|
Name |
Accession |
Description |
Interval |
E-value |
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
48-427 |
0e+00 |
|
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: 616.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGMTNKRNYVKFGMLDRKQTTFAH 127
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQKTFGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 128 LLKSAGYRTCIAGKWQLGS---ELDSPRHFGFEESLLWQHTRGRMDSQKRDTRYPNprlERNGTKEDYDEGEFSSDLFAD 204
Cdd:cd16151 81 LLKDAGYATAIAGKWQLGGgrgDGDYPHEFGFDEYCLWQLTETGEKYSRPATPTFN---IRNGKLLETTEGDYGPDLFAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 205 FLCDFMETNRDQPFLAYYPMALVHCPFCPTPDSEDWDPTShgsKTYKGQPEYFGDMVAYVDKIVGRIDQKLGDLGIRENT 284
Cdd:cd16151 158 FLIDFIERNKDQPFFAYYPMVLVHDPFVPTPDSPDWDPDD---KRKKDDPEYFPDMVAYMDKLVGKLVDKLEELGLRENT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 285 LLIFTGDNGTDKPIVTQTRFGEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPANLTI 364
Cdd:cd16151 235 IIIFTGDNGTHRPITSRTNGREVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270232598 365 DGQSFLPVLQGIEGQGRESMFMWYERNGRPNKAREFARNQRYKLYGDGSFFDVEMDRNEKSPL 427
Cdd:cd16151 315 DGRSFAPQLLGKTGSPRREWIYWYYRNPHKKFGSRFVRTKRYKLYADGRFFDLREDPLEKNPL 377
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
22-449 |
3.01e-100 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 305.26 E-value: 3.01e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 22 ILACSLAFTAASVPADEPspqrsgDRPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRV 100
Cdd:COG3119 4 LLLLLLALLAAAAAAAAA------KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTsPVCSPSRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 101 KLMTGMTNKRNYV------KFGMLDRKQTTFAHLLKSAGYRTCIAGKWQLgseldsprhfgfeesllwqhtrgrmdsqkr 174
Cdd:COG3119 78 SLLTGRYPHRTGVtdngegYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 175 dtrypnprlerngtkedydegeFSSDLFADFLCDFMETNR--DQPFLAYYPMALVHCPFCPTPDSED------------W 240
Cdd:COG3119 128 ----------------------YLTDLLTDKAIDFLERQAdkDKPFFLYLAFNAPHAPYQAPEEYLDkydgkdiplppnL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 241 DPTSHGSKTYKGQPEYFGDMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGtdkpivtqTRFGE--VVGAKGEMVDAG 318
Cdd:COG3119 186 APRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNG--------PSLGEhgLRGGKGTLYEGG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 319 NHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPANLtiDGQSFLPVLQGIEGQGRESMFMWYERNGrPNKAr 398
Cdd:COG3119 258 IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDL--DGRSLLPLLTGEKAEWRDYLYWEYPRGG-GNRA- 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1270232598 399 efARNQRYKL------YGDGSFFDVEMDRNEkspLQSLTDDQKEIRSKLQAKIDSFA 449
Cdd:COG3119 334 --IRTGRWKLiryyddDGPWELYDLKNDPGE---TNNLAADYPEVVAELRALLEAWL 385
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
47-427 |
2.16e-90 |
|
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: 280.22 E-value: 2.16e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKRNyvkfGM-------- 117
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAaAPVCSPSRAALLTGRYPVRV----GLpgvvgppg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 118 ----LDRKQTTFAHLLKSAGYRTCIAGKWQLGSELDS-PRHFGFEE--SLLWQHTRGRMDSQKRDTRYPNPRLERNGTKE 190
Cdd:cd16026 77 skggLPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFlPTRHGFDEyfGIPYSNDMWPFPLYRNDPPGPLPPLMENEEVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 191 DYDEGEFS-SDLFADFLCDFMETNRDQPFLAYYPMALVHCP-FCptpdSEDWDPTSHGSKtykgqpeyFGDMVAYVDKIV 268
Cdd:cd16026 157 EQPADQSSlTQRYTDEAVDFIERNKDQPFFLYLAHTMPHVPlFA----SEKFKGRSGAGL--------YGDVVEELDWSV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 269 GRIDQKLGDLGIRENTLLIFTGDNGtdkPIVTQTRF----GEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFS 344
Cdd:cd16026 225 GRILDALKELGLEENTLVIFTSDNG---PWLEYGGHggsaGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 345 DFLPTMCEVADAEVPANLTIDGQSFLPVLQGIEGQGRESMFmWYERNGRPNKarefARNQRYKL-----YGDGSFFDVEM 419
Cdd:cd16026 302 DLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFF-YYYDGGDLQA----VRSGRWKLhlpttYRTGTDPGGLD 376
|
....*...
gi 1270232598 420 DRNEKSPL 427
Cdd:cd16026 377 PTKLEPPL 384
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
48-446 |
8.01e-89 |
|
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: 276.35 E-value: 8.01e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGMTNKRN-----YVKFGMLDRKQ 122
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTgvwhtILGRERMRLDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 123 TTFAHLLKSAGYRTCIAGKWQLGselDSPRHF----GFEESL-----LWQHTRGRMDSQkrdtrYPNPRLERNGTKEDYd 193
Cdd:cd16146 81 TTLAEVFKDAGYRTGIFGKWHLG---DNYPYRpqdrGFDEVLghgggGIGQYPDYWGND-----YFDDTYYHNGKFVKT- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 194 EGeFSSDLFADFLCDFMETNRDQPFLAYYPMALVHCPF-CPTpdsEDWDPtshgsktYKGQ------PEYFGdMVAYVDK 266
Cdd:cd16146 152 EG-YCTDVFFDEAIDFIEENKDKPFFAYLATNAPHGPLqVPD---KYLDP-------YKDMglddklAAFYG-MIENIDD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 267 IVGRIDQKLGDLGIRENTLLIFTGDNGTDKPivTQTRF-GEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSD 345
Cdd:cd16146 220 NVGRLLAKLKELGLEENTIVIFMSDNGPAGG--VPKRFnAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHID 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 346 FLPTMCEVADAEVPANLTIDGQSFLPVLQGIEGQGRESMFMWY--ERNGRPNKAREFA-RNQRYKLYGDGSF----FDVE 418
Cdd:cd16146 298 LLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLFTHsgRWPPPPKKKRNAAvRTGRWRLVSPKGFqpelYDIE 377
|
410 420
....*....|....*....|....*...
gi 1270232598 419 MDRNEKsplQSLTDDQKEIRSKLQAKID 446
Cdd:cd16146 378 NDPGEE---NDVADEHPEVVKRLKAAYE 402
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
48-448 |
3.95e-88 |
|
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: 275.19 E-value: 3.95e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMT------------NKRNYVK 114
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAaAPVCSPSRASILTGQYparlgitdvipgRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 115 FGM--------LDRKQTTFAHLLKSAGYRTCIAGKWQLG-SELDSPRHFGFEESLlwqHTRGrmdsQKRDTRYPNPRLER 185
Cdd:cd16144 81 TKLipppsttrLPLEEVTIAEALKDAGYATAHFGKWHLGgEGGYGPEDQGFDVNI---GGTG----NGGPPSYYFPPGKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 186 NGTKEDYDEGEFSSDLFADFLCDFMETNRDQPFLAYYPMALVHCPFCPTPDSEDwDPTSHGSKTYKGQ--PEYFGdMVAY 263
Cdd:cd16144 154 NPDLEDGPEGEYLTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELIE-KYEKKKKGLRKGQknPVYAA-MIES 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 264 VDKIVGRIDQKLGDLGIRENTLLIFTGDNG---TDKPIVTQT---RFGevvgaKGEMVDAGNHVTCIAKWPGVIQPQRLT 337
Cdd:cd16144 232 LDESVGRILDALEELGLADNTLVIFTSDNGglsTRGGPPTSNaplRGG-----KGSLYEGGIRVPLIVRWPGVIKPGSVS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 338 SQIIDFSDFLPTMCEVADAEVPANLTIDGQSFLPVLQGIEGQ-GRESMFmWYERNGRPNKAREFA--RNQRYKL---YGD 411
Cdd:cd16144 307 DVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADlPRRALF-WHFPHYHGQGGRPASaiRKGDWKLiefYED 385
|
410 420 430
....*....|....*....|....*....|....*....
