|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
40-563 |
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: 797.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMEASNGYRALQWN 119
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 120 AGSGGLPENETTFARILQQRGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYFYGMPFTLTNDCDPGRPPEVDAALRAQ 199
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 200 LWGYTQFLALGILTVAAGKTCGFISvsGRVVTGMACVLFLFFISWYSSFGFVRRWNCVLMRNHDVTEQPMVLEKTASLML 279
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLYLGAVS--KRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 280 KEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFVGKSQHGLYGDNVEEMDWLIGKILNAIEDNGLKNSTFTYFTSDHGG 359
Cdd:cd16159 239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 360 HLEARDGHSQLGGWNGIYKGGKGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGHS 439
Cdd:cd16159 319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 440 LVPLLQGAEARSAHEFLFHYCGQHLHAARWHQRDSGSVWKVHYTTPQFHPEGAGaCYGRGVCPCSGEGVTHHRPPLLFDL 519
Cdd:cd16159 399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2309511958 520 SRDPSEARPLTPDSEPlYHAVIARVGAAVSEHRHTLSPVPQQFS 563
Cdd:cd16159 478 SADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
40-530 |
1.08e-150 |
|
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: 439.69 E-value: 1.08e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMeasngYRALQWN 119
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 120 AGSGGLPENETTFARILQQRGYATGLIGKWHQGvncasrgDH-CHHPLNHGFDYFYGMPFTltNDCDPGRPPEVDAALRa 198
Cdd:cd16026 76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLG-------HQpEFLPTRHGFDEYFGIPYS--NDMWPFPLYRNDPPGP- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 199 qlwgytqflalgiltvaagktcgfisvsgrvvtgmacvlflffiswyssfgfvrrwNCVLMRNHDVTEQPMVLEKTASLM 278
Cdd:cd16026 146 --------------------------------------------------------LPPLMENEEVIEQPADQSSLTQRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 279 LKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFVGKSQHGLYGDNVEEMDWLIGKILNAIEDNGLKNSTFTYFTSDHG 358
Cdd:cd16026 170 TDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 359 GHLEARDGH-SQL-----------GGwngiykggkgmggweggIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLAG 426
Cdd:cd16026 250 PWLEYGGHGgSAGplrggkgttweGG-----------------VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 427 GEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQrdsgsvWKVHYTTpqfhpegagacYGRGVCPCSGE 506
Cdd:cd16026 313 APLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPT-----------TYRTGTDPGGL 375
|
490 500
....*....|....*....|....
gi 2309511958 507 GVTHHRPPLLFDLSRDPSEARPLT 530
Cdd:cd16026 376 DPTKLEPPLLYDLEEDPGETYNVA 399
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
40-531 |
5.56e-121 |
|
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: 365.21 E-value: 5.56e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMEASNGYrALQWn 119
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRV-FLPW- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 120 aGSGGLPENETTFARILQQRGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYF-YGMPFTLTNDCDPgrppevdaalra 198
Cdd:cd16160 79 -DIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFDFVgTNLPFTNSWACDD------------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 199 qlWGYTQflalgiltvaagktcgfisvsgrvvtgmacvlflffiswyssfGFVRRWNCVLMRNHDVTEQPMVLEKTASLM 278
Cdd:cd16160 146 --TGRHV-------------------------------------------DFPDRSACFLYYNDTIVEQPIQHEHLTETL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 279 LKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFVGKSQHGLYGDNVEEMDWLIGKILNAIEDNGLKNSTFTYFTSDHG 358
Cdd:cd16160 181 VGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 359 GHLEardgHSQLGGwNGIYKGGKGMGGWEGGIRVPGIFHWPGVLPaGRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIDGH 438
Cdd:cd16160 261 PHVE----YCLEGG-STGGLKGGKGNSWEGGIRVPFIAYWPGTIK-PRVSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 439 SLVPLLQGAEARSAHEFLFHYCgQHLHAARwhqrdSGSvWKVHYTTPQFHPEGAGACYGRGVCP---------CSGEGVT 509
Cdd:cd16160 335 SITDLLLGEADSPHDDILYYCC-SRLMAVR-----YGS-YKIHFKTQPLPSQESLDPNCDGGGPlsdyivcydCEDECVT 407
|
490 500
....*....|....*....|..
gi 2309511958 510 HHRPPLLFDLSRDPSEARPLTP 531
Cdd:cd16160 408 KHNPPLIFDVEKDPGEQYPLQP 429
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
41-527 |
9.52e-91 |
|
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: 286.36 E-value: 9.52e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMEA-------SNGY 113
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDvipgrrgPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 114 RALQWNAGSGGLPENETTFARILQQRGYATGLIGKWHQGvncasrGDHCHHPLNHGFDYFYGmpftltnDCDPGRPPevd 193
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLG------GEGGYGPEDQGFDVNIG-------GTGNGGPP--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 194 aalraqlwgytqflalgiltvaagktcgfisvsgrvvtgmacvlflffiSWYSSFGFvrrwncvlmrNHDVTEQPMVLEK 273
Cdd:cd16144 145 -------------------------------------------------SYYFPPGK----------PNPDLEDGPEGEY 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 274 TASLMLKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFVGKSQHGLYGDN-----------VEEMDWLIGKILNAIED 342
Cdd:cd16144 166 LTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELIEKYEKKKKGLRkgqknpvyaamIESLDESVGRILDALEE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 343 NGLKNSTFTYFTSDHGGHLEARDGHSQL------------GGwngiykggkgmggweggIRVPGIFHWPGVLPAGRVIGE 410
Cdd:cd16144 246 LGLADNTLVIFTSDNGGLSTRGGPPTSNaplrggkgslyeGG-----------------IRVPLIVRWPGVIKPGSVSDV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 411 PTSLMDVFPTVVQLAGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHycgqHLHAARWHQRDSGSV-----WKVHYttp 485
Cdd:cd16144 309 PVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFW----HFPHYHGQGGRPASAirkgdWKLIE--- 381
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2309511958 486 qFHpegagacygrgvcpcsgegvtHHRPPLLFDLSRDPSEAR 527
Cdd:cd16144 382 -FY---------------------EDGRVELYNLKNDIGETN 401
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
40-530 |
8.51e-90 |
|
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.
Pssm-ID: 293780 [Multi-domain] Cd Length: 383 Bit Score: 282.82 E-value: 8.51e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGIGDLGCYGN-NTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMEASNGYRALqw 118
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 119 nagsGGLPENETTFARILQQRGYATGLIGKWHQGVNCAsrgdhcHHPLNHGFDYFYGMPFTltndcdpgrppevdaalra 198
Cdd:cd16161 79 ----GGLPLNETTLAEVLRQAGYATGMIGKWHLGQREA------YLPNSRGFDYYFGIPFS------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 199 qlwgytqflalgiltvaagktcgfisvsgrvvtgmacvlflffiswyssfgfvrrwncvlmrnHDVTEQPMVLEKtaslm 278
Cdd:cd16161 130 ---------------------------------------------------------------HDSSLADRYAQF----- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 279 lkeAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFVGKSQH-GLYGDNVEEMDWLIGKILNAIEDNGLKNSTFTYFTS 355
Cdd:cd16161 142 ---ATDFIQRASAKdrPFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTS 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 356 DHGGHLEARDGHSQLGGWNGIYKGGKGMGGWEG---GIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQD 432
Cdd:cd16161 219 DNGPWEVKCELAVGPGTGDWQGNLGGSVAKASTwegGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 433 RVIDGHSLVPLLQGaEARSAHEFLFHYCGQH-----LHAARWHQrdsgsvWKVHYTTpqfhpEGAGACYGRGvCPcsgeg 507
Cdd:cd16161 299 RIYDGKDLSPVLFG-GSKTGHRCLFHPNSGAagagaLSAVRCGD------YKAHYAT-----GGALACCGST-GP----- 360
|
490 500
....*....|....*....|...
