|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
40-473 |
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: 665.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALQWN 119
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 AGSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYFYGMPFTLTNDCDPGRPPEVDAALRAQ 199
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 200 LWGYTQFLALGILTLAAGQTCGFfsVSARAVTGMAGVGCLFFISWYSSFGFVRRWNCILMRNHDVTEQPMVLEKTASLML 279
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLYLGA--VSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 280 KEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGG 359
Cdd:cd16159 239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 360 HLEARDGHSQLGGWNGIYKGGKGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDRVIDGHS 439
Cdd:cd16159 319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
|
410 420 430
....*....|....*....|....*....|....
gi 530421102 440 LVPLLQGAEARSAHEFLFHYCGQHLHAARWHQKD 473
Cdd:cd16159 399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRD 432
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
40-471 |
2.59e-139 |
|
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: 405.79 E-value: 2.59e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngYRALQWN 119
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 AGSGGLPENETTFARILQQHGYATGLIGKWHQGvncasrgDH-CHHPLNHGFDYFYGMPFTltNDCDPGRPPEVDAALRa 198
Cdd:cd16026 76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYS--NDMWPFPLYRNDPPGP- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 199 qlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwNCILMRNHDVTEQPMVLEKTASLM 278
Cdd:cd16026 146 --------------------------------------------------------LPPLMENEEVIEQPADQSSLTQRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 279 LKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHG 358
Cdd:cd16026 170 TDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 359 GHLEARDGH-SQL-----------GGwngiykggkgmggweggIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVG 426
Cdd:cd16026 250 PWLEYGGHGgSAGplrggkgttweGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAG 312
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 530421102 427 GEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQ 471
Cdd:cd16026 313 APLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR 357
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
40-468 |
1.20e-106 |
|
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: 324.00 E-value: 1.20e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYrALQWn 119
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRV-FLPW- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 aGSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYF-YGMPFTLTNDCDPgrppevdaalra 198
Cdd:cd16160 79 -DIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFDFVgTNLPFTNSWACDD------------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 199 qlWGYTQflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfGFVRRWNCILMRNHDVTEQPMVLEKTASLM 278
Cdd:cd16160 146 --TGRHV-------------------------------------------DFPDRSACFLYYNDTIVEQPIQHEHLTETL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 279 LKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHG 358
Cdd:cd16160 181 VGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 359 GHLEardgHSQLGGwNGIYKGGKGMGGWEGGIRVPGIFHWPGVLPaGRVIGEPTSLMDVFPTVVQLVGGEVPQDRVIDGH 438
Cdd:cd16160 261 PHVE----YCLEGG-STGGLKGGKGNSWEGGIRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGL 334
|
410 420 430
....*....|....*....|....*....|
gi 530421102 439 SLVPLLQGAEARSAHEFLFHYCgQHLHAAR 468
Cdd:cd16160 335 SITDLLLGEADSPHDDILYYCC-SRLMAVR 363
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
41-459 |
1.47e-89 |
|
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: 279.43 E-value: 1.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM-DASNGYRALQWN 119
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItDVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 A------GSGGLPENETTFARILQQHGYATGLIGKWHQGvncasrGDHCHHPLNHGFDYFYGmpftltnDCDPGRPPevd 193
Cdd:cd16144 81 TklipppSTTRLPLEEVTIAEALKDAGYATAHFGKWHLG------GEGGYGPEDQGFDVNIG-------GTGNGGPP--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 194 aalraqlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiSWYSSFGFvrrwncilmrNHDVTEQPMVLEK 273
Cdd:cd16144 145 -------------------------------------------------SYYFPPGK----------PNPDLEDGPEGEY 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 274 TASLMLKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDN-----------VEEMDWLIGKVLNAIED 342
Cdd:cd16144 166 LTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELIEKYEKKKKGLRkgqknpvyaamIESLDESVGRILDALEE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 343 NGLKNSTFTYFTSDHGGHLEARDGHSQL------------GGwngiykggkgmggweggIRVPGIFHWPGVLPAGRVIGE 410
Cdd:cd16144 246 LGLADNTLVIFTSDNGGLSTRGGPPTSNaplrggkgslyeGG-----------------IRVPLIVRWPGVIKPGSVSDV 308
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 530421102 411 PTSLMDVFPTVVQLVGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLF-HY 459
Cdd:cd16144 309 PVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFwHF 358
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
40-459 |
2.33e-86 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 270.21 E-value: 2.33e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdASNGYralqwn 119
Cdd:COG3119 23 RPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGV-TDNGE------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 AGSGGLPENETTFARILQQHGYATGLIGKWHqgvncasrgdhchhplnhgfdyfygmpftltndcdpgrppevdaalraq 199
Cdd:COG3119 96 GYNGGLPPDEPTLAELLKEAGYRTALFGKWH------------------------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 200 lwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwnciLMRNHDVTEqpmvlektaslml 279
Cdd:COG3119 127 ----------------------------------------------------------LYLTDLLTD------------- 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 280 kEAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFLGK-----------------------SQHGLYGDNVEEMDWLIG 334
Cdd:COG3119 136 -KAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVG 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 335 KVLNAIEDNGLKNSTFTYFTSDHGGHLEA---RDGHSQL--GGwngiykggkgmggweggIRVPGIFHWPGVLPAGRVIG 409
Cdd:COG3119 215 RLLDALEELGLADNTIVVFTSDNGPSLGEhglRGGKGTLyeGG-----------------IRVPLIVRWPGKIKAGSVSD 277
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 530421102 410 EPTSLMDVFPTVVQLVGGEVPQDrvIDGHSLVPLLQGAEARSAHEFLFHY 459
Cdd:COG3119 278 ALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEY 325
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
41-458 |
1.68e-81 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 257.51 E-value: 1.68e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYG-NNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM--DASNGYRALQ 117
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLkgGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 118 wnagsggLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHH----------------PLNHGFDYFYGMPftlT 181
Cdd:cd16143 81 -------IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIP---A 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 182 NDCDPgrppevdaalraqlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwncilmrn 261
Cdd:cd16143 151 SEVLP--------------------------------------------------------------------------- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 262 hdvteqpmvlektasLMLKEAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNA 339
Cdd:cd16143 156 ---------------TLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDA 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 340 IEDNGLKNSTFTYFTSDHGGHLEARD------GHSQLGGWNGIYKGgkgmggweggI-----RVPGIFHWPGVLPAGRVI 408
Cdd:cd16143 221 LKELGLAENTLVIFTSDNGPSPYADYkelekfGHDPSGPLRGMKAD----------IyegghRVPFIVRWPGKIPAGSVS 290
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 530421102 409 GEPTSLMDVFPTVVQLVGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLFH 458
Cdd:cd16143 291 DQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH 340
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
40-464 |
2.82e-79 |
|
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: 251.62 E-value: 2.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTGDLGCYGN-NTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALqw 118
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 119 nagsGGLPENETTFARILQQHGYATGLIGKWHQGVNCAsrgdhcHHPLNHGFDYFYGMPFTltndcdpgrppevdaalra 198
Cdd:cd16161 79 ----GGLPLNETTLAEVLRQAGYATGMIGKWHLGQREA------YLPNSRGFDYYFGIPFS------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 199 qlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwncilmrnHDVTEQPMVLEKtaslm 278
Cdd:cd16161 130 ---------------------------------------------------------------HDSSLADRYAQF----- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 279 lkeAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFLGKSQH-GLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTS 355
Cdd:cd16161 142 ---ATDFIQRASAKdrPFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTS 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 356 DHGGHLEARDGHSQLGGWNGIYKGGKGMGGWEG---GIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQD 432
Cdd:cd16161 219 DNGPWEVKCELAVGPGTGDWQGNLGGSVAKASTwegGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPG 298
|
410 420 430
....*....|....*....|....*....|..
gi 530421102 433 RVIDGHSLVPLLQGaEARSAHEFLFHYCGQHL 464
Cdd:cd16161 299 RIYDGKDLSPVLFG-GSKTGHRCLFHPNSGAA 329
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
41-469 |
2.31e-76 |
|
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: 245.20 E-value: 2.31e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngyRALQWNA 120
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 121 GSGGLPENETTFARILQQHGYATGLIGKWHqgvncasRGDHCH--HPLNHGFDYFYGmpFTLTNDCDPGRPPEvdaalra 198
Cdd:cd16145 75 GQDPLPPDDVTLAEVLKKAGYATAAFGKWG-------LGGPGTpgHPTKQGFDYFYG--YLDQVHAHNYYPEY------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 199 qLW--GYTQFLAlgiltlaagQTCGFFSVSARAVTGMAGVgclffiswYSsfgfvrrwncilmrnHDvteqpmvlektas 276
Cdd:cd16145 139 -LWrnGEKVPLP---------NNVIPPLDEGNNAGGGGGT--------YS---------------HD------------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 277 LMLKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDN---------------VEEMDWLIGKVLNAIE 341
Cdd:cd16145 173 LFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDDGPYKYKPKDPGIYaylpwpqpekayaamVTRLDRDVGRILALLK 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 342 DNGLKNSTFTYFTSDHGGHLEARDGHSQL-----------------GGwngiykggkgmggweggIRVPGIFHWPGVLPA 404
Cdd:cd16145 253 ELGIDENTLVVFTSDNGPHSEGGSEHDPDffdsngplrgykrslyeGG-----------------IRVPFIARWPGKIPA 315
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530421102 405 GRVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHSLVPLLQGAEARSAHEFL---FHYCGQHlHAARW 469
Cdd:cd16145 316 GSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLyweFYEGGGA-QAVRM 380
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
40-471 |
6.37e-76 |
|
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.
Pssm-ID: 293777 [Multi-domain] Cd Length: 479 Bit Score: 245.82 E-value: 6.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngYRALQWN 119
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGV-----YPGVFYP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 AGSGGLPENETTFARILQQHGYATGLIGKWHQGVNcasrGDHCHHPLNHGFDYFYGMPFTltndcdpgrppevdaalraQ 199
Cdd:cd16158 76 GSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVG----LNGTYLPTHQGFDHYLGIPYS-------------------H 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 200 LWGYTQFLalgiltlaagqTCgffsvsaravtgmagvgclfFISWYSSFGFVRRW--NCILMRNHDVTEQPMVLEKTASL 277
Cdd:cd16158 133 DQGPCQNL-----------TC--------------------FPPNIPCFGGCDQGevPCPLFYNESIVQQPVDLLTLEER 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 278 MLKEAVSYIER--HKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTS 355
Cdd:cd16158 182 YAKFAKDFIADnaKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 356 DHGGHL--EARDGHSQL----------GGwngiykggkgmggweggIRVPGIFHWPGVLPAGRVIgEPTSLMDVFPTVVQ 423
Cdd:cd16158 262 DNGPSTmrKSRGGNAGLlkcgkgttyeGG-----------------VREPAIAYWPGRIKPGVTH-ELASTLDILPTIAK 323
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 530421102 424 LVGGEVPqDRVIDGHSLVPLLQGaEARSAHEFLFHYCGQH-----LHAARWHQ 471
Cdd:cd16158 324 LAGAPLP-NVTLDGVDMSPILFE-QGKSPRQTFFYYPTSPdpdkgVFAVRWGK 374
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
40-468 |
1.62e-75 |
|
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: 244.30 E-value: 1.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRAlqwN 119
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHAR---N 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 AGS-----GGLPENETTFARILQQHGYATGLIGKWHQGvncasrgdH--CHHPLNHGFDYFYGMPftltnDCDPGRPPEV 192
Cdd:cd16157 78 AYTpqnivGGIPDSEILLPELLKKAGYRNKIVGKWHLG--------HrpQYHPLKHGFDEWFGAP-----NCHFGPYDNK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 193 DaalRAQLWGYTQFLalgiltlaagqtcgffsvsaravtgMAGvgclffiSWYSSFGFvrrwncilmrNHDVTEQPMVle 272
Cdd:cd16157 145 A---YPNIPVYRDWE-------------------------MIG-------RYYEEFKI----------DKKTGESNLT-- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 273 ktaSLMLKEAVSYIERH--KHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTF 350
Cdd:cd16157 178 ---QIYLQEALEFIEKQhdAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTF 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 351 TYFTSDHGGhleARDGHSQLGGWNgIYKGGKGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVP 430
Cdd:cd16157 255 VFFSSDNGA---ALISAPEQGGSN-GPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIP 330
|
410 420 430
....*....|....*....|....*....|....*....
gi 530421102 431 QDRVIDGHSLVP-LLQGAEARSAHeflFHYCGQHLHAAR 468
Cdd:cd16157 331 SDRAIDGIDLLPvLLNGKEKDRPI---FYYRGDELMAVR 366
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
41-471 |
4.13e-74 |
|
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: 237.82 E-value: 4.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLR---TPNIDQLAEEGVRLTQHLAAaPLCTPSRAAFLTGRHSFRSGMdasngyRALQ 117
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVE-PSCTPGRAAFITGRHPIRTGL------TTVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 118 WNAGSGGLPENETTFARILQQHGYATGLIGKWHQGvncASRGdhcHHPLNHGFDYFYGMPFTltndcdpgrppEVDAALR 197
Cdd:cd16142 74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG---DEDG---RLPTDHGFDEFYGNLYH-----------TIDEEIV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 198 AQlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwncilmrnhdvteqpmvlektasl 277
Cdd:cd16142 137 DK------------------------------------------------------------------------------ 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 278 mlkeAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFLGKSQ-HGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFT 354
Cdd:cd16142 139 ----AIDFIKRNAKAdkPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFT 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 355 SDHGGHLEARDGHSQL-----------GGWngiykggkgmggweggiRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQ 423
Cdd:cd16142 215 TDNGPEQDVWPDGGYTpfrgekgttweGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAA 277
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 530421102 424 LVGGEVP------QDRVIDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQ 471
Cdd:cd16142 278 LAGAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN 331
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
41-439 |
2.78e-73 |
|
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: 230.79 E-value: 2.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngyraLQWNA 120
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGV--------RGNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 121 GSGGLPENETTFARILQQHGYATGLIGKWHQgvncasrgdhchhplnhgfdyfygmpftltndcdpgrppevdaalraql 200
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWHD------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 201 wgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwncilmrnhdvteqpmvlektaslmlk 280
Cdd:cd16022 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 281 EAVSYIERHKHG-PFLLFLSLLHVHIPLVttsaflgksqhglYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGG 359
Cdd:cd16022 104 EAIDFIERRDKDkPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 360 HLEarDGHSQLGGWNgiykggkgmgGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHS 439
Cdd:cd16022 171 MLG--DHGLRGKKGS----------LYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
41-457 |
6.88e-70 |
|
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: 227.82 E-value: 6.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQ-HlaAAPLCTPSRAAFLTGRHSFRSGMdasngyralqWN 119
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfH--VSPVCAPTRAALLTGRYPFRTGV----------WH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 AGSGG--LPENETTFARILQQHGYATGLIGKWHQGVNCAsrgdhcHHPLNHGFDYFYGmpftltndcdpgrppevdaaLR 197
Cdd:cd16146 69 TILGRerMRLDETTLAEVFKDAGYRTGIFGKWHLGDNYP------YRPQDRGFDEVLG--------------------HG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 198 AQLWGYTQFLALGiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvRRWNCILMRNHdvteqpmVLEKT--- 274
Cdd:cd16146 123 GGGIGQYPDYWGN-----------------------------------------DYFDDTYYHNG-------KFVKTegy 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 275 -ASLMLKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAF--------LGKSQHGLYGdNVEEMDWLIGKVLNAIEDNGL 345
Cdd:cd16146 155 cTDVFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYldpykdmgLDDKLAAFYG-MIENIDDNVGRLLAKLKELGL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 346 KNSTFTYFTSDHG----------GHLEARDGHSQLGGwngiykggkgmggweggIRVPGIFHWPGVLPAGRVIGEPTSLM 415
Cdd:cd16146 234 EENTIVIFMSDNGpaggvpkrfnAGMRGKKGSVYEGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHI 296
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 530421102 416 DVFPTVVQLVGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLF 457
Cdd:cd16146 297 DLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLF 338
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-459 |
6.50e-69 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 224.40 E-value: 6.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTqHLAAAPLCTPSRAAFLTGRHSFRSGmdasngyralqwnA 120
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNY-------------V 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 121 GSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASrGDHCHHplnHGFDYFYgmpftltndcdpgrppevdaalraqL 200
Cdd:cd16151 67 VFGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGD-GDYPHE---FGFDEYC-------------------------L 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 201 WGYTqflalgiltlaagqtcgffsvsaraVTGMAGvgclffiswysSFGFVRRWNCILMRNHDVTEQ---PmvlektaSL 277
Cdd:cd16151 118 WQLT-------------------------ETGEKY-----------SRPATPTFNIRNGKLLETTEGdygP-------DL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 278 MLKEAVSYIERHKHGPFLLFLSLLHVHIPLVTT--------SAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNST 349
Cdd:cd16151 155 FADFLIDFIERNKDQPFFAYYPMVLVHDPFVPTpdspdwdpDDKRKKDDPEYFPDMVAYMDKLVGKLVDKLEELGLRENT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 350 FTYFTSDHGGHLEA---RDGHSQLGGwngiykggkGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVG 426
Cdd:cd16151 235 IIIFTGDNGTHRPItsrTNGREVRGG---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAG 305
|
410 420 430
....*....|....*....|....*....|...
gi 530421102 427 GEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHY 459
Cdd:cd16151 306 APLPEDYPLDGRSFAPQLLGKTGSPRREWIYWY 338
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
41-426 |
3.15e-59 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 196.87 E-value: 3.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGyralqwna 120
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 121 gsGGLPENETTFARILQQHGYATGLIGKWHQGVNCASrgdhchHPLNHGFDYFYGMPFTLTNDCDPGRPPevdaalraql 200
Cdd:pfam00884 73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQ------SPCNLGFDKFFGRNTGSDLYADPPDVP---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 201 wgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrWNCILMRNHDVteqpmvlektasLMLK 280
Cdd:pfam00884 135 -----------------------------------------------------YNCSGGGVSDE------------ALLD 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 281 EAVSYIERHkHGPFLLFLSLLHVHIPL------------VTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNS 348
Cdd:pfam00884 150 EALEFLDNN-DKPFFLVLHTLGSHGPPyypdrypekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDN 228
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530421102 349 TFTYFTSDHGGHLEARDGHSQLGGWNgiykggkgmGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVG 426
Cdd:pfam00884 229 TLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-475 |
2.39e-56 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 192.01 E-value: 2.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdASNGYRalqwn 119
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGV-FGNDVP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 agsggLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHH----PLNHGFDYFYGMpftLTNDcDPGRPP-EVDA 194
Cdd:cd16034 75 -----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY---ECNH-DHNNPHyYDDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 195 ALRAQLWGYTqflalgiltlAAGQTcgffsvsaravtgmagvgclffiswyssfgfvrrwncilmrnhdvteqpmvlekt 274
Cdd:cd16034 146 GKRIYIKGYS----------PDAET------------------------------------------------------- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 275 aslmlKEAVSYIERHKHG--PFLLFLS------------------------LLHVHIPL-VTTSAFLGKSQHGLYGdNVE 327
Cdd:cd16034 161 -----DLAIEYLENQADKdkPFALVLSwnpphdpyttapeeyldmydpkklLLRPNVPEdKKEEAGLREDLRGYYA-MIT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 328 EMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGGHLEArdgHSQLG---GWNgiykggkgmggweGGIRVPGIFHWPGVLPA 404
Cdd:cd16034 235 ALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGS---HGLMNkqvPYE-------------ESIRVPFIIRYPGKIKA 298
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530421102 405 GRVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHSLVPLLQGAEARSAHEFLFhYCGQHLHAARWHQKDKR 475
Cdd:cd16034 299 GRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLL-QCFVPFGGGSARDGGEW 366
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
41-459 |
1.09e-55 |
|
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: 190.07 E-value: 1.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLaAAPLCTPSRAAFLTGRHSFRSGMdasngYRALQWNA 120
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYY-VQPICTPSRAALMTGRYPIHTGM-----QHGVILAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 121 GSGGLPENETTFARILQQHGYATGLIGKWHQGvncasrgdHCHH---PLNHGFDYFYGMpftltndcdpgrppevdaaLR 197
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYGY-------------------YG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 198 AQLWGYTQflalgiltlaagQTCGFFSvsaravtgmagvgclffiswyssfgfvrrWNCILMRNHDVTEQPMVLEKTASL 277
Cdd:cd16029 128 GAEDYYTH------------TSGGAND-----------------------------YGNDDLRDNEEPAWDYNGTYSTDL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 278 MLKEAVSYIERH-KHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDN----------VEEMDWLIGKVLNAIEDNGLK 346
Cdd:cd16029 167 FTDRAVDIIENHdPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKdedrrtyaamVSALDESVGNVVDALKAKGML 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 347 NSTFTYFTSDHGGHLEARDGHSQL-----------GGwngiykggkgmggweggIRVPGIFHWPGVLP-AGRVIGEPTSL 414
Cdd:cd16029 247 DNTLIVFTSDNGGPTGGGDGGSNYplrggkntlweGG-----------------VRVPAFVWSPLLPPkRGTVSDGLMHV 309
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 530421102 415 MDVFPTVVQLVGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHY 459
Cdd:cd16029 310 TDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNI 354
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
41-463 |
5.49e-54 |
|
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: 185.02 E-value: 5.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTgDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngyralQWNA 120
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---------HGLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 121 GSGG-LPENETTFARILQQHGYATGLIGKWHqgvncasrgdhchhplnHGFDYFYGMPFTLTNDCDPGRPPEVDAALRAq 199
Cdd:cd16027 71 SRGFpLPDGVKTLPELLREAGYYTGLIGKTH-----------------YNPDAVFPFDDEMRGPDDGGRNAWDYASNAA- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 200 lwgytQFLAlgilTLAAGQtcgffsvsaravtgmagvgclffiSWYSSFGFV---RRWncilmrNHDVTEQPMVLEKTAS 276
Cdd:cd16027 133 -----DFLN----RAKKGQ------------------------PFFLWFGFHdphRPY------PPGDGEEPGYDPEKVK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 277 LmlkeavsyierhkhGPFLlflsllhVHIPLVttsaflgKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSD 356
Cdd:cd16027 174 V--------------PPYL-------PDTPEV-------REDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSD 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 357 HGGhleardghsQL---------GGwngiykggkgmggweggIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGG 427
Cdd:cd16027 226 HGM---------PFprakgtlydSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGI 279
|
410 420 430
....*....|....*....|....*....|....*.
gi 530421102 428 EVPQDrvIDGHSLVPLLQGaEARSAHEFLFHYCGQH 463
Cdd:cd16027 280 EPPEY--LQGRSFLPLLKG-EKDPGRDYVFAERDRH 312
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
40-459 |
1.61e-49 |
|
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: 174.64 E-value: 1.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGyralqwn 119
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 agsGGLPENETTFARILQQHGYATGLIGKWHQGVNcasrgdhcHHPLNHGFDYFYGMPftltndcDPGR---PPEVDAAL 196
Cdd:cd16031 75 ---PLFDASQPTYPKLLRKAGYQTAFIGKWHLGSG--------GDLPPPGFDYWVSFP-------GQGSyydPEFIENGK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 197 RAQLWGYtqflalgiltlaagqtcgffsvSARAVTGMAgvgclffISWyssfgfvrrwnciLMRNHDvtEQPMVLektaS 276
Cdd:cd16031 137 RVGQKGY----------------------VTDIITDKA-------LDF-------------LKERDK--DKPFCL----S 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 277 LMLKeAV----SYIERHKHgpflLFLSllhVHIPLVTTSA---FLGKSQ-------------------HGLYGDNVE--- 327
Cdd:cd16031 169 LSFK-APhrpfTPAPRHRG----LYED---VTIPEPETFDdddYAGRPEwareqrnrirgvldgrfdtPEKYQRYMKdyl 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 328 ----EMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGGHLeardGHSQLGG-WNgiykggkgmgGWEGGIRVPGIFHWPGVL 402
Cdd:cd16031 241 rtvtGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL----GEHGLFDkRL----------MYEESIRVPLIIRDPRLI 306
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 530421102 403 PAGRVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHSLVPLLQGAEARS-AHEFLFHY 459
Cdd:cd16031 307 KAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEY 362
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-446 |
1.26e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 166.63 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdASNGYRAlqwNA 120
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGV-LNNVENA---GA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 121 GSGGLPENETTFARILQQHGYATGLIGKWHQGVNC--ASRGDHCHHPLNHGFDYFY--------------GMPFTLTNDC 184
Cdd:cd16033 77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEEtpLDYGFDEYLPVETTIEYFLadraiemleelaadDKPFFLRVNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 185 ----DPGRPPEvdaalraqlwgytQFLALgiltlaagqtcgffsvsARAVTgmagvgclffISWYSSFgfvrrwncilmr 260
Cdd:cd16033 157 wgphDPYIPPE-------------PYLDM-----------------YDPED----------IPLPESF------------ 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 261 NHDVTEQPMVLEKTaSLMLKEAVSYIERHKHgpfllflSLLHvhiplvttsaflgksqhglYGDNVEEMDWLIGKVLNAI 340
Cdd:cd16033 185 ADDFEDKPYIYRRE-RKRWGVDTEDEEDWKE-------IIAH-------------------YWGYITLIDDAIGRILDAL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 341 EDNGLKNSTFTYFTSDHGGHLEARDGHSQlgGWNGIYKGGkgmggweggiRVPGIFHWPGVLPAGRVIGEPTSLMDVFPT 420
Cdd:cd16033 238 EELGLADDTLVIFTSDHGDALGAHRLWDK--GPFMYEETY----------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPT 305
|
410 420
....*....|....*....|....*.
gi 530421102 421 VVQLVGGEVPQDrvIDGHSLVPLLQG 446
Cdd:cd16033 306 ILDLAGVDVPPK--VDGRSLLPLLRG 329
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-448 |
1.27e-46 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 164.25 E-value: 1.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRsgmdasNGYralqWNa 120
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHE------TGV----WD- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 121 GSGGLPENETTFARILQQHGYATGLIGKWHQGvncaSRGDhchhplNHGFDYfygmpftltndcdpgrppevDaalraql 200
Cdd:cd16037 70 NADPYDGDVPSWGHALRAAGYETVLIGKLHFR----GEDQ------RHGFRY--------------------D------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 201 wgytqflalgiltlaagqtcgffsvsaRAVTgmagvgclffiswyssfgfvrrwncilmrnhdvteqpmvlektaslmlK 280
Cdd:cd16037 113 ---------------------------RDVT------------------------------------------------E 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 281 EAVSYIERHKH--GPFLLFLSLLHVHIPLVTTSAFLGKSQHGL---YGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTS 355
Cdd:cd16037 118 AAVDWLREEAAddKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTS 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 356 DHGGHLEARdghsqlGGWNgiykggkGMGGWEGGIRVPGIFHWPGVlPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDRvi 435
Cdd:cd16037 198 DHGDMLGER------GLWG-------KSTMYEESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAPPPPDL-- 261
|
410
....*....|...
gi 530421102 436 DGHSLVPLLQGAE 448
Cdd:cd16037 262 DGRSLLPLAEGPD 274
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
40-449 |
3.61e-45 |
|
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.
Pssm-ID: 293754 [Multi-domain] Cd Length: 435 Bit Score: 163.13 E-value: 3.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTgDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSG-MDASNGYRALQW 118
Cdd:cd16030 2 KPNVLFIAVDDLRP-WLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGvYDNNSYFRKVAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 119 NAgsgglpeneTTFARILQQHGYATGLIGK-WHQGVnCASRGDHchhplnHGFDYFYGMPFTltndcdPGRPPEVDAALR 197
Cdd:cd16030 81 DA---------VTLPQYFKENGYTTAGVGKiFHPGI-PDGDDDP------ASWDEPPNPPGP------EKYPPGKLCPGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 198 AQLWGYTQFLALGILTLAAGQTCGFFSVS--ARAVTGMAGVGCLFFIswysSFGFVR---RWNC------------ILMR 260
Cdd:cd16030 139 KGGKGGGGGPAWEAADVPDEAYPDGKVADeaIEQLRKLKDSDKPFFL----AVGFYKphlPFVApkkyfdlyplesIPLP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 261 NHDVTEQ-PMVLEKTaslmLKEAVSYIERHKHGPFLLFLSL-LHVHIPLVttsaflgksqHGLYGdNVEEMDWLIGKVLN 338
Cdd:cd16030 215 NPFDPIDlPEVAWND----LDDLPKYGDIPALNPGDPKGPLpDEQARELR----------QAYYA-SVSYVDAQVGRVLD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 339 AIEDNGLKNSTFTYFTSDHGGHLeardG-HSQLG---GWNgiykggkgmggweGGIRVPGIFHWPGVLPAGRVIGEPTSL 414
Cdd:cd16030 280 ALEELGLADNTIVVLWSDHGWHL----GeHGHWGkhtLFE-------------EATRVPLIIRAPGVTKPGKVTDALVEL 342
|
410 420 430
....*....|....*....|....*....|....*
gi 530421102 415 MDVFPTVVQLVGgeVPQDRVIDGHSLVPLLQGAEA 449
Cdd:cd16030 343 VDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSA 375
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
40-457 |
4.80e-44 |
|
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: 159.53 E-value: 4.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTGDLGCYGNNtLRTPNIDQLAEEGVRLTQ-HlaAAPLCTPSRAAFLTGRHSFRSGMdASNGYRALQW 118
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 119 NAGSGGLPENETTFARILQQHGYATGLIGKWHQGVNcasrgdhchhplnhgfDYFYGMPFT------LTNDCDPGRP--- 189
Cdd:cd16025 78 PGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------------DYYSTDDLTdkaieyIDEQKAPDKPffl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 190 -------------PEVDA------------ALRAQLwgYTQFLALGIltLAAGQTcgffsVSARAVTgmagvgclffisw 244
Cdd:cd16025 142 ylafgaphaplqaPKEWIdkykgkydagwdALREER--LERQKELGL--IPADTK-----LTPRPPG------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 245 yssfgfVRRWNcilmrnhDVTEQpmvlEKT--ASLMlkeAVsYierhkhgpfllflsllhvhiplvttSAFlgksqhgly 322
Cdd:cd16025 200 ------VPAWD-------SLSPE----EKKleARRM---EV-Y-------------------------AAM--------- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 323 gdnVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGGHLEAR------------DGHSQLGGwngiykggkgmggweggI 390
Cdd:cd16025 225 ---VEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEPGwanasntpfrlyKQASHEGG-----------------I 284
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530421102 391 RVPGIFHWP-GVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDRV------IDGHSLVPLLQGAEARSAHEFLF 457
Cdd:cd16025 285 RTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRTQY 358
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
41-466 |
1.35e-41 |
|
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: 150.81 E-value: 1.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM-DasngyralqwN 119
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAyD----------N 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 AGSggLPENETTFARILQQHGYATGLIGKWH-----QgvncasrgdhchhplNHGFDYfygmpftltndcdpgrppEVDA 194
Cdd:cd16032 71 AAE--FPADIPTFAHYLRAAGYRTALSGKMHfvgpdQ---------------LHGFDY------------------DEEV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 195 ALRAQLWGYTqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwnciLMRNHDvteqpmvlekt 274
Cdd:cd16032 116 AFKAVQKLYD-----------------------------------------------------LARGED----------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 275 aslmlkeavsyiERhkhgPFLLFLSLLHVHIPLVTTSAFLG----KSQHGLYGdNVEEMDWLIGKVLNAIEDNGLKNSTF 350
Cdd:cd16032 132 ------------GR----PFFLTVSFTHPHDPYVIPQEYWDlyvrRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTI 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 351 TYFTSDHGGHLEARdghsqlGGWngiykggKGMGGWEGGIRVPGIFHWPGvLPAGRVIGEPTSLMDVFPTVVQLVGGEVP 430
Cdd:cd16032 195 VIFTSDHGDMLGER------GLW-------YKMSFFEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTA 260
|
410 420 430
....*....|....*....|....*....|....*..
gi 530421102 431 QDRV-IDGHSLVPLLQGAEARSAHEFLFHYCGQHLHA 466
Cdd:cd16032 261 PHVPpLDGRSLLPLLEGGDSGGEDEVISEYLAEGAVA 297
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-442 |
7.88e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 147.31 E-value: 7.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLgTGD-LGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRsgmdasngyralqWN 119
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFY-------------HG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 AGSGGLPENETTFARILQQHGYATGLIgkwhqgvncasrGDHCHHPLNHGFDYfygmpftltndcdpgrppevdaalraq 199
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFDR--------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 200 lwgytqflalgiltlaagqtcGFFSVsaravtgmagvgclFFISWYSSFGFVRRWNcilmrnhdvteqpmvlekTASLML 279
Cdd:cd16148 108 ---------------------GFDTF--------------EDFRGQEGDPGEEGDE------------------RAERVT 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 280 KEAVSYIERHKHG-PFLLFLSLLHVHIPLvttsaflgksqhgLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHG 358
Cdd:cd16148 135 DRALEWLDRNADDdPFFLFLHYFDPHEPY-------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 359 GHL-EardgHSQLGGWNgiykggkgMGGWEGGIRVPGIFHWPGVLPAGRvIGEPTSLMDVFPTVVQLVGGEVPQDrvIDG 437
Cdd:cd16148 202 EEFgE----HGLYWGHG--------SNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SDG 266
|
....*
gi 530421102 438 HSLVP 442
Cdd:cd16148 267 RSLLP 271
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-442 |
1.57e-39 |
|
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: 143.15 E-value: 1.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGR-------HSFRSGMDASNGY 113
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRmpsqhgiHDWIVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 114 RALQWnagsgglPENETTFARILQQHGYATGLIGKWHQGVNcasrgdhchhplnhgfdyfygmpftltndcdpgrppevd 193
Cdd:cd16149 81 KPEGY-------LEGQTTLPEVLQDAGYRCGLSGKWHLGDD--------------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 194 aalraqlwgytqflalgiltlaagqtcgffsvsaravtgmagvGCLFFIswyssfgfvrrwncilmRNHDvteqpmvlek 273
Cdd:cd16149 115 -------------------------------------------AADFLR-----------------RRAE---------- 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 274 taslmlkeavsyierhKHGPFLLFLSLLHVHiplvttsaflgkSQHGlYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYF 353
Cdd:cd16149 125 ----------------AEKPFFLSVNYTAPH------------SPWG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIF 175
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 354 TSDHG---GH---LEARDGHSQLGGWNgiykggkgmggweGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGG 427
Cdd:cd16149 176 TSDNGfnmGHhgiWGKGNGTFPLNMYD-------------NSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGV 242
|
410
....*....|....*
gi 530421102 428 EVPQDRVIDGHSLVP 442
Cdd:cd16149 243 DPPADPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-461 |
4.56e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 139.62 E-value: 4.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQ-HLAAA---PLCTPSRAAFLTGRHSFRSGMDasngyra 115
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNMGGwsgAVCVPSRAMLMTGRTLFHAPEG------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 116 lqwnaGSGGLPENETTFARILQQHGYATGLIGKWHQGVncasrgdhchhplnhgfdyfygmpftltndcdpgrppeVDAA 195
Cdd:cd16155 75 -----GKAAIPSDDKTWPETFKKAGYRTFATGKWHNGF--------------------------------------ADAA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 196 LRaqlwgytqFLAlgiltlaagqtcgffsvsARAVTGMAgvgclFFIswYSSFgfvrrwncilMRNHD---VTEQPMVLE 272
Cdd:cd16155 112 IE--------FLE------------------EYKDGDKP-----FFM--YVAF----------TAPHDprqAPPEYLDMY 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 273 KTASLMLKEavSYIERH--KHGPFLLFLSLLHvhiPLVTTSAFLgKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTF 350
Cdd:cd16155 149 PPETIPLPE--NFLPQHpfDNGEGTVRDEQLA---PFPRTPEAV-RQHLAEYYAMITHLDAQIGRILDALEASGELDNTI 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 351 TYFTSDHGghLeARDGHSQLGGWNgiykggkgmgGWEGGIRVPGIFHWPGVlPAGRVIGEPTSLMDVFPTVVQLVGGEVP 430
Cdd:cd16155 223 IVFTSDHG--L-AVGSHGLMGKQN----------LYEHSMRVPLIISGPGI-PKGKRRDALVYLQDVFPTLCELAGIEIP 288
|
410 420 430
....*....|....*....|....*....|..
gi 530421102 431 QDrvIDGHSLVPLLQGaEARSAHEFLF-HYCG 461
Cdd:cd16155 289 ES--VEGKSLLPVIRG-EKKAVRDTLYgAYRD 317
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
40-449 |
2.30e-35 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 137.11 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLgTGD-LGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasNGYralqw 118
Cdd:PRK13759 6 KPNIILIMVDQM-RGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGR---VGY----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 119 naGSGGLPENETTFARILQQHGYATGLIGKWHqgvncasrgdhcHHPLN--HGFDYfygmpfTLTNDCDPGRPPEVDAAL 196
Cdd:PRK13759 77 --GDVVPWNYKNTLPQEFRDAGYYTQCIGKMH------------VFPQRnlLGFHN------VLLHDGYLHSGRNEDKSQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 197 RAQLWGYTQFLALGILTLAAGQTcgffsvsaravtgmaGVGclffiswyssfgfvrrWNC--ILMRNHDVTEQpmvLEKT 274
Cdd:PRK13759 137 FDFVSDYLAWLREKAPGKDPDLT---------------DIG----------------WDCnsWVARPWDLEER---LHPT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 275 AsLMLKEAVSYIERHKHG-PFLLFLSLLHVHIPLVTTSAFL-------------------------GKSQHGLYGD---- 324
Cdd:PRK13759 183 N-WVGSESIEFLRRRDPTkPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgee 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 325 -----------NVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDH----GGHLEARDGHSQLGGwngiykggkgmggwegg 389
Cdd:PRK13759 262 yarraraayygLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHgdmlGDHYLFRKGYPYEGS----------------- 324
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530421102 390 IRVPGIFHWPG---VLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHSLVPLLQGAEA 449
Cdd:PRK13759 325 AHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYE 385
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
41-448 |
1.46e-34 |
|
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: 134.31 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFrsgmdasnGYRALqWNA 120
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLM--------NHRSV-WNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 121 GSggLPENETTFARILQQHGYATGLIGKWHQGVNcaSRGdhcHHPLnhgfdyfygmpftltndcDPgrppevdaalraQL 200
Cdd:cd16028 72 TP--LDARHLTLALELRKAGYDPALFGYTDTSPD--PRG---LAPL------------------DP------------RL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 201 WGYtqflalgiltlaAGQTCGFfsvsaravtgmagvgclffiSWYSSFGFVRRwncilmRNHDvteqpmvlekTASLMlK 280
Cdd:cd16028 115 LSY------------ELAMPGF--------------------DPVDRLDEYPA------EDSD----------TAFLT-D 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 281 EAVSYIERHKHGPFLLFLSLLHVHIPLV-------------------TTSAFLGKSQH-------------GLYGDN--- 325
Cdd:cd16028 146 RAIEYLDERQDEPWFLHLSYIRPHPPFVapapyhalydpadvpppirAESLAAEAAQHpllaaflerieslSFSPGAana 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 326 ------------------VEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGGHLeardG-HSQLG--GWNGIYKggkgmg 384
Cdd:cd16028 226 adlddeevaqmratylglIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQL----GdHWLWGkdGFFDQAY------ 295
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530421102 385 gweggiRVPGIFHWPGVL---PAGRVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHSLVPLLQGAE 448
Cdd:cd16028 296 ------RVPLIVRDPRREadaTRGQVVDAFTESVDVMPTILDWLGGEIPHQ--CDGRSLLPLLAGAQ 354
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-446 |
1.74e-33 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 130.04 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngYRalqwN 119
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR----N 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 AGSggLPENETTFARILQQHGYATGLIGKWHqgvncasrgdhchhplnhgfdyfygmpftltndcdpgrppevdaalraq 199
Cdd:cd16152 72 GIP--LPADEKTLAHYFRDAGYETGYVGKWH------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 200 LWGYtqflalgiltlaagqtcgffsvSARAVTGMagvgclffiswyssfgfvrrwncilmrnhdvteqpmvlektaslml 279
Cdd:cd16152 101 LAGY----------------------RVDALTDF---------------------------------------------- 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 280 keAVSYIERHKHG-PFLLFLSLLHVH----------------------IP--LvttSAFLGKSQHGL---YGdNVEEMDW 331
Cdd:cd16152 113 --AIDYLDNRQKDkPFFLFLSYLEPHhqndrdryvapegsaerfanfwVPpdL---AALPGDWAEELpdyLG-CCERLDE 186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 332 LIGKVLNAIEDNGLKNSTFTYFTSDHGGHLEARDG------HSqlggwngiykggkgmggweGGIRVPGIFHWPGVLpAG 405
Cdd:cd16152 187 NVGRIRDALKELGLYDNTIIVFTSDHGCHFRTRNAeykrscHE-------------------SSIRVPLVIYGPGFN-GG 246
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 530421102 406 RVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHSLVPLLQG 446
Cdd:cd16152 247 GRVEELVSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDG 285
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-449 |
2.36e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 121.96 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGR--HsfrsgmdaSNGYRALqw 118
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWypH--------VNGHRTL-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 119 nagSGGLPENETTFARILQQHGYATGLIGKwhqgvncasrgdhchhplnhgfdyfygmpftltNDCDPGRppevdaalra 198
Cdd:cd16150 71 ---HHLLRPDEPNLLKTLKDAGYHVAWAGK---------------------------------NDDLPGE---------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 199 qlwgytqflalgiltLAAGQTCgffsvsaravtgmagvgclffiswyssfgfVRRWNCIlmrnhdvteqpmvlektaslm 278
Cdd:cd16150 105 ---------------FAAEAYC------------------------------DSDEACV--------------------- 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 279 lKEAVSYIERHK-HGPFLLFLSLLHVH------------------IPLVTT--------SAFLGKSQHGLYGDN------ 325
Cdd:cd16150 119 -RTAIDWLRNRRpDKPFCLYLPLIFPHppygveepwfsmidreklPPRRPPglrakgkpSMLEGIEKQGLDRWSeerwre 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 326 --------VEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHG------GHLEARDG--HSQLggwngiykggkgmggwegg 389
Cdd:cd16150 198 lratylgmVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGdytgdyGLVEKWPNtfEDCL------------------- 258
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 390 IRVPGIFHWPGvLPAGRVIGEPTSLMDVFPTVVQLVGgeVPQDRVIDGHSLVPLLQGAEA 449
Cdd:cd16150 259 TRVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAG--IPLSHTHFGRSLLPVLAGETE 315
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
40-439 |
3.05e-29 |
|
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: 118.42 E-value: 3.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLgtgDLGCYGNNTLRtPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM----DASNGYRA 115
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVtnnsPPGGGYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 116 lQWNAGsgglpENETTFARILQQHGYATGLIGKWHQGVNcaSRGDHCHHPLnhGFDYFYGMPFTLTNDcdpgrppevdaa 195
Cdd:cd16147 77 -FWQNG-----LERSTLPVWLQEAGYRTAYAGKYLNGYG--VPGGVSYVPP--GWDEWDGLVGNSTYY------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 196 lraqlwGYTqflalgiltlaagqtcgffsvsarAVTGMAGVGCLFFISWYSSfgfvrrwncilmrnhDVteqpmVLEKta 275
Cdd:cd16147 135 ------NYT------------------------LSNGGNGKHGVSYPGDYLT---------------DV-----IANK-- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 276 slmlkeAVSYIERHKHG--PFLLFLSLLHVHIPLV-----------------TTSAFLGKSQH--------GLYGDNVEE 328
Cdd:cd16147 163 ------ALDFLRRAAADdkPFFLVVAPPAPHGPFTpapryanlfpnvtapprPPPNNPDVSDKphwlrrlpPLNPTQIAY 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 329 MDW--------------LIGKVLNAIEDNGLKNSTFTYFTSDHGGHLeardG-HSQLGGwngiykggkGMGGWEGGIRVP 393
Cdd:cd16147 237 IDElyrkrlrtlqsvddLVERLVNTLEATGQLDNTYIIYTSDNGYHL----GqHRLPPG---------KRTPYEEDIRVP 303
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 530421102 394 GIFHWPGVlPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHS 439
Cdd:cd16147 304 LLVRGPGI-PAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGRS 346
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
41-450 |
3.67e-29 |
|
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: 119.41 E-value: 3.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngyralqWnA 120
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------W-T 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 121 GSGGLPENETTFARILQQHGYATGLIGKWHqgvncasrgdhchhpLNhGFDYF-YGMpftltndCDPGRPPEvdaalraq 199
Cdd:cd16156 70 NCMALGDNVKTIGQRLSDNGIHTAYIGKWH---------------LD-GGDYFgNGI-------CPQGWDPD-------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 200 lwgYtqflalgiltlaagqtcgffsvsaravtgmagvgclffisWYSsfgfvrrwncilMRNH--DVTEQPMVLEKTASL 277
Cdd:cd16156 119 ---Y----------------------------------------WYD------------MRNYldELTEEERRKSRRGLT 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 278 ML----------------KEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAF----------LGKSQHglygDNVEE--- 328
Cdd:cd16156 144 SLeaegikeeftyghrctNRALDFIEKHKDEDFFLVVSYDEPHHPFLCPKPYasmykdfefpKGENAY----DDLENkpl 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 329 ------------------------------MDWLIGKVLNAIEDNgLKNSTFTYfTSDHGGHLEARDGHSQlggwngiyk 378
Cdd:cd16156 220 hqrlwagakphedgdkgtikhplyfgcnsfVDYEIGRVLDAADEI-AEDAWVIY-TSDHGDMLGAHKLWAK--------- 288
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530421102 379 ggkGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGgeVPQDRVIDGHSLVPLLQGAEAR 450
Cdd:cd16156 289 ---GPAVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATIEDPEIP 355
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-441 |
7.52e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 112.08 E-value: 7.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 40 KPNILLIMADDLGTGDLGCYGN----------NTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDA 109
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 110 SNGYralqWNAGSGGLPenetTFARILQQHGYATGLIGKWHqgvncasrgdhchhplnhgfdyfygmpftltndcdpgrp 189
Cdd:cd16153 81 FEAA----HPALDHGLP----TFPEVLKKAGYQTASFGKSH--------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 190 peVDAALRaqlwgYTQflalgiltlAAGQTcgFFSVSARAVTGMAGvgclffiswyssfgfvrrwncilmrnhdvteqpm 269
Cdd:cd16153 114 --LEAFQR-----YLK---------NANQS--YKSFWGKIAKGADS---------------------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 270 vlektaslmlkeavsyierhkHGPFLLFLSLLHVHIPLVTTSAFlgkSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKN-- 347
Cdd:cd16153 142 ---------------------DKPFFVRLSFLQPHTPVLPPKEF---RDRFDYYAFCAYGDAQVGRAVEAFKAYSLKQdr 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 348 -STFTYFTSDHGGHLEARDGHSQLGGWNgiykggkgmggweGGIRVPGIFHWPGVL--PAGRVIGEPTSLMDVFPTVVQL 424
Cdd:cd16153 198 dYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QSHRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTLLAA 264
|
410
....*....|....*..
gi 530421102 425 VGGEVPQDRVIDGHSLV 441
Cdd:cd16153 265 AGVDVDAPDYLDGRDLF 281
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
41-424 |
3.13e-27 |
|
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: 109.05 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRL-TQHLAAAPLCTPSRAAFLTGRHSFRSGMdASNGYRALQWN 119
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGY-TGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 120 AGSGGLPENETTFARILQQHGYATGLIGkwhqgvncasrgdhchhplnhgfdyfygmpftltndcdpgrppevdaalraq 199
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG---------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 200 lwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwncilmrnhdvteqpmvlektaslmL 279
Cdd:cd00016 108 -------------------------------------------------------------------------------L 108
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 280 KEAVSYIERHKhgPFLLFLSLLHVHIPLvttsaFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGG 359
Cdd:cd00016 109 LKAIDETSKEK--PFVLFLHFDGPDGPG-----HAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG 181
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530421102 360 HLEardGHSQLGGwngiykGGKGMGGWEGGIRVPGIFHWPGVlPAGRVIGEPTSLMDVFPTVVQL 424
Cdd:cd00016 182 IDK---GHGGDPK------ADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADL 236
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-449 |
3.14e-25 |
|
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: 106.67 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTL--RTPNIDQLAEEGVRLTqHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRAlqw 118
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGVLAVPDELL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 119 nagsggLPENETTFARILQQ--HGYATGLIGKWHQGvncasrGDHCHHPLNHGFDYFYGmpftltndcdpgrppevdaAL 196
Cdd:cd16154 77 ------LSEETLLQLLIKDAttAGYSSAVIGKWHLG------GNDNSPNNPGGIPYYAG-------------------IL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 197 RAQLWGYTQflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrWNcilMRNHDVTEQpmVLEKTAS 276
Cdd:cd16154 126 GGGVQDYYN------------------------------------------------WN---LTNNGQTTN--STEYATT 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 277 LMLKEAVSYIERhKHGPFLLFLSLL--HV--HIP--------LVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNG 344
Cdd:cd16154 153 KLTNLAIDWIDQ-QTKPWFLWLAYNapHTpfHLPpaelhsrsLLGDSADIEANPRPYYLAAIEAMDTEIGRLLASIDEEE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 345 LKNsTFTYFTSDHGGHLEARD-----GHSQ----LGGwngiykggkgmggweggIRVPGIFHWPGVlpaGRVIGEPTSLM 415
Cdd:cd16154 232 REN-TIIIFIGDNGTPGQVVDlpytrNHAKgslyEGG-----------------INVPLIVSGAGV---ERANERESALV 290
|
410 420 430
....*....|....*....|....*....|....*..
gi 530421102 416 ---DVFPTVVQLVGGEVPQdrVIDGHSLVPLLQGAEA 449
Cdd:cd16154 291 natDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNA 325
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-459 |
8.55e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 98.43 E-value: 8.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMAD------DLGTGDLGcygnntLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDAsngyr 114
Cdd:cd16035 1 PNILLILTDqeryppPWPAGWAA------LNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTD----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 115 alqwNAGSGGLPENETTF---ARILQQHGYATGLIGKWHqgvncasrgdhchhplnhgfdyfygmpftltndcdpgrppe 191
Cdd:cd16035 70 ----TLGSPMQPLLSPDVptlGHMLRAAGYYTAYKGKWH----------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 192 vdaaLRAQLWGYTQFlalgiltlaagqtcgffsvsARAVTGMAgvgclffISWyssfgfvrrwncilMRNHDVteqpmvl 271
Cdd:cd16035 105 ----LSGAAGGGYKR--------------------DPGIAAQA-------VEW--------------LRERGA------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 272 ektaslmlkeavsyiERHKHGPFLLFLSLLHVH----IPLVTTSAFLgksQHGLYGDNVEEMDWLIGKVLNAIEDNGLKN 347
Cdd:cd16035 133 ---------------KNADGKPWFLVVSLVNPHdimfPPDDEERWRR---FRNFYYNLIRDVDRQIGRVLDALDASGLAD 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 348 STFTYFTSDHGGHLEARDGHSQLGgwngiykggkgmGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGG 427
Cdd:cd16035 195 NTIVVFTSDHGEMGGAHGLRGKGF------------NAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGV 262
|
410 420 430
....*....|....*....|....*....|....*..
gi 530421102 428 EVPQDRVID----GHSLVPLLQGAEARSAHE-FLFHY 459
Cdd:cd16035 263 DAEARATEApplpGRDLSPLLTDADADAVRDgILFTY 299
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
41-444 |
1.44e-22 |
|
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: 98.77 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSfrsgmdasngYRALQWNa 120
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT----------HLTESWN- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 121 GSGGLPENETTFARILQQHGYATGLIGK--WHQGvncasrgdhcHHPLNHGFD-YFYGMPFTLTNDcdpGRPpevdaalR 197
Cdd:cd16171 70 NYKGLDPNYPTWMDRLEKHGYHTQKYGKldYTSG----------HHSVSNRVEaWTRDVPFLLRQE---GRP-------T 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 198 AQLWGytqflalgiltlaagqtcgffsvSARAVTGMAgvgclffiswyssfgfvRRWNcilmrnhdvteqpmVLEKTASL 277
Cdd:cd16171 130 VNLVG-----------------------DRSTVRVML-----------------KDWQ--------------NTDKAVHW 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 278 MLKEAVSYIErhkhgPFLLFLSLlhvHIPLVTTSAFLGKSQHGL------YGDNVEEMDWLIGKVLNAIEDNGLKNSTFT 351
Cdd:cd16171 156 IRKEAPNLTQ-----PFALYLGL---NLPHPYPSPSMGENFGSIrnirafYYAMCAETDAMLGEIISALKDTGLLDKTYV 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 352 YFTSDHGghlEARDGHSQLggwngiykggKGMGGWEGGIRVPGIFHWPGVlPAGRVIGEPTSLMDVFPTVVQLVGGEVPQ 431
Cdd:cd16171 228 FFTSDHG---ELAMEHRQF----------YKMSMYEGSSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
|
410
....*....|...
gi 530421102 432 DrvIDGHSLVPLL 444
Cdd:cd16171 294 N--LSGYSLLPLL 304
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
287-423 |
5.12e-09 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 58.38 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 287 ERHKHGPFLLFLSLLHVHI------------------PLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNS 348
Cdd:COG3083 376 QRDSDRPWFSYLFLDAPHAysfpadypkpfqpsedcnYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLEN 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530421102 349 TFTYFTSDHGGHLEARDGHSQLGGWNGIYKGgkgmggweggIRVPGIFHWPGVLPagRVIGEPTSLMDVFPTVVQ 423
Cdd:COG3083 456 TIVIITADHGEEFNENGQNYWGHNSNFSRYQ----------LQVPLVIHWPGTPP--QVISKLTSHLDIVPTLMQ 518
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
451-471 |
2.21e-07 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 49.62 E-value: 2.21e-07
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
41-426 |
8.64e-07 |
|
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: 50.37 E-value: 8.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRA--AFLTGRHSFRSGMDASNGYRalqw 118
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 119 nagsgglPENETTFARILQQHGYATGLIgkwhqgvncasrgdhchhplnHGFD-YFYGMpftltndcdpgrppevDAALR 197
Cdd:cd16015 77 -------LNPLPSLPSILKEQGYETIFI---------------------HGGDaSFYNR----------------DSVYP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 198 AQlwGYTQFLalgiltlaagqTCGFFSVSARavtgmagvgclFFISWYSSfgfvrrwncilmrnhDvteqpmvlektaSL 277
Cdd:cd16015 113 NL--GFDEFY-----------DLEDFPDDEK-----------ETNGWGVS---------------D------------ES 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 278 MLKEAVSYIERHKHGPFLLFLSLLHVH----IPLVTTSAFLGKSQHGLYGDN----VEEMDWLIGKVLNAIEDNGL-KNS 348
Cdd:cd16015 142 LFDQALEELEELKKKPFFIFLVTMSNHgpydLPEEKKDEPLKVEEDKTELENylnaIHYTDKALGEFIEKLKKSGLyENT 221
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530421102 349 TFtYFTSDHGGHLEARDGHSQLGGWNGIykggkgmggweggiRVPGIFHWPGVLPaGRVIGEPTSLMDVFPTVVQLVG 426
Cdd:cd16015 222 II-VIYGDHLPSLGSDYDETDEDPLDLY--------------RTPLLIYSPGLKK-PKKIDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
33-440 |
2.99e-06 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 49.65 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 33 PKTANAFKPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAaaplctpsraaflTGRHSFRS------G 106
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYS-------------QGGRTSRGefavltG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 107 MDASNGYRALQwnagsggLPENET--TFARILQQHGYATGLIgkwhqgvncasrgdhchhplnHGFD-YFYGMpftltnd 183
Cdd:COG1368 294 LPPLPGGSPYK-------RPGQNNfpSLPSILKKQGYETSFF---------------------HGGDgSFWNR------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 184 cdpgrppevDAALRAQlwGYTQFLALGiltlaagqtcgFFSVSARAVTGMagvgclffiswyssfgfvrrwncilmrnHD 263
Cdd:COG1368 339 ---------DSFYKNL--GFDEFYDRE-----------DFDDPFDGGWGV----------------------------SD 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 264 vteqpmvlektaSLMLKEAVSYIERHKhGPFLLFLsllhvhiplVTTS--------------AFLGKSQHGLYGDNVEEM 329
Cdd:COG1368 369 ------------EDLFDKALEELEKLK-KPFFAFL---------ITLSnhgpytlpeedkkiPDYGKTTLNNYLNAVRYA 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421102 330 DWLIGKVLNAIEDNGL-KNSTFtYFTSDHGGHLEARDGHSQLggwngiykggkgmggwEGGIRVPGIFHWPGvLPAGRVI 408
Cdd:COG1368 427 DQALGEFIEKLKKSGWyDNTIF-VIYGDHGPRSPGKTDYENP----------------LERYRVPLLIYSPG-LKKPKVI 488
|
410 420 430
....*....|....*....|....*....|..
gi 530421102 409 GEPTSLMDVFPTVVQLVGGEVPQDRVIdGHSL 440
Cdd:COG1368 489 DTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDL 519
|
|
| |
