|
Name |
Accession |
Description |
Interval |
E-value |
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
45-488 |
0e+00 |
|
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: 631.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSCVP 123
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDqIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEPYGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 124 LDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHERCTLIDALNVtrcalDFRDGEEVA 203
Cdd:cd16029 81 LNETLLPQYLKELGYATHLVGKWHLGFYTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGGANDYGND-----DLRDNEEPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 204 TGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPY----DFIQDKNRHHYAGMVSLMDEAVGN 279
Cdd:cd16029 156 WDYNGTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPYedkfAHIKDEDRRTYAAMVSALDESVGN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 280 VTAALKSSGLWNNTVFIFSTDNGGQTLAG--GNNWPLRGRKWSLWEGGVRGVGFVASPLLK-QKGVKNRELIHISDWLPT 356
Cdd:cd16029 236 VVDALKAKGMLDNTLIVFTSDNGGPTGGGdgGSNYPLRGGKNTLWEGGVRVPAFVWSPLLPpKRGTVSDGLMHVTDWLPT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 357 LVKLARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNIDPNfvdsspcprnsmapakddsslpeysaFNTSVHAAIRHG 436
Cdd:cd16029 316 LLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILLNIDDI--------------------------TRTTGGAAIRVG 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 38569405 437 NWKLLTGYPgcgywfpppsqynvseipssdpptktlwLFDIDRDPEERHDLS 488
Cdd:cd16029 370 DWKLIVGKP----------------------------LFNIENDPCERNDLA 393
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
44-488 |
4.35e-98 |
|
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: 302.56 E-value: 4.35e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 44 PPHLVFLLADDLGWNDVGFHGS-RIRTPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSC 121
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSpLIKTPNIDRLAAEGVRFTDFYaAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 122 VPLDEKLLPQLLKEAGYTTHMVGKWHLGMyRKECLPTRRGFDTYFGYLlgsedyYSHERCTLIDALNVTRCALDFRDGEE 201
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGH-QPEFLPTRHGFDEYFGIP------YSNDMWPFPLYRNDPPGPLPPLMENE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 202 VATGYKNMYS--TNIFTKRAIALITNHPpEKPLFLYLALQSVHEPLQVPEEYLKPydfiqdKNRHHYAGMVSLMDEAVGN 279
Cdd:cd16026 154 EVIEQPADQSslTQRYTDEAVDFIERNK-DQPFFLYLAHTMPHVPLFASEKFKGR------SGAGLYGDVVEELDWSVGR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 280 VTAALKSSGLWNNTVFIFSTDNG---GQTLAGGNNWPLRGRKWSLWEGGVRgVGFVAS-PLLKQKGVKNRELIHISDWLP 355
Cdd:cd16026 227 ILDALKELGLEENTLVIFTSDNGpwlEYGGHGGSAGPLRGGKGTTWEGGVR-VPFIAWwPGVIPAGTVSDELASTMDLLP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 356 TLVKLARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNidpnfvdsspcprnsmapakddsslpeysaFNTSVHAAIRH 435
Cdd:cd16026 306 TLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYY------------------------------YDGGDLQAVRS 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 38569405 436 GNWKLLtgypgcgywFPPPSQYNVSEIPSSDPPTKTLWLFDIDRDPEERHDLS 488
Cdd:cd16026 356 GRWKLH---------LPTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGETYNVA 399
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
35-507 |
4.59e-97 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 299.49 E-value: 4.59e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 35 PGSGAGASRPPHLVFLLADDLGWNDVGFHGS-RIRTPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQHq 112
Cdd:COG3119 14 AAAAAAAAKRPNILFILADDLGYGDLGCYGNpLIKTPNIDRLAAEGVRFTNAYvTSPVCSPSRASLLTGRYPHRTGVTD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 113 iIWPCQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLgmyrkeclptrrgfdtyfgyllgsedyysherctlidalnvtrc 192
Cdd:COG3119 93 -NGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL-------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 193 aldfrdgeevatgyknmYSTNIFTKRAIALITNH-PPEKPLFLYLALQSVHEPLQVPEEYLKPYD--------------- 256
Cdd:COG3119 128 -----------------YLTDLLTDKAIDFLERQaDKDKPFFLYLAFNAPHAPYQAPEEYLDKYDgkdiplppnlaprdl 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 257 --FIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQtlagGNNWPLRGRKWSLWEGGVRgVGFVAS 334
Cdd:COG3119 191 teEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS----LGEHGLRGGKGTLYEGGIR-VPLIVR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 335 -PLLKQKGVKNRELIHISDWLPTLVKLArghtnGTKP---LDGFDVWKTISEGSPSPRiellhniDPNFVdsspcprnsm 410
Cdd:COG3119 266 wPGKIKAGSVSDALVSLIDLLPTLLDLA-----GVPIpedLDGRSLLPLLTGEKAEWR-------DYLYW---------- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 411 apakddsslpEYSAFNTsvHAAIRHGNWKLLTGYPGCGYWfpppsqynvseipssdpptktlWLFDIDRDPEERHDLSRE 490
Cdd:COG3119 324 ----------EYPRGGG--NRAIRTGRWKLIRYYDDDGPW----------------------ELYDLKNDPGETNNLAAD 369
|
490
....*....|....*..
