|
Name |
Accession |
Description |
Interval |
E-value |
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
27-448 |
0e+00 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 514.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYHNGV-MSSETPNIDSIAEKGMLLTDYYAQPSCTAGRSAFLTGQLPVRTGMHSVGLPGGPVG 105
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIgRGAPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGLTTVGLPGSPGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 106 LSADTPTLPEVLKTMGYVTGQFGKNHLGDRDEFLPTMHGFDEYWGWLYHlnameytedpdwpkdgsldafaprnviyars 185
Cdd:cd16142 81 LPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYH------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 186 dgkggqtieddgalsiermrTLDDEVNKHAINFIERAVEADKPFFTWYCPSRGHVWTHLSPEYEAMLGqnGWGLQEVVMK 265
Cdd:cd16142 130 --------------------TIDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSS--GKGKYADSMV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 266 DLDDHVGEMMAKMEELGIADNTIIIFTADNGPEIMTWPDGGMTPFHGEKGTTWEGGVRAPALVSWPGKIPAGTVGNGIFD 345
Cdd:cd16142 188 ELDDHVGQILDALDELGIADNTIVIFTTDNGPEQDVWPDGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVS 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 346 GMDWLPTLVAAAGGPtDLKEKMLkghdGFKAHLDGYNQVDMLTEKGE-SNRKEIYYYERDKLQAVRIGDWKAHFVVQNHG 424
Cdd:cd16142 268 HLDWFPTLAALAGAP-DPKDKLL----GKDRHIDGVDQSPFLLGKSEkSRRSEFFYFGEGELGAVRWKNWKVHFKAQEDT 342
|
410 420
....*....|....*....|....*..
gi 1376796650 425 W---SGPKEELNAPLLFNLRRDPYERA 448
Cdd:cd16142 343 GgptGEPFYVLTFPLIFNLRRDPKERY 369
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
26-447 |
5.53e-128 |
|
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: 378.06 E-value: 5.53e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 26 QPNIFVIFTDDIGISNLSAYhnGVMSSETPNIDSIAEKGMLLTDYYA-QPSCTAGRSAFLTGQLPVRTGMHS-VGLPGGP 103
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCY--GSPLIKTPNIDRLAAEGVRFTDFYAaAPVCSPSRAALLTGRYPVRVGLPGvVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 104 VGLSADTPTLPEVLKTMGYVTGQFGKNHLGDRDEFLPTMHGFDEYWGWLY--HLNAMEYTEDPDWPKDGSLDAfaPRNVI 181
Cdd:cd16026 79 GGLPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYsnDMWPFPLYRNDPPGPLPPLME--NEEVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 182 YARSDgkggqtieddgalsierMRTLDDEVNKHAINFIERAveADKPFFTWYCPSRGHVWTHLSPEYEamlGQNGWGLQE 261
Cdd:cd16026 157 EQPAD-----------------QSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFK---GRSGAGLYG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 262 VVMKDLDDHVGEMMAKMEELGIADNTIIIFTADNGPEIMTWPDGGMT-PFHGEKGTTWEGGVRAPALVSWPGKIPAGTVG 340
Cdd:cd16026 215 DVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHGGSAgPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 341 NGIFDGMDWLPTLVAAAGG--PTDLKekmlkghdgfkahLDGYNQVDMLTEKGESNRKEIYYYERDK-LQAVRIGDWKAH 417
Cdd:cd16026 295 DELASTMDLLPTLAALAGAplPEDRV-------------IDGKDISPLLLGGSKSPPHPFFYYYDGGdLQAVRSGRWKLH 361
|
410 420 430
....*....|....*....|....*....|....
gi 1376796650 418 FVVQNHGWSGPKEE----LNAPLLFNLRRDPYER 447
Cdd:cd16026 362 LPTTYRTGTDPGGLdptkLEPPLLYDLEEDPGET 395
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-485 |
4.39e-101 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 308.73 E-value: 4.39e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 1 MKRIFHLVTLSVLSSFslsAWSAQEQPNIFVIFTDDIGISNLSAYHNGVMssETPNIDSIAEKGMLLTDYYAQ-PSCTAG 79
Cdd:COG3119 1 MKRLLLLLLALLAAAA---AAAAAKRPNILFILADDLGYGDLGCYGNPLI--KTPNIDRLAAEGVRFTNAYVTsPVCSPS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 80 RSAFLTGQLPVRTGMHSVGlPGGPVGLSADTPTLPEVLKTMGYVTGQFGKNHLgdrdeflptmhgfdeywgwlyhlname 159
Cdd:COG3119 76 RASLLTGRYPHRTGVTDNG-EGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 160 ytedpdwpkdgsldafaprnviyarsdgkggqtieddgalsiermrTLDDEVNKHAINFIERAVEADKPFFTWYCPSRGH 239
Cdd:COG3119 128 ----------------------------------------------YLTDLLTDKAIDFLERQADKDKPFFLYLAFNAPH 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 240 VWTHLSPEYEAMLGQNGWGLQEVVMKD--------------------LDDHVGEMMAKMEELGIADNTIIIFTADNGPEi 299
Cdd:COG3119 162 APYQAPEEYLDKYDGKDIPLPPNLAPRdlteeelrraraayaamieeVDDQVGRLLDALEELGLADNTIVVFTSDNGPS- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 300 mtWPDGGmtpFHGEKGTTWEGGVRAPALVSWPGKIPAGTVGNGIFDGMDWLPTLVAAAGGPTDlkekmlkghdgfkAHLD 379
Cdd:COG3119 241 --LGEHG---LRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIP-------------EDLD 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 380 GYNQVDMLTEKGESNRKEIY--YYERDKLQAVRIGDWKAhfvVQNHGWSGPKEelnaplLFNLRRDPYER---AAEESGM 454
Cdd:COG3119 303 GRSLLPLLTGEKAEWRDYLYweYPRGGGNRAIRTGRWKL---IRYYDDDGPWE------LYDLKNDPGETnnlAADYPEV 373
|
490 500 510
....*....|....*....|....*....|.
gi 1376796650 455 yLKWMgqkmwafgpaQAAVQQHLATFQEWPP 485
Cdd:COG3119 374 -VAEL----------RALLEAWLKELGDPPL 393
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
27-447 |
1.23e-86 |
|
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: 272.55 E-value: 1.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYHNGVMSseTPNIDSIAEKGMLLTDYYA-QPSCTAGRSAFLTGQLPVRTGMHSVGLPGGPVG 105
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIK--TPNLDRLAAEGMRFTQHYAgAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 106 LSADTPTLPEVLKTMGYVTGQFGKNHLGDRD-EFLPTMHGFDEYWGWLYHLNAMEYTEDPDWPKDGSLDAfaPRNVIYAR 184
Cdd:cd16145 79 LPPDDVTLAEVLKKAGYATAAFGKWGLGGPGtPGHPTKQGFDYFYGYLDQVHAHNYYPEYLWRNGEKVPL--PNNVIPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 185 SDGKGGQTIEDDGAlsiermrtlDDEVNKHAINFIERAveADKPFF------------------------TWYCPSRGHV 240
Cdd:cd16145 157 DEGNNAGGGGGTYS---------HDLFTDEALDFIREN--KDKPFFlylaytlphaplqvpddgpykykpKDPGIYAYLP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 241 WTHLSPEYEAMlgqngwglqevvMKDLDDHVGEMMAKMEELGIADNTIIIFTADNGPEI-------MTWPDGGmTPFHGE 313
Cdd:cd16145 226 WPQPEKAYAAM------------VTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFFDSN-GPLRGY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 314 KGTTWEGGVRAPALVSWPGKIPAGTVGNGIFDGMDWLPTLVAAAGGPtdlkekmlkghdgFKAHLDGYNQVDMLTEKGES 393
Cdd:cd16145 293 KRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAE-------------PPEDIDGISLLPTLLGKPQQ 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1376796650 394 NRKEIYYYERDKL---QAVRIGDWKAhfvVQNHGWSGPKEelnaplLFNLRRDPYER 447
Cdd:cd16145 360 QQHDYLYWEFYEGggaQAVRMGGWKA---VRHGKKDGPFE------LYDLSTDPGET 407
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
27-447 |
7.89e-84 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 265.18 E-value: 7.89e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYhngvMSS--ETPNIDSIAEKGMLLTDYYA-QPSCTAGRSAFLTGQLPVRTGM--HSVGLPG 101
Cdd:cd16144 1 PNIVLILVDDLGWADLGCY----GSKfyETPNIDRLAKEGMRFTQAYAaAPVCSPSRASILTGQYPARLGItdVIPGRRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 102 GP-----------VGLSADTPTLPEVLKTMGYVTGQFGKNHLGDRDEFLPTMHGFDEYWGwlyhlnameYTEDPDWPKDG 170
Cdd:cd16144 77 PPdntklipppstTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIG---------GTGNGGPPSYY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 171 SLDAFAPRNVIYARSDGKggqtieddgalsiermrtLDDEVNKHAINFIERAveADKPFFTWYCPSRGHVWTHLSPE--- 247
Cdd:cd16144 148 FPPGKPNPDLEDGPEGEY------------------LTDRLTDEAIDFIEQN--KDKPFFLYLSHYAVHTPIQARPElie 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 248 -YEAMLGQNGWGLQEVV----MKDLDDHVGEMMAKMEELGIADNTIIIFTADNGPeiMTWPDGGMT---PFHGEKGTTWE 319
Cdd:cd16144 208 kYEKKKKGLRKGQKNPVyaamIESLDESVGRILDALEELGLADNTLVIFTSDNGG--LSTRGGPPTsnaPLRGGKGSLYE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 320 GGVRAPALVSWPGKIPAGTVGNGIFDGMDWLPTLVAAAGGPTDLKEkmlkghdgfkaHLDGYNQVDMLTEKGE-SNRKEI 398
Cdd:cd16144 286 GGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQ-----------HLDGVSLVPLLKGGEAdLPRRAL 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1376796650 399 Y----YYERDKLQ---AVRIGDWKahfVVQNHgwsgpkeELNAPLLFNLRRDPYER 447
Cdd:cd16144 355 FwhfpHYHGQGGRpasAIRKGDWK---LIEFY-------EDGRVELYNLKNDIGET 400
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
27-447 |
6.35e-78 |
|