gi 1270232598 412 GSF--FDVEMDRNEKsplQSLTDDQKEIRSKLQAKIDSF 448
Cdd:cd16144 386 GRVelYNLKNDIGET---NNLAAEMPEKAAELKKKLDAW 421
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
48-424 |
2.06e-85 |
|
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: 267.92 E-value: 2.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGM----TNKR-NYVKFGM--LD 119
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAgAPVCAPSRASLLTGLhtghTRVRgNSEPGGQdpLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 120 RKQTTFAHLLKSAGYRTCIAGKWQLGSELD--SPRHFGFEESLlwqhtrGRMDSQKRDTRYPnPRLERNGTKEDYDE--- 194
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTpgHPTKQGFDYFY------GYLDQVHAHNYYP-EYLWRNGEKVPLPNnvi 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 195 -------------GEFSSDLFADFLCDFMETNRDQPFLAYYPMALVHCPFCPTPDSEDWD-PTSHGSKTYKGQPE---YF 257
Cdd:cd16145 154 ppldegnnaggggGTYSHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDDGPYKYkPKDPGIYAYLPWPQpekAY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 258 GDMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGTDK---PIVTQTRF---GEVVGAKGEMVDAGNHVTCIAKWPGVI 331
Cdd:cd16145 234 AAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggSEHDPDFFdsnGPLRGYKRSLYEGGIRVPFIARWPGKI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 332 QPQRLTSQIIDFSDFLPTMCEVADAEVPANltIDGQSFLPVLQGIEGQGRESMFMWYERNGRPNKArefARNQRYKLY-- 409
Cdd:cd16145 314 PAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLYWEFYEGGGAQA---VRMGGWKAVrh 388
|
410
....*....|....*....
gi 1270232598 410 --GDGSF--FDVEMDRNEK 424
Cdd:cd16145 389 gkKDGPFelYDLSTDPGET 407
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
48-386 |
5.67e-71 |
|
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: 229.78 E-value: 5.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGS-NGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKRNYVKFG--------M 117
Cdd:cd16143 1 PNIVIILADDLGYGDISCyNPDSKIPTPNIDRLAAEGMRFTDAHSpSSVCTPSRYGLLTGRYPWRSRLKGGvlggfsppL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 118 LDRKQTTFAHLLKSAGYRTCIAGKWqlgseldsprHFGFEESLLWQHTRGRMDSQKRD-TRYPnprleRNGTKE---DYD 193
Cdd:cd16143 81 IEPDRVTLAKMLKQAGYRTAMVGKW----------HLGLDWKKKDGKKAATGTGKDVDySKPI-----KGGPLDhgfDYY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 194 EGEFSS---DLFADFLCDFMETNR--DQPFLAYYPMALVHCPFCPtpdSEDWDPTSHGSKtykgqpeyFGDMVAYVDKIV 268
Cdd:cd16143 146 FGIPASevlPTLTDKAVEFIDQHAkkDKPFFLYFALPAPHTPIVP---SPEFQGKSGAGP--------YGDFVYELDWVV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 269 GRIDQKLGDLGIRENTLLIFTGDNGTDKPIVTQTRF-------GEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQII 341
Cdd:cd16143 215 GRILDALKELGLAENTLVIFTSDNGPSPYADYKELEkfghdpsGPLRGMKADIYEGGHRVPFIVRWPGKIPAGSVSDQLV 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1270232598 342 DFSDFLPTMCEVADAEVPANLTIDGQSFLPVLQGIEGQ-GRESMFM 386
Cdd:cd16143 295 SLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQeVRESLVH 340
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
46-443 |
6.81e-71 |
|
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: 230.49 E-value: 6.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 46 DRPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCY-SQPICTPSRVKLMTGMTNKRNYVKFG---MLDRK 121
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFvTTSICAPSRASILTGQYSHRHGVTDNngpLFDAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 122 QTTFAHLLKSAGYRTCIAGKWQLGSELDSPR-HFGFEESLLWQHTrgrmdsqkrdtrYPNPRLERNGtKEDYDEGeFSSD 200
Cdd:cd16031 81 QPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPpGFDYWVSFPGQGS------------YYDPEFIENG-KRVGQKG-YVTD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 201 LFADFLCDFMETNR-DQPFLAYYPMALVHCPFCPTP-------DSEDWDPTSHGSKTYKGQPEYFGD------------- 259
Cdd:cd16031 147 IITDKALDFLKERDkDKPFCLSLSFKAPHRPFTPAPrhrglyeDVTIPEPETFDDDDYAGRPEWAREqrnrirgvldgrf 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 260 ---------------MVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNG--------TDKpivtqtRFgevvgakgeMVD 316
Cdd:cd16031 227 dtpekyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGfflgehglFDK------RL---------MYE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 317 AGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPANltIDGQSFLPVLQGIEGQGRESMFM--WYERNGRP 394
Cdd:cd16031 292 ESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDWRKEFYyeYYEEPNFH 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270232598 395 NKAREFA-RNQRYKL---YGDGSF---FDVEMDRNEkspLQSLTDD------QKEIRSKLQA 443
Cdd:cd16031 370 NVPTHEGvRTERYKYiyyYGVWDEeelYDLKKDPLE---LNNLANDpeyaevLKELRKRLEE 428
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
48-368 |
6.11e-69 |
|
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: 219.23 E-value: 6.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMTNKR-----NYVKFGMLDRK 121
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVAsPVCSPSRASLLTGRYPHRhgvrgNVGNGGGLPPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 122 QTTFAHLLKSAGYRTCIAGKWqlgseldsprhfgfeesllwqHTRGrmdsqkrdtrypnprlerngtkedydegefssdl 201
Cdd:cd16022 81 EPTLAELLKEAGYRTALIGKW---------------------HDEA---------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 202 fadflCDFMETN-RDQPFLAYYPMALVHCPFcptpdsedwdptshgsktykgqpEYFGdMVAYVDKIVGRIDQKLGDLGI 280
Cdd:cd16022 106 -----IDFIERRdKDKPFFLYVSFNAPHPPF-----------------------AYYA-MVSAIDDQIGRILDALEELGL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 281 RENTLLIFTGDNGtDKPIVTQTRFGevvgaKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPA 360
Cdd:cd16022 157 LDNTLIVFTSDHG-DMLGDHGLRGK-----KGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPE 230
|
....*...
gi 1270232598 361 nlTIDGQS 368
Cdd:cd16022 231 --GLDGRS 236
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
48-448 |
1.66e-68 |
|
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: 222.77 E-value: 1.66e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDyQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGM---TNK--RNYVKFGMLDRK 121
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVV-KTPNLDRLAAEGVRFTNAFTtAPVCSPSRSALLTGLyphQNGahGLRSRGFPLPDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 122 QTTFAHLLKSAGYRTCIAGKWqlgseldsprHFGFEESLLWQHtrgrmdsqkrdtrYPNPRLERNGTKEDYdegefsSDL 201
Cdd:cd16027 80 VKTLPELLREAGYYTGLIGKT----------HYNPDAVFPFDD-------------EMRGPDDGGRNAWDY------ASN 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 202 FADFLcdfMETNRDQPFLAYYPMALVHcpfcptpdsEDWDPTSHGSKTYKGQ----PEYFGD-------------MVAYV 264
Cdd:cd16027 131 AADFL---NRAKKGQPFFLWFGFHDPH---------RPYPPGDGEEPGYDPEkvkvPPYLPDtpevredladyydEIERL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 265 DKIVGRIDQKLGDLGIRENTLLIFTGDNGTDKPivtqtrfgevvGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFS 344
Cdd:cd16027 199 DQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP-----------RAKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 345 DFLPTMCEVADAEVPANLtiDGQSFLPVLQGIEGQGRESMFMWYERNG-RPNKAReFARNQRYKL---YGDGSFFDVEMD 420
Cdd:cd16027 268 DLAPTLLDLAGIEPPEYL--QGRSFLPLLKGEKDPGRDYVFAERDRHDeTYDPIR-SVRTGRYKYirnYMPEELYDLKND 344
|
410 420 430
....*....|....*....|....*....|
gi 1270232598 421 RNEkspLQSLTDD--QKEIRSKLQAKIDSF 448
Cdd:cd16027 345 PDE---LNNLADDpeYAEVLEELRAALDAW 371
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
48-389 |
2.30e-66 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 217.02 E-value: 2.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGS---LDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGmtnkRNYVKFGM------- 117
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGgigRGAPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITG----RHPIRTGLttvglpg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 118 ----LDRKQTTFAHLLKSAGYRTCIAGKWQLGselDSPRHF----GFEEslLWQHTRGRMDsqkrdtrypnprlerngtk 189
Cdd:cd16142 77 spggLPPWEPTLAELLKDAGYATAQFGKWHLG---DEDGRLptdhGFDE--FYGNLYHTID------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 190 edydegefssDLFADFLCDFMETNR--DQPFLAYYPMALVHCPFCPTPDSEdwdptshGSKTYKGQpeyFGDMVAYVDKI 267
Cdd:cd16142 133 ----------EEIVDKAIDFIKRNAkaDKPFFLYVNFTKMHFPTLPSPEFE-------GKSSGKGK---YADSMVELDDH 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 268 VGRIDQKLGDLGIRENTLLIFTGDNGTDK---PIVTQTRFGevvGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFS 344
Cdd:cd16142 193 VGQILDALDELGIADNTIVIFTTDNGPEQdvwPDGGYTPFR---GEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHL 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1270232598 345 DFLPTMCEVADAEVPANLT------IDGQSFLPVLQGIEGQGRESMFMWYE 389
Cdd:cd16142 270 DWFPTLAALAGAPDPKDKLlgkdrhIDGVDQSPFLLGKSEKSRRSEFFYFG 320
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
48-427 |
7.50e-59 |
|
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: 198.16 E-value: 7.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGmtnkRNYVKFGM---------- 117
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTG----RYPIHTGMqhgvilagep 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 118 --LDRKQTTFAHLLKSAGYRTCIAGKWQLG--SELDSPRHFGFEESLL--------WQHTRGrmdsqkRDTRYPNPRLER 185
Cdd:cd16029 77 ygLPLNETLLPQYLKELGYATHLVGKWHLGfyTWEYTPTNRGFDSFYGyyggaedyYTHTSG------GANDYGNDDLRD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 186 NGTKEDYDEGEFSSDLFADFLCDFMET-NRDQPFLAYYPMALVHCP-------FCPTPDSEDWDPTsHGSKTYKGqpeyf 257
Cdd:cd16029 151 NEEPAWDYNGTYSTDLFTDRAVDIIENhDPSKPLFLYLAFQAVHAPlqvppeyADPYEDKFAHIKD-EDRRTYAA----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 258 gdMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGtdkpivTQTRFGEVV------GAKGEMVDAGNHVTCIAkWPGVI 331
Cdd:cd16029 225 --MVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG------GPTGGGDGGsnyplrGGKNTLWEGGVRVPAFV-WSPLL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 332 QPQRLTS--QIIDFSDFLPTMCEVADAEVPANLTIDGQSFLPVLQGIEGQGRESMFmwYERNGRPNKAREFA-RNQRYKL 408
Cdd:cd16029 296 PPKRGTVsdGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEIL--LNIDDITRTTGGAAiRVGDWKL 373
|
410
....*....|....*....
