDSVLL 349
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
25-443 |
8.21e-65 |
|
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: 215.86 E-value: 8.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMaaysrvgVFLFSA 104
Cdd:cd16031 3 PNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGV-------TDNNGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SsggLPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndfcHHPLSHGFDYFYGLTmtnlrdcklGQGSvflkgteksi 184
Cdd:cd16031 76 L---FDASQPTYPKLLRKAGYQTAFIGKWHLGSG--------GDLPPPGFDYWVSFP---------GQGS---------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 185 vtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrYLNCFLMRNHQIIQQplsYENLTQRLTK 264
Cdd:cd16031 126 ----------------------------------------------------YYDPEFIENGKRVGQ---KGYVTDIITD 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 265 EAVQFIGRNTDA-PFLLILSYLHVHT--------------------ALYASKNFIGKSK---------HGLYGD------ 308
Cdd:cd16031 151 KALDFLKERDKDkPFCLSLSFKAPHRpftpaprhrglyedvtipepETFDDDDYAGRPEwareqrnriRGVLDGrfdtpe 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 309 -----------AVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGGYngiykgGKSMNWEGGIRVP 377
Cdd:cd16031 231 kyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL------GE-HGLF------DKRLMYEESIRVP 297
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444497660 378 GLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKIIQS-KHEFLFHY 443
Cdd:cd16031 298 LIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEY 362
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
25-445 |
2.34e-57 |
|
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: 194.65 E-value: 2.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIgDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAysrvgvflFSA 104
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHG--------LRS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHlgMNCESSNDFCHHPLSHGFDYFYG-LTMTNLRDcklgqgsvFLKGTEKs 183
Cdd:cd16027 72 RGFPLPDGVKTLPELLREAGYYTGLIGKTH--YNPDAVFPFDDEMRGPDDGGRNAwDYASNAAD--------FLNRAKK- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 184 ivtsiqifgitllslatvhfigflKVPFqalgycllitaillvvllFFFYNFRYlncflmrNHQiIQQPLSYENLTQRLT 263
Cdd:cd16027 141 ------------------------GQPF------------------FLWFGFHD-------PHR-PYPPGDGEEPGYDPE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 264 KEAVQFIGRNTDApfllilsyLHVHTALYAsknfigkskhglygDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGa 343
Cdd:cd16027 171 KVKVPPYLPDTPE--------VREDLADYY--------------DEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 344 hveeisssgevhggynGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPcdRIIDGHD 423
Cdd:cd16027 228 ----------------MPFPRAKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPP--EYLQGRS 289
|
410 420
....*....|....*....|..
gi 1444497660 424 LMPLLQGKiIQSKHEFLFHYCN 445
Cdd:cd16027 290 FLPLLKGE-KDPGRDYVFAERD 310
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
25-456 |
2.13e-52 |
|
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: 182.26 E-value: 2.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRtLRTPNIDRLAKEGVTLTQ-HiaASPLCTPSRAAFLTGRYPIRSGMA--AYSRVGvfl 101
Cdd:cd16025 3 PNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGMGtmAELATG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 102 FSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndfchhplshgfDYFygltmtnlrdcklgqgsvflkgte 181
Cdd:cd16025 77 KPGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------------DYY------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 182 ksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiqqplsyenLTQR 261
Cdd:cd16025 117 ----------------------------------------------------------------------------STDD 120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 262 LTKEAVQFI--GRNTDAPFLLILSYLHVHTALYASKNFIGKSKhGLYG---DA--------------------------- 309
Cdd:cd16025 121 LTDKAIEYIdeQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYK-GKYDagwDAlreerlerqkelglipadtkltprppg 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 310 -------------------------VEEMDWSVGRILDVLEKSN-LNNkTLVYFTSDQGAhveeissSGEVHGGY--NGI 361
Cdd:cd16025 200 vpawdslspeekklearrmevyaamVEHMDQQIGRLIDYLKELGeLDN-TLIIFLSDNGA-------SAEPGWANasNTP 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 362 YKGGKSMNWEGGIRVPGLLLWPGVIQA-GTYIDEPTSNMDIFPTVIKLAGAQLPcDRI-------IDGHDLMPLLQGKII 433
Cdd:cd16025 272 FRLYKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHVIDIAPTILELAGVEYP-KTVngvpqlpLDGVSLLPTLDGAAA 350
|
490 500 510
....*....|....*....|....*....|
gi 1444497660 434 QSKHEFLF--HYCNAYL-----NAVRWHPR 456
Cdd:cd16025 351 PSRRRTQYfeLFGNRAIrkggwKAVALHPP 380
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-426 |
3.33e-51 |
|
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: 174.73 E-value: 3.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYP--------IRSGMAAYSR 96
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPsqhgihdwIVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 97 VGVflfsassgGLPSEEITFSKLLKQRGYSTALIGKWHLGmncessndfchhplshgfdyfygltmtnlrdcklgqgsvf 176
Cdd:cd16149 81 KPE--------GYLEGQTTLPEVLQDAGYRCGLSGKWHLG---------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 177 lkgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfRYLNCFLMRNHQiiqqplsye 256
Cdd:cd16149 113 -----------------------------------------------------------DDAADFLRRRAE--------- 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 257 nltqrltkeavqfigrnTDAPFLLILSYLHVHtalyasknfigkSKHGlYGDAVEEMDWSVGRILDVLEKSNLNNKTLVY 336
Cdd:cd16149 125 -----------------AEKPFFLSVNYTAPH------------SPWG-YFAAVTGVDRNVGRLLDELEELGLTENTLVI 174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 337 FTSDqgahveeisssgevHG---GYNGIY-KG-GKS-MN-WEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLA 409
Cdd:cd16149 175 FTSD--------------NGfnmGHHGIWgKGnGTFpLNmYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELA 240
|
410
....*....|....*..