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: 249.00 E-value: 6.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSaYHNGvMSSETPNIDSIAEKGMLLTDYYAQPSCTAGRSAFLTGQLPVRTGM-HSVGLPGGPVG 105
Cdd:cd16029 1 PHIVFILADDLGWNDVG-FHGS-DQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMqHGVILAGEPYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 106 LSADTPTLPEVLKTMGYVTGQFGKNHLG-DRDEFLPTMHGFDEYWGwlyHLNAME--YTEDPDWPKDGSLDAFAPRNVIY 182
Cdd:cd16029 79 LPLNETLLPQYLKELGYATHLVGKWHLGfYTWEYTPTNRGFDSFYG---YYGGAEdyYTHTSGGANDYGNDDLRDNEEPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 183 ARSDGKGGQTIEDDGALSIermrtlddeVNKHAinfieraveADKPFFTW-------------------YCPSRGHVWTH 243
Cdd:cd16029 156 WDYNGTYSTDLFTDRAVDI---------IENHD---------PSKPLFLYlafqavhaplqvppeyadpYEDKFAHIKDE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 244 LSPEYEAMlgqngwglqevvMKDLDDHVGEMMAKMEELGIADNTIIIFTADNGPEIMTWPDGGMTPFHGEKGTTWEGGVR 323
Cdd:cd16029 218 DRRTYAAM------------VSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGGSNYPLRGGKNTLWEGGVR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 324 APALVSWPG-KIPAGTVGNGIFDGMDWLPTLVAAAGG-PTDLKekmlkghdgfkaHLDGYNQVDMLTEKGESNRKEI-YY 400
Cdd:cd16029 286 VPAFVWSPLlPPKRGTVSDGLMHVTDWLPTLLSLAGGdPDDLP------------PLDGVDQWDALSGGAPSPRTEIlLN 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1376796650 401 YERDKLQ----AVRIGDWKahFVVqnhgwsgpkeelNAPlLFNLRRDPYER 447
Cdd:cd16029 354 IDDITRTtggaAIRVGDWK--LIV------------GKP-LFNIENDPCER 389
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
26-490 |
9.29e-77 |
|
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: 248.54 E-value: 9.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 26 QPNIFVIFTDDIGISNLSAYhnGVMSSETPNIDSIAEKGMLLTDYY-AQPSCTAGRSAFLTGQLPVRTGMHSVG------ 98
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVF--GEPSRETPNLDRMAAEGMLFTDFYsANPLCSPSRAALLTGRLPIRNGFYTTNaharna 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 99 -LPGGPVGLSADTPTL-PEVLKTMGYVTGQFGKNHLGDRDEFLPTMHGFDEYWGwlyhlnameyteDPDWPKDGSLDAFA 176
Cdd:cd16157 79 yTPQNIVGGIPDSEILlPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFG------------APNCHFGPYDNKAY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 177 PRNVIYaRSDGKGGQTIEDdgaLSIERMRTLDDEVN---KHAINFIERAVEADKPFFTWYCPSRGHvwthlSPEY--EAM 251
Cdd:cd16157 147 PNIPVY-RDWEMIGRYYEE---FKIDKKTGESNLTQiylQEALEFIEKQHDAQKPFFLYWAPDATH-----APVYasKPF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 252 LGQNGWGLQEVVMKDLDDHVGEMMAKMEELGIADNTIIIFTADNGPEIMTWPD--GGMTPFHGEKGTTWEGGVRAPALVS 329
Cdd:cd16157 218 LGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALISAPEqgGSNGPFLCGKQTTFEGGMREPAIAW 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 330 WPGKIPAGTVGNGIFDGMDWLPTLVAAAG--GPTDLkekmlkghdgfkaHLDGYNQVDMLTEKGESNRKeIYYYERDKLQ 407
Cdd:cd16157 298 WPGHIKPGQVSHQLGSLMDLFTTSLALAGlpIPSDR-------------AIDGIDLLPVLLNGKEKDRP-IFYYRGDELM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 408 AVRIGDWKAHFvvqnHGWSGPKEELN------------------------APLLFNLRRDPYER--AAEESGMYLKWMGQ 461
Cdd:cd16157 364 AVRLGQYKAHF----WTWSNSWEEFRkginfcpgqnvpgvtthnqtdhtkLPLLFHLGRDPGEKypISFKSAEYKQAMPR 439
|
490 500
....*....|....*....|....*....
gi 1376796650 462 KMwafgpaqAAVQQHLATFQewpPVTPDL 490
Cdd:cd16157 440 IS-------KVVQQHQKTLV---PGEPQL 458
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
27-447 |
1.24e-75 |
|
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: 243.61 E-value: 1.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYHNGVMssETPNIDSIAEKGMLLTDYYAQPSCTAGRSAFLTGQLPVRTGMHSVgLPGGPVgL 106
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPIL--KTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTGVWHT-ILGRER-M 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 107 SADTPTLPEVLKTMGYVTGQFGKNHLGDRDEFLPTMHGFDEywgWLYHLNAmEYTEDPDWPKDGSLDAFAPRNviyarsd 186
Cdd:cd16146 77 RLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDE---VLGHGGG-GIGQYPDYWGNDYFDDTYYHN------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 187 gkgGQTIEDDGalsiermrTLDDEVNKHAINFIERAveADKPFFTWYCPSRGHVWTHLSPEYEAMLGQNGWGLQEVV--- 263
Cdd:cd16146 146 ---GKFVKTEG--------YCTDVFFDEAIDFIEEN--KDKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAfyg 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 264 -MKDLDDHVGEMMAKMEELGIADNTIIIFTADNGPEIMTW--PDGGMTpfhGEKGTTWEGGVRAPALVSWPGKIPAGTVG 340
Cdd:cd16146 213 mIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPkrFNAGMR---GKKGSVYEGGHRVPFFIRWPGKILAGKDV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 341 NGIFDGMDWLPTLVAAAGGPTDLKEKmlkghdgfkahLDGYNQVDMLTEKGESNRKEIYYYERDklQAVRIGDWKAHFVV 420
Cdd:cd16146 290 DTLTAHIDLLPTLLDLCGVKLPEGIK-----------LDGRSLLPLLKGESDPWPERTLFTHSG--RWPPPPKKKRNAAV 356
|
410 420
....*....|....*....|....*..
gi 1376796650 421 QNHGWSGPKEELNAPLLFNLRRDPYER 447
Cdd:cd16146 357 RTGRWRLVSPKGFQPELYDIENDPGEE 383
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
27-447 |
1.56e-75 |
|
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: 242.88 E-value: 1.56e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYhNGVMSSETPNIDSIAEKGMLLTDYYAqPS--CTAGRSAFLTGQLPVRTGMHSVGLPG-GP 103
Cdd:cd16143 1 PNIVIILADDLGYGDISCY-NPDSKIPTPNIDRLAAEGMRFTDAHS-PSsvCTPSRYGLLTGRYPWRSRLKGGVLGGfSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 104 VGLSADTPTLPEVLKTMGYVTGQFGKNHLGdrdeflptmhgFDEYWGWLYHLNAMEYtEDPDW---PKDGSLD-----AF 175
Cdd:cd16143 79 PLIEPDRVTLAKMLKQAGYRTAMVGKWHLG-----------LDWKKKDGKKAATGTG-KDVDYskpIKGGPLDhgfdyYF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 176 AprnviYARSDgkggqtieddgalsiermrtLDDEVNKHAINFIERAVEADKPFFTWYCPSRGHvwTHLSPEyEAMLGQN 255
Cdd:cd16143 147 G-----IPASE--------------------VLPTLTDKAVEFIDQHAKKDKPFFLYFALPAPH--TPIVPS-PEFQGKS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 256 GWGLQEVVMKDLDDHVGEMMAKMEELGIADNTIIIFTADNGPEIMtwPDGGMT---------PFHGEKGTTWEGGVRAPA 326
Cdd:cd16143 199 GAGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPY--ADYKELekfghdpsgPLRGMKADIYEGGHRVPF 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 327 LVSWPGKIPAGTVGNGIFDGMDWLPTLVAAAGGPtdlkekmLKGHDGfkahLDGYNQVDMLT-EKGESNRKEIYYYERDK 405
Cdd:cd16143 277 IVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQK-------LPDNAA----EDSFSFLPALLgPKKQEVRESLVHHSGNG 345
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1376796650 406 LQAVRIGDWKAHFVVQNHGWSGP----KEELNAPLLFNLRRDPYER 447
Cdd:cd16143 346 SFAIRKGDWKLIDGTGSGGFSYPrgkeKLGLPPGQLYNLSTDPGES 391
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
27-446 |
1.55e-74 |
|
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: 243.12 E-value: 1.55e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYhnGVMSSETPNIDSIAEKGMLLTDYYAQ-PSCTAGRSAFLTGQLPVRTGMH-SVGLPGGPV 104
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCY--GHPSSSTPNLDRLAANGLRFTDFYSSsPVCSPSRAALLTGRYQVRSGVYpGVFYPGSRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 105 GLSADTPTLPEVLKTMGYVTGQFGKNHLG--DRDEFLPTMHGFDEYWGwlyhlnaMEYTED-----------PDWPKDGS 171
Cdd:cd16158 80 GLPLNETTIAEVLKTVGYQTAMVGKWHLGvgLNGTYLPTHQGFDHYLG-------IPYSHDqgpcqnltcfpPNIPCFGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 172 LD-AFAPRNVIYarsdgkgGQTIEDDGAlsieRMRTLDDEVNKHAINFIERAVEADKPFFTWYCPSRGHVWTHLSPEYEa 250
Cdd:cd16158 153 CDqGEVPCPLFY-------NESIVQQPV----DLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFA- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 251 mlGQNGWGLQEVVMKDLDDHVGEMMAKMEELGIADNTIIIFTADNGPEIMTWPDGGMTPF-HGEKGTTWEGGVRAPALVS 329
Cdd:cd16158 221 --GRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRKSRGGNAGLlKCGKGTTYEGGVREPAIAY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 330 WPGKIPAGtVGNGIFDGMDWLPTLVAAAGGPtdLKEkmlkghdgfkAHLDGYNQVDMLTEKGESNRKEIYYYERDKLQ-- 407
Cdd:cd16158 299 WPGRIKPG-VTHELASTLDILPTIAKLAGAP--LPN----------VTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPdk 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1376796650 408 ---AVRIGDWKAHFVVQNHGWSG--------PKEEL---NAPLLFNLRRDPYE 446
Cdd:cd16158 366 gvfAVRWGKYKAHFYTQGAAHSGttpdkdchPSAELtshDPPLLFDLSQDPSE 418
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
26-446 |
2.48e-72 |
|
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.