gi 1270232598 409 YGDGSFFDVEMDRNEKSPL 427
Cdd:cd16029 374 IVGKPLFNIENDPCERNDL 392
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
46-423 |
2.51e-55 |
|
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: 189.19 E-value: 2.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 46 DRPNIVLIMADDMGFECIGSNGSlDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGMTNKRNYVKF---------- 115
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGG-EIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTmaelatgkpg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 116 --GMLDRKQTTFAHLLKSAGYRTCIAGKWQLGseldsprhfgfeesllwqhtrgrmdsqkrdtrypnprlerngtKEDYd 193
Cdd:cd16025 80 yeGYLPDSAATIAEVLKDAGYHTYMSGKWHLG-------------------------------------------PDDY- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 194 egeFSSDLFADFLCDFMETNR--DQPFLAYYPMALVHCPF---------------------------------------- 231
Cdd:cd16025 116 ---YSTDDLTDKAIEYIDEQKapDKPFFLYLAFGAPHAPLqapkewidkykgkydagwdalreerlerqkelglipadtk 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 232 -CPTPDS-EDWD-PTSHGSKTYKGQPEYFGDMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGTDkpivtqtrfGEV- 307
Cdd:cd16025 193 lTPRPPGvPAWDsLSPEEKKLEARRMEVYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGAS---------AEPg 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 308 ---VGA------KGEMVDAGNHVTCIAKWPGVI-QPQRLTSQIIDFSDFLPTMCEVADAEVPAN------LTIDGQSFLP 371
Cdd:cd16025 264 wanASNtpfrlyKQASHEGGIRTPLIVSWPKGIkAKGGIRHQFAHVIDIAPTILELAGVEYPKTvngvpqLPLDGVSLLP 343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270232598 372 VLQGIEGQGRESmFMWYERNGrpNKArefARNQRYKL------YGDGSF---FDVEMDRNE 423
Cdd:cd16025 344 TLDGAAAPSRRR-TQYFELFG--NRA---IRKGGWKAvalhppPGWGDQwelYDLAKDPSE 398
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
47-428 |
3.43e-55 |
|
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: 188.06 E-value: 3.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 47 RPNIVLIMADDMGFECIGSNGS-LDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMTNKRNYV-------KFGM 117
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAaSVCSPSRASLMTGRLGLRNGVghnflptSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 118 LDRKQTTFAHLLKSAGYRTCIAGKWQLGseldsprhfgfeesllwqhtrgrmdsqKRDTRYPNPRlerngtKEDYDEG-E 196
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLG---------------------------QREAYLPNSR------GFDYYFGiP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 197 FSSDL-----FADFLCDFME--TNRDQPFLAYYPMALVHCPFCPTPDSEDwdPTSHGSKtykgqpeyFGDMVAYVDKIVG 269
Cdd:cd16161 128 FSHDSsladrYAQFATDFIQraSAKDRPFFLYAALAHVHVPLANLPRFQS--PTSGRGP--------YGDALQEMDDLVG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 270 RIDQKLGDLGIRENTLLIFTGDNG--------TDKPIVTQTR-FGEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQI 340
Cdd:cd16161 198 QIMDAVKHAGLKDNTLTWFTSDNGpwevkcelAVGPGTGDWQgNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAAL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 341 IDFSDFLPTMCEVADAEVPANLTIDGQSFLPVLQGIEGQGRESMFMWyerNGRPNKAREF--ARNQRYKLY--------G 410
Cdd:cd16161 278 VSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHP---NSGAAGAGALsaVRCGDYKAHyatggalaC 354
|
410 420
....*....|....*....|....*....
gi 1270232598 411 DGSF-----------FDVEMDRNEKSPLQ 428
Cdd:cd16161 355 CGSTgpklyhdppllFDLEVDPAESFPLT 383
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-428 |
5.69e-55 |
|
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: 188.16 E-value: 5.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGM---TNK--RNYVkfgMLDR 120
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNyPVCSPYRASLLTGQyplTNGvfGNDV---PLPP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 121 KQTTFAHLLKSAGYRTCIAGKWQL-GSELDSPRH----------FGFEEsllWqhtRGRMdsqkRDTRYPNPRLERNGTK 189
Cdd:cd16034 78 DAPTIADVLKDAGYRTGYIGKWHLdGPERNDGRAddytppperrHGFDY---W---KGYE----CNHDHNNPHYYDDDGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 190 EDYDEGeFSSDLFADFLCDFMET--NRDQPFLAYYPMALVHCPF--CPTPDSEDWDP---------------TSHGSKTY 250
Cdd:cd16034 148 RIYIKG-YSPDAETDLAIEYLENqaDKDKPFALVLSWNPPHDPYttAPEEYLDMYDPkklllrpnvpedkkeEAGLREDL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 251 KGqpeYFGdMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNgtdkpivtqtrfGEVVGAKGEM-----VDAGNHVTCIA 325
Cdd:cd16034 227 RG---YYA-MITALDDNIGRLLDALKELGLLENTIVVFTSDH------------GDMLGSHGLMnkqvpYEESIRVPFII 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 326 KWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPAnlTIDGQSFLPVLQGIEGQGRESM-FMWYERNGRPN----KAREF 400
Cdd:cd16034 291 RYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPD--TVEGRDLSPLLLGGKDDEPDSVlLQCFVPFGGGSardgGEWRG 368
|
410 420 430
....*....|....*....|....*....|..