gi 1444497660 410 GAQLPCDRIIDGHDLMP 426
Cdd:cd16149 241 GVDPPADPRLPGRSFAD 257
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
25-431 |
3.61e-47 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 166.21 E-value: 3.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPirsgmaaySRVGVFLFSA 104
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLP--------SRIGAYDNAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SsggLPSEEITFSKLLKQRGYSTALIGKWHlgmncessndFCHHPLSHGFDYfygltmtnlrDcklgqgsvflkgtEksi 184
Cdd:cd16032 73 E---FPADIPTFAHYLRAAGYRTALSGKMH----------FVGPDQLHGFDY----------D-------------E--- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 185 vtsiqifgitllslatvhfigflKVPFQAlgycllitaillvvllfffynfrylncflmrnhqiiqqplsyenlTQRLTK 264
Cdd:cd16032 114 -----------------------EVAFKA---------------------------------------------VQKLYD 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 265 EAvqfiGRNTDAPFLLILSYLHVHTALYASKNF----IGKSKHGLYGdAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSD 340
Cdd:cd16032 126 LA----RGEDGRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSD 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 341 QGAHVeeisssGEvHGGYngiYKggksMNW-EGGIRVPGLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLAGAQL-PCDRI 418
Cdd:cd16032 201 HGDML------GE-RGLW---YK----MSFfEGSARVPLIISAPGRFAPRR-VAEPVSLVDLLPTLVDLAGGGTaPHVPP 265
|
410
....*....|...
gi 1444497660 419 IDGHDLMPLLQGK 431
Cdd:cd16032 266 LDGRSLLPLLEGG 278
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-430 |
2.72e-46 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 163.87 E-value: 2.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPirsgmaaySRVGVFlfsA 104
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYV--------HETGVW---D 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGmncesSNDFChhplsHGFDYfygltmtnlrdcklgqgsvflkgteksi 184
Cdd:cd16037 70 NADPYDGDVPSWGHALRAAGYETVLIGKLHFR-----GEDQR-----HGFRY---------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 185 vtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiqqplsyenlTQRLTK 264
Cdd:cd16037 112 --------------------------------------------------------------------------DRDVTE 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 265 EAVQFIGRN--TDAPFLLILSYLHVHTALYASKNFIGKSKHGL---YGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTS 339
Cdd:cd16037 118 AAVDWLREEaaDDKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTS 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 340 DQGAHVeeisssgevhgGYNGIYkgGKSMNWEGGIRVPGLLLWPGvIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDRii 419
Cdd:cd16037 198 DHGDML-----------GERGLW--GKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL-- 261
|
410
....*....|.
gi 1444497660 420 DGHDLMPLLQG 430
Cdd:cd16037 262 DGRSLLPLAEG 272
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
25-430 |
3.36e-44 |
|
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: 161.20 E-value: 3.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGiGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPirsgmaaySRVGVFLFSA 104
Cdd:cd16030 3 PNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRP--------DTTGVYDNNS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SSGGLPSEEITFSKLLKQRGYSTALIGK-WHlGMNCESSND------FCHHPLSHGFDYFYGLTMTNLRDCKLGQGSVFL 177
Cdd:cd16030 74 YFRKVAPDAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDpaswdePPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 178 KGTEKSIVTSIQI--FGITLLS----------LAtvhfIGFLK--VPFQA---------LGYCLLITAILLVVLLFFFYN 234
Cdd:cd16030 153 ADVPDEAYPDGKVadEAIEQLRklkdsdkpffLA----VGFYKphLPFVApkkyfdlypLESIPLPNPFDPIDLPEVAWN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 235 fRYLNCFLMRNHQIIQQPLSYENLTQRLTKEAVQfigrntdapfllilSYlhvhtalYASknfigkskhglygdaVEEMD 314
Cdd:cd16030 229 -DLDDLPKYGDIPALNPGDPKGPLPDEQARELRQ--------------AY-------YAS---------------VSYVD 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 315 WSVGRILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGGYngiykgGKSMNWEGGIRVPglLLW--PGVIQAGTYI 392
Cdd:cd16030 272 AQVGRVLDALEELGLADNTIVVLWSDHGWHL------GE-HGHW------GKHTLFEEATRVP--LIIraPGVTKPGKVT 336
|
410 420 430
....*....|....*....|....*....|....*...