Pssm-ID: 293780 [Multi-domain] Cd Length: 383 Bit Score: 234.29 E-value: 2.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 26 QPNIFVIFTDDIGISNLSAyhNGVMSS-ETPNIDSIAEKGMLLTDYY-AQPSCTAGRSAFLTGQLPVRTGMHSVGLPGGP 103
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGA--NWAPNAiLTPNLDKLAAEGTRFVDWYsAASVCSPSRASLMTGRLGLRNGVGHNFLPTSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 104 VGLSADTPTLPEVLKTMGYVTGQFGKNHLGDRDEFLPTMHGFDEYWGWLYhlnameytedpdwpkdgSLDAfaprnviya 183
Cdd:cd16161 79 GGLPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPF-----------------SHDS--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 184 rsdgkggqtieddgalsiermrTLDDEVNKHAINFIERAVEADKPFFTWYCPSRGHVWTHLSPEYEAML---GQNGWGLQ 260
Cdd:cd16161 133 ----------------------SLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTsgrGPYGDALQ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 261 EvvmkdLDDHVGEMMAKMEELGIADNTIIIFTADNGP---------EIMTWPDGGMTPFHGEKGTTWEGGVRAPALVSWP 331
Cdd:cd16161 191 E-----MDDLVGQIMDAVKHAGLKDNTLTWFTSDNGPwevkcelavGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 332 GKIPAGTVGNGIFDGMDWLPTLVAAAGG--PTDlkekmlkghdgfkAHLDGYNQVDMLTEKGESNRKEIYYY-----ERD 404
Cdd:cd16161 266 GRIPANSTSAALVSTLDIFPTVVALAGAslPPG-------------RIYDGKDLSPVLFGGSKTGHRCLFHPnsgaaGAG 332
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1376796650 405 KLQAVRIGDWKAHFVVQN----HGWSGPKEELNAPLLFNLRRDPYE 446
Cdd:cd16161 333 ALSAVRCGDYKAHYATGGalacCGSTGPKLYHDPPLLFDLEVDPAE 378
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
26-446 |
4.15e-69 |
|
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: 227.70 E-value: 4.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 26 QPNIFVIFTDDIGISNLSAYhnGVMSSETPNIDSIAEKGMLLTDYYAQPS-CTAGRSAFLTGQLPVRTGMHS---VGLPG 101
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASY--GHPTQERGPIDDMAAEGIRFTQAYSADSvCTPSRAALLTGRLPIRSGMYGgtrVFLPW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 102 GPVGLSADTPTLPEVLKTMGYVTGQFGKNHLG------DRDEFLPTMHGFDEYWGWLYHLNAM--EYTEDPDWPKDGSLD 173
Cdd:cd16160 79 DIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennhSDGAHLPSHHGFDFVGTNLPFTNSWacDDTGRHVDFPDRSAC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 174 AFAPRNVIYArsdgkggQTIEDDgalsiermrTLDDEVNKHAINFIERAVEadKPFFTWYCPSRGHVWTHLSPEY--EAM 251
Cdd:cd16160 159 FLYYNDTIVE-------QPIQHE---------HLTETLVGDAKSFIEDNQE--NPFFLYFSFPQTHTPLFASKRFkgKSK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 252 LGQNGWGLQEvvmkdLDDHVGEMMAKMEELGIADNTIIIFTADNGPEIMTWPDGGMT-PFHGEKGTTWEGGVRAPALVSW 330
Cdd:cd16160 221 RGRYGDNINE-----MSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTgGLKGGKGNSWEGGIRVPFIAYW 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 331 PGKIPAGtVGNGIFDGMDWLPTLVAAAGG--PTDLkekmlkghdgfkaHLDGYNQVDMLTEKGESNRKEIYYYERDKLQA 408
Cdd:cd16160 296 PGTIKPR-VSHEVVSTMDIFPTFVDLAGGtlPTDR-------------IYDGLSITDLLLGEADSPHDDILYYCCSRLMA 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376796650 409 VRIGDWKAHF----------VVQNHGWSGPKE--------------ELNAPLLFNLRRDPYE 446
Cdd:cd16160 362 VRYGSYKIHFktqplpsqesLDPNCDGGGPLSdyivcydcedecvtKHNPPLIFDVEKDPGE 423
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-447 |
8.17e-68 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 222.47 E-value: 8.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYhnGVMSSETPNIDSIAEKGMLLTDYYAQPSCTAGRSAFLTGQLPVRTGMHsvglpGGPvgL 106
Cdd:cd16151 1 PNIILIMADDLGYECIGCY--GGESYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVV-----FGY--L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 107 SADTPTLPEVLKTMGYVTGQFGKNHLGDRDEFLPTMH--GFDEYwgWLYHLNAMEYtedpdwpkdgslDAFAPRNVIYAR 184
Cdd:cd16151 72 DPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGDYPHefGFDEY--CLWQLTETGE------------KYSRPATPTFNI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 185 SDGKGGQTIEDD-GAlsiermrtldDEVNKHAINFIERavEADKPFFTWY------CPsrgHVWTHLSPeyeamlgqnGW 257
Cdd:cd16151 138 RNGKLLETTEGDyGP----------DLFADFLIDFIER--NKDQPFFAYYpmvlvhDP---FVPTPDSP---------DW 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 258 GLQEVVMKD-----------LDDHVGEMMAKMEELGIADNTIIIFTADNG--PEIMTWPDGGMTPfhGEKGTTWEGGVRA 324
Cdd:cd16151 194 DPDDKRKKDdpeyfpdmvayMDKLVGKLVDKLEELGLRENTIIIFTGDNGthRPITSRTNGREVR--GGKGKTTDAGTHV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 325 PALVSWPGKIPAGTVGNGIFDGMDWLPTLVAAAGGPtdlkekMLKGHDgfkahLDGYNQVDMLT-EKGESNRKEIYYYER 403
Cdd:cd16151 272 PLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAP------LPEDYP-----LDGRSFAPQLLgKTGSPRREWIYWYYR 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1376796650 404 -----DKLQAVRIGDWKahfvvqnhgwsgpkeeLNAP-LLFNLRRDPYER 447
Cdd:cd16151 341 nphkkFGSRFVRTKRYK----------------LYADgRFFDLREDPLEK 374
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
27-362 |
4.76e-62 |
|
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: 202.67 E-value: 4.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYHNGVMssETPNIDSIAEKGMLLTDYYAQ-PSCTAGRSAFLTGQLPVRTGMHSVglPGGPVG 105
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDI--KTPNLDRLAAEGVRFTNAYVAsPVCSPSRASLLTGRYPHRHGVRGN--VGNGGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 106 LSADTPTLPEVLKTMGYVTGQFGKNHlgdrdeflptmhgfdeywgwlyhlnameytedpdwpkdgsldafaprnviyars 185
Cdd:cd16022 77 LPPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 186 dgkggqtieddgalsiermrtlddevnKHAINFIERAVEaDKPFFTWYCPSRGHvwthlSP-EYEAMlgqngwglqevvM 264
Cdd:cd16022 103 ---------------------------DEAIDFIERRDK-DKPFFLYVSFNAPH-----PPfAYYAM------------V 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 265 KDLDDHVGEMMAKMEELGIADNTIIIFTADNGPEIMtwpDGGMtpfHGEKGTTWEGGVRAPALVSWPGKIPAGTVGNGIF 344
Cdd:cd16022 138 SAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLG---DHGL---RGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALV 211
|
330
....*....|....*...
gi 1376796650 345 DGMDWLPTLVAAAGGPTD 362
Cdd:cd16022 212 SLLDLLPTLLDLAGIEPP 229
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
25-447 |
2.20e-60 |
|
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: 203.44 E-value: 2.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 25 EQPNIFVIFTDDIGISNLSAYhnGvmsSE--TPNIDSIAEKGMLLTDYYAQPSCTAGRSAFLTGQLPVRTGMHSV----- 97
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCF--G---GEipTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTMaelat 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 98 GLPGGPVGLSADTPTLPEVLKTMGYVTGQFGKNHLGDRDeflptmhgfdeywgwlYHLNameytedpdwpkdgslDAFAp 177
Cdd:cd16025 76 GKPGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPDD----------------YYST----------------DDLT- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 178 rnviyarsdgkggqtieddgalsiermrtlddevnKHAINFIERAVEADKPFFTWYCPSRGHvWTHLSPE---------- 247
Cdd:cd16025 123 -----------------------------------DKAIEYIDEQKAPDKPFFLYLAFGAPH-APLQAPKewidkykgky 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 248 ---YEAM----------LG--QNGWGL------------------------QEV---VMKDLDDHVGEMMAKMEELGIAD 285
Cdd:cd16025 167 dagWDALreerlerqkeLGliPADTKLtprppgvpawdslspeekklearrMEVyaaMVEHMDQQIGRLIDYLKELGELD 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 286 NTIIIFTADNGPEIMT-WPDGGMTPFHGEKGTTWEGGVRAPALVSWPGKIPA-GTVGNGIFDGMDWLPTLVAAAGGPTDl 363
Cdd:cd16025 247 NTLIIFLSDNGASAEPgWANASNTPFRLYKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHVIDIAPTILELAGVEYP- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 364 kekmlKGHDGFKAH-LDGYNQVDMLTEKGESNRKEIYYYERDKLQAVRIGDWKAHFVVQNHGWSGPKEelnaplLFNLRR 442
Cdd:cd16025 326 -----KTVNGVPQLpLDGVSLLPTLDGAAAPSRRRTQYFELFGNRAIRKGGWKAVALHPPPGWGDQWE------LYDLAK 394
|
....*
gi 1376796650 443 DPYER 447
Cdd:cd16025 395 DPSET 399
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
26-447 |
6.35e-57 |
|
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: 197.51 E-value: 6.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 26 QPNIFVIFTDDIGISNLSAYHNGvmSSETPNIDSIAEKGMLLT-DYYAQPSCTAGRSAFLTGQLPVRTGMHSVGLP---- 100
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGND--TIRTPNIDRLAKEGVKLThHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMrvil 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 101 --GGPVGLSADTPTLPEVLKTMGYVTGQFGKNHLG------DRDEFLPTMHGFDEYWGW-LYHLN--------AMEYTED 163
Cdd:cd16159 79 ftASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGlhcesrNDFCHHPLNHGFDYFYGLpLTNLKdcgdgsngEYDLSFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 164 PDWPK----------------------------------------DGSLDAFAPRNVIYARSDGKGGQTIEddgalsier 203
Cdd:cd16159 159 PLFPLltafvlitaltiflllylgavskrffvfllilsllfislfFLLLITNRYFNCILMRNHEVVEQPMS--------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 204 MRTLDDEVNKHAINFIERAVEadKPFFTWYcpSRGHVWTHL--SPEYeamLGQNGWGLQEVVMKDLDDHVGEMMAKMEEL 281
Cdd:cd16159 230 LENLTQRLTKEAISFLERNKE--RPFLLVM--SFLHVHTALftSKKF---KGRSKHGRYGDNVEEMDWSVGQILDALDEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 282 GIADNTIIIFTADNGPEIMTWPDGGMTPFH------GEKGTTWEGGVRAPALVSWPGKIPAGTVGNGIFDGMDWLPTLVA 355
Cdd:cd16159 303 GLKDNTFVYFTSDNGGHLEEISVGGEYGGGnggiygGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 356 AAGG--PTDLkekmlkghdgfkaHLDGYNQVDMLTekGESNRKE---IYYYERDKLQAVRIGD------WKAHFVVQN-- 422
Cdd:cd16159 383 LAGAplPSDR-------------IIDGRDLMPLLT--GQEKRSPhefLFHYCGAELHAVRYRPrdggavWKAHYFTPNfy 447
|
490 500 510
....*....|....*....|....*....|....*..