gi 1270232598 401 ARNQRYKLY----GDGSFFDvemdrNEKSPLQ 428
Cdd:cd16034 369 VRTDRYTYVrdknGPWLLFD-----NEKDPYQ 395
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
48-431 |
1.28e-52 |
|
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: 183.80 E-value: 1.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKRNYVKFGMLD------- 119
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSsSPVCSPSRAALLTGRYQVRSGVYPGVFYpgsrggl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 120 -RKQTTFAHLLKSAGYRTCIAGKWQLGSELDS---PRHFGFEESLLWQHTRGRMDSQKRdTRYPnPRLERNGTkedYDEG 195
Cdd:cd16158 82 pLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGtylPTHQGFDHYLGIPYSHDQGPCQNL-TCFP-PNIPCFGG---CDQG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 196 EFSSDLFAD-------------------FLCDFMETN--RDQPFLAYYPMALVHCPfcptpdsedwdptSHGSKTYKGQP 254
Cdd:cd16158 157 EVPCPLFYNesivqqpvdlltleeryakFAKDFIADNakEGKPFFLYYASHHTHYP-------------QFAGQKFAGRS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 255 EY--FGDMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGtdkPIVTQTRFGEVVG----AKGEMVDAGNHVTCIAKWP 328
Cdd:cd16158 224 SRgpFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNG---PSTMRKSRGGNAGllkcGKGTTYEGGVREPAIAYWP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 329 GVIQPQRlTSQIIDFSDFLPTMCEVADAEVPaNLTIDGQSFLPVLQGIEGQGRESMFmWYERNGRPNKAREFARNQRYK- 407
Cdd:cd16158 301 GRIKPGV-THELASTLDILPTIAKLAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFF-YYPTSPDPDKGVFAVRWGKYKa 377
|
410 420
....*....|....*....|....*
gi 1270232598 408 -LYGDGSFFDVEMDRNEKSPLQSLT 431
Cdd:cd16158 378 hFYTQGAAHSGTTPDKDCHPSAELT 402
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
47-454 |
2.36e-48 |
|
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: 173.24 E-value: 2.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMT-------GMTNKRNYVKF--- 115
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAaAPLCTPSRAAFLTgrypirsGMASSHGMRVIlft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 116 ---GMLDRKQTTFAHLLKSAGYRTCIAGKWQLG----SELD---SPRHFGF-----------------EESLLWQ----- 163
Cdd:cd16159 81 assGGLPPNETTFAEVLKQQGYSTALIGKWHLGlhceSRNDfchHPLNHGFdyfyglpltnlkdcgdgSNGEYDLsfdpl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 164 -------------HTRGRMDSQKRDTR------------------------YPNPRLERNgtkEDYDEGEFSSDLFADFL 206
Cdd:cd16159 161 fplltafvlitalTIFLLLYLGAVSKRffvfllilsllfislfflllitnrYFNCILMRN---HEVVEQPMSLENLTQRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 207 CD----FMETNRDQPFLAYYPMALVHCPFCPTPdsEDWDPTSHGsktykgqpEYfGDMVAYVDKIVGRIDQKLGDLGIRE 282
Cdd:cd16159 238 TKeaisFLERNKERPFLLVMSFLHVHTALFTSK--KFKGRSKHG--------RY-GDNVEEMDWSVGQILDALDELGLKD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 283 NTLLIFTGDNGtdkPIVTQTRFGEVV---------GAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEV 353
Cdd:cd16159 307 NTFVYFTSDNG---GHLEEISVGGEYgggnggiygGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAAL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 354 ADAEVPANLTIDGQSFLPVLQGIEGQG-RESMFM----------WYERNGR---------PNKAREFARNQRYKL---YG 410
Cdd:cd16159 384 AGAPLPSDRIIDGRDLMPLLTGQEKRSpHEFLFHycgaelhavrYRPRDGGavwkahyftPNFYPGTEGCCGTLLcrcFG 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1270232598 411 DGS-------FFDVEMDRNEKSPLQSLTDDQKEIRSKLQAKIDSFANIIPP 454
Cdd:cd16159 464 DSVthhdpplLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIEP 514
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
48-444 |
5.54e-46 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 164.32 E-value: 5.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKR-----NYVKFGMLDRK 121
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTpSPVCCPARASLLTGLYPHEhgvlnNVENAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 122 ----QTTFAHLLKSAGYRTCIAGKWQLGSElDSPRHFGFEEsllwqhtrgrmdsqkrdtrypnprlerNGTKEDYDEGeF 197
Cdd:cd16033 81 lppgVETFSEDLREAGYRNGYVGKWHVGPE-ETPLDYGFDE---------------------------YLPVETTIEY-F 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 198 SSDLFADFLCDFMEtnRDQPFLAYY----PmalvHCPFCPTPDSEDW-DPTS---HGS--KTYKGQPE------------ 255
Cdd:cd16033 132 LADRAIEMLEELAA--DDKPFFLRVnfwgP----HDPYIPPEPYLDMyDPEDiplPESfaDDFEDKPYiyrrerkrwgvd 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 256 -------------YFGdMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNgtdkpivtqtrfGEVVGAKGeMVDAGN--- 319
Cdd:cd16033 206 tedeedwkeiiahYWG-YITLIDDAIGRILDALEELGLADDTLVIFTSDH------------GDALGAHR-LWDKGPfmy 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 320 ----HVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPanLTIDGQSFLPVLQG-IEGQGRESMFMwyERNGrp 394
Cdd:cd16033 272 eetyRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVP--PKVDGRSLLPLLRGeQPEDWRDEVVT--EYNG-- 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270232598 395 nkaREF------ARNQRYKL-YGDGSF---FDVEMDRNEkspLQSLTDDQ--KEIRSKLQAK 444
Cdd:cd16033 346 ---HEFylpqrmVRTDRYKYvFNGFDIdelYDLESDPYE---LNNLIDDPeyEEILREMRTR 401
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
47-373 |
7.18e-46 |
|
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: 164.91 E-value: 7.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGmtnkRNYVKFGM-------- 117
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSaDSVCTPSRAALLTG----RLPIRSGMyggtrvfl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 118 ------LDRKQTTFAHLLKSAGYRTCIAGKWQLG-SELDS------PRHFGFE-------ESLLWQhtrgrMDSQKRDTR 177
Cdd:cd16160 77 pwdiggLPKTEVTMAEALKEAGYTTGMVGKWHLGiNENNHsdgahlPSHHGFDfvgtnlpFTNSWA-----CDDTGRHVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 178 YPNPRLERNGTKEDYDEGEFSSDLFADFLCD----FMETNRDQPFLAYYPMALVHCP-FCptpdSEDWDPTSHgsktyKG 252
Cdd:cd16160 152 FPDRSACFLYYNDTIVEQPIQHEHLTETLVGdaksFIEDNQENPFFLYFSFPQTHTPlFA----SKRFKGKSK-----RG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 253 QpeyFGDMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGTDKPIV-TQTRFGEVVGAKGEMVDAGNHVTCIAKWPGVI 331
Cdd:cd16160 223 R---YGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEYClEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTI 299
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1270232598 332 QPQRlTSQIIDFSDFLPTMCEVADAEVPANLTIDGQSFLPVL 373
Cdd:cd16160 300 KPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLL 340
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
48-424 |
1.62e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 159.44 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIG--SNGSLDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGMTNKRNYVKF--GMLDRKQT 123
Cdd:cd16154 1 PNILLIIADDQGLDSSAqySLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGVLAvpDELLLSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 124 TFAHLLK----SAGYRTCIAGKWQLGSELDSPRHFGfeeslLWQHTRGRMDSQKRDtrYPNPRLERNGTKEDYDE--GEF 197
Cdd:cd16154 81 TLLQLLIkdatTAGYSSAVIGKWHLGGNDNSPNNPG-----GIPYYAGILGGGVQD--YYNWNLTNNGQTTNSTEyaTTK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 198 SSDLFADFLcdfmeTNRDQPFLAYypMALV--HCPFcPTPDSEDWDPTSHGSKTYKGQP--EYFGDMVAYVDKIVGRIDQ 273
Cdd:cd16154 154 LTNLAIDWI-----DQQTKPWFLW--LAYNapHTPF-HLPPAELHSRSLLGDSADIEANprPYYLAAIEAMDTEIGRLLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 274 KLgDLGIRENTLLIFTGDNGTDKPiVTQTRFgEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEV 353
Cdd:cd16154 226 SI-DEEERENTIIIFIGDNGTPGQ-VVDLPY-TRNHAKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAEL 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270232598 354 ADAEVPAnlTIDGQSFLPVLQGIEGQGRESMFMWYERNGRPNKARefaRNQRYKL--YGDG--SFFDVEMDRNEK 424
Cdd:cd16154 303 AGVDAAE--IHDSVSFKPLLSDVNASTRQYNYTEYESPTTTGWAT---RNQYYKLieSENGqeELYDLINDPSEQ 372
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
48-371 |
3.42e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 155.78 E-value: 3.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMAD----DMgfecIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMTNKRNYVKFGMLDRKQ 122
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGsNPTLPSRFSLFTGLYPFYHGVWGGPLEPDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 123 TTFAHLLKSAGYRTCIAGkwqlgselDSPRHFGFeesllWQHTRGRmdsqkrDTRYPNPRLERNGTKEDYdegEFSSDLF 202
