|
Name |
Accession |
Description |
Interval |
E-value |
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
6-456 |
0e+00 |
|
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: 536.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYSDGL-MGYHTPNIDRIAAEGMRFTDSYGEQSCTAGRAAFISGQSVYRTGMSKVGVPGVDIG 84
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIgRGAPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGLTTVGLPGSPGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 85 WAAEDPTIAELLKPLGYATGQFGKNHFGDLNKFLPTVHGFDEFFGNLYHlnaeeepenfdyphadqfpqlhefalprgvl 164
Cdd:cd16142 81 LPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYH------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 165 kckaldevstepddprygpvgrqtiedtgpltakrmeTIDDDIADATVDYIKRQHSEGNSFFVWCNFTHMHLYTHVKPES 244
Cdd:cd16142 130 -------------------------------------TIDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEF 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 245 KGQAGlWQSDYHDAMIDHDRNVGTVLDVLDELGIAEDTIVLYSTDNGPHRNTWPDGGMTPFRSEKDTNWEGAFRVPELIR 324
Cdd:cd16142 173 EGKSS-GKGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGPEQDVWPDGGYTPFRGEKGTTWEGGVRVPAIVR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 325 WPGKIKAGSVSNEIIQHHDWLPTLLAAAGDPDISEKLKkghkigdtEYKVHIDGYNLLPYLTGEVEHSPRRGFFYFsDDG 404
Cdd:cd16142 252 WPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPKDKLL--------GKDRHIDGVDQSPFLLGKSEKSRRSEFFYF-GEG 322
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1039668828 405 DLVAMRFENWKAVFLEQrcPGTLQVWAEPFTHLRLPKLYNLRTDPFEFADVT 456
Cdd:cd16142 323 ELGAVRWKNWKVHFKAQ--EDTGGPTGEPFYVLTFPLIFNLRRDPKERYDVT 372
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
5-456 |
2.70e-103 |
|
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: 315.27 E-value: 2.70e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 5 KPNIVVIWGDDIGITNLSCYsdGLMGYHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGM-SKVGVPGVD 82
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCY--GSPLIKTPNIDRLAAEGVRFTDFYAAAPvCSPSRAALLTGRYPVRVGLpGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 83 IGWAAEDPTIAELLKPLGYATGQFGKNHFGDLNKFLPTVHGFDEFFGNLY-HLNAEEEPENFDYPHADQFPQlhefalpr 161
Cdd:cd16026 79 GGLPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYsNDMWPFPLYRNDPPGPLPPLM-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 162 gvlkckALDEVSTEPDDPRYgpvgrqtiedtgpLTAkrmetiddDIADATVDYIKRQHseGNSFFVWCNFTHMHLYTHVK 241
Cdd:cd16026 151 ------ENEEVIEQPADQSS-------------LTQ--------RYTDEAVDFIERNK--DQPFFLYLAHTMPHVPLFAS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 242 PESKG--QAGLwqsdYHDAM--IDHdrNVGTVLDVLDELGIAEDTIVLYSTDNGPHRNTWPDGGMT-PFRSEKDTNWEGA 316
Cdd:cd16026 202 EKFKGrsGAGL----YGDVVeeLDW--SVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHGGSAgPLRGGKGTTWEGG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 317 FRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGdpdiseklkkghkiGDTEYKVHIDGYNLLPYLTGEvEHSPRRG 396
Cdd:cd16026 276 VRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAG--------------APLPEDRVIDGKDISPLLLGG-SKSPPHP 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 397 FFYFSDDGDLVAMRFENWKAVFlEQRCPGTLQVWAEPFTHLRLPKLYNLRTDPFEFADVT 456
Cdd:cd16026 341 FFYYYDGGDLQAVRSGRWKLHL-PTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGETYNVA 399
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-490 |
1.35e-99 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 305.65 E-value: 1.35e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 1 MPNGKPNIVVIWGDDIGITNLSCYSDGLmgYHTPNIDRIAAEGMRFTDSY-GEQSCTAGRAAFISGQSVYRTGMSKVGvP 79
Cdd:COG3119 19 AAAKRPNILFILADDLGYGDLGCYGNPL--IKTPNIDRLAAEGVRFTNAYvTSPVCSPSRASLLTGRYPHRTGVTDNG-E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 80 GVDIGWAAEDPTIAELLKPLGYATGQFGKNHFgdlnkflptvhgfdeffgnlyhlnaeeepenfdyphadqfpqlhefal 159
Cdd:COG3119 96 GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------------------------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 160 prgvlkckaldevstepddprygpvgrqtiedtgpltakrmeTIDDDIADATVDYIKRQHSEGNSFFVWCNFTHMHLYTH 239
Cdd:COG3119 128 ------------------------------------------YLTDLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQ 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 240 VKPESKG------------------QAGLWQSDYHD--AMIDH-DRNVGTVLDVLDELGIAEDTIVLYSTDNGPHrntWP 298
Cdd:COG3119 166 APEEYLDkydgkdiplppnlaprdlTEEELRRARAAyaAMIEEvDDQVGRLLDALEELGLADNTIVVFTSDNGPS---LG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 299 DGGmtpFRSEKDTNWEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGdpdiseklkkghkigdTEYKVHIDG 378
Cdd:COG3119 243 EHG---LRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAG----------------VPIPEDLDG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 379 YNLLPYLTGEVEHSPRRGFFYFSDDGDLVAMRFENWKAVFLEQRcpgtlqvwaepfthLRLPKLYNLRTDPFEFADVtSN 458
Cdd:COG3119 304 RSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTGRWKLIRYYDD--------------DGPWELYDLKNDPGETNNL-AA 368
|
490 500 510
....*....|....*....|....*....|..
gi 1039668828 459 TYYEWLLRhdyfifyMTAMASKFLETFKEFPP 490
Cdd:COG3119 369 DYPEVVAE-------LRALLEAWLKELGDPPL 393
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
6-455 |
1.32e-82 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 262.53 E-value: 1.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYsdGLMGYHTPNIDRIAAEGMRFTDSY-GEQSCTAGRAAFISGQSVYRTGMSKVGVPGVDIG 84
Cdd:cd16145 1 PNIIFILADDLGYGDLGCY--GQKKIKTPNLDRLAAEGMRFTQHYaGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 85 WAAEDPTIAELLKPLGYATGQFGKNHFGDLNKF-LPTVHGFDEFFGNLYHLNAEeepeNFdYPhadqfPQLHE----FAL 159
Cdd:cd16145 79 LPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYGYLDQVHAH----NY-YP-----EYLWRngekVPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 160 PRGVLKCkaldevstePDDPRYGPVGRQTIedtgpltakrmetIDDDIADATVDYIKRQHSEgnSFFVWCNFTHMHLYTH 239
Cdd:cd16145 149 PNNVIPP---------LDEGNNAGGGGGTY-------------SHDLFTDEALDFIRENKDK--PFFLYLAYTLPHAPLQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 240 VKPESK-GQAGLWQSDYHD-----------AMIDH-DRNVGTVLDVLDELGIAEDTIVLYSTDNGPH-------RNTWPD 299
Cdd:cd16145 205 VPDDGPyKYKPKDPGIYAYlpwpqpekayaAMVTRlDRDVGRILALLKELGIDENTLVVFTSDNGPHseggsehDPDFFD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 300 GGmTPFRSEKDTNWEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGdpdiseklkkghkigdTEYKVHIDGY 379
Cdd:cd16145 285 SN-GPLRGYKRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAG----------------AEPPEDIDGI 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039668828 380 NLLPYLTGEVEHSPRRGFFY-FSDDGDLVAMRFENWKAVfleqrcpgTLQVWAEPFthlrlpKLYNLRTDPFEFADV 455
Cdd:cd16145 348 SLLPTLLGKPQQQQHDYLYWeFYEGGGAQAVRMGGWKAV--------RHGKKDGPF------ELYDLSTDPGETNNL 410
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
6-451 |
1.72e-78 |
|
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: 252.08 E-value: 1.72e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYSDGLmgYHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGMSKVGVPGVDIG 84
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKF--YETPNIDRLAKEGMRFTQAYAAAPvCSPSRASILTGQYPARLGITDVIPGRRGPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 85 W-------------AAEDPTIAELLKPLGYATGQFGKNHFGDLNKFLPTVHGFDEFFGNlyhlnaeeepenfdyphadqf 151
Cdd:cd16144 79 DntklipppsttrlPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIGG--------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 152 pqlHEFALPRGvlkckaldevstePDDPRYGPVGRQTIEDTGP-LTakrmetidDDIADATVDYIKRQHSEgnSFFVwcN 230
Cdd:cd16144 138 ---TGNGGPPS-------------YYFPPGKPNPDLEDGPEGEyLT--------DRLTDEAIDFIEQNKDK--PFFL--Y 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 231 FTH--MHLYTHVKPES-----KGQAGLWQSDYHD---AMIDH-DRNVGTVLDVLDELGIAEDTIVLYSTDNGPHRNtwPD 299
Cdd:cd16144 190 LSHyaVHTPIQARPELiekyeKKKKGLRKGQKNPvyaAMIESlDESVGRILDALEELGLADNTLVIFTSDNGGLST--RG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 300 GGMT---PFRSEKDTNWEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGDPDISEKlkkghkigdteykvHI 376
Cdd:cd16144 268 GPPTsnaPLRGGKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQ--------------HL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 377 DGYNLLPYLTGEVEHSPRRGFF----YFSDDGDL--VAMRFENWKAV-FLEQRCpgtlqvwaepfthlrlPKLYNLRTDP 449
Cdd:cd16144 334 DGVSLVPLLKGGEADLPRRALFwhfpHYHGQGGRpaSAIRKGDWKLIeFYEDGR----------------VELYNLKNDI 397
|
..