gi 2309511958 508 VTHHRPPLLFDLSRDPSEARPLT 530
Cdd:cd16161 361 KLYHDPPLLFDLEVDPAESFPLT 383
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
40-560 |
1.03e-89 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 282.54 E-value: 1.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMeASNGYralqwn 119
Cdd:COG3119 23 RPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGV-TDNGE------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 120 AGSGGLPENETTFARILQQRGYATGLIGKWHqgvncasrgdhchhplnhgfdyfygmpftltndcdpgrppevdaalraq 199
Cdd:COG3119 96 GYNGGLPPDEPTLAELLKEAGYRTALFGKWH------------------------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 200 lwgytqflalgiltvaagktcgfisvsgrvvtgmacvlflffiswyssfgfvrrwncvLMRNHDVTEqpmvlektaslml 279
Cdd:COG3119 127 ----------------------------------------------------------LYLTDLLTD------------- 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 280 kEAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFVGK-----------------------SQHGLYGDNVEEMDWLIG 334
Cdd:COG3119 136 -KAIDFLERQADKdkPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVG 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 335 KILNAIEDNGLKNSTFTYFTSDHGGHLEA---RDGHSQL--GGwngiykggkgmggweggIRVPGIFHWPGVLPAGRVIG 409
Cdd:COG3119 215 RLLDALEELGLADNTIVVFTSDNGPSLGEhglRGGKGTLyeGG-----------------IRVPLIVRWPGKIKAGSVSD 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 410 EPTSLMDVFPTVVQLAGGEVPQDrvIDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQRdsgsvWK-VHYTTPQFH 488
Cdd:COG3119 278 ALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTGR-----WKlIRYYDDDGP 350
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2309511958 489 PEgagacygrgvcpcsgegvthhrpplLFDLSRDPSEARPLTPDseplYHAVIARVGAAVSEHRHTLSPVPQ 560
Cdd:COG3119 351 WE-------------------------LYDLKNDPGETNNLAAD----YPEVVAELRALLEAWLKELGDPPL 393
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
40-562 |
2.35e-88 |
|
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: 281.66 E-value: 2.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMEASNGYRAlqwN 119
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHAR---N 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 120 AGS-----GGLPENETTFARILQQRGYATGLIGKWHQGvncasrgdH--CHHPLNHGFDYFYGMPftltnDCDPGRPPEV 192
Cdd:cd16157 78 AYTpqnivGGIPDSEILLPELLKKAGYRNKIVGKWHLG--------HrpQYHPLKHGFDEWFGAP-----NCHFGPYDNK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 193 DaalRAQLWGYTQFLALGiltvaagktcgfisvsgrvvtgmacvlflffiSWYSSFGFvrrwncvlmrNHDVTEQPMVle 272
Cdd:cd16157 145 A---YPNIPVYRDWEMIG--------------------------------RYYEEFKI----------DKKTGESNLT-- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 273 ktaSLMLKEAVSYIERH--KHGPFLLFLSLLHVHIPLVTTSAFVGKSQHGLYGDNVEEMDWLIGKILNAIEDNGLKNSTF 350
Cdd:cd16157 178 ---QIYLQEALEFIEKQhdAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTF 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 351 TYFTSDHGGhleARDGHSQLGGWNgIYKGGKGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVP 430
Cdd:cd16157 255 VFFSSDNGA---ALISAPEQGGSN-GPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIP 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 431 QDRVIDGHSLVP-LLQGAEARSAHeflFHYCGQHLHAARWHQrdsgsvWKVHYTTpqfhPEGAGACYGRGVCPCSGE--- 506
Cdd:cd16157 331 SDRAIDGIDLLPvLLNGKEKDRPI---FYYRGDELMAVRLGQ------YKAHFWT----WSNSWEEFRKGINFCPGQnvp 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2309511958 507 GVT------HHRPPLLFDLSRDPSEARPLTPDSePLYHAVIARVGAAVSEHRHTLSPVPQQF 562
Cdd:cd16157 398 GVTthnqtdHTKLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQL 458
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
41-586 |
4.78e-88 |
|
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: 281.26 E-value: 4.78e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMeasngYRALQWNA 120
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGV-----YPGVFYPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 121 GSGGLPENETTFARILQQRGYATGLIGKWHQGVNcasrGDHCHHPLNHGFDYFYGMPFTltNDCDPgrppevdaalraql 200
Cdd:cd16158 77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVG----LNGTYLPTHQGFDHYLGIPYS--HDQGP-------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 201 wgytqflalgiltvaagktcgfisvsgrvvtgmaCVLFLFFISWYSSFGFVRRW--NCVLMRNHDVTEQPMVLEKTASLM 278
Cdd:cd16158 137 ----------------------------------CQNLTCFPPNIPCFGGCDQGevPCPLFYNESIVQQPVDLLTLEERY 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 279 LKEAVSYIER--HKHGPFLLFLSLLHVHIPLVTTSAFVGKSQHGLYGDNVEEMDWLIGKILNAIEDNGLKNSTFTYFTSD 356
Cdd:cd16158 183 AKFAKDFIADnaKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 357 HGGHL--EARDGHSQL----------GGwngiykggkgmggweggIRVPGIFHWPGVLPAGRVIgEPTSLMDVFPTVVQL 424
Cdd:cd16158 263 NGPSTmrKSRGGNAGLlkcgkgttyeGG-----------------VREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 425 AGGEVPqDRVIDGHSLVPLLQGaEARSAHEFLFHYCGQH-----LHAARWHQrdsgsvWKVH-YTTPQFHPEGAG--ACY 496
Cdd:cd16158 325 AGAPLP-NVTLDGVDMSPILFE-QGKSPRQTFFYYPTSPdpdkgVFAVRWGK------YKAHfYTQGAAHSGTTPdkDCH 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 497 GRGVcpcsgegVTHHRPPLLFDLSRDPSEARPLtpDSEPLYHAVIARVGAAVSEHRHTLSPVPQQFSTSNilwKPWLQPC 576
Cdd:cd16158 397 PSAE-------LTSHDPPLLFDLSQDPSENYNL--LGLPEYNQVLKQIQQVKERFEASMKFGESEINKGE---DPALEPC 464
|
570
....*....|....*
gi 2309511958 577 C--GHFPF---CSCH 586
Cdd:cd16158 465 CkpGCTPKpscCQCH 479
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
41-525 |
5.15e-84 |
|
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: 267.91 E-value: 5.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYG-NNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM--EASNGYRALQ 117
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLkgGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 118 wnagsggLPENETTFARILQQRGYATGLIGKWHQGVNCASRGDHCHH----------------PLNHGFDYFYGMPftlT 181
Cdd:cd16143 81 -------IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIP---A 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 182 NDCDPgrppevdaalraqlwgytqflalgiltvaagktcgfisvsgrvvtgmacvlflffiswyssfgfvrrwncvlmrn 261
Cdd:cd16143 151 SEVLP--------------------------------------------------------------------------- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 262 hdvteqpmvlektasLMLKEAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFVGKSQHGLYGDNVEEMDWLIGKILNA 339
Cdd:cd16143 156 ---------------TLTDKAVEFIDQHAKKdkPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDA 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 340 IEDNGLKNSTFTYFTSDHGGHLEARD------GHSQLGGWNGIYKGgkgmggweggI-----RVPGIFHWPGVLPAGRVI 408
Cdd:cd16143 221 LKELGLAENTLVIFTSDNGPSPYADYkelekfGHDPSGPLRGMKAD----------IyegghRVPFIVRWPGKIPAGSVS 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 409 GEPTSLMDVFPTVVQLAGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHycgqhlHAARWHQ--RDSGsvWK--VHYTT 484
Cdd:cd16143 291 DQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSFaiRKGD--WKliDGTGS 362
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2309511958 485 PQFHPEGAGACYGRGvcpcsgegvthhrPPLLFDLSRDPSE 525
Cdd:cd16143 363 GGFSYPRGKEKLGLP-------------PGQLYNLSTDPGE 390
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
41-530 |
4.81e-81 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 259.39 E-value: 4.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLR---TPNIDQLAEEGVRLTQHLAAaPLCTPSRAAFLTGRHSFRSGMeasngyRALQ 117
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVE-PSCTPGRAAFITGRHPIRTGL------TTVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 118 WNAGSGGLPENETTFARILQQRGYATGLIGKWHQGvncASRGdhcHHPLNHGFDYFYGMPFTltndcdpgrppEVDAALR 197
Cdd:cd16142 74 LPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLG---DEDG---RLPTDHGFDEFYGNLYH-----------TIDEEIV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 198 AQlwgytqflalgiltvaagktcgfisvsgrvvtgmacvlflffiswyssfgfvrrwncvlmrnhdvteqpmvlektasl 277
Cdd:cd16142 137 DK------------------------------------------------------------------------------ 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 278 mlkeAVSYIERHKHG--PFLLFLSLLHVHIPLVTTSAFVGKSQ-HGLYGDNVEEMDWLIGKILNAIEDNGLKNSTFTYFT 354
Cdd:cd16142 139 ----AIDFIKRNAKAdkPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFT 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 355 SDHGGHLEARDGHSQL-----------GGWngiykggkgmggweggiRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQ 423
Cdd:cd16142 215 TDNGPEQDVWPDGGYTpfrgekgttweGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAA 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 424 LAGGEVP------QDRVIDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQrdsgsvWKVHYTtpQFHPEGAGACYG 497
Cdd:cd16142 278 LAGAPDPkdkllgKDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTGEP 349
|
490 500 510
....*....|....*....|....*....|...
