|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
21-545 |
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: 952.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 21 RPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFT 100
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 101 ASSGGLPTDEITFAKLLKDQGYSTALIGKWHLGMSCHSKTDFCHHPLHHGFNYFYGISLTNLRDCKPGEGSVFTTGFKRL 180
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGDGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 181 VFLPLQIVGVTLLTLAALNCLGllHVPLGVFFSLLFLAALILTLFLGFLHYFRPLNCFMMRNYEIIQQPMSYDNLTQRLT 260
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLYLG--AVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVEQPMSLENLTQRLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 261 VEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFAGKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGA 340
Cdd:cd16159 239 KEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 341 HVEEVSSKGEIHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRIIDGRD 420
Cdd:cd16159 319 HLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 421 LMPLLEGKSQRSDHEFLFHYCNAYLNAVRWHPQNSTSIWKAFFFTPNFNPvGSNGCFATHVCFCFGSYVTHHDPPLLFDI 500
Cdd:cd16159 399 LMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYP-GTEGCCGTLLCRCFGDSVTHHDPPLLFDL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1002913047 501 SKDPRERNPLTPASEPrFYEILKVMQEAADRHTQTLPEVPDQFSW 545
Cdd:cd16159 478 SADPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLSF 521
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
21-511 |
0e+00 |
|
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: 569.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 21 RPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMAswsrtGVFLFT 100
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLP-----GVVGPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 101 ASSGGLPTDEITFAKLLKDQGYSTALIGKWHLGMSchsktdFCHHPLHHGFNYFYGISLTNLRDCKPGEGSVFttgfkrl 180
Cdd:cd16026 76 GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQ------PEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDP------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 181 vflplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfRPLNCFMMRNYEIIQQPMSYDNLTQRLT 260
Cdd:cd16026 143 ----------------------------------------------------PGPLPPLMENEEVIEQPADQSSLTQRYT 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 261 VEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFAGKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGA 340
Cdd:cd16026 171 DEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 341 HVEEvsskgEIHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRIIDGRD 420
Cdd:cd16026 251 WLEY-----GGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 421 LMPLLEGKSQRSDHEFLFHYCNAYLNAVRWHPqnstsiWKAFFFTPNFNPvgsngcfathvCFCFGSYVTHHDPPLLFDI 500
Cdd:cd16026 326 ISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTG-----------TDPGGLDPTKLEPPLLYDL 388
|
490
....*....|.
gi 1002913047 501 SKDPRERNPLT 511
Cdd:cd16026 389 EEDPGETYNVA 399
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
21-527 |
4.50e-148 |
|
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: 433.78 E-value: 4.50e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 21 RPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMasWSRTGVFLfT 100
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGM--YGGTRVFL-P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 101 ASSGGLPTDEITFAKLLKDQGYSTALIGKWHLGMSCHSKTDFCHHPLHHGFNyFYGISL--TNLRDCKPGEgsvfttgfk 178
Cdd:cd16160 78 WDIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVGTNLpfTNSWACDDTG--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 179 rlvflplqivgvtlltlaalnclglLHVPlgvffsllflaaliltlflgFLHyfrPLNCFMMRNYEIIQQPMSYDNLTQR 258
Cdd:cd16160 148 -------------------------RHVD--------------------FPD---RSACFLYYNDTIVEQPIQHEHLTET 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 259 LTVEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFAGKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQ 338
Cdd:cd16160 180 LVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDH 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 339 GAHVEEVSskgeiHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKiDEPTSNMDIFPTVAKLAGAPLPEDRIIDG 418
Cdd:cd16160 260 GPHVEYCL-----EGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIKPRVS-HEVVSTMDIFPTFVDLAGGTLPTDRIYDG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 419 RDLMPLLEGKSQRSDHEFLFHYCNaYLNAVRWHPqnstsiWKAFFFT---PNFNPVGSN---GCFATH--VC-FCFGSYV 489
Cdd:cd16160 334 LSITDLLLGEADSPHDDILYYCCS-RLMAVRYGS------YKIHFKTqplPSQESLDPNcdgGGPLSDyiVCyDCEDECV 406
|
490 500 510
....*....|....*....|....*....|....*....
gi 1002913047 490 THHDPPLLFDISKDPRERNPLTPA-SEPRFYEILKVMQE 527
Cdd:cd16160 407 TKHNPPLIFDVEKDPGEQYPLQPSvYEHMLEAVEKLIAH 445
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-541 |
9.94e-116 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 349.18 E-value: 9.94e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 1 MK--IPFLLLFFLWEAESHAASRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFM 78
Cdd:COG3119 1 MKrlLLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 79 TGRYPVRSGMASWSrtgvflfTASSGGLPTDEITFAKLLKDQGYSTALIGKWHLgmschsktdfchhplhhgfnyfygis 158
Cdd:COG3119 81 TGRYPHRTGVTDNG-------EGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL-------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 159 ltnlrdckpgegsvfttgfkrlvflplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfrplncf 238
Cdd:COG3119 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 239 mmrnyeiiqqpmsydNLTQRLTVEAAQFIQRNT--ETPFLLVLSYLHVHT---------ALFSSKDFA------------ 295
Cdd:COG3119 128 ---------------YLTDLLTDKAIDFLERQAdkDKPFFLYLAFNAPHApyqapeeylDKYDGKDIPlppnlaprdlte 192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 296 --GKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGAHVEEvsskgeiHGgsngiYKGGKANNWEGGIRV 373
Cdd:COG3119 193 eeLRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGE-------HG-----LRGGKGTLYEGGIRV 260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 374 PGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDriIDGRDLMPLLEGKSQRSDHEFLFHYCNAYLN-AVRWHP 452
Cdd:COG3119 261 PLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNrAIRTGR 338
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 453 qnstsiWKAFFftpnfnpvgsngcfathvcfcfgsYVTHHDPPLLFDISKDPRERNPLTpASEPrfyEILKVMQEAADRH 532
Cdd:COG3119 339 ------WKLIR------------------------YYDDDGPWELYDLKNDPGETNNLA-ADYP---EVVAELRALLEAW 384
|
....*....
gi 1002913047 533 TQTLPEVPD 541
Cdd:COG3119 385 LKELGDPPL 393
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
22-567 |
1.82e-114 |
|
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: 349.05 E-value: 1.82e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASwsrtGVFlFTA 101
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYP----GVF-YPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 SSGGLPTDEITFAKLLKDQGYSTALIGKWHLGMSCHSKtdfcHHPLHHGFNYFYGISLT-------NLrDCKPGEGSVFT 174
Cdd:cd16158 77 SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLGIPYShdqgpcqNL-TCFPPNIPCFG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 175 TGFKRLVFLPLqivgvtlltlaalnclgllhvplgvFFsllflaaliltlflgflhyfrplncfmmrNYEIIQQPMSYDN 254
Cdd:cd16158 152 GCDQGEVPCPL-------------------------FY-----------------------------NESIVQQPVDLLT 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 255 LTQRLTVEAAQFIQRNTE--TPFLLVLSYLHVHTALFSSKDFAGKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLI 332
Cdd:cd16158 178 LEERYAKFAKDFIADNAKegKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 333 YFTSDQGAHVEEVSskgeiHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIdEPTSNMDIFPTVAKLAGAPLPE 412
Cdd:cd16158 258 FFTSDNGPSTMRKS-----RGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLPN 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 413 dRIIDGRDLMPLL--EGKSQRSDheflFHYCNAYLN------AVRWHPqnstsiWKAFFFTPNFNPVGSNGCFATHVCfc 484
Cdd:cd16158 332 -VTLDGVDMSPILfeQGKSPRQT----FFYYPTSPDpdkgvfAVRWGK------YKAHFYTQGAAHSGTTPDKDCHPS-- 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 485 fgSYVTHHDPPLLFDISKDPRERNPLTpaSEPRFYEILKVMQEAADRHTQTLPEVPDQFSWNNflwKPWLQLCC------ 558
Cdd:cd16158 399 --AELTSHDPPLLFDLSQDPSENYNLL--GLPEYNQVLKQIQQVKERFEASMKFGESEINKGE---DPALEPCCkpgctp 471
|
570
....*....|
gi 1002913047 559 -PSTglsCQC 567
Cdd:cd16158 472 kPSC---CQC 478
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
22-532 |
1.34e-113 |
|
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: 344.53 E-value: 1.34e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFTA 101
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 -------SSGGLPTDEITFAKLLKDQGYSTALIGKWHLGMschsktDFCHHPLHHGFNYFYGisltnlrDCKPGEGSVFT 174
Cdd:cd16144 81 tklipppSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGG------EGGYGPEDQGFDVNIG-------GTGNGGPPSYY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 175 TGFKRLVFLPlqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfrplncfmmrnyeiiQQPMSYDN 254
Cdd:cd16144 148 FPPGKPNPDL--------------------------------------------------------------EDGPEGEY 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 255 LTQRLTVEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDF----------AGKSQHG-VYGDAVEEMDWSVGQILNLLDE 323
Cdd:cd16144 166 LTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELiekyekkkkgLRKGQKNpVYAAMIESLDESVGRILDALEE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 324 LRLANDTLIYFTSDQGAHveevsSKGEIHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVA 403
Cdd:cd16144 246 LGLADNTLVIFTSDNGGL-----STRGGPPTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 404 KLAGAPLPEDRIIDGRDLMPLLEGKSQRSDHEFLFHYCNAYLNAvRWHPqnSTSI----WK--AFFFTPNFnpvgsngcf 477
Cdd:cd16144 321 ELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFWHFPHYHGQ-GGRP--ASAIrkgdWKliEFYEDGRV--------- 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1002913047 478 athvcfcfgsyvthhdppLLFDISKDPRERNPLTpASEPrfyEILKVMQEAADRH 532
Cdd:cd16144 389 ------------------ELYNLKNDIGETNNLA-AEMP---EKAAELKKKLDAW 421
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
22-508 |
1.97e-105 |
|
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: 322.61 E-value: 1.97e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYG-NKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASwsrtGVFLFT 100
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKG----GVLGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 101 ASSGgLPTDEITFAKLLKDQGYSTALIGKWHLGMSCHSKTDFCHH----------------PLHHGFNYFYGISLTNLrd 164
Cdd:cd16143 77 SPPL-IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYYFGIPASEV-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 165 ckpgegsvfttgfkrlvfLPlqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfrplncfmmrnye 244
Cdd:cd16143 154 ------------------LP------------------------------------------------------------ 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 245 iiqqpmsydnltqRLTVEAAQFI--QRNTETPFLLVLSYLHVHTALFSSKDFAGKSQHGVYGDAVEEMDWSVGQILNLLD 322
Cdd:cd16143 156 -------------TLTDKAVEFIdqHAKKDKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALK 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 323 ELRLANDTLIYFTSDQGAHVEEVSSKGEIHGG-SNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPT 401
Cdd:cd16143 223 ELGLAENTLVIFTSDNGPSPYADYKELEKFGHdPSGPLRGMKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFAT 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 402 VAKLAGAPLPEDRIIDGRDLMPLLEGKSQRSDHEFLFHYCNAYLNAVR---W---HPQNSTSIWKAFFFTPNFNPvgsng 475
Cdd:cd16143 303 LAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGSFAIRkgdWkliDGTGSGGFSYPRGKEKLGLP----- 377
|
490 500 510
....*....|....*....|....*....|...