Cdd:cd16148 77 PTLAEILRKAGYYTAAVS--------SNPHLFGG-----PGFDRGF------DTFEDFRGQEGDPGEEGD---ERAERVT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 203 ADFLcDFMETN-RDQPFLAYypmalVHCpfcptpdsedWDPtsHGSKTYKGQpeyfgdmVAYVDKIVGRIDQKLGDLGIR 281
Cdd:cd16148 135 DRAL-EWLDRNaDDDPFFLF-----LHY----------FDP--HEPYLYDAE-------VRYVDEQIGRLLDKLKELGLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 282 ENTLLIFTGDNGTDkpivtqtrFGEvvgaKGEMVDAGN-------HVTCIAKWPGVIQPQR---LTSQIidfsDFLPTMC 351
Cdd:cd16148 190 EDTLVIVTSDHGEE--------FGE----HGLYWGHGSnlydeqlHVPLIIRWPGKEPGKRvdaLVSHI----DIAPTLL 253
|
330 340
....*....|....*....|
gi 1270232598 352 EVADAEVPAnlTIDGQSFLP 371
Cdd:cd16148 254 DLLGVEPPD--YSDGRSLLP 271
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
48-356 |
4.76e-44 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 156.43 E-value: 4.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKRNYVKFGMLD---RKQT 123
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSgGTLTAPSRFALLTGLPPHNFGSYVSTPVglpRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 124 TFAHLLKSAGYRTCIAGKWQLG-SELDSPRHFGFEESLLWQHtrGRMDSQKRDTRYPNPRLerngtkedydeGEFSSDLF 202
Cdd:pfam00884 81 SLPDLLKRAGYNTGAIGKWHLGwYNNQSPCNLGFDKFFGRNT--GSDLYADPPDVPYNCSG-----------GGVSDEAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 203 ADFLCDFmETNRDQPFLAYY-PMAlVHCPFcptPDSEDWDPTSHGSKTYKG----QPEYFGDMVAYVDKIVGRIDQKLGD 277
Cdd:pfam00884 148 LDEALEF-LDNNDKPFFLVLhTLG-SHGPP---YYPDRYPEKYATFKPSSCseeqLLNSYDNTLLYTDDAIGRVLDKLEE 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270232598 278 LGIRENTLLIFTGDNGtdkPIVTQTRFGEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADA 356
Cdd:pfam00884 223 NGLLDNTLVVYTSDHG---ESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-444 |
2.27e-43 |
|
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: 156.57 E-value: 2.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-----PICTPSRVKLMTGMTNKRNYVKFGM-LDR 120
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMggwsgAVCVPSRAMLMTGRTLFHAPEGGKAaIPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 121 KQTTFAHLLKSAGYRTCIAGKWqlgseldsprHfgfeesllwqhtrgrmdsqkrdtrypnprlerNGtkedydegefssd 200
Cdd:cd16155 82 DDKTWPETFKKAGYRTFATGKW----------H--------------------------------NG------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 201 lFADFLCDFME--TNRDQPFLAYYPMALVHCPFCPTPDSED-WDPTSHG-SKTYKGQ-PEYFGD---------------- 259
Cdd:cd16155 107 -FADAAIEFLEeyKDGDKPFFMYVAFTAPHDPRQAPPEYLDmYPPETIPlPENFLPQhPFDNGEgtvrdeqlapfprtpe 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 260 -----------MVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGTdkpivtqtrfgeVVGAKG-----EMVDAGNHVTC 323
Cdd:cd16155 186 avrqhlaeyyaMITHLDAQIGRILDALEASGELDNTIIVFTSDHGL------------AVGSHGlmgkqNLYEHSMRVPL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 324 IAKWPGvIQPQRLTSQIIDFSDFLPTMCEVADAEVPAnlTIDGQSFLPVLQGIEGQGRESMFMWYERNGRPnkarefARN 403
Cdd:cd16155 254 IISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPE--SVEGKSLLPVIRGEKKAVRDTLYGAYRDGQRA------IRD 324
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1270232598 404 QRYKL--YGDGSF----FDVEMDRNEKSPLQSLTDDQKEIRsKLQAK 444
Cdd:cd16155 325 DRWKLiiYVPGVKrtqlFDLKKDPDELNNLADEPEYQERLK-KLLAE 370
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
47-373 |
2.54e-43 |
|
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: 158.40 E-value: 2.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKRN-------------- 111
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSaNPLCSPSRAALLTGRLPIRNgfyttnaharnayt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 112 --YVKFGMLDRKQtTFAHLLKSAGYRTCIAGKWQLG-SELDSPRHFGFEEsllWQHTRGRMDSQKRDTRYPNPRLERNGT 188
Cdd:cd16157 81 pqNIVGGIPDSEI-LLPELLKKAGYRNKIVGKWHLGhRPQYHPLKHGFDE---WFGAPNCHFGPYDNKAYPNIPVYRDWE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 189 ---------KEDYDEGEFS-SDLFADFLCDFMET--NRDQPFLAYYPMALVHCPFcptpdsedwdptsHGSKTYKG--QP 254
Cdd:cd16157 157 migryyeefKIDKKTGESNlTQIYLQEALEFIEKqhDAQKPFFLYWAPDATHAPV-------------YASKPFLGtsQR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 255 EYFGDMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNG--TDKPIVTQTRFGEVVGAKGEMVDAGNHVTCIAKWPGVIQ 332
Cdd:cd16157 224 GLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaaLISAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIK 303
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1270232598 333 PQRLTSQIIDFSDFLPTMCEVADAEVPANLTIDGQSFLPVL 373
Cdd:cd16157 304 PGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVL 344
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
48-420 |
6.52e-42 |
|
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: 151.16 E-value: 6.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGM--TNKRNYVKFGMLDRKQTT 124
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPsPICVPSRASFLTGRyvHETGVWDNADPYDGDVPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 125 FAHLLKSAGYRTCIAGKwqlgseldsprhfgfeesllwQHTRGRMDsqkrdtrypnprleRNGTkeDYDEgefssdLFAD 204
Cdd:cd16037 81 WGHALRAAGYETVLIGK---------------------LHFRGEDQ--------------RHGF--RYDR------DVTE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 205 FLCDFMETN--RDQPFLAYYPMALVHCPFCPTPdsEDWDPTSHGSKTykgqpEYFGdMVAYVDKIVGRIDQKLGDLGIRE 282
Cdd:cd16037 118 AAVDWLREEaaDDKPWFLFVGFVAPHFPLIAPQ--EFYDLYVRRARA-----AYYG-LVEFLDENIGRVLDALEELGLLD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 283 NTLLIFTGDNgtdkpivtqtrfGEVVGAKG-----EMVDAGNHVTCIAKWPGVIQPQRlTSQIIDFSDFLPTMCEVADAE 357
Cdd:cd16037 190 NTLIIYTSDH------------GDMLGERGlwgksTMYEESVRVPMIISGPGIPAGKR-VKTPVSLVDLAPTILEAAGAP 256
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270232598 358 VPANLtiDGQSFLPVLQGIEGQGRE--SMFMWyerNGRPNKAReFARNQRYKL---YGDGS-FFDVEMD 420
Cdd:cd16037 257 PPPDL--DGRSLLPLAEGPDDPDRVvfSEYHA---HGSPSGAF-MLRKGRWKYiyyVGYPPqLFDLEND 319
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
48-371 |
1.36e-40 |
|
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: 145.84 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCY-SQPICTPSRVKLMTGM-------------TNKRNYV 113
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFcTSPVCSPARASLLTGRmpsqhgihdwiveGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 114 KFGMLDRKQTTFAHLLKSAGYRTCIAGKWQLGSELdsprhfgfeesllwqhtrgrmdsqkrdtrypnprlerngtkedyd 193
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLGDDA--------------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 194 egefssdlfADFLCDfmETNRDQPFLAYYPMALVHCPFcptpdsedwdptshgsktykgqpEYFGDMVAyVDKIVGRIDQ 273
Cdd:cd16149 116 ---------ADFLRR--RAEAEKPFFLSVNYTAPHSPW-----------------------GYFAAVTG-VDRNVGRLLD 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 274 KLGDLGIRENTLLIFTGDNGTDkpivtqtrfgevVG-----AKG------EMVDAGNHVTCIAKWPGVIQPQRLTSQIID 342
Cdd:cd16149 161 ELEELGLTENTLVIFTSDNGFN------------MGhhgiwGKGngtfplNMYDNSVKVPFIIRWPGVVPAGRVVDSLVS 228
|
330 340
....*....|....*....|....*....
gi 1270232598 343 FSDFLPTMCEVADAEVPANLTIDGQSFLP 371
Cdd:cd16149 229 AYDFFPTLLELAGVDPPADPRLPGRSFAD 257
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
48-420 |
1.21e-39 |
|
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: 145.41 E-value: 1.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMTNKRNyvkfGMLDR------ 120
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNsPLCAPSRASMMTGRLPSRI----GAYDNaaefpa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 121 KQTTFAHLLKSAGYRTCIAGKwqlgseldspRHF-------GFeesllwqhtrgrmdsqkrdtrypnprlerngtkeDYD 193
Cdd:cd16032 77 DIPTFAHYLRAAGYRTALSGK----------MHFvgpdqlhGF----------------------------------DYD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 194 -EGEFSSdlfADFLCDFMETNRDQPFLAYYPMALVHCPFCPTPdsEDWD----PTSHGsktykgqpeYFGdMVAYVDKIV 268
Cdd:cd16032 113 eEVAFKA---VQKLYDLARGEDGRPFFLTVSFTHPHDPYVIPQ--EYWDlyvrRARRA---------YYG-MVSYVDDKV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 269 GRIDQKLGDLGIRENTLLIFTGDNgtdkpivtqtrfGEVVGAKG---EMV--DAGNHVTCIAKWPGVIQPQRLtSQIIDF 343
Cdd:cd16032 178 GQLLDTLERTGLADDTIVIFTSDH------------GDMLGERGlwyKMSffEGSARVPLIISAPGRFAPRRV-AEPVSL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 344 SDFLPTMCEVADAEVPANLT-IDGQSFLPVLQGIEGQGRESMFMWYERNGRPNKAReFARNQRYKL---YGDGS-FFDVE 418
Cdd:cd16032 245 VDLLPTLVDLAGGGTAPHVPpLDGRSLLPLLEGGDSGGEDEVISEYLAEGAVAPCV-MIRRGRWKFiycPGDPDqLFDLE 323
|
..