gi 2309511958 498 RGVCPCsgegvthhrpPLLFDLSRDPSEARPLT 530
Cdd:cd16142 350 FYVLTF----------PLIFNLRRDPKERYDVT 372
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
41-527 |
3.76e-79 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 255.98 E-value: 3.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMEASNGYRalqwna 120
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 121 GSGGLPENETTFARILQQRGYATGLIGKWHqgvncasRGDHCH--HPLNHGFDYFYGmpFTLTNDCDPGRPPEvdaalra 198
Cdd:cd16145 75 GQDPLPPDDVTLAEVLKKAGYATAAFGKWG-------LGGPGTpgHPTKQGFDYFYG--YLDQVHAHNYYPEY------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 199 qLW-GYTQFLALGilTVAAGKTCGFISVSGRVVtgmacvlflffiswYSsfgfvrrwncvlmrnHDvteqpmvlektasL 277
Cdd:cd16145 139 -LWrNGEKVPLPN--NVIPPLDEGNNAGGGGGT--------------YS---------------HD-------------L 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 278 MLKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTS---AFVGKSQHGLYGDN------------VEEMDWLIGKILNAIED 342
Cdd:cd16145 174 FTDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDdgpYKYKPKDPGIYAYLpwpqpekayaamVTRLDRDVGRILALLKE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 343 NGLKNSTFTYFTSDHGGHLEARDGHSQL-----------------GGwngiykggkgmggweggIRVPGIFHWPGVLPAG 405
Cdd:cd16145 254 LGIDENTLVVFTSDNGPHSEGGSEHDPDffdsngplrgykrslyeGG-----------------IRVPFIARWPGKIPAG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 406 RVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGHSLVPLLQGAEARSAHEFL---FHYCGQHlHAARWHQrdsgsvWKvhy 482
Cdd:cd16145 317 SVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLyweFYEGGGA-QAVRMGG------WK--- 384
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2309511958 483 ttpqfhpegagacygrGVCPCSGEGvthhrPPLLFDLSRDPSEAR 527
Cdd:cd16145 385 ----------------AVRHGKKDG-----PFELYDLSTDPGETN 408
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
41-439 |
4.54e-72 |
|
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: 231.17 E-value: 4.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMeasngyraLQWNA 120
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGV--------RGNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 121 GSGGLPENETTFARILQQRGYATGLIGKWHQgvncasrgdhchhplnhgfdyfygmpftltndcdpgrppevdaalraql 200
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWHD------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 201 wgytqflalgiltvaagktcgfisvsgrvvtgmacvlflffiswyssfgfvrrwncvlmrnhdvteqpmvlektaslmlk 280
Cdd:cd16022 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 281 EAVSYIERHKHG-PFLLFLSLLHVHIPLVttsafvgksqhglYGDNVEEMDWLIGKILNAIEDNGLKNSTFTYFTSDHGG 359
Cdd:cd16022 104 EAIDFIERRDKDkPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 360 HLEarDGHSQLGGWNgiykggkgmgGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGHS 439
Cdd:cd16022 171 MLG--DHGLRGKKGS----------LYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
41-525 |
1.94e-71 |
|
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: 235.52 E-value: 1.94e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQ-HlaAAPLCTPSRAAFLTGRHSFRSGMeasngyralqWN 119
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfH--VSPVCAPTRAALLTGRYPFRTGV----------WH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 120 AGSGG--LPENETTFARILQQRGYATGLIGKWHQGVNCAsrgdhcHHPLNHGFDYFYGmpftltndcdpgrppevdaaLR 197
Cdd:cd16146 69 TILGRerMRLDETTLAEVFKDAGYRTGIFGKWHLGDNYP------YRPQDRGFDEVLG--------------------HG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 198 AQLWGYTQFLALGiltvaagktcgfisvsgrvvtgmacvlflffiswyssfgfvRRWNCVLMRNHdvteqpmVLEKT--- 274
Cdd:cd16146 123 GGGIGQYPDYWGN-----------------------------------------DYFDDTYYHNG-------KFVKTegy 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 275 -ASLMLKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAF--------VGKSQHGLYGdNVEEMDWLIGKILNAIEDNGL 345
Cdd:cd16146 155 cTDVFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYldpykdmgLDDKLAAFYG-MIENIDDNVGRLLAKLKELGL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 346 KNSTFTYFTSDHG----------GHLEARDGHSQLGGwngiykggkgmggweggIRVPGIFHWPGVLPAGRVIGEPTSLM 415
Cdd:cd16146 234 EENTIVIFMSDNGpaggvpkrfnAGMRGKKGSVYEGG-----------------HRVPFFIRWPGKILAGKDVDTLTAHI 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 416 DVFPTVVQLAGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLFhycgqhLHAARW----HQRDSGSVWKVHYttpqfhpeg 491
Cdd:cd16146 297 DLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLF------THSGRWppppKKKRNAAVRTGRW--------- 361
|
490 500 510
....*....|....*....|....*....|....
gi 2309511958 492 agacygRGVCPcsgegvtHHRPPLLFDLSRDPSE 525
Cdd:cd16146 362 ------RLVSP-------KGFQPELYDIENDPGE 382
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-459 |
1.33e-68 |
|
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: 227.10 E-value: 1.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTqHLAAAPLCTPSRAAFLTGRHSFRSGmeasngyralqwnA 120
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNY-------------V 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 121 GSGGLPENETTFARILQQRGYATGLIGKWHQGVNCASrGDHCHHplnHGFDYFYgmpftltndcdpgrppevdaalraqL 200
Cdd:cd16151 67 VFGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGD-GDYPHE---FGFDEYC-------------------------L 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 201 WGytqflalgiLTVAAGKTCGFISVSGRVVTGmacVLFLFFISWYSSFGFVRrwncvlmrnhdvteqpMVLEktaslmlk 280
Cdd:cd16151 118 WQ---------LTETGEKYSRPATPTFNIRNG---KLLETTEGDYGPDLFAD----------------FLID-------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 281 eavsYIERHKHGPFLLFLSLLHVHIPLVTT----------SAFVGKSQHglYGDNVEEMDWLIGKILNAIEDNGLKNSTF 350
Cdd:cd16151 162 ----FIERNKDQPFFAYYPMVLVHDPFVPTpdspdwdpddKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTI 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 351 TYFTSDHGGHLEA---RDGHSQLGGwngiykggkGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLAGG 427
Cdd:cd16151 236 IIFTGDNGTHRPItsrTNGREVRGG---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGA 306
|
410 420 430
....*....|....*....|....*....|..
gi 2309511958 428 EVPQDRVIDGHSLVPLLQGAEARSAHEFLFHY 459
Cdd:cd16151 307 PLPEDYPLDGRSFAPQLLGKTGSPRREWIYWY 338
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
451-585 |
3.09e-62 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 201.39 E-value: 3.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 451 SAHEFLFHYCGQHLHAARWHQrdsgsvWKVHYTTPQFHPEGAGACYGRGVCpcsgegVTHHRPPLLFDLSRDPSEARPLT 530
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2309511958 531 PDSePLYHAVIARVGAAVSEHRHTLSPVPQQFSTSNILWKPWLQPCCGHFPFCSC 585
Cdd:pfam14707 69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
41-426 |
1.95e-59 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 200.34 E-value: 1.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMEASNGyralqwna 120
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 121 gsGGLPENETTFARILQQRGYATGLIGKWHQGVNCASrgdhchHPLNHGFDYFYGMPFTLTNDCDPGRPPevdaalraql 200
Cdd:pfam00884 73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQ------SPCNLGFDKFFGRNTGSDLYADPPDVP---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 201 wgytqflalgiltvaagktcgfisvsgrvvtgmacvlflffiswyssfgfvrrWNCVLMRNHDVteqpmvlektasLMLK 280
Cdd:pfam00884 135 -----------------------------------------------------YNCSGGGVSDE------------ALLD 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 281 EAVSYIERHkHGPFLLFLSLLHVHIPL------------VTTSAFVGKSQHGLYGDNVEEMDWLIGKILNAIEDNGLKNS 348
Cdd:pfam00884 150 EALEFLDNN-DKPFFLVLHTLGSHGPPyypdrypekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDN 228
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2309511958 349 TFTYFTSDHGGHLEARDGHSQLGGWNgiykggkgmGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLAG 426
Cdd:pfam00884 229 TLVVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-529 |
4.96e-57 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 197.02 E-value: 4.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMeASNGYRalqwn 119
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGV-FGNDVP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 120 agsggLPENETTFARILQQRGYATGLIGKWHQGVNCASRGDHCHH----PLNHGFDYFYGMpftLTNDcDPGRPPevdaa 195
Cdd:cd16034 75 -----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKGY---ECNH-DHNNPH----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 196 lraqlwgYtqflalgiltvaagktcgFISVSGRVVTGMacvlflffiswYSSFGFVRRwncvlmrnhdvteqpmvlekta 275
Cdd:cd16034 141 -------Y------------------YDDDGKRIYIKG-----------YSPDAETDL---------------------- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 276 slmlkeAVSYIERHKHG--PFLLFLS------------------------LLHVHIPL-VTTSAFVGKSQHGLYGdNVEE 328
Cdd:cd16034 163 ------AIEYLENQADKdkPFALVLSwnpphdpyttapeeyldmydpkklLLRPNVPEdKKEEAGLREDLRGYYA-MITA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 329 MDWLIGKILNAIEDNGLKNSTFTYFTSDHGGHLEArdgHSQLG---GWNgiykggkgmggweGGIRVPGIFHWPGVLPAG 405
Cdd:cd16034 236 LDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGS---HGLMNkqvPYE-------------ESIRVPFIIRYPGKIKAG 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 406 RVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGHSLVPLLQGAEARSAHEFLFhYCGQHLHA-ARWHQRDSGSVWKVHYTt 484
Cdd:cd16034 300 RVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLL-QCFVPFGGgSARDGGEWRGVRTDRYT- 375
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2309511958 485 pqfhpegagacYGRgvcpcsgegvTHHRPPLLFDLSRDPSEARPL 529
Cdd:cd16034 376 -----------YVR----------DKNGPWLLFDNEKDPYQLNNL 399
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
41-529 |
2.51e-56 |
|
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: 195.08 E-value: 2.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLaAAPLCTPSRAAFLTGRHSFRSGMeasngYRALQWNA 120
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYY-VQPICTPSRAALMTGRYPIHTGM-----QHGVILAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 121 GSGGLPENETTFARILQQRGYATGLIGKWHQGvncasrgdHCHH---PLNHGFDYFYGMpftltndcdpgrppevdaaLR 197
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLG--------FYTWeytPTNRGFDSFYGY-------------------YG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 198 AQLWGYTQflalgilTVAAGKTCGFISvsgrvvtgmacvlflffiswyssfgfvrrwncvlMRNHDVTEQPMVLEKTASL 277
Cdd:cd16029 128 GAEDYYTH-------TSGGANDYGNDD----------------------------------LRDNEEPAWDYNGTYSTDL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 278 MLKEAVSYIERH-KHGPFLLFLSLLHVHIPLVTTSAFVGKSQHGLYGDN----------VEEMDWLIGKILNAIEDNGLK 346
Cdd:cd16029 167 FTDRAVDIIENHdPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKdedrrtyaamVSALDESVGNVVDALKAKGML 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 347 NSTFTYFTSDHGGHLEARDGHSQL-----------GGwngiykggkgmggweggIRVPGIFHWPGVLP-AGRVIGEPTSL 414
Cdd:cd16029 247 DNTLIVFTSDNGGPTGGGDGGSNYplrggkntlweGG-----------------VRVPAFVWSPLLPPkRGTVSDGLMHV 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 415 MDVFPTVVQLAGGEVPQDRVIDGHSLVPLLQGAEARSAHEFL----FHYCGQHLHAARWHQrdsgsvWKVHYTTPqfhpe 490
Cdd:cd16029 310 TDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILlnidDITRTTGGAAIRVGD------WKLIVGKP----- 378
|
490 500 510
....*....|....*....|....*....|....*....
gi 2309511958 491 gagacygrgvcpcsgegvthhrpplLFDLSRDPSEARPL 529
Cdd:cd16029 379 -------------------------LFNIENDPCERNDL 392
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
41-543 |
2.88e-52 |
|
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: 183.48 E-value: 2.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIgDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMEasnGYRALQWNa 120
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAH---GLRSRGFP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 121 gsggLPENETTFARILQQRGYATGLIGKWHqgvncasrgdhchhplnHGFDYFYGMPFTLTNDCDPGRPPEVDAALRAql 200
Cdd:cd16027 76 ----LPDGVKTLPELLREAGYYTGLIGKTH-----------------YNPDAVFPFDDEMRGPDDGGRNAWDYASNAA-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 201 wgytQFLAlgilTVAAGKtcgfisvsgrvvtgmacvlflffiSWYSSFGFV---RRWncvlmrNHDVTEQPMVLEKTASL 277
Cdd:cd16027 133 ----DFLN----RAKKGQ------------------------PFFLWFGFHdphRPY------PPGDGEEPGYDPEKVKV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 278 mlkeavsyierhkhGPFLlflsllhVHIPLVttsafvgKSQHGLYGDNVEEMDWLIGKILNAIEDNGLKNSTFTYFTSDH 357
Cdd:cd16027 175 --------------PPYL-------PDTPEV-------REDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDH 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 358 GGhleardghsQL---------GGwngiykggkgmggweggIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGE 428
Cdd:cd16027 227 GM---------PFprakgtlydSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIE 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 429 VPQDrvIDGHSLVPLLQGaEARSAHEFLFHYCGQHlHAARWHQRdsgSV----WK-VHYttpqFHPEgagacygrgvcpc 503
Cdd:cd16027 281 PPEY--LQGRSFLPLLKG-EKDPGRDYVFAERDRH-DETYDPIR---SVrtgrYKyIRN----YMPE------------- 336
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2309511958 504 sgEgvthhrpplLFDLSRDPSEARPLTPDSEplYHAVIAR 543
Cdd:cd16027 337 --E---------LYDLKNDPDELNNLADDPE--YAEVLEE 363
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
40-542 |
1.94e-49 |
|
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.
Pssm-ID: 293755 [Multi-domain] Cd Length: 429 Bit Score: 177.34 E-value: 1.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMEASNGyralqwn 119
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 120 agsGGLPENETTFARILQQRGYATGLIGKWHQGVNcasrgdhcHHPLNHGFDYFYGMPftltndcDPGRPpevdaalraq 199
Cdd:cd16031 75 ---PLFDASQPTYPKLLRKAGYQTAFIGKWHLGSG--------GDLPPPGFDYWVSFP-------GQGSY---------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 200 lwgytqflalgiltvaagKTCGFISVSGRVVTGmacvlflffisWYSSfgfvrrwncvlmrnhD-VTEQpmvlektaslm 278
Cdd:cd16031 127 ------------------YDPEFIENGKRVGQK-----------GYVT---------------DiITDK----------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 279 lkeAVSYI-ERHKHGPFLLFLSLLHVH-----------------IPLVTTSA---FVGKSQ------------------- 318
Cdd:cd16031 152 ---ALDFLkERDKDKPFCLSLSFKAPHrpftpaprhrglyedvtIPEPETFDdddYAGRPEwareqrnrirgvldgrfdt 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 319 HGLYGDNVE-------EMDWLIGKILNAIEDNGLKNSTFTYFTSDHGGHLeardGHSQLGG-WNgiykggkgmgGWEGGI 390
Cdd:cd16031 229 PEKYQRYMKdylrtvtGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL----GEHGLFDkRL----------MYEESI 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 391 RVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGHSLVPLLQGAEARS-AHEFLFHYcgqhlhaaRW 469
Cdd:cd16031 295 RVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEY--------YE 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 470 HqrdsgsvWKVHYTTPQFhpegagacygrGVcpcsgegVT--------HHRPPL--LFDLSRDPSEARPLTPDSEplYHA 539
Cdd:cd16031 365 E-------PNFHNVPTHE-----------GV-------RTerykyiyyYGVWDEeeLYDLKKDPLELNNLANDPE--YAE 417
|
...
gi 2309511958 540 VIA 542
Cdd:cd16031 418 VLK 420
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
40-529 |
5.17e-48 |
|
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: 172.63 E-value: 5.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGIGDLGCYGNNtLRTPNIDQLAEEGVRLTQ-HlaAAPLCTPSRAAFLTGRHSFRSGM----EASNGYR 114
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGMgtmaELATGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 115 alqwnAGSGGLPENETTFARILQQRGYATGLIGKWHQGVNcasrgdhchhplnhgfDYFYGMPFT------LTNDCDPGR 188
Cdd:cd16025 79 -----GYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------------DYYSTDDLTdkaieyIDEQKAPDK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 189 P----------------PEVDA------------ALRAQLwgYTQFLALGIltVAAGktcgfISVSGRVVTgmacvlflf 240
Cdd:cd16025 138 PfflylafgaphaplqaPKEWIdkykgkydagwdALREER--LERQKELGL--IPAD-----TKLTPRPPG--------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 241 fiswyssfgfVRRWNcvlmrnhDVTEQpmvlEKT--ASLMlkeAVsYierhkhgpfllflsllhvhiplvttSAFvgksq 318
Cdd:cd16025 200 ----------VPAWD-------SLSPE----EKKleARRM---EV-Y-------------------------AAM----- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 319 hglygdnVEEMDWLIGKILNAIEDNGLKNSTFTYFTSDHGGHLEAR------------DGHSQLGGwngiykggkgmggw 386
Cdd:cd16025 225 -------VEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGASAEPGwanasntpfrlyKQASHEGG-------------- 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 387 eggIRVPGIFHWP-GVLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRV------IDGHSLVPLLQGAEARSAHEFLFHY 459
Cdd:cd16025 284 ---IRTPLIVSWPkGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRTQYFE 360
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2309511958 460 CGQhlHAARWHQRdsgsvWKVhyttpqfhpegagacygrgvcpcsgegVTHHRPPL------LFDLSRDPSEARPL 529
Cdd:cd16025 361 LFG--NRAIRKGG-----WKA---------------------------VALHPPPGwgdqweLYDLAKDPSETHDL 402
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-523 |
8.72e-47 |
|
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: 166.95 E-value: 8.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRsgmeasNGYralqWNa 120
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHE------TGV----WD- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 121 GSGGLPENETTFARILQQRGYATGLIGKWHQGvncaSRGDhchhplNHGFDYfygmpftltndcdpgrppevDaalraql 200
Cdd:cd16037 70 NADPYDGDVPSWGHALRAAGYETVLIGKLHFR----GEDQ------RHGFRY--------------------D------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 201 wgytqflalgiltvaagktcgfisvsgRVVTgmacvlflffiswyssfgfvrrwncvlmrnhdvteqpmvlektaslmlK 280
Cdd:cd16037 113 ---------------------------RDVT------------------------------------------------E 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 281 EAVSYIERHKH--GPFLLFLSLLHVHIPLVTTSAFVGKSQHGL---YGDNVEEMDWLIGKILNAIEDNGLKNSTFTYFTS 355
Cdd:cd16037 118 AAVDWLREEAAddKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTS 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 356 DHGGHLEARdghsqlGGWNgiykggkGMGGWEGGIRVPGIFHWPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDRvi 435
Cdd:cd16037 198 DHGDMLGER------GLWG-------KSTMYEESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAPPPPDL-- 261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 436 DGHSLVPLLQGAE--ARSAheflfhYCGQHlhaarWHQRDSGSV------WK-VHYttpqfhpegagacygrgvcpcsge 506
Cdd:cd16037 262 DGRSLLPLAEGPDdpDRVV------FSEYH-----AHGSPSGAFmlrkgrWKyIYY------------------------ 306
|
490
....*....|....*..
gi 2309511958 507 gvtHHRPPLLFDLSRDP 523
Cdd:cd16037 307 ---VGYPPQLFDLENDP 320
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-446 |
3.85e-46 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 167.78 E-value: 3.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMEAsNGYRAlqwNA 120
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLN-NVENA---GA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 121 GSGGLPENETTFARILQQRGYATGLIGKWHQGVNC--ASRGDHCHHPLNHGFDYFY--------------GMPFTLTNDC 184
Cdd:cd16033 77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEEtpLDYGFDEYLPVETTIEYFLadraiemleelaadDKPFFLRVNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 185 ----DPGRPPEVdaalraqlwgytqflalgiltvaagktcgfisvsgrvvtgmacvlflfFISWYS--------SFgfvr 252
Cdd:cd16033 157 wgphDPYIPPEP------------------------------------------------YLDMYDpediplpeSF---- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 253 rwncvlmrNHDVTEQPMVLEKTaSLMLKEAVSYIERHKHgpfllflSLLHvhiplvttsafvgksqhglYGDNVEEMDWL 332
Cdd:cd16033 185 --------ADDFEDKPYIYRRE-RKRWGVDTEDEEDWKE-------IIAH-------------------YWGYITLIDDA 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 333 IGKILNAIEDNGLKNSTFTYFTSDHGGHLEARDGHSQlgGWNGIYKGGkgmggweggiRVPGIFHWPGVLPAGRVIGEPT 412
Cdd:cd16033 230 IGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDK--GPFMYEETY----------RIPLIIKWPGVIAAGQVVDEFV 297
|
410 420 430
....*....|....*....|....*....|....
gi 2309511958 413 SLMDVFPTVVQLAGGEVPQDrvIDGHSLVPLLQG 446
Cdd:cd16033 298 SLLDLAPTILDLAGVDVPPK--VDGRSLLPLLRG 329
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
41-523 |
1.11e-43 |
|
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: 158.90 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMeasngyralqW-N 119
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA----------YdN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 120 AGSggLPENETTFARILQQRGYATGLIGKWH-----QgvncasrgdhchhplNHGFDYfygmpftltndcdpgrppEVDA 194
Cdd:cd16032 71 AAE--FPADIPTFAHYLRAAGYRTALSGKMHfvgpdQ---------------LHGFDY------------------DEEV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 195 ALRAQLWGYTqflalgiltvaagktcgfisvsgrvvtgmacvlflffiswyssfgfvrrwncvLMRNHDvteqpmvlekt 274
Cdd:cd16032 116 AFKAVQKLYD-----------------------------------------------------LARGED----------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 275 aslmlkeavsyiERhkhgPFLLFLSLLHVHIPLVTTSAF----VGKSQHGLYGdNVEEMDWLIGKILNAIEDNGLKNSTF 350
Cdd:cd16032 132 ------------GR----PFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTI 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 351 TYFTSDHGGHLEARdghsqlGGWngiykggKGMGGWEGGIRVPGIFHWPGvLPAGRVIGEPTSLMDVFPTVVQLAGGEVP 430
Cdd:cd16032 195 VIFTSDHGDMLGER------GLW-------YKMSFFEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTA 260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 431 QDRV-IDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQRDSGsvWKVHYttpqfhpegagacygrgvcpcsgegvT 509
Cdd:cd16032 261 PHVPpLDGRSLLPLLEGGDSGGEDEVISEYLAEGAVAPCVMIRRGR--WKFIY--------------------------C 312
|
490
....*....|....
gi 2309511958 510 HHRPPLLFDLSRDP 523
Cdd:cd16032 313 PGDPDQLFDLEADP 326
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
40-449 |
4.71e-42 |
|
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: 156.96 E-value: 4.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGiGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMEASNGY-RALQW 118
Cdd:cd16030 2 KPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYfRKVAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 119 NAgsgglpeneTTFARILQQRGYATGLIGK-WHQGVnCASRGDHchhplnHGFDYFYGMPFTltndcdPGRPPEVDAALR 197
Cdd:cd16030 81 DA---------VTLPQYFKENGYTTAGVGKiFHPGI-PDGDDDP------ASWDEPPNPPGP------EKYPPGKLCPGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 198 AQLWGYTQFLALGILTVAAGKTcgfisVSGRVVTgmACVLFL---------FFIswysSFGFVR---RWNC--------- 256
Cdd:cd16030 139 KGGKGGGGGPAWEAADVPDEAY-----PDGKVAD--EAIEQLrklkdsdkpFFL----AVGFYKphlPFVApkkyfdlyp 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 257 ----VLMRNHDVTEQPMVLEKTaslmLKEAVSYIERHKHGPFLLFLSLlhvhiplvtTSAFVGKSQHGLYGdNVEEMDWL 332
Cdd:cd16030 208 lesiPLPNPFDPIDLPEVAWND----LDDLPKYGDIPALNPGDPKGPL---------PDEQARELRQAYYA-SVSYVDAQ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 333 IGKILNAIEDNGLKNSTFTYFTSDHGGHLeardG-HSQLG---GWNgiykggkgmggweGGIRVPGIFHWPGVLPAGRVI 408
Cdd:cd16030 274 VGRVLDALEELGLADNTIVVLWSDHGWHL----GeHGHWGkhtLFE-------------EATRVPLIIRAPGVTKPGKVT 336
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2309511958 409 GEPTSLMDVFPTVVQLAGgeVPQDRVIDGHSLVPLLQGAEA 449
Cdd:cd16030 337 DALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSA 375
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-442 |
1.78e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 145.38 E-value: 1.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLgIGD-LGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRsgmeasngyralqWN 119
Cdd:cd16148 1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFY-------------HG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 120 AGSGGLPENETTFARILQQRGYATGLIgkwhqgvncasrGDHCHH----PLNHGFDYFygmpftltndcDPGRPPEVDAA 195
Cdd:cd16148 67 VWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLfggpGFDRGFDTF-----------EDFRGQEGDPG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 196 LRAqlwgytqflalgiltvaagktcgfiSVSGRVVTGMACvlflffiswyssfgfvrRWncvlmrnhdvteqpmvLEkta 275
Cdd:cd16148 124 EEG-------------------------DERAERVTDRAL-----------------EW----------------LD--- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 276 slmlkeavsyiERHKHGPFLLFLSLLHVHIPLvttsafvgksqhgLYGDNVEEMDWLIGKILNAIEDNGLKNSTFTYFTS 355
Cdd:cd16148 143 -----------RNADDDPFFLFLHYFDPHEPY-------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTS 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 356 DHGGHL-EardgHSQLGGWNgiykggkgMGGWEGGIRVPGIFHWPGVLPAGRvIGEPTSLMDVFPTVVQLAGGEVPQDrv 434
Cdd:cd16148 199 DHGEEFgE----HGLYWGHG--------SNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY-- 263
|
....*...