gi 1444497660 393 DEPTSNMDIFPTVIKLAGaqLPCDRIIDGHDLMPLLQG 430
Cdd:cd16030 337 DALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKN 372
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-432 |
8.09e-43 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 157.00 E-value: 8.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMaaYSRVGVFLfsA 104
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGV--LNNVENAG--A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGmNCESSNDFC---HHPLSHGFDYFYG-LTMTNLRDCKLGQGSVFLkgt 180
Cdd:cd16033 77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVG-PEETPLDYGfdeYLPVETTIEYFLAdRAIEMLEELAADDKPFFL--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 181 eksivtsiqifgitllslaTVHFIG-----FLKVPFqalgycllitaillvvllfffynfrylncFLMRNHQIIQQPLSY 255
Cdd:cd16033 153 -------------------RVNFWGphdpyIPPEPY-----------------------------LDMYDPEDIPLPESF 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 256 ENltQRLTKEAVQfigRNTDAPFLLILSYLHVHtalyasKNFIGKskhglYGDAVEEMDWSVGRILDVLEKSNLNNKTLV 335
Cdd:cd16033 185 AD--DFEDKPYIY---RRERKRWGVDTEDEEDW------KEIIAH-----YWGYITLIDDAIGRILDALEELGLADDTLV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 336 YFTSDQGAHVeeisssGEvHGGYNgiyKgGKSMnWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAqlPC 415
Cdd:cd16033 249 IFTSDHGDAL------GA-HRLWD---K-GPFM-YEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGV--DV 314
|
410
....*....|....*..
gi 1444497660 416 DRIIDGHDLMPLLQGKI 432
Cdd:cd16033 315 PPKVDGRSLLPLLRGEQ 331
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-426 |
1.82e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 149.24 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLgIGD-LGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIrsgmaaYSRVGVFLfs 103
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPF------YHGVWGGP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 104 assggLPSEEITFSKLLKQRGYSTALIGkwhlgmncessnDFCHHPLSHGFDyfygltmtnlrdcklgQGsvflkgteks 183
Cdd:cd16148 72 -----LEPDDPTLAEILRKAGYYTAAVS------------SNPHLFGGPGFD----------------RG---------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 184 ivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllFFFYNFRylncflmRNHQIIQQPLSYENlTQRLT 263
Cdd:cd16148 109 ----------------------------------------------FDTFEDF-------RGQEGDPGEEGDER-AERVT 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 264 KEAVQFIGRN-TDAPFLLILSYLHVHtALYasknfigkskhgLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQG 342
Cdd:cd16148 135 DRALEWLDRNaDDDPFFLFLHYFDPH-EPY------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 343 ahvEEIsssGEvhggyNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLAGAQLPcdRIIDGH 422
Cdd:cd16148 202 ---EEF---GE-----HGLYWGHGSNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPP--DYSDGR 267
|
....
gi 1444497660 423 DLMP 426
Cdd:cd16148 268 SLLP 271
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-445 |
1.64e-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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 141.55 E-value: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 23 SNPNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQ-HIAAS---PLCTPSRAAFLTGRYpirsgmaaysrvg 98
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNMGGwsgAVCVPSRAMLMTGRT------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 99 vfLFSASSGG---LPSEEITFSKLLKQRGYSTALIGKWHlgmncessNDFCHHPLShgfdyfygltmtnlrdcklgqgsv 175
Cdd:cd16155 68 --LFHAPEGGkaaIPSDDKTWPETFKKAGYRTFATGKWH--------NGFADAAIE------------------------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 176 FLKGTEKSivtsiqifgitllslatvhfigflKVPFqalgycllitaillvvllfffynFRYLnCFL------------- 242
Cdd:cd16155 114 FLEEYKDG------------------------DKPF-----------------------FMYV-AFTaphdprqappeyl 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 243 -MRNHQIIQQPLSYENLTqrlTKEAVQFIGRntD---APFLLILSYLHVHTALYasknfigkskhglYGdAVEEMDWSVG 318
Cdd:cd16155 146 dMYPPETIPLPENFLPQH---PFDNGEGTVR--DeqlAPFPRTPEAVRQHLAEY-------------YA-MITHLDAQIG 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 319 RILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGGYngiykgGKSMNWEGGIRVPGLLLWPGvIQAGTYIDEPTSN 398
Cdd:cd16155 207 RILDALEASGELDNTIIVFTSDHGLAV------GS-HGLM------GKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYL 272