gi 1270232598 419 MD 420
Cdd:cd16032 324 AD 325
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
46-406 |
4.17e-38 |
|
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: 143.48 E-value: 4.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 46 DRPNIVLIMADDMGFEcIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGM--TNKRNYVkFGMLDRKQ 122
Cdd:cd16030 1 KKPNVLFIAVDDLRPW-LGCYGGHPAKTPNIDRLAARGVLFTNAYCQqPVCGPSRASLLTGRrpDTTGVYD-NNSYFRKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 123 ----TTFAHLLKSAGYRTCIAGK---WQLGSELDSPRHFgfeeSLLWQHTRGRMDSQKRDTRYPNPRLERNGTK----ED 191
Cdd:cd16030 79 apdaVTLPQYFKENGYTTAGVGKifhPGIPDGDDDPASW----DEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPaweaAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 192 YDEGEFSSDLFADFLCDFMET--NRDQP-FLA---YYPmalvHCPF-CPT------PDSE------------------DW 240
Cdd:cd16030 155 VPDEAYPDGKVADEAIEQLRKlkDSDKPfFLAvgfYKP----HLPFvAPKkyfdlyPLESiplpnpfdpidlpevawnDL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 241 -DPTSHGSKTYKGQPEYFGDM---------------VAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGtdkpivtqtrF 304
Cdd:cd16030 231 dDLPKYGDIPALNPGDPKGPLpdeqarelrqayyasVSYVDAQVGRVLDALEELGLADNTIVVLWSDHG----------W 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 305 --GEvvgaKGE-----MVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPANLtiDGQSFLPVLQGIE 377
Cdd:cd16030 301 hlGE----HGHwgkhtLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPPCL--EGKSLVPLLKNPS 374
|
410 420
....*....|....*....|....*....
gi 1270232598 378 GQGRESMFMWYERNGRPNKArefARNQRY 406
Cdd:cd16030 375 AKWKDAAFSQYPRPSIMGYS---IRTERY 400
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
48-445 |
1.27e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 141.99 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMtnkrnY--VK-----FGMLD 119
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQnPVCSPSRCSFLTGW-----YphVNghrtlHHLLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 120 RKQTTFAHLLKSAGYRTCIAGKwqlgseldspRHFgfeesllwqhtrgrmdsqkrdtrypnprLERNGTKEDYdegEFSS 199
Cdd:cd16150 76 PDEPNLLKTLKDAGYHVAWAGK----------NDD----------------------------LPGEFAAEAY---CDSD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 200 DLFADFLCDFMET-NRDQPFLAYYPMALVHCPF-CPTP-----DSEDWDPTSHGSKTYKGQPE----------------- 255
Cdd:cd16150 115 EACVRTAIDWLRNrRPDKPFCLYLPLIFPHPPYgVEEPwfsmiDREKLPPRRPPGLRAKGKPSmlegiekqgldrwseer 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 256 -------YFGdMVAYVDKIVGRIDQKLGDLGIRENTLLIF-------TGDNG-TDKpivTQTRFGEVVgakgemvdagNH 320
Cdd:cd16150 195 wrelratYLG-MVSRLDHQFGRLLEALKETGLYDDTAVFFfsdhgdyTGDYGlVEK---WPNTFEDCL----------TR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 321 VTCIAKWPGVIqPQRLTSQIIDFSDFLPTMCEVADaeVPANLTIDGQSFLPVLQGIEGQGRESMF------------Mwy 388
Cdd:cd16150 261 VPLIIKPPGGP-AGGVSDALVELVDIPPTLLDLAG--IPLSHTHFGRSLLPVLAGETEEHRDAVFseggrlhgeeqaM-- 335
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270232598 389 ERNGRPN---KAREFA-------------RNQRYK----LYGDGSFFDVEMDRNEkspLQSLTDDQ--KEIRSKLQAKI 445
Cdd:cd16150 336 EGGHGPYdlkWPRLLQqeeppehtkavmiRTRRYKyvyrLYEPDELYDLEADPLE---LHNLIGDPayAEIIAEMKQRL 411
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
47-446 |
2.25e-37 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 142.50 E-value: 2.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMTNKRNyvkfGMLDRKQ--- 122
Cdd:PRK13759 6 KPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAvPSCTPARAALLTGLSQWHH----GRVGYGDvvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 123 ----TTFAHLLKSAGYRT-CIaGKWQLGSEldSPRHfGFEESLL---WQHTrGRMDSQKR-----DTRY--------PNP 181
Cdd:PRK13759 82 wnykNTLPQEFRDAGYYTqCI-GKMHVFPQ--RNLL-GFHNVLLhdgYLHS-GRNEDKSQfdfvsDYLAwlrekapgKDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 182 RLERNGTKE--------DYDEGEFSSDLFADFLCDFMET-NRDQPFLAYYPMALVHCPF--------------CPTPDSE 238
Cdd:PRK13759 157 DLTDIGWDCnswvarpwDLEERLHPTNWVGSESIEFLRRrDPTKPFFLKMSFARPHSPYdppkryfdmykdadIPDPHIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 239 DW------DPTSHGSKTYKGQ-PE---------YFGDMvAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNgtdkpivtqt 302
Cdd:PRK13759 237 DWeyaedqDPEGGSIDALRGNlGEeyarraraaYYGLI-THIDHQIGRFLQALKEFGLLDNTIILFVSDH---------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 303 rfGEVVG-----AKGEMVDAGNHVTCIAKWPG-VIQPQRLTS--QIIDFSDFLPTMCEVADAEVPAnlTIDGQSFLPVLQ 374
Cdd:PRK13759 306 --GDMLGdhylfRKGYPYEGSAHIPFIIYDPGgLLAGNRGTVidQVVELRDIMPTLLDLAGGTIPD--DVDGRSLKNLIF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 375 GIEGQGRESM----FMWYERNGRPNKARE----FARNQRYKLygdgsfFDVEMDRNEKSPLQSLTDDQKEIRSKLQAKID 446
Cdd:PRK13759 382 GQYEGWRPYLhgehALGYSSDNYLTDGKWkyiwFSQTGEEQL------FDLKKDPHELHNLSPSEKYQPRLREMRKKLVD 455
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
48-445 |
5.98e-33 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293775 [Multi-domain] Cd Length: 468 Bit Score: 129.81 E-value: 5.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKRNyvkfGM------LDR 120
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTtQPVCGPARSGLFTGLYPHTN----GSwtncmaLGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 121 KQTTFAHLLKSAGYRTCIAGKWQLgselDSPRHFGFEE------SLLWQHTRGRMDSQKRDTRY----PNPRLERNGTKE 190
Cdd:cd16156 77 NVKTIGQRLSDNGIHTAYIGKWHL----DGGDYFGNGIcpqgwdPDYWYDMRNYLDELTEEERRksrrGLTSLEAEGIKE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 191 DYDEGEFSSDLfadfLCDFMETNRDQPFLayypmaLV------HCPF-CPTPDSE------------DWD-----PTSH- 245
Cdd:cd16156 153 EFTYGHRCTNR----ALDFIEKHKDEDFF------LVvsydepHHPFlCPKPYASmykdfefpkgenAYDdlenkPLHQr 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 246 ----------GSKTYKGQPEYFGdMVAYVDKIVGRIDQKLGDlgIRENTLLIFTGDNGtdkpivtqtrfgEVVGA----- 310
Cdd:cd16156 223 lwagakphedGDKGTIKHPLYFG-CNSFVDYEIGRVLDAADE--IAEDAWVIYTSDHG------------DMLGAhklwa 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 311 KGE-MVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPANLtiDGQSFLPVLQGIEGQGRESMFM--- 386