gi 2309511958 435 IDGHSLVP 442
Cdd:cd16148 264 SDGRSLLP 271
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
41-552 |
3.13e-39 |
|
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: 149.33 E-value: 3.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFrsgmeasnGYRALqWNA 120
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLM--------NHRSV-WNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 121 GSggLPENETTFARILQQRGYATGLIGKWHQGVNcaSRGDHCHHPLNH-------GFDYFYGMPFTLTNDCDpgrppevd 193
Cdd:cd16028 72 TP--LDARHLTLALELRKAGYDPALFGYTDTSPD--PRGLAPLDPRLLsyelampGFDPVDRLDEYPAEDSD-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 194 aalraqlwgyTQFLalgiltvaAGKTCGFISVSGRVvtgmacvlflffiSWYSSFGFVR-RWNCVLMR--NHDVTEQPMV 270
Cdd:cd16028 140 ----------TAFL--------TDRAIEYLDERQDE-------------PWFLHLSYIRpHPPFVAPApyHALYDPADVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 271 LEKTASLMLKEAvsyierHKHgPFL-LFL------SLLHVHIPLVTTSAFVGKSQHGLYGDNVEEMDWLIGKILNAIEDN 343
Cdd:cd16028 189 PPIRAESLAAEA------AQH-PLLaAFLerieslSFSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKET 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 344 GLKNSTFTYFTSDHGGHLeardG-HSQLG--GWNGIYKggkgmggweggiRVPGIFHWPGVL---PAGRVIGEPTSLMDV 417
Cdd:cd16028 262 GQWDDTLIVFTSDHGEQL----GdHWLWGkdGFFDQAY------------RVPLIVRDPRREadaTRGQVVDAFTESVDV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 418 FPTVVQLAGGEVPQDrvIDGHSLVPLLQGAEA---RSA--HEFLFHYC---------GQHLHAARWHQRDSGSvWK-VHY 482
Cdd:cd16028 326 MPTILDWLGGEIPHQ--CDGRSLLPLLAGAQPsdwRDAvhYEYDFRDVstrrpqealGLSPDECSLAVIRDER-WKyVHF 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 483 ttPQFhpegagacygrgvcpcsgegvthhrPPLLFDLSRDPSEARPLTPDsePLYHAVIARVGAAVSEHR 552
Cdd:cd16028 403 --AAL-------------------------PPLLFDLKNDPGELRDLAAD--PAYAAVVLRYAQKLLSWR 443
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-543 |
3.73e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 147.33 E-value: 3.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQ-HLAAA---PLCTPSRAAFLTGRHSFRSGMEasngyra 115
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNMGGwsgAVCVPSRAMLMTGRTLFHAPEG------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 116 lqwnaGSGGLPENETTFARILQQRGYATGLIGKWHQGVncasrgdhchhplnhgfdyfygmpftltndcdpgrppeVDAA 195
Cdd:cd16155 75 -----GKAAIPSDDKTWPETFKKAGYRTFATGKWHNGF--------------------------------------ADAA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 196 LRaqlwgytqflalgiltvaagktcgfisvsgrvvtgmacvlFL---------FFIswYSSFgfvrrwncvlMRNHD--- 263
Cdd:cd16155 112 IE----------------------------------------FLeeykdgdkpFFM--YVAF----------TAPHDprq 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 264 VTEQPMVLEKTASLMLKEavSYIERH--KHGPFLLFLSLLHvhiPLVTTSAFVgKSQHGLYGDNVEEMDWLIGKILNAIE 341
Cdd:cd16155 140 APPEYLDMYPPETIPLPE--NFLPQHpfDNGEGTVRDEQLA---PFPRTPEAV-RQHLAEYYAMITHLDAQIGRILDALE 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 342 DNGLKNSTFTYFTSDHGghLeARDGHSQLGGWNgiykggkgmgGWEGGIRVPGIFHWPGVlPAGRVIGEPTSLMDVFPTV 421
Cdd:cd16155 214 ASGELDNTIIVFTSDHG--L-AVGSHGLMGKQN----------LYEHSMRVPLIISGPGI-PKGKRRDALVYLQDVFPTL 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 422 VQLAGGEVPQDrvIDGHSLVPLLQGaEARSAHEFLF-HYCGqhlhaarwHQRD-SGSVWKVHYTTPqfhpegagacygrg 499
Cdd:cd16155 280 CELAGIEIPES--VEGKSLLPVIRG-EKKAVRDTLYgAYRD--------GQRAiRDDRWKLIIYVP-------------- 334
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2309511958 500 vcpcsgeGVTHhrpPLLFDLSRDPSEARPLtpDSEPLYHAVIAR 543
Cdd:cd16155 335 -------GVKR---TQLFDLKKDPDELNNL--ADEPEYQERLKK 366
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-442 |
1.61e-38 |
|
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: 142.38 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGR-------HSFRSGMEASNGY 113
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRmpsqhgiHDWIVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 114 RALQWnagsgglPENETTFARILQQRGYATGLIGKWHQGvncasrgdhchhplnhgfdyfygmpftltndcdpgrppevD 193
Cdd:cd16149 81 KPEGY-------LEGQTTLPEVLQDAGYRCGLSGKWHLG----------------------------------------D 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 194 AALRaqlwgytqflalgiltvaagktcgfisvsgrvvtgmacvlflFFIswyssfgfvrrwncvlmRNHDvteqpmvlek 273
Cdd:cd16149 114 DAAD------------------------------------------FLR-----------------RRAE---------- 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 274 taslmlkeavsyierhKHGPFLLFLSLLHVHiplvttsafvgkSQHGlYGDNVEEMDWLIGKILNAIEDNGLKNSTFTYF 353
Cdd:cd16149 125 ----------------AEKPFFLSVNYTAPH------------SPWG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIF 175
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 354 TSDHG---GH---LEARDGHSQLGGWNgiykggkgmggweGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLAGG 427
Cdd:cd16149 176 TSDNGfnmGHhgiWGKGNGTFPLNMYD-------------NSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGV 242
|
410
....*....|....*
gi 2309511958 428 EVPQDRVIDGHSLVP 442
Cdd:cd16149 243 DPPADPRLPGRSFAD 257
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
40-534 |
1.16e-34 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 137.11 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGiGD-LGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMEasnGYralqw 118
Cdd:PRK13759 6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---GY----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 119 naGSGGLPENETTFARILQQRGYATGLIGKWHqgvncasrgdhcHHPLN--HGFDYfygmpfTLTNDCDPGRPPEVDAAL 196
Cdd:PRK13759 77 --GDVVPWNYKNTLPQEFRDAGYYTQCIGKMH------------VFPQRnlLGFHN------VLLHDGYLHSGRNEDKSQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 197 RAQLWGYTQFLALGiltvAAGKTCGFISVsgrvvtGMACVlflffiSWYSsfgfvRRWncvlmrnhDVTEQpmvLEKTAs 276
Cdd:PRK13759 137 FDFVSDYLAWLREK----APGKDPDLTDI------GWDCN------SWVA-----RPW--------DLEER---LHPTN- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 277 LMLKEAVSYIERHKHG-PFLLFLSLLHVHIPL---------------------------------VTTSAFVG------- 315
Cdd:PRK13759 184 WVGSESIEFLRRRDPTkPFFLKMSFARPHSPYdppkryfdmykdadipdphigdweyaedqdpegGSIDALRGnlgeeya 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 316 -KSQHGLYGdNVEEMDWLIGKILNAIEDNGLKNSTFTYFTSDH----GGHLEARDGHSQLGgwngiykggkgmggwegGI 390
Cdd:PRK13759 264 rRARAAYYG-LITHIDHQIGRFLQALKEFGLLDNTIILFVSDHgdmlGDHYLFRKGYPYEG-----------------SA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 391 RVPGIFHWPG---VLPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGHSLVPLLQGAEARSAHEFlfhycgqHLHAA 467
Cdd:PRK13759 326 HIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYEGWRPYL-------HGEHA 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2309511958 468 RWHQRDsgsvwkvHYTTPQFHPegagacYGRGvcpcSGEGVTHhrpplLFDLSRDPSEARPLTPDSE 534
Cdd:PRK13759 397 LGYSSD-------NYLTDGKWK------YIWF----SQTGEEQ-----LFDLKKDPHELHNLSPSEK 441
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-446 |
2.99e-33 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 130.81 E-value: 2.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMeasngYRalqwN 119
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR----N 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 120 AGSggLPENETTFARILQQRGYATGLIGKWHqgvncasrgdhchhplnhgfdyfygmpftltndcdpgrppevdaalraq 199
Cdd:cd16152 72 GIP--LPADEKTLAHYFRDAGYETGYVGKWH------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 200 LWGYtqflalgiltvaagktcgfisvsgRV--VTGMACvlflffiswyssfgfvrrwncvlmrnhdvteqpmvlektasl 277
Cdd:cd16152 101 LAGY------------------------RVdaLTDFAI------------------------------------------ 114
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 278 mlkeavSYIERHKHG-PFLLFLSLLHVH----------------------IP--LvttSAFVGKSQHGL---YGdNVEEM 329
Cdd:cd16152 115 ------DYLDNRQKDkPFFLFLSYLEPHhqndrdryvapegsaerfanfwVPpdL---AALPGDWAEELpdyLG-CCERL 184
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 330 DWLIGKILNAIEDNGLKNSTFTYFTSDHGGHLEARDG------HSqlggwngiykggkgmggweGGIRVPGIFHWPGVLp 403
Cdd:cd16152 185 DENVGRIRDALKELGLYDNTIIVFTSDHGCHFRTRNAeykrscHE-------------------SSIRVPLVIYGPGFN- 244
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2309511958 404 AGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGHSLVPLLQG 446
Cdd:cd16152 245 GGGRVEELVSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDG 285
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
40-439 |
4.60e-31 |
|