gi 38569405 491 YPHIVTKLLSRLQFYHK 507
Cdd:COG3119 370 YPEVVAELRALLEAWLK 386
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
45-507 |
1.44e-96 |
|
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: 299.08 E-value: 1.44e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIiwpCQPSCVP 123
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPiLKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTGVWHTI---LGRERMR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 124 LDEKLLPQLLKEAGYTTHMVGKWHLGM---YRkeclPTRRGFDTYFGYLLGS-EDYYSHErctlidaLNVTRCALDFRDG 199
Cdd:cd16146 78 LDETTLAEVFKDAGYRTGIFGKWHLGDnypYR----PQDRGFDEVLGHGGGGiGQYPDYW-------GNDYFDDTYYHNG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 200 EEVATgykNMYSTNIFTKRAIALITNHpPEKPLFLYLALQSVHEPLQVPEEYLKPY-DFIQDKNRHHYAGMVSLMDEAVG 278
Cdd:cd16146 147 KFVKT---EGYCTDVFFDEAIDFIEEN-KDKPFFAYLATNAPHGPLQVPDKYLDPYkDMGLDDKLAAFYGMIENIDDNVG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 279 NVTAALKSSGLWNNTVFIFSTDNGGQTL-AGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTL 357
Cdd:cd16146 223 RLLAKLKELGLEENTIVIFMSDNGPAGGvPKRFNAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 358 VKLARGHTNGTKPLDGFDVWKTISEGSPSPRIELLhnidpnFVDSSPCPRNsmapakddsslPEYSAfntsvHAAIRHGN 437
Cdd:cd16146 303 LDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTL------FTHSGRWPPP-----------PKKKR-----NAAVRTGR 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 438 WKLLtgypgcgywfpppsqynvseipssDPPTKTLWLFDIDRDPEERHDLSREYPHIVTKLLSRLQFYHK 507
Cdd:cd16146 361 WRLV------------------------SPKGFQPELYDIENDPGEENDVADEHPEVVKRLKAAYEAWWD 406
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
45-503 |
2.63e-93 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 290.98 E-value: 2.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYQIRTGL-QHQIIWPCQPSC 121
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKfYETPNIDRLAKEGMRFTQAYAaAPVCSPSRASILTGQYPARLGItDVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 122 -----------VPLDEKLLPQLLKEAGYTTHMVGKWHLGMyRKECLPTRRGFDTYFGY-LLGSEDYYSHERCTLIDALNv 189
Cdd:cd16144 81 tklipppsttrLPLEEVTIAEALKDAGYATAHFGKWHLGG-EGGYGPEDQGFDVNIGGtGNGGPPSYYFPPGKPNPDLE- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 190 trcalDFRDGEevatgyknmYSTNIFTKRAIALITNHPpEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNRH----- 264
Cdd:cd16144 159 -----DGPEGE---------YLTDRLTDEAIDFIEQNK-DKPFFLYLSHYAVHTPIQARPELIEKYEKKKKGLRKgqknp 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 265 HYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLAGGN---NWPLRGRKWSLWEGGVRgVGFVAS-PLLKQK 340
Cdd:cd16144 224 VYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPptsNAPLRGGKGSLYEGGIR-VPLIVRwPGVIKP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 341 GVKNRELIHISDWLPTLVKLARGHTNGTKPLDGFDVWKTIS-EGSPSPRIELLHNidpnfvdsspcprnsmapakddssL 419
Cdd:cd16144 303 GSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKgGEADLPRRALFWH------------------------F 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 420 PEYSAFNTSVHAAIRHGNWKLLtgypgcgYWFpppsqynvsEipssdppTKTLWLFDIDRDPEERHDLSREYPHIVTKLL 499
Cdd:cd16144 359 PHYHGQGGRPASAIRKGDWKLI-------EFY---------E-------DGRVELYNLKNDIGETNNLAAEMPEKAAELK 415
|
....
gi 38569405 500 SRLQ 503
Cdd:cd16144 416 KKLD 419
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
44-487 |
8.24e-78 |
|
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: 250.05 E-value: 8.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 44 PPHLVFLLADDLGWNDVGFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQH----QIIWPCQP 119
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGEIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTmaelATGKPGYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 120 SCVPLDEKLLPQLLKEAGYTTHMVGKWHLGMyrkeclptrrgfdtyfgyllgsEDYysherctlidalnvtrcaldfrdg 199
Cdd:cd16025 82 GYLPDSAATIAEVLKDAGYHTYMSGKWHLGP----------------------DDY------------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 200 eevatgyknmYSTNIFTKRAIALI-TNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDK----------------- 261
Cdd:cd16025 116 ----------YSTDDLTDKAIEYIdEQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKGKYDAgwdalreerlerqkelg 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 262 ---------NRHH----------------------YAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGqtlAGGN 310
Cdd:cd16025 186 lipadtkltPRPPgvpawdslspeekklearrmevYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGA---SAEP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 311 NW------PLRGRKWSLWEGGVRgVGFVASP--LLKQKGVKNRELIHISDWLPTLVKLAR----GHTNG--TKPLDGFdv 376
Cdd:cd16025 263 GWanasntPFRLYKQASHEGGIR-TPLIVSWpkGIKAKGGIRHQFAHVIDIAPTILELAGveypKTVNGvpQLPLDGV-- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 377 wktisegspspriellhnidpnfvdsspcprnSMAPAKDDSSLP---EYSAFNTSVHAAIRHGNWKLLtgypgcgyWFPP 453
Cdd:cd16025 340 --------------------------------SLLPTLDGAAAPsrrRTQYFELFGNRAIRKGGWKAV--------ALHP 379
|
490 500 510
....*....|....*....|....*....|....*
gi 38569405 454 PsqynvseipssdPPTKTLW-LFDIDRDPEERHDL 487
Cdd:cd16025 380 P------------PGWGDQWeLYDLAKDPSETHDL 402
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
45-375 |
4.61e-77 |
|
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: 242.34 E-value: 4.61e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTGLQHqiiWPCQPSCV 122
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPdIKTPNLDRLAAEGVRFTNAYVAsPVCSPSRASLLTGRYPHRHGVRG---NVGNGGGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 123 PLDEKLLPQLLKEAGYTTHMVGKWHlgmyrkeclptrrgfdtyfgyllgsedyysherctlidalnvtrcaldfrdgeev 202
Cdd:cd16022 78 PPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 203 atgyknmystniftKRAIALITNHPPEKPLFLYLALQSVHEPLqvpeeylkpydfiqdknrhHYAGMVSLMDEAVGNVTA 282
Cdd:cd16022 103 --------------DEAIDFIERRDKDKPFFLYVSFNAPHPPF-------------------AYYAMVSAIDDQIGRILD 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 283 ALKSSGLWNNTVFIFSTDNGGQTLAGGnnwpLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKLAR 362
Cdd:cd16022 150 ALEELGLLDNTLIVFTSDHGDMLGDHG----LRGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAG 225
|
330
....*....|...