gi 1002913047 476 cfathvcfcfgsyvthhdPPLLFDISKDPRERN 508
Cdd:cd16143 378 ------------------PGQLYNLSTDPGESN 392
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
21-545 |
1.65e-101 |
|
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: 315.18 E-value: 1.65e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 21 RPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFT 100
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 101 ASS--GGLPTDEITFAKLLKDQGYSTALIGKWHLGmscHSKTdfcHHPLHHGFNYFYGISltnlrDCKpgEGSVFTTGFK 178
Cdd:cd16157 81 PQNivGGIPDSEILLPELLKKAGYRNKIVGKWHLG---HRPQ---YHPLKHGFDEWFGAP-----NCH--FGPYDNKAYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 179 RL-VFLPLQIVGvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfrplncfmmRNYE--IIQQPMSYDNL 255
Cdd:cd16157 148 NIpVYRDWEMIG---------------------------------------------------RYYEefKIDKKTGESNL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 256 TQRLTVEAAQFI--QRNTETPFLLVLSYLHVHTALFSSKDFAGKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIY 333
Cdd:cd16157 177 TQIYLQEALEFIekQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVF 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 334 FTSDQGAhveeVSSKGEIHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPED 413
Cdd:cd16157 257 FSSDNGA----ALISAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSD 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 414 RIIDGRDLMPLLegKSQRSDHEFLFHYCNAYLNAVRWhpqnstSIWKAFFFTPNfnpvGSNGCFATHVCFCFGSYVT--- 490
Cdd:cd16157 333 RAIDGIDLLPVL--LNGKEKDRPIFYYRGDELMAVRL------GQYKAHFWTWS----NSWEEFRKGINFCPGQNVPgvt 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002913047 491 ------HHDPPLLFDISKDPRERNPLTPASePRFYEILKVMQEAADRHTQTLPEVPDQFSW 545
Cdd:cd16157 401 thnqtdHTKLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLNV 460
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
22-511 |
4.00e-100 |
|
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: 308.31 E-value: 4.00e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIR---TPNIDRLASGGVKLTQHLAaSPLCTPSRAAFMTGRYPVRSGMASWSRTGvfl 98
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYV-EPSCTPGRAAFITGRHPIRTGLTTVGLPG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 99 ftaSSGGLPTDEITFAKLLKDQGYSTALIGKWHLGmschSKTDfcHHPLHHGFNYFYGISLTNLRDckpgegsvfttgfk 178
Cdd:cd16142 77 ---SPGGLPPWEPTLAELLKDAGYATAQFGKWHLG----DEDG--RLPTDHGFDEFYGNLYHTIDE-------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 179 rlvflplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfrplncfmmrnyEIIQQpmsydnltqr 258
Cdd:cd16142 134 -----------------------------------------------------------------EIVDK---------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 259 ltveAAQFIQRN--TETPFLLVLSYLHVHTALFSSKDFAGKSQ-HGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFT 335
Cdd:cd16142 139 ----AIDFIKRNakADKPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFT 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 336 SDQGAHVEEVsskgeiHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPE--- 412
Cdd:cd16142 215 TDNGPEQDVW------PDGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPKdkl 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 413 ---DRIIDGRDLMPLLEGKSQRSDHEFLFHYCNAYLNAVRWHPqnstsiWKAFFFTpnFNPVGSNGcfathvcfCFGSYV 489
Cdd:cd16142 289 lgkDRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFKA--QEDTGGPT--------GEPFYV 352
|
490 500
....*....|....*....|..
gi 1002913047 490 THHdpPLLFDISKDPRERNPLT 511
Cdd:cd16142 353 LTF--PLIFNLRRDPKERYDVT 372
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
21-511 |
1.30e-99 |
|
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: 307.47 E-value: 1.30e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 21 RPNIILVMADDLGIGDPGCYGNKT-IRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMaswsrTGVFLF 99
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNaILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-----GHNFLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 100 TaSSGGLPTDEITFAKLLKDQGYSTALIGKWHLGmscHSKTdfcHHPLHHGFNYFYGIsltnlrdckpgegsvfttgfkr 179
Cdd:cd16161 76 T-SVGGLPLNETTLAEVLRQAGYATGMIGKWHLG---QREA---YLPNSRGFDYYFGI---------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 180 lvflplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfrplncfmmrnyeiiqqPMSYD-NLTQR 258
Cdd:cd16161 127 ---------------------------------------------------------------------PFSHDsSLADR 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 259 LTVEAAQFIQRNTET--PFLLVLSYLHVHTALFSSKDFAGKSQH-GVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFT 335
Cdd:cd16161 138 YAQFATDFIQRASAKdrPFFLYAALAHVHVPLANLPRFQSPTSGrGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFT 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 336 SDQGAHVEEVSSKGEIHGG---SNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPE 412
Cdd:cd16161 218 SDNGPWEVKCELAVGPGTGdwqGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPP 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 413 DRIIDGRDLMPLLEGKSQrSDHEFLFHYCNAY-----LNAVRWHPqnstsiWKAFFFTPNFNPVGSNGCFAthvcfcfgs 487
Cdd:cd16161 298 GRIYDGKDLSPVLFGGSK-TGHRCLFHPNSGAagagaLSAVRCGD------YKAHYATGGALACCGSTGPK--------- 361
|
490 500
....*....|....*....|....
gi 1002913047 488 yvTHHDPPLLFDISKDPRERNPLT 511
Cdd:cd16161 362 --LYHDPPLLFDLEVDPAESFPLT 383
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
22-508 |
3.07e-93 |
|
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: 291.81 E-value: 3.07e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLfta 101
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 ssgGLPTDEITFAKLLKDQGYSTALIGKWHLGMSCHSKtdfchHPLHHGFNYFYGIslTNLRDCkpgegsvfttgfkrlv 181
Cdd:cd16145 78 ---PLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPG-----HPTKQGFDYFYGY--LDQVHA---------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 182 flplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflHYFRPLncFMMRNYEIIQQPMSYDNL------ 255
Cdd:cd16145 132 ------------------------------------------------HNYYPE--YLWRNGEKVPLPNNVIPPldegnn 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 256 ---------TQRLTVEAAQFIQRNTETPFLLVLSYLHVHTALF---SSKDFAGKSQHGVYGDA------------VEEMD 311
Cdd:cd16145 162 agggggtysHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQvpdDGPYKYKPKDPGIYAYLpwpqpekayaamVTRLD 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 312 WSVGQILNLLDELRLANDTLIYFTSDQGAHVEEVSSKGEIHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDE 391
Cdd:cd16145 242 RDVGRILALLKELGIDENTLVVFTSDNGPHSEGGSEHDPDFFDSNGPLRGYKRSLYEGGIRVPFIARWPGKIPAGSVSDH 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 392 PTSNMDIFPTVAKLAGAPLPEDriIDGRDLMPLLEGKSQRSDHEFLF--HYCNAYLNAVRWHPqnstsiWKAFFFTPNFN 469
Cdd:cd16145 322 PSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLYweFYEGGGAQAVRMGG------WKAVRHGKKDG 393
|
490 500 510
....*....|....*....|....*....|....*....