gi 1376796650 423 ---HGW--------SGPK-EELNAPLLFNLRRDPYER 447
Cdd:cd16159 448 pgtEGCcgtllcrcFGDSvTHHDPPLLFDLSADPSES 484
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
27-447 |
2.61e-56 |
|
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: 191.95 E-value: 2.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYHNGVmssETPNIDSIAEKGMLLTDYY-AQPSCTAGRSAFLTGQLPVRTGMHsvGLPGGPVG 105
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVV---KTPNLDRLAAEGVRFTNAFtTAPVCSPSRSALLTGLYPHQNGAH--GLRSRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 106 LSADTPTLPEVLKTMGYVTGQFGKNHlgdrdeflptmHGFDEYWGWLYHLNAMEYTEDPDWPKDGSldafaprnviyars 185
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTH-----------YNPDAVFPFDDEMRGPDDGGRNAWDYASN-------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 186 dgkggqtieddgalsiermrtlddevnkhAINFIERAvEADKPFFTWYCPSRGHV-WTHLSPEyeamlgQNGWGLQEVV- 263
Cdd:cd16027 131 -----------------------------AADFLNRA-KKGQPFFLWFGFHDPHRpYPPGDGE------EPGYDPEKVKv 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 264 --------------------MKDLDDHVGEMMAKMEELGIADNTIIIFTADNGPeimtwpdggmtPFHGEKGTTWEGGVR 323
Cdd:cd16027 175 ppylpdtpevredladyydeIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----------PFPRAKGTLYDSGLR 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 324 APALVSWPGKIPAGTVGNGIFDGMDWLPTLVAAAGGPTDlkekmlkghdgfkAHLDGYNQVDMLTEKGESNRKEI----- 398
Cdd:cd16027 244 VPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPP-------------EYLQGRSFLPLLKGEKDPGRDYVfaerd 310
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1376796650 399 -----YYYERdklqAVRIGDWKAHFvvqnHGWSgpkEElnaplLFNLRRDPYER 447
Cdd:cd16027 311 rhdetYDPIR----SVRTGRYKYIR----NYMP---EE-----LYDLKNDPDEL 348
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
27-358 |
5.19e-52 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 178.39 E-value: 5.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYHNGVmsSETPNIDSIAEKGMLLTDYY-AQPSCTAGRSAFLTGQLPVRTGMHSVGlpggPVG 105
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPR--PTTPFLDRLAEEGLLFSNFYsGGTLTAPSRFALLTGLPPHNFGSYVST----PVG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 106 LSADTPTLPEVLKTMGYVTGQFGKNHLGDRDEFLPTMHGFDEYWGWLYHLNAMEYTEDPDWPKDGsldafaprnviyars 185
Cdd:pfam00884 75 LPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNCSG--------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 186 dgkggqtieddgalsierMRTLDDEVNKHAINFIERAveaDKPFFTWYCPSRGHVWTHLSPEYEAMLGQ---NGWGLQEV 262
Cdd:pfam00884 140 ------------------GGVSDEALLDEALEFLDNN---DKPFFLVLHTLGSHGPPYYPDRYPEKYATfkpSSCSEEQL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 263 V------MKDLDDHVGEMMAKMEELGIADNTIIIFTADNGPEImtwpDGGMTPFHGEKG-TTWEGGVRAPALVSWPGKIP 335
Cdd:pfam00884 199 LnsydntLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESL----GEGGGYLHGGKYdNAPEGGYRVPLLIWSPGGKA 274
|
330 340
....*....|....*....|...
gi 1376796650 336 AGTVGNGIFDGMDWLPTLVAAAG 358
Cdd:pfam00884 275 KGQKSEALVSHVDLFPTILDLAG 297
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
25-447 |
8.98e-49 |
|
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.
Pssm-ID: 293755 [Multi-domain] Cd Length: 429 Bit Score: 173.48 E-value: 8.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 25 EQPNIFVIFTDDIGISNLSAYHNGVMssETPNIDSIAEKGMLLTDYYAQPS-CTAGRSAFLTGQLPVRTGMhsVGLPGGp 103
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIV--KTPNIDRLAKEGVRFDNAFVTTSiCAPSRASILTGQYSHRHGV--TDNNGP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 104 vGLSADTPTLPEVLKTMGYVTGQFGKNHLGDRDEFLPTmhGFDEYWGWlyhlnameytedPDWPKDgsldaFAPRNVIYA 183
Cdd:cd16031 76 -LFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--GFDYWVSF------------PGQGSY-----YDPEFIENG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 184 RSDGKGGQTieddgalsiermrtlDDEVNKHAINFIERAvEADKPFF---------TWYCPSRGHV-------------- 240
Cdd:cd16031 136 KRVGQKGYV---------------TDIITDKALDFLKER-DKDKPFClslsfkaphRPFTPAPRHRglyedvtipepetf 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 241 ----------WTHLSPEYEAMLGQNGWGLQEVV---MKD-------LDDHVGEMMAKMEELGIADNTIIIFTADNGpeim 300
Cdd:cd16031 200 ddddyagrpeWAREQRNRIRGVLDGRFDTPEKYqryMKDylrtvtgVDDNVGRILDYLEEQGLADNTIIIYTSDNG---- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 301 twpdggmtPFHGEKG-----TTWEGGVRAPALVSWPGKIPAGTVGNGIFDGMDWLPTLVAAAGGPTDlkekmlkghdgfk 375
Cdd:cd16031 276 --------FFLGEHGlfdkrLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIP------------- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 376 AHLDGYNQVDMLT-EKGESNRKEIYY---YERD-----KLQAVRIGDWK-AHFVVQNhgwsgPKEElnaplLFNLRRDPY 445
Cdd:cd16031 335 EDMQGRSLLPLLEgEKPVDWRKEFYYeyyEEPNfhnvpTHEGVRTERYKyIYYYGVW-----DEEE-----LYDLKKDPL 404
|
..
gi 1376796650 446 ER 447
Cdd:cd16031 405 EL 406
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
26-446 |
5.31e-47 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 167.75 E-value: 5.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 26 QPNIFVIFTDDIGISNLSAYHNGVMssETPNIDSIAEKGMLLTDYYAQ-PSCTAGRSAFLTGQLPVRTGMHSVGLPggpv 104
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPV--KTPNLDRLAKEGVVFTNAVSNyPVCSPYRASLLTGQYPLTNGVFGNDVP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 105 gLSADTPTLPEVLKTMGYVTGQFGKNHL--------GDRDEFLPTM--HGFDEYWGWL---YHLNAMEYTEDPDWPKDGS 171
Cdd:cd16034 75 -LPPDAPTIADVLKDAGYRTGYIGKWHLdgperndgRADDYTPPPErrHGFDYWKGYEcnhDHNNPHYYDDDGKRIYIKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 172 LDAFAprnviyarsdgkggQTieddgalsiermrtlDDevnkhAINFIERAVEADKPFFTWYCPSRGHVWTHLSPE-YEA 250
Cdd:cd16034 154 YSPDA--------------ET---------------DL-----AIEYLENQADKDKPFALVLSWNPPHDPYTTAPEeYLD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 251 MLGQNGWGLQEVVMKD--------------------LDDHVGEMMAKMEELGIADNTIIIFTADNGpEIMtwpdGGmtpf 310
Cdd:cd16034 200 MYDPKKLLLRPNVPEDkkeeaglredlrgyyamitaLDDNIGRLLDALKELGLLENTIVVFTSDHG-DML----GS---- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 311 HG--EKGTTWEGGVRAPALVSWPGKIPAGTVGNGIFDGMDWLPTLVAAAGGPTDlkekmlkghdgfkAHLDGYNQVDMLT 388
Cdd:cd16034 271 HGlmNKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIP-------------DTVEGRDLSPLLL 337
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1376796650 389 EKGESNRKEIYYYERDKLQAVRIGDWKAHFVVQNHGWSGPKEELNAPLLFNLRRDPYE 446
Cdd:cd16034 338 GGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVRTDRYTYVRDKNGPWLLFDNEKDPYQ 395
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-360 |
9.43e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 138.91 E-value: 9.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYHNgvmsSE--TPNIDSIAEKGMLLTDYY-AQPSCTAGRSAFLTGQLPVRTGMH------SV 97
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGN----SEavTPNLDRLAAEGVRFENFFcTSPVCSPARASLLTGRMPSQHGIHdwivegSH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 98 GLPGGPVGLSADTPTLPEVLKTMGYVTGQFGKNHLGDrdeflptmhgfdeywgwlyhlnameytedpdwpkdgsldafap 177
Cdd:cd16149 77 GKTKKPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLGD------------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 178 rnviyarsdgkggqtieddgalsiermrtlddevnkHAINFIERAVEADKPFFtwycpsrghvwthLSPEYEAMLGQngW 257
Cdd:cd16149 114 ------------------------------------DAADFLRRRAEAEKPFF-------------LSVNYTAPHSP--W 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 258 GLQEVVmKDLDDHVGEMMAKMEELGIADNTIIIFTADNGpeiMTWPDGGMtpFHGEKGTT----WEGGVRAPALVSWPGK 333
Cdd:cd16149 143 GYFAAV-TGVDRNVGRLLDELEELGLTENTLVIFTSDNG---FNMGHHGI--WGKGNGTFplnmYDNSVKVPFIIRWPGV 216
|
330 340
....*....|....*....|....*..
gi 1376796650 334 IPAGTVGNGIFDGMDWLPTLVAAAGGP 360
Cdd:cd16149 217 VPAGRVVDSLVSAYDFFPTLLELAGVD 243
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-446 |
7.33e-36 |
|
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: 136.93 E-value: 7.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 25 EQPNIFVIFTDDIGISNLSAYHNGVMssETPNIDSIAEKGMLLTDYYAQPS-----CTAGRSAFLTGqlpvRTGMHSvgL 99
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEI--QTPNLDRLARRGTSFTNAYNMGGwsgavCVPSRAMLMTG----RTLFHA--P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 100 PGGPVGLSADTPTLPEVLKTMGYVTGQFGKNHLGdrdeflptmhgfdeywgwlyhlnameytedpdwpkdgsldaFAprn 179
Cdd:cd16155 73 EGGKAAIPSDDKTWPETFKKAGYRTFATGKWHNG-----------------------------------------FA--- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 180 viyarsdgkggqtieddgalsiermrtlDDevnkhAINFIERAVEADKPFFTWYCPSRGHVWTHLSPEYEAMLG------ 253
Cdd:cd16155 109 ----------------------------DA-----AIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPpetipl 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 254 ----------QNGWGL------------QEVVMKDL----------DDHVGEMMAKMEELGIADNTIIIFTADNGPEImt 301
Cdd:cd16155 156 penflpqhpfDNGEGTvrdeqlapfprtPEAVRQHLaeyyamithlDAQIGRILDALEASGELDNTIIVFTSDHGLAV-- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 302 wpdGGmtpfHG--EKGTTWEGGVRAPALVSWPGkIPAGTVGNGIFDGMDWLPTLVAAAGGPTDlkekmlkghdgfkAHLD 379
Cdd:cd16155 234 ---GS----HGlmGKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIP-------------ESVE 292
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376796650 380 GYNQVDMLTEKGESNRKEIYYYERDKLQAVRIGDWKAHFVVqnhgwsgpkEELNAPLLFNLRRDPYE 446
Cdd:cd16155 293 GKSLLPVIRGEKKAVRDTLYGAYRDGQRAIRDDRWKLIIYV---------PGVKRTQLFDLKKDPDE 350
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-361 |
1.05e-34 |
|
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: 131.13 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTD----DigisNLSAYHNGVMssETPNIDSIAEKGMLLTDYYAQ-PSCTAGRSAFLTGQLPVRTGMHSVGLPG 101
Cdd:cd16148 1 MNVILIVIDslraD----HLGCYGYDRV--TTPNLDRLAAEGVVFDNHYSGsNPTLPSRFSLFTGLYPFYHGVWGGPLEP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 102 GPvglsadtPTLPEVLKTMGYVTGQFGKN-HLGDRDEFLptmHGFDEYWGWLYHLNAMEYTEDPDwpkdgsldafaprnv 180
Cdd:cd16148 75 DD-------PTLAEILRKAGYYTAAVSSNpHLFGGPGFD---RGFDTFEDFRGQEGDPGEEGDER--------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 181 iyarsdgkggqtieddgalsiermrtlDDEVNKHAINFIERAvEADKPFFTWYcpsrgHVW-THLSPEYEAmlgqngwgl 259
Cdd:cd16148 130 ---------------------------AERVTDRALEWLDRN-ADDDPFFLFL-----HYFdPHEPYLYDA--------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 260 qEVVMkdLDDHVGEMMAKMEELGIADNTIIIFTADNGPEIMtwpDGGMTPFHGekGTTWEGGVRAPALVSWPGKIPAGTV 339
Cdd:cd16148 168 -EVRY--VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFG---EHGLYWGHG--SNLYDEQLHVPLIIRWPGKEPGKRV 239
|
330 340
....*....|....*....|..
gi 1376796650 340 gNGIFDGMDWLPTLVAAAGGPT 361
Cdd:cd16148 240 -DALVSHIDIAPTLLDLLGVEP 260
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
25-446 |
2.06e-32 |
|
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: 128.46 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 25 EQPNIFVIFTDDIgisN--LSAYHNGVMSseTPNIDSIAEKGMLLTDYYAQ-PSCTAGRSAFLTGQLPVRTGMHsvGLPG 101
Cdd:cd16030 1 KKPNVLFIAVDDL---RpwLGCYGGHPAK--TPNIDRLAARGVLFTNAYCQqPVCGPSRASLLTGRRPDTTGVY--DNNS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 102 GPVGLSADTPTLPEVLKTMGYVTGQFGKNHLGDRDEFLPTMHGFDEYWgwlyhlnameYTEDPDWPKDGSLDAFAPRNVI 181
Cdd:cd16030 74 YFRKVAPDAVTLPQYFKENGYTTAGVGKIFHPGIPDGDDDPASWDEPP----------NPPGPEKYPPGKLCPGKKGGKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 182 YARSDGKGGQTIEDDgalsiermRTLDDEVNKHAINFIERAVEADKPFF----------TWYCPSR-------------- 237
Cdd:cd16030 144 GGGGPAWEAADVPDE--------AYPDGKVADEAIEQLRKLKDSDKPFFlavgfykphlPFVAPKKyfdlyplesiplpn 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 238 --------GHVWTHLS--PEYEAMLGQNGWGLQEVVMKDL---------------DDHVGEMMAKMEELGIADNTIIIFT 292
Cdd:cd16030 216 pfdpidlpEVAWNDLDdlPKYGDIPALNPGDPKGPLPDEQarelrqayyasvsyvDAQVGRVLDALEELGLADNTIVVLW 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 293 ADNGpeimtwpdggmtpFH-GEKG-----TTWEGGVRAPALVSWPGKIPAGTVGNGIFDGMDWLPTLVAAAGGPTdlkek 366
Cdd:cd16030 296 SDHG-------------WHlGEHGhwgkhTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPA----- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 367 mlkghdgfKAHLDGYNQVDMLTEKGESNRKEIY-YYERDKLQ--AVRIGDWkaHFVVQNHGWSGPKEElnaplLFNLRRD 443
Cdd:cd16030 358 --------PPCLEGKSLVPLLKNPSAKWKDAAFsQYPRPSIMgySIRTERY--RYTEWVDFDKVGAEE-----LYDHKND 422
|
...
gi 1376796650 444 PYE 446
Cdd:cd16030 423 PNE 425
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-467 |
2.96e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 127.72 E-value: 2.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYHNGVMssETPNIDSIAEKGMLLTDYYA-QPSCTAGRSAFLTGQLPVRTGMHS-VGLPGGPV 104
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIV--KTPNIDRLAAEGVRFTNAYTpSPVCCPARASLLTGLYPHEHGVLNnVENAGAYS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 105 -GLSADTPTLPEVLKTMGYVTGQFGKNHLGDRDefLPTMHGFDEYwgwlyhlnameytedpdWPKDGSLDAFAprnviya 183
Cdd:cd16033 79 rGLPPGVETFSEDLREAGYRNGYVGKWHVGPEE--TPLDYGFDEY-----------------LPVETTIEYFL------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 184 rsdgkggqtieddgalsIERmrtlddevnkhAINFIERAVEADKPFFTW-------------------YCPSRGHVWT-- 242
Cdd:cd16033 133 -----------------ADR-----------AIEMLEELAADDKPFFLRvnfwgphdpyippepyldmYDPEDIPLPEsf 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 243 ----HLSPE----YEAMLGQngWGLQEVVMKD-----------LDDHVGEMMAKMEELGIADNTIIIFTADNGPeimtwp 303
Cdd:cd16033 185 addfEDKPYiyrrERKRWGV--DTEDEEDWKEiiahywgyitlIDDAIGRILDALEELGLADDTLVIFTSDHGD------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 304 dggMTPFHG--EKGT-TWEGGVRAPALVSWPGKIPAGTVGNGIFDGMDWLPTLVAAAGGPTDLKekmlkghdgfkahLDG 380
Cdd:cd16033 257 ---ALGAHRlwDKGPfMYEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK-------------VDG 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 381 YNQVDMLTEKGESN-RKEIY--------YYERdklQAVRIGDWKAhfvVQNHgwsgpkEELNAplLFNLRRDPYE---RA 448
Cdd:cd16033 321 RSLLPLLRGEQPEDwRDEVVteynghefYLPQ---RMVRTDRYKY---VFNG------FDIDE--LYDLESDPYElnnLI 386
|
490 500
....*....|....*....|
gi 1376796650 449 AE-ESGMYLKWMGQKMWAFG 467
Cdd:cd16033 387 DDpEYEEILREMRTRLYEWM 406
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
27-444 |
6.24e-31 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 122.30 E-value: 6.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYHNGVMssETPNIDSIAEKGMLLTDYYAQ-PSCTAGRSAFLTGQLPVRTGMHSVGLPggpvg 105
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVV--KTPNLDRLAARGVVFDNAYCNsPLCAPSRASMMTGRLPSRIGAYDNAAE----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 106 LSADTPTLPEVLKTMGYVTGQFGKNHLGDRDEflptMHGFDeywgwlyhlnameytedpdwpkdgsldafaprnviYars 185
Cdd:cd16032 74 FPADIPTFAHYLRAAGYRTALSGKMHFVGPDQ----LHGFD-----------------------------------Y--- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 186 dgkggqtieddgalsiermrtlDDEVNKHAINFI-ERAVEADK-PFFTWYCPSRGHVWTHLSPEY---------EAMLGQ 254
Cdd:cd16032 112 ----------------------DEEVAFKAVQKLyDLARGEDGrPFFLTVSFTHPHDPYVIPQEYwdlyvrrarRAYYGM 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 255 NGWglqevvmkdLDDHVGEMMAKMEELGIADNTIIIFTADNGpEIMtwpdggmtpfhGEKG-----TTWEGGVRAPALVS 329
Cdd:cd16032 170 VSY---------VDDKVGQLLDTLERTGLADDTIVIFTSDHG-DML-----------GERGlwykmSFFEGSARVPLIIS 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 330 WPGKIPAGTVGNGIfDGMDWLPTLVAAAGGptdlkekmlkGHDGFKAHLDGYNQVDMLTEKGESNRKEIY-YYERDKLQA 408
Cdd:cd16032 229 APGRFAPRRVAEPV-SLVDLLPTLVDLAGG----------GTAPHVPPLDGRSLLPLLEGGDSGGEDEVIsEYLAEGAVA 297
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1376796650 409 ----VRIGDWKahFVvqnhgWSgpkeELNAPLLFNLRRDP 444
Cdd:cd16032 298 pcvmIRRGRWK--FI-----YC----PGDPDQLFDLEADP 326
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-359 |
5.39e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 114.75 E-value: 5.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYHNGVMSSETPNIDSIAEKGMLLTDYYAQPSCTAGRSAFLTGQLPVRTGMHSVGLPggpvgL 106
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGVLAVPDE-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 107 SADTPTLPEVLK----TMGYVTGQFGKNHLGDRDEFLPTMHGFDEYWGwLYHLNAMEYTedpDWPKdgSLDAFAPRNVIY 182
Cdd:cd16154 76 LLSEETLLQLLIkdatTAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAG-ILGGGVQDYY---NWNL--TNNGQTTNSTEY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 183 ARSDgkggqtIEDDgalsiermrtlddevnkhAINFIEravEADKPFFTWYCPSRGHVWTHLSP---------EYEAMLG 253
Cdd:cd16154 150 ATTK------LTNL------------------AIDWID---QQTKPWFLWLAYNAPHTPFHLPPaelhsrsllGDSADIE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 254 QNGWGLQEVVMKDLDDHVGEMMAKM--EELgiaDNTIIIFTADNG---PEIMTWPDGGmtpfhGEKGTTWEGGVRAPALV 328
Cdd:cd16154 203 ANPRPYYLAAIEAMDTEIGRLLASIdeEER---ENTIIIFIGDNGtpgQVVDLPYTRN-----HAKGSLYEGGINVPLIV 274
|
330 340 350
....*....|....*....|....*....|.
gi 1376796650 329 SWPGKIPAGTVGNGIFDGMDWLPTLVAAAGG 359
Cdd:cd16154 275 SGAGVERANERESALVNATDLYATIAELAGV 305
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-445 |
5.48e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 113.79 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDigisnlsayHNGVMSS-------ETPNIDSIAEKGMLLTDYYAQ-PSCTAGRSAFLTGQLPVRTGMHSVG 98
Cdd:cd16037 1 PNILIIMSDE---------HNPDAMGcyghpvvRTPNLDRLAARGTRFENAYTPsPICVPSRASFLTGRYVHETGVWDNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 99 LPggpvgLSADTPTLPEVLKTMGYVTGQFGKNHLgdrdeflptmHGFDEYWGWLYhlnameytedpdwpkdgsldafapr 178
Cdd:cd16037 72 DP-----YDGDVPSWGHALRAAGYETVLIGKLHF----------RGEDQRHGFRY------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 179 nviyarsdgkggqtieddgalsiermrtlDDEVNKHAINFIERAVEADKPFFTW---YCPsrgHVWTHLSPEY------E 249
Cdd:cd16037 112 -----------------------------DRDVTEAAVDWLREEAADDKPWFLFvgfVAP---HFPLIAPQEFydlyvrR 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 250 AMLGQngWGLQEVvmkdLDDHVGEMMAKMEELGIADNTIIIFTADNGpEIMtwpdgGMtpfHG--EKGTTWEGGVRAPAL 327
Cdd:cd16037 160 ARAAY--YGLVEF----LDENIGRVLDALEELGLLDNTLIIYTSDHG-DML-----GE---RGlwGKSTMYEESVRVPMI 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 328 VSWPGkIPAGTVGNGIFDGMDWLPTLVAAAGGPtdlkekmlkghdgFKAHLDGYNQVDMLTEKGESNRkEIY--YYERDK 405
Cdd:cd16037 225 ISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAP-------------PPPDLDGRSLLPLAEGPDDPDR-VVFseYHAHGS 289
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1376796650 406 LQA---VRIGDWKAHFvvqNHGWsgpkeelnAPLLFNLRRDPY 445
Cdd:cd16037 290 PSGafmLRKGRWKYIY---YVGY--------PPQLFDLENDPE 321
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
26-446 |
2.09e-26 |
|
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: 110.72 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 26 QPNIFVIFTDDigisnLSAYHNGvMSSETPNIDSIAEKGMLLTDYYA-QPSCTAGRSAFLTGQLPVRTGMHSVGLPGG-- 102
Cdd:cd16147 1 RPNIVLILTDD-----QDVELGS-MDPMPKTKKLLADQGTTFTNAFVtTPLCCPSRASILTGQYAHNHGVTNNSPPGGgy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 103 PVGLSADTP--TLPEVLKTMGYVTGQFGK--NHLGDRDEFLPTMHGFDEyWGWLYHlNAMEYtedpdwpkdgsldafapR 178
Cdd:cd16147 75 PKFWQNGLErsTLPVWLQEAGYRTAYAGKylNGYGVPGGVSYVPPGWDE-WDGLVG-NSTYY-----------------N 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 179 NVIYARSDGKGGQTIEDDgalsiermrTLDDEVNKHAINFIERAVEADKPFF---TWYCPsrgHVWTHLSPEYE------ 249
Cdd:cd16147 136 YTLSNGGNGKHGVSYPGD---------YLTDVIANKALDFLRRAAADDKPFFlvvAPPAP---HGPFTPAPRYAnlfpnv 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 250 -----------AMLGQNGW-----GLQEVVMKDL--------------DDHVGEMMAKMEELGIADNTIIIFTADNGpei 299
Cdd:cd16147 204 tapprpppnnpDVSDKPHWlrrlpPLNPTQIAYIdelyrkrlrtlqsvDDLVERLVNTLEATGQLDNTYIIYTSDNG--- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 300 mtwpdggmtpFH-GE------KGTTWEGGVRAPALVSWPGkIPAGTVGNGIFDGMDWLPTLVAAAGGPTDlkekmlKGHD 372
Cdd:cd16147 281 ----------YHlGQhrlppgKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPP------SDMD 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376796650 373 GfKAHLDGYNqvdmltekgesNRkeiYyyerdklQAVRIGDWKAHFVVQNHGwSGPKEelnaplLFNLRRDPYE 446
Cdd:cd16147 344 G-RSCGDSNN-----------NT---Y-------KCVRTVDDTYNLLYFEWC-TGFRE------LYDLTTDPYQ 388
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
26-385 |
2.36e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 108.23 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 26 QPNIFVIFTDDIGISNLSAY---HNGVMSS-----ETPNIDSIAEKGMLLTDYYAQ-PSCTAGRSAFLTGQLPVRTGMHS 96
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYnnaHTGKSESrlgyvESPNIDALAAEGVLFTNAYCNsPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 97 VG--LPGGPVGLsadtPTLPEVLKTMGYVTGQFGKNHLgdrDEFLptmhgfdeywgwlyhlnamEYTEDPDWPkdgslda 174
Cdd:cd16153 81 FEaaHPALDHGL----PTFPEVLKKAGYQTASFGKSHL---EAFQ-------------------RYLKNANQS------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 175 faprnviYARSDGKggqtieddgalsiermrtlddevnkhainfIERAVEADKPFFTwycpSRGHVWTH---LSPE---- 247
Cdd:cd16153 128 -------YKSFWGK------------------------------IAKGADSDKPFFV----RLSFLQPHtpvLPPKefrd 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 248 ---YEAMLgqnGWGlqevvmkdlDDHVGEMMAKMEELGIA---DNTIIIFTADNGpeimtWPDGGmtpfHG--EKGTTWE 319
Cdd:cd16153 167 rfdYYAFC---AYG---------DAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHG-----WHLGE----QGilAKFTFWP 225
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376796650 320 GGVRAPALVSWPGKI--PAGTVGNGIFDGMDWLPTLVAAAGGPTDlkekmlkGHDgfkaHLDGYNQVD 385
Cdd:cd16153 226 QSHRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTLLAAAGVDVD-------APD----YLDGRDLFE 282
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
26-447 |
2.18e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 104.62 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 26 QPNIFVIFTDDIGISNLSAYhnGVMSSETPNIDSIAEKGMLLTD-YYAQPSCTAGRSAFLTGQLPVRTGMHSVGLPggpv 104
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCY--GQPLDLTPNLDALAEEGVLFENaFTPQPVCGPARACLQTGLYPTETGCFRNGIP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 105 gLSADTPTLPEVLKTMGYVTGQFGKNHLGdrdeflptmhgfdeywgwlyhlnameytedpdwpkdgsldafaprnviyar 184
Cdd:cd16152 75 -LPADEKTLAHYFRDAGYETGYVGKWHLA--------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 185 sdgkggqtieddgalsieRMRTldDEVNKHAINFIeRAVEADKPFFTwycpsrghVWTHLSP-------EYEAMLG---- 253
Cdd:cd16152 103 ------------------GYRV--DALTDFAIDYL-DNRQKDKPFFL--------FLSYLEPhhqndrdRYVAPEGsaer 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 254 -QNGWglqevVMKDL---------------------DDHVGEMMAKMEELGIADNTIIIFTADNGPEIMTWPdggmtpfh 311
Cdd:cd16152 154 fANFW-----VPPDLaalpgdwaeelpdylgccerlDENVGRIRDALKELGLYDNTIIVFTSDHGCHFRTRN-------- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 312 GE-KGTTWEGGVRAPALVSWPGkIPAGTVGNGIFDGMDWLPTLVAAAGGPTDlkEKMlkghdgfkahlDGYNQVDMLTEK 390
Cdd:cd16152 221 AEyKRSCHESSIRVPLVIYGPG-FNGGGRVEELVSLIDLPPTLLDAAGIDVP--EEM-----------QGRSLLPLVDGK 286
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 391 GESNRKEIYyyerdkLQ--------AVRIGDWKahFVVQNHGwSGPKEELNAP-----LLFNLRRDPYER 447
Cdd:cd16152 287 VEDWRNEVF------IQisesqvgrAIRTDRWK--YSVAAPD-KDGWKDSGSDvyvedYLYDLEADPYEL 347
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
54-446 |
9.18e-24 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 103.49 E-value: 9.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 54 TPNIDSIAEKGMLLTDYYAQ-PSCTAGRSAFLTGQLPVRTGMHSVGLPggpvgLSADTPTLPEVLKTMGYVTGQFGKNHL 132
Cdd:cd16028 26 TPNLDRLAAEGVRFRNHYTQaAPCGPSRASLYTGRYLMNHRSVWNGTP-----LDARHLTLALELRKAGYDPALFGYTDT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 133 --------------------------GDRDEFLP------------TMHGFDEYWG--WLYHLNameYTEdPDWPkdgsL 172
Cdd:cd16028 101 spdprglapldprllsyelampgfdpVDRLDEYPaedsdtafltdrAIEYLDERQDepWFLHLS---YIR-PHPP----F 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 173 DAFAPRNVIYARSDGkggqtieddgaLSIERMRTLDDEVNKHAI--NFIERavEADKPFFTWYCPS---RGHVWTHLSPE 247
Cdd:cd16028 173 VAPAPYHALYDPADV-----------PPPIRAESLAAEAAQHPLlaAFLER--IESLSFSPGAANAadlDDEEVAQMRAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 248 YeamlgqngWGLqevvMKDLDDHVGEMMAKMEELGIADNTIIIFTADNGPeimTWPDGGMtpfhGEKGTTWEGGVRAPAL 327
Cdd:cd16028 240 Y--------LGL----IAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGE---QLGDHWL----WGKDGFFDQAYRVPLI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 328 VSWPGKiPAGTVGNGIFDGM----DWLPTLVAAAGGPTDlkekmlkghdgfkAHLDGYNQVDMLT-EKGESNRKEIYYYE 402
Cdd:cd16028 301 VRDPRR-EADATRGQVVDAFtesvDVMPTILDWLGGEIP-------------HQCDGRSLLPLLAgAQPSDWRDAVHYEY 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376796650 403 RDK-------------------LQAVRIGDWK-AHFvvqnhgwsgpkEELnAPLLFNLRRDPYE 446
Cdd:cd16028 367 DFRdvstrrpqealglspdecsLAVIRDERWKyVHF-----------AAL-PPLLFDLKNDPGE 418
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
23-447 |
1.29e-23 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 103.60 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 23 AQEQPNIFVIFTDDIGISNLSAyhNGVMSSETPNIDSIAEKGMLLTD-YYAQPSCTAGRSAFLTGQLPVRTGMhsVGLpg 101
Cdd:PRK13759 3 QTKKPNIILIMVDQMRGDCLGC--NGNKAVETPNLDMLASEGYNFENaYSAVPSCTPARAALLTGLSQWHHGR--VGY-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 102 GPVGLSADTPTLPEVLKTMGYVTGQFGKNHlgdrdeFLP--TMHGFDeywGWLYHlnamEYTEDPDWPKDGSLDAFAPRN 179
Cdd:PRK13759 77 GDVVPWNYKNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFH---NVLLH----DGYLHSGRNEDKSQFDFVSDY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 180 VIYARSDGKG------GQTIEDDGALSiermRTLDDEVNKH--------AINFIERAvEADKPFFTWYCPSRGHV----- 240
Cdd:PRK13759 144 LAWLREKAPGkdpdltDIGWDCNSWVA----RPWDLEERLHptnwvgseSIEFLRRR-DPTKPFFLKMSFARPHSpydpp 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 241 -------------------WTHLSPE------YEAMLGQNGwglQEVV----------MKDLDDHVGEMMAKMEELGIAD 285
Cdd:PRK13759 219 kryfdmykdadipdphigdWEYAEDQdpeggsIDALRGNLG---EEYArraraayyglITHIDHQIGRFLQALKEFGLLD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 286 NTIIIFTADNGpEIMTwpdggmTPFHGEKGTTWEGGVRAPALVSWPGKIPAGTVGnGIFDGM----DWLPTLVAAAGG-- 359
Cdd:PRK13759 296 NTIILFVSDHG-DMLG------DHYLFRKGYPYEGSAHIPFIIYDPGGLLAGNRG-TVIDQVvelrDIMPTLLDLAGGti 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 360 PTDlkekmlkghdgfkahLDGYNQVDMLTEKGESNRKEI---YYYERDKLQAVRIGDWKAHFvvqnhgWSGPKEElnapL 436
Cdd:PRK13759 368 PDD---------------VDGRSLKNLIFGQYEGWRPYLhgeHALGYSSDNYLTDGKWKYIW------FSQTGEE----Q 422
|
490
....*....|.
gi 1376796650 437 LFNLRRDPYER 447
Cdd:PRK13759 423 LFDLKKDPHEL 433
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
27-353 |
3.50e-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: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYHNGVmsSETPNIDSIAEKGMLL--TDYYAQPSCTAGRSAFLTGQLPVRTG-----MHSVGL 99
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPA--PTTPNLKRLASEGATFnfRSVSPPTSSAPNHAALLTGAYPTLHGytgngSADPEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 100 PGGPVGLSADTPTLPEVLKTMGYVTGQFG-KNHLgdrDEFLPTMHGFdeywgwlYHLNameyTEDPDWPkdgsldafapr 178
Cdd:cd00016 79 PSRAAGKDEDGPTIPELLKQAGYRTGVIGlLKAI---DETSKEKPFV-------LFLH----FDGPDGP----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 179 nviyarsdgkggqtieddgalsiermrtlddevnkhainfieraveadkpfftwycpsrGHVWTHLSPEYEAMLgqngwg 258
Cdd:cd00016 134 -----------------------------------------------------------GHAYGPNTPEYYDAV------ 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 259 lqevvmKDLDDHVGEMMAKMEELGIADNTIIIFTADNGpeiMTWPDGGMTPFHGEKGTTWEGGVRAPALVSWPGkIPAGT 338
Cdd:cd00016 149 ------EEIDERIGKVLDALKKAGDADDTVIIVTADHG---GIDKGHGGDPKADGKADKSHTGMRVPFIAYGPG-VKKGG 218
|
330
....*....|....*
gi 1376796650 339 VGNGIFDGMDWLPTL 353
Cdd:cd00016 219 VKHELISQYDIAPTL 233
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
27-446 |
8.09e-20 |
|
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: 92.06 E-value: 8.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYHNGVMSseTPNIDSIAEKGMLLTDYYA-QPSCTAGRSAFLTGQLPvrtgmHSVGLPGGPVG 105
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMK--TPNLDRLAAEGVRFDSAYTtQPVCGPARSGLFTGLYP-----HTNGSWTNCMA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 106 LSADTPTLPEVLKTMGYVTGQFGKNHLGDRDEF----LPTmhgfdeywGWlyhlnameyteDPDWPKDGS--LDAFaPRN 179
Cdd:cd16156 74 LGDNVKTIGQRLSDNGIHTAYIGKWHLDGGDYFgngiCPQ--------GW-----------DPDYWYDMRnyLDEL-TEE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 180 VIYARSDGKggQTIEDDGalsIERMRTLDDEVNKHAINFIERavEADKPFF-----------------------TWYCPS 236
Cdd:cd16156 134 ERRKSRRGL--TSLEAEG---IKEEFTYGHRCTNRALDFIEK--HKDEDFFlvvsydephhpflcpkpyasmykDFEFPK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 237 RGHVWTHLS--PEY-----EAMLGQNGwGLQEVVMKDL-------DDHVGEMMAKMEElgIADNTIIIFTADNGpEIMtw 302
Cdd:cd16156 207 GENAYDDLEnkPLHqrlwaGAKPHEDG-DKGTIKHPLYfgcnsfvDYEIGRVLDAADE--IAEDAWVIYTSDHG-DML-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 303 pdgGMTPFHGEKGTTWEGGVRAPALVSWPGKIPAGTVGNGIFDGMDWLPTLVAAAGGPtdlKEKMLKGHDGFKAHLDGYN 382
Cdd:cd16156 281 ---GAHKLWAKGPAVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIP---QPKVLEGESILATIEDPEI 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 383 QVD---MLtekgESNRKEIYYYERDKLQAVRI---GDWKahfVVQNHgwsgpkeeLNAPLLFNLRRDPYE 446
Cdd:cd16156 355 PENrgvFV----EFGRYEVDHDGFGGFQPVRCvvdGRYK---LVINL--------LSTDELYDLEKDPYE 409
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-362 |
1.15e-16 |
|
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: 81.90 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGISNLSAYHNGVmsSETPNIDSIAEKGMLLTDYYAQ-PSCTAGRSAFLTGQLPVRTG---MHSVglpgg 102
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPA--AVTPNLDALAAEGVRFSNAYCQnPVCSPSRCSFLTGWYPHVNGhrtLHHL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 103 pvgLSADTPTLPEVLKTMGYVTGQFGKNHLgdrdefLPTMHGFDEYwgwlyhlnameytEDPDWpkdgsldafaprnviy 182
Cdd:cd16150 74 ---LRPDEPNLLKTLKDAGYHVAWAGKNDD------LPGEFAAEAY-------------CDSDE---------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 183 arsdgkggqtieddgalsiermrtlddEVNKHAINFIERAvEADKPFFTwYCPSRG-HV-------W------------- 241
Cdd:cd16150 116 ---------------------------ACVRTAIDWLRNR-RPDKPFCL-YLPLIFpHPpygveepWfsmidreklpprr 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 242 --THLSPEYEAML------GQNGWG---LQEV-------VMKdLDDHVGEMMAKMEELGIADNTIIIFTADNgpeimtwp 303
Cdd:cd16150 167 ppGLRAKGKPSMLegiekqGLDRWSeerWRELratylgmVSR-LDHQFGRLLEALKETGLYDDTAVFFFSDH-------- 237
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376796650 304 dGGMTPFHG--EKgttWEGG-----VRAPALVSwPGKIPAGTVGNGIFDGMDWLPTLVAAAGGPTD 362
Cdd:cd16150 238 -GDYTGDYGlvEK---WPNTfedclTRVPLIIK-PPGGPAGGVSDALVELVDIPPTLLDLAGIPLS 298
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-372 |
3.48e-15 |
|
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: 76.09 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIgiSNLSAYHNGVMSSETPNIDSIAEKGMLLTDYY-AQPSCTAGRSAFLTGQLPVRTGMHSVGLPGGPVG 105
Cdd:cd16035 1 PNILLILTDQE--RYPPPWPAGWAALNLPARERLAANGLSFENHYtAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 106 LSADTPTLPEVLKTMGYVTGQFGKNHLGDrdeflptmHGfdeyWGwlyhlnamEYTEDPdwpkdgsldAFAPRNVIYARS 185
Cdd:cd16035 79 LSPDVPTLGHMLRAAGYYTAYKGKWHLSG--------AA----GG--------GYKRDP---------GIAAQAVEWLRE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 186 DGKGGqtiEDDG----ALSIermrtlddeVNKHAINFIERAVEADKPFFTWY--Cpsrghvwthlspeyeamlgqngwgl 259
Cdd:cd16035 130 RGAKN---ADGKpwflVVSL---------VNPHDIMFPPDDEERWRRFRNFYynL------------------------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 260 qevvMKDLDDHVGEMMAKMEELGIADNTIIIFTADNGpeimtwpDGGMTpfHG--EKG-TTWEGGVRAPALVSWPGKIPA 336
Cdd:cd16035 173 ----IRDVDRQIGRVLDALDASGLADNTIVVFTSDHG-------EMGGA--HGlrGKGfNAYEEALHVPLIISHPDLFGT 239
|
330 340 350
....*....|....*....|....*....|....*....
gi 1376796650 337 GTVGNGIFDGMDWLPTLVAAAGGPTDLKEKM---LKGHD 372
Cdd:cd16035 240 GQTTDALTSHIDLLPTLLGLAGVDAEARATEappLPGRD 278
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
25-410 |
2.10e-14 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 75.46 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 25 EQPNIFVI----FTDDIgiSNLSAYHNGVmsseTPNIDSIAEKGMLLTDYYAQpsctAGRS-----AFLTGQLPvrtgmh 95
Cdd:COG1368 233 KKPNVVVIllesFSDFF--IGALGNGKDV----TPFLDSLAKESLYFGNFYSQ----GGRTsrgefAVLTGLPP------ 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 96 svgLPGGPV---GLSADTPTLPEVLKTMGYVTgQF---GKNHLGDRDEFLPTMhGFDEYwgwlYHLNAMEYTEDPDWP-K 168
Cdd:COG1368 297 ---LPGGSPykrPGQNNFPSLPSILKKQGYET-SFfhgGDGSFWNRDSFYKNL-GFDEF----YDREDFDDPFDGGWGvS 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 169 DGSLdafaprnviYARSdgkggqtieddgalsiermrtlddevnkhainfIERAVEADKPFFTwycpsrgHVWThLS--- 245
Cdd:COG1368 368 DEDL---------FDKA---------------------------------LEELEKLKKPFFA-------FLIT-LSnhg 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 246 ----PEYEAMLGQNGWGLQEVV---MKDLDDHVGEMMAKMEELGIADNTIIIFTADNGPeimtwPDGGMTPFHgekgtTW 318
Cdd:COG1368 398 pytlPEEDKKIPDYGKTTLNNYlnaVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGP-----RSPGKTDYE-----NP 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 319 EGGVRAPALVsWPGKIPAGTVGNGIFDGMDWLPTLVAAAGGPTDlKEKMLkGHDGFKAHLDGY--NQVDMLTEKGesnrk 396
Cdd:COG1368 468 LERYRVPLLI-YSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYP-SYYAF-GRDLLSPDTDPFafRNGGFITDDY----- 539
|
410
....*....|....
gi 1376796650 397 eIYYYERDKLQAVR 410
Cdd:COG1368 540 -VYVLKTGELTEED 552
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
27-358 |
7.65e-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: 71.95 E-value: 7.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVI----FTDDigisnlsaYHNGVMSSE--TPNIDSIAEKGMLLTDYYAQpsCTAGRS-----AFLTGQLPVRTGMH 95
Cdd:cd16015 1 PNVIVIllesFSDP--------YIDKDVGGEdlTPNLNKLAKEGLYFGNFYSP--GFGGGTangefEVLTGLPPLPLGSG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 96 SVGLPGGPvglsaDTPTLPEVLKTMGYVTgQF---GKNHLGDRDEFLPtMHGFDEYWGwLYHLNAMEYTEDPDWPKDGSL 172
Cdd:cd16015 71 SYTLYKLN-----PLPSLPSILKEQGYET-IFihgGDASFYNRDSVYP-NLGFDEFYD-LEDFPDDEKETNGWGVSDESL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 173 dafaprnviYARsdgkggqtieddgalSIERMRTLDdevnkhainfieraveaDKPFFTwycpsrgHVWT---H----LS 245
Cdd:cd16015 143 ---------FDQ---------------ALEELEELK-----------------KKPFFI-------FLVTmsnHgpydLP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 246 PEYEAMLGQNGWGLQEV-----VMKDLDDHVGEMMAKMEELGIADNTIIIFTADNGPeimtwpdgGMTPFHGEKGTTWEG 320
Cdd:cd16015 175 EEKKDEPLKVEEDKTELenylnAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLP--------SLGSDYDETDEDPLD 246
|
330 340 350
....*....|....*....|....*....|....*...
gi 1376796650 321 GVRAPALVSWPGKIPAGTVgNGIFDGMDWLPTLVAAAG 358
Cdd:cd16015 247 LYRTPLLIYSPGLKKPKKI-DRVGSQIDIAPTLLDLLG 283
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
393-447 |
1.72e-13 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 66.95 E-value: 1.72e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376796650 393 SNRKEIYYYERDKLQAVRIGDWKAHFVVQN---------HGWSGPKEELNAPLLFNLRRDPYER 447
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGPYKAHFFTPSfdppgaegcYGSKVPVTHHDPPLLFDLERDPSEK 64
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
1-296 |
1.02e-09 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 60.15 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 1 MKRIFHLVTLSVLSSFslsAWSAQEQPNIFVIFTDDIGISNLSAYHngvmsseTPNIDSIAEKGMLLTDYYAQ-PSCTA- 78
Cdd:COG1524 1 MKRGLSLLLASLLAAA---AAAAPPAKKVVLILVDGLRADLLERAH-------APNLAALAARGVYARPLTSVfPSTTAp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 79 GRSAFLTGQLPVRTGMhsvglpggpVGLSADTPTLPEVLKTMGYVTGQFGKNHLGDRdeflPTM------HGFD-EYWGW 151
Cdd:COG1524 71 AHTTLLTGLYPGEHGI---------VGNGWYDPELGRVVNSLSWVEDGFGSNSLLPV----PTIferaraAGLTtAAVFW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 152 LYHLNAMEYTEDPDWPKDGSLDAFAprnviYARSDgkggqtieddgalsiermrtlddevnKHAINFIERAVEADKPFFT 231
Cdd:COG1524 138 PSFEGSGLIDAARPYPYDGRKPLLG-----NPAAD--------------------------RWIAAAALELLREGRPDLL 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1376796650 232 W-YCP---SRGHVWTHLSPEYEAMLgqngwglqevvmKDLDDHVGEMMAKMEELGIADNTIIIFTADNG 296
Cdd:COG1524 187 LvYLPdldYAGHRYGPDSPEYRAAL------------REVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
216-353 |
3.92e-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: 55.68 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 216 INFIERAvEADKPFFTW--------YCPSRGHVWTHLSPEYEAMLGQNGWGLQEVVM-------KDLDDHVGEMMAKMEE 280
Cdd:COG3083 371 LQWLDQR-DSDRPWFSYlfldaphaYSFPADYPKPFQPSEDCNYLALDNESDPTPFKnryrnavHYVDSQIGRVLDTLEQ 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376796650 281 LGIADNTIIIFTADNGPEIMtwPDGGMTPFHGEKGTTWEggVRAPALVSWPGKiPAGTVgNGIFDGMDWLPTL 353
Cdd:COG3083 450 RGLLENTIVIITADHGEEFN--ENGQNYWGHNSNFSRYQ--LQVPLVIHWPGT-PPQVI-SKLTSHLDIVPTL 516
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
27-444 |
1.92e-06 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 49.85 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 27 PNIFVIFTDDIGiSNLSAY-HNGVMSseTPNIDSIAEKGML-LTDYYAQPSCTAGRSAFLTGQLPvrtgmHSVGLPGGPV 104
Cdd:cd16171 1 PNVVMVMSDSFD-GRLTFRpGNQVVD--LPYINFMKQHGSVfLNAYTNSPICCPSRAAMWSGLFT-----HLTESWNNYK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 105 GLSADTPTLPEVLKTMGYVTGQFGKnhlgdrdeflptmhgfdeywgwlyhlnaMEYTEDpDWPKDGSLDAFApRNVIYA- 183
Cdd:cd16171 73 GLDPNYPTWMDRLEKHGYHTQKYGK----------------------------LDYTSG-HHSVSNRVEAWT-RDVPFLl 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 184 RSDGKggQTIEDDGALSIERMRTLDDEVNKHAINFIER-AVEADKPFFTWYCPSRGHvwthlsPEYEAMLGQNGWGLQEV 262
Cdd:cd16171 123 RQEGR--PTVNLVGDRSTVRVMLKDWQNTDKAVHWIRKeAPNLTQPFALYLGLNLPH------PYPSPSMGENFGSIRNI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 263 ------VMKDLDDHVGEMMAKMEELGIADNTIIIFTADNGpeimtwpDGGMTPFHGEKGTTWEGGVRAPALVSWPGkIPA 336
Cdd:cd16171 195 rafyyaMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHG-------ELAMEHRQFYKMSMYEGSSHVPLLIMGPG-IKA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 337 GTVGNGIFDGMDWLPTLVAAAGGPTdlkekmlkghdgfKAHLDGYNQVDMLTEKGESNRKEIYYYERDKLQA-------- 408
Cdd:cd16171 267 GQQVSDVVSLVDIYPTMLDIAGVPQ-------------PQNLSGYSLLPLLSESSIKESPSRVPHPDWVLSEfhgcnvna 333
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1376796650 409 ----VRIGDWKahFVVQNHGWSGPkeelnaPLLFNLRRDP 444
Cdd:cd16171 334 stymLRTNSWK--YIAYADGNSVP------PQLFDLSKDP 365
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
207-296 |
8.85e-04 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 41.03 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 207 LDDEVNKHAINFIERAVEADKPFF-TWYCP---SRGHVWTHLSPEYEAMLgqngwglqevvmKDLDDHVGEMMAKMEELG 282
Cdd:cd16018 136 NDSFPFEERVDTILEWLDLERPDLiLLYFEepdSAGHKYGPDSPEVNEAL------------KRVDRRLGYLIEALKERG 203
|
90
....*....|....
gi 1376796650 283 IADNTIIIFTADNG 296
Cdd:cd16018 204 LLDDTNIIVVSDHG 217
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
217-296 |
9.33e-03 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 38.48 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376796650 217 NFIERAVeaDKPFFTWYCpsrghvWTHLSPEYEAMLGQngwglqevvmkdLDDHVGEMMAKMEELGIADNTIIIFTADNG 296
Cdd:pfam02995 283 QFLPRYR--DSPFFGFFW------SNSLSHDDFNYASA------------LDEDFLKYLKKLHKRGLLDNTIVIFMSDHG 342
|
|
| |