gi 38569405 363 GhtNGTKPLDGFD 375
Cdd:cd16022 226 I--EPPEGLDGRS 236
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
45-492 |
5.29e-77 |
|
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: 248.28 E-value: 5.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGS-RIRTPHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYQ----IRTGLQHQIIWPCQ 118
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQkKIKTPNLDRLAAEGMRFTQHYAgAPVCAPSRASLLTGLHTghtrVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 119 PscvplDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYL--LGSEDYYSHErctLIDalNVTRCALD- 195
Cdd:cd16145 81 P-----DDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHPTKQGFDYFYGYLdqVHAHNYYPEY---LWR--NGEKVPLPn 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 196 ----FRDGEEVATGYKNMYSTNIFTKRAIALITNHpPEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNRHH------ 265
Cdd:cd16145 151 nvipPLDEGNNAGGGGGTYSHDLFTDEALDFIREN-KDKPFFLYLAYTLPHAPLQVPDDGPYKYKPKDPGIYAYlpwpqp 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 266 ---YAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNG----GQTLAGGNNW----PLRGRKWSLWEGGVRGVGFVAS 334
Cdd:cd16145 230 ekaYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGphseGGSEHDPDFFdsngPLRGYKRSLYEGGIRVPFIARW 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 335 PLLKQKGVKNRELIHISDWLPTLVKLArghtnGTKPldgfdvwktisegspspriellhnidPNFVDSSpcprnSMAPA- 413
Cdd:cd16145 310 PGKIPAGSVSDHPSAFWDFMPTLADLA-----GAEP--------------------------PEDIDGI-----SLLPTl 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 414 --KDDSSLPEY---SAFNTSVHAAIRHGNWKLLtgypgcgywfpppsqynvseipSSDPPTKTLWLFDIDRDPEERHDLS 488
Cdd:cd16145 354 lgKPQQQQHDYlywEFYEGGGAQAVRMGGWKAV----------------------RHGKKDGPFELYDLSTDPGETNNLA 411
|
....
gi 38569405 489 REYP 492
Cdd:cd16145 412 AQHP 415
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
45-488 |
1.31e-73 |
|
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: 239.03 E-value: 1.31e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHG--SRIRTPHLDALAAGGV-LLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSC 121
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpdSKIPTPNIDRLAAEGMrFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 122 VPLDEKLLPQLLKEAGYTTHMVGKWHLGM--YRKECL-------------------PTRRGFDTYFGyllgsedyysher 180
Cdd:cd16143 81 IEPDRVTLAKMLKQAGYRTAMVGKWHLGLdwKKKDGKkaatgtgkdvdyskpikggPLDHGFDYYFG------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 181 ctlIDALNVTRcaldfrdgeevatgyknmystnIFTKRAIALITNHP-PEKPLFLYLALQSVHEPLQVPEEYLK-----P 254
Cdd:cd16143 148 ---IPASEVLP----------------------TLTDKAVEFIDQHAkKDKPFFLYFALPAPHTPIVPSPEFQGksgagP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 255 Y-DFIQDknrhhyagmvslMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLAGGN---------NWPLRGRKWSLWEG 324
Cdd:cd16143 203 YgDFVYE------------LDWVVGRILDALKELGLAENTLVIFTSDNGPSPYADYKelekfghdpSGPLRGMKADIYEG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 325 GVRgVGFVAS-PLLKQKGVKNRELIHISDWLPTLVKLArghtngtkpldGFDVWKTISEGSpspriellHNIDPNFV-DS 402
Cdd:cd16143 271 GHR-VPFIVRwPGKIPAGSVSDQLVSLTDLFATLAAIV-----------GQKLPDNAAEDS--------FSFLPALLgPK 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 403 SPCPRNSMAPAKDDSSLpeysafntsvhaAIRHGNWKLLTGYPGCGYWFPppsqynvseIPSSDPPTKTLWLFDIDRDPE 482
Cdd:cd16143 331 KQEVRESLVHHSGNGSF------------AIRKGDWKLIDGTGSGGFSYP---------RGKEKLGLPPGQLYNLSTDPG 389
|
....*.