gi 1039668828 450 FE 451
Cdd:cd16144 398 GE 399
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
6-457 |
2.53e-71 |
|
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293765 [Multi-domain] Cd Length: 409 Bit Score: 232.83 E-value: 2.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYSDGLMgyHTPNIDRIAAEGMRFTDSYGEQSCTAGRAAFISGQSVYRTGmskvgVPGVDIGW 85
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPIL--KTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTG-----VWHTILGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 86 ---AAEDPTIAELLKPLGYATGQFGKNHFGDLNKFLPTVHGFDEFFGN-LYHLNaeeepENFDYPHADQFpqlhefalpr 161
Cdd:cd16146 74 ermRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHgGGGIG-----QYPDYWGNDYF---------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 162 gvlkckaldevstepdDPRYGPVGrqtiedtgplTAKRMET-IDDDIADATVDYIKRQHseGNSFFVWCNFTHMHLYTHV 240
Cdd:cd16146 139 ----------------DDTYYHNG----------KFVKTEGyCTDVFFDEAIDFIEENK--DKPFFAYLATNAPHGPLQV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 241 KPE----------SKGQAGLWqsdyhdAMIDH-DRNVGTVLDVLDELGIAEDTIVLYSTDNGP-HRNTWP-DGGMtpfRS 307
Cdd:cd16146 191 PDKyldpykdmglDDKLAAFY------GMIENiDDNVGRLLAKLKELGLEENTIVIFMSDNGPaGGVPKRfNAGM---RG 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 308 EKDTNWEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGDPdISEKLKkghkigdteykvhIDGYNLLPYLTG 387
Cdd:cd16146 262 KKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVK-LPEGIK-------------LDGRSLLPLLKG 327
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039668828 388 EVEHSPRRGFFYFSDDGDLV-------AMRFENWKAvfleqrcpgtlqVWAEPFThlrlPKLYNLRTDPFEFADVTS 457
Cdd:cd16146 328 ESDPWPERTLFTHSGRWPPPpkkkrnaAVRTGRWRL------------VSPKGFQ----PELYDIENDPGEENDVAD 388
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
6-451 |
3.59e-68 |
|
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: 224.00 E-value: 3.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYSDGlMGYHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGMSKVGVPGVDIG 84
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPD-SKIPTPNIDRLAAEGMRFTDAHSPSSvCTPSRYGLLTGRYPWRSRLKGGVLGGFSPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 85 W-AAEDPTIAELLKPLGYATGQFGKNHFG-------------------DLNKFL---PTVHGFDEFFGnlyhlnaeeepe 141
Cdd:cd16143 80 LiEPDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkaatgtgkdvDYSKPIkggPLDHGFDYYFG------------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 142 nfdyphadqfpqlhefaLPRGvlkckaldevstepddprygpvgrqtiedtgpltakrmeTIDDDIADATVDYIKRQHSE 221
Cdd:cd16143 148 -----------------IPAS---------------------------------------EVLPTLTDKAVEFIDQHAKK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 222 GNSFFVWCNFTHMHLYTHVKPESKGQAGLwqSDYHDAMIDHDRNVGTVLDVLDELGIAEDTIVLYSTDNGPHRNtwPDGG 301
Cdd:cd16143 172 DKPFFLYFALPAPHTPIVPSPEFQGKSGA--GPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPY--ADYK 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 302 MT---------PFRSEKDTNWEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGdpdisEKLKKGhkigdtey 372
Cdd:cd16143 248 ELekfghdpsgPLRGMKADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVG-----QKLPDN-------- 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 373 kVHIDGYNLLPYLTGEVEHSPRRGFFYFSDDGDLvAMRFENWKAVFleqrCPGTlQVWAEPFTHLRLPK----LYNLRTD 448
Cdd:cd16143 315 -AAEDSFSFLPALLGPKKQEVRESLVHHSGNGSF-AIRKGDWKLID----GTGS-GGFSYPRGKEKLGLppgqLYNLSTD 387
|
...
gi 1039668828 449 PFE 451
Cdd:cd16143 388 PGE 390
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
5-466 |
1.61e-59 |
|
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: 204.83 E-value: 1.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 5 KPNIVVIWGDDIGITNLSCYsdGLMGYHTPNIDRIAAEGMRFT-DSYGEQSCTAGRAAFISGQSVYRTGMSKVGVPGVDI 83
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCF--GNDTIRTPNIDRLAKEGVKLThHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 84 ------GWAAEDPTIAELLKPLGYATGQFGKNHFGdLNK-------FLPTVHGFDEFFG-NLYHLNAEEEPEN--FDYPH 147
Cdd:cd16159 79 ftassgGLPPNETTFAEVLKQQGYSTALIGKWHLG-LHCesrndfcHHPLNHGFDYFYGlPLTNLKDCGDGSNgeYDLSF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 148 ADQFPQLHEF---------------ALPRGVLKCKALdevstepddpryGPVGRQTIEDTGPLTAKRMETI---DDDIAD 209
Cdd:cd16159 158 DPLFPLLTAFvlitaltiflllylgAVSKRFFVFLLI------------LSLLFISLFFLLLITNRYFNCIlmrNHEVVE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 210 ATVDY---IKRQHSEGNS---------FFVWCNFTHMH--LYTHVKPESKGQAGLwqsdYHDAMIDHDRNVGTVLDVLDE 275
Cdd:cd16159 226 QPMSLenlTQRLTKEAISflernkerpFLLVMSFLHVHtaLFTSKKFKGRSKHGR----YGDNVEEMDWSVGQILDALDE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 276 LGIAEDTIVLYSTDNGPH-----RNTWPDGGMTPFR-SEKDTNWEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLL 349
Cdd:cd16159 302 LGLKDNTFVYFTSDNGGHleeisVGGEYGGGNGGIYgGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 350 AAAGDPDISEKlkkghkigdteykvHIDGYNLLPYLTGEVEHSPRRgFFYFSDDGDLVAMRFEN------WKAVF----- 418
Cdd:cd16159 382 ALAGAPLPSDR--------------IIDGRDLMPLLTGQEKRSPHE-FLFHYCGAELHAVRYRPrdggavWKAHYftpnf 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1039668828 419 --LEQRCPGTL--QVWAEPFTHLRLPKLYNLRTDPFEFA--DVTSNTYYEWLLR 466
Cdd:cd16159 447 ypGTEGCCGTLlcRCFGDSVTHHDPPLLFDLSADPSESNplDPTDEPYQEIIKK 500
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
5-466 |
1.77e-59 |
|
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: 203.83 E-value: 1.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 5 KPNIVVIWGDDIGITNLSCYsdGLMGYHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGM-SKVGVPGVD 82
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCY--GHPSSSTPNLDRLAANGLRFTDFYSSSPvCSPSRAALLTGRYQVRSGVyPGVFYPGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 83 IGWAAEDPTIAELLKPLGYATGQFGKNH--FGDLNKFLPTVHGFDEFFGnlyhlnaeeepenFDYPHaDQFPQLHEFALP 160
Cdd:cd16158 79 GGLPLNETTIAEVLKTVGYQTAMVGKWHlgVGLNGTYLPTHQGFDHYLG-------------IPYSH-DQGPCQNLTCFP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 161 rgvlkckaldevstePDDPRYGpvGRQTIEDTGPLTAKrmETIDDDIADATV----------DYIKRQHSEGNSFFVWCN 230
Cdd:cd16158 145 ---------------PNIPCFG--GCDQGEVPCPLFYN--ESIVQQPVDLLTleeryakfakDFIADNAKEGKPFFLYYA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 231 FTHMHLYTHVKPESKGQAGlwQSDYHDAMIDHDRNVGTVLDVLDELGIAEDTIVLYSTDNGPHRNTWPDGGMTPF-RSEK 309
Cdd:cd16158 206 SHHTHYPQFAGQKFAGRSS--RGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRKSRGGNAGLlKCGK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 310 DTNWEGAFRVPELIRWPGKIKAGsVSNEIIQHHDWLPTLLAAAGDPdisekLKkghkigdteyKVHIDGYNLLPYLTgEV 389
Cdd:cd16158 284 GTTYEGGVREPAIAYWPGRIKPG-VTHELASTLDILPTIAKLAGAP-----LP----------NVTLDGVDMSPILF-EQ 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 390 EHSPRRGFFYFSDDGDLV----AMRFENWKAVFLEQ-----------RC-PGTLQVWAEPfthlrlPKLYNLRTDPFEFA 453
Cdd:cd16158 347 GKSPRQTFFYYPTSPDPDkgvfAVRWGKYKAHFYTQgaahsgttpdkDChPSAELTSHDP------PLLFDLSQDPSENY 420
|
490
....*....|...