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: 124.97 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLgigDLGCYGNNTLRtPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGM----EASNGYRA 115
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVtnnsPPGGGYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 116 lQWNAGsgglpENETTFARILQQRGYATGLIGKWHQGVNcaSRGDHCHHPLnhGFDYFYGMPFTLTNDcdpgrppevdaa 195
Cdd:cd16147 77 -FWQNG-----LERSTLPVWLQEAGYRTAYAGKYLNGYG--VPGGVSYVPP--GWDEWDGLVGNSTYY------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 196 lraqlwGYTqflalgiltvaagktcgfISVSGRVVTGmacvlfLFFISWYSSfgfvrrwncvlmrnhDVteqpmVLEKta 275
Cdd:cd16147 135 ------NYT------------------LSNGGNGKHG------VSYPGDYLT---------------DV-----IANK-- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 276 slmlkeAVSYIERHKHG--PFLLFLSLLHVHIPLV-----------------TTSAFVGKSQH--------GLYGDNVEE 328
Cdd:cd16147 163 ------ALDFLRRAAADdkPFFLVVAPPAPHGPFTpapryanlfpnvtapprPPPNNPDVSDKphwlrrlpPLNPTQIAY 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 329 MDW--------------LIGKILNAIEDNGLKNSTFTYFTSDHGGHLeardG-HSQLGGwngiykggkGMGGWEGGIRVP 393
Cdd:cd16147 237 IDElyrkrlrtlqsvddLVERLVNTLEATGQLDNTYIIYTSDNGYHL----GqHRLPPG---------KRTPYEEDIRVP 303
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2309511958 394 GIFHWPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVPQDrvIDGHS 439
Cdd:cd16147 304 LLVRGPGI-PAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGRS 346
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-449 |
7.73e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 119.26 E-value: 7.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGR--HsfrsgmeaSNGYRALqw 118
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWypH--------VNGHRTL-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 119 nagSGGLPENETTFARILQQRGYATGLIGKwhqgvncasrgdhchhplnhgfdyfygmpftltNDCDPGRppevdaalra 198
Cdd:cd16150 71 ---HHLLRPDEPNLLKTLKDAGYHVAWAGK---------------------------------NDDLPGE---------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 199 qlwgytqflalgiltVAAGKTCgfisvsgrvvtgmacvlflffiswyssfgfvrrwncvlmrnhDVTEqpmvlektasLM 278
Cdd:cd16150 105 ---------------FAAEAYC------------------------------------------DSDE----------AC 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 279 LKEAVSYIERHK-HGPFLLFLSLLHVH------------------IPLVTT--------SAFVGKSQHGLYGDN------ 325
Cdd:cd16150 118 VRTAIDWLRNRRpDKPFCLYLPLIFPHppygveepwfsmidreklPPRRPPglrakgkpSMLEGIEKQGLDRWSeerwre 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 326 --------VEEMDWLIGKILNAIEDNGLKNSTFTYFTSDHG------GHLEARDG--HSQLggwngiykggkgmggwegg 389
Cdd:cd16150 198 lratylgmVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGdytgdyGLVEKWPNtfEDCL------------------- 258
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 390 IRVPGIFHWPGvLPAGRVIGEPTSLMDVFPTVVQLAGgeVPQDRVIDGHSLVPLLQGAEA 449
Cdd:cd16150 259 TRVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAG--IPLSHTHFGRSLLPVLAGETE 315
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
41-450 |
6.87e-28 |
|
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: 117.10 E-value: 6.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMeasngyralqWnA 120
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------W-T 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 121 GSGGLPENETTFARILQQRGYATGLIGKWHqgvncasrgdhchhpLNhGFDYF-YGMpftltndCDPGRPPEvdaalraq 199
Cdd:cd16156 70 NCMALGDNVKTIGQRLSDNGIHTAYIGKWH---------------LD-GGDYFgNGI-------CPQGWDPD-------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 200 LWgYTQFLALGILTVAAgktcgfISVSGRVVTgmacvlflffiswyssfgfvrrwncvLMRNHDVTEqpmvlEKT-ASLM 278
Cdd:cd16156 119 YW-YDMRNYLDELTEEE------RRKSRRGLT--------------------------SLEAEGIKE-----EFTyGHRC 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 279 LKEAVSYIERHKHGPFLLFLSLLHVHIPLVTTSAFV----------GKSQHglygDNVEE-------------------- 328
Cdd:cd16156 161 TNRALDFIEKHKDEDFFLVVSYDEPHHPFLCPKPYAsmykdfefpkGENAY----DDLENkplhqrlwagakphedgdkg 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 329 -------------MDWLIGKILNAIEDNgLKNSTFTYfTSDHGGHLEARDGHSQlggwngiykggkGMGGWEGGIRVPGI 395
Cdd:cd16156 237 tikhplyfgcnsfVDYEIGRVLDAADEI-AEDAWVIY-TSDHGDMLGAHKLWAK------------GPAVYDEITNIPLI 302
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2309511958 396 FHWPGVLPAGRVIGEPTSLMDVFPTVVQLAGgeVPQDRVIDGHSLVPLLQGAEAR 450
Cdd:cd16156 303 IRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILATIEDPEIP 355
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
40-441 |
7.23e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 113.24 E-value: 7.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 40 RPNILLIMADDLGIGDLGCYGN----------NTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMEA 109
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 110 SNGYralqWNAGSGGLPenetTFARILQQRGYATGLIGKWHqgvncasrgdhchhplnhgfdyfygmpftltndcdpgrp 189
Cdd:cd16153 81 FEAA----HPALDHGLP----TFPEVLKKAGYQTASFGKSH--------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 190 peVDAALRAqlwgytqflalgilTVAAGKTcgFISVSGRVVTGMAcvlflffiswyssfgfvrrwncvlmrnhdvteqpm 269
Cdd:cd16153 114 --LEAFQRY--------------LKNANQS--YKSFWGKIAKGAD----------------------------------- 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 270 vlektaslmlkeavsyierhKHGPFLLFLSLLHVHIPLVTTSAFVgksQHGLYGDNVEEMDWLIGKILNAIEDNGLKN-- 347
Cdd:cd16153 141 --------------------SDKPFFVRLSFLQPHTPVLPPKEFR---DRFDYYAFCAYGDAQVGRAVEAFKAYSLKQdr 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 348 -STFTYFTSDHGGHLEARDGHSQLGGWNgiykggkgmggweGGIRVPGIFHWPGVL--PAGRVIGEPTSLMDVFPTVVQL 424
Cdd:cd16153 198 dYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QSHRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTLLAA 264
|
410
....*....|....*..
gi 2309511958 425 AGGEVPQDRVIDGHSLV 441
Cdd:cd16153 265 AGVDVDAPDYLDGRDLF 281
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
41-425 |
4.24e-27 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 109.82 E-value: 4.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTLRTPNIDQLAEEGVRL-TQHLAAAPLCTPSRAAFLTGRHSFRSGMeASNGYRALQWN 119
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGY-TGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 120 AGSGGLPENETTFARILQQRGYATGLIGkwhqgvncasrgdhchhplnhgfdyfygmpftltndcdpgrppevdaalraq 199
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG---------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 200 lwgytqflalgiltvaagktcgfisvsgrvvtgmacvlflffiswyssfgfvrrwncvlmrnhdvteqpmvlektaslmL 279
Cdd:cd00016 108 -------------------------------------------------------------------------------L 108
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 280 KEAVSYIERHKhgPFLLFLSLLHVHIPLVTTsafvgKSQHGLYGDNVEEMDWLIGKILNAIEDNGLKNSTFTYFTSDHGG 359
Cdd:cd00016 109 LKAIDETSKEK--PFVLFLHFDGPDGPGHAY-----GPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG 181
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2309511958 360 HLEardGHSQLGGwngiykGGKGMGGWEGGIRVPGIFHWPGVlPAGRVIGEPTSLMDVFPTVVQLA 425
Cdd:cd00016 182 IDK---GHGGDPK------ADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-449 |
4.68e-27 |
|
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: 112.83 E-value: 4.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGIGDLGCYGNNTL--RTPNIDQLAEEGVRLTqHLAAAPLCTPSRAAFLTGRHSFRSGMEASNGYRAlqw 118
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTGVLAVPDELL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 119 nagsggLPENETTFARILQQR--GYATGLIGKWHQGvncasrGDHCHHPLNHGFDYFYGmpftltndcdpgrppevdaAL 196
Cdd:cd16154 77 ------LSEETLLQLLIKDATtaGYSSAVIGKWHLG------GNDNSPNNPGGIPYYAG-------------------IL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 197 RAQLWGYTQflalgiltvaagktcgfisvsgrvvtgmacvlflffiswyssfgfvrrWNCVlmrNHDVTEQpmVLEKTAS 276
Cdd:cd16154 126 GGGVQDYYN------------------------------------------------WNLT---NNGQTTN--STEYATT 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 277 LMLKEAVSYIERhKHGPFLLFLSLL--HV--HIP--------LVTTSAFVGKSQHGLYGDNVEEMDWLIGKILNAIEDNG 344
Cdd:cd16154 153 KLTNLAIDWIDQ-QTKPWFLWLAYNapHTpfHLPpaelhsrsLLGDSADIEANPRPYYLAAIEAMDTEIGRLLASIDEEE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 345 LKNsTFTYFTSDHGGHLEARD-----GHSQ----LGGwngiykggkgmggweggIRVPGIFHWPGVlpaGRVIGEPTSLM 415
Cdd:cd16154 232 REN-TIIIFIGDNGTPGQVVDlpytrNHAKgslyEGG-----------------INVPLIVSGAGV---ERANERESALV 290
|
410 420 430
....*....|....*....|....*....|....*..
gi 2309511958 416 ---DVFPTVVQLAGGEVPQdrVIDGHSLVPLLQGAEA 449
Cdd:cd16154 291 natDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNA 325
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
41-524 |
1.19e-23 |
|
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: 103.00 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADDLGiGDLGCY-GNNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSgmEASNGYRalqwn 119
Cdd:cd16171 1 PNVVMVMSDSFD-GRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLT--ESWNNYK----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 120 agsgGLPENETTFARILQQRGYATGLIGK--WHQGvncasrgdhcHHPLNHGFD-YFYGMPFTLTNDcdpGRPPEVdaal 196
Cdd:cd16171 73 ----GLDPNYPTWMDRLEKHGYHTQKYGKldYTSG----------HHSVSNRVEaWTRDVPFLLRQE---GRPTVN---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 197 raqlwgytqflalgiLTVAAGKTcgfisvsgRVVtgmacvlflffiswyssfgfVRRWNcvlmrnhdvteqpmVLEKTAS 276
Cdd:cd16171 132 ---------------LVGDRSTV--------RVM--------------------LKDWQ--------------NTDKAVH 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 277 LMLKEAVSYIErhkhgPFLLFLSLlhvHIPLVTTSAFVGKSQHGL------YGDNVEEMDWLIGKILNAIEDNGLKNSTF 350
Cdd:cd16171 155 WIRKEAPNLTQ-----PFALYLGL---NLPHPYPSPSMGENFGSIrnirafYYAMCAETDAMLGEIISALKDTGLLDKTY 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 351 TYFTSDHGghlEARDGHSQLggwngiykggKGMGGWEGGIRVPGIFHWPGVlPAGRVIGEPTSLMDVFPTVVQLAGGEVP 430
Cdd:cd16171 227 VFFTSDHG---ELAMEHRQF----------YKMSMYEGSSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQP 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 431 QDrvIDGHSLVPLLQGAEARSAHEFLFH-------YCGQHLHAARWHQRDSGsvWKvhYTTpqfhpegagacYGRGVcpc 503
Cdd:cd16171 293 QN--LSGYSLLPLLSESSIKESPSRVPHpdwvlseFHGCNVNASTYMLRTNS--WK--YIA-----------YADGN--- 352
|
490 500
....*....|....*....|.
gi 2309511958 504 sgegvthHRPPLLFDLSRDPS 524
Cdd:cd16171 353 -------SVPPQLFDLSKDPD 366
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
41-459 |
8.20e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 99.20 E-value: 8.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADD--------LGIGDLGCygnntlrtPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMeASNG 112
Cdd:cd16035 1 PNILLILTDQerypppwpAGWAALNL--------PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGV-TDTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 113 YRALQWNAgSGGLPenetTFARILQQRGYATGLIGKWHqgvncasrgdhchhplnhgfdyfygmpftltndcdpgrppev 192
Cdd:cd16035 72 GSPMQPLL-SPDVP----TLGHMLRAAGYYTAYKGKWH------------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 193 daaLRAQLWGYTQFlalgiltvaagktcgfisvsGRVVTGMACvlflffiswyssfgfvrRWncvlMRNHDVteqpmvle 272
Cdd:cd16035 105 ---LSGAAGGGYKR--------------------DPGIAAQAV-----------------EW----LRERGA-------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 273 ktaslmlkeavsyiERHKHGPFLLFLSLL--H-VHIPLVTTSAFVgkSQHGLYGDNVEEMDWLIGKILNAIEDNGLKNST 349
Cdd:cd16035 133 --------------KNADGKPWFLVVSLVnpHdIMFPPDDEERWR--RFRNFYYNLIRDVDRQIGRVLDALDASGLADNT 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 350 FTYFTSDHGGHLEARDGHSQLGgwngiykggkgmGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPTVVQLAGGEV 429
Cdd:cd16035 197 IVVFTSDHGEMGGAHGLRGKGF------------NAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDA 264
|
410 420 430
....*....|....*....|....*....|....*
gi 2309511958 430 PQDRVID----GHSLVPLLQGAEARSAHE-FLFHY 459
Cdd:cd16035 265 EARATEApplpGRDLSPLLTDADADAVRDgILFTY 299
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
287-423 |
7.04e-09 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 58.76 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 287 ERHKHGPFLLFLSLLHVHI------------------PLVTTSAFVGKSQHGLYGDNVEEMDWLIGKILNAIEDNGLKNS 348
Cdd:COG3083 376 QRDSDRPWFSYLFLDAPHAysfpadypkpfqpsedcnYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLEN 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2309511958 349 TFTYFTSDHGGHLEARDGHSQLGGWNGIYKGgkgmggweggIRVPGIFHWPGVLPagRVIGEPTSLMDVFPTVVQ 423
Cdd:COG3083 456 TIVIITADHGEEFNENGQNYWGHNSNFSRYQ----------LQVPLVIHWPGTPP--QVISKLTSHLDIVPTLMQ 518
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
41-426 |
5.95e-06 |
|
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: 48.45 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 41 PNILLIMADdlGIGD--LGCYGNNTLRTPNIDQLAEEGVRLTQHLAAAplctpsraaflTGRHSFRSGMEASNGYRALQW 118
Cdd:cd16015 1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPG-----------FGGGTANGEFEVLTGLPPLPL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 119 NAGSGGLPENET--TFARILQQRGYATGLIgkwhqgvncasrgdhchhplnHGFD-YFYGMpftltndcdpgrppevDAA 195
Cdd:cd16015 68 GSGSYTLYKLNPlpSLPSILKEQGYETIFI---------------------HGGDaSFYNR----------------DSV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 196 LRAQlwGYTQFLALGILTVAAGKTcgfisvsgrvvtgmacvlflffISWYSSfgfvrrwncvlmrnhDvteqpmvlekta 275
Cdd:cd16015 111 YPNL--GFDEFYDLEDFPDDEKET----------------------NGWGVS---------------D------------ 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 276 SLMLKEAVSYIERHKHGPFLLFLSLLHVH----IPLVTTSAFVGKSQHGLYGDN----VEEMDWLIGKILNAIEDNGL-K 346
Cdd:cd16015 140 ESLFDQALEELEELKKKPFFIFLVTMSNHgpydLPEEKKDEPLKVEEDKTELENylnaIHYTDKALGEFIEKLKKSGLyE 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 347 NSTFtYFTSDHGGHLEARDGHSQLGGWNGIykggkgmggweggiRVPGIFHWPGVLPaGRVIGEPTSLMDVFPTVVQLAG 426
Cdd:cd16015 220 NTII-VIYGDHLPSLGSDYDETDEDPLDLY--------------RTPLLIYSPGLKK-PKKIDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
33-440 |
9.61e-06 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 48.50 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 33 PKTANAFRPNILLIM----ADDLgigdLGCYGNNTLRTPNIDQLAEEGVRLTQHLAaaplctpsraaflTGRHSFRS--- 105
Cdd:COG1368 227 NPFGPAKKPNVVVILlesfSDFF----IGALGNGKDVTPFLDSLAKESLYFGNFYS-------------QGGRTSRGefa 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 106 ---GMEASNGYRALQwnagsggLPENET--TFARILQQRGYATGLIgkwhqgvncasrgdhchhplnHGFD-YFYGMpft 179
Cdd:COG1368 290 vltGLPPLPGGSPYK-------RPGQNNfpSLPSILKKQGYETSFF---------------------HGGDgSFWNR--- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 180 ltndcdpgrppevDAALRAQlwGYTQFlalgiltvaagktcgfisvsgrvvtgmacvlflFFISWYSSfGFVRRWNCvlm 259
Cdd:COG1368 339 -------------DSFYKNL--GFDEF---------------------------------YDREDFDD-PFDGGWGV--- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 260 rnHDvteqpmvlektaSLMLKEAVSYIERHKhGPFLLFLsllhvhiplVTTS--------------AFVGKSQHGLYGDN 325
Cdd:COG1368 367 --SD------------EDLFDKALEELEKLK-KPFFAFL---------ITLSnhgpytlpeedkkiPDYGKTTLNNYLNA 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309511958 326 VEEMDWLIGKILNAIEDNGL-KNSTFtYFTSDHGGHLEARDGHSQLggwngiykggkgmggwEGGIRVPGIFHWPGvLPA 404
Cdd:COG1368 423 VRYADQALGEFIEKLKKSGWyDNTIF-VIYGDHGPRSPGKTDYENP----------------LERYRVPLLIYSPG-LKK 484
|
410 420 430
....*....|....*....|....*....|....*.
gi 2309511958 405 GRVIGEPTSLMDVFPTVVQLAGGEVPQDRVIdGHSL 440
Cdd:COG1368 485 PKVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDL 519
|
|
| |