Cdd:cd16156 288 KGPaVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVL--EGESILATIEDPEIPENRGVFVefg 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270232598 387 WYERNGRPNKAREFAR---NQRYK----LYGDGSFFDVEMDRNEkspLQSLTDDQ--KEIRSKLQAKI 445
Cdd:cd16156 366 RYEVDHDGFGGFQPVRcvvDGRYKlvinLLSTDELYDLEKDPYE---MHNLIDDPdyADVRDQLHDEL 430
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-385 |
9.71e-33 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 127.34 E-value: 9.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 47 RPNIVLIMADDMGFECIGSNGS-LDYqTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGM--TNKRNYVKFGMLDRKQ 122
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQpLDL-TPNLDALAEEGVLFENAFTpQPVCGPARACLQTGLypTETGCFRNGIPLPADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 123 TTFAHLLKSAGYRTCIAGKWQLgseldsprhfgfeesllwqhtrgrmdsqkrdtrypnprlerngtkedydeGEFSSDLF 202
Cdd:cd16152 80 KTLAHYFRDAGYETGYVGKWHL--------------------------------------------------AGYRVDAL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 203 ADFLCDFMET-NRDQPFLAYYPMALVHcpfcptpDSEDWD--PTSHGSK------------------TYKGQPEYFGdMV 261
Cdd:cd16152 110 TDFAIDYLDNrQKDKPFFLFLSYLEPH-------HQNDRDryVAPEGSAerfanfwvppdlaalpgdWAEELPDYLG-CC 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 262 AYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGTDkpivTQTRFGEVvgaKGEMVDAGNHVTCIAKWPGVIQPQRLTsQII 341
Cdd:cd16152 182 ERLDENVGRIRDALKELGLYDNTIIVFTSDHGCH----FRTRNAEY---KRSCHESSIRVPLVIYGPGFNGGGRVE-ELV 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1270232598 342 DFSDFLPTMCEVADAEVPAnlTIDGQSFLPVLQGIEGQGRESMF 385
Cdd:cd16152 254 SLIDLPPTLLDAAGIDVPE--EMQGRSLLPLVDGKVEDWRNEVF 295
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
47-368 |
5.06e-32 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 126.13 E-value: 5.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 47 RPNIVLIMADDMGFECigsnGSLDYQTPNIDRIASEGLRFEHCY-SQPICTPSRVKLMTGM----TNKRN-------YVK 114
Cdd:cd16147 1 RPNIVLILTDDQDVEL----GSMDPMPKTKKLLADQGTTFTNAFvTTPLCCPSRASILTGQyahnHGVTNnsppgggYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 115 FGMLDRKQTTFAHLLKSAGYRTCIAGK----WQLGSELDS-PRhfGFEESLLWQHTRgrmdsqkRDTRYpNPRLERNGTK 189
Cdd:cd16147 77 FWQNGLERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYvPP--GWDEWDGLVGNS-------TYYNY-TLSNGGNGKH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 190 EDYDEGEFSSDLFADFLCDFMET--NRDQPFLAYYPMALVHCPFCPTPDSED-------------WDPTSHGSKTY-KGQ 253
Cdd:cd16147 147 GVSYPGDYLTDVIANKALDFLRRaaADDKPFFLVVAPPAPHGPFTPAPRYANlfpnvtapprpppNNPDVSDKPHWlRRL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 254 PEYFGDMVAY--------------VDKIVGRIDQKLGDLGIRENTLLIFTGDNG---------TDKpivtQTRFGEVVga 310
Cdd:cd16147 227 PPLNPTQIAYidelyrkrlrtlqsVDDLVERLVNTLEATGQLDNTYIIYTSDNGyhlgqhrlpPGK----RTPYEEDI-- 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270232598 311 kgemvdagnHVTCIAKWPGVIQPQR---LTSQIidfsDFLPTMCEVADAEVPANLtiDGQS 368
Cdd:cd16147 301 ---------RVPLLVRGPGIPAGVTvdqLVSNI----DLAPTILDLAGAPPPSDM--DGRS 346
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
48-427 |
7.62e-32 |
|
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: 126.60 E-value: 7.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGM--TNKRNYVKFGMLDRKQTT 124
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQaAPCGPSRASLYTGRylMNHRSVWNGTPLDARHLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 125 FAHLLKSAGYRTCIAGKWQLGSELD--SPRHfgfeESLLWQHT-RGRMDSQKRDTRYPnprlerngtKEDYDegefsSDL 201
Cdd:cd16028 81 LALELRKAGYDPALFGYTDTSPDPRglAPLD----PRLLSYELaMPGFDPVDRLDEYP---------AEDSD-----TAF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 202 FADFLCDFMETNRDQPF---LAYY----------PMALVHCP------------------------FCPTPDSEDWDPTS 244
Cdd:cd16028 143 LTDRAIEYLDERQDEPWflhLSYIrphppfvapaPYHALYDPadvpppiraeslaaeaaqhpllaaFLERIESLSFSPGA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 245 HGSKTYKG------QPEYFGdMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNgtdkpivtqtrfGEVVG-----AKGE 313
Cdd:cd16028 223 ANAADLDDeevaqmRATYLG-LIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDH------------GEQLGdhwlwGKDG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 314 MVDAGNHVTCIAKWPGVIQPQRLTSQIIDFS---DFLPTMCEVADAEVPAnlTIDGQSFLPVLQGIEGQGRESMFMWYER 390
Cdd:cd16028 290 FFDQAYRVPLIVRDPRREADATRGQVVDAFTesvDVMPTILDWLGGEIPH--QCDGRSLLPLLAGAQPSDWRDAVHYEYD 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1270232598 391 NG-------------RPNKAREFA-RNQRYKL--YGDGS--FFDVEMDRNEKSPL 427
Cdd:cd16028 368 FRdvstrrpqealglSPDECSLAViRDERWKYvhFAALPplLFDLKNDPGELRDL 422
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-366 |
9.57e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 103.22 E-value: 9.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 47 RPNIVLIMADDM---GFECIG------SNGSLDY-QTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMTNKRNYV-K 114
Cdd:cd16153 1 KPNILWIITDDQrvdSLSCYNnahtgkSESRLGYvESPNIDALAAEGVLFTNAYCNsPVCVPSRTSMLTGRYPHRTGVyG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 115 FGM----LDRKQTTFAHLLKSAGYRTCIAGKwqlgseldsprhFGFEESLLWqhtrgrmdsqkrdTRYPNPRLERNGTKE 190
Cdd:cd16153 81 FEAahpaLDHGLPTFPEVLKKAGYQTASFGK------------SHLEAFQRY-------------LKNANQSYKSFWGKI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 191 dydegefssdlfadflcdFMETNRDQPFLAYYPMALVHCPFCPtpdsedwdptshgSKTYKGQPEYFGdMVAYVDKIVGR 270
Cdd:cd16153 136 ------------------AKGADSDKPFFVRLSFLQPHTPVLP-------------PKEFRDRFDYYA-FCAYGDAQVGR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 271 IDQKLGDLGI---RENTLLIFTGDNGtdkpivtqTRFGEV-VGAKGEMVDAGNHVTCIAKWPGVIQPQRLT--SQIIDFS 344
Cdd:cd16153 184 AVEAFKAYSLkqdRDYTIVYVTGDHG--------WHLGEQgILAKFTFWPQSHRVPLIVVSSDKLKAPAGKvrHDFVEFV 255
|
330 340
....*....|....*....|..
gi 1270232598 345 DFLPTMCEVADAEVPANLTIDG 366
Cdd:cd16153 256 DLAPTLLAAAGVDVDAPDYLDG 277
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
48-390 |
1.52e-21 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 94.58 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFE-HCYSQPICTPSRVKLMTG-------MTNKRNYVKFGMLD 119
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFEnHYTAACMCSPSRSTLYTGlhpqqtgVTDTLGSPMQPLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 120 RKQTTFAHLLKSAGYRTCIAGKWQLGSeldsprhfgfeesllwqHTRGrmdsqkrdtrypnprlernGTKEDydegefss 199
Cdd:cd16035 81 PDVPTLGHMLRAAGYYTAYKGKWHLSG-----------------AAGG-------------------GYKRD-------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 200 DLFADFLCDFMET-----NRDQPFLAYypMALV--HCPFCPTPDSEDWdptshgsktyKGQPEYFGDMVAYVDKIVGRID 272
Cdd:cd16035 117 PGIAAQAVEWLRErgaknADGKPWFLV--VSLVnpHDIMFPPDDEERW----------RRFRNFYYNLIRDVDRQIGRVL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 273 QKLGDLGIRENTLLIFTGDNgtdkpivtqtrfGEVVGAKGEMVDAGN------HVtciakwPGVI-------QPQR---L 336
Cdd:cd16035 185 DALDASGLADNTIVVFTSDH------------GEMGGAHGLRGKGFNayeealHV------PLIIshpdlfgTGQTtdaL 246
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1270232598 337 TSQIidfsDFLPTMCEVADAEVPANLTID----GQSFLPVLQGIEG-QGRESMFMWYER 390
Cdd:cd16035 247 TSHI----DLLPTLLGLAGVDAEARATEApplpGRDLSPLLTDADAdAVRDGILFTYDR 301
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
48-395 |
2.38e-20 |
|
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: 92.22 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTG----MTNKRNyvKFGMLDRKQ 122
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNsPICCPSRAAMWSGlfthLTESWN--NYKGLDPNY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 123 TTFAHLLKSAGYRTCIAGKWQLGSELDSprhfgfeesllwqhTRGRMDSQKRDTRY-------PNPRLERNGTKEDYDEG 195
Cdd:cd16171 79 PTWMDRLEKHGYHTQKYGKLDYTSGHHS--------------VSNRVEAWTRDVPFllrqegrPTVNLVGDRSTVRVMLK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 196 EFSSDLFADFLCDFMETNRDQPFLAYYPMALVHcPFcPTPDSedwDPTSHGSKTYKgqpEYFGDMVAYVDKIVGRIDQKL 275
Cdd:cd16171 145 DWQNTDKAVHWIRKEAPNLTQPFALYLGLNLPH-PY-PSPSM---GENFGSIRNIR---AFYYAMCAETDAMLGEIISAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 276 GDLGIRENTLLIFTGDNGtdKPIVTQTRFgevvgAKGEMVDAGNHVTCIAKWPGvIQPQRLTSQIIDFSDFLPTMCEVAD 355
Cdd:cd16171 217 KDTGLLDKTYVFFTSDHG--ELAMEHRQF-----YKMSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAG 288
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1270232598 356 AEVPANLTidGQSFLPVLQgiegqgRESMFMWYERNGRPN 395
Cdd:cd16171 289 VPQPQNLS--GYSLLPLLS------ESSIKESPSRVPHPD 320
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
48-354 |
2.82e-20 |
|
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: 89.40 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFE--HCYSQPICTPSRVKLMTG------------MTNKRNYV 113
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNfrSVSPPTSSAPNHAALLTGayptlhgytgngSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 114 KFGMLDRKQTTFAHLLKSAGYRTCIAGkwqlgseldsprhfgfeeslLWQHtrgrmdsqkrdtrypnprlerngtkedyd 193
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIG--------------------LLKA----------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 194 egefssdlfadflcdFMETNRDQPFLAYypmalVHCpfcptpDSEDWDPTSHGSKTykgqPEYFgDMVAYVDKIVGRIDQ 273
Cdd:cd00016 112 ---------------IDETSKEKPFVLF-----LHF------DGPDGPGHAYGPNT----PEYY-DAVEEIDERIGKVLD 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 274 KLGDLGIRENTLLIFTGDNG-TDKPIVTQTRFGEVVGAKGemvdAGNHVTCIAKWPGVIQPQ---RLTSQIidfsDFLPT 349
Cdd:cd00016 161 ALKKAGDADDTVIIVTADHGgIDKGHGGDPKADGKADKSH----TGMRVPFIAYGPGVKKGGvkhELISQY----DIAPT 232
|
....*
gi 1270232598 350 MCEVA 354
Cdd:cd00016 233 LADLL 237
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
36-350 |
1.01e-14 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 76.23 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 36 ADEPSPQRSGDRPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQpicTPSRVK----LMTGM--TNK 109
Cdd:COG1368 223 RPTPNPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQ---GGRTSRgefaVLTGLppLPG 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 110 RNYVKfGMLDRKQTTFAHLLKSAGYRTciagkwqlgseldsprHF--GFEESllwqhtrgrmdSQKRDTRYPNprlerNG 187
Cdd:COG1368 300 GSPYK-RPGQNNFPSLPSILKKQGYET----------------SFfhGGDGS-----------FWNRDSFYKN-----LG 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 188 TKEDYDEGEFSS-----------DLFADFLcDFMETNrDQPFLAYYpMALV-HCPFcpTPDSEDWDPTSHGSKTYKgqpE 255
Cdd:COG1368 347 FDEFYDREDFDDpfdggwgvsdeDLFDKAL-EELEKL-KKPFFAFL-ITLSnHGPY--TLPEEDKKIPDYGKTTLN---N 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 256 YFGdMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGtdkPIVTQTRFGEVVGAKgemvdagNHVTCIAKWPGVIQPQ- 334
Cdd:COG1368 419 YLN-AVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG---PRSPGKTDYENPLER-------YRVPLLIYSPGLKKPKv 487
|
330
....*....|....*...
gi 1270232598 335 --RLTSQIidfsDFLPTM 350
Cdd:COG1368 488 idTVGSQI----DIAPTL 501
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
48-355 |
1.30e-14 |
|
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: 73.87 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 48 PNIVLIMADDMGFECIGS-NGSLDYqTPNIDRIASEGLRFEHCYSQPICTPSrVK----LMTG--MTNKRNYVKFGMLDR 120
Cdd:cd16015 1 PNVIVILLESFSDPYIDKdVGGEDL-TPNLNKLAKEGLYFGNFYSPGFGGGT-ANgefeVLTGlpPLPLGSGSYTLYKLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 121 KQTTFAHLLKSAGYRTC--IAGK---WQLGSELdspRHFGFEESLlwqhtrgrmdsQKRDTRYPNPRLERNGTkedYDEg 195
Cdd:cd16015 79 PLPSLPSILKEQGYETIfiHGGDasfYNRDSVY---PNLGFDEFY-----------DLEDFPDDEKETNGWGV---SDE- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 196 efssDLFaDFLCDFMETNRDQPFLAYypmaLV----HCPFcptPDSEDWDPTSHGSKTYKGQPEYFGDMVAYVDKIVGRI 271
Cdd:cd16015 141 ----SLF-DQALEELEELKKKPFFIF----LVtmsnHGPY---DLPEEKKDEPLKVEEDKTELENYLNAIHYTDKALGEF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 272 DQKLGDLGIRENTLLIFTGDNgtdkpivtQTRFGEVVGAKGEMVDAGNHVTCIAKWPGVIQPQ---RLTSQIidfsDFLP 348
Cdd:cd16015 209 IEKLKKSGLYENTIIVIYGDH--------LPSLGSDYDETDEDPLDLYRTPLLIYSPGLKKPKkidRVGSQI----DIAP 276
|
....*..
gi 1270232598 349 TMCEVAD 355
Cdd:cd16015 277 TLLDLLG 283
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
42-350 |
2.75e-08 |
|
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: 56.07 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 42 QRSGDRPNIVLIMADDMGFEcigsngSLDYQT-PNIDRIASEGLRFEHCYSQPICTpsrvklMTGMTN-----KRNYVkF 115
Cdd:COG3083 239 SDPAKPPNILLIVVDSLRAD------MLDPEVmPNLYAFAQRSLRFTNHYSSGNST------RAGLFGlfyglPGNYW-D 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 116 GMLD-RKQTTFAHLLKSAGYRTCIAGkwqlGSELDSPRhfgFEESLLwqhtrgrmdsqkrdTRYPNPRLERNGTKEDYDe 194
Cdd:COG3083 306 SILAeRTPPVLIDALQQQGYQFGLFS----SAGFNSPL---FRQTIF--------------SDVSLPRLHTPGGPAQRD- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 195 gefsSDLFADFLCDFMETNRDQPFLAYYPMALVH---------CPFCPTPDSEDWDPTSHGSKT-----YKGQpeyfgdm 260
Cdd:COG3083 364 ----RQITAQWLQWLDQRDSDRPWFSYLFLDAPHaysfpadypKPFQPSEDCNYLALDNESDPTpfknrYRNA------- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 261 VAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGTDkpivtqtrFGEV----VGAKGEMVDAGNHVTCIAKWPGvIQPQ-- 334
Cdd:COG3083 433 VHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEE--------FNENgqnyWGHNSNFSRYQLQVPLVIHWPG-TPPQvi 503
|
330
....*....|....*..
gi 1270232598 335 -RLTSQIidfsDFLPTM 350
Cdd:COG3083 504 sKLTSHL----DIVPTL 516
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
358-446 |
2.80e-03 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 37.23 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 358 VPANltIDGQSFLPVLQGIEGQG-RESMFM-WYERNGRPNKAREFA-RNQRYKL---YGD---GSFFDVEMDRNEkspLQ 428
Cdd:pfam16347 1 IPAD--MQGKSFLPLLKGKKPKNwRDALYYhYYEYPAEHAVKRHYGvRTERYKLihfYNDideWELYDLQKDPKE---MN 75
|
90 100
....*....|....*....|
gi 1270232598 429 SLTDDQK--EIRSKLQAKID 446
Cdd:pfam16347 76 NVYGDPEyaEVQAELKEELE 95
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
46-136 |
4.22e-03 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 39.14 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 46 DRPNIVLIM-----ADDMGfecigSNGsldYQ---TPNIDRIASEGLRFEHCYSQ-PICTPSrVKLM-TGMTNKrNYVKF 115
Cdd:cd16017 1 KPKNVVLVIgesarRDHMS-----LYG---YPrdtTPFLSKLKKNLIVFDNVISCgTSTAVS-LPCMlSFANRE-NYDRA 70
|
90 100
....*....|....*....|.
gi 1270232598 116 gmldRKQTTFAHLLKSAGYRT 136
Cdd:cd16017 71 ----YYQENLIDLAKKAGYKT 87
|
|
| |