gi 1039668828 454 DVTSNTYYEWLLR 466
Cdd:cd16158 421 NLLGLPEYNQVLK 433
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-451 |
9.16e-57 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 193.58 E-value: 9.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYsdGLMGYHTPNIDRIAAEGMRFTDSYGEQSCTAGRAAFISGQSVYRTGMskvgVPGVdigW 85
Cdd:cd16151 1 PNIILIMADDLGYECIGCY--GGESYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYV----VFGY---L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 86 AAEDPTIAELLKPLGYATGQFGKNHFGDLNKFLPTVH--GFDEFFgnLYHLNAEEEPENfdyPHADQFPQLHEFALPrgv 163
Cdd:cd16151 72 DPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGDYPHefGFDEYC--LWQLTETGEKYS---RPATPTFNIRNGKLL--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 164 lkckaldevSTEPDDprYGPvgrqtiedtgpltakrmetidDDIADATVDYIKRQHSEgnSFFVW-------CNFTHMHL 236
Cdd:cd16151 144 ---------ETTEGD--YGP---------------------DLFADFLIDFIERNKDQ--PFFAYypmvlvhDPFVPTPD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 237 YTHVKPESKGQAGLWqsDYHDAMIDH-DRNVGTVLDVLDELGIAEDTIVLYSTDNGPHRN--TWPDGGMTpfRSEKDTNW 313
Cdd:cd16151 190 SPDWDPDDKRKKDDP--EYFPDMVAYmDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitSRTNGREV--RGGKGKTT 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 314 EGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAgdpdiseklkkGHKIGDteyKVHIDGYNLLPYLTGEVEHSP 393
Cdd:cd16151 266 DAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELA-----------GAPLPE---DYPLDGRSFAPQLLGKTGSPR 331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039668828 394 RRGFFY----FSDDGDLVAMRFENWKavfleqrcpgtlqvwaepftHLRLPKLYNLRTDPFE 451
Cdd:cd16151 332 REWIYWyyrnPHKKFGSRFVRTKRYK--------------------LYADGRFFDLREDPLE 373
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
6-353 |
2.67e-56 |
|
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: 187.64 E-value: 2.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYsdGLMGYHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGMskVGVPGVDIG 84
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCY--GNPDIKTPNLDRLAAEGVRFTNAYVASPvCSPSRASLLTGRYPHRHGV--RGNVGNGGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 85 WAAEDPTIAELLKPLGYATGQFGKNHfgdlnkflptvhgfdeffgnlyhlnaeeepenfdyphadqfpqlhefalprgvl 164
Cdd:cd16022 77 LPPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 165 kckaldevstepddprygpvgrqtiedtgpltakrmetidddiaDATVDYIKRqHSEGNSFFVWCNFTHMHLYTHvkpes 244
Cdd:cd16022 103 --------------------------------------------DEAIDFIER-RDKDKPFFLYVSFNAPHPPFA----- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 245 kgqaglwqsdYHdAMIDH-DRNVGTVLDVLDELGIAEDTIVLYSTDNGPHRNtwpDGGMtpfRSEKDTNWEGAFRVPELI 323
Cdd:cd16022 133 ----------YY-AMVSAiDDQIGRILDALEELGLLDNTLIVFTSDHGDMLG---DHGL---RGKKGSLYEGGIRVPFIV 195
|
330 340 350
....*....|....*....|....*....|
gi 1039668828 324 RWPGKIKAGSVSNEIIQHHDWLPTLLAAAG 353
Cdd:cd16022 196 RWPGKIPAGQVSDALVSLLDLLPTLLDLAG 225
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
5-451 |
2.41e-55 |
|
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: 191.87 E-value: 2.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 5 KPNIVVIWGDDIGITNLSCYsdglmGYHTPN---IDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGM---SKVG 77
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASY-----GHPTQErgpIDDMAAEGIRFTQAYSADSvCTPSRAALLTGRLPIRSGMyggTRVF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 78 VPGVDIGWAAEDPTIAELLKPLGYATGQFGKNHFGdLNKF-------LPTVHGFDeFFG-NL-YHLNAEEEPENFDYPHA 148
Cdd:cd16160 76 LPWDIGGLPKTEVTMAEALKEAGYTTGMVGKWHLG-INENnhsdgahLPSHHGFD-FVGtNLpFTNSWACDDTGRHVDFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 149 DqfpqlhefalprgVLKCKAL--DEVSTEPDDPRYgpvgrqtiedtgpLTAKrmetidddIADATVDYIK-RQHsegNSF 225
Cdd:cd16160 154 D-------------RSACFLYynDTIVEQPIQHEH-------------LTET--------LVGDAKSFIEdNQE---NPF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 226 FVWCNFTHMHLYTHVKPESKGQAGlwQSDYHDAMIDHDRNVGTVLDVLDELGIAEDTIVLYSTDNGPHRNTWPDGGMT-P 304
Cdd:cd16160 197 FLYFSFPQTHTPLFASKRFKGKSK--RGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTgG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 305 FRSEKDTNWEGAFRVPELIRWPGKIKAGsVSNEIIQHHDWLPTLLAAAGdpdiseklkkGHKIGDTeykvHIDGYNLLPY 384
Cdd:cd16160 275 LKGGKGNSWEGGIRVPFIAYWPGTIKPR-VSHEVVSTMDIFPTFVDLAG----------GTLPTDR----IYDGLSITDL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 385 LTGEVEHSPRRGFFYFSDDgdLVAMRFENWKAVFLEQR-----------CPGTLQ----VWAEPF----THLRLPKLYNL 445
Cdd:cd16160 340 LLGEADSPHDDILYYCCSR--LMAVRYGSYKIHFKTQPlpsqesldpncDGGGPLsdyiVCYDCEdecvTKHNPPLIFDV 417
|
....*.
gi 1039668828 446 RTDPFE 451
Cdd:cd16160 418 EKDPGE 423
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
6-455 |
3.82e-53 |
|
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: 184.29 E-value: 3.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGitnlscYSDglMGYH------TPNIDRIAAEGMRFTDSYGEQSCTAGRAAFISGQSVYRTGM-SKVGV 78
Cdd:cd16029 1 PHIVFILADDLG------WND--VGFHgsdqikTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMqHGVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 79 PGVDIGWAAEDPTIAELLKPLGYATGQFGKNHFGDLN-KFLPTVHGFDEFFGnlYHLNAEeepenfDY--PHADQFPQLH 155
Cdd:cd16029 73 AGEPYGLPLNETLLPQYLKELGYATHLVGKWHLGFYTwEYTPTNRGFDSFYG--YYGGAE------DYytHTSGGANDYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 156 EFALPRGvlkckaldevsTEPDDPRYGpvgrqtiedtgpltakRMETidDDIADATVDYIkRQHSEGNSFFVWCNFTHMH 235
Cdd:cd16029 145 NDDLRDN-----------EEPAWDYNG----------------TYST--DLFTDRAVDII-ENHDPSKPLFLYLAFQAVH 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 236 LYTHVKPESKGQAGLWQSDYHD-------AMIDH-DRNVGTVLDVLDELGIAEDTIVLYSTDNGphrnTWPDGGMT---- 303
Cdd:cd16029 195 APLQVPPEYADPYEDKFAHIKDedrrtyaAMVSAlDESVGNVVDALKAKGMLDNTLIVFTSDNG----GPTGGGDGgsny 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 304 PFRSEKDTNWEGAFRVPELIRWPG-KIKAGSVSNEIIQHHDWLPTLLAAAGdpdiseklkkghkiGDTEYKVHIDGYNLL 382
Cdd:cd16029 271 PLRGGKNTLWEGGVRVPAFVWSPLlPPKRGTVSDGLMHVTDWLPTLLSLAG--------------GDPDDLPPLDGVDQW 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039668828 383 PYLTGEVEhSPRRGFFY----FSDDGDLVAMRFENWKAVFLEQrcpgtlqvwaepfthlrlpkLYNLRTDPFEFADV 455
Cdd:cd16029 337 DALSGGAP-SPRTEILLniddITRTTGGAAIRVGDWKLIVGKP--------------------LFNIENDPCERNDL 392
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
4-451 |
1.78e-51 |
|
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: 180.33 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 4 GKPNIVVIWGDDIGITNLSCYsdglmG--YHTPNIDRIAAEGMRFTDSYGEQSCTAGRAAFISGQSVYRTGMSKV----- 76
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCF-----GgeIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTMaelat 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 77 GVPGVDIGWAAEDPTIAELLKPLGYATGQFGKNHFGdlnkflptvhgfdeffgnlyhlnaeeePENFdypHADqfpqlhe 156
Cdd:cd16025 76 GKPGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG---------------------------PDDY---YST------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 157 falprgvlkckaldevstepddprygpvgrqtiedtgpltakrmetidDDIADATVDYIKRQHSEGNSFFVWCNFTHMHL 236
Cdd:cd16025 119 ------------------------------------------------DDLTDKAIEYIDEQKAPDKPFFLYLAFGAPHA 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 237 YTHVKPES----KG------------------QAGL----------------WQS------DYHD-------AMIDH-DR 264
Cdd:cd16025 151 PLQAPKEWidkyKGkydagwdalreerlerqkELGLipadtkltprppgvpaWDSlspeekKLEArrmevyaAMVEHmDQ 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 265 NVGTVLDVLDELGIAEDTIVLYSTDNGPHRNT-WPDGGMTPFRSEKDTNWEGAFRVPELIRWPGKIKA-GSVSNEIIQHH 342
Cdd:cd16025 231 QIGRLIDYLKELGELDNTLIIFLSDNGASAEPgWANASNTPFRLYKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHVI 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 343 DWLPTLLAAAG-DPDISEKLKKGHKigdteykvhIDGYNLLPYLTGEVEHSPRRgFFYFSDDGDLvAMRFENWKAVFLeQ 421
Cdd:cd16025 311 DIAPTILELAGvEYPKTVNGVPQLP---------LDGVSLLPTLDGAAAPSRRR-TQYFELFGNR-AIRKGGWKAVAL-H 378
|
490 500 510
....*....|....*....|....*....|
gi 1039668828 422 RCPGTLQVWAepfthlrlpkLYNLRTDPFE 451
Cdd:cd16025 379 PPPGWGDQWE----------LYDLAKDPSE 398
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
4-465 |
1.89e-51 |
|
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: 180.80 E-value: 1.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 4 GKPNIVVIWGDDIGITNLSCYSDGLMgyHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGMSKVGVPGVD 82
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIV--KTPNIDRLAKEGVRFDNAFVTTSiCAPSRASILTGQYSHRHGVTDNNGPLFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 83 igwaAEDPTIAELLKPLGYATGQFGKNHFGDLNKFLPTvhGFDEFFGnlyhlnaeeepenfdypHADQfpqlhefalprg 162
Cdd:cd16031 79 ----ASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--GFDYWVS-----------------FPGQ------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 163 vlkckaldevsTEPDDPRYGPVGRQTIEDtGPLTakrmetidDDIADATVDYIKRQHsEGNSFFVWCNFT---------- 232
Cdd:cd16031 124 -----------GSYYDPEFIENGKRVGQK-GYVT--------DIITDKALDFLKERD-KDKPFCLSLSFKaphrpftpap 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 233 -HMHLYTHV---------------KPESKGQAG-----------LWQSDYHDAMIDH-------DRNVGTVLDVLDELGI 278
Cdd:cd16031 183 rHRGLYEDVtipepetfddddyagRPEWAREQRnrirgvldgrfDTPEKYQRYMKDYlrtvtgvDDNVGRILDYLEEQGL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 279 AEDTIVLYSTDNG----PHRntWPDggmtpfrseKDTNWEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGD 354
Cdd:cd16031 263 ADNTIIIYTSDNGfflgEHG--LFD---------KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGV 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 355 PdISEklkkghkigdteykvHIDGYNLLPYLTGEVEHSPRRGFFY---FSDDGDLV----AMRFENWKAVfleqRCPGTL 427
Cdd:cd16031 332 P-IPE---------------DMQGRSLLPLLEGEKPVDWRKEFYYeyyEEPNFHNVptheGVRTERYKYI----YYYGVW 391
|
490 500 510
....*....|....*....|....*....|....*...