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1444497660 399 MDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKiIQSKHEFLF-HYCN 445
Cdd:cd16155 273 QDVFPTLCELAGIEIPES--VEGKSLLPVIRGE-KKAVRDTLYgAYRD 317
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
25-431 |
1.29e-35 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 138.26 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGiGD-LGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVGVFLFs 103
Cdd:PRK13759 7 PNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVPWNY- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 104 assgglpseEITFSKLLKQRGYSTALIGKWHLgmncessndfchHP--LSHGFDYfygltmTNLRDCKLGQGSVFLKGTE 181
Cdd:PRK13759 85 ---------KNTLPQEFRDAGYYTQCIGKMHV------------FPqrNLLGFHN------VLLHDGYLHSGRNEDKSQF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 182 KSIVTSIQIFGItllslatvhfigflkvpfQALGYCLLITAIllvvllfffynfrYLNCflmrnHQIIQQPLSY-ENL-- 258
Cdd:PRK13759 138 DFVSDYLAWLRE------------------KAPGKDPDLTDI-------------GWDC-----NSWVARPWDLeERLhp 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 259 TQRLTKEAVQFI-GRNTDAPFLLILSYLHVH------------------------------------TALYASKNFIGK- 300
Cdd:PRK13759 182 TNWVGSESIEFLrRRDPTKPFFLKMSFARPHspydppkryfdmykdadipdphigdweyaedqdpegGSIDALRGNLGEe 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 301 ----SKHGLYGDaVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDqgaHveeisssGEVHGGYngiYKGGKSMNWEGGIRV 376
Cdd:PRK13759 262 yarrARAAYYGL-ITHIDHQIGRFLQALKEFGLLDNTIILFVSD---H-------GDMLGDH---YLFRKGYPYEGSAHI 327
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1444497660 377 PGLLLWPG---VIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGK 431
Cdd:PRK13759 328 PFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQ 383
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-424 |
4.38e-35 |
|
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: 132.50 E-value: 4.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGN----------RTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSgmaay 94
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRT----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 95 srvGVFLFSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGmncessndfchhplshgfdyfygltmtnlrdcklgqgs 174
Cdd:cd16153 77 ---GVYGFEAAHPALDHGLPTFPEVLKKAGYQTASFGKSHLE-------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 175 vflkgteksivtsiqifgitllslatvhfigflkvPFQalgycllitaillvvllfffynfRYLNcflmrnhqiiQQPLS 254
Cdd:cd16153 116 -----------------------------------AFQ-----------------------RYLK----------NANQS 127
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 255 YENLTQRLTKeavqfiGRNTDAPFLLILSYLHVHTALYASKNFIGK-SKHGL--YGDAVeemdwsVGRILDVLEKSNLNN 331
Cdd:cd16153 128 YKSFWGKIAK------GADSDKPFFVRLSFLQPHTPVLPPKEFRDRfDYYAFcaYGDAQ------VGRAVEAFKAYSLKQ 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 332 K---TLVYFTSDQGAHVeeisssgevhgGYNGIYkgGKSMNWEGGIRVPGLLLWPGVIQ--AGTYIDEPTSNMDIFPTVI 406
Cdd:cd16153 196 DrdyTIVYVTGDHGWHL-----------GEQGIL--AKFTFWPQSHRVPLIVVSSDKLKapAGKVRHDFVEFVDLAPTLL 262
|
410
....*....|....*...
gi 1444497660 407 KLAGAQLPCDRIIDGHDL 424
Cdd:cd16153 263 AAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-432 |
7.99e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 133.89 E-value: 7.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPirsgmaaySRVGVFlfsA 104
Cdd:cd16152 2 PNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYP--------TETGCF---R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGmncessndfchhplshgfdyfygltmtnlrdcklgqgsvflkgteksi 184
Cdd:cd16152 71 NGIPLPADEKTLAHYFRDAGYETGYVGKWHLA------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 185 vtsiqifgitllslatvhfigflkvpfqalGYcllitaillvvllfffynfRylncflmrnhqiiqqplsyenlTQRLTK 264
Cdd:cd16152 103 ------------------------------GY-------------------R----------------------VDALTD 111
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 265 EAVQFI-GRNTDAPFLLILSYLHVH----------TALYASK---NFIGKSKHGLYGDA----------VEEMDWSVGRI 320
Cdd:cd16152 112 FAIDYLdNRQKDKPFFLFLSYLEPHhqndrdryvaPEGSAERfanFWVPPDLAALPGDWaeelpdylgcCERLDENVGRI 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 321 LDVLEKSNLNNKTLVYFTSDQGAHVEEisssgevhggYNGIYKggKSMNwEGGIRVPGLLLWPGvIQAGTYIDEPTSNMD 400
Cdd:cd16152 192 RDALKELGLYDNTIIVFTSDHGCHFRT----------RNAEYK--RSCH-ESSIRVPLVIYGPG-FNGGGRVEELVSLID 257
|
410 420 430
....*....|....*....|....*....|..
gi 1444497660 401 IFPTVIKLAGAQLPCDriIDGHDLMPLLQGKI 432
Cdd:cd16152 258 LPPTLLDAAGIDVPEE--MQGRSLLPLVDGKV 287
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
25-414 |
1.50e-34 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 133.83 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLgigDLGCYGNRTLRtPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPirsgmaaySRVGVFLFSA 104
Cdd:cd16147 2 PNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYA--------HNHGVTNNSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SSGGLPS------EEITFSKLLKQRGYSTALIGKWhlgMN-CESSNDFCHHPLshGFDYFYGLTMtnlrdcklgqgsvfl 177
Cdd:cd16147 70 PGGGYPKfwqnglERSTLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVPP--GWDEWDGLVG--------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 178 kgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffyNFRYLNCFLmRNHQIIQQPLSYEN 257
Cdd:cd16147 130 --------------------------------------------------------NSTYYNYTL-SNGGNGKHGVSYPG 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 258 --LTQRLTKEAVQFIGR--NTDAPFLLILSYL--HV-------HTALYA--------SKNFIGKS--KHGL--------- 305
Cdd:cd16147 153 dyLTDVIANKALDFLRRaaADDKPFFLVVAPPapHGpftpaprYANLFPnvtapprpPPNNPDVSdkPHWLrrlpplnpt 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 306 ---YGD-----------AVEEMdwsVGRILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGgyngiYKGGKSMNWE 371
Cdd:cd16147 233 qiaYIDelyrkrlrtlqSVDDL---VERLVNTLEATGQLDNTYIIYTSDNGYHL------GQ-HR-----LPPGKRTPYE 297
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1444497660 372 GGIRVPGLLLWPGvIQAGTYIDEPTSNMDIFPTVIKLAGAQLP 414
Cdd:cd16147 298 EDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPP 339
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
25-409 |
2.75e-34 |
|
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: 129.08 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTL-TQHIAASPLCTPSRAAFLTGRYPIRSGMAAYSRVGVFLFS 103
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 104 aSSGGLPSEEITFSKLLKQRGYSTALIGkwhlgmncessndfchhplshgfdyfygltmtnlrdcklgqgsvflkgteks 183
Cdd:cd00016 81 -RAAGKDEDGPTIPELLKQAGYRTGVIG---------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 184 ivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiqqplsyenltqrlt 263
Cdd:cd00016 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 264 keAVQFIGRNTDA-PFLLILSYLHVHTALYASKnfigkSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQG 342
Cdd:cd00016 108 --LLKAIDETSKEkPFVLFLHFDGPDGPGHAYG-----PNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHG 180
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444497660 343 AHVEEisssgevHGGYNGiyKGGKSMNWEGGIRVPGLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLA 409
Cdd:cd00016 181 GIDKG-------HGGDPK--ADGKADKSHTGMRVPFIAYGPGVKKGGV-KHELISQYDIAPTLADLL 237
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
25-441 |
2.56e-33 |
|
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: 131.23 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGiGD-LGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAaysRVGVflfs 103
Cdd:cd16028 1 RNVLFITADQWR-ADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV---WNGT---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 104 assgGLPSEEITFSKLLKQRGYSTALIGKWHL-----GMNCESSNDFCHHPLSHGFDyfYGLTMTNLRDcklgqgsvflk 178
Cdd:cd16028 73 ----PLDARHLTLALELRKAGYDPALFGYTDTspdprGLAPLDPRLLSYELAMPGFD--PVDRLDEYPA----------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 179 gtEKSIVTSIqifgitllslaTVHFIGFLKV----PFqalgyCLLITAIllvvllfffynfrylncflmRNHQIIQQPLS 254
Cdd:cd16028 136 --EDSDTAFL-----------TDRAIEYLDErqdePW-----FLHLSYI--------------------RPHPPFVAPAP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 255 YENLTQrltKEAVQFIGRNTDA-------PFlliLSYLHVHtalYASKNFIGKSKHGLYGDA-------------VEEMD 314
Cdd:cd16028 178 YHALYD---PADVPPPIRAESLaaeaaqhPL---LAAFLER---IESLSFSPGAANAADLDDeevaqmratylglIAEVD 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 315 WSVGRILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHggyngiYKGGKSMNWEGGIRVPGLLLWPGV---IQAGTY 391
Cdd:cd16028 249 DHLGRLFDYLKETGQWDDTLIVFTSDHGEQL------GD-H------WLWGKDGFFDQAYRVPLIVRDPRReadATRGQV 315
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1444497660 392 IDEPTSNMDIFPTVIKLAGaqLPCDRIIDGHDLMPLLQGKIIQSKHEFLF 441
Cdd:cd16028 316 VDAFTESVDVMPTILDWLG--GEIPHQCDGRSLLPLLAGAQPSDWRDAVH 363
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-430 |
2.28e-32 |
|
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: 127.08 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTL--RTPNIDRLAKEGVTLTqHIAASPLCTPSRAAFLTGRYPIRSGMaaysrvgvfLF 102
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGV---------LA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 103 SASSGGLPSEEITFSKLLKQR--GYSTALIGKWHLGmNCESSNDfcHHPlshGFDYFYGLTMTNLRDcklgqgsvflkgt 180
Cdd:cd16154 71 VPDELLLSEETLLQLLIKDATtaGYSSAVIGKWHLG-GNDNSPN--NPG---GIPYYAGILGGGVQD------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 181 eksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllffFYNFRYLNcflmrNHqiiQQPLSYENLTQ 260
Cdd:cd16154 132 ---------------------------------------------------YYNWNLTN-----NG---QTTNSTEYATT 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 261 RLTKEAVQFIGRNTDaPFLLILSYLHVHT-------ALYASKNF-----IGKSKHGLYGDAVEEMDWSVGRILDVLEKSN 328
Cdd:cd16154 153 KLTNLAIDWIDQQTK-PWFLWLAYNAPHTpfhlppaELHSRSLLgdsadIEANPRPYYLAAIEAMDTEIGRLLASIDEEE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 329 LNNkTLVYFTSDQGAHVEEISSSGEVHGGYNGIYkggksmnwEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKL 408
Cdd:cd16154 232 REN-TIIIFIGDNGTPGQVVDLPYTRNHAKGSLY--------EGGINVPLIVSGAGVERANERESALVNATDLYATIAEL 302
|
410 420
....*....|....*....|..
gi 1444497660 409 AGAQLPcdRIIDGHDLMPLLQG 430
Cdd:cd16154 303 AGVDAA--EIHDSVSFKPLLSD 322
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
25-440 |
1.79e-31 |
|
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: 126.34 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMAaysrvgvflfsA 104
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSW-----------T 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFChhPLSHGFDYFYglTMTNLRDcKLgqgsvflkgTEKSI 184
Cdd:cd16156 70 NCMALGDNVKTIGQRLSDNGIHTAYIGKWHLDGGDYFGNGIC--PQGWDPDYWY--DMRNYLD-EL---------TEEER 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 185 VTSiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfRYLNCFLMRNHqiIQQPLSYenlTQRLTK 264
Cdd:cd16156 136 RKS------------------------------------------------RRGLTSLEAEG--IKEEFTY---GHRCTN 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 265 EAVQFIGRNTDAPFLLILSYLHVH-----TALYASK--------------NFIGKSKH------GLYGDAVEEM------ 313
Cdd:cd16156 163 RALDFIEKHKDEDFFLVVSYDEPHhpflcPKPYASMykdfefpkgenaydDLENKPLHqrlwagAKPHEDGDKGtikhpl 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 314 --------DWSVGRILDVLEKSNLNnkTLVYFTSD----QGAHveeisssgevhggynGIYKGGKSMnWEGGIRVPGLLL 381
Cdd:cd16156 243 yfgcnsfvDYEIGRVLDAADEIAED--AWVIYTSDhgdmLGAH---------------KLWAKGPAV-YDEITNIPLIIR 304
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1444497660 382 WPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPcdRIIDGHDLMPLLQGKIIQSKHEFL 440
Cdd:cd16156 305 GKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQP--KVLEGESILATIEDPEIPENRGVF 361
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-430 |
1.24e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 117.34 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGmaaySRVGVFLfsa 104
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG----HRTLHHL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 105 ssggLPSEEITFSKLLKQRGYSTALIGKwhlgmncessNDFchhplshgFDYFYGLTMTNLRDcklgqgsvflkgtEKSI 184
Cdd:cd16150 74 ----LRPDEPNLLKTLKDAGYHVAWAGK----------NDD--------LPGEFAAEAYCDSD-------------EACV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 185 VTSIQifgitllslatvhfigFLKVPFQALGYCLlitaillvvllfffynfrYLNcfLMRNHQIIQQPLSYENLTQRLTK 264
Cdd:cd16150 119 RTAID----------------WLRNRRPDKPFCL------------------YLP--LIFPHPPYGVEEPWFSMIDREKL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 265 EAVQFIGRNTDAPFLLIlsylhvhtalyasknfIGKSKHGLYG--DA------------VEEMDWSVGRILDVLEKSNLN 330
Cdd:cd16150 163 PPRRPPGLRAKGKPSML----------------EGIEKQGLDRwsEErwrelratylgmVSRLDHQFGRLLEALKETGLY 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 331 NKTLVYFTSDqgahveeisssgevHGGYNGIYkgGKSMNWEGGI-----RVPGLLLWPGVIQAGTyIDEPTSNMDIFPTV 405
Cdd:cd16150 227 DDTAVFFFSD--------------HGDYTGDY--GLVEKWPNTFedcltRVPLIIKPPGGPAGGV-SDALVELVDIPPTL 289
|
410 420
....*....|....*....|....*
gi 1444497660 406 IKLAGAQLPCDRIidGHDLMPLLQG 430
Cdd:cd16150 290 LDLAGIPLSHTHF--GRSLLPVLAG 312
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-443 |
1.48e-22 |
|
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: 98.05 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADD--------LGIGDLGCygnrtlrtPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGMaaYSR 96
Cdd:cd16035 1 PNILLILTDQerypppwpAGWAALNL--------PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGV--TDT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 97 VGvflfSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLgmncesSNdfchhplshgfdyfygltmtnlrdckLGQGsvf 176
Cdd:cd16035 71 LG----SPMQPLLSPDVPTLGHMLRAAGYYTAYKGKWHL------SG--------------------------AAGG--- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 177 lkgteksivtsiqifgitllslatvhfigflkvpfqalGYcllitaillvvllfffynfrylncflMRNHQIIQQplsye 256
Cdd:cd16035 112 --------------------------------------GY--------------------------KRDPGIAAQ----- 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 257 nltqrltkeAVQFI---GRNTDA--PFLLILSYLHVHTALY---ASKNFIGKSKhgLYGDAVEEMDWSVGRILDVLEKSN 328
Cdd:cd16035 123 ---------AVEWLrerGAKNADgkPWFLVVSLVNPHDIMFppdDEERWRRFRN--FYYNLIRDVDRQIGRVLDALDASG 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 329 LNNKTLVYFTSD----QGAHveeisssGEVHGGYNgIYkggksmnwEGGIRVPglLLW--PGVIQAGTYIDEPTSNMDIF 402
Cdd:cd16035 192 LADNTIVVFTSDhgemGGAH-------GLRGKGFN-AY--------EEALHVP--LIIshPDLFGTGQTTDALTSHIDLL 253
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1444497660 403 PTVIKLAGAQLPCDRIID----GHDLMPLLQGKIIQS-KHEFLFHY 443
Cdd:cd16035 254 PTLLGLAGVDAEARATEApplpGRDLSPLLTDADADAvRDGILFTY 299
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
25-464 |
2.77e-19 |
|
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: 89.14 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMADDLGiGDLGCY-GNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYP-IRSGMAAYSrvgvflf 102
Cdd:cd16171 1 PNVVMVMSDSFD-GRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFThLTESWNNYK------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 103 sassgGLPSEEITFSKLLKQRGYSTALIGKwhlgmncessNDFC--HHPLSHGFDYFYGLTMTNLRdcKLGQGSVFLKGT 180
Cdd:cd16171 73 -----GLDPNYPTWMDRLEKHGYHTQKYGK----------LDYTsgHHSVSNRVEAWTRDVPFLLR--QEGRPTVNLVGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 181 EKSivTSIQIFGITLLSLATvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiqqplsyenltQ 260
Cdd:cd16171 136 RST--VRVMLKDWQNTDKAV-----------------------------------------------------------H 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 261 RLTKEAVqfigrNTDAPFLLIL--SYLHVHTALYASKNFIG-KSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYF 337
Cdd:cd16171 155 WIRKEAP-----NLTQPFALYLglNLPHPYPSPSMGENFGSiRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFF 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 338 TSDQGAHVEEisssgevhggYNGIYKggKSMnWEGGIRVPGLLLWPGvIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDr 417
Cdd:cd16171 230 TSDHGELAME----------HRQFYK--MSM-YEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN- 294
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1444497660 418 iIDGHDLMPLLQGKIIQSKHEFL---------FHYCNAylNAVRWHPRNsfNQVKY 464
Cdd:cd16171 295 -LSGYSLLPLLSESSIKESPSRVphpdwvlseFHGCNV--NASTYMLRT--NSWKY 345
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
245-407 |
6.93e-11 |
|
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: 64.54 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 245 NHQIIQQPLSYENLTQRLTKEAVQFIG-RNTDAPFLLILSYLHVHtALYASKNFIGKSKHGLYGD--------------- 308
Cdd:COG3083 349 SLPRLHTPGGPAQRDRQITAQWLQWLDqRDSDRPWFSYLFLDAPH-AYSFPADYPKPFQPSEDCNylaldnesdptpfkn 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 309 ----AVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGahvEEISSSGEVHGGYNGIYKggksmnwEGGIRVPGLLLWPG 384
Cdd:COG3083 428 ryrnAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHG---EEFNENGQNYWGHNSNFS-------RYQLQVPLVIHWPG 497
|
170 180
....*....|....*....|...
gi 1444497660 385 vIQAGTyIDEPTSNMDIFPTVIK 407
Cdd:COG3083 498 -TPPQV-ISKLTSHLDIVPTLMQ 518
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
1-137 |
1.23e-08 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 56.68 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 1 MRLLSFLIICQCAIkSLSSHSASNPNVILLMADDLGIGDLgcygnRTLRTPNIDRLAKEGVTLTQHIAASPLCT-PSRAA 79
Cdd:COG1524 1 MKRGLSLLLASLLA-AAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFPSTTaPAHTT 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444497660 80 FLTGRYPIRSGMAAYS-------RVGVFLFSASSGGLPSEEI---TFSKLLKQRGYSTALIGKWHLGM 137
Cdd:COG1524 75 LLTGLYPGEHGIVGNGwydpelgRVVNSLSWVEDGFGSNSLLpvpTIFERARAAGLTTAAVFWPSFEG 142
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
25-410 |
2.59e-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: 55.00 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 25 PNVILLMA---DDLGIGDLGCYGNRTlrtPNIDRLAKEGVTLTQHIAASPLCTPSRA--AFLTGRYPIRSGMAAYSRVGV 99
Cdd:cd16015 1 PNVIVILLesfSDPYIDKDVGGEDLT---PNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 100 FLFSassgglpseeiTFSKLLKQRGYSTALIgkwhlgmncessndfchhplsHGFD-YFYGltmtnlrdcklgQGSVFlk 178
Cdd:cd16015 78 NPLP-----------SLPSILKEQGYETIFI---------------------HGGDaSFYN------------RDSVY-- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 179 gteksivtsiqifgitllslatvhfigflkvpfQALGycllitaillvvllffFYNFRYLNCFLMRNHQIIQQPLSYENL 258
Cdd:cd16015 112 ---------------------------------PNLG----------------FDEFYDLEDFPDDEKETNGWGVSDESL 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 259 TQRLTKEavqfIGRNTDAPFLLIL---------SYLHVHTALYASKNFiGKSKHGLYGDAVEEMDWSVGRILDVLEKSNL 329
Cdd:cd16015 143 FDQALEE----LEELKKKPFFIFLvtmsnhgpyDLPEEKKDEPLKVEE-DKTELENYLNAIHYTDKALGEFIEKLKKSGL 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 330 NNKTLVYFTSDqgahveeisssgevHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLA 409
Cdd:cd16015 218 YENTIIVIYGD--------------HLPSLGSDYDETDEDPLDLYRTPLLIYSPGLKKPKK-IDRVGSQIDIAPTLLDLL 282
|
.
gi 1444497660 410 G 410
Cdd:cd16015 283 G 283
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
435-455 |
5.09e-08 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 51.54 E-value: 5.09e-08
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
21-425 |
2.79e-05 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 46.57 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 21 SASNPNVILLMADDLGIGDLGCYGNRTLRTPNIDRLAKEGVTLTQHIAASPLCTPSRAAFLTGRYPIRSGmaaysrvgVF 100
Cdd:COG1368 231 PAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGG--------SP 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 101 LFSASSGGLPSeeitFSKLLKQRGYSTALI----GKWhlgMNCessNDFCHHplsHGFDYFYGLT-MTNLRDCKLGQ--G 173
Cdd:COG1368 303 YKRPGQNNFPS----LPSILKKQGYETSFFhggdGSF---WNR---DSFYKN---LGFDEFYDREdFDDPFDGGWGVsdE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 174 SVFLKgteksivtSIQIFGItllslatvhfigfLKVPFqalgYCLLITaillvvllfffynfrylncflMRNHQiiqqPL 253
Cdd:COG1368 370 DLFDK--------ALEELEK-------------LKKPF----FAFLIT---------------------LSNHG----PY 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 254 SYENLTQRLTKeavqfigrntdapfllilsylhvhtalyasknfIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKT 333
Cdd:COG1368 400 TLPEEDKKIPD---------------------------------YGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 334 LVYFTSDqgahveeisssgevHGGynGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLAGAQL 413
Cdd:COG1368 447 IFVIYGD--------------HGP--RSPGKTDYENPLERYRVPLLIYSPGLKKPKV-IDTVGSQIDIAPTLLDLLGIDY 509
|
410
....*....|..
gi 1444497660 414 PcDRIIDGHDLM 425
Cdd:COG1368 510 P-SYYAFGRDLL 520
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
27-128 |
7.72e-05 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 44.72 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 27 VILLMADDLGIGDLgcygNRTLRTPNIDRLAKEGVTLTQHIAASPLCT-PSRAAFLTGRYPIRSGMAA---YSRVG--VF 100
Cdd:pfam01663 1 LLVISLDGFRADYL----DRFELTPNLAALAKEGVSAPNLTPVFPTLTfPNHYTLVTGLYPGSHGIVGntfYDPKTgeYL 76
|
90 100 110
....*....|....*....|....*....|.
gi 1444497660 101 LFSASSGGLP---SEEITFSKLLKQrGYSTA 128
Cdd:pfam01663 77 VFVISDPEDPrwwQGEPIWDTAAKA-GVRAA 106
|
|
| iPGM_like |
cd16011 |
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ... |
27-62 |
3.19e-03 |
|
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) and bacterial phosphopentomutases; The proteins in this subfamily of alkaline phosphatase are not characterized. Their sequences show similarity to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) which catalyzes the interconversion of 3-phosphoglycerate to 2-phosphoglycerate, and to bacterial phosphopentomutases (PPMs) which interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate).
Pssm-ID: 293735 Cd Length: 368 Bit Score: 39.76 E-value: 3.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1444497660 27 VILLMADdlGIGDLG--CYGNRT-L---RTPNIDRLAKEGVT 62
Cdd:cd16011 3 YVLLILD--GLGDRPipELGGKTpLeaaKTPNLDRLAAEGIC 42
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
308-410 |
5.11e-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: 38.72 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497660 308 DAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGahveeISSSGeVHGGYNGIykggKSMNweggirvPGLLLWPGVIQ 387
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG-----MTDVG-THGYDNEL----PDMR-------AIFIARGPAFK 245
|
90 100
....*....|....*....|...
gi 1444497660 388 AGTYIdEPTSNMDIFPTVIKLAG 410
Cdd:cd16018 246 KGKKL-GPFRNVDIYPLMCNLLG 267
|
|
| |