gi 38569405 483 ERHDLS 488
Cdd:cd16143 390 ESNNLY 395
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
45-361 |
1.48e-71 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 230.39 E-value: 1.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGSRIR-TPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQHQIIWPcqpscV 122
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPtTPFLDRLAEEGLLFSNFYsGGTLTAPSRFALLTGLPPHNFGSYVSTPVG-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 123 PLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKEClPTRRGFDTYFGYLLGSEDYYSHERCTLIDALNvtrcaldfrdgeev 202
Cdd:pfam00884 76 PRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS-PCNLGFDKFFGRNTGSDLYADPPDVPYNCSGG-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 203 atgyknMYSTNIFTKRAIALITNhpPEKPLFLYLALQSVHEPLQVPEEYLKPY----DFIQDKNRHH--YAGMVSLMDEA 276
Cdd:pfam00884 141 ------GVSDEALLDEALEFLDN--NDKPFFLVLHTLGSHGPPYYPDRYPEKYatfkPSSCSEEQLLnsYDNTLLYTDDA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 277 VGNVTAALKSSGLWNNTVFIFSTDNGGQtLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPT 356
Cdd:pfam00884 213 IGRVLDKLEENGLLDNTLVVYTSDHGES-LGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPT 291
|
....*
gi 38569405 357 LVKLA 361
Cdd:pfam00884 292 ILDLA 296
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
45-487 |
1.72e-71 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 232.81 E-value: 1.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGSRI----RTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLqHQIIWPCQPS 120
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIgrgaPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGL-TTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 121 CVPLDEKLLPQLLKEAGYTTHMVGKWHLGMyRKECLPTRRGFDTYFGYLLgsedyyshercTLIDAlnvtrcaldfrdge 200
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGD-EDGRLPTDHGFDEFYGNLY-----------HTIDE-------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 201 evatgyknmystnIFTKRAIALIT-NHPPEKPLFLYLALQSVHEPLQVPEEYLKpydfiQDKNRHHYAGMVSLMDEAVGN 279
Cdd:cd16142 134 -------------EIVDKAIDFIKrNAKADKPFFLYVNFTKMHFPTLPSPEFEG-----KSSGKGKYADSMVELDDHVGQ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 280 VTAALKSSGLWNNTVFIFSTDNGGQTLA--GGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTL 357
Cdd:cd16142 196 ILDALDELGIADNTIVIFTTDNGPEQDVwpDGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 358 VKLArGHTNGTKPLDGFDVWktisegspspriellhnIDpnFVDSSPcprnsMAPAKDDSSLPEYSAFNTSVH-AAIRHG 436
Cdd:cd16142 276 AALA-GAPDPKDKLLGKDRH-----------------ID--GVDQSP-----FLLGKSEKSRRSEFFYFGEGElGAVRWK 330
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 38569405 437 NWKLLTGYPGcGYWFPPPSQYNVSEIPssdpptktlWLFDIDRDPEERHDL 487
Cdd:cd16142 331 NWKVHFKAQE-DTGGPTGEPFYVLTFP---------LIFNLRRDPKERYDV 371
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-487 |
1.22e-64 |
|
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: 214.77 E-value: 1.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPScvp 123
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGEsYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQKT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 124 ldeklLPQLLKEAGYTTHMVGKWHLGMYR-KECLPTRRGFDTYFGY-LLGSEDYYSHERctlidalNVTRCAldfRDGEE 201
Cdd:cd16151 78 -----FGHLLKDAGYATAIAGKWQLGGGRgDGDYPHEFGFDEYCLWqLTETGEKYSRPA-------TPTFNI---RNGKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 202 VATgYKNMYSTNIFTKRAIALITNHpPEKPLFLYLALQSVHEPLQV--PEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGN 279
Cdd:cd16151 143 LET-TEGDYGPDLFADFLIDFIERN-KDQPFFAYYPMVLVHDPFVPtpDSPDWDPDDKRKKDDPEYFPDMVAYMDKLVGK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 280 VTAALKSSGLWNNTVFIFSTDNG----GQTLAGGNNwpLRGRKWSLWEGGVRgVGFVAS-PLLKQKGVKNRELIHISDWL 354
Cdd:cd16151 221 LVDKLEELGLRENTIIIFTGDNGthrpITSRTNGRE--VRGGKGKTTDAGTH-VPLIVNwPGLIPAGGVSDDLVDFSDFL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 355 PTLVKLArghtnGTK-----PLDGFDVWKTIS-EGSPSPRIELLHNIDPNfvdsspcprnsmapakddsslpeysaFNTS 428
Cdd:cd16151 298 PTLAELA-----GAPlpedyPLDGRSFAPQLLgKTGSPRREWIYWYYRNP--------------------------HKKF 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 38569405 429 VHAAIRHGNWKLltgypgcgYWfpppsqynvseipssdpPTKtlwLFDIDRDPEERHDL 487
Cdd:cd16151 347 GSRFVRTKRYKL--------YA-----------------DGR---FFDLREDPLEKNPL 377
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
44-483 |
8.71e-60 |
|
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: 202.31 E-value: 8.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 44 PPHLVFLLADDLGWNDVGFHG--SRIRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTGLQHQIIwPCQPS 120
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWapNAILTPNLDKLAAEGTRFVDWYSAaSVCSPSRASLMTGRLGLRNGVGHNFL-PTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 121 CVPLDEKLLPQLLKEAGYTTHMVGKWHLGmYRKECLPTRRGFDTYFGYLlgsedyYSHerctliDALNVTRCAldfrdge 200
Cdd:cd16161 80 GLPLNETTLAEVLRQAGYATGMIGKWHLG-QREAYLPNSRGFDYYFGIP------FSH------DSSLADRYA------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 201 EVATGyknmystniFTKRAIAlitnhpPEKPLFLYLALQSVHEPLQVPEEYLKPydfiqDKNRHHYAGMVSLMDEAVGNV 280
Cdd:cd16161 140 QFATD---------FIQRASA------KDRPFFLYAALAHVHVPLANLPRFQSP-----TSGRGPYGDALQEMDDLVGQI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 281 TAALKSSGLWNNTVFIFSTDNG----GQTLAGG-------NNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIH 349
Cdd:cd16161 200 MDAVKHAGLKDNTLTWFTSDNGpwevKCELAVGpgtgdwqGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVS 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 350 ISDWLPTLVKLARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNidpnfvdsspcprNSMAPAKDDSSlpeysafntsv 429
Cdd:cd16161 280 TLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHP-------------NSGAAGAGALS----------- 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 38569405 430 haAIRHGNWKL--LTG--YPGCGYwFPPPSQYnvseipssDPPTktlwLFDIDRDPEE 483
Cdd:cd16161 336 --AVRCGDYKAhyATGgaLACCGS-TGPKLYH--------DPPL----LFDLEVDPAE 378
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
45-503 |
7.78e-57 |
|
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: 194.26 E-value: 7.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGSRIRTPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQ--HQIIWPcqpsc 121
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFtTAPVCSPSRSALLTGLYPHQNGAHglRSRGFP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 122 VPLDEKLLPQLLKEAGYTTHMVGKWHLGmyrkeclptrrgfdtyFGYLLGSEDYYSHERCTLIDALNVTRCALDFRDgee 201
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTHYN----------------PDAVFPFDDEMRGPDDGGRNAWDYASNAADFLN--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 202 vatgyknmystniftkraialitNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYD--------FIQD--KNRH---HYAG 268
Cdd:cd16027 137 -----------------------RAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDpekvkvppYLPDtpEVREdlaDYYD 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 269 MVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQtlaggnnWPlRGrKWSLWEGGVRgVGFVAS-PLLKQKGVKNREL 347
Cdd:cd16027 194 EIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMP-------FP-RA-KGTLYDSGLR-VPLIVRwPGKIKPGSVSDAL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 348 IHISDWLPTLVKLArghtnGTKPLDGFDvwktiseGspspriellHNIDPNFVDSSPCPRNSMapakddsslpeYSAFNT 427
Cdd:cd16027 264 VSFIDLAPTLLDLA-----GIEPPEYLQ-------G---------RSFLPLLKGEKDPGRDYV-----------FAERDR 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 428 SVHA-----AIRHGNWKLLtgypgcgYWFPPPsqynvsEipssdpptktlwLFDIDRDPEERHDL--SREYPHIVTKLLS 500
Cdd:cd16027 312 HDETydpirSVRTGRYKYI-------RNYMPE------E------------LYDLKNDPDELNNLadDPEYAEVLEELRA 366
|
...
gi 38569405 501 RLQ 503
Cdd:cd16027 367 ALD 369
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
45-495 |
3.14e-54 |
|
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: 189.18 E-value: 3.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHG--SRIRTPhLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGL--QHQIIWPCQP 119
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGhpTQERGP-IDDMAAEGIRFTQAYsADSVCTPSRAALLTGRLPIRSGMygGTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 120 SCVPLDEKLLPQLLKEAGYTTHMVGKWHLGM--YRKE---CLPTRRGFDtYFGYLLgseDYYSHERCT----LIDALNVT 190
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGIneNNHSdgaHLPSHHGFD-FVGTNL---PFTNSWACDdtgrHVDFPDRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 191 RCALDFRDgEEVATGYKNMYSTNIFTKRAIALITNHpPEKPLFLYLALQSVHEPLqvpeeYLKPyDFIQDKNRHHYAGMV 270
Cdd:cd16160 157 ACFLYYND-TIVEQPIQHEHLTETLVGDAKSFIEDN-QENPFFLYFSFPQTHTPL-----FASK-RFKGKSKRGRYGDNI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 271 SLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQT---LAGGNNWPLRGRKWSLWEGGVRgVGFVA-SPLLKQKGVKNrE 346
Cdd:cd16160 229 NEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVeycLEGGSTGGLKGGKGNSWEGGIR-VPFIAyWPGTIKPRVSH-E 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 347 LIHISDWLPTLVKLARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNidpnfvdsspCPRNSMApakddsslPEYSAFN 426
Cdd:cd16160 307 VVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDILYY----------CCSRLMA--------VRYGSYK 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38569405 427 TSVHAAIRHGNWKLLtgyPGCGYWFPPPSQYNVSEIPSS-----DPPTktlwLFDIDRDPEERHDLSRE-YPHIV 495
Cdd:cd16160 369 IHFKTQPLPSQESLD---PNCDGGGPLSDYIVCYDCEDEcvtkhNPPL----IFDVEKDPGEQYPLQPSvYEHML 436
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
44-383 |
1.07e-53 |
|
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: 188.44 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 44 PPHLVFLLADDLGWNDVGFHGSRIR-TPHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYQIRTGL----QH------ 111
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSReTPNLDRMAAEGMLFTDFYSaNPLCSPSRAALLTGRLPIRNGFyttnAHarnayt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 112 -QIIwpcqPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLGmYRKECLPTRRGFDTYFGY---LLGSEDYYSHERCTLI-DA 186
Cdd:cd16157 81 pQNI----VGGIPDSEILLPELLKKAGYRNKIVGKWHLG-HRPQYHPLKHGFDEWFGApncHFGPYDNKAYPNIPVYrDW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 187 LNVTRCALDFRDgeEVATGYKNMysTNIFTKRAIALITN-HPPEKPLFLYLALQSVHEPLQVPEEylkpydFIQDKNRHH 265
Cdd:cd16157 156 EMIGRYYEEFKI--DKKTGESNL--TQIYLQEALEFIEKqHDAQKPFFLYWAPDATHAPVYASKP------FLGTSQRGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 266 YAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLA----GGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKG 341
Cdd:cd16157 226 YGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALISapeqGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPG 305
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 38569405 342 VKNRELIHISDWLPTLVKLARGHTNGTKPLDGFDVWKTISEG 383
Cdd:cd16157 306 QVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNG 347
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
44-526 |
1.69e-53 |
|
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: 188.04 E-value: 1.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 44 PPHLVFLLADDLGWNDVGFHG-SRIRTPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSC 121
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGhPSSSTPNLDRLAANGLRFTDFYsSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 122 VPLDEKLLPQLLKEAGYTTHMVGKWHLGM-YRKECLPTRRGFDTYFGYLlgsedyYSHERCTLIDA-------------- 186
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLGVgLNGTYLPTHQGFDHYLGIP------YSHDQGPCQNLtcfppnipcfggcd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 187 LNVTRCALdFRDGEEVA-----TGYKNMYSTniFTKRAIAliTNHPPEKPLFLYLALQSVHEPlQVPEEylkpyDFIQDK 261
Cdd:cd16158 155 QGEVPCPL-FYNESIVQqpvdlLTLEERYAK--FAKDFIA--DNAKEGKPFFLYYASHHTHYP-QFAGQ-----KFAGRS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 262 NRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTL---AGGNNWPLRGRKWSLWEGGVRGVGFVASPLLK 338
Cdd:cd16158 224 SRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMrksRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 339 QKGVkNRELIHISDWLPTLVKLArghtNGTKP---LDGFDVWKTISEGSPSPRIELLhnidpnFVDSSPCprnsmapakd 415
Cdd:cd16158 304 KPGV-THELASTLDILPTIAKLA----GAPLPnvtLDGVDMSPILFEQGKSPRQTFF------YYPTSPD---------- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 416 dsslPEYSAFntsvhaAIRHGNWK---LLTGYPGCGYwFPPPSQYNVSEIPSSDPPTktlwLFDIDRDPEERHDLSREyP 492
Cdd:cd16158 363 ----PDKGVF------AVRWGKYKahfYTQGAAHSGT-TPDKDCHPSAELTSHDPPL----LFDLSQDPSENYNLLGL-P 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 38569405 493 HIVTKLLSRLQFYHKHSVPVYF----------PAQDPRCDPKAT 526
Cdd:cd16158 427 EYNQVLKQIQQVKERFEASMKFgeseinkgedPALEPCCKPGCT 470
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-503 |
3.48e-52 |
|
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: 181.61 E-value: 3.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHG-SRIRTPHLDALAAGGVLLDNYYTQ-----PLCTPSRSQLLTGRYqirtglqhqiIW--- 115
Cdd:cd16155 3 PNILFILADDQRADTIGALGnPEIQTPNLDRLARRGTSFTNAYNMggwsgAVCVPSRAMLMTGRT----------LFhap 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 116 PCQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHlgmyrkeclptrrgfdtyfgyllgsedyysherctlidalnvtrcald 195
Cdd:cd16155 73 EGGKAAIPSDDKTWPETFKKAGYRTFATGKWH------------------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 196 frdgeevatgyknmystNIFTKRAIALITNHP-PEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQ--------------- 259
Cdd:cd16155 105 -----------------NGFADAAIEFLEEYKdGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETiplpenflpqhpfdn 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 260 -----------------DKNRHHYA---GMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGgqtLAGGNNwPLRGrKW 319
Cdd:cd16155 168 gegtvrdeqlapfprtpEAVRQHLAeyyAMITHLDAQIGRILDALEASGELDNTIIVFTSDHG---LAVGSH-GLMG-KQ 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 320 SLWEGGVRGVGFVASPLLKqKGVKNRELIHISDWLPTLVKLArghtngtkpldGFDVWKTISEGSPSPRIEllhnidpnf 399
Cdd:cd16155 243 NLYEHSMRVPLIISGPGIP-KGKRRDALVYLQDVFPTLCELA-----------GIEIPESVEGKSLLPVIR--------- 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 400 vDSSPCPRNSMapakddsslpeYSAFnTSVHAAIRHGNWKLLTGYPGcgywfpppsqynvseipssdppTKTLWLFDIDR 479
Cdd:cd16155 302 -GEKKAVRDTL-----------YGAY-RDGQRAIRDDRWKLIIYVPG----------------------VKRTQLFDLKK 346
|
490 500
....*....|....*....|....*.
gi 38569405 480 DPEERHDLS--REYPHIVTKLLSRLQ 503
Cdd:cd16155 347 DPDELNNLAdePEYQERLKKLLAELK 372
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
43-503 |
5.69e-52 |
|
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: 182.73 E-value: 5.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 43 RPPHLVFLLADDLGWNDVGFHGSRI-RTPHLDALAAGGVLLDN-YYTQPLCTPSRSQLLTGRYQIRTGlqhqiIWPCQPS 120
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIvKTPNIDRLAKEGVRFDNaFVTTSICAPSRASILTGQYSHRHG-----VTDNNGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 121 CVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKEClptRRGFDtYFGYLLGSEDYYsherctliDALNVTRCALDFRDGe 200
Cdd:cd16031 76 LFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLP---PPGFD-YWVSFPGQGSYY--------DPEFIENGKRVGQKG- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 201 evatgyknmYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPY--------------------DFIQ- 259
Cdd:cd16031 143 ---------YVTDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYedvtipepetfddddyagrpEWARe 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 260 -------------------DKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNG---G-QTLAGgnnwplrg 316
Cdd:cd16031 214 qrnrirgvldgrfdtpekyQRYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGfflGeHGLFD-------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 317 rKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKLArghtnGTKP---LDGFDVWKTISEGSPSP-RIELL 392
Cdd:cd16031 286 -KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLA-----GVPIpedMQGRSLLPLLEGEKPVDwRKEFY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 393 HnidpnfvdsspcpRNSMapakddsslpEYSAFNTSVHAAIRHGNWKLLTGYPGCGYWFpppsqynvseipssdpptktl 472
Cdd:cd16031 360 Y-------------EYYE----------EPNFHNVPTHEGVRTERYKYIYYYGVWDEEE--------------------- 395
|
490 500 510
....*....|....*....|....*....|...
gi 38569405 473 wLFDIDRDPEERHDL--SREYPHIVTKLLSRLQ 503
Cdd:cd16031 396 -LYDLKKDPLELNNLanDPEYAEVLKELRKRLE 427
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
44-376 |
2.87e-47 |
|
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: 172.09 E-value: 2.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 44 PPHLVFLLADDLGWNDVGFHG-SRIRTPHLDALAAGGV-LLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQ-----IIWP 116
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGnDTIRTPNIDRLAKEGVkLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASShgmrvILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 117 CQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECL-----PTRRGFDTYFGYLL----------GSEDYYSHER- 180
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNdfchhPLNHGFDYFYGLPLtnlkdcgdgsNGEYDLSFDPl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 181 ----------CTLIDALNVTRCALDFRDGEEVATGY----------------------KN-------MYSTNI---FTKR 218
Cdd:cd16159 161 fplltafvliTALTIFLLLYLGAVSKRFFVFLLILSllfislfflllitnryfncilmRNhevveqpMSLENLtqrLTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 219 AIALITNHpPEKPLFLYLALQSVHEPLQVPEEYLkpydfiqDKNRH-HYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIF 297
Cdd:cd16159 241 AISFLERN-KERPFLLVMSFLHVHTALFTSKKFK-------GRSKHgRYGDNVEEMDWSVGQILDALDELGLKDNTFVYF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 298 STDNGG--------QTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKLARGHTNGTK 369
Cdd:cd16159 313 TSDNGGhleeisvgGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDR 392
|
....*..