gi 1039668828 428 QVWaepfthlrlpKLYNLRTDPFEFADVTSNTYYEWLL 465
Cdd:cd16031 392 DEE----------ELYDLKKDPLELNNLANDPEYAEVL 419
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
5-451 |
4.72e-51 |
|
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: 178.82 E-value: 4.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 5 KPNIVVIWGDDIGITNLscysdGLMGYH----TPNIDRIAAEGMRFTDSY-GEQSCTAGRAAFISGQSVYRTGMSKVGVP 79
Cdd:cd16161 1 KPNFLLLFADDLGWGDL-----GANWAPnailTPNLDKLAAEGTRFVDWYsAASVCSPSRASLMTGRLGLRNGVGHNFLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 80 GVDIGWAAEDPTIAELLKPLGYATGQFGKNHFGDLNKFLPTVHGFDEFFGnlyhlnaeeepenFDYPHADQFPQlhefal 159
Cdd:cd16161 76 TSVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFG-------------IPFSHDSSLAD------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 160 prgvlkckaldevstepddpRYgpvgrqtiedtgpltakrmetidddiADATVDYIKRQHSEGNSFFVWCNFTHMHL--- 236
Cdd:cd16161 137 --------------------RY--------------------------AQFATDFIQRASAKDRPFFLYAALAHVHVpla 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 237 YTHVKPESKGQAGLwqsdYHDAMIDHDRNVGTVLDVLDELGIAEDTIVLYSTDNGP---------HRNTWPDGGMTPFRS 307
Cdd:cd16161 171 NLPRFQSPTSGRGP----YGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGPwevkcelavGPGTGDWQGNLGGSV 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 308 EKDTNWEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGDPDISEKLkkghkigdteykvhIDGYNLLPYLTG 387
Cdd:cd16161 247 AKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPGRI--------------YDGKDLSPVLFG 312
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039668828 388 EVEhSPRRGFFYFSDD----GDLVAMRFENWKAVFLEQRCPGTLQVWAEPFTHlRLPKLYNLRTDPFE 451
Cdd:cd16161 313 GSK-TGHRCLFHPNSGaagaGALSAVRCGDYKAHYATGGALACCGSTGPKLYH-DPPLLFDLEVDPAE 378
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
5-451 |
2.64e-44 |
|
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: 162.64 E-value: 2.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 5 KPNIVVIWGDDIGITNLSCYsdGLMGYHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGM------SKVG 77
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVF--GEPSRETPNLDRMAAEGMLFTDFYSANPlCSPSRAALLTGRLPIRNGFyttnahARNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 78 VPGVDI--GWAAEDPTIAELLKPLGYATGQFGKNHFGDLNKFLPTVHGFDEFFGNlyhlnaeeepenfdyphadqfPQLH 155
Cdd:cd16157 79 YTPQNIvgGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGA---------------------PNCH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 156 eFALPrgvlkckalDEVSTePDDPRYGP---VGRQTIEDTGPLTAKRMETIDDDIADAtVDYIKRQHSEGNSFFV-WC-N 230
Cdd:cd16157 138 -FGPY---------DNKAY-PNIPVYRDwemIGRYYEEFKIDKKTGESNLTQIYLQEA-LEFIEKQHDAQKPFFLyWApD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 231 FTHMHLYTHVKPESKGQAGLwqsdYHDAMIDHDRNVGTVLDVLDELGIAEDTIVLYSTDNGPHRNTWPD--GGMTPFRSE 308
Cdd:cd16157 206 ATHAPVYASKPFLGTSQRGL----YGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALISAPEqgGSNGPFLCG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 309 KDTNWEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGDPDISEKLkkghkigdteykvhIDGYNLLPYLTGe 388
Cdd:cd16157 282 KQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRA--------------IDGIDLLPVLLN- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 389 vEHSPRRGFFYFSDDgDLVAMRFENWKAVFL-------EQR-----CPG------TLQVWAEpftHLRLPKLYNLRTDPF 450
Cdd:cd16157 347 -GKEKDRPIFYYRGD-ELMAVRLGQYKAHFWtwsnsweEFRkginfCPGqnvpgvTTHNQTD---HTKLPLLFHLGRDPG 421
|
.
gi 1039668828 451 E 451
Cdd:cd16157 422 E 422
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
6-353 |
1.19e-43 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 156.43 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYSDGLMgyHTPNIDRIAAEGMRFTDSYGEQSCTA-GRAAFISGQSVYRTGMSKVGVPGVdig 84
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRP--TTPFLDRLAEEGLLFSNFYSGGTLTApSRFALLTGLPPHNFGSYVSTPVGL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 85 wAAEDPTIAELLKPLGYATGQFGKNHFGDLNKFLPTVHGFDEFFGNLYHLNAEEEPENFDYPHadqfpqlhefalprgvl 164
Cdd:pfam00884 76 -PRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNC----------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 165 kckaldevstepddprygpvgrqtiedtgpltaKRMETIDDDIADATVDYIKRQHsegNSFFVWCNFTHMHL-------- 236
Cdd:pfam00884 138 ---------------------------------SGGGVSDEALLDEALEFLDNND---KPFFLVLHTLGSHGppyypdry 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 237 ---YTHVKPESKGQAGLWQSdYHDAMIDHDRNVGTVLDVLDELGIAEDTIVLYSTDNGPHRntwpDGGMTPFRSEK-DTN 312
Cdd:pfam00884 182 pekYATFKPSSCSEEQLLNS-YDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESL----GEGGGYLHGGKyDNA 256
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1039668828 313 WEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAG 353
Cdd:pfam00884 257 PEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
6-452 |
4.40e-43 |
|
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: 156.90 E-value: 4.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGiTNLSCYSDGLMgyHTPNIDRIAAEGMRFTDSYGEQ-SCTAGRAAFISGQSVYRTGMSkvGVPGVDIG 84
Cdd:cd16027 1 PNILWIIADDLS-PDLGGYGGNVV--KTPNLDRLAAEGVRFTNAFTTApVCSPSRSALLTGLYPHQNGAH--GLRSRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 85 WAAEDPTIAELLKPLGYATGQFGKNHfgdlnkflptvhgfdeffgnlyhlnaeeepENFDYPHADQFPQLHEFALPRgvl 164
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTH------------------------------YNPDAVFPFDDEMRGPDDGGR--- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 165 kckaldevstepddprygpvgrqtiedtgpltakrmetIDDDIADATVDYIKRQhSEGNSFFVWCNFTHMHLYTHVKPES 244
Cdd:cd16027 123 --------------------------------------NAWDYASNAADFLNRA-KKGQPFFLWFGFHDPHRPYPPGDGE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 245 KGQAGLWQ-----------------SDYHDAMIDHDRNVGTVLDVLDELGIAEDTIVLYSTDNGPhrntwpdggmtPFRS 307
Cdd:cd16027 164 EPGYDPEKvkvppylpdtpevredlADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----------PFPR 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 308 EKDTNWEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGdpdiseklkkghkigdTEYKVHIDGYNLLPYLTG 387
Cdd:cd16027 233 AKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAG----------------IEPPEYLQGRSFLPLLKG 296
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039668828 388 EVEHSPRR---GFFYFSDDGDLV-AMRFENWKAVFleqrcpgtlqvwaepftHLRLPKLYNLRTDPFEF 452
Cdd:cd16027 297 EKDPGRDYvfaERDRHDETYDPIrSVRTGRYKYIR-----------------NYMPEELYDLKNDPDEL 348
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
5-400 |
3.44e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 144.25 E-value: 3.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 5 KPNIVVIWGDDIGITNLSCYSDglMGYHTPNIDRIAAEGMRFTDSY-GEQSCTAGRAAFISGQSVYRTGMskvgvPGVDI 83
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGD--DPVKTPNLDRLAKEGVVFTNAVsNYPVCSPYRASLLTGQYPLTNGV-----FGNDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 84 GWAAEDPTIAELLKPLGYATGQFGKNH-------FGDLNKFLPTV---HGFDEFFGNlyhlnaeeepENFDYPHadqfpq 153
Cdd:cd16034 74 PLPPDAPTIADVLKDAGYRTGYIGKWHldgpernDGRADDYTPPPerrHGFDYWKGY----------ECNHDHN------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 154 lhefalprgvlkckaldevstepdDPRYgpvgrqtiEDTGPLTAKRMETIDDDIADATVDYIKRQHSEGNSFF-VWC-NF 231
Cdd:cd16034 138 ------------------------NPHY--------YDDDGKRIYIKGYSPDAETDLAIEYLENQADKDKPFAlVLSwNP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 232 TH----------MHLYTHVK-------PESKGQAGLWQSDYHD--AMIDH-DRNVGTVLDVLDELGIAEDTIVLYSTDNG 291
Cdd:cd16034 186 PHdpyttapeeyLDMYDPKKlllrpnvPEDKKEEAGLREDLRGyyAMITAlDDNIGRLLDALKELGLLENTIVVFTSDHG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 292 ----PHrntwpdgGMTpfrsEKDTNWEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAG--DPDiseklkkgh 365
Cdd:cd16034 266 dmlgSH-------GLM----NKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGlpIPD--------- 325
|
410 420 430
....*....|....*....|....*....|....*
gi 1039668828 366 kigdteykvHIDGYNLLPYLTGEVEHSPRRGFFYF 400
Cdd:cd16034 326 ---------TVEGRDLSPLLLGGKDDEPDSVLLQC 351
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
6-449 |
5.08e-31 |
|
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: 122.69 E-value: 5.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYSDGLMgyHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGMSKVGVPgvdig 84
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVV--KTPNLDRLAARGVVFDNAYCNSPlCAPSRASMMTGRLPSRIGAYDNAAE----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 85 WAAEDPTIAELLKPLGYATGQFGKNHF--GDlnkflpTVHGFDeffgnlyhlnaeeepenFDyphadqfpqlhefalprg 162
Cdd:cd16032 74 FPADIPTFAHYLRAAGYRTALSGKMHFvgPD------QLHGFD-----------------YD------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 163 vlkckalDEVSTEpddprygpvGRQTIEDTGpltakrmetidddiadatvdyikRQHsEGNSFFVWCNFTHMHLYTHVKP 242
