|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
34-531 |
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: 632.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGHRVLQWA 113
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 114 AGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTVSDLCHHPLNHGFHHFLGLPLGMMGDCAGAEPSEKRAGLeRR 193
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSF-DP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 194 LRGAGRALAAVAVAIAALAWGRGrglapaCWAPWAAIALGAVAAIFEAGSYVVGGAVARYDCFLMRNATVTQQPLQLDHV 273
Cdd:cd16159 160 LFPLLTAFVLITALTIFLLLYLG------AVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 274 TPLLLREAKDFLRRHRHAPFLLFLSLLHTHTPLVTSPEFRGRSAHGRYGDNVEEMDWVVGQILEVLEHEGLTDSTLVHFT 353
Cdd:cd16159 234 TQRLTKEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 354 SDNGAWLEAQAGGEQLGGSNGVFRGGKGMGGWEGGIRVPGVFRWPGVLPRGRVLDQPVSLMDVFPTVVRLGGGVLPSDRE 433
Cdd:cd16159 314 SDNGGHLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 434 IDGRDLLPLLRGETWHSAHEVLLHYCEVFLHAVRWVQRDSGQVWKAHFVTPTFDPLgsgscSGAGGAAAVCPCVGK-VEE 512
Cdd:cd16159 394 IDGRDLMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPG-----TEGCCGTLLCRCFGDsVTH 468
|
490
....*....|....*....
gi 564336247 513 HDPPLLFELTSDPGEVRPL 531
Cdd:cd16159 469 HDPPLLFDLSADPSESNPL 487
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
34-531 |
7.24e-154 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293750 [Multi-domain] Cd Length: 399 Bit Score: 448.17 E-value: 7.24e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGHrvlqwA 113
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGP-----P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 114 AGAGGLPPKEITFARILQGQGYVTGLVGKWHLGlscrtvsDL-CHHPLNHGFHHFLGLPLGMMGDCagaepsekragler 192
Cdd:cd16026 76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYSNDMWP-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 193 rlrgagralaavavaiaaLAWGRGRGLApacwapwaaialgavaaifeagsyvvggavarYDCFLMRNATVTQQPLQLDH 272
Cdd:cd16026 135 ------------------FPLYRNDPPG--------------------------------PLPPLMENEEVIEQPADQSS 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 273 VTPLLLREAKDFLRRHRHAPFLLFLSLLHTHTPLVTSPEFRGRSAHGRYGDNVEEMDWVVGQILEVLEHEGLTDSTLVHF 352
Cdd:cd16026 165 LTQRYTDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIF 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 353 TSDNGAWLEAQAGgeqlGGSNGVFRgGKGMGGWEGGIRVPGVFRWPGVLPRGRVLDQPVSLMDVFPTVVRLGGGVLPSDR 432
Cdd:cd16026 245 TSDNGPWLEYGGH----GGSAGPLR-GGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPEDR 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 433 EIDGRDLLPLLRGETWHSAHEVLLHYCEVFLHAVRWvqrdsGQvWKAHFVTPTFDPLGSGSCSGAGgaaavcpcvgkvee 512
Cdd:cd16026 320 VIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRS-----GR-WKLHLPTTYRTGTDPGGLDPTK-------------- 379
|
490
....*....|....*....
gi 564336247 513 HDPPLLFELTSDPGEVRPL 531
Cdd:cd16026 380 LEPPLLYDLEEDPGETYNV 398
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
34-531 |
5.33e-122 |
|
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: 368.30 E-value: 5.33e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLGIGDLGCYGN-TSIRTPnIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGhRVLQW 112
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHpTQERGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTR-VFLPW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 113 aaGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTVSDLCHHPLNHGFHhFLG--LPLGMMGDCAgaepsekragl 190
Cdd:cd16160 79 --DIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGtnLPFTNSWACD----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 191 errlrgagralaavavaiaalAWGRgrglapacwapwaaialgavaaifeagsYVVGGAVARydCFLMRNATVTQQPLQL 270
Cdd:cd16160 145 ---------------------DTGR----------------------------HVDFPDRSA--CFLYYNDTIVEQPIQH 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 271 DHVTPLLLREAKDFLRRHRHAPFLLFLSLLHTHTPLVTSPEFRGRSAHGRYGDNVEEMDWVVGQILEVLEHEGLTDSTLV 350
Cdd:cd16160 174 EHLTETLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 351 HFTSDNGAWLEAQaggeQLGGSNGVFRgGKGMGGWEGGIRVPGVFRWPGVLPrGRVLDQPVSLMDVFPTVVRLGGGVLPS 430
Cdd:cd16160 254 FFLSDHGPHVEYC----LEGGSTGGLK-GGKGNSWEGGIRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTFVDLAGGTLPT 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 431 DREIDGRDLLPLLRGETwHSAHEVLLHYCEVFLHAVRwvqrdSGQvWKAHFVT---PTFDPLGSGSCSGAGGAA----AV 503
Cdd:cd16160 328 DRIYDGLSITDLLLGEA-DSPHDDILYYCCSRLMAVR-----YGS-YKIHFKTqplPSQESLDPNCDGGGPLSDyivcYD 400
|
490 500
....*....|....*....|....*...
gi 564336247 504 CPCVgKVEEHDPPLLFELTSDPGEVRPL 531
Cdd:cd16160 401 CEDE-CVTKHNPPLIFDVEKDPGEQYPL 427
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
17-531 |
1.63e-90 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 285.23 E-value: 1.63e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 17 IVLLGLQYVDALRSPPPRPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYP 96
Cdd:COG3119 6 LLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 97 IRSGMTsGNGHrvlqwaAGAGGLPPKEITFARILQGQGYVTGLVGKWHLglscrtvsdlchhplnhgfhhflglplgmmg 176
Cdd:COG3119 86 HRTGVT-DNGE------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 177 dcagaepsekraglerrlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvggavarydcf 256
Cdd:COG3119 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 257 lmrnatvtqqplqldHVTPLLLREAKDFLRRHRHA--PFLLFLSLLHTHTPLVTSPEFRG-------------------- 314
Cdd:COG3119 128 ---------------YLTDLLTDKAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDkydgkdiplppnlaprdlte 192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 315 ---RSAHGRYGDNVEEMDWVVGQILEVLEHEGLTDSTLVHFTSDNGAWLEAQA--GGEQL---GGsngvfrggkgmggwe 386
Cdd:COG3119 193 eelRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGlrGGKGTlyeGG--------------- 257
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 387 ggIRVPGVFRWPGVLPRGRVLDQPVSLMDVFPTVVRLGGGVLPSDreIDGRDLLPLLRGETWHSAHEVLLHYCEVF-LHA 465
Cdd:COG3119 258 --IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGgNRA 333
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564336247 466 VRWvqrdsGQvWKAHFvtptfdplgsgscsgaggaaavcpcvgKVEEHDPPLLFELTSDPGEVRPL 531
Cdd:COG3119 334 IRT-----GR-WKLIR---------------------------YYDDDGPWELYDLKNDPGETNNL 366
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
35-527 |
1.77e-85 |
|
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: 271.33 E-value: 1.77e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIR---TPNIDRLAEDGVRLTQYLAaESVCTPSRAAFLTGRYPIRSGMTSgnghrvLQ 111
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYV-EPSCTPGRAAFITGRHPIRTGLTT------VG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 112 WAAGAGGLPPKEITFARILQGQGYVTGLVGKWHLGlscrtvsDLCHH-PLNHGFHHFLGLPLGMMGDcagaEPSEKragl 190
Cdd:cd16142 74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG-------DEDGRlPTDHGFDEFYGNLYHTIDE----EIVDK---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 191 errlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvggavarydcflmrnatvtqqplql 270
Cdd:cd16142 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 271 dhvtplllreAKDFLRRHRHA--PFLLFLSLLHTHTPLVTSPEFRGRS-AHGRYGDNVEEMDWVVGQILEVLEHEGLTDS 347
Cdd:cd16142 139 ----------AIDFIKRNAKAdkPFFLYVNFTKMHFPTLPSPEFEGKSsGKGKYADSMVELDDHVGQILDALDELGIADN 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 348 TLVHFTSDNGAWLEA--QAGGEQLGGSNGVFRGGKgmggweggIRVPGVFRWPGVLPRGRVLDQPVSLMDVFPTVVRLGG 425
Cdd:cd16142 209 TIVIFTTDNGPEQDVwpDGGYTPFRGEKGTTWEGG--------VRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAG 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 426 GVLP------SDREIDGRDLLPLLRGETWHSAHEVLLHYCEVFLHAVRWVQrdsgqvWKAHF--VTPTFDPLGSGSCSGA 497
Cdd:cd16142 281 APDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFkaQEDTGGPTGEPFYVLT 354
|
490 500 510
....*....|....*....|....*....|
gi 564336247 498 GgaaavcpcvgkveehdpPLLFELTSDPGE 527
Cdd:cd16142 355 F-----------------PLIFNLRRDPKE 367
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
35-457 |
4.84e-85 |
|
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: 271.00 E-value: 4.84e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTS-IRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNghrvlQWA 113
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSkIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGV-----LGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 114 AGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTVSDLCHH----------------PLNHGFHHFLGLPlgmmgd 177
Cdd:cd16143 76 FSPPLIEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIP------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 178 cagaepsekraglerrlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeaGSYVVggavarydcfl 257
Cdd:cd16143 150 ----------------------------------------------------------------ASEVL----------- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 258 mrnatvtqqplqldhvtPLLLREAKDFLRRHRHA--PFLLFLSLLHTHTPLVTSPEFRGRSAHGRYGDNVEEMDWVVGQI 335
Cdd:cd16143 155 -----------------PTLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRI 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 336 LEVLEHEGLTDSTLVHFTSDNGAWLEAQAGGEQLGG--SNGVFRggkgmgGWEGGI-----RVPGVFRWPGVLPRGRVLD 408
Cdd:cd16143 218 LDALKELGLAENTLVIFTSDNGPSPYADYKELEKFGhdPSGPLR------GMKADIyegghRVPFIVRWPGKIPAGSVSD 291
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 564336247 409 QPVSLMDVFPTVVRLGGGVLPSDREIDGRDLLPLLRGETWHSAHEVLLH 457
Cdd:cd16143 292 QLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH 340
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
34-531 |
5.49e-85 |
|
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: 270.49 E-value: 5.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLGIGDLGCYGN-TSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGhrvlqw 112
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 113 AAGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRtvsdlcHHPLNHGFHHFLGLPlgmmgdcagaepsekragler 192
Cdd:cd16161 75 PTSVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQREA------YLPNSRGFDYYFGIP--------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 193 rlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvggavarYDCflmrNATVTQQPLQldh 272
Cdd:cd16161 128 ------------------------------------------------------------FSH----DSSLADRYAQ--- 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 273 vtplllrEAKDFLRRHRHA--PFLLFLSLLHTHTPLVTSPEFRGRSAH-GRYGDNVEEMDWVVGQILEVLEHEGLTDSTL 349
Cdd:cd16161 141 -------FATDFIQRASAKdrPFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTL 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 350 VHFTSDNGAWL-EAQAGGE--------QLGGSNGvfrggkGMGGWEGGIRVPGVFRWPGVLPRGRVLDQPVSLMDVFPTV 420
Cdd:cd16161 214 TWFTSDNGPWEvKCELAVGpgtgdwqgNLGGSVA------KASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTV 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 421 VRLGGGVLPSDREIDGRDLLPLLRGETwHSAHEVLLHYCEVF-----LHAVRWVQrdsgqvWKAHFVTptfdplgsgscs 495
Cdd:cd16161 288 VALAGASLPPGRIYDGKDLSPVLFGGS-KTGHRCLFHPNSGAagagaLSAVRCGD------YKAHYAT------------ 348
|
490 500 510
....*....|....*....|....*....|....*.
gi 564336247 496 gaGGAAAVCPCVGKVEEHDPPLLFELTSDPGEVRPL 531
Cdd:cd16161 349 --GGALACCGSTGPKLYHDPPLLFDLEVDPAESFPL 382
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
35-603 |
2.32e-83 |
|
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: 269.31 E-value: 2.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGnghrVLQwAA 114
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPG----VFY-PG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 115 GAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTVsdlcHHPLNHGFHHFLGLPLGM-MGDCAGAE---PSEKRAGL 190
Cdd:cd16158 77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYSHdQGPCQNLTcfpPNIPCFGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 191 ERRlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsYVVGgavarydCFLMRNATVTQQPLQL 270
Cdd:cd16158 153 CDQ--------------------------------------------------GEVP-------CPLFYNESIVQQPVDL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 271 DHVTPLLLREAKDFLRR--HRHAPFLLFLSLLHTHTPLVTSPEFRGRSAHGRYGDNVEEMDWVVGQILEVLEHEGLTDST 348
Cdd:cd16158 176 LTLEERYAKFAKDFIADnaKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 349 LVHFTSDNGAWLEAQAggeqLGGSNGVFRgGKGMGGWEGGIRVPGVFRWPGVLPRGRVLDQPVSLmDVFPTVVRLGGGVL 428
Cdd:cd16158 256 LVFFTSDNGPSTMRKS----RGGNAGLLK-CGKGTTYEGGVREPAIAYWPGRIKPGVTHELASTL-DILPTIAKLAGAPL 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 429 PsDREIDGRDLLPLLRgETWHSAHEVLLHY-----CEVFLHAVRWVQrdsgqvWKAHFVT-------PTFDPlgsgscsg 496
Cdd:cd16158 330 P-NVTLDGVDMSPILF-EQGKSPRQTFFYYptspdPDKGVFAVRWGK------YKAHFYTqgaahsgTTPDK-------- 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 497 aggaaaVCPCVGKVEEHDPPLLFELTSDPGEVRPLRAPakmseaPNLTAAITSeavtaamataarVRQEYDMLRPTAGHV 576
Cdd:cd16158 394 ------DCHPSAELTSHDPPLLFDLSQDPSENYNLLGL------PEYNQVLKQ------------IQQVKERFEASMKFG 449
|
570 580 590
....*....|....*....|....*....|.
gi 564336247 577 PQQMGSLYNlwlPWLQPC----CGHFPACAC 603
Cdd:cd16158 450 ESEINKGED---PALEPCckpgCTPKPSCCQ 477
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
35-452 |
5.82e-82 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 263.64 E-value: 5.82e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTS-GNGHRVLQWA 113
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDvIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 114 A------GAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRtvsdlcHHPLNHGFHHFLGlplgmmGDCAGAEPSEkr 187
Cdd:cd16144 81 TklipppSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGG------YGPEDQGFDVNIG------GTGNGGPPSY-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 188 aglerrlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaiFEAGSYVVGGAVARYDcflmrnatvtqqp 267
Cdd:cd16144 147 ---------------------------------------------------YFPPGKPNPDLEDGPE------------- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 268 lqLDHVTPLLLREAKDFLRRHRHAPFLLFLSLLHTHTPLVTSPE----FRGRSAHGRYGDN-------VEEMDWVVGQIL 336
Cdd:cd16144 163 --GEYLTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPEliekYEKKKKGLRKGQKnpvyaamIESLDESVGRIL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 337 EVLEHEGLTDSTLVHFTSDNGAWleaqAGGEQLGGSNGVFRggkgmggweggIRVPGVFRWPGVLPRGRVLDQPVSLMDV 416
Cdd:cd16144 241 DALEELGLADNTLVIFTSDNGGL----STRGGPPTSNAPLRggkgs-lyeggIRVPLIVRWPGVIKPGSVSDVPVIGTDL 315
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 564336247 417 FPTVVRLGGGVLPSDREIDGRDLLPLLRGET---------WHSAH 452
Cdd:cd16144 316 YPTFLELAGGPLPPPQHLDGVSLVPLLKGGEadlprralfWHFPH 360
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
34-531 |
5.92e-81 |
|
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: 262.79 E-value: 5.92e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGHrvlqwA 113
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAH-----A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 114 AGA-------GGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRtvsdlcHHPLNHGFHHFLGLPlgmmgDCAGAEPSEK 186
Cdd:cd16157 76 RNAytpqnivGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NCHFGPYDNK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 187 raglerrlrgagralaavavaiaalawgrgrglapacwapwaaiaLGAVAAIFE----AGSYvvggavarYDCFLMRNAT 262
Cdd:cd16157 145 ---------------------------------------------AYPNIPVYRdwemIGRY--------YEEFKIDKKT 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 263 vtqqplQLDHVTPLLLREAKDFLRRHRHA--PFLLFLSLLHTHTPLVTSPEFRGRSAHGRYGDNVEEMDWVVGQILEVLE 340
Cdd:cd16157 172 ------GESNLTQIYLQEALEFIEKQHDAqkPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 341 HEGLTDSTLVHFTSDNGAwleAQAGGEQLGGSNGVFrGGKGMGGWEGGIRVPGVFRWPGVLPRGRVLDQPVSLMDVFPTV 420
Cdd:cd16157 246 SLGIENNTFVFFSSDNGA---ALISAPEQGGSNGPF-LCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTS 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 421 VRLGGGVLPSDREIDGRDLLPLLRgeTWHSAHEVLLHYCEVFLHAVRWVQrdsgqvWKAHFVTPTfdplgsGSCSGAGGA 500
Cdd:cd16157 322 LALAGLPIPSDRAIDGIDLLPVLL--NGKEKDRPIFYYRGDELMAVRLGQ------YKAHFWTWS------NSWEEFRKG 387
|
490 500 510
....*....|....*....|....*....|....*....
gi 564336247 501 AAVCPC--VGKVEEH------DPPLLFELTSDPGEVRPL 531
Cdd:cd16157 388 INFCPGqnVPGVTTHnqtdhtKLPLLFHLGRDPGEKYPI 426
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
35-482 |
5.01e-75 |
|
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293765 [Multi-domain] Cd Length: 409 Bit Score: 245.15 E-value: 5.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAeSVCTPSRAAFLTGRYPIRSGM--TSGNGHRvlqw 112
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVwhTILGRER---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 113 aagaggLPPKEITFARILQGQGYVTGLVGKWHLGLSCRtvsdlcHHPLNHGFHHFLGLPLGMMGDCAGAepsekragler 192
Cdd:cd16146 76 ------MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYP------YRPQDRGFDEVLGHGGGGIGQYPDY----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 193 rlrgagralaavavaiaalaWGRGRglapacwapwaaialgavaaifEAGSYVVGGAVARYDCFlmrnatvtqqplqldh 272
Cdd:cd16146 133 --------------------WGNDY----------------------FDDTYYHNGKFVKTEGY---------------- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 273 VTPLLLREAKDFLRRHRHAPFLLFLSLLHTHTPLVTSPEFRGRSAHGRYGDN-------VEEMDWVVGQILEVLEHEGLT 345
Cdd:cd16146 155 CTDVFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKlaafygmIENIDDNVGRLLAKLKELGLE 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 346 DSTLVHFTSDNGAWLEAQ----AGgeqLGGSNG-VFRggkgmggweGGIRVPGVFRWPGVLPRGRVLDQPVSLMDVFPTV 420
Cdd:cd16146 235 ENTIVIFMSDNGPAGGVPkrfnAG---MRGKKGsVYE---------GGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTL 302
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564336247 421 VRLGGGVLPSDREIDGRDLLPLLRGETWHSAHEVLlhycevFLHAVRWvqrDSGQVWKAHFV 482
Cdd:cd16146 303 LDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTL------FTHSGRW---PPPPKKKRNAA 355
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
35-438 |
1.32e-68 |
|
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: 222.31 E-value: 1.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRsgmtsgngHRVLQWAA 114
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHR--------HGVRGNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 115 GAGGLPPKEITFARILQGQGYVTGLVGKWHlglscrtvsdlchhplnhgfhhflglplgmmgdcagaepsekraglerrl 194
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 195 rgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvggavarydcflmrnatvtqqplqldhvt 274
Cdd:cd16022 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 275 plllREAKDFLRRHRH-APFLLFLSLLHTHTPLVtspefrgrsahgrYGDNVEEMDWVVGQILEVLEHEGLTDSTLVHFT 353
Cdd:cd16022 103 ----DEAIDFIERRDKdKPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFT 165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 354 SDNGAWLEaqAGGEQLGGSN---GVfrggkgmggweggIRVPGVFRWPGVLPRGRVLDQPVSLMDVFPTVVRLGGgvLPS 430
Cdd:cd16022 166 SDHGDMLG--DHGLRGKKGSlyeGG-------------IRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAG--IEP 228
|
....*...
gi 564336247 431 DREIDGRD 438
Cdd:cd16022 229 PEGLDGRS 236
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
35-527 |
1.10e-67 |
|
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: 225.94 E-value: 1.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTgrypirsGMTSGNGH-RVLQWA 113
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLT-------GLHTGHTRvRGNSEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 114 AGAGGLPPKEITFARILQGQGYVTGLVGKWHLGlsCRTVSDlchHPLNHGFHHFlglpLGMMG--DCAGAEPSEKragle 191
Cdd:cd16145 74 GGQDPLPPDDVTLAEVLKKAGYATAAFGKWGLG--GPGTPG---HPTKQGFDYF----YGYLDqvHAHNYYPEYL----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 192 rrlrgagralaavavaiaalaWGRGRGLAPACWAPWAaialgavaaifEAGSYVVGGAVARYdcflmrnatvtqqplqld 271
Cdd:cd16145 140 ---------------------WRNGEKVPLPNNVIPP-----------LDEGNNAGGGGGTY------------------ 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 272 hVTPLLLREAKDFLRRHRHAPFLLFLSLLHTHTPLVT---SPEFRGRSAHGRYGDN------------VEEMDWVVGQIL 336
Cdd:cd16145 170 -SHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVpddGPYKYKPKDPGIYAYLpwpqpekayaamVTRLDRDVGRIL 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 337 EVLEHEGLTDSTLVHFTSDNGAWLEaqaGGEQLGG----SNGVFRggkgmggweggIRVPGVFRWPGVLPRGRVLDQPVS 412
Cdd:cd16145 249 ALLKELGIDENTLVVFTSDNGPHSE---GGSEHDPdffdSNGPLRgykrs-lyeggIRVPFIARWPGKIPAGSVSDHPSA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 413 LMDVFPTVVRLGGGVLPSDreIDGRDLLPLLRGETWHSAHEVLlhYCEVFLH----AVRWVQrdsgqvWKAhfvtptfdp 488
Cdd:cd16145 325 FWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFYEGggaqAVRMGG------WKA--------- 385
|
490 500 510
....*....|....*....|....*....|....*....
gi 564336247 489 lgsgscsgaggaaavcpcVGKVEEHDPPLLFELTSDPGE 527
Cdd:cd16145 386 ------------------VRHGKKDGPFELYDLSTDPGE 406
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-458 |
3.58e-67 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 223.63 E-value: 3.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQ-YlaAESVCTPSRAAFLTGRYPIRSGmtsgnghrvlqwa 113
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNaY--AQPLCTPSRVQLMTGKYNFRNY------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 114 AGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLScRTVSDlchHPLNHGFHHFLglplgMMGDCAGAEPSEKRAGLERR 193
Cdd:cd16151 66 VVFGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGG-RGDGD---YPHEFGFDEYC-----LWQLTETGEKYSRPATPTFN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 194 LRgagralaavavaiaalawgRGRGLApacwapwaaialgavaaiFEAGSYvvgGA--VARYdcflmrnatvtqqplqld 271
Cdd:cd16151 137 IR-------------------NGKLLE------------------TTEGDY---GPdlFADF------------------ 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 272 hvtplllreAKDFLRRHRHAPFLLFLSLLHTHTPLVTSPE------FRGRSAH--GRYGDNVEEMDWVVGQILEVLEHEG 343
Cdd:cd16151 159 ---------LIDFIERNKDQPFFAYYPMVLVHDPFVPTPDspdwdpDDKRKKDdpEYFPDMVAYMDKLVGKLVDKLEELG 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 344 LTDSTLVHFTSDNGAWLEAQA---GGEQLGGSNGVfrggkgmggWEGGIRVPGVFRWPGVLPRGRVLDQPVSLMDVFPTV 420
Cdd:cd16151 230 LRENTIIIFTGDNGTHRPITSrtnGREVRGGKGKT---------TDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTL 300
|
410 420 430
....*....|....*....|....*....|....*...
gi 564336247 421 VRLGGGVLPSDREIDGRDLLPLLRGETWHSAHEVLLHY 458
Cdd:cd16151 301 AELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWY 338
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
35-487 |
5.17e-64 |
|
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: 215.88 E-value: 5.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAeSVCTPSRAAFLTGRYPIRSGMtsgnGHRVLqWAA 114
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGM----QHGVI-LAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 115 GAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTvsdlcHHPLNHGFHHFLGLPLGMMGDcagaepsekraglerrl 194
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLGFYTWE-----YTPTNRGFDSFYGYYGGAEDY----------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 195 rgagralaavavaiaalaWgrgrglapacwapwaaialgavaaifeagSYVVGGAVARYDCFLMRNATVTqQPLQLDHVT 274
Cdd:cd16029 133 ------------------Y-----------------------------THTSGGANDYGNDDLRDNEEPA-WDYNGTYST 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 275 PLLLREAKDFLRRH-RHAPFLLFLSLLHTHTPL----VTSPEFRGRSAHGRYGD------NVEEMDWVVGQILEVLEHEG 343
Cdd:cd16029 165 DLFTDRAVDIIENHdPSKPLFLYLAFQAVHAPLqvppEYADPYEDKFAHIKDEDrrtyaaMVSALDESVGNVVDALKAKG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 344 LTDSTLVHFTSDNGAWLEAQAggeqlGGSN-------------GVfrggkgmggweggiRVPGvFRWPGVLP--RGRVLD 408
Cdd:cd16029 245 MLDNTLIVFTSDNGGPTGGGD-----GGSNyplrggkntlwegGV--------------RVPA-FVWSPLLPpkRGTVSD 304
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564336247 409 QPVSLMDVFPTVVRLGGGVLPSDREIDGRDLLPLLRGETWHSAHEVLLHYCEVFLHAVRWVQRdSGQvWKAHFVTPTFD 487
Cdd:cd16029 305 GLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNIDDITRTTGGAAIR-VGD-WKLIVGKPLFN 381
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-531 |
8.59e-57 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 196.64 E-value: 8.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTsGNGHRvlqwa 113
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF-GNDVP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 114 agaggLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTVSDLCHH----PLNHGFHHFLGlplgmmgdcagaepsekrag 189
Cdd:cd16034 75 -----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKG-------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 190 lerrlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvggavarYDCFLMRNA----TVTQ 265
Cdd:cd16034 130 ---------------------------------------------------------------YECNHDHNNphyyDDDG 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 266 QPLQLDHVTPLLL-REAKDFLRRHRHA--PFLLFLSLLHTHTPLVTSPE-------------------------FRGRSA 317
Cdd:cd16034 147 KRIYIKGYSPDAEtDLAIEYLENQADKdkPFALVLSWNPPHDPYTTAPEeyldmydpkklllrpnvpedkkeeaGLREDL 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 318 HGRYGdNVEEMDWVVGQILEVLEHEGLTDSTLVHFTSDNgawleaqagGEQLgGSNGVFRggkGMGGWEGGIRVPGVFRW 397
Cdd:cd16034 227 RGYYA-MITALDDNIGRLLDALKELGLLENTIVVFTSDH---------GDML-GSHGLMN---KQVPYEESIRVPFIIRY 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 398 PGVLPRGRVLDQPVSLMDVFPTVVRLGGgvLPSDREIDGRDLLPLLRGETWHSAHEVLLhYCEVFLHAVRWVQRDSGQVW 477
Cdd:cd16034 293 PGKIKAGRVVDLLINTVDIMPTLLGLCG--LPIPDTVEGRDLSPLLLGGKDDEPDSVLL-QCFVPFGGGSARDGGEWRGV 369
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 564336247 478 KAH---FVtptfdplgsgscsgaggaaavcpcvgkVEEHDPPLLFELTSDPGEVRPL 531
Cdd:cd16034 370 RTDrytYV---------------------------RDKNGPWLLFDNEKDPYQLNNL 399
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
35-425 |
1.09e-56 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 193.41 E-value: 1.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGhrvlqwaa 114
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 115 gaGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTvsdlchHPLNHGFHHFLGLPLGM--MGDCAgaepsekragler 192
Cdd:pfam00884 73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQ------SPCNLGFDKFFGRNTGSdlYADPP------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 193 rlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaiFEAGSYVVGGAvarydcflmrnatvtqqplqLDH 272
Cdd:pfam00884 132 ----------------------------------------------DVPYNCSGGGV--------------------SDE 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 273 VtplLLREAKDFLRRHrHAPFLLFLSLLHTHTPLVTSPEF------------RGRSAHGRYGDNVEEMDWVVGQILEVLE 340
Cdd:pfam00884 146 A---LLDEALEFLDNN-DKPFFLVLHTLGSHGPPYYPDRYpekyatfkpsscSEEQLLNSYDNTLLYTDDAIGRVLDKLE 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 341 HEGLTDSTLVHFTSDNgawleaqagGEQLGGSNGVFRGGKGMGGWEGGIRVPGVFRWPGVLPRGRVLDQPVSLMDVFPTV 420
Cdd:pfam00884 222 ENGLLDNTLVVYTSDH---------GESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTI 292
|
....*
gi 564336247 421 VRLGG 425
Cdd:pfam00884 293 LDLAG 297
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
35-470 |
3.72e-55 |
|
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: 191.57 E-value: 3.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIgDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTsgnGHRVLQWAa 114
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAH---GLRSRGFP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 115 gaggLPPKEITFARILQGQGYVTGLVGKWHlglscrtvsdlchhplnHGFHHFLGLPLGMMGDCAGAEPSEKRAGlerrl 194
Cdd:cd16027 76 ----LPDGVKTLPELLREAGYYTGLIGKTH-----------------YNPDAVFPFDDEMRGPDDGGRNAWDYAS----- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 195 rgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvggavarydcflmrnatvtqqplqldhvt 274
Cdd:cd16027 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 275 plllrEAKDFLRRHRH-APFLLFLSLLHTHTPLVTSPEFRG-------------------RSAHGRYGDNVEEMDWVVGQ 334
Cdd:cd16027 130 -----NAADFLNRAKKgQPFFLWFGFHDPHRPYPPGDGEEPgydpekvkvppylpdtpevREDLADYYDEIERLDQQVGE 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 335 ILEVLEHEGLTDSTLVHFTSDNGAwleAQAGGEQLGGSNGvfrggkgmggweggIRVPGVFRWPGVLPRGRVLDQPVSLM 414
Cdd:cd16027 205 ILDELEEDGLLDNTIVIFTSDHGM---PFPRAKGTLYDSG--------------LRVPLIVRWPGKIKPGSVSDALVSFI 267
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 564336247 415 DVFPTVVRLGGGVLPSdrEIDGRDLLPLLRGETWHSAHEVLL--HYCEVFLHAVRWVQ 470
Cdd:cd16027 268 DLAPTLLDLAGIEPPE--YLQGRSFLPLLKGEKDPGRDYVFAerDRHDETYDPIRSVR 323
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
34-458 |
2.37e-52 |
|
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: 185.43 E-value: 2.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNGHrvlqwa 113
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 114 agagGLPPKEITFARILQGQGYVTGLVGKWHLGLScrtvsdlcHHPLNHGFHHFLGLPlgmmgdcagaepsekraglerr 193
Cdd:cd16031 76 ----LFDASQPTYPKLLRKAGYQTAFIGKWHLGSG--------GDLPPPGFDYWVSFP---------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 194 lrgagralaavavaiaalawGRgrglapacwapwaaialgavaaifeaGSYvvggavarYDCFLMRNATVTQQPLqldHV 273
Cdd:cd16031 122 --------------------GQ--------------------------GSY--------YDPEFIENGKRVGQKG---YV 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 274 TPLLLREAKDFLRRHRHA-PFLLFLSLLHTHTPLVTSPEFRGR------------------------------------- 315
Cdd:cd16031 145 TDIITDKALDFLKERDKDkPFCLSLSFKAPHRPFTPAPRHRGLyedvtipepetfddddyagrpewareqrnrirgvldg 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 316 --SAHGRYGDNVE-------EMDWVVGQILEVLEHEGLTDSTLVHFTSDNGAWLeaqagGE-QLGG-------Sngvfrg 378
Cdd:cd16031 225 rfDTPEKYQRYMKdylrtvtGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL-----GEhGLFDkrlmyeeS------ 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 379 gkgmggweggIRVPGVFRWPGVLPRGRVLDQPVSLMDVFPTVVRLGGGVLPSDreIDGRDLLPLLRGETWHS-AHEVLLH 457
Cdd:cd16031 294 ----------IRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYE 361
|
.
gi 564336247 458 Y 458
Cdd:cd16031 362 Y 362
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
34-479 |
2.73e-47 |
|
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: 171.09 E-value: 2.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLGIGDLGCYGNtSIRTPNIDRLAEDGVRLTQYLAAeSVCTPSRAAFLTGRYPIRSGMtsGNghrVLQWA 113
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGG-EIPTPNLDALAAEGLRFTNFHTT-ALCSPTRAALLTGRNHHQVGM--GT---MAELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 114 AGAGG----LPPKEITFARILQGQGYVTGLVGKWHLGLScrtvsdlchhplnhGFhhflglplgmmgdcagaepsekrag 189
Cdd:cd16025 75 TGKPGyegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD--------------DY------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 190 lerrlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvggavarydcflmrnatvtqqplq 269
Cdd:cd16025 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 270 ldHVTPLLLREAKDFLRRHRHA--PFLLFLSLLHTHTPLVTSPE----FRGRSAHG-------RY--------------- 321
Cdd:cd16025 116 --YSTDDLTDKAIEYIDEQKAPdkPFFLYLAFGAPHAPLQAPKEwidkYKGKYDAGwdalreeRLerqkelglipadtkl 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 322 ---GDN-------------------------VEEMDWVVGQILEVLEHEGLTDSTLVHFTSDNGA-----WleAQAGG-- 366
Cdd:cd16025 194 tprPPGvpawdslspeekklearrmevyaamVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGAsaepgW--ANASNtp 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 367 -------EQLGGsngvfrggkgmggweggIRVPGVFRWP-GVLPRGRVLDQPVSLMDVFPTVVRLGGGVLPSDRE----- 433
Cdd:cd16025 272 frlykqaSHEGG-----------------IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpql 334
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 564336247 434 -IDGRDLLPLLRGETWHSAHEVLlhYCEVFLHavRWVQRDSgqvWKA 479
Cdd:cd16025 335 pLDGVSLLPTLDGAAAPSRRRTQ--YFELFGN--RAIRKGG---WKA 374
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-441 |
3.30e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 163.56 E-value: 3.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPirsgmtsgNGHRVLQW-- 112
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMP--------SQHGIHDWiv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 113 ------AAGAGGLPPKEITFARILQGQGYVTGLVGKWHLGlscrtvsdlchhplnhgfhhflglplgmmgdcagaepsek 186
Cdd:cd16149 73 egshgkTKKPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG---------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 187 raglerrlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvggavarydcflmrnatvtqq 266
Cdd:cd16149 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 267 plqldhvtplllREAKDFLRRHRHA--PFLLFLSLLHTHTPlvtspefrgrsaHGrYGDNVEEMDWVVGQILEVLEHEGL 344
Cdd:cd16149 113 ------------DDAADFLRRRAEAekPFFLSVNYTAPHSP------------WG-YFAAVTGVDRNVGRLLDELEELGL 167
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 345 TDSTLVHFTSDN-------GAWleaqaggeqlGGSNGVFRggkgMGGWEGGIRVPGVFRWPGVLPRGRVLDQPVSLMDVF 417
Cdd:cd16149 168 TENTLVIFTSDNgfnmghhGIW----------GKGNGTFP----LNMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFF 233
|
410 420
....*....|....*....|....
gi 564336247 418 PTVVRLGGGVLPSDREIDGRDLLP 441
Cdd:cd16149 234 PTLLELAGVDPPADPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-446 |
8.26e-43 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 156.55 E-value: 8.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPirsgmtSGNGHrvlqWAa 114
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYV------HETGV----WD- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 115 GAGGLPPKEITFARILQGQGYVTGLVGKWHlglscrtvsdlchhplnhgfhhFLGlplgmMGDCAGAepsekraglerrl 194
Cdd:cd16037 70 NADPYDGDVPSWGHALRAAGYETVLIGKLH----------------------FRG-----EDQRHGF------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 195 rgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvggavaRYDcflmrnatvtqqplqlDHVT 274
Cdd:cd16037 110 ---------------------------------------------------------RYD----------------RDVT 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 275 plllREAKDFLRRHRHA--PFLLFLSLLHTHTPLVTSPEF------RGRSAhgrYGDNVEEMDWVVGQILEVLEHEGLTD 346
Cdd:cd16037 117 ----EAAVDWLREEAADdkPWFLFVGFVAPHFPLIAPQEFydlyvrRARAA---YYGLVEFLDENIGRVLDALEELGLLD 189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 347 STLVHFTSDNgawleaqagGEQLG-----GSNGVFRggkgmggweGGIRVPGVFRWPGVLPrGRVLDQPVSLMDVFPTVV 421
Cdd:cd16037 190 NTLIIYTSDH---------GDMLGerglwGKSTMYE---------ESVRVPMIISGPGIPA-GKRVKTPVSLVDLAPTIL 250
|
410 420
....*....|....*....|....*
gi 564336247 422 RLGGgvLPSDREIDGRDLLPLLRGE 446
Cdd:cd16037 251 EAAG--APPPPDLDGRSLLPLAEGP 273
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-447 |
6.26e-40 |
|
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: 150.83 E-value: 6.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSgNGHRVLqwaA 114
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLN-NVENAG---A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 115 GAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRtvsdlchhPLNHGFHHFLGLplgmmgdcagaEPSEKRaglerrl 194
Cdd:cd16033 77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEET--------PLDYGFDEYLPV-----------ETTIEY------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 195 rgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsYVVGGAVARydcflMRNATVTQQP--LQLDH 272
Cdd:cd16033 131 -------------------------------------------------FLADRAIEM-----LEELAADDKPffLRVNF 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 273 VTPlllreakdflrrhrHAPFLL---FLSL---------------------LH----THTPLVTSPEFRGRSAHGRYGDN 324
Cdd:cd16033 157 WGP--------------HDPYIPpepYLDMydpediplpesfaddfedkpyIYrrerKRWGVDTEDEEDWKEIIAHYWGY 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 325 VEEMDWVVGQILEVLEHEGLTDSTLVHFTSDNGAWLeaqaggeqlgGSNGVFRGGKGMGGWEGgiRVPGVFRWPGVLPRG 404
Cdd:cd16033 223 ITLIDDAIGRILDALEELGLADDTLVIFTSDHGDAL----------GAHRLWDKGPFMYEETY--RIPLIIKWPGVIAAG 290
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 564336247 405 RVLDQPVSLMDVFPTVVRLGGgvLPSDREIDGRDLLPLLRGET 447
Cdd:cd16033 291 QVVDEFVSLLDLAPTILDLAG--VDVPPKVDGRSLLPLLRGEQ 331
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
35-525 |
1.84e-38 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 144.64 E-value: 1.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGnghrvlqwaa 114
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDN---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 115 gAGGLPPKEITFARILQGQGYVTGLVGKWHLglscrtvsdlCHHPLNHGFHhflglplgmmgdcagaepsekraglerrl 194
Cdd:cd16032 71 -AAEFPADIPTFAHYLRAAGYRTALSGKMHF----------VGPDQLHGFD----------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 195 rgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvggavarYDcflmrnatvtqqplqlDHVT 274
Cdd:cd16032 111 ----------------------------------------------------------YD----------------EEVA 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 275 PLLLREAKDFLRRHRHAPFLLFLSLLHTHTPLVTSPEF----RGRSAHGRYGdNVEEMDWVVGQILEVLEHEGLTDSTLV 350
Cdd:cd16032 117 FKAVQKLYDLARGEDGRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIV 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 351 HFTSDNgawleaqagGEQLGGSNGVFRggkgMGGWEGGIRVPGVFRWPGVLPRGRVlDQPVSLMDVFPTVVRL-GGGVLP 429
Cdd:cd16032 196 IFTSDH---------GDMLGERGLWYK----MSFFEGSARVPLIISAPGRFAPRRV-AEPVSLVDLLPTLVDLaGGGTAP 261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 430 SDREIDGRDLLPLLRGETWHSAHEVLLHYC-EVFLHAVRWVQRDSgqvWKahFVtptfdplgsgscsgaggaaaVCPcvg 508
Cdd:cd16032 262 HVPPLDGRSLLPLLEGGDSGGEDEVISEYLaEGAVAPCVMIRRGR---WK--FI--------------------YCP--- 313
|
490
....*....|....*..
gi 564336247 509 kveeHDPPLLFELTSDP 525
Cdd:cd16032 314 ----GDPDQLFDLEADP 326
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
450-603 |
2.29e-34 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 126.66 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 450 SAHEVLLHYCEVFLHAVRWVQrdsgqvWKAHFVTPTFDPlgsgscsgaGGAAAVCPCVGKVEEHDPPLLFELTSDPGEVR 529
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDP---------PGAEGCYGSKVPVTHHDPPLLFDLERDPSEKY 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564336247 530 PLraPAKMSEAPNLTAAITseavtaamataarvrQEYDMLRPTAGHVPQQMGSLYNLWLPWLQPCCGHFPACAC 603
Cdd:pfam14707 66 PL--SPDSPEYPEVLAEIK---------------AAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-441 |
1.01e-33 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 129.59 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLgIGD-LGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRsgmtsgnghrvlqWA 113
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFY-------------HG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 114 AGAGGLPPKEITFARILQGQGYVTGLVgkwhlglscrtvSDLCHHPLNHGFHHflglplgmmgdcaGAEPSEKRAGLERR 193
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFDR-------------GFDTFEDFRGQEGD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 194 LRGAGralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvggavarydcflmrnatvtqqplqlDHV 273
Cdd:cd16148 122 PGEEG------------------------------------------------------------------------DER 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 274 TPLLLREAKDFLRRHRHA-PFLLFLSLLHTHTPLvtspefrgrsahgRYGDNVEEMDWVVGQILEVLEHEGLTDSTLVHF 352
Cdd:cd16148 130 AERVTDRALEWLDRNADDdPFFLFLHYFDPHEPY-------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIV 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 353 TSD-------NGAWleaqaGGEQLGGSNGVfrggkgmggweggIRVPGVFRWPGVLPRGRVlDQPVSLMDVFPTVVRLGG 425
Cdd:cd16148 197 TSDhgeefgeHGLY-----WGHGSNLYDEQ-------------LHVPLIIRWPGKEPGKRV-DALVSHIDIAPTLLDLLG 257
|
410
....*....|....*.
gi 564336247 426 GVLPSDreIDGRDLLP 441
Cdd:cd16148 258 VEPPDY--SDGRSLLP 271
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
34-458 |
5.04e-32 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 129.79 E-value: 5.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLGiGD-LGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTsgnghrvlqw 112
Cdd:PRK13759 6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 113 aaGAGGLPPK--EITFARILQGQGYVTGLVGKWHLglscrtvsdlchHPLN--HGFHHFlglplgMMGDcagaepsekra 188
Cdd:PRK13759 75 --GYGDVVPWnyKNTLPQEFRDAGYYTQCIGKMHV------------FPQRnlLGFHNV------LLHD----------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 189 GLERRLRGAGRALAAVAVAIAALAWGRGRGLAPAcwapwaaialgavaaIFEAGsyvvggavarYDCFlmrnaTVTQQPL 268
Cdd:PRK13759 124 GYLHSGRNEDKSQFDFVSDYLAWLREKAPGKDPD---------------LTDIG----------WDCN-----SWVARPW 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 269 QLD---HVTPLLLREAKDFLRRH-RHAPFLLFLSLLHTHTPL-------------------------------------- 306
Cdd:PRK13759 174 DLEerlHPTNWVGSESIEFLRRRdPTKPFFLKMSFARPHSPYdppkryfdmykdadipdphigdweyaedqdpeggsida 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 307 ---VTSPEFRGRSAHGRYGdNVEEMDWVVGQILEVLEHEGLTDSTLVHFTSDNgawleaqagGEQLgGSNGVFRggkGMG 383
Cdd:PRK13759 254 lrgNLGEEYARRARAAYYG-LITHIDHQIGRFLQALKEFGLLDNTIILFVSDH---------GDML-GDHYLFR---KGY 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 384 GWEGGIRVPGVFRWPG---VLPRGRVLDQPVSLMDVFPTVVRLGGGVLPsdREIDGRDLLPLLRG--ETW-------HSA 451
Cdd:PRK13759 320 PYEGSAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIP--DDVDGRSLKNLIFGqyEGWrpylhgeHAL 397
|
....*..
gi 564336247 452 HEVLLHY 458
Cdd:PRK13759 398 GYSSDNY 404
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-539 |
3.65e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 122.29 E-value: 3.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQ-YLA---AESVCTPSRAAFLTGRYPIRSGMtsgnghrv 109
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNMggwSGAVCVPSRAMLMTGRTLFHAPE-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 110 lqwaAGAGGLPPKEITFARILQGQGYVTGLVGKWHLGLSCRTVSDLCHHPLNH-------GFHHflglplgmmgdcagae 182
Cdd:cd16155 74 ----GGKAAIPSDDKTWPETFKKAGYRTFATGKWHNGFADAAIEFLEEYKDGDkpffmyvAFTA---------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 183 PSEKRAGLErrlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvgGAVARYDcflmrnAT 262
Cdd:cd16155 134 PHDPRQAPP--------------------------------------------------------EYLDMYP------PE 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 263 VTQQPLQLDHVTPllLREAKDFLRRHRHAPFllflsllhthtPLvTSPEFRGRSAhgRYGDNVEEMDWVVGQILEVLEHE 342
Cdd:cd16155 152 TIPLPENFLPQHP--FDNGEGTVRDEQLAPF-----------PR-TPEAVRQHLA--EYYAMITHLDAQIGRILDALEAS 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 343 GLTDSTLVHFTSDNGAwleaqAGGEQ--LGGSNGVFRggkgmggwegGIRVPGVFRWPGVlPRGRVLDQPVSLMDVFPTV 420
Cdd:cd16155 216 GELDNTIIVFTSDHGL-----AVGSHglMGKQNLYEH----------SMRVPLIISGPGI-PKGKRRDALVYLQDVFPTL 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 421 VRLGGgvLPSDREIDGRDLLPLLRGETwHSAHEVLLHyceVFLHAVRWVQRDsgqVWKAHFVTPtfdplgsgscsgagga 500
Cdd:cd16155 280 CELAG--IEIPESVEGKSLLPVIRGEK-KAVRDTLYG---AYRDGQRAIRDD---RWKLIIYVP---------------- 334
|
490 500 510
....*....|....*....|....*....|....*....
gi 564336247 501 aavcpcvgKVEEhdpPLLFELTSDPGEVRPLRAPAKMSE 539
Cdd:cd16155 335 --------GVKR---TQLFDLKKDPDELNNLADEPEYQE 362
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-447 |
1.39e-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: 118.49 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPirsgmtSGNGHRVLQWAa 114
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYP------HVNGHRTLHHL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 115 gaggLPPKEITFARILQGQGYVTGLVGKwhlglscrtvsdlchhplNHGFhhflglplgmmgdcagaepsekraglerrl 194
Cdd:cd16150 74 ----LRPDEPNLLKTLKDAGYHVAWAGK------------------NDDL------------------------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 195 rgagralaavavaiaalawgrgrglapacwapwaaialgavAAIFEAGSYVvggavaryDCflmrnatvtqqplqlDHVT 274
Cdd:cd16150 102 -----------------------------------------PGEFAAEAYC--------DS---------------DEAC 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 275 pllLREAKDFLRRHR-HAPFLLFLSLLHTHTPL-VTSPEF-------------------------RGRSAHGRYGDN--- 324
Cdd:cd16150 118 ---VRTAIDWLRNRRpDKPFCLYLPLIFPHPPYgVEEPWFsmidreklpprrppglrakgkpsmlEGIEKQGLDRWSeer 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 325 -----------VEEMDWVVGQILEVLEHEGLTDSTLVHFTSDNGAWL-------EAQAGGEQlggsngvfrggkgmggwe 386
Cdd:cd16150 195 wrelratylgmVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTgdyglveKWPNTFED------------------ 256
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564336247 387 GGIRVPGVFRWPGVLPrGRVLDQPVSLMDVFPTVVRLGGgvLPSDREIDGRDLLPLLRGET 447
Cdd:cd16150 257 CLTRVPLIIKPPGGPA-GGVSDALVELVDIPPTLLDLAG--IPLSHTHFGRSLLPVLAGET 314
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
35-531 |
1.65e-28 |
|
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: 118.90 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIrsgmtsgnGHRVLQwaa 114
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLM--------NHRSVW--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 115 GAGGLPPKEITFARILQGQGYVTGLVGKWHL-----GLSCRTVSDLCHHPLNHGFHHFLGLPLgmmgdcAGAEPSEKRAG 189
Cdd:cd16028 70 NGTPLDARHLTLALELRKAGYDPALFGYTDTspdprGLAPLDPRLLSYELAMPGFDPVDRLDE------YPAEDSDTAFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 190 LERRLRgagralaavavaiaalaWGRGRGlapacwapwaaialgaVAAIFEAGSYV------VggAVARYdcflmrNATV 263
Cdd:cd16028 144 TDRAIE-----------------YLDERQ----------------DEPWFLHLSYIrphppfV--APAPY------HALY 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 264 TQQPLQLDHVTPLLLREAKD--FLRRHRHAPFLlfLSLLHTHTPLVTSPEFRGRSAHGRYGDNVEEMDWVVGQILEVLEH 341
Cdd:cd16028 183 DPADVPPPIRAESLAAEAAQhpLLAAFLERIES--LSFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 342 EGLTDSTLVHFTSDNGawleAQAGGEQLGGSNGVFrggkgmggwEGGIRVPGVFRWPGVL---PRGRVLDQPVSLMDVFP 418
Cdd:cd16028 261 TGQWDDTLIVFTSDHG----EQLGDHWLWGKDGFF---------DQAYRVPLIVRDPRREadaTRGQVVDAFTESVDVMP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 419 TVVRLGGGvlPSDREIDGRDLLPLLRGET---WHSA-HEVLLHYCEVFLHAVRWVQRDSGQ-----VWKAHFVTPTFDPL 489
Cdd:cd16028 328 TILDWLGG--EIPHQCDGRSLLPLLAGAQpsdWRDAvHYEYDFRDVSTRRPQEALGLSPDEcslavIRDERWKYVHFAAL 405
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 564336247 490 gsgscsgaggaaavcpcvgkveehdPPLLFELTSDPGEVRPL 531
Cdd:cd16028 406 -------------------------PPLLFDLKNDPGELRDL 422
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-447 |
1.90e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 117.33 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMtsgngHRvlqwa 113
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 114 aGAGGLPPKEITFARILQGQGYVTGLVGKWHLglscrtvsdlchhplnhgfhhflglplgmmgdcagaepsekraglerr 193
Cdd:cd16152 71 -NGIPLPADEKTLAHYFRDAGYETGYVGKWHL------------------------------------------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 194 lrgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvggAVARYDCFlmrnatvtqqplqLDHv 273
Cdd:cd16152 102 -------------------------------------------------------AGYRVDAL-------------TDF- 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 274 tplllreAKDFLRRHRH-APFLLFLSLLHTH---------TPLVTSPEFRGR-----------SAHGRYGD---NVEEMD 329
Cdd:cd16152 113 -------AIDYLDNRQKdKPFFLFLSYLEPHhqndrdryvAPEGSAERFANFwvppdlaalpgDWAEELPDylgCCERLD 185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 330 WVVGQILEVLEHEGLTDSTLVHFTSDNGAWLEAQAGGEQLGGSNGVfrggkgmggweggIRVPGVFRWPGVLpRGRVLDQ 409
Cdd:cd16152 186 ENVGRIRDALKELGLYDNTIIVFTSDHGCHFRTRNAEYKRSCHESS-------------IRVPLVIYGPGFN-GGGRVEE 251
|
410 420 430
....*....|....*....|....*....|....*...
gi 564336247 410 PVSLMDVFPTVVRLGGgvLPSDREIDGRDLLPLLRGET 447
Cdd:cd16152 252 LVSLIDLPPTLLDAAG--IDVPEEMQGRSLLPLVDGKV 287
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
34-437 |
5.45e-28 |
|
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: 116.11 E-value: 5.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLgigDLGcYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTS----GNGHRV 109
Cdd:cd16147 1 RPNIVLILTDDQ---DVE-LGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNnsppGGGYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 110 LQWAagagGLPPKeiTFARILQGQGYVTGLVGKWhlgL-SCRTVSDLCHHPLnhGFHHFLGLPLGMMGDcagaepsekra 188
Cdd:cd16147 77 FWQN----GLERS--TLPVWLQEAGYRTAYAGKY---LnGYGVPGGVSYVPP--GWDEWDGLVGNSTYY----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 189 glerrlrgagralaavavaiaalAWgrgrglapacwapwaaialgavaaifeagSYVVGGAVARYDCFlmrnatvtqqpl 268
Cdd:cd16147 135 -----------------------NY-----------------------------TLSNGGNGKHGVSY------------ 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 269 QLDHVTPLLLREAKDFLRRHRHA--PFLLFLSLLHTHTPLVTSPE----FRGRSAHGRYG-------------------- 322
Cdd:cd16147 151 PGDYLTDVIANKALDFLRRAAADdkPFFLVVAPPAPHGPFTPAPRyanlFPNVTAPPRPPpnnpdvsdkphwlrrlppln 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 323 -DNVEEMDWV--------------VGQILEVLEHEGLTDSTLVHFTSDNGAWLeaqagGE--QLGGSNGVFRggkgmggw 385
Cdd:cd16147 231 pTQIAYIDELyrkrlrtlqsvddlVERLVNTLEATGQLDNTYIIYTSDNGYHL-----GQhrLPPGKRTPYE-------- 297
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 564336247 386 eGGIRVPGVFRWPGVlPRGRVLDQPVSLMDVFPTVVRLGGGVLPSDreIDGR 437
Cdd:cd16147 298 -EDIRVPLLVRGPGI-PAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
34-445 |
1.25e-27 |
|
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: 115.75 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLGiGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTsGNGHRvlqWA 113
Cdd:cd16030 2 KPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVY-DNNSY---FR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 114 AGAgglpPKEITFARILQGQGYVTGLVGK-WHLGLSCRTV-----SDLCHHPLNHGFHHFLGLPLGMMGDCAGAEPSekr 187
Cdd:cd16030 77 KVA----PDAVTLPQYFKENGYTTAGVGKiFHPGIPDGDDdpaswDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPA--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 188 aglerrlrgagralaavavaiaalaWGrgrglapacwapwaaialgavaaifeagsyvvggavarydcflmrnatVTQQP 267
Cdd:cd16030 150 -------------------------WE------------------------------------------------AADVP 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 268 lqlDHVTP--LLLREAKDFLRRHRHA--PFLLFLSLLHTHTPLV-----------------------TSPEFR------G 314
Cdd:cd16030 157 ---DEAYPdgKVADEAIEQLRKLKDSdkPFFLAVGFYKPHLPFVapkkyfdlyplesiplpnpfdpiDLPEVAwndlddL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 315 RSAHGRYGDNVEEMDWV-----------------------VGQILEVLEHEGLTDSTLVHFTSDNGaWleaqaggeQLG- 370
Cdd:cd16030 234 PKYGDIPALNPGDPKGPlpdeqarelrqayyasvsyvdaqVGRVLDALEELGLADNTIVVLWSDHG-W--------HLGe 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 371 ------GSNgvFRggkgmggweGGIRVPGVFRWPGVLPRGRVLDQPVSLMDVFPTVVRLGGgvLPSDREIDGRDLLPLLR 444
Cdd:cd16030 305 hghwgkHTL--FE---------EATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLK 371
|
.
gi 564336247 445 G 445
Cdd:cd16030 372 N 372
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
35-423 |
1.60e-26 |
|
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: 108.28 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLtQYLAAESVC--TPSRAAFLTGRYPIRSGMTsGNGHRVLQW 112
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYT-GNGSADPEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 113 AAGAGGLPPKEITFARILQGQGYVTGLVGkwhlglscrtvsdlchhplnhgfhhflglplgmmgdcagaepsekragler 192
Cdd:cd00016 79 PSRAAGKDEDGPTIPELLKQAGYRTGVIG--------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 193 rlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvggavarydcflmrnatvtqqplqldh 272
Cdd:cd00016 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 273 vtpllLREAKDFLRRHRhaPFLLFLSLLHTHTPLVTSpefrgRSAHGRYGDNVEEMDWVVGQILEVLEHEGLTDSTLVHF 352
Cdd:cd00016 108 -----LLKAIDETSKEK--PFVLFLHFDGPDGPGHAY-----GPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIV 175
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564336247 353 TSDNGAwleaqaggeQLGGSNGVFRGGKGMGGWEGGIRVPGVFRWPGVlPRGRVLDQPVSLMDVFPTVVRL 423
Cdd:cd00016 176 TADHGG---------IDKGHGGDPKADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADL 236
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-445 |
2.75e-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: 97.66 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADD--------LGIGDLGCygntsirtPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNG 106
Cdd:cd16035 1 PNILLILTDQerypppwpAGWAALNL--------PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 107 hrvlqwAAGAGGLPPKEITFARILQGQGYVTGLVGKWHLGlscrtvsdlchhplnhgfhhflglplgmmgdcagaepsek 186
Cdd:cd16035 73 ------SPMQPLLSPDVPTLGHMLRAAGYYTAYKGKWHLS---------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 187 raglerrlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvGGAVARYDcflmRNATVTQQ 266
Cdd:cd16035 107 ------------------------------------------------------------GAAGGGYK----RDPGIAAQ 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 267 plqldhvtplllreAKDFLRRHR-----HAPFLLFLSLLHTHTPLVTSPEFRG-RSAHGRYGDNVEEMDWVVGQILEVLE 340
Cdd:cd16035 123 --------------AVEWLRERGaknadGKPWFLVVSLVNPHDIMFPPDDEERwRRFRNFYYNLIRDVDRQIGRVLDALD 188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 341 HEGLTDSTLVHFTSDNGawleaqaggeQLGGSNG-------VFRggkgmggweGGIRVPGVFRWPGVLPRGRVLDQPVSL 413
Cdd:cd16035 189 ASGLADNTIVVFTSDHG----------EMGGAHGlrgkgfnAYE---------EALHVPLIISHPDLFGTGQTTDALTSH 249
|
410 420 430
....*....|....*....|....*....|....*.
gi 564336247 414 MDVFPTVVRLGGGVLPSDREID----GRDLLPLLRG 445
Cdd:cd16035 250 IDLLPTLLGLAGVDAEARATEApplpGRDLSPLLTD 285
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-439 |
7.15e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 95.91 E-value: 7.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 34 RPNFLIIMADDLGIGDLGCYGN----------TSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTs 103
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 104 GNG--HRVLQWAagagglppkEITFARILQGQGYVTGLVGKWHLglscrtvsdlchhplnhgfhhflglplgmmgdcaga 181
Cdd:cd16153 80 GFEaaHPALDHG---------LPTFPEVLKKAGYQTASFGKSHL------------------------------------ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 182 epsekraglerrlrgagralaavavaiaalawgrgrglapacwapwaaialgavaaifeagsyvvgGAVARYdcflMRNA 261
Cdd:cd16153 115 ------------------------------------------------------------------EAFQRY----LKNA 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 262 TVTQQplQLDHVTPLLLREAKdflrrhrhaPFLLFLSLLHTHTPLVTSPEFRGR---SAHGRYGDNveemdwVVGQILEV 338
Cdd:cd16153 125 NQSYK--SFWGKIAKGADSDK---------PFFVRLSFLQPHTPVLPPKEFRDRfdyYAFCAYGDA------QVGRAVEA 187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 339 LEHEGLT---DSTLVHFTSDNGAWLeaqagGEQlgGSNGVFrggkgmGGWEGGIRVPGVFRWPGVL--PRGRVLDQPVSL 413
Cdd:cd16153 188 FKAYSLKqdrDYTIVYVTGDHGWHL-----GEQ--GILAKF------TFWPQSHRVPLIVVSSDKLkaPAGKVRHDFVEF 254
|
410 420
....*....|....*....|....*.
gi 564336247 414 MDVFPTVVRLGGGVLPSDREIDGRDL 439
Cdd:cd16153 255 VDLAPTLLAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
35-145 |
4.48e-21 |
|
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: 96.68 E-value: 4.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYGNTSIRTPNIDRLAEDGVRLTQYLAAESVCTPSRAAFLTGRYPIRSGMTSGNghrvlqwaa 114
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNC--------- 71
|
90 100 110
....*....|....*....|....*....|...
gi 564336247 115 gaggLPPKE--ITFARILQGQGYVTGLVGKWHL 145
Cdd:cd16156 72 ----MALGDnvKTIGQRLSDNGIHTAYIGKWHL 100
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-146 |
2.11e-19 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 90.49 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 35 PNFLIIMADDLGIGDLGCYG-NTSI-RTPNIDRLAEDGVRLTQYLAAeSVCTPSRAAFLTGRYPIRSGMTsgnghrvlqW 112
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSlSSDLpVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVL---------A 70
|
90 100 110
....*....|....*....|....*....|....*.
gi 564336247 113 AAGAGGLPPKEITFARILQG--QGYVTGLVGKWHLG 146
Cdd:cd16154 71 VPDELLLSEETLLQLLIKDAttAGYSSAVIGKWHLG 106
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
292-457 |
4.38e-09 |
|
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: 58.71 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 292 PFLLFL--SLLHTHTPLVTSPEFRG-RSAHGRYGDNVEEMDWVVGQILEVLEHEGLTDSTLVHFTSDNGawleaqaggeQ 368
Cdd:cd16171 166 PFALYLglNLPHPYPSPSMGENFGSiRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHG----------E 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 369 LGGSNgvfRGGKGMGGWEGGIRVPGVFRWPGVlPRGRVLDQPVSLMDVFPTVVRLGGGVLPSDreIDGRDLLPLLRGETW 448
Cdd:cd16171 236 LAMEH---RQFYKMSMYEGSSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLLSESSI 309
|
....*....
gi 564336247 449 HSAHEVLLH 457
Cdd:cd16171 310 KESPSRVPH 318
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
280-451 |
2.69e-08 |
|
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: 56.84 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 280 EAKDFL-RRHRHAPFLLFLSLLHTH------------TPLVTSPEFRGRSAHG------RYGDNVEEMDWVVGQILEVLE 340
Cdd:COG3083 369 QWLQWLdQRDSDRPWFSYLFLDAPHaysfpadypkpfQPSEDCNYLALDNESDptpfknRYRNAVHYVDSQIGRVLDTLE 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 341 HEGLTDSTLVHFTSDNGawLEAQAGGEQLGGSNGVFRGGKgmggweggIRVPGVFRWPGVLPrgRVLDQPVSLMDVFPTV 420
Cdd:COG3083 449 QRGLLENTIVIITADHG--EEFNENGQNYWGHNSNFSRYQ--------LQVPLVIHWPGTPP--QVISKLTSHLDIVPTL 516
|
170 180 190
....*....|....*....|....*....|...
gi 564336247 421 VR--LGGGVLPSDREIdGRDLLPLLRGETWHSA 451
Cdd:COG3083 517 MQrlLGVQNPASDYSQ-GEDLFDPQRRRDWVLA 548
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
292-440 |
9.57e-05 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 45.41 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 292 PFLLFLSLLHTHTPLVTSPEFR-----GRSAHGRYGDNVEEMDWVVGQILEVLEHEGLTDSTLVHFTSDNGAWLEAQAGG 366
Cdd:COG1368 385 PFFAFLITLSNHGPYTLPEEDKkipdyGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDY 464
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564336247 367 EQLGGSNgvfrggkgmggweggiRVPGVFRWPGvLPRGRVLDQPVSLMDVFPTVVRLGGgvLPSDREID-GRDLL 440
Cdd:COG1368 465 ENPLERY----------------RVPLLIYSPG-LKKPKVIDTVGSQIDIAPTLLDLLG--IDYPSYYAfGRDLL 520
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|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
277-420 |
1.40e-03 |
|
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: 41.13 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336247 277 LLREAKDFLRRHRHAPFLLFLSLLHTHTPLVTSPEFRGRSAHGRYGDN--------VEEMDWVVGQILEVLEHEGLTDST 348
Cdd:cd16015 142 LFDQALEELEELKKKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTelenylnaIHYTDKALGEFIEKLKKSGLYENT 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564336247 349 LVHFTSDNGAWLEAQAGGEQLGGSNgvfrggkgmggwegGIRVPGVFRWPGVLPrGRVLDQPVSLMDVFPTV 420
Cdd:cd16015 222 IIVIYGDHLPSLGSDYDETDEDPLD--------------LYRTPLLIYSPGLKK-PKKIDRVGSQIDIAPTL 278
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