|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
40-518 |
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: 712.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALQWN 119
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 120 AGSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYFYGMPFTLTNDCDPGRPPEVDAALRAQ 199
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 200 LWGYTQFLALGILTLAAGQTCGFfsVSARAVTGMAGVGCLFFISWYSSFGFVRRWNCILMRNHDVTEQPMVLEKTASLML 279
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLYLGA--VSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 280 KEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGG------------------------ 335
Cdd:cd16159 239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQildaldelglkdntfvyftsdngg 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 336 ---------------------KGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDRVIDGHS 394
Cdd:cd16159 319 hleeisvggeygggnggiyggKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 395 LVPLLQGAEARSAHEFLFHYCGQHLHAARWHQKDSGSVWKVHYTTPQFHPEGAGaCYGRGVCPCSGEGVTHHRPPLLFDL 474
Cdd:cd16159 399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 530421100 475 SRDPSEARPLTPDSEPlYHAVIARVGAAVSEHRQTLSPVPQQFS 518
Cdd:cd16159 478 SADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
40-485 |
2.76e-130 |
|
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: 385.76 E-value: 2.76e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngYRALQWN 119
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 120 AGSGGLPENETTFARILQQHGYATGLIGKWHQgvncasrGDH-CHHPLNHGFDYFYGMPFtlTNDCDPGRPPEVDAALRa 198
Cdd:cd16026 76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHL-------GHQpEFLPTRHGFDEYFGIPY--SNDMWPFPLYRNDPPGP- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 199 qlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwNCILMRNHDVTEQPMVLEKTASLM 278
Cdd:cd16026 146 --------------------------------------------------------LPPLMENEEVIEQPADQSSLTQRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 279 LKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLI------------------------- 333
Cdd:cd16026 170 TDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVgrildalkelgleentlviftsdng 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 334 -GGKGMGGWEGG--------------IRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDRVIDGHSLVPL 398
Cdd:cd16026 250 pWLEYGGHGGSAgplrggkgttweggVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPL 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 399 LQGAEARSAHEFLFHYCGQHLHAARWHQkdsgsvWKVHYTTpqfhpegagacYGRGVCPCSGEGVTHHRPPLLFDLSRDP 478
Cdd:cd16026 330 LLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPT-----------TYRTGTDPGGLDPTKLEPPLLYDLEEDP 392
|
....*..
gi 530421100 479 SEARPLT 485
Cdd:cd16026 393 GETYNVA 399
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
40-486 |
4.49e-102 |
|
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: 314.75 E-value: 4.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYrALQWn 119
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRV-FLPW- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 120 aGSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYF-YGMPFTLTNDCDPgrppevdaalra 198
Cdd:cd16160 79 -DIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFDFVgTNLPFTNSWACDD------------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 199 qlWGYTQflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfGFVRRWNCILMRNHDVTEQPMVLEKTASLM 278
Cdd:cd16160 146 --TGRHV-------------------------------------------DFPDRSACFLYYNDTIVEQPIQHEHLTETL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 279 LKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGGKGMGGWEGG-------------- 344
Cdd:cd16160 181 VGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGldqntlvfflsdhg 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 345 --------------------------IRVPGIFHWPGVLPaGRVIGEPTSLMDVFPTVVQLVGGEVPQDRVIDGHSLVPL 398
Cdd:cd16160 261 phveycleggstgglkggkgnsweggIRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 399 LQGAEARSAHEFLFHYCgQHLHAARwhqkdSGSvWKVHYTTPQFHPEGAGACYGRGVCP---------CSGEGVTHHRPP 469
Cdd:cd16160 340 LLGEADSPHDDILYYCC-SRLMAVR-----YGS-YKIHFKTQPLPSQESLDPNCDGGGPlsdyivcydCEDECVTKHNPP 412
|
490
....*....|....*..
gi 530421100 470 LLFDLSRDPSEARPLTP 486
Cdd:cd16160 413 LIFDVEKDPGEQYPLQP 429
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
40-521 |
5.84e-74 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293776 [Multi-domain] Cd Length: 466 Bit Score: 242.37 E-value: 5.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRAlqwN 119
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHAR---N 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 120 AGS-----GGLPENETTFARILQQHGYATGLIGKWHQGvncasrgdH--CHHPLNHGFDYFYGMPftltnDCDPGRPPEV 192
Cdd:cd16157 78 AYTpqnivGGIPDSEILLPELLKKAGYRNKIVGKWHLG--------HrpQYHPLKHGFDEWFGAP-----NCHFGPYDNK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 193 DaalRAQLWGYTQFLalgiltlaagqtcgffsvsaravtgMAGvgclffiSWYSSFGFvrrwncilmrNHDVTEQPMvle 272
Cdd:cd16157 145 A---YPNIPVYRDWE-------------------------MIG-------RYYEEFKI----------DKKTGESNL--- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 273 ktASLMLKEAVSYIERH--KHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGGKGMGGWEGGI----- 345
Cdd:cd16157 177 --TQIYLQEALEFIEKQhdAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIenntf 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 346 ------------------------------------RVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDRV 389
Cdd:cd16157 255 vffssdngaalisapeqggsngpflcgkqttfeggmREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 390 IDGHSLVP-LLQGAEARSAHeflFHYCGQHLHAARWHQkdsgsvWKVHYTTpqfhPEGAGACYGRGVCPCSGE---GVT- 464
Cdd:cd16157 335 IDGIDLLPvLLNGKEKDRPI---FYYRGDELMAVRLGQ------YKAHFWT----WSNSWEEFRKGINFCPGQnvpGVTt 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530421100 465 -----HHRPPLLFDLSRDPSEARPLTPDSePLYHAVIARVGAAVSEHRQTLSPVPQQFSMSN 521
Cdd:cd16157 402 hnqtdHTKLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLNVCD 462
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
41-482 |
4.94e-72 |
|
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: 235.90 E-value: 4.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM-DASNGYRALQWN 119
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItDVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 120 A------GSGGLPENETTFARILQQHGYATGLIGKWHQGvncasrGDHCHHPLNHGFDYFYGmpftltnDCDPGRPPevd 193
Cdd:cd16144 81 TklipppSTTRLPLEEVTIAEALKDAGYATAHFGKWHLG------GEGGYGPEDQGFDVNIG-------GTGNGGPP--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 194 aalraqlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiSWYSSFGFvrrwncilmrNHDVTEQPMVLEK 273
Cdd:cd16144 145 -------------------------------------------------SYYFPPGK----------PNPDLEDGPEGEY 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 274 TASLMLKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDN-----------VEEMDW----------- 331
Cdd:cd16144 166 LTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELIEKYEKKKKGLRkgqknpvyaamIESLDEsvgrildalee 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 332 -----------------LIGGKGMGGWEGG------------IRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGG 382
Cdd:cd16144 246 lgladntlviftsdnggLSTRGGPPTSNAPlrggkgslyeggIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 383 EVPQDRVIDGHSLVPLLQGAEARSAHEFLFHycgqHLHAARWHQKDSGSV-----WKVHYttpqFHpegagacygrgvcp 457
Cdd:cd16144 326 PLPPPQHLDGVSLVPLLKGGEADLPRRALFW----HFPHYHGQGGRPASAirkgdWKLIE----FY-------------- 383
|
490 500
....*....|....*....|....*
gi 530421100 458 csgegvtHHRPPLLFDLSRDPSEAR 482
Cdd:cd16144 384 -------EDGRVELYNLKNDIGETN 401
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
40-485 |
6.72e-72 |
|
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: 234.67 E-value: 6.72e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTGDLGCYGN-NTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALqw 118
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 119 nagsGGLPENETTFARILQQHGYATGLIGKWHQGVNCAsrgdhcHHPLNHGFDYFYGMPFTltndcdpgrppevdaalra 198
Cdd:cd16161 79 ----GGLPLNETTLAEVLRQAGYATGMIGKWHLGQREA------YLPNSRGFDYYFGIPFS------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 199 qlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwncilmrnHDVTEQPMVLEKtaslm 278
Cdd:cd16161 130 ---------------------------------------------------------------HDSSLADRYAQF----- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 279 lkeAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFLGKSQH-GLYGDNVEEMDWLIGGKGMGGWEGG----------- 344
Cdd:cd16161 142 ---ATDFIQRASAKdrPFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGlkdntltwfts 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 345 -------------------------------------IRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQD 387
Cdd:cd16161 219 dngpwevkcelavgpgtgdwqgnlggsvakastweggHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 388 RVIDGHSLVPLLQGaEARSAHEFLFHYCGQH-----LHAARWHQkdsgsvWKVHYTTpqfhpEGAGACYGRGvCPcsgeg 462
Cdd:cd16161 299 RIYDGKDLSPVLFG-GSKTGHRCLFHPNSGAagagaLSAVRCGD------YKAHYAT-----GGALACCGST-GP----- 360
|
490 500
....*....|....*....|...
gi 530421100 463 VTHHRPPLLFDLSRDPSEARPLT 485
Cdd:cd16161 361 KLYHDPPLLFDLEVDPAESFPLT 383
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
40-515 |
2.53e-71 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 233.23 E-value: 2.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdASNGYralqwn 119
Cdd:COG3119 23 RPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGV-TDNGE------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 120 AGSGGLPENETTFARILQQHGYATGLIGKWHqgvncasrgdhchhplnhgfdyfygmpftltndcdpgrppevdaalraq 199
Cdd:COG3119 96 GYNGGLPPDEPTLAELLKEAGYRTALFGKWH------------------------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 200 lwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwnciLMRNHDVTEqpmvlektaslml 279
Cdd:COG3119 127 ----------------------------------------------------------LYLTDLLTD------------- 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 280 kEAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFLGK-----------------------SQHGLYGDNVEEMDWLI- 333
Cdd:COG3119 136 -KAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVg 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 334 ------------------------GGKGMGGWEGG--------IRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVG 381
Cdd:COG3119 215 rlldaleelgladntivvftsdngPSLGEHGLRGGkgtlyeggIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAG 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 382 GEVPQDrvIDGHSLVPLLQGAEARSAHEFLFHY-CGQHLHAARWHQkdsgsvWK-VHYTTPQFHPEgagacygrgvcpcs 459
Cdd:COG3119 295 VPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYpRGGGNRAIRTGR------WKlIRYYDDDGPWE-------------- 352
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 530421100 460 gegvthhrpplLFDLSRDPSEARPLTPDseplYHAVIARVGAAVSEHRQTLSPVPQ 515
Cdd:COG3119 353 -----------LYDLKNDPGETNNLAAD----YPEVVAELRALLEAWLKELGDPPL 393
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
40-541 |
4.39e-71 |
|
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: 235.42 E-value: 4.39e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngYRALQWN 119
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGV-----YPGVFYP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 120 AGSGGLPENETTFARILQQHGYATGLIGKWHQGVNcasrGDHCHHPLNHGFDYFYGMPFTltndcdpgrppevdaalraQ 199
Cdd:cd16158 76 GSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVG----LNGTYLPTHQGFDHYLGIPYS-------------------H 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 200 LWGYTQFLalgiltlaagqTCgffsvsaravtgmagvgclfFISWYSSFGFVRRW--NCILMRNHDVTEQPMVLEKTASL 277
Cdd:cd16158 133 DQGPCQNL-----------TC--------------------FPPNIPCFGGCDQGevPCPLFYNESIVQQPVDLLTLEER 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 278 MLKEAVSYIER--HKHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGGKGMGGWEGGI---------- 345
Cdd:cd16158 182 YAKFAKDFIADnaKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIdnntlvffts 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 346 ------------------------------RVPGIFHWPGVLPAGRVIgEPTSLMDVFPTVVQLVGGEVPqDRVIDGHSL 395
Cdd:cd16158 262 dngpstmrksrggnagllkcgkgttyeggvREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLP-NVTLDGVDM 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 396 VPLLQGaEARSAHEFLFHYCGQH-----LHAARWHQkdsgsvWKVH-YTTPQFHPEGAG--ACYGRGVcpcsgegVTHHR 467
Cdd:cd16158 340 SPILFE-QGKSPRQTFFYYPTSPdpdkgVFAVRWGK------YKAHfYTQGAAHSGTTPdkDCHPSAE-------LTSHD 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530421100 468 PPLLFDLSRDPSEARPLtpDSEPLYHAVIARVGAAVSEHRQTLSPVPQQFSMSNilwKPWLQPCC--GHFPF---CSCH 541
Cdd:cd16158 406 PPLLFDLSQDPSENYNL--LGLPEYNQVLKQIQQVKERFEASMKFGESEINKGE---DPALEPCCkpGCTPKpscCQCH 479
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
41-480 |
3.68e-67 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 222.46 E-value: 3.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYG-NNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM--DASNGYRALQ 117
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLkgGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 118 wnagsggLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHH----------------PLNHGFDYFYGMPftlT 181
Cdd:cd16143 81 -------IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIP---A 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 182 NDCDPgrppevdaalraqlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwncilmrn 261
Cdd:cd16143 151 SEVLP--------------------------------------------------------------------------- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 262 hdvteqpmvlektasLMLKEAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLI------ 333
Cdd:cd16143 156 ---------------TLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVgrilda 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 334 --------------------GGKGMGGWEGGI--------------------RVPGIFHWPGVLPAGRVIGEPTSLMDVF 373
Cdd:cd16143 221 lkelglaentlviftsdngpSPYADYKELEKFghdpsgplrgmkadiyegghRVPFIVRWPGKIPAGSVSDQLVSLTDLF 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 374 PTVVQLVGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHycgqhlHAARWH----QKDsgsvWK--VHYTTPQFHPEGA 447
Cdd:cd16143 301 ATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSfairKGD----WKliDGTGSGGFSYPRG 370
|
490 500 510
....*....|....*....|....*....|...
gi 530421100 448 GACYGRGvcpcsgegvthhrPPLLFDLSRDPSE 480
Cdd:cd16143 371 KEKLGLP-------------PGQLYNLSTDPGE 390
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
41-485 |
1.18e-66 |
|
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: 220.48 E-value: 1.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLR---TPNIDQLAEEGVRLTQHLAAaPLCTPSRAAFLTGRHSFRSGMdasngyRALQ 117
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVE-PSCTPGRAAFITGRHPIRTGL------TTVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 118 WNAGSGGLPENETTFARILQQHGYATGLIGKWHQGvncASRGdhcHHPLNHGFDYFYGMPFTltndcdpgrppEVDAALR 197
Cdd:cd16142 74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG---DEDG---RLPTDHGFDEFYGNLYH-----------TIDEEIV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 198 AQlwgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwncilmrnhdvteqpmvlektasl 277
Cdd:cd16142 137 DK------------------------------------------------------------------------------ 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 278 mlkeAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFLGKSQ-HGLYGDNVEEMD------------------------ 330
Cdd:cd16142 139 ----AIDFIKRNAKAdkPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDdhvgqildaldelgiadntivift 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 331 -----WLIGGKGMGGWEGG----------IRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVP------QDRV 389
Cdd:cd16142 215 tdngpEQDVWPDGGYTPFRgekgttweggVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRH 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 390 IDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQkdsgsvWKVHYTtpQFHPEGAGACYGRGVCPCsgegvthhrpP 469
Cdd:cd16142 295 IDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTGEPFYVLTF----------P 356
|
490
....*....|....*.
gi 530421100 470 LLFDLSRDPSEARPLT 485
Cdd:cd16142 357 LIFNLRRDPKERYDVT 372
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
406-540 |
7.07e-63 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 201.77 E-value: 7.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 406 SAHEFLFHYCGQHLHAARWHQkdsgsvWKVHYTTPQFHPEGAGACYGRGVCpcsgegVTHHRPPLLFDLSRDPSEARPLT 485
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 530421100 486 PDSePLYHAVIARVGAAVSEHRQTLSPVPQQFSMSNILWKPWLQPCCGHFPFCSC 540
Cdd:pfam14707 69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
41-482 |
3.77e-61 |
|
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: 207.06 E-value: 3.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngyRALQWNA 120
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 121 GSGGLPENETTFARILQQHGYATGLIGKWHqgvncasRGDHCH--HPLNHGFDYFYGmpFTLTNDCDPGRPPEvdaalra 198
Cdd:cd16145 75 GQDPLPPDDVTLAEVLKKAGYATAAFGKWG-------LGGPGTpgHPTKQGFDYFYG--YLDQVHAHNYYPEY------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 199 qLW--GYTQFLAlgiltlaagQTCGFFSVSARAVTGMAGVgclffiswYSsfgfvrrwncilmrnHDvteqpmvlektas 276
Cdd:cd16145 139 -LWrnGEKVPLP---------NNVIPPLDEGNNAGGGGGT--------YS---------------HD------------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 277 LMLKEAVSYIERHKHGPFLLFLSL----LHVHIPLVTTSAFLGKS----------------------------------- 317
Cdd:cd16145 173 LFTDEALDFIRENKDKPFFLYLAYtlphAPLQVPDDGPYKYKPKDpgiyaylpwpqpekayaamvtrldrdvgrilallk 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 318 QHGLY--------GDNVEEMDWLIGGKGMGGWEGG-------------IRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTV 376
Cdd:cd16145 253 ELGIDentlvvftSDNGPHSEGGSEHDPDFFDSNGplrgykrslyeggIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 377 VQLVGGEVPQDrvIDGHSLVPLLQGAEARSAHEFL---FHYCGQHlHAARWHQkdsgsvWKvhyttpqfhpegagacygr 453
Cdd:cd16145 333 ADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLyweFYEGGGA-QAVRMGG------WK------------------- 384
|
490 500
....*....|....*....|....*....
gi 530421100 454 GVCPCSGEGvthhrPPLLFDLSRDPSEAR 482
Cdd:cd16145 385 AVRHGKKDG-----PFELYDLSTDPGETN 408
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
41-480 |
7.11e-59 |
|
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293765 [Multi-domain] Cd Length: 409 Bit Score: 200.85 E-value: 7.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQ-HlaAAPLCTPSRAAFLTGRHSFRSGMdasngyralqWN 119
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfH--VSPVCAPTRAALLTGRYPFRTGV----------WH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 120 AGSGG--LPENETTFARILQQHGYATGLIGKWHQGVNCAsrgdhcHHPLNHGFDYFYGmpftltndcdpgrppevdaaLR 197
Cdd:cd16146 69 TILGRerMRLDETTLAEVFKDAGYRTGIFGKWHLGDNYP------YRPQDRGFDEVLG--------------------HG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 198 AQLWGYTQFLALGiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvRRWNCILMRNHdvteqpmVLEKT--- 274
Cdd:cd16146 123 GGGIGQYPDYWGN-----------------------------------------DYFDDTYYHNG-------KFVKTegy 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 275 -ASLMLKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAF--------LGKSQHGLYG------DNVEE-MDWLIGGK-- 336
Cdd:cd16146 155 cTDVFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYldpykdmgLDDKLAAFYGmienidDNVGRlLAKLKELGle 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 337 ------------GMGGWEGG----------------IRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDR 388
Cdd:cd16146 235 entivifmsdngPAGGVPKRfnagmrgkkgsvyeggHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGI 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 389 VIDGHSLVPLLQGAEARSAHEFLFhycgqhLHAARW----HQKDSGSVWKVHYttpqfhpegagacygRGVCPcsgegvt 464
Cdd:cd16146 315 KLDGRSLLPLLKGESDPWPERTLF------THSGRWppppKKKRNAAVRTGRW---------------RLVSP------- 366
|
490
....*....|....*.
gi 530421100 465 HHRPPLLFDLSRDPSE 480
Cdd:cd16146 367 KGFQPELYDIENDPGE 382
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
41-394 |
2.40e-54 |
|
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: 183.41 E-value: 2.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngyraLQWNA 120
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGV--------RGNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 121 GSGGLPENETTFARILQQHGYATGLIGKWHQgvncasrgdhchhplnhgfdyfygmpftltndcdpgrppevdaalraql 200
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWHD------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 201 wgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwncilmrnhdvteqpmvlektaslmlk 280
Cdd:cd16022 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 281 EAVSYIERHKHG-PFLLFLSLLHVHIPLvTTSAFL-------GK-----SQHGLY--------GDNVEEM-DWLIGGKGM 338
Cdd:cd16022 104 EAIDFIERRDKDkPFFLYVSFNAPHPPF-AYYAMVsaiddqiGRildalEELGLLdntlivftSDHGDMLgDHGLRGKKG 182
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 530421100 339 GGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHS 394
Cdd:cd16022 183 SLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-414 |
7.95e-53 |
|
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: 183.95 E-value: 7.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTqHLAAAPLCTPSRAAFLTGRHSFRSGmdasngyralqwnA 120
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNY-------------V 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 121 GSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASrGDHCHHplnHGFDYFYgmpftltndcdpgrppevdaalraqL 200
Cdd:cd16151 67 VFGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGD-GDYPHE---FGFDEYC-------------------------L 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 201 WGYTqflalgiltlaagqtcgffsvsaraVTGMAGvgclffiswysSFGFVRRWNCILMRNHDVTEQ---PmvlektaSL 277
Cdd:cd16151 118 WQLT-------------------------ETGEKY-----------SRPATPTFNIRNGKLLETTEGdygP-------DL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 278 MLKEAVSYIERHKHGPFLLFLSLLHVHIPLVTT--------SAFLGKSQHGLYGDNVEEMDWL----------------- 332
Cdd:cd16151 155 FADFLIDFIERNKDQPFFAYYPMVLVHDPFVPTpdspdwdpDDKRKKDDPEYFPDMVAYMDKLvgklvdkleelglrent 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 333 ----------------------IGGKGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDRVI 390
Cdd:cd16151 235 iiiftgdngthrpitsrtngreVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPL 314
|
410 420
....*....|....*....|....
gi 530421100 391 DGHSLVPLLQGAEARSAHEFLFHY 414
Cdd:cd16151 315 DGRSFAPQLLGKTGSPRREWIYWY 338
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-484 |
3.01e-44 |
|
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: 161.58 E-value: 3.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdASNGYRalqwn 119
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGV-FGNDVP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 120 agsggLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHH----PLNHGFDYFYGMpftLTNDcDPGRPP-EVDA 194
Cdd:cd16034 75 -----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY---ECNH-DHNNPHyYDDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 195 ALRAQLWGYTqflalgiltlAAGQTcgffsvsaravtgmagvgclffiswyssfgfvrrwncilmrnhdvteqpmvlekt 274
Cdd:cd16034 146 GKRIYIKGYS----------PDAET------------------------------------------------------- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 275 aslmlKEAVSYIERHKHG--PFLLFLS------------------------LLHVHIPLVTTSAFLGKSQ---------- 318
Cdd:cd16034 161 -----DLAIEYLENQADKdkPFALVLSwnpphdpyttapeeyldmydpkklLLRPNVPEDKKEEAGLREDlrgyyamita 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 319 -----------------------------------HGLYGDNV--EEmdwliggkgmggwegGIRVPGIFHWPGVLPAGR 361
Cdd:cd16034 236 lddnigrlldalkelgllentivvftsdhgdmlgsHGLMNKQVpyEE---------------SIRVPFIIRYPGKIKAGR 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 362 VIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHSLVPLLQGAEARSAHEFLFhYCGQHLHA-ARWHQKDSGSVWKVHYTtp 440
Cdd:cd16034 301 VVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLL-QCFVPFGGgSARDGGEWRGVRTDRYT-- 375
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 530421100 441 qfhpegagacYGRgvcpcsgegvTHHRPPLLFDLSRDPSEARPL 484
Cdd:cd16034 376 ----------YVR----------DKNGPWLLFDNEKDPYQLNNL 399
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
41-484 |
6.00e-42 |
|
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: 155.02 E-value: 6.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLaAAPLCTPSRAAFLTGRHSFRSGMdasngYRALQWNA 120
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYY-VQPICTPSRAALMTGRYPIHTGM-----QHGVILAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 121 GSGGLPENETTFARILQQHGYATGLIGKWHQGvncasrgdHCHH---PLNHGFDYFYGMpftltndcdpgrppevdaaLR 197
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYGY-------------------YG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 198 AQLWGYTQflalgiltlaagQTCGFFSvsaravtgmagvgclffiswyssfgfvrrWNCILMRNHDVTEQPMVLEKTASL 277
Cdd:cd16029 128 GAEDYYTH------------TSGGAND-----------------------------YGNDDLRDNEEPAWDYNGTYSTDL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 278 MLKEAVSYIERH-KHGPFLLFLSLLHVHIPLVTTSAFLGKSQHGLYGDN----------VEEMDWLIGG----------- 335
Cdd:cd16029 167 FTDRAVDIIENHdPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKdedrrtyaamVSALDESVGNvvdalkakgml 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 336 -------------KGMGGWEGG---------------IRVPGIFHWPGVLP-AGRVIGEPTSLMDVFPTVVQLVGGEVPQ 386
Cdd:cd16029 247 dntlivftsdnggPTGGGDGGSnyplrggkntlweggVRVPAFVWSPLLPPkRGTVSDGLMHVTDWLPTLLSLAGGDPDD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 387 DRVIDGHSLVPLLQGAEARSAHEFL----FHYCGQHLHAARWHQkdsgsvWKVHYTTPqfhpegagacygrgvcpcsgeg 462
Cdd:cd16029 327 LPPLDGVDQWDALSGGAPSPRTEILlnidDITRTTGGAAIRVGD------WKLIVGKP---------------------- 378
|
490 500
....*....|....*....|..
gi 530421100 463 vthhrpplLFDLSRDPSEARPL 484
Cdd:cd16029 379 --------LFNIENDPCERNDL 392
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
40-497 |
1.94e-41 |
|
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: 154.61 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGyralqwn 119
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 120 agsGGLPENETTFARILQQHGYATGLIGKWHQGVNcasrgdhcHHPLNHGFDYF--------YGMPFTLTNDCDPGRPPE 191
Cdd:cd16031 75 ---PLFDASQPTYPKLLRKAGYQTAFIGKWHLGSG--------GDLPPPGFDYWvsfpgqgsYYDPEFIENGKRVGQKGY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 192 V-----DAALRaqlwgytqFLAlgilTLAAGQ----TCGFFSVSARAVTGMAGVGC----------LFFISWYSSFG-FV 251
Cdd:cd16031 144 VtdiitDKALD--------FLK----ERDKDKpfclSLSFKAPHRPFTPAPRHRGLyedvtipepeTFDDDDYAGRPeWA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 252 RRWnciLMRNHDVTEQPMVLEKTASLMLK----------EAV----SYIERHKhgpfllflsLLHVHIpLVTTSA---FL 314
Cdd:cd16031 212 REQ---RNRIRGVLDGRFDTPEKYQRYMKdylrtvtgvdDNVgrilDYLEEQG---------LADNTI-IIYTSDngfFL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 315 GksQHGLYGDNV--EEmdwliggkgmggwegGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDG 392
Cdd:cd16031 279 G--EHGLFDKRLmyEE---------------SIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 393 HSLVPLLQGAEARS-AHEFLFHYcgqhlhaaRWHqkdsgsvWKVHYTTPQFhpegagacygrGVcpcsgegVT------- 464
Cdd:cd16031 340 RSLLPLLEGEKPVDwRKEFYYEY--------YEE-------PNFHNVPTHE-----------GV-------RTerykyiy 386
|
490 500 510
....*....|....*....|....*....|....*.
gi 530421100 465 -HHRPPL--LFDLSRDPSEARPLTPDSEplYHAVIA 497
Cdd:cd16031 387 yYGVWDEeeLYDLKKDPLELNNLANDPE--YAEVLK 420
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
41-381 |
4.89e-41 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 149.88 E-value: 4.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGyralqwna 120
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 121 gsGGLPENETTFARILQQHGYATGLIGKWHQGVNCASrgdhchHPLNHGFDYFYGMPFTLTNDCDPGRPPevdaalraql 200
Cdd:pfam00884 73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQ------SPCNLGFDKFFGRNTGSDLYADPPDVP---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 201 wgytqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrWNCILMRNHDVteqpmvlektasLMLK 280
Cdd:pfam00884 135 -----------------------------------------------------YNCSGGGVSDE------------ALLD 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 281 EAVSYIERHkHGPFLLFLSLLHVHIPL------------VTTSAFLGKSQHGLYGDNVEEMDWLI--------------- 333
Cdd:pfam00884 150 EALEFLDNN-DKPFFLVLHTLGSHGPPyypdrypekyatFKPSSCSEEQLLNSYDNTLLYTDDAIgrvldkleenglldn 228
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530421100 334 ---------------------GGKGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVG 381
Cdd:pfam00884 229 tlvvytsdhgeslgegggylhGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
41-418 |
7.39e-40 |
|
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: 148.81 E-value: 7.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTgDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngyralQWNA 120
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---------HGLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 121 GSGG-LPENETTFARILQQHGYATGLIGKWHqgvncasrgdhchhplnHGFDYFYGMPFTLTNDCDPGRPPEVDAALRAq 199
Cdd:cd16027 71 SRGFpLPDGVKTLPELLREAGYYTGLIGKTH-----------------YNPDAVFPFDDEMRGPDDGGRNAWDYASNAA- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 200 lwgytQFLAlgilTLAAGQtcgffsvsaravtgmagvgclffiSWYSSFGFV---RRWncilmrNHDVTEQPMVLEKTAS 276
Cdd:cd16027 133 -----DFLN----RAKKGQ------------------------PFFLWFGFHdphRPY------PPGDGEEPGYDPEKVK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 277 LmlkeavsyierhkhGPFLlflsllhVHIPLVttsaflgKSQHGLYGDNVEEMD-------------------------- 330
Cdd:cd16027 174 V--------------PPYL-------PDTPEV-------REDLADYYDEIERLDqqvgeildeleedglldntiviftsd 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 331 ----------WLiggkgmggWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHSLVPLLQ 400
Cdd:cd16027 226 hgmpfprakgTL--------YDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLK 295
|
410
....*....|....*...
gi 530421100 401 GaEARSAHEFLFHYCGQH 418
Cdd:cd16027 296 G-EKDPGRDYVFAERDRH 312
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
40-484 |
1.52e-37 |
|
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293749 [Multi-domain] Cd Length: 402 Bit Score: 142.97 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTGDLGCYGNNtLRTPNIDQLAEEGVRLTQ-HlaAAPLCTPSRAAFLTGRHSFRSGMdASNGYRALQW 118
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 119 NAGSGGLPENETTFARILQQHGYATGLIGKWHQGVNcasrgdhchhplnhgfDYFYGMPFT------LTNDCDPGRP--- 189
Cdd:cd16025 78 PGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------------DYYSTDDLTdkaieyIDEQKAPDKPffl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 190 -------------PEVDA------------ALRAQLwgYTQFLALGIltLAAGQTcgffsVSARAVTgmagvgclffisw 244
Cdd:cd16025 142 ylafgaphaplqaPKEWIdkykgkydagwdALREER--LERQKELGL--IPADTK-----LTPRPPG------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 245 yssfgfVRRWNcilmrnhDVTEQpmvlEKT--ASLMlkEA----VSYIERH---------KHGPF----LLFLS------ 299
Cdd:cd16025 200 ------VPAWD-------SLSPE----EKKleARRM--EVyaamVEHMDQQigrlidylkELGELdntlIIFLSdngasa 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 300 ---LLHVhiplVTTSAFLGKSQHGLYGdnveemdwliggkgmggweggIRVPGIFHWP-GVLPAGRVIGEPTSLMDVFPT 375
Cdd:cd16025 261 epgWANA----SNTPFRLYKQASHEGG---------------------IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPT 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 376 VVQLVGGEVPQDRV------IDGHSLVPLLQGAEARSAHEFLFHYCGQhlHAARWHQKdsgsvWKVhyttpqfhpegaga 449
Cdd:cd16025 316 ILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRTQYFELFG--NRAIRKGG-----WKA-------------- 374
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 530421100 450 cygrgvcpcsgegVTHHRPPL------LFDLSRDPSEARPL 484
Cdd:cd16025 375 -------------VALHPPPGwgdqweLYDLAKDPSETHDL 402
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-397 |
9.04e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 131.59 E-value: 9.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGR-------HSFRSGMDASNGY 113
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRmpsqhgiHDWIVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 114 RALQWnagsgglPENETTFARILQQHGYATGLIGKWHQGVNCASRgdhchhplnhgFDYFYGM--PFTLT-NDCDPGRPp 190
Cdd:cd16149 81 KPEGY-------LEGQTTLPEVLQDAGYRCGLSGKWHLGDDAADF-----------LRRRAEAekPFFLSvNYTAPHSP- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 191 evdaalraqlWGYtqfLAlgiltlaagqtcgffsvsarAVTGM-AGVGclffiswyssfgfvrrwncilmrnhdvteqpM 269
Cdd:cd16149 142 ----------WGY---FA--------------------AVTGVdRNVG-------------------------------R 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 270 VLEKTASLMLKEAVSYIERHKHGpfllflsllhvhiplvttsafLGKSQHGLYG-----------DNVeemdwliggkgm 338
Cdd:cd16149 158 LLDELEELGLTENTLVIFTSDNG---------------------FNMGHHGIWGkgngtfplnmyDNS------------ 204
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 530421100 339 ggweggIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDRVIDGHSLVP 397
Cdd:cd16149 205 ------VKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-401 |
2.15e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 131.57 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdASNGYRAlqwNA 120
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGV-LNNVENA---GA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 121 GSGGLPENETTFARILQQHGYATGLIGKWHQGVNC--ASRGDHCHHPLNHGFDYFY--------------GMPFTLTNDC 184
Cdd:cd16033 77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEEtpLDYGFDEYLPVETTIEYFLadraiemleelaadDKPFFLRVNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 185 ----DPGRPPEVDAAL----RAQLWG----------YTQFlalgiltlaagQTCGFFSVSAravtgmagvgclffISWYS 246
Cdd:cd16033 157 wgphDPYIPPEPYLDMydpeDIPLPEsfaddfedkpYIYR-----------RERKRWGVDT--------------EDEED 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 247 SFGFVRR-WNCILMRNHDVTeqpMVLEKtaslmLKEavsyierhkHG----PFLLFLSllhVHiplvttSAFLGksQHGL 321
Cdd:cd16033 212 WKEIIAHyWGYITLIDDAIG---RILDA-----LEE---------LGladdTLVIFTS---DH------GDALG--AHRL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 322 YGDNV---EEMdwliggkgmggweggIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHSLVPL 398
Cdd:cd16033 264 WDKGPfmyEET---------------YRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK--VDGRSLLPL 326
|
...
gi 530421100 399 LQG 401
Cdd:cd16033 327 LRG 329
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-397 |
1.61e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 125.74 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLgTGD-LGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRsgmdasngyralqWN 119
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFY-------------HG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 120 AGSGGLPENETTFARILQQHGYATGLIgkwhqgvncasrGDHCHHPLNHGFDYfygmpftltndcdpgrppevdaalraq 199
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFDR--------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 200 lwgytqflalgiltlaagqtcGFFSVsaravtgmagvgclFFISWYSSFGFVRRWNcilmrnhdvteqpmvlekTASLML 279
Cdd:cd16148 108 ---------------------GFDTF--------------EDFRGQEGDPGEEGDE------------------RAERVT 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 280 KEAVSYIERHKHG-PFLLFLSLLHVHIP------LVTTSAFLGK-----SQHGLY-----------GDNVEEMDWLiGGK 336
Cdd:cd16148 135 DRALEWLDRNADDdPFFLFLHYFDPHEPylydaeVRYVDEQIGRlldklKELGLLedtlvivtsdhGEEFGEHGLY-WGH 213
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530421100 337 GMGGWEGGIRVPGIFHWPGVLPAGRvIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHSLVP 397
Cdd:cd16148 214 GSNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SDGRSLLP 271
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-478 |
3.23e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 126.12 E-value: 3.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRsgmdasNGYralqWNa 120
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHE------TGV----WD- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 121 GSGGLPENETTFARILQQHGYATGLIGKWHQGvncaSRGDhchhplNHGFDYfygmpftltnDcdpgrppevdaalraql 200
Cdd:cd16037 70 NADPYDGDVPSWGHALRAAGYETVLIGKLHFR----GEDQ------RHGFRY----------D----------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 201 wgytqflalgiltlaagqtcgffsvsaRAVTgmagvgclffiswyssfgfvrrwncilmrnhdvteqpmvlektaslmlK 280
Cdd:cd16037 113 ---------------------------RDVT------------------------------------------------E 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 281 EAVSYIERHKH--GPFLLFLSLLHVHIPLVTTSAF--------------------------------LGKSQ-------- 318
Cdd:cd16037 118 AAVDWLREEAAddKPWFLFVGFVAPHFPLIAPQEFydlyvrraraayyglvefldenigrvldaleeLGLLDntliiyts 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 319 --------HGLYGDNV--EEmdwliggkgmggwegGIRVPGIFHWPGVlPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDR 388
Cdd:cd16037 198 dhgdmlgeRGLWGKSTmyEE---------------SVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAPPPPDL 261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 389 viDGHSLVPLLQGAE--ARSAheflfhYCGQHLHAA-------RWHQkdsgsvWK-VHYttpqfhpegagacygrgvcpc 458
Cdd:cd16037 262 --DGRSLLPLAEGPDdpDRVV------FSEYHAHGSpsgafmlRKGR------WKyIYY--------------------- 306
|
490 500
....*....|....*....|
gi 530421100 459 sgegvtHHRPPLLFDLSRDP 478
Cdd:cd16037 307 ------VGYPPQLFDLENDP 320
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
40-404 |
2.38e-31 |
|
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: 126.15 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTgDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSG-MDASNGYRALQW 118
Cdd:cd16030 2 KPNVLFIAVDDLRP-WLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGvYDNNSYFRKVAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 119 NAgsgglpeneTTFARILQQHGYATGLIGK-WHQGVNC-----ASRGDHCHHPLNHGFDYFYGMPFTLTNDCDPGRPPE- 191
Cdd:cd16030 81 DA---------VTLPQYFKENGYTTAGVGKiFHPGIPDgdddpASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWe 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 192 --------------VDAALRA--QLWGYTQ--FLALGI----LTLAAGQTcgFF------SVSARAVTGMAGVGclfFIS 243
Cdd:cd16030 152 aadvpdeaypdgkvADEAIEQlrKLKDSDKpfFLAVGFykphLPFVAPKK--YFdlypleSIPLPNPFDPIDLP---EVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 244 WYSsfgfvrrWNCILMRNHDVTEQPMVLEKTASL-MLKEA-------VSYI-----------ERHK------------HG 292
Cdd:cd16030 227 WND-------LDDLPKYGDIPALNPGDPKGPLPDeQARELrqayyasVSYVdaqvgrvldalEELGladntivvlwsdHG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 293 pfllflslLHvhiplvttsafLGksQHGLYG--DNVEEmdwliggkgmggwegGIRVPGIFHWPGVLPAGRVIGEPTSLM 370
Cdd:cd16030 300 --------WH-----------LG--EHGHWGkhTLFEE---------------ATRVPLIIRAPGVTKPGKVTDALVELV 343
|
410 420 430
....*....|....*....|....*....|....
gi 530421100 371 DVFPTVVQLVGgeVPQDRVIDGHSLVPLLQGAEA 404
Cdd:cd16030 344 DIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSA 375
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
41-478 |
1.83e-29 |
|
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: 118.45 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM-DasngyralqwN 119
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAyD----------N 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 120 AGSggLPENETTFARILQQHGYATGLIGKWH-----QgvncasrgdhchhplNHGFDYfygmpftltndcdpgrppEVDA 194
Cdd:cd16032 71 AAE--FPADIPTFAHYLRAAGYRTALSGKMHfvgpdQ---------------LHGFDY------------------DEEV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 195 ALRAQLWGYTqflalgiltlaagqtcgffsvsaravtgmagvgclffiswyssfgfvrrwnciLMRNHDvteqpmvlekt 274
Cdd:cd16032 116 AFKAVQKLYD-----------------------------------------------------LARGED----------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 275 aslmlkeavsyiERhkhgPFLLFLSLLHVHIPLVTTSAFLG----KSQHGLYG-------------DNVEEMD------- 330
Cdd:cd16032 132 ------------GR----PFFLTVSFTHPHDPYVIPQEYWDlyvrRARRAYYGmvsyvddkvgqllDTLERTGladdtiv 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 331 ---------------WLiggkGMGGWEGGIRVPGIFHWPGvLPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDRV-IDGHS 394
Cdd:cd16032 196 iftsdhgdmlgerglWY----KMSFFEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpLDGRS 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 395 LVPLLQGAEARSAHEFLFHYCGQHLHA-ARWHQKDSgsvWKVHYttpqfhpegagacygrgvcpcsgegvTHHRPPLLFD 473
Cdd:cd16032 271 LLPLLEGGDSGGEDEVISEYLAEGAVApCVMIRRGR---WKFIY--------------------------CPGDPDQLFD 321
|
....*
gi 530421100 474 LSRDP 478
Cdd:cd16032 322 LEADP 326
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-498 |
5.37e-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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 115.35 E-value: 5.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQ-HLAAA---PLCTPSRAAFLTGRHSFRSGMDasngyra 115
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNMGGwsgAVCVPSRAMLMTGRTLFHAPEG------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 116 lqwnaGSGGLPENETTFARILQQHGYATGLIGKWHQGV--------NCASRGD----------HCHHPLNhGFDYFYGM- 176
Cdd:cd16155 75 -----GKAAIPSDDKTWPETFKKAGYRTFATGKWHNGFadaaieflEEYKDGDkpffmyvaftAPHDPRQ-APPEYLDMy 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 177 -PFTLT--------NDCDPGRPPEVD----------AALRAQLWGYtqfLALgiltlaagqtcgffsvsaraVTGM-AGV 236
Cdd:cd16155 149 pPETIPlpenflpqHPFDNGEGTVRDeqlapfprtpEAVRQHLAEY---YAM--------------------ITHLdAQI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 237 GclffiswyssfgfvRrwncILmrnhDVTEQPMVLEKTaslmlkeavsYIerhkhgpfllflsllhvhiplVTTS----A 312
Cdd:cd16155 206 G--------------R----IL----DALEASGELDNT----------II---------------------VFTSdhglA 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 313 fLGksQHGLYG-DNVEEmdwliggkgmggweGGIRVPGIFHWPGVlPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDrvID 391
Cdd:cd16155 233 -VG--SHGLMGkQNLYE--------------HSMRVPLIISGPGI-PKGKRRDALVYLQDVFPTLCELAGIEIPES--VE 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 392 GHSLVPLLQGaEARSAHEFLF-HYCGqhlhaarWHQKDSGSVWKVHYTTPqfhpegagacygrgvcpcsgeGVTHhrpPL 470
Cdd:cd16155 293 GKSLLPVIRG-EKKAVRDTLYgAYRD-------GQRAIRDDRWKLIIYVP---------------------GVKR---TQ 340
|
490 500
....*....|....*....|....*...
gi 530421100 471 LFDLSRDPSEARPLtpDSEPLYHAVIAR 498
Cdd:cd16155 341 LFDLKKDPDELNNL--ADEPEYQERLKK 366
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
41-508 |
2.23e-25 |
|
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: 108.89 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFrsgmdasnGYRALqWNA 120
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLM--------NHRSV-WNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 121 GSggLPENETTFARILQQHGYATGLIGKWHQGVNcaSRGDHCHHPLNH-------GFDYFYGMPFTLTNDCDP------- 186
Cdd:cd16028 72 TP--LDARHLTLALELRKAGYDPALFGYTDTSPD--PRGLAPLDPRLLsyelampGFDPVDRLDEYPAEDSDTafltdra 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 187 -----GR---------------PPEVDAALRAQLWGYTQFLALgiltlaagqtcgffsvsARAVTGMAGVGCLFFISWY- 245
Cdd:cd16028 148 ieyldERqdepwflhlsyirphPPFVAPAPYHALYDPADVPPP-----------------IRAESLAAEAAQHPLLAAFl 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 246 -----SSFgFVRRWNCILMRNHDVTEqpmvLEKTASLMLKEA-------VSYIERHKHGPFLLflsllhvhipLVTTsaf 313
Cdd:cd16028 211 eriesLSF-SPGAANAADLDDEEVAQ----MRATYLGLIAEVddhlgrlFDYLKETGQWDDTL----------IVFT--- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 314 lgkSQHGLY-GDNveemdWLIGGKGMGGWEGgiRVPGIFHWPGVL---PAGRVIGEPTSLMDVFPTVVQLVGGEVPQDrv 389
Cdd:cd16028 273 ---SDHGEQlGDH-----WLWGKDGFFDQAY--RVPLIVRDPRREadaTRGQVVDAFTESVDVMPTILDWLGGEIPHQ-- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 390 IDGHSLVPLLQGAEA---RSAHEFLFHYcgqHLHAARWHQKDSGsvwkvhyttpqFHPEGAGACYGRGvcpcsgegvTHH 466
Cdd:cd16028 341 CDGRSLLPLLAGAQPsdwRDAVHYEYDF---RDVSTRRPQEALG-----------LSPDECSLAVIRD---------ERW 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 530421100 467 R-------PPLLFDLSRDPSEARPLTPDsePLYHAVIARVGAAVSEHRQ 508
Cdd:cd16028 398 KyvhfaalPPLLFDLKNDPGELRDLAAD--PAYAAVVLRYAQKLLSWRM 444
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-150 |
2.49e-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: 293771 [Multi-domain] Cd Length: 373 Bit Score: 107.70 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngYRalqwN 119
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR----N 71
|
90 100 110
....*....|....*....|....*....|.
gi 530421100 120 AGSggLPENETTFARILQQHGYATGLIGKWH 150
Cdd:cd16152 72 GIP--LPADEKTLAHYFRDAGYETGYVGKWH 100
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
40-489 |
9.78e-24 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 104.37 E-value: 9.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLgTGD-LGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasNGYralqw 118
Cdd:PRK13759 6 KPNIILIMVDQM-RGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGR---VGY----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 119 naGSGGLPENETTFARILQQHGYATGLIGKWHqgvncasrgdhcHHPLN--HGFDYfygmpfTLTNDCDPGRPPEVDAAL 196
Cdd:PRK13759 77 --GDVVPWNYKNTLPQEFRDAGYYTQCIGKMH------------VFPQRnlLGFHN------VLLHDGYLHSGRNEDKSQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 197 RAQLWGYTQFLALGILTLAAGQTcgffsvsaravtgmaGVGclffiswyssfgfvrrWNC--ILMRNHDVTEQpmvLEKT 274
Cdd:PRK13759 137 FDFVSDYLAWLREKAPGKDPDLT---------------DIG----------------WDCnsWVARPWDLEER---LHPT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 275 AsLMLKEAVSYIERHKHG-PFLLFLSLLHVHIPLVTTSAFL-------------------------GKSQHGLYGD---- 324
Cdd:PRK13759 183 N-WVGSESIEFLRRRDPTkPFFLKMSFARPHSPYDPPKRYFdmykdadipdphigdweyaedqdpeGGSIDALRGNlgee 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 325 -----------NVEEMDWLIGGKGMGGWEG--------------------------------GIRVPGIFHWPG---VLP 358
Cdd:PRK13759 262 yarraraayygLITHIDHQIGRFLQALKEFglldntiilfvsdhgdmlgdhylfrkgypyegSAHIPFIIYDPGgllAGN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 359 AGRVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHSLVPLLQGAEARSAHEFlfhycgqHLHAARWHQKDsgsvwkvHYT 438
Cdd:PRK13759 342 RGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYEGWRPYL-------HGEHALGYSSD-------NYL 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 530421100 439 TPQFHPegagacYGRGvcpcSGEGVTHhrpplLFDLSRDPSEARPLTPDSE 489
Cdd:PRK13759 406 TDGKWK------YIWF----SQTGEEQ-----LFDLKKDPHELHNLSPSEK 441
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-175 |
1.22e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 102.81 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTL--RTPNIDQLAEEGVRLTqHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRAlqw 118
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGVLAVPDELL--- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 530421100 119 nagsggLPENETTFARILQQ--HGYATGLIGKWHQGvncasrGDHCHHPLNHGFDYFYG 175
Cdd:cd16154 77 ------LSEETLLQLLIKDAttAGYSSAVIGKWHLG------GNDNSPNNPGGIPYYAG 123
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-150 |
1.64e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 100.53 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLGTGDLGCYGN----------NTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDA 109
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 530421100 110 SNGYralqWNAGSGGLPenetTFARILQQHGYATGLIGKWH 150
Cdd:cd16153 81 FEAA----HPALDHGLP----TFPEVLKKAGYQTASFGKSH 113
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
41-150 |
2.33e-21 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293775 [Multi-domain] Cd Length: 468 Bit Score: 97.07 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMdasngyralqWnA 120
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------W-T 69
|
90 100 110
....*....|....*....|....*....|
gi 530421100 121 GSGGLPENETTFARILQQHGYATGLIGKWH 150
Cdd:cd16156 70 NCMALGDNVKTIGQRLSDNGIHTAYIGKWH 99
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-162 |
5.48e-21 |
|
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: 95.38 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGR--HsfrsgmdaSNGYRALqw 118
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWypH--------VNGHRTL-- 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530421100 119 nagSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHC 162
Cdd:cd16150 71 ---HHLLRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYC 111
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
40-176 |
1.84e-19 |
|
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: 90.69 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 40 KPNILLIMADDLgtgDLGCYGNNTLRtPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM----DASNGYRA 115
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVtnnsPPGGGYPK 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530421100 116 lQWNAGsgglpENETTFARILQQHGYATGLIGKWHQGVNcaSRGDHCHHPLnhGFDYFYGM 176
Cdd:cd16147 77 -FWQNG-----LERSTLPVWLQEAGYRTAYAGKYLNGYG--VPGGVSYVPP--GWDEWDGL 127
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
41-147 |
1.66e-16 |
|
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: 79.00 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRL-TQHLAAAPLCTPSRAAFLTGRHSFRSGMdASNGYRALQWN 119
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGY-TGNGSADPELP 79
|
90 100
....*....|....*....|....*...
gi 530421100 120 AGSGGLPENETTFARILQQHGYATGLIG 147
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG 107
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-150 |
1.82e-13 |
|
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: 71.47 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMAD------DLGTGDLGcygnntLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDaSNGYR 114
Cdd:cd16035 1 PNILLILTDqeryppPWPAGWAA------LNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT-DTLGS 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 530421100 115 ALQWNAgSGGLPenetTFARILQQHGYATGLIGKWH 150
Cdd:cd16035 74 PMQPLL-SPDVP----TLGHMLRAAGYYTAYKGKWH 104
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
41-479 |
1.65e-11 |
|
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: 66.03 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSfrsgmdasngYRALQWNa 120
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFT----------HLTESWN- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 121 GSGGLPENETTFARILQQHGYATGLIGK--WHQGvncasrgdhcHHPLNHGFD-YFYGMPFTLTNDcdpGRPPEVDAALR 197
Cdd:cd16171 70 NYKGLDPNYPTWMDRLEKHGYHTQKYGKldYTSG----------HHSVSNRVEaWTRDVPFLLRQE---GRPTVNLVGDR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 198 AQL------WGYTQFLALGILTLAAGQTCGFF-----SVSARAVTGMAGvgclffiswySSFGFVRRwncilMRNHdvtE 266
Cdd:cd16171 137 STVrvmlkdWQNTDKAVHWIRKEAPNLTQPFAlylglNLPHPYPSPSMG----------ENFGSIRN-----IRAF---Y 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 267 QPMVLEKTAslMLKEAVSYIerHKHG----PFLLFLS----LLHVHIPLVTTSAFLGKSQhglygdnveemdwliggkgm 338
Cdd:cd16171 199 YAMCAETDA--MLGEIISAL--KDTGlldkTYVFFTSdhgeLAMEHRQFYKMSMYEGSSH-------------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 339 ggweggirVPGIFHWPGVlPAGRVIGEPTSLMDVFPTVVQLVGGEVPQDrvIDGHSLVPLLQGAEARSAHEFLFH----- 413
Cdd:cd16171 255 --------VPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLLSESSIKESPSRVPHpdwvl 323
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530421100 414 --YCGQHLHAARWHQKDSGsvWKvhYTTpqfhpegagacYGRGVcpcsgegvthHRPPLLFDLSRDPS 479
Cdd:cd16171 324 seFHGCNVNASTYMLRTNS--WK--YIA-----------YADGN----------SVPPQLFDLSKDPD 366
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
33-176 |
1.82e-04 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 44.26 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 33 PKTANAFKPNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAaaplctpsraaflTGRHSFRS------G 106
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYS-------------QGGRTSRGefavltG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 107 MDASNGYRALQwnagsggLPENET--TFARILQQHGYATgligkwhqgvncasrgdHCHHP------------LNHGFDY 172
Cdd:COG1368 294 LPPLPGGSPYK-------RPGQNNfpSLPSILKKQGYET-----------------SFFHGgdgsfwnrdsfyKNLGFDE 349
|
....
gi 530421100 173 FYGM 176
Cdd:COG1368 350 FYDR 353
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
41-176 |
1.14e-03 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 41.13 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421100 41 PNILLIMADDLGTGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRA--AFLTGRHSFRSGMDASNGYRalqw 118
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK---- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530421100 119 nagsgglPENETTFARILQQHGYATGLIgkwhqgvncasrgdHCHHP---------LNHGFDYFYGM 176
Cdd:cd16015 77 -------LNPLPSLPSILKEQGYETIFI--------------HGGDAsfynrdsvyPNLGFDEFYDL 122
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
345-378 |
5.05e-03 |
|
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: 39.50 E-value: 5.05e-03
10 20 30
....*....|....*....|....*....|....
gi 530421100 345 IRVPGIFHWPGVLPagRVIGEPTSLMDVFPTVVQ 378
Cdd:COG3083 487 LQVPLVIHWPGTPP--QVISKLTSHLDIVPTLMQ 518
|
|
| |