Cdd:cd16032 113 -------EEVAFK---------AVQKLYDLA-----------------------RGE-DGRPFFLTVSFTHPHDPYVIPQ 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 243 EskgqaglwqsdYHD-----------AMIDH-DRNVGTVLDVLDELGIAEDTIVLYSTDNGP---HRNTWPDggMTPFrs 307
Cdd:cd16032 153 E-----------YWDlyvrrarrayyGMVSYvDDKVGQLLDTLERTGLADDTIVIFTSDHGDmlgERGLWYK--MSFF-- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 308 ekdtnwEGAFRVPELIRWPGKIKAGSVSnEIIQHHDWLPTLLAAAGDpdiseklkkghkiGDTEYKVHIDGYNLLPYLTG 387
Cdd:cd16032 218 ------EGSARVPLIISAPGRFAPRRVA-EPVSLVDLLPTLVDLAGG-------------GTAPHVPPLDGRSLLPLLEG 277
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039668828 388 EVEHSPRRGFFYFSDDG---DLVAMRFENWKAVFleqrCPGtlqvwaEPfthlrlPKLYNLRTDP 449
Cdd:cd16032 278 GDSGGEDEVISEYLAEGavaPCVMIRRGRWKFIY----CPG------DP------DQLFDLEADP 326
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-364 |
2.43e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 118.88 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYsdGLMGYHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGM------SKVGV 78
Cdd:cd16149 1 PNILFILTDDQGPWALGCY--GNSEAVTPNLDRLAAEGVRFENFFCTSPvCSPARASLLTGRMPSQHGIhdwiveGSHGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 79 PGVDIGWAAEDPTIAELLKPLGYATGQFGKNHFGDlnkflptvhgfdeffgnlyhlnaeeepenfdyphadqfpqlhefa 158
Cdd:cd16149 79 TKKPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLGD--------------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 159 lprgvlkckaldevstepddprygpvgrqtiedtgpltakrmetidddiaDAtVDYIKRQHSEGNSFFVWCNFTHMHlyt 238
Cdd:cd16149 114 --------------------------------------------------DA-ADFLRRRAEAEKPFFLSVNYTAPH--- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 239 hvKPeskgqaglWQsdYHDAMIDHDRNVGTVLDVLDELGIAEDTIVLYSTDNG---PHRNTWPDG-GMTPFrsekdtN-W 313
Cdd:cd16149 140 --SP--------WG--YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGfnmGHHGIWGKGnGTFPL------NmY 201
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1039668828 314 EGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGDPDISEKLKKG 364
Cdd:cd16149 202 DNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPG 252
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-451 |
1.06e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 115.01 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYSDGLMgyHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGM-SKVGVPGVDI 83
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIV--KTPNIDRLAAEGVRFTNAYTPSPvCCPARASLLTGLYPHEHGVlNNVENAGAYS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 84 GWAAED-PTIAELLKPLGYATGQFGKNHFGDLNkfLPTVHGFDEffgnlyhlnaeeepenfdyphadqfpqlhefalprg 162
Cdd:cd16033 79 RGLPPGvETFSEDLREAGYRNGYVGKWHVGPEE--TPLDYGFDE------------------------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 163 vlkckaldevstepddprYGPVgrqtiedtgpltakrMETIDDDIADATVDYIKRQHSEGNSFFVWCNFTHMHL------ 236
Cdd:cd16033 121 ------------------YLPV---------------ETTIEYFLADRAIEMLEELAADDKPFFLRVNFWGPHDpyippe 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 237 --YTHVKPESkgqAGLWQSdYHDAMIDH-----------------------------------DRNVGTVLDVLDELGIA 279
Cdd:cd16033 168 pyLDMYDPED---IPLPES-FADDFEDKpyiyrrerkrwgvdtedeedwkeiiahywgyitliDDAIGRILDALEELGLA 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 280 EDTIVLYSTDNG----PHRnTWpDGGMTPFrsekdtnwEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGdp 355
Cdd:cd16033 244 DDTLVIFTSDHGdalgAHR-LW-DKGPFMY--------EETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAG-- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 356 diseklkkghkiGDTEYKVhiDGYNLLPYLTGEVEHSPRRGFFyFSDDGDLV-----AMRFENWKAVF-LEQRCpgtlqv 429
Cdd:cd16033 312 ------------VDVPPKV--DGRSLLPLLRGEQPEDWRDEVV-TEYNGHEFylpqrMVRTDRYKYVFnGFDID------ 370
|
490 500
....*....|....*....|..
gi 1039668828 430 waepfthlrlpKLYNLRTDPFE 451
Cdd:cd16033 371 -----------ELYDLESDPYE 381
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
5-451 |
3.07e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 106.93 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 5 KPNIVVIWGDDIGITNLSCYsdglmGYH---TPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQsvYRTgmsKVGVPG 80
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCY-----GQPldlTPNLDALAEEGVLFENAFTPQPvCGPARACLQTGL--YPT---ETGCFR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 81 VDIGWAAEDPTIAELLKPLGYATGQFGKnhfgdlnkflptvhgfdeffgnlYHLNaeeepenfdyphadqfpqlhefalp 160
Cdd:cd16152 71 NGIPLPADEKTLAHYFRDAGYETGYVGK-----------------------WHLA------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 161 rgvlkckaldevstepddpRYgpvgrqtiedtgpltakRMetidDDIADATVDYIkRQHSEGNSFFVWCNFT--HM--HL 236
Cdd:cd16152 103 -------------------GY-----------------RV----DALTDFAIDYL-DNRQKDKPFFLFLSYLepHHqnDR 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 237 YTHVKPES--------------KGQAGLWQSDYHD--AMIDH-DRNVGTVLDVLDELGIAEDTIVLYSTDNGPH---RNt 296
Cdd:cd16152 142 DRYVAPEGsaerfanfwvppdlAALPGDWAEELPDylGCCERlDENVGRIRDALKELGLYDNTIIVFTSDHGCHfrtRN- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 297 wpdggmtpfRSEKDTNWEGAFRVPELIRWPGkIKAGSVSNEIIQHHDWLPTLLAAAGDPdiseklkkghkIGDTeykvhI 376
Cdd:cd16152 221 ---------AEYKRSCHESSIRVPLVIYGPG-FNGGGRVEELVSLIDLPPTLLDAAGID-----------VPEE-----M 274
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039668828 377 DGYNLLPYLTGEVEHSPRRGFFYFSDDGDLVAMRFENWK-AVFLEQRCPgtlqvWAEPFTHLRLPK-LYNLRTDPFE 451
Cdd:cd16152 275 QGRSLLPLVDGKVEDWRNEVFIQISESQVGRAIRTDRWKySVAAPDKDG-----WKDSGSDVYVEDyLYDLEADPYE 346
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-449 |
4.43e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 105.70 E-value: 4.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYSDGLMgyHTPNIDRIAAEGMRFTDSYgEQS--CTAGRAAFISGQSVYRTGmskvgVPGVDI 83
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVV--RTPNLDRLAARGTRFENAY-TPSpiCVPSRASFLTGRYVHETG-----VWDNAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 84 GWAAEDPTIAELLKPLGYATGQFGKNHFgdlnkflptvhgfdeffgnlyhlNAEEEPENFDYphadqfpqlhefalprgv 163
Cdd:cd16037 73 PYDGDVPSWGHALRAAGYETVLIGKLHF-----------------------RGEDQRHGFRY------------------ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 164 lkckaldevstepddprygpvgrqtiedtgpltakrmetiDDDIADATVDYIKRQHSEGNSFFVWCNFTHMHLYTHVKPE 243
Cdd:cd16037 112 ----------------------------------------DRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQE 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 244 skgqagLWQ-------SDYHdAMID-HDRNVGTVLDVLDELGIAEDTIVLYSTDNGPH---RNTWpdggmtpfrsEKDTN 312
Cdd:cd16037 152 ------FYDlyvrrarAAYY-GLVEfLDENIGRVLDALEELGLLDNTLIIYTSDHGDMlgeRGLW----------GKSTM 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 313 WEGAFRVPELIRWPGkIKAGSVSNEIIQHHDWLPTLLAAAGdpdiseklkkghkigdTEYKVHIDGYNLLPYLTGEVEHS 392
Cdd:cd16037 215 YEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAG----------------APPPPDLDGRSLLPLAEGPDDPD 277
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 393 pRRGFFYFSDDGDLVAM---RFENWKAVFLEqrcpgtlqvwAEPfthlrlPKLYNLRTDP 449
Cdd:cd16037 278 -RVVFSEYHAHGSPSGAfmlRKGRWKYIYYV----------GYP------PQLFDLENDP 320
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
5-467 |
1.91e-24 |
|
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: 104.57 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 5 KPNIVVIWGDDIGITNLSCYsdGLMGYHTPNIDRIAAEGMRFTDSY--GEQS---CTAGRAAFISGQSVYRTGMSKVGVp 79
Cdd:cd16155 2 KPNILFILADDQRADTIGAL--GNPEIQTPNLDRLARRGTSFTNAYnmGGWSgavCVPSRAMLMTGRTLFHAPEGGKAA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 80 gvdigWAAEDPTIAELLKPLGYATGQFGKNHfgdlnkflptvhgfdeffgNLYHLNAEEEPEnfDYPHADQfPQLHEFAL 159
Cdd:cd16155 79 -----IPSDDKTWPETFKKAGYRTFATGKWH-------------------NGFADAAIEFLE--EYKDGDK-PFFMYVAF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 160 prgvlkckaldevsTEPDDPRYGPVGRQTIEDTGPLTAKRmetidddiadatvdyikrqhsegnsffvwcNFTHMHLYTH 239
Cdd:cd16155 132 --------------TAPHDPRQAPPEYLDMYPPETIPLPE------------------------------NFLPQHPFDN 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 240 VKPESKGQAGLW-----------QSDYHdAMIDH-DRNVGTVLDVLDELGIAEDTIVLYSTDN----GPHrntwpdGGMT 303
Cdd:cd16155 168 GEGTVRDEQLAPfprtpeavrqhLAEYY-AMITHlDAQIGRILDALEASGELDNTIIVFTSDHglavGSH------GLMG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 304 pfrseKDTNWEGAFRVPELIRWPGkIKAGSVSNEIIQHHDWLPTLLAAAGDPdISEklkkghkigdteykvHIDGYNLLP 383
Cdd:cd16155 241 -----KQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIE-IPE---------------SVEGKSLLP 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 384 YLTGEVEhsPRRGFFYFSDDGDLVAMRFENWKavfLEQRCPGTlqvwaepfthlRLPKLYNLRTDPFEFADVTSNTYYEW 463
Cdd:cd16155 299 VIRGEKK--AVRDTLYGAYRDGQRAIRDDRWK---LIIYVPGV-----------KRTQLFDLKKDPDELNNLADEPEYQE 362
|
....
gi 1039668828 464 LLRH 467
Cdd:cd16155 363 RLKK 366
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
21-468 |
3.02e-24 |
|
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: 105.42 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 21 LSCYSDGLMgyHTPNIDRIAAEGMRFTDSYGeQS--CTAGRAAFISGQSVYRTGMSKVGVPgvdigWAAEDPTIAELLKP 98
Cdd:cd16028 16 LSCLGHPLV--KTPNLDRLAAEGVRFRNHYT-QAapCGPSRASLYTGRYLMNHRSVWNGTP-----LDARHLTLALELRK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 99 LGYATGQFGKNH----FGDLNKFLPTVHGfdeffgnlYHLnaeeEPENFDYP-HADQFP-QLHEFALprgvLKCKALDEV 172
Cdd:cd16028 88 AGYDPALFGYTDtspdPRGLAPLDPRLLS--------YEL----AMPGFDPVdRLDEYPaEDSDTAF----LTDRAIEYL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 173 STEPDDP----------------------RYGPvgrqtiEDTGPltAKRMETIDDDIADATVDYIKRQHSEGNSFFvwcn 230
Cdd:cd16028 152 DERQDEPwflhlsyirphppfvapapyhaLYDP------ADVPP--PIRAESLAAEAAQHPLLAAFLERIESLSFS---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 231 fTHMHLYTHVKPESKGQaglWQSDYHDAMIDHDRNVGTVLDVLDELGIAEDTIVLYSTDNGPHrntWPDGGMTpfrsEKD 310
Cdd:cd16028 220 -PGAANAADLDDEEVAQ---MRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQ---LGDHWLW----GKD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 311 TNWEGAFRVPELIRWPG---KIKAGSVSNEIIQHHDWLPTLLAAAGDPDISeklkkghkigdteykvHIDGYNLLPYLTG 387
Cdd:cd16028 289 GFFDQAYRVPLIVRDPRreaDATRGQVVDAFTESVDVMPTILDWLGGEIPH----------------QCDGRSLLPLLAG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 388 EVEHSPRRGFFYFSDDGD------------------LVAMRFENWKAVFleqrcpgtlqvwaepFTHLRlPKLYNLRTDP 449
Cdd:cd16028 353 AQPSDWRDAVHYEYDFRDvstrrpqealglspdecsLAVIRDERWKYVH---------------FAALP-PLLFDLKNDP 416
|
490 500 510
....*....|....*....|....*....|.
gi 1039668828 450 FEFADVTSNTYYE------------WLLRHD 468
Cdd:cd16028 417 GELRDLAADPAYAavvlryaqkllsWRMRHA 447
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-353 |
7.89e-24 |
|
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: 100.70 E-value: 7.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVI----W-GDdigitNLSCYsdglmGYH---TPNIDRIAAEGMRFTDSY-GEQSCTAGRAAFISGQSVYRTGMSKV 76
Cdd:cd16148 1 MNVILIvidsLrAD-----HLGCY-----GYDrvtTPNLDRLAAEGVVFDNHYsGSNPTLPSRFSLFTGLYPFYHGVWGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 77 GVPgvdigwaAEDPTIAELLKPLGYATGQFGKNHFgdlnkfLPTVHGFDEFFgnlyhlnaeEEPENFDYPHADQfpqlhe 156
Cdd:cd16148 71 PLE-------PDDPTLAEILRKAGYYTAAVSSNPH------LFGGPGFDRGF---------DTFEDFRGQEGDP------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 157 falprgvlkckaldevSTEPDDPrygpvgrqtiedtgpltakrmetiDDDIADATVDYIKRQHSEGNsFFVWCNF--TH- 233
Cdd:cd16148 123 ----------------GEEGDER------------------------AERVTDRALEWLDRNADDDP-FFLFLHYfdPHe 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 234 MHLYthvkpeskgQAGLWQSDYHdamidhdrnVGTVLDVLDELGIAEDTIVLYSTDNGPH---RNTWPDGGMTPfrsekd 310
Cdd:cd16148 162 PYLY---------DAEVRYVDEQ---------IGRLLDKLKELGLLEDTLVIVTSDHGEEfgeHGLYWGHGSNL------ 217
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1039668828 311 tnWEGAFRVPELIRWPGKIKAGSVSnEIIQHHDWLPTLLAAAG 353
Cdd:cd16148 218 --YDEQLHVPLIIRWPGKEPGKRVD-ALVSHIDIAPTLLDLLG 257
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
5-451 |
1.98e-22 |
|
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: 99.16 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 5 KPNIVVIWGDDigitnLScYSDGLMGYHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGMSKVGVP--GV 81
Cdd:cd16147 1 RPNIVLILTDD-----QD-VELGSMDPMPKTKKLLADQGTTFTNAFVTTPlCCPSRASILTGQYAHNHGVTNNSPPggGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 82 DIGWAAEDP--TIAELLKPLGYATGQFGK--NHFGDLNKFLPTVHGFDEFFG------NLYHLNAEEEPENfdypHADQF 151
Cdd:cd16147 75 PKFWQNGLErsTLPVWLQEAGYRTAYAGKylNGYGVPGGVSYVPPGWDEWDGlvgnstYYNYTLSNGGNGK----HGVSY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 152 PQLHefalprgvlkckaldevstepddprygpvgrQTiedtgpltakrmetidDDIADATVDYIKRQHSEGNSFFVWCNF 231
Cdd:cd16147 151 PGDY-------------------------------LT----------------DVIANKALDFLRRAAADDKPFFLVVAP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 232 T-----------HMHLYTHVKPES----------------KGQAGLWQSdyHDAMIDH------------DRNVGTVLDV 272
Cdd:cd16147 184 PaphgpftpaprYANLFPNVTAPPrpppnnpdvsdkphwlRRLPPLNPT--QIAYIDElyrkrlrtlqsvDDLVERLVNT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 273 LDELGIAEDTIVLYSTDNG----PHRntWPDGGMTPFrsEKDTnwegafRVPELIRWPGkIKAGSVSNEIIQHHDWLPTL 348
Cdd:cd16147 262 LEATGQLDNTYIIYTSDNGyhlgQHR--LPPGKRTPY--EEDI------RVPLLVRGPG-IPAGVTVDQLVSNIDLAPTI 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 349 LAAAGDPDiseklkkghkigdteyKVHIDGynllpyltgeveHSPRRgffyfSDDGDLVAMRFENWKAVFLEqrcpgtlQ 428
Cdd:cd16147 331 LDLAGAPP----------------PSDMDG------------RSCGD-----SNNNTYKCVRTVDDTYNLLY-------F 370
|
490 500
....*....|....*....|...
gi 1039668828 429 VWAEPFThlrlpKLYNLRTDPFE 451
Cdd:cd16147 371 EWCTGFR-----ELYDLTTDPYQ 388
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
5-461 |
3.68e-22 |
|
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: 98.80 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 5 KPNIVVIWGDDIgitN--LSCYSDGLMgyHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGMSKVGVPGV 81
Cdd:cd16030 2 KPNVLFIAVDDL---RpwLGCYGGHPA--KTPNIDRLAARGVLFTNAYCQQPvCGPSRASLLTGRRPDTTGVYDNNSYFR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 82 DIGWAAedPTIAELLKPLGYATGQFGKnhfgdlnkflptvhgfdeffgnLYH---LNAEEEPENFDYPHADQFPQLH--- 155
Cdd:cd16030 77 KVAPDA--VTLPQYFKENGYTTAGVGK----------------------IFHpgiPDGDDDPASWDEPPNPPGPEKYppg 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 156 --EFALPRGVLKCKALD-EVSTEPDDprygpvgrqtiedtgpltakrmETIDDDIADATVDYIKRQHSEGNSFFVWCNF- 231
Cdd:cd16030 133 klCPGKKGGKGGGGGPAwEAADVPDE----------------------AYPDGKVADEAIEQLRKLKDSDKPFFLAVGFy 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 232 ------------------THMHLYTHVKPE--------------SKGQAGLWQSDYHDAMIDH----------------- 262
Cdd:cd16030 191 kphlpfvapkkyfdlyplESIPLPNPFDPIdlpevawndlddlpKYGDIPALNPGDPKGPLPDeqarelrqayyasvsyv 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 263 DRNVGTVLDVLDELGIAEDTIVLYSTDNGPH---RNTWpdggmtpfrsEKDTNWEGAFRVPELIRWPGKIKAGSVSNEII 339
Cdd:cd16030 271 DAQVGRVLDALEELGLADNTIVVLWSDHGWHlgeHGHW----------GKHTLFEEATRVPLIIRAPGVTKPGKVTDALV 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 340 QHHDWLPTLLAAAGdpdisekLKKghkigdteyKVHIDGYNLLPYLTGEVEHSPRRGF-FYFSDDGDLVAMRFENW---- 414
Cdd:cd16030 341 ELVDIYPTLAELAG-------LPA---------PPCLEGKSLVPLLKNPSAKWKDAAFsQYPRPSIMGYSIRTERYryte 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1039668828 415 -----KAVFLEqrcpgtlqvwaepfthlrlpkLYNLRTDPFEFADVTSNTYY 461
Cdd:cd16030 405 wvdfdKVGAEE---------------------LYDHKNDPNEWKNLANDPEY 435
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
5-381 |
8.94e-22 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 95.13 E-value: 8.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 5 KPNIVVIWGDDIGITNLSCY-------SDGLMGY-HTPNIDRIAAEGMRFTDSY-GEQSCTAGRAAFISGQSVYRTGMSK 75
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYnnahtgkSESRLGYvESPNIDALAAEGVLFTNAYcNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 76 VGV--PGVDIGWaaedPTIAELLKPLGYATGQFGKNHFGDLNKFLPtvhgfdeffgnlyhlNAEEEPENFDyphadqfpq 153
Cdd:cd16153 81 FEAahPALDHGL----PTFPEVLKKAGYQTASFGKSHLEAFQRYLK---------------NANQSYKSFW--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 154 lhefalprgvlkckaldevstepDDPRYGPVGRQtiedtgpltakrmetidddiadatvdyikrqhsegnSFFVWCNFTH 233
Cdd:cd16153 133 -----------------------GKIAKGADSDK------------------------------------PFFVRLSFLQ 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 234 MHlyTHVKPESKgqaglWQS--DYHD--AMIDHdrNVGTVLDVLDELGIA---EDTIVLYSTDNGPHRNtwpDGGMtpfr 306
Cdd:cd16153 154 PH--TPVLPPKE-----FRDrfDYYAfcAYGDA--QVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLG---EQGI---- 217
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039668828 307 SEKDTNWEGAFRVPELIRWPGKIK--AGSVSNEIIQHHDWLPTLLAAAGdpdiseklkkghkIGDTEYKvHIDGYNL 381
Cdd:cd16153 218 LAKFTFWPQSHRVPLIVVSSDKLKapAGKVRHDFVEFVDLAPTLLAAAG-------------VDVDAPD-YLDGRDL 280
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
4-355 |
4.41e-20 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 93.19 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 4 GKPNIVVIWGDDIGITNLSCYSDGLMgyHTPNIDRIAAEGMRFTDSYGE-QSCTAGRAAFISGQSVYRTGMskvgvpgvd 82
Cdd:PRK13759 5 KKPNIILIMVDQMRGDCLGCNGNKAV--ETPNLDMLASEGYNFENAYSAvPSCTPARAALLTGLSQWHHGR--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 83 IGWAAEDP-----TIAELLKPLGYATGQFGKNHfgdlnkFLP--TVHGFDEFF---GNLYHlNAEEEPENFDYpHADQFP 152
Cdd:PRK13759 74 VGYGDVVPwnyknTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHNVLlhdGYLHS-GRNEDKSQFDF-VSDYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 153 QLHEFALPRGV------LKCKALdEVSTEPDDPRYGP---VGRQTIE------DTGPLTAK-----------------RM 200
Cdd:PRK13759 146 WLREKAPGKDPdltdigWDCNSW-VARPWDLEERLHPtnwVGSESIEflrrrdPTKPFFLKmsfarphspydppkryfDM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 201 eTIDDDIADATV---DYIKRQHSEGNSFFVWcnfthmhlYTHVKPES--KGQAGLWQSDYHdamIDHdrNVGTVLDVLDE 275
Cdd:PRK13759 225 -YKDADIPDPHIgdwEYAEDQDPEGGSIDAL--------RGNLGEEYarRARAAYYGLITH---IDH--QIGRFLQALKE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 276 LGIAEDTIVLYSTDNGphrNTWPDGGMtpFRseKDTNWEGAFRVPELIRWPG---KIKAGSVSNEIIQHHDWLPTLLAAA 352
Cdd:PRK13759 291 FGLLDNTIILFVSDHG---DMLGDHYL--FR--KGYPYEGSAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLA 363
|
...
gi 1039668828 353 GDP 355
Cdd:PRK13759 364 GGT 366
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-451 |
2.45e-19 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 89.72 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYSDGLMGYHTPNIDRIAAEGMRFTDSYGEQSCTAGRAAFISGQSVYRTgmskvGVPGVDIGW 85
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRT-----GVLAVPDEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 86 AAEDPTIAELLK----PLGYATGQFGKNHFGdlnkflptvhgfdeffGNLYHLNAeeePENFDYphadqfpqlheFAlpr 161
Cdd:cd16154 76 LLSEETLLQLLIkdatTAGYSSAVIGKWHLG----------------GNDNSPNN---PGGIPY-----------YA--- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 162 GVLkckaldeVSTEPDDPRYGPV--GRQTIEDtgpltakrmETIDDDIADATVDYIKRQHSegnSFFVWCNFTHMHLYTH 239
Cdd:cd16154 123 GIL-------GGGVQDYYNWNLTnnGQTTNST---------EYATTKLTNLAIDWIDQQTK---PWFLWLAYNAPHTPFH 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 240 VKPE---SKGQAGLWQS------DYHDAMIDH-DRNVGTVLDVLDElGIAEDTIVLYSTDNG-PHRNTwpdggMTPFRSE 308
Cdd:cd16154 184 LPPAelhSRSLLGDSADieanprPYYLAAIEAmDTEIGRLLASIDE-EERENTIIIFIGDNGtPGQVV-----DLPYTRN 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 309 --KDTNWEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGDpDISEklkkghkigdteykVHiDGYNLLPYLT 386
Cdd:cd16154 258 haKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGV-DAAE--------------IH-DSVSFKPLLS 321
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039668828 387 GEVEHSPRRGF-FYFSDDGDLVAMRFENWKAVFLEQrcpGTlqvwaepfthlrlPKLYNLRTDPFE 451
Cdd:cd16154 322 DVNASTRQYNYtEYESPTTTGWATRNQYYKLIESEN---GQ-------------EELYDLINDPSE 371
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
6-355 |
3.02e-15 |
|
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: 77.81 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYSDGLMgyHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQSVYRTGMSkvgvpGVDIG 84
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAM--KTPNLDRLAAEGVRFDSAYTTQPvCGPARSGLFTGLYPHTNGSW-----TNCMA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 85 WAAEDPTIAELLKPLGYATGQFGKNHF--GDlnkflptvhgfdeFFGNlyhlnaEEEPENFDyphADQFPQLHEFalprg 162
Cdd:cd16156 74 LGDNVKTIGQRLSDNGIHTAYIGKWHLdgGD-------------YFGN------GICPQGWD---PDYWYDMRNY----- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 163 vlkckaLDEVStepDDPRYgpVGRQtiedtgPLTAKRMETIDDD------IADATVDYIkRQHSEGNSFFV--------- 227
Cdd:cd16156 127 ------LDELT---EEERR--KSRR------GLTSLEAEGIKEEftyghrCTNRALDFI-EKHKDEDFFLVvsydephhp 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 228 ----------------------WCNFT----HMHLYTHVKPESKGQAGLWQSDYHDAMIDH-DRNVGTVLDVLDElgIAE 280
Cdd:cd16156 189 flcpkpyasmykdfefpkgenaYDDLEnkplHQRLWAGAKPHEDGDKGTIKHPLYFGCNSFvDYEIGRVLDAADE--IAE 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039668828 281 DTIVLYSTDNGPHRNTWPDGGMTPFRSEKDTNwegafrVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGDP 355
Cdd:cd16156 267 DAWVIYTSDHGDMLGAHKLWAKGPAVYDEITN------IPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIP 335
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-451 |
7.69e-14 |
|
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: 73.42 E-value: 7.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIWGDDIGITNLSCYsdGLMGYHTPNIDRIAAEGMRFTDSYGEQS-CTAGRAAFISGQ----SVYRTgMSKVGVPg 80
Cdd:cd16150 1 PNIVIFVADQLRADSLGHL--GNPAAVTPNLDALAAEGVRFSNAYCQNPvCSPSRCSFLTGWyphvNGHRT-LHHLLRP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 81 vdigwaaEDPTIAELLKPLGYATGQFGKNHFGDLNKFLPTVHGFDEFF--GNLYHLNAEEEPENF------DYPHAdqfp 152
Cdd:cd16150 77 -------DEPNLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYCDSDEACvrTAIDWLRNRRPDKPFclylplIFPHP---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 153 qlhefalPRGVlkckaldevsTEPDDPRYG----PVGRQTIEDTG--PLTAKRMETI-DDDIADATVDYIKRQhsegnsf 225
Cdd:cd16150 146 -------PYGV----------EEPWFSMIDreklPPRRPPGLRAKgkPSMLEGIEKQgLDRWSEERWRELRAT------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 226 fvwcnfthmhlythvkpeskgqaglwqsdYHdAMIDH-DRNVGTVLDVLDELGIAEDTIVLYSTDNGPHRNtwpDGGMTp 304
Cdd:cd16150 202 -----------------------------YL-GMVSRlDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTG---DYGLV- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 305 frsEKdtnWEGAF-----RVPELIRWPGKIKaGSVSNEIIQHHDWLPTLLAAAGDPdiseklkkghkigdTEYkVHIdGY 379
Cdd:cd16150 248 ---EK---WPNTFedcltRVPLIIKPPGGPA-GGVSDALVELVDIPPTLLDLAGIP--------------LSH-THF-GR 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 380 NLLPYLTGEVEHsPRR-----GFFYFS----------------------DDGDL----VAMRFENWKAVFLEQrcpgtlq 428
Cdd:cd16150 305 SLLPVLAGETEE-HRDavfseGGRLHGeeqamegghgpydlkwprllqqEEPPEhtkaVMIRTRRYKYVYRLY------- 376
|
490 500
....*....|....*....|...
gi 1039668828 429 vwaEPfthlrlPKLYNLRTDPFE 451
Cdd:cd16150 377 ---EP------DELYDLEADPLE 390
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
6-403 |
5.39e-13 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 69.93 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVIwgddigITN----LSCYSDGLMGYHTPNIDRIAAEGMRFTDSY-GEQSCTAGRAAFISGQSVYRTGMSKVgvpg 80
Cdd:cd16035 1 PNILLI------LTDqeryPPPWPAGWAALNLPARERLAANGLSFENHYtAACMCSPSRSTLYTGLHPQQTGVTDT---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 81 VDIGWAAED----PTIAELLKPLGYATGQFGKnhfgdlnkflptvhgfdeffgnlYHLNAeeepenfdyphadqfpqlhe 156
Cdd:cd16035 71 LGSPMQPLLspdvPTLGHMLRAAGYYTAYKGK-----------------------WHLSG-------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 157 faLPRGVLKckaldevstepddprygpvgrqtiedtgpltakrmetIDDDIADATVDYIK---RQHSEGNSFFVWCNFTH 233
Cdd:cd16035 108 --AAGGGYK-------------------------------------RDPGIAAQAVEWLRergAKNADGKPWFLVVSLVN 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 234 MH--LYThvkPESKGQAGLWQSDYHDAMIDHDRNVGTVLDVLDELGIAEDTIVLYSTDNG----PHrntwpdGGMtpfrs 307
Cdd:cd16035 149 PHdiMFP---PDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGemggAH------GLR----- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 308 EKDTN-WEGAFRVPELIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAGDPDISEKLK----KGHkigdteykvhidgyNLL 382
Cdd:cd16035 215 GKGFNaYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATEapplPGR--------------DLS 280
|
410 420
....*....|....*....|.
gi 1039668828 383 PYLTGEVEHSPRRGFFYFSDD 403
Cdd:cd16035 281 PLLTDADADAVRDGILFTYDR 301
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
210-352 |
4.15e-11 |
|
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: 63.21 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 210 ATVDYIKRQhSEGNSFFVWCNF--THM--HLYTHVKPEskgqaglwqsdYHDAMIDHDRNVGTVLDVLDELGIAEDTIVL 285
Cdd:cd00016 107 GLLKAIDET-SKEKPFVLFLHFdgPDGpgHAYGPNTPE-----------YYDAVEEIDERIGKVLDALKKAGDADDTVII 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039668828 286 YSTDNGPHRNtwpDGGMTPFRSEKDTNWEGAFRVPELIRWPGkIKAGSVSNEIIQHHDWLPTLLAAA 352
Cdd:cd00016 175 VTADHGGIDK---GHGGDPKADGKADKSHTGMRVPFIAYGPG-VKKGGVKHELISQYDIAPTLADLL 237
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
6-353 |
3.05e-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: 58.08 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 6 PNIVVI----WGDDigitnlscYSDGLMGYH--TPNIDRIAAEGMRFTDSYgeQSCTAGR-----AAFISGQSVYRTG-M 73
Cdd:cd16015 1 PNVIVIllesFSDP--------YIDKDVGGEdlTPNLNKLAKEGLYFGNFY--SPGFGGGtangeFEVLTGLPPLPLGsG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 74 SKVGVPGVDIgwaaedPTIAELLKPLGYATgQF---GKNHFGDLNKFLPTvHGFDEFFGnLYHLNAEEEPENFDYPHadq 150
Cdd:cd16015 71 SYTLYKLNPL------PSLPSILKEQGYET-IFihgGDASFYNRDSVYPN-LGFDEFYD-LEDFPDDEKETNGWGVS--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 151 fpqlhefalprgvlkckaldevstepddprygpvgrqtiedtgpltakrmetiDDDIADATVDYIKRQHSEgnSFFVwCN 230
Cdd:cd16015 139 -----------------------------------------------------DESLFDQALEELEELKKK--PFFI-FL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 231 FT---HM------HLYTHVKPESKGQAGLwqSDYHDAMIDHDRNVGTVLDVLDELGIAEDTIVLYSTDNGPhrntwpdgG 301
Cdd:cd16015 163 VTmsnHGpydlpeEKKDEPLKVEEDKTEL--ENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLP--------S 232
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039668828 302 MTPFRSEKDTNWEGAFRVPeLIRWPGKIKAGSVSNEIIQHHDWLPTLLAAAG 353
Cdd:cd16015 233 LGSDYDETDEDPLDLYRTP-LLIYSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
5-353 |
9.24e-08 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 54.66 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 5 KPNIVVI----WGDDigitnlscYSDGLMGYH--TPNIDRIAAEGMRFTDSY--------GEQSCTAGrAAFISGQSVYR 70
Cdd:COG1368 234 KPNVVVIllesFSDF--------FIGALGNGKdvTPFLDSLAKESLYFGNFYsqggrtsrGEFAVLTG-LPPLPGGSPYK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 71 TGmskvgvpgvdigWAAEDPTIAELLKPLGYATgQF---GKNHFGDLNKFLPTvHGFDEFFGnlyhlnaeeePENFDYPH 147
Cdd:COG1368 305 RP------------GQNNFPSLPSILKKQGYET-SFfhgGDGSFWNRDSFYKN-LGFDEFYD----------REDFDDPF 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 148 ADQFPqlhefalprgvlkckaldeVStepddprygpvgrqtiedtgpltakrmetiDDDIADATVDYIKRQhseGNSFFV 227
Cdd:COG1368 361 DGGWG-------------------VS------------------------------DEDLFDKALEELEKL---KKPFFA 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 228 wCNFT---HM--HL---YTHVKPESKGQAGlwqsDYHDAMIDHDRNVGTVLDVLDELGIAEDTI-VLYstdnGPHRNTWP 298
Cdd:COG1368 389 -FLITlsnHGpyTLpeeDKKIPDYGKTTLN----NYLNAVRYADQALGEFIEKLKKSGWYDNTIfVIY----GDHGPRSP 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1039668828 299 DGGMTPFRSEKdtnwegaFRVPELIrWPGKIKAGSVSNEIIQHHDWLPTLLAAAG 353
Cdd:COG1368 460 GKTDYENPLER-------YRVPLLI-YSPGLKKPKVIDTVGSQIDIAPTLLDLLG 506
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
204-349 |
1.46e-07 |
|
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: 54.14 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 204 DDDIADATVDYIKRQhSEGNSFFVWCNFTHMHLYTHVKPESK----------------GQAGLWQSDYHDAMIDHDRNVG 267
Cdd:COG3083 363 DRQITAQWLQWLDQR-DSDRPWFSYLFLDAPHAYSFPADYPKpfqpsedcnylaldneSDPTPFKNRYRNAVHYVDSQIG 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 268 TVLDVLDELGIAEDTIVLYSTDNGphrntwpdggmTPFRSEKDTNWE--GAF-----RVPELIRWPGKiKAGSVSNeIIQ 340
Cdd:COG3083 442 RVLDTLEQRGLLENTIVIITADHG-----------EEFNENGQNYWGhnSNFsryqlQVPLVIHWPGT-PPQVISK-LTS 508
|
....*....
gi 1039668828 341 HHDWLPTLL 349
Cdd:COG3083 509 HLDIVPTLM 517
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
185-396 |
4.20e-06 |
|
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: 49.08 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 185 GRQTIEDTGPLTAKRMETIDDDIADATVDYIKRQ-HSEGNSFFVWCNFTHMHLY-THVKPESKGQAGLWQSDYHDAMIDH 262
Cdd:cd16171 126 GRPTVNLVGDRSTVRVMLKDWQNTDKAVHWIRKEaPNLTQPFALYLGLNLPHPYpSPSMGENFGSIRNIRAFYYAMCAET 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 263 DRNVGTVLDVLDELGIAEDTIVLYSTDNG----PHRNTWpdggmtpfrseKDTNWEGAFRVPELIRWPGkIKAGSVSNEI 338
Cdd:cd16171 206 DAMLGEIISALKDTGLLDKTYVFFTSDHGelamEHRQFY-----------KMSMYEGSSHVPLLIMGPG-IKAGQQVSDV 273
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039668828 339 IQHHDWLPTLLAAAGDPDISeklkkghkigdteykvHIDGYNLLPYLTGEVEH-SPRRG 396
Cdd:cd16171 274 VSLVDIYPTMLDIAGVPQPQ----------------NLSGYSLLPLLSESSIKeSPSRV 316
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
392-500 |
1.57e-04 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 41.53 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039668828 392 SPRRGFFYFSDDgDLVAMRFENWKAVFLEQR--------CPGTlqvwAEPFTHLRLPKLYNLRTDPFEFADVTSNTyyew 463
Cdd:pfam14707 1 SPHEFLFHYCGA-ALHAVRWGPYKAHFFTPSfdppgaegCYGS----KVPVTHHDPPLLFDLERDPSEKYPLSPDS---- 71
|
90 100 110
....*....|....*....|....*....|....*..
gi 1039668828 464 lLRHDYFIFYMTAMASKFLETFKEFPPRHAPASFSVD 500
Cdd:pfam14707 72 -PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWD 107
|
|
| |