gi 1002913047 470 PVgsngcfathvcfcfgsyvthhdppLLFDISKDPRERN 508
Cdd:cd16145 394 PF------------------------ELYDLSTDPGETN 408
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
22-531 |
9.56e-85 |
|
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: 269.80 E-value: 9.56e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQ-HlaASPLCTPSRAAFMTGRYPVrsgmaswsRTGVflfT 100
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfH--VSPVCAPTRAALLTGRYPF--------RTGV---W 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 101 ASSGG---LPTDEITFAKLLKDQGYSTALIGKWHLGMSchsktdFCHHPLHHGFNYFYGisltnlrdckpgegsvfttgf 177
Cdd:cd16146 68 HTILGrerMRLDETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLG--------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 178 krlvflplqivgvtlltlaalNCLGllHVplGVFFSLLFLAALILTLFlgflhyfrplncfmmRNYEIIQqpmsYDN-LT 256
Cdd:cd16146 121 ---------------------HGGG--GI--GQYPDYWGNDYFDDTYY---------------HNGKFVK----TEGyCT 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 257 QRLTVEAAQFIQRNTETPFLLVLSY------LHVHTALFssKDFAGKSQH----GVYGdAVEEMDWSVGQILNLLDELRL 326
Cdd:cd16146 157 DVFFDEAIDFIEENKDKPFFAYLATnaphgpLQVPDKYL--DPYKDMGLDdklaAFYG-MIENIDDNVGRLLAKLKELGL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 327 ANDTLIYFTSDQGahveevsSKGEIHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLA 406
Cdd:cd16146 234 EENTIVIFMSDNG-------PAGGVPKRFNAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLC 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 407 GAPLPEDRIIDGRDLMPLLEGKSQRSDHEFLF-HYCNAYLNAVRWHPqnsTSIWkafffTPNFNPVGSngcfathvcfcf 485
Cdd:cd16146 307 GVKLPEGIKLDGRSLLPLLKGESDPWPERTLFtHSGRWPPPPKKKRN---AAVR-----TGRWRLVSP------------ 366
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1002913047 486 gsyvtHHDPPLLFDISKDPRERNPLTpASEPrfyEILKVMQEAADR 531
Cdd:cd16146 367 -----KGFQPELYDIENDPGEENDVA-DEHP---EVVKRLKAAYEA 403
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
22-420 |
1.34e-83 |
|
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: 260.45 E-value: 1.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPvrsgmaswSRTGVFLFTA 101
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYP--------HRHGVRGNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 SSGGLPTDEITFAKLLKDQGYSTALIGKWHlgmschsktDfchhplhhgfnyfygisltnlrdckpgegsvfttgfkrlv 181
Cdd:cd16022 73 NGGGLPPDEPTLAELLKEAGYRTALIGKWH---------D---------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 182 flplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfrplncfmmrnyeiiqqpmsydnltqrltv 261
Cdd:cd16022 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 262 EAAQFIQRN-TETPFLLVLSYLHVHTALfsskdfagksqhgVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGA 340
Cdd:cd16022 104 EAIDFIERRdKDKPFFLYVSFNAPHPPF-------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 341 HVEEvsskgeiHGGsngiyKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDriIDGRD 420
Cdd:cd16022 171 MLGD-------HGL-----RGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEG--LDGRS 236
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
22-510 |
2.45e-76 |
|
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: 246.74 E-value: 2.45e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTqHLAASPLCTPSRAAFMTGRYPVRSGMaswsrtgVFlfta 101
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYV-------VF---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 ssGGLPTDEITFAKLLKDQGYSTALIGKWHLGMSCHSKTdfchHPLHHGFNYFYGISLTNLRDCKPGEGSVFttgfkrlv 181
Cdd:cd16151 69 --GYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGD----YPHEFGFDEYCLWQLTETGEKYSRPATPT-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 182 flPLQIVGVTLLTLAalnclgllhvplGVFFSLLFLAALIltlflgflhyfrplncfmmrnyeiiqqpmsydnltqrltv 261
Cdd:cd16151 135 --FNIRNGKLLETTE------------GDYGPDLFADFLI---------------------------------------- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 262 eaaQFIQRNTETPFLLVLSYLHVHT----------ALFSSKDFAGKSQHgvYGDAVEEMDWSVGQILNLLDELRLANDTL 331
Cdd:cd16151 161 ---DFIERNKDQPFFAYYPMVLVHDpfvptpdspdWDPDDKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTI 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 332 IYFTSDQGAHveevsskGEIHGGSNG-IYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPL 410
Cdd:cd16151 236 IIFTGDNGTH-------RPITSRTNGrEVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPL 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 411 PEDRIIDGRDLMPLLEGKSQRSDHEFLFhycnaylnavrWHPQNSTSIWKA-FFFTPNFNpvgsngcfathvcfcfgSYV 489
Cdd:cd16151 309 PEDYPLDGRSFAPQLLGKTGSPRREWIY-----------WYYRNPHKKFGSrFVRTKRYK-----------------LYA 360
|
490 500
....*....|....*....|.
gi 1002913047 490 THHdpplLFDISKDPRERNPL 510
Cdd:cd16151 361 DGR----FFDLREDPLEKNPL 377
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
22-510 |
2.48e-76 |
|
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: 247.46 E-value: 2.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAAsPLCTPSRAAFMTGRYPVRSGMASWSrtgvfLFTA 101
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGV-----ILAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 SSGGLPTDEITFAKLLKDQGYSTALIGKWHLGMSCHSKTdfchhPLHHGFNYFYGisltnlrdckpgegsvfttgfkrlv 181
Cdd:cd16029 75 EPYGLPLNETLLPQYLKELGYATHLVGKWHLGFYTWEYT-----PTNRGFDSFYG------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 182 flplqivgvtlltlaalnclgllhvplgvffsllflaaliltLFLGFLHYF-------RPLNCFMMRNYEIIQQpmSYDN 254
Cdd:cd16029 125 ------------------------------------------YYGGAEDYYthtsggaNDYGNDDLRDNEEPAW--DYNG 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 255 --LTQRLTVEAAQFIQR-NTETPFLLVLSYLHVHTALFSSKDFA----GKSQHG------VYGDAVEEMDWSVGQILNLL 321
Cdd:cd16029 161 tySTDLFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLQVPPEYAdpyeDKFAHIkdedrrTYAAMVSALDESVGNVVDAL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 322 DELRLANDTLIYFTSDQGAHVEEVsskgeiHGGSNGIYKGGKANNWEGGIRVPGILRWP-RVIQAGQKIDEPTSNMDIFP 400
Cdd:cd16029 241 KAKGMLDNTLIVFTSDNGGPTGGG------DGGSNYPLRGGKNTLWEGGVRVPAFVWSPlLPPKRGTVSDGLMHVTDWLP 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 401 TVAKLAGAPLPEDRIIDGRDLMPLLEG--KSQRSD--HEFLFHYCNAYLNAVRWHPqnstsiWKAFFFTPnfnpvgsngc 476
Cdd:cd16029 315 TLLSLAGGDPDDLPPLDGVDQWDALSGgaPSPRTEilLNIDDITRTTGGAAIRVGD------WKLIVGKP---------- 378
|
490 500 510
....*....|....*....|....*....|....
gi 1002913047 477 fathvcfcfgsyvthhdpplLFDISKDPRERNPL 510
Cdd:cd16029 379 --------------------LFNIENDPCERNDL 392
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
20-527 |
2.34e-72 |
|
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: 237.81 E-value: 2.34e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 20 SRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMaswsrtgVFLF 99
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGV-------TDNN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 100 TASsggLPTDEITFAKLLKDQGYSTALIGKWHLGmschskTDFCHHPlhHGFNYFYGIsltnlrdckPGEGsvfttgfkr 179
Cdd:cd16031 74 GPL---FDASQPTYPKLLRKAGYQTAFIGKWHLG------SGGDLPP--PGFDYWVSF---------PGQG--------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 180 lvflplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflHYFRPLNCFMmrNYEIIQQPMSYDNLTQRl 259
Cdd:cd16031 125 --------------------------------------------------SYYDPEFIEN--GKRVGQKGYVTDIITDK- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 260 tveAAQFIQRNTET-PFLLVLSYLHVHT--------------------ALFSSKDFAGKSQ---------HGVYGD---- 305
Cdd:cd16031 152 ---ALDFLKERDKDkPFCLSLSFKAPHRpftpaprhrglyedvtipepETFDDDDYAGRPEwareqrnriRGVLDGrfdt 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 306 -------------AVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGAHVeevsskGEiHGgsngiyKGGKANNWEGGIR 372
Cdd:cd16031 229 pekyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL------GE-HG------LFDKRLMYEESIR 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 373 VPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDriIDGRDLMPLLEGKSQRS-DHEFLFHYcnaylnavRWH 451
Cdd:cd16031 296 VPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEY--------YEE 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 452 PqnstsiwkAFFFTPNfnpvgsngcfathvcfCFGsYVT--------HHDPPL--LFDISKDPRERNPLtpASEPRFYEI 521
Cdd:cd16031 366 P--------NFHNVPT----------------HEG-VRTerykyiyyYGVWDEeeLYDLKKDPLELNNL--ANDPEYAEV 418
|
....*.
gi 1002913047 522 LKVMQE 527
Cdd:cd16031 419 LKELRK 424
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-510 |
4.17e-70 |
|
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: 231.30 E-value: 4.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 21 RPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTgvflft 100
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 101 assggLPTDEITFAKLLKDQGYSTALIGKWHLG----MSCHSKTDFCHHPLHHGFNYFYGisltnlrdckpgegsvfttg 176
Cdd:cd16034 75 -----LPPDAPTIADVLKDAGYRTGYIGKWHLDgperNDGRADDYTPPPERRHGFDYWKG-------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 177 fkrlvflplqivgvtlltlaaLNClgllhvplgvffsllflaaliltlflgFLHYFRPlncFMMRNYEIIQQPMSYDnlT 256
Cdd:cd16034 130 ---------------------YEC---------------------------NHDHNNP---HYYDDDGKRIYIKGYS--P 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 257 QRLTVEAAQFI--QRNTETPFLLVLSYLHVHT-------------------------ALFSSKDFAGKSQHGVYGdAVEE 309
Cdd:cd16034 157 DAETDLAIEYLenQADKDKPFALVLSWNPPHDpyttapeeyldmydpkklllrpnvpEDKKEEAGLREDLRGYYA-MITA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 310 MDWSVGQILNLLDELRLANDTLIYFTSDqgahveevsskgeiHG---GSNGIYkgGKANNWEGGIRVPGILRWPRVIQAG 386
Cdd:cd16034 236 LDDNIGRLLDALKELGLLENTIVVFTSD--------------HGdmlGSHGLM--NKQVPYEESIRVPFIIRYPGKIKAG 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 387 QKIDEPTSNMDIFPTVAKLAGAPLPEDriIDGRDLMPLLEGKSQRSDHEFLFhYCNAYLNavrWHPQNSTSIWKAfFFTP 466
Cdd:cd16034 300 RVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLL-QCFVPFG---GGSARDGGEWRG-VRTD 372
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1002913047 467 NFnpvgsngcfaTHVCFcfgsyvtHHDPPLLFDISKDPRERNPL 510
Cdd:cd16034 373 RY----------TYVRD-------KNGPWLLFDNEKDPYQLNNL 399
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
22-532 |
2.60e-64 |
|
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: 215.06 E-value: 2.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDpGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFlfta 101
Cdd:cd16027 1 PNILWIIADDLSPDL-GGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFP---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 ssggLPTDEITFAKLLKDQGYSTALIGKWhlgmschsktdfchhplHHGFNYFYgisltnlrdckpgegsvfttgfkrlv 181
Cdd:cd16027 76 ----LPDGVKTLPELLREAGYYTGLIGKT-----------------HYNPDAVF-------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 182 flplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflGFLHYFRPLNCFMMRNYEIIQqpmsydnltqrltv 261
Cdd:cd16027 109 ---------------------------------------------PFDDEMRGPDDGGRNAWDYAS-------------- 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 262 EAAQFIQR-NTETPFLLVLSYLHVHTALFSS-------------------------KDFAGksqhgvYGDAVEEMDWSVG 315
Cdd:cd16027 130 NAADFLNRaKKGQPFFLWFGFHDPHRPYPPGdgeepgydpekvkvppylpdtpevrEDLAD------YYDEIERLDQQVG 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 316 QILNLLDELRLANDTLIYFTSDQGahveevsskgeihggsnGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSN 395
Cdd:cd16027 204 EILDELEEDGLLDNTIVIFTSDHG-----------------MPFPRAKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSF 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 396 MDIFPTVAKLAGAPLPEDriIDGRDLMPLLEGKSQRSdHEFLFHYCNaylnavrWHpqnstsiwkafffTPNFNPVGS-- 473
Cdd:cd16027 267 IDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPG-RDYVFAERD-------RH-------------DETYDPIRSvr 323
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002913047 474 NGCFathvcfcfgSYVTHHDPPLLFDISKDPRERNPLtpASEPRFYEILKVMQEAADRH 532
Cdd:cd16027 324 TGRY---------KYIRNYMPEELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAW 371
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
22-408 |
1.99e-63 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 210.36 E-value: 1.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRtgvflfta 101
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 ssGGLPTDEITFAKLLKDQGYSTALIGKWHLGMscHSKTDFCHHplhhGFNYFYGisltnlrdckpgegsvfttgfkrlv 181
Cdd:pfam00884 73 --VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGW--YNNQSPCNL----GFDKFFG------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 182 flplqivGVTLLTLAALNclgllhvplgvffsllflaaliltlflgflhYFRPLNCFMMRNYeiiqqpmsydnlTQRLTV 261
Cdd:pfam00884 120 -------RNTGSDLYADP-------------------------------PDVPYNCSGGGVS------------DEALLD 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 262 EAAQFIQRNTEtPFLLVLSYLHVHTALFSSKDFAGK------------SQHGVYGDAVEEMDWSVGQILNLLDELRLAND 329
Cdd:pfam00884 150 EALEFLDNNDK-PFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscseeQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDN 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 330 TLIYFTSDQGAHVEEvsskgeihggSNGIYKGGK-ANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGA 408
Cdd:pfam00884 229 TLVVYTSDHGESLGE----------GGGYLHGGKyDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
21-510 |
4.21e-61 |
|
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: 207.30 E-value: 4.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 21 RPNIILVMADDLGIGDPGCYGNKtIRTPNIDRLASGGVKLTQ-HlaASPLCTPSRAAFMTGRYPVRSGMA--SWSRTGvf 97
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGMGtmAELATG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 98 lFTASSGGLPTDEITFAKLLKDQGYSTALIGKWHLGMSchsktdfchhplhhgfNYFYGISLTN-----LRDCKPGEgsv 172
Cdd:cd16025 77 -KPGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------------DYYSTDDLTDkaieyIDEQKAPD--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 173 fttgfKrlvflPlqivgvtlltlaalnclgllhvplgvFFslLFLAaliltlfLGFLHYfrPLncfmmrnyeiiQQP--- 249
Cdd:cd16025 137 -----K-----P--------------------------FF--LYLA-------FGAPHA--PL-----------QAPkew 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 250 ---------MSYDNL-TQRLtveAAQ----FIQRNTEtpfllvlsyLHVHTALFSS---------KDFAGKSQhgVYGDA 306
Cdd:cd16025 159 idkykgkydAGWDALrEERL---ERQkelgLIPADTK---------LTPRPPGVPAwdslspeekKLEARRME--VYAAM 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 307 VEEMDWSVGQILNLLDELRLANDTLIYFTSDQG-------AHVeevsskgeihggSNGIYKGGKANNWEGGIRVPGILRW 379
Cdd:cd16025 225 VEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGasaepgwANA------------SNTPFRLYKQASHEGGIRTPLIVSW 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 380 PRVIQAGQKI-DEPTSNMDIFPTVAKLAGAPLPEDR------IIDGRDLMPLLEGKSQRSDHEFLF--HYCNAYLnavrW 450
Cdd:cd16025 293 PKGIKAKGGIrHQFAHVIDIAPTILELAGVEYPKTVngvpqlPLDGVSLLPTLDGAAAPSRRRTQYfeLFGNRAI----R 368
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002913047 451 HPQnstsiWKAffftpnfnpvgsngcfathvcfcfgsyVTHHDPPL------LFDISKDPRERNPL 510
Cdd:cd16025 369 KGG-----WKA---------------------------VALHPPPGwgdqweLYDLAKDPSETHDL 402
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
432-567 |
6.81e-56 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 184.05 E-value: 6.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 432 SDHEFLFHYCNAYLNAVRWHPqnstsiWKAFFFTPNFNPVGSNGCFATHVCfcfgsyVTHHDPPLLFDISKDPRERNPLT 511
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002913047 512 PASePRFYEILKVMQEAADRHTQTLPEVPDQFSWNNFLWKPWLQLCCPSTGLsCQC 567
Cdd:pfam14707 69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPA-CTC 122
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
22-423 |
3.60e-53 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 181.67 E-value: 3.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFTA 101
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 SSGGLPTDEITFAKLLKDQGYSTALIGKWHLGmschsktdfchhplhhgfnyfygisltnlrdckpgegsvfttgfkrlv 181
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 182 flplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfrplncfmmrnyeiiqqpmsydnltqrltV 261
Cdd:cd16149 113 -------------------------------------------------------------------------------D 113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 262 EAAQFIQRN--TETPFLLVLSYLHVHtalfsskdfagkSQHGvYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQG 339
Cdd:cd16149 114 DAADFLRRRaeAEKPFFLSVNYTAPH------------SPWG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNG 180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 340 AHVeevsskgeihgGSNGIYKGGKA----NNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRI 415
Cdd:cd16149 181 FNM-----------GHHGIWGKGNGtfplNMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPR 249
|
....*...
gi 1002913047 416 IDGRDLMP 423
Cdd:cd16149 250 LPGRSFAD 257
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
22-504 |
7.17e-50 |
|
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: 175.04 E-value: 7.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPvrsgmaswSRTGVFlftA 101
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYV--------HETGVW---D 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 SSGGLPTDEITFAKLLKDQGYSTALIGKWHLgmscHSKTDfchhplHHGFNYfygisltnlrdckpgegsvfttgfkrlv 181
Cdd:cd16037 70 NADPYDGDVPSWGHALRAAGYETVLIGKLHF----RGEDQ------RHGFRY---------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 182 flplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfrplncfmmrnyeiiqqpmsydnlTQRLTV 261
Cdd:cd16037 112 --------------------------------------------------------------------------DRDVTE 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 262 EAAQFIQRN--TETPFLLVLSYLHVHTALFSSKDFAGKSQHGV---YGDAVEEMDWSVGQILNLLDELRLANDTLIYFTS 336
Cdd:cd16037 118 AAVDWLREEaaDDKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTS 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 337 DQGAHVeevsskgeihgGSNGIYkgGKANNWEGGIRVPGILRWPRvIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRii 416
Cdd:cd16037 198 DHGDML-----------GERGLW--GKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL-- 261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 417 DGRDLMPLLEGKSQRSD---HEFLFHYCNAYLNAVRWHPqnstsiWKaffftpnfnpvgsngcfathvcfcfgsYVTHH- 492
Cdd:cd16037 262 DGRSLLPLAEGPDDPDRvvfSEYHAHGSPSGAFMLRKGR------WK---------------------------YIYYVg 308
|
490
....*....|..
gi 1002913047 493 DPPLLFDISKDP 504
Cdd:cd16037 309 YPPQLFDLENDP 320
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
20-434 |
7.92e-48 |
|
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: 172.76 E-value: 7.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 20 SRPNIILVMADDLgigDP--GCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPvrsgmaswSRTGVF 97
Cdd:cd16030 1 KKPNVLFIAVDDL---RPwlGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRP--------DTTGVY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 98 LF-TASSGGLPtDEITFAKLLKDQGYSTALIGKWHlgmschsktdfcHHPLHHGFNYFYGIS--LTNLRDCKPGEGSVFT 174
Cdd:cd16030 70 DNnSYFRKVAP-DAVTLPQYFKENGYTTAGVGKIF------------HPGIPDGDDDPASWDepPNPPGPEKYPPGKLCP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 175 TGFKRLVFLPLQIVGVT----------LLTLAALNCLGLLHVPLGVFFsllflaaliltLFLGFL--H--------YF-- 232
Cdd:cd16030 137 GKKGGKGGGGGPAWEAAdvpdeaypdgKVADEAIEQLRKLKDSDKPFF-----------LAVGFYkpHlpfvapkkYFdl 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 233 RPLNCFMMRN-YEIIQQPM-SYDNLTQRltVEAAQFIQRNTETPFLLVlsylhvhtalfsSKDFAGKSQHGVYGdAVEEM 310
Cdd:cd16030 206 YPLESIPLPNpFDPIDLPEvAWNDLDDL--PKYGDIPALNPGDPKGPL------------PDEQARELRQAYYA-SVSYV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 311 DWSVGQILNLLDELRLANDTLIYFTSDQGAHVEEvssKGEIhggsngiykgGKANNWEGGIRVPGILRWPRVIQAGQKID 390
Cdd:cd16030 271 DAQVGRVLDALEELGLADNTIVVLWSDHGWHLGE---HGHW----------GKHTLFEEATRVPLIIRAPGVTKPGKVTD 337
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1002913047 391 EPTSNMDIFPTVAKLAGAPLPEDriIDGRDLMPLLEGKSQRSDH 434
Cdd:cd16030 338 ALVELVDIYPTLAELAGLPAPPC--LEGKSLVPLLKNPSAKWKD 379
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
22-427 |
1.92e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 170.86 E-value: 1.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMasWSRTGVFLftA 101
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGV--LNNVENAG--A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 SSGGLPTDEITFAKLLKDQGYSTALIGKWHLGMScHSKTDFC---HHPLHHGFNYFYgISLTN--LRDCKPGEGSVFT-T 175
Cdd:cd16033 77 YSRGLPPGVETFSEDLREAGYRNGYVGKWHVGPE-ETPLDYGfdeYLPVETTIEYFL-ADRAIemLEELAADDKPFFLrV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 176 GFkrlvFLPlqivgvtlltlaalnclgllHVPlgvffsllflaaliltlflgflhYFRPLNCFMMRNYEIIQQPMSYDNl 255
Cdd:cd16033 155 NF----WGP--------------------HDP-----------------------YIPPEPYLDMYDPEDIPLPESFAD- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 256 tqrlTVEAAQFIQRNTETPFLLVlsylhvhtaLFSSKDFAGKSQHgvYGDAVEEMDWSVGQILNLLDELRLANDTLIYFT 335
Cdd:cd16033 187 ----DFEDKPYIYRRERKRWGVD---------TEDEEDWKEIIAH--YWGYITLIDDAIGRILDALEELGLADDTLVIFT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 336 SDqgaHveevsskGEIHGGSNGIYKGgkANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDri 415
Cdd:cd16033 252 SD---H-------GDALGAHRLWDKG--PFMYEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK-- 317
|
410
....*....|..
gi 1002913047 416 IDGRDLMPLLEG 427
Cdd:cd16033 318 VDGRSLLPLLRG 329
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
22-406 |
1.30e-46 |
|
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: 163.75 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVkLTQHLAASPLC--TPSRAAFMTGRYPVRSGMASWSRTGVFLf 99
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGA-TFNFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPEL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 100 TASSGGLPTDEITFAKLLKDQGYSTALIGkwhlgmschsktdfchhplhhgfnyfygisltnlrdckpgegsvfttgfkr 179
Cdd:cd00016 79 PSRAAGKDEDGPTIPELLKQAGYRTGVIG--------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 180 lvflplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfrplncfmmrnyeiiqqpmsydnltqrl 259
Cdd:cd00016 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 260 tveAAQFIQRNT-ETPFLLVLSYLHVHTALFSSKdfagkSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQ 338
Cdd:cd00016 108 ---LLKAIDETSkEKPFVLFLHFDGPDGPGHAYG-----PNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADH 179
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002913047 339 GAHVEEVSSKGEihggsngiyKGGKANNWEGGIRVPGILRWPRViQAGQKIDEPTSNMDIFPTVAKLA 406
Cdd:cd00016 180 GGIDKGHGGDPK---------ADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
22-504 |
1.48e-46 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 166.21 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPvrsgmaswSRTGVFlFTA 101
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLP--------SRIGAY-DNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 SSggLPTDEITFAKLLKDQGYSTALIGKWHlgmschsktdFCHHPLHHGFnyfygisltnlrdckpgegsvfttgfkrlv 181
Cdd:cd16032 72 AE--FPADIPTFAHYLRAAGYRTALSGKMH----------FVGPDQLHGF------------------------------ 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 182 flplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfrplncfmmrnyeiiqqpmSYDNLTqrlTV 261
Cdd:cd16032 110 ---------------------------------------------------------------------DYDEEV---AF 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 262 EAAQFI----QRNTETPFLLVLSYLHVHTALFSSKDF----AGKSQHGVYGdAVEEMDWSVGQILNLLDELRLANDTLIY 333
Cdd:cd16032 118 KAVQKLydlaRGEDGRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVI 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 334 FTSDqgahveevsskgeiHG---GSNGIYKggKANNWEGGIRVPGILRWPRvIQAGQKIDEPTSNMDIFPTVAKLAGAPL 410
Cdd:cd16032 197 FTSD--------------HGdmlGERGLWY--KMSFFEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGT 259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 411 PEDRI-IDGRDLMPLLEGKSQRSDHEFLFHYCnaylnavrwhpqnstsiwkaffftpnfnpvgSNGCFATHVCFCFGSY- 488
Cdd:cd16032 260 APHVPpLDGRSLLPLLEGGDSGGEDEVISEYL-------------------------------AEGAVAPCVMIRRGRWk 308
|
490
....*....|....*...
gi 1002913047 489 --VTHHDPPLLFDISKDP 504
Cdd:cd16032 309 fiYCPGDPDQLFDLEADP 326
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
20-527 |
2.14e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 153.49 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 20 SRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQ-HLAAS---PLCTPSRAAFMTGRYpvrsgmaswsrtg 95
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNMGGwsgAVCVPSRAMLMTGRT------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 96 vfLFTASSGG---LPTDEITFAKLLKDQGYSTALIGKWHLGMsCHSKTDFCHHPLHHGfnyfygisltnlrdcKPgegsv 172
Cdd:cd16155 68 --LFHAPEGGkaaIPSDDKTWPETFKKAGYRTFATGKWHNGF-ADAAIEFLEEYKDGD---------------KP----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 173 fttgfkrlvflplqivgvtlltlaalnclgllhvplgvFFsllflaaliltLFLGFLHYFRPLncfmmrnyeiiQQPMSY 252
Cdd:cd16155 125 --------------------------------------FF-----------MYVAFTAPHDPR-----------QAPPEY 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 253 DNL--TQRLTVEAaqfiqrntetpfllvlSYLHVHT---ALFSSKDFAG----------KSQHGVYGDAVEEMDWSVGQI 317
Cdd:cd16155 145 LDMypPETIPLPE----------------NFLPQHPfdnGEGTVRDEQLapfprtpeavRQHLAEYYAMITHLDAQIGRI 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 318 LNLLDELRLANDTLIYFTSDQGAHVeevsskgeihgGSNGIYkgGKANNWEGGIRVPGILRWPRvIQAGQKIDEPTSNMD 397
Cdd:cd16155 209 LDALEASGELDNTIIVFTSDHGLAV-----------GSHGLM--GKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQD 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 398 IFPTVAKLAGAPLPEDriIDGRDLMPLLEGKSQRSdHEFLFHycnAYLN---AVRwhpqnsTSIWKAFFFTPnfnpvgsn 474
Cdd:cd16155 275 VFPTLCELAGIEIPES--VEGKSLLPVIRGEKKAV-RDTLYG---AYRDgqrAIR------DDRWKLIIYVP-------- 334
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1002913047 475 gcfathvcfcfGSYVThhdppLLFDISKDPRERNPLtpASEPRFYEILKVMQE 527
Cdd:cd16155 335 -----------GVKRT-----QLFDLKKDPDELNNL--ADEPEYQERLKKLLA 369
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
22-423 |
1.63e-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: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVM-----ADDLGigdpgCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPvrsgmaswsrtgv 96
Cdd:cd16148 1 MNVILIVidslrADHLG-----CYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 97 FLFTASSGGLPTDEITFAKLLKDQGYSTALIgkwhlgmschskTDFCHHPLHHGFNyfygisltnlrdckpgegsvftTG 176
Cdd:cd16148 63 FYHGVWGGPLEPDDPTLAEILRKAGYYTAAV------------SSNPHLFGGPGFD----------------------RG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 177 FKRLVFLPLQivgvtlltlaalnclgllhvplgvffsllflaalilTLFLGFLHYFRplncfmmrnyeiiqqpmsydnlT 256
Cdd:cd16148 109 FDTFEDFRGQ------------------------------------EGDPGEEGDER----------------------A 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 257 QRLTVEAAQFIQRN-TETPFLLVLSYLHVHTalfsskDFAgksqhgvYGDAVEEMDWSVGQILNLLDELRLANDTLIYFT 335
Cdd:cd16148 131 ERVTDRALEWLDRNaDDDPFFLFLHYFDPHE------PYL-------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVT 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 336 SDQGahvEEVsskGEihggsNGIYKGGKANNWEGGIRVPGILRWPRViQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDri 415
Cdd:cd16148 198 SDHG---EEF---GE-----HGLYWGHGSNLYDEQLHVPLIIRWPGK-EPGKRVDALVSHIDIAPTLLDLLGVEPPDY-- 263
|
....*...
gi 1002913047 416 IDGRDLMP 423
Cdd:cd16148 264 SDGRSLLP 271
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-527 |
2.81e-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: 293771 [Multi-domain] Cd Length: 373 Bit Score: 147.76 E-value: 2.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 21 RPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPvrsgmaswSRTGVFlft 100
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYP--------TETGCF--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 101 ASSGGLPTDEITFAKLLKDQGYSTALIGKWHLGmschsktdfchhplhhgfnyfygisltnlrdckpgegsvfttGFKrl 180
Cdd:cd16152 70 RNGIPLPADEKTLAHYFRDAGYETGYVGKWHLA------------------------------------------GYR-- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 181 vflplqivgVTLLTLAALNclgllhvplgvffsllflaaliltlflgFLHyfrplncfmmrnyeiiqqpmsydnltqrlt 260
Cdd:cd16152 106 ---------VDALTDFAID----------------------------YLD------------------------------ 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 261 veaaqfiQRNTETPFLLVLSYLHVH---------TALFSSKDFAGKS-------------QH--GVYGdAVEEMDWSVGQ 316
Cdd:cd16152 119 -------NRQKDKPFFLFLSYLEPHhqndrdryvAPEGSAERFANFWvppdlaalpgdwaEElpDYLG-CCERLDENVGR 190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 317 ILNLLDELRLANDTLIYFTSDQGAHVEEvsskgeihggSNGIYkggKANNWEGGIRVPGILRWPRvIQAGQKIDEPTSNM 396
Cdd:cd16152 191 IRDALKELGLYDNTIIVFTSDHGCHFRT----------RNAEY---KRSCHESSIRVPLVIYGPG-FNGGGRVEELVSLI 256
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 397 DIFPTVAKLAGAPLPEDriIDGRDLMPLLEGKSQRSDHEFLFHYCNAYL-NAVRwhpqnsTSIWKAFFFTPNFNPVGSNG 475
Cdd:cd16152 257 DLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNEVFIQISESQVgRAIR------TDRWKYSVAAPDKDGWKDSG 328
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1002913047 476 CfathvcfcfGSYVTHHdpplLFDISKDPRERNPLtpASEPRFYEILKVMQE 527
Cdd:cd16152 329 S---------DVYVEDY----LYDLEADPYELVNL--IGRPEYREVAAELRE 365
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
18-532 |
6.30e-39 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 149.05 E-value: 6.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 18 AASRPNIILVMADDLGiGDP-GCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGV 96
Cdd:PRK13759 3 QTKKPNIILIMVDQMR-GDClGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 97 FLFTassgglptdeITFAKLLKDQGYSTALIGKWHLGMScHSKTDFCHHPLHHGFnyfygisltnLRDCKPGEGSVFTTG 176
Cdd:PRK13759 82 WNYK----------NTLPQEFRDAGYYTQCIGKMHVFPQ-RNLLGFHNVLLHDGY----------LHSGRNEDKSQFDFV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 177 FKRLVFLPLQIVGVTL-LTLAALNClgllhvplgvffsllflaaliltlflgflhyfrplNCFMMRNYEiiqqpmsydnL 255
Cdd:PRK13759 141 SDYLAWLREKAPGKDPdLTDIGWDC-----------------------------------NSWVARPWD----------L 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 256 TQRL-----TV-EAAQFIQRNTET-PFLLVLSYLHVH---------------------------------------TALF 289
Cdd:PRK13759 176 EERLhptnwVGsESIEFLRRRDPTkPFFLKMSFARPHspydppkryfdmykdadipdphigdweyaedqdpeggsiDALR 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 290 S--SKDFAGKSQHGVYGDaVEEMDWSVGQILNLLDELRLANDTLIYFTSDqgahveevsskgeiHG---GSNGIYKggKA 364
Cdd:PRK13759 256 GnlGEEYARRARAAYYGL-ITHIDHQIGRFLQALKEFGLLDNTIILFVSD--------------HGdmlGDHYLFR--KG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 365 NNWEGGIRVPGILRWP---RVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDriIDGRDLMPLLEGKsqrsdheflfhyc 441
Cdd:PRK13759 319 YPYEGSAHIPFIIYDPgglLAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQ------------- 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 442 naylnavrwhpqnsTSIWKAFFFTPNFNPVGSNGCFAT-HVCFCFGSYVTHHDpplLFDISKDPRERNPLTPAsePRFYE 520
Cdd:PRK13759 384 --------------YEGWRPYLHGEHALGYSSDNYLTDgKWKYIWFSQTGEEQ---LFDLKKDPHELHNLSPS--EKYQP 444
|
570
....*....|..
gi 1002913047 521 ILKVMQEAADRH 532
Cdd:PRK13759 445 RLREMRKKLVDH 456
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
22-427 |
3.13e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 137.37 E-value: 3.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGmaswSRTGVFLfta 101
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG----HRTLHHL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 ssggLPTDEITFAKLLKDQGYSTALIGKWHLGMSCHSKTDFCHHP---LHHGFNYfygisLTNLRDCKPgegsvFttgfk 178
Cdd:cd16150 74 ----LRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYCDSDeacVRTAIDW-----LRNRRPDKP-----F----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 179 rLVFLPLQivgvtlltlaalnclgLLHVPLGV---FFSLLFLAALILTLFLGFLHYFRPLncfMMRNYEiiqqpmsYDNL 255
Cdd:cd16150 135 -CLYLPLI----------------FPHPPYGVeepWFSMIDREKLPPRRPPGLRAKGKPS---MLEGIE-------KQGL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 256 tQRLTVEAAQFIQrntetpfllvlsylhvhtalfsskdfagksqhGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFT 335
Cdd:cd16150 188 -DRWSEERWRELR--------------------------------ATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFF 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 336 SDqgahveevsskgeiHGGSNGIYkgGKANNWEGGI-----RVPGILRWPRVIqAGQKIDEPTSNMDIFPTVAKLAGAPL 410
Cdd:cd16150 235 SD--------------HGDYTGDY--GLVEKWPNTFedcltRVPLIIKPPGGP-AGGVSDALVELVDIPPTLLDLAGIPL 297
|
410
....*....|....*..
gi 1002913047 411 PEDRIidGRDLMPLLEG 427
Cdd:cd16150 298 SHTHF--GRSLLPVLAG 312
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
22-532 |
3.59e-35 |
|
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: 137.78 E-value: 3.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYpVRSGMASWSRTgvflfta 101
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRY-LMNHRSVWNGT------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 ssgGLPTDEITFAKLLKDQGYSTALIGKWHLgmschSKTDFCHHPLHhgfnyfygISLTNLRDCKPGegsvFTTGFkRLV 181
Cdd:cd16028 73 ---PLDARHLTLALELRKAGYDPALFGYTDT-----SPDPRGLAPLD--------PRLLSYELAMPG----FDPVD-RLD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 182 FLPLQIVGVTLLTLAALNCLGllHVPLGVFFsllflaaliltLFLGFLH----YFRPLNCFMMRNYEIIQQPMSYDNLTQ 257
Cdd:cd16028 132 EYPAEDSDTAFLTDRAIEYLD--ERQDEPWF-----------LHLSYIRphppFVAPAPYHALYDPADVPPPIRAESLAA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 258 rltvEAAQ------FIQRNTETPFllvlsylHVHTALFSSKDFAGKSQH-GVYGDAVEEMDWSVGQILNLLDELRLANDT 330
Cdd:cd16028 199 ----EAAQhpllaaFLERIESLSF-------SPGAANAADLDDEEVAQMrATYLGLIAEVDDHLGRLFDYLKETGQWDDT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 331 LIYFTSDQGAHVeevsskGEIH-GGSNGIYkggkannwEGGIRVPGILRWPRV---IQAGQKIDEPTSNMDIFPTVAKLA 406
Cdd:cd16028 268 LIVFTSDHGEQL------GDHWlWGKDGFF--------DQAYRVPLIVRDPRReadATRGQVVDAFTESVDVMPTILDWL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 407 GAPLPedRIIDGRDLMPLLEGkSQRSDHEFLFHYCNAYLNAVRWHPQNSTSIwkaffftpnfnpvGSNGCFATHVCFCFG 486
Cdd:cd16028 334 GGEIP--HQCDGRSLLPLLAG-AQPSDWRDAVHYEYDFRDVSTRRPQEALGL-------------SPDECSLAVIRDERW 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1002913047 487 SYVtHHD--PPLLFDISKDPRERNPLtpASEPRFYEILKVMQEAADRH 532
Cdd:cd16028 398 KYV-HFAalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKLLSW 442
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
22-437 |
3.00e-33 |
|
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: 132.51 E-value: 3.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMasWsrtgvflftA 101
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS--W---------T 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 SSGGLPTDEITFAKLLKDQGYSTALIGKWHLgmschsktdfchhplhHGFNYF-YGIsltnlrdCKPGEGSvfttgfkrl 180
Cdd:cd16156 70 NCMALGDNVKTIGQRLSDNGIHTAYIGKWHL----------------DGGDYFgNGI-------CPQGWDP--------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 181 vflplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflHYFrplncFMMRNY-------EII-----QQ 248
Cdd:cd16156 118 -------------------------------------------------DYW-----YDMRNYldelteeERRksrrgLT 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 249 PMSYDNLTQ------RLTVEAAQFIQRNTETPFLLVLSYLHVH-----TALFSS--KDF--------------------- 294
Cdd:cd16156 144 SLEAEGIKEeftyghRCTNRALDFIEKHKDEDFFLVVSYDEPHhpflcPKPYASmyKDFefpkgenayddlenkplhqrl 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 295 -AGKSQHGVYGDAVEEM----------DWSVGQILNLLDElrLANDTLIYFTSDqgahveevsskgeiHG---GSNGIYK 360
Cdd:cd16156 224 wAGAKPHEDGDKGTIKHplyfgcnsfvDYEIGRVLDAADE--IAEDAWVIYTSD--------------HGdmlGAHKLWA 287
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002913047 361 GGKAnNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEdrIIDGRDLMPLLEGKSQRSDHEFL 437
Cdd:cd16156 288 KGPA-VYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPK--VLEGESILATIEDPEIPENRGVF 361
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-421 |
8.23e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 127.11 E-value: 8.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 21 RPNIILVMADDLGIGDPGCYGNKT----------IRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPvrsgmas 90
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNAHtgksesrlgyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 91 wSRTGVFLFTASSGGLPTDEITFAKLLKDQGYSTALIGKWHLGmschsktdfchhplhhgfnyfygisltnlrdckpgeg 170
Cdd:cd16153 74 -HRTGVYGFEAAHPALDHGLPTFPEVLKKAGYQTASFGKSHLE------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 171 svfttgfkrlvflplqivgvtlltlAALNCLGllhvplgvffsllflaaliltlflgflhyfRPLNCFMMRNYEIIQQPm 250
Cdd:cd16153 116 -------------------------AFQRYLK------------------------------NANQSYKSFWGKIAKGA- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 251 sydnltqrltveaaqfiqrNTETPFLLVLSYLHVHTALFSSKDFAGK-SQHG--VYGDAVeemdwsVGQILNLLDELRLA 327
Cdd:cd16153 140 -------------------DSDKPFFVRLSFLQPHTPVLPPKEFRDRfDYYAfcAYGDAQ------VGRAVEAFKAYSLK 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 328 ND---TLIYFTSDQGAHVeevsskgeihgGSNGIYkgGKANNWEGGIRVPGILRWPRVIQ--AGQKIDEPTSNMDIFPTV 402
Cdd:cd16153 195 QDrdyTIVYVTGDHGWHL-----------GEQGIL--AKFTFWPQSHRVPLIVVSSDKLKapAGKVRHDFVEFVDLAPTL 261
|
410
....*....|....*....
gi 1002913047 403 AKLAGAPLPEDRIIDGRDL 421
Cdd:cd16153 262 LAAAGVDVDAPDYLDGRDL 280
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
21-419 |
3.89e-32 |
|
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: 128.05 E-value: 3.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 21 RPNIILVMADDLGIGDPG-CYGNKTIRtpnidRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPvrsgmaswSRTGVFLF 99
Cdd:cd16147 1 RPNIVLILTDDQDVELGSmDPMPKTKK-----LLADQGTTFTNAFVTTPLCCPSRASILTGQYA--------HNHGVTNN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 100 TASSGGLPT------DEITFAKLLKDQGYSTALIGKWhlgMSCHSKTDFCHH-PLhhGFNYFYGisltnlrdckpgegsv 172
Cdd:cd16147 68 SPPGGGYPKfwqnglERSTLPVWLQEAGYRTAYAGKY---LNGYGVPGGVSYvPP--GWDEWDG---------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 173 fttgfkrlvflplqivgvtlltlaalnclgllhvplgvffsllflaaliltlfLGFLHYFRPLNCFMMRNyeiIQQPMSY 252
Cdd:cd16147 127 -----------------------------------------------------LVGNSTYYNYTLSNGGN---GKHGVSY 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 253 DN--LTQRLTVEAAQFIQRNTET--PFLLVLSYLHVHT----ALFSSKDFAGKSQ---------------HGV------- 302
Cdd:cd16147 151 PGdyLTDVIANKALDFLRRAAADdkPFFLVVAPPAPHGpftpAPRYANLFPNVTApprpppnnpdvsdkpHWLrrlppln 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 303 -----YGD-----------AVEEMdwsVGQILNLLDELRLANDTLIYFTSDQGAHVeevsskGEiHGgsngiYKGGKANN 366
Cdd:cd16147 231 ptqiaYIDelyrkrlrtlqSVDDL---VERLVNTLEATGQLDNTYIIYTSDNGYHL------GQ-HR-----LPPGKRTP 295
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1002913047 367 WEGGIRVPGILRWPRvIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDriIDGR 419
Cdd:cd16147 296 YEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDGR 345
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
22-440 |
6.33e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 119.62 E-value: 6.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPvrsgmaswSRTGVFLfTA 101
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHP--------QQTGVTD-TL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 102 SSG---GLPTDEITFAKLLKDQGYSTALIGKWHLGmschsktdfchhplhhgfNYFYGisltnlrdckpgegsvfttGFK 178
Cdd:cd16035 72 GSPmqpLLSPDVPTLGHMLRAAGYYTAYKGKWHLS------------------GAAGG-------------------GYK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 179 RlvflplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfrplncfmmrnyeiiqqpmsydnlTQR 258
Cdd:cd16035 115 R----------------------------------------------------------------------------DPG 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 259 LTVEAAQFIQR-----NTETPFLLVLSYLHVHTALFSSKDfAGKSQHGV--YGDAVEEMDWSVGQILNLLDELRLANDTL 331
Cdd:cd16035 119 IAAQAVEWLRErgaknADGKPWFLVVSLVNPHDIMFPPDD-EERWRRFRnfYYNLIRDVDRQIGRVLDALDASGLADNTI 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 332 IYFTSDqgaHveevsskGEI---HGGSngiykgGKANN-WEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAG 407
Cdd:cd16035 198 VVFTSD---H-------GEMggaHGLR------GKGFNaYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAG 261
|
410 420 430
....*....|....*....|....*....|....*...
gi 1002913047 408 APLPEDRIID----GRDLMPLLEGKSQRSDHE-FLFHY 440
Cdd:cd16035 262 VDAEARATEApplpGRDLSPLLTDADADAVRDgILFTY 299
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
22-430 |
2.25e-26 |
|
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: 110.90 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLGIGDPGCY--GNKTIRTPNIDRLASGGVKLTqHLAASPLCTPSRAAFMTGRYPVrsgmaswsRTGVflf 99
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYslSSDLPVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGF--------RTGV--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 100 TASSGGLPT-DEITFAKLLKDQ---GYSTALIGKWHLGmschskTDFCHHPLHHGFNYFYGISLTNLRDckpgegsvftt 175
Cdd:cd16154 69 LAVPDELLLsEETLLQLLIKDAttaGYSSAVIGKWHLG------GNDNSPNNPGGIPYYAGILGGGVQD----------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 176 gfkrlvflplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhYFR-PLNcfmmrNYEIIQQPMSYdn 254
Cdd:cd16154 132 -------------------------------------------------------YYNwNLT-----NNGQTTNSTEY-- 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 255 LTQRLTVEAAQFIQRNTeTPFLLVLSYLHVHT-------ALFSSKDFAGKSQHGV-----YGDAVEEMDWSVGQILNLLD 322
Cdd:cd16154 150 ATTKLTNLAIDWIDQQT-KPWFLWLAYNAPHTpfhlppaELHSRSLLGDSADIEAnprpyYLAAIEAMDTEIGRLLASID 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 323 ELRLANdTLIYFTSDQGAHVEEVSSKGEIHGGSNGIYkggkannwEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTV 402
Cdd:cd16154 229 EEEREN-TIIIFIGDNGTPGQVVDLPYTRNHAKGSLY--------EGGINVPLIVSGAGVERANERESALVNATDLYATI 299
|
410 420
....*....|....*....|....*...
gi 1002913047 403 AKLAGAPLPEdrIIDGRDLMPLLEGKSQ 430
Cdd:cd16154 300 AELAGVDAAE--IHDSVSFKPLLSDVNA 325
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
22-504 |
1.27e-19 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 90.68 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADDLG---IGDPGcygNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSgmASWSrtgvfl 98
Cdd:cd16171 1 PNVVMVMSDSFDgrlTFRPG---NQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLT--ESWN------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 99 ftaSSGGLPTDEITFAKLLKDQGYSTALIGKwhlgmschskTDFC--HHplhhgfnyfygiSLTN-----LRDC-----K 166
Cdd:cd16171 70 ---NYKGLDPNYPTWMDRLEKHGYHTQKYGK----------LDYTsgHH------------SVSNrveawTRDVpfllrQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 167 PGEGSVFTTGFKRLVFLplqivgvtlltlaalnclgllhvplgvffsllflaaliltlflgflhyfrplncfMMRNYEII 246
Cdd:cd16171 125 EGRPTVNLVGDRSTVRV-------------------------------------------------------MLKDWQNT 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 247 qqpmsyDNLTQRLTVEAAQFIQrntetPFLLVL--SYLHVHTALFSSKDFAG-KSQHGVYGDAVEEMDWSVGQILNLLDE 323
Cdd:cd16171 150 ------DKAVHWIRKEAPNLTQ-----PFALYLglNLPHPYPSPSMGENFGSiRNIRAFYYAMCAETDAMLGEIISALKD 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 324 LRLANDTLIYFTSDQGahveevsskgEIHGGSNGIYKggkANNWEGGIRVPGILRWPRvIQAGQKIDEPTSNMDIFPTVA 403
Cdd:cd16171 219 TGLLDKTYVFFTSDHG----------ELAMEHRQFYK---MSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTML 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 404 KLAGAPLPEDriIDGRDLMPLLEGKSQ-----RSDHEFL----FHYCNAylNAVRWHPQnsTSIWKaffftpnfnpvgsn 474
Cdd:cd16171 285 DIAGVPQPQN--LSGYSLLPLLSESSIkespsRVPHPDWvlseFHGCNV--NASTYMLR--TNSWK-------------- 344
|
490 500 510
....*....|....*....|....*....|....
gi 1002913047 475 gcfathvcfcfgsYVTHHD----PPLLFDISKDP 504
Cdd:cd16171 345 -------------YIAYADgnsvPPQLFDLSKDP 365
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
257-401 |
1.00e-10 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 64.54 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 257 QRLTVEAAQFI-QRNTETPFLLVLSYLHVHTALFSsKDFAGKSQHGVYGD-------------------AVEEMDWSVGQ 316
Cdd:COG3083 364 RQITAQWLQWLdQRDSDRPWFSYLFLDAPHAYSFP-ADYPKPFQPSEDCNylaldnesdptpfknryrnAVHYVDSQIGR 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 317 ILNLLDELRLANDTLIYFTSDQGahvEEVSSKGEIHGGSNGIYkggkaNNWEggIRVPGILRWPRviQAGQKIDEPTSNM 396
Cdd:COG3083 443 VLDTLEQRGLLENTIVIITADHG---EEFNENGQNYWGHNSNF-----SRYQ--LQVPLVIHWPG--TPPQVISKLTSHL 510
|
....*
gi 1002913047 397 DIFPT 401
Cdd:COG3083 511 DIVPT 515
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
22-407 |
6.57e-09 |
|
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: 57.31 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 22 PNIILVMADdlGIGDP--GCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRA--AFMTGRYPVRSGMASWSRTGVF 97
Cdd:cd16015 1 PNVIVILLE--SFSDPyiDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 98 LFTassgglptdeiTFAKLLKDQGYSTALIgkwhlgmschsktdfchhplhHGFN-YFYGisltnlRDckpgegsvfttg 176
Cdd:cd16015 79 PLP-----------SLPSILKEQGYETIFI---------------------HGGDaSFYN------RD------------ 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 177 fkrlVFLPLqivgvtlltlaalnclgllhvplgvffsllflaaliltlfLGFLHYFrPLNCFMMRNYEIIQQPMSYDNLT 256
Cdd:cd16015 109 ----SVYPN----------------------------------------LGFDEFY-DLEDFPDDEKETNGWGVSDESLF 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 257 QRltveAAQFIQRNTETPFLLVL---------SYLHVHTALFSSKDfAGKSQHGVYGDAVEEMDWSVGQILNLLDELRLA 327
Cdd:cd16015 144 DQ----ALEELEELKKKPFFIFLvtmsnhgpyDLPEEKKDEPLKVE-EDKTELENYLNAIHYTDKALGEFIEKLKKSGLY 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 328 NDTLIYFTSDqgahveevsskgeiHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQaGQKIDEPTSNMDIFPTVAKLAG 407
Cdd:cd16015 219 ENTIIVIYGD--------------HLPSLGSDYDETDEDPLDLYRTPLLIYSPGLKK-PKKIDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
296-422 |
7.86e-07 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 51.96 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 296 GKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDqgahveevsskgeiHGGSngIYKGGKANNWEGGIRVPG 375
Cdd:COG1368 412 GKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGD--------------HGPR--SPGKTDYENPLERYRVPL 475
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1002913047 376 ILrWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRIIdGRDLM 422
Cdd:COG1368 476 LI-YSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
1-161 |
3.58e-06 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 49.36 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 1 MKIPFLLLFF--LWEAESHAASRPNIILV-----MADDLGIGDpgcygnktirTPNIDRLASGGVKLTQHLAASPLCT-P 72
Cdd:COG1524 1 MKRGLSLLLAslLAAAAAAAPPAKKVVLIlvdglRADLLERAH----------APNLAALAARGVYARPLTSVFPSTTaP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 73 SRAAFMTGRYPVRSGMASWS------RTGVFLFTASSGGLPTDEI----TFAKLLKDQGYSTALIGKWHLGMSchSKTDF 142
Cdd:COG1524 71 AHTTLLTGLYPGEHGIVGNGwydpelGRVVNSLSWVEDGFGSNSLlpvpTIFERARAAGLTTAAVFWPSFEGS--GLIDA 148
|
170
....*....|....*....
gi 1002913047 143 CHHPLHHGFNYFYGISLTN 161
Cdd:COG1524 149 ARPYPYDGRKPLLGNPAAD 167
|
|
| GPI_EPT |
cd16019 |
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ... |
275-415 |
5.26e-04 |
|
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293743 [Multi-domain] Cd Length: 292 Bit Score: 42.35 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 275 FLLVLSYLHVHtalfsskdfaGKSQHGVYGDAVEEMDWSVGQILNlldelRLANDTLIYFTSDQGahveeVSSKGEiHGG 354
Cdd:cd16019 160 FLGLDHLGHKH----------NTTSSPELEKKLDQMDNLIRDIYD-----RMDNDTLLVVVSDHG-----MNNDGN-HGG 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002913047 355 SN---------GIYKGGKANNweggiRVPGILRWPRVIQAGQKIDEP-----TSNMDIFPTVAKLAGAPLPEDRI 415
Cdd:cd16019 219 SSteetssfffFISKKGFFKK-----RPIDQIEKIKQNNEQQKIDPSeyiriIYQIDILPTICYLLGIPIPFNNI 288
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
240-407 |
3.54e-03 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 39.49 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 240 MRNYEIIQQPMSYDNLTQRLTVEAAQFIQR--NTETPFLLVLSYLHVhtalfsskDFAGksqHGvYG-------DAVEEM 310
Cdd:cd16018 121 YNPTPIPLGGYWQPYNDSFPFEERVDTILEwlDLERPDLILLYFEEP--------DSAG---HK-YGpdspevnEALKRV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 311 DWSVGQILNLLDELRLANDTLIYFTSDQGAhveevSSKGEiHGGSNGiykggkannwEGGIRVPGILRWPRvIQAGQKId 390
Cdd:cd16018 189 DRRLGYLIEALKERGLLDDTNIIVVSDHGM-----TDVGT-HGYDNE----------LPDMRAIFIARGPA-FKKGKKL- 250
|
170
....*....|....*..
gi 1002913047 391 EPTSNMDIFPTVAKLAG 407
Cdd:cd16018 251 GPFRNVDIYPLMCNLLG 267
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
46-88 |
4.20e-03 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 39.71 E-value: 4.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1002913047 46 RTPNIDRLASGGVKLTQHLAASPLCT-PSRAAFMTGRYPVRSGM 88
Cdd:pfam01663 19 LTPNLAALAKEGVSAPNLTPVFPTLTfPNHYTLVTGLYPGSHGI 62
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
263-352 |
7.03e-03 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 38.94 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002913047 263 AAQFIQRNTETPFLLVLSYLHVhtalfsskDFAGKsQHGVYG----DAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQ 338
Cdd:pfam01663 152 DLPFADVAAERPDLLLVYLEEP--------DYAGH-RYGPDSpeveDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDH 222
|
90
....*....|....
gi 1002913047 339 GAhvEEVSSKGEIH 352
Cdd:pfam01663 223 GM--TPVSDDKVIF 234
|
|
| |