gi 38569405 370 PLDGFDV 376
Cdd:cd16159 393 IIDGRDL 399
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-361 |
1.83e-46 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 166.97 E-value: 1.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQHqiiwpcqpSCV 122
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDpVKTPNLDRLAKEGVVFTNAVsNYPVCSPYRASLLTGQYPLTNGVFG--------NDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 123 PL--DEKLLPQLLKEAGYTTHMVGKWHL-GMYRKECL-------PTRR-GFDTYFGYllGSEDYYSHerctlidalnvtr 191
Cdd:cd16034 74 PLppDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGRaddytppPERRhGFDYWKGY--ECNHDHNN------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 192 cALDFRDGEEvaTGYKNMYSTNIFTKRAIALITNH-PPEKPLFLYLALQSVHEP-LQVPEEYLKPYDFIQDKNR------ 263
Cdd:cd16034 139 -PHYYDDDGK--RIYIKGYSPDAETDLAIEYLENQaDKDKPFALVLSWNPPHDPyTTAPEEYLDMYDPKKLLLRpnvped 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 264 -----------HHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLAGGNNwplrgRKWSLWEGGVRgVGFV 332
Cdd:cd16034 216 kkeeaglredlRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-----NKQVPYEESIR-VPFI 289
|
330 340 350
....*....|....*....|....*....|
gi 38569405 333 AS-PLLKQKGVKNRELIHISDWLPTLVKLA 361
Cdd:cd16034 290 IRyPGKIKAGRVVDLLINTVDIMPTLLGLC 319
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-361 |
9.58e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 142.49 E-value: 9.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGW---NDVGFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGlqhqIIWPcqPSC 121
Cdd:cd16154 1 PNILLIIADDQGLdssAQYSLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTG----VLAV--PDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 122 VPLDEKLLPQLLKE----AGYTTHMVGKWHLGmyrkECLPTRR---GFDTYFGYLLGS-EDYYSHERCTLIDALNVTRca 193
Cdd:cd16154 75 LLLSEETLLQLLIKdattAGYSSAVIGKWHLG----GNDNSPNnpgGIPYYAGILGGGvQDYYNWNLTNNGQTTNSTE-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 194 ldfrdgeevatgyknmYSTNIFTKRAIALITNHppEKPLFLYLALQSVHEPLQVPEEYLKPYDF------IQDKNRHHYA 267
Cdd:cd16154 149 ----------------YATTKLTNLAIDWIDQQ--TKPWFLWLAYNAPHTPFHLPPAELHSRSLlgdsadIEANPRPYYL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 268 GMVSLMDEAVGNVTAALKSSGLwNNTVFIFSTDNGGQTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNREL 347
Cdd:cd16154 211 AAIEAMDTEIGRLLASIDEEER-ENTIIIFIGDNGTPGQVVDLPYTRNHAKGSLYEGGINVPLIVSGAGVERANERESAL 289
|
330
....*....|....
gi 38569405 348 IHISDWLPTLVKLA 361
Cdd:cd16154 290 VNATDLYATIAELA 303
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-503 |
1.03e-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: 293771 [Multi-domain] Cd Length: 373 Bit Score: 139.67 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 44 PPHLVFLLADDLGWNDVGFHGSRI-RTPHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYQIRTGLQHQIIwpcqpsC 121
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLdLTPNLDALAEEGVLFENAFTpQPVCGPARACLQTGLYPTETGCFRNGI------P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 122 VPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRkeclptrrgfdtyfgyllgsedyysherctlIDALnvtrcaldfrdgee 201
Cdd:cd16152 75 LPADEKTLAHYFRDAGYETGYVGKWHLAGYR-------------------------------VDAL-------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 202 vatgyknmystnifTKRAIALITNHPPEKPLFLYLAL-----QSVHEPLQVPEEYLKPY----------DFIQDKNRHH- 265
Cdd:cd16152 110 --------------TDFAIDYLDNRQKDKPFFLFLSYlephhQNDRDRYVAPEGSAERFanfwvppdlaALPGDWAEELp 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 266 -YAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQtlaggnnwpLRGR----KWSLWEGGVR------GVGFvas 334
Cdd:cd16152 176 dYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCH---------FRTRnaeyKRSCHESSIRvplviyGPGF--- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 335 pllkQKGVKNRELIHISDWLPTLVKLArghtngtkpldGFDVWKTISeGspspriellHNIDPNFVDSSPCPRNsmapak 414
Cdd:cd16152 244 ----NGGGRVEELVSLIDLPPTLLDAA-----------GIDVPEEMQ-G---------RSLLPLVDGKVEDWRN------ 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 415 ddsslpeySAF----NTSVHAAIRHGNWKLLTGYPGCGYWFPPPSQYNVSEipssdpptktlWLFDIDRDPEERHDL--S 488
Cdd:cd16152 293 --------EVFiqisESQVGRAIRTDRWKYSVAAPDKDGWKDSGSDVYVED-----------YLYDLEADPYELVNLigR 353
|
490
....*....|....*
gi 38569405 489 REYPHIVTKLLSRLQ 503
Cdd:cd16152 354 PEYREVAAELRERLL 368
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-482 |
5.44e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 136.52 E-value: 5.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHG-SRIRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTGlqhqiIWpcqPSCV 122
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGhPVVRTPNLDRLAARGTRFENAYTPsPICVPSRASFLTGRYVHETG-----VW---DNAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 123 PLDEKL--LPQLLKEAGYTTHMVGKWHlgmYRKECLPTrrGFDtyfgyllgsedyysHERctlidalNVTRCALDFrdge 200
Cdd:cd16037 73 PYDGDVpsWGHALRAAGYETVLIGKLH---FRGEDQRH--GFR--------------YDR-------DVTEAAVDW---- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 201 evatgyknmystniftkraiaLITNHPPEKPLFLYLALQSVHEPLQVPEEYlkpYDFIQDKNRHHYAGMVSLMDEAVGNV 280
Cdd:cd16037 123 ---------------------LREEAADDKPWFLFVGFVAPHFPLIAPQEF---YDLYVRRARAAYYGLVEFLDENIGRV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 281 TAALKSSGLWNNTVFIFSTDNGGQTLAGGNNWplrgrKWSLWEGGVRGVGFVASPLLKQKGVKNR--ELIHISdwlPTLV 358
Cdd:cd16037 179 LDALEELGLLDNTLIIYTSDHGDMLGERGLWG-----KSTMYEESVRVPMIISGPGIPAGKRVKTpvSLVDLA---PTIL 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 359 KLArgHTNGTKPLDGFDVWKTISEGSPSPRiellhnidpnFVDSspcprnsmapakddsslpEYSAFNTSV-HAAIRHGN 437
Cdd:cd16037 251 EAA--GAPPPPDLDGRSLLPLAEGPDDPDR----------VVFS------------------EYHAHGSPSgAFMLRKGR 300
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 38569405 438 WKLLTgYPGcgywfpPPSQynvseipssdpptktlwLFDIDRDPE 482
Cdd:cd16037 301 WKYIY-YVG------YPPQ-----------------LFDLENDPE 321
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-375 |
1.07e-33 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 132.34 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGSRI-RTPHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSCV 122
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIvKTPNIDRLAAEGVRFTNAYTpSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 123 -PLDEKLLPQLLKEAGYTTHMVGKWHLGmyrKECLPTRRGFDTYFGYllgsedyysherctlidalnvtrcaldfrdgEE 201
Cdd:cd16033 81 lPPGVETFSEDLREAGYRNGYVGKWHVG---PEETPLDYGFDEYLPV-------------------------------ET 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 202 VATGYknmystniFTKRAIALITNH-PPEKPLFLYLALQSVHEPLQVPEEYL--------------------KPYdfIQD 260
Cdd:cd16033 127 TIEYF--------LADRAIEMLEELaADDKPFFLRVNFWGPHDPYIPPEPYLdmydpediplpesfaddfedKPY--IYR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 261 KNR-----------------HHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLAGGnnwpLRGRKWSLWE 323
Cdd:cd16033 197 RERkrwgvdtedeedwkeiiAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHR----LWDKGPFMYE 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 38569405 324 GGVRgVGFVAS-PLLKQKGVKNRELIHISDWLPTLVKLArghtnGTKPLDGFD 375
Cdd:cd16033 273 ETYR-IPLIIKwPGVIAAGQVVDEFVSLLDLAPTILDLA-----GVDVPPKVD 319
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
44-361 |
7.62e-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: 127.30 E-value: 7.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 44 PPHLVFLLADDLgwND-VGFHGSR-IRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTGLQ--HQIIWPCQ 118
Cdd:cd16030 2 KPNVLFIAVDDL--RPwLGCYGGHpAKTPNIDRLAARGVLFTNAYCQqPVCGPSRASLLTGRRPDTTGVYdnNSYFRKVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 119 PscvplDEKLLPQLLKEAGYTTHMVGK-WHlgMYRKECLPTRRGFDTYFgYLLGSEDYYSHERCTLIDALNVTRCALDFr 197
Cdd:cd16030 80 P-----DAVTLPQYFKENGYTTAGVGKiFH--PGIPDGDDDPASWDEPP-NPPGPEKYPPGKLCPGKKGGKGGGGGPAW- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 198 dgeEVATGYKNMYSTNIFTKRAIALITN-HPPEKPLFLylalqSV-----HEPLQVPEEYLKPYDF-------------- 257
Cdd:cd16030 151 ---EAADVPDEAYPDGKVADEAIEQLRKlKDSDKPFFL-----AVgfykpHLPFVAPKKYFDLYPLesiplpnpfdpidl 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 258 --------------------------------IQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNG--- 302
Cdd:cd16030 223 pevawndlddlpkygdipalnpgdpkgplpdeQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGwhl 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38569405 303 GQTlaggNNWplrgRKWSLWEGGVRgVGF-VASPLLKQKGVKNR---ELIhisDWLPTLVKLA 361
Cdd:cd16030 303 GEH----GHW----GKHTLFEEATR-VPLiIRAPGVTKPGKVTDalvELV---DIYPTLAELA 353
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-361 |
1.27e-31 |
|
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: 122.73 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHG-SRIRTPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYqirtGLQHQII-----WPC 117
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGnSEAVTPNLDRLAAEGVRFENFFcTSPVCSPARASLLTGRM----PSQHGIHdwiveGSH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 118 QPSCVPLD----EKLLPQLLKEAGYTTHMVGKWHLGMYrkeclptrrgfdtyfgyllgsedyysherctlidalnvtrcA 193
Cdd:cd16149 77 GKTKKPEGylegQTTLPEVLQDAGYRCGLSGKWHLGDD-----------------------------------------A 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 194 LDFrdgeevatgyknmystniftkraiaLITNHPPEKPLFLYLALQSVHEPlqvpeeylkpydfiqdknrHHYAGMVSLM 273
Cdd:cd16149 116 ADF-------------------------LRRRAEAEKPFFLSVNYTAPHSP-------------------WGYFAAVTGV 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 274 DEAVGNVTAALKSSGLWNNTVFIFSTDNG---GQTlaG----GN-NWPLrgrkwSLWEGGVRgVGFVAS-PLLKQKGVKN 344
Cdd:cd16149 152 DRNVGRLLDELEELGLTENTLVIFTSDNGfnmGHH--GiwgkGNgTFPL-----NMYDNSVK-VPFIIRwPGVVPAGRVV 223
|
330
....*....|....*..
gi 38569405 345 RELIHISDWLPTLVKLA 361
Cdd:cd16149 224 DSLVSAYDFFPTLLELA 240
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
45-502 |
3.69e-30 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 123.24 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTG-LQHQiiwpcqpSC 121
Cdd:PRK13759 7 PNIILIMVDQMRGDCLGCNGNKaVETPNLDMLASEGYNFENAYSAvPSCTPARAALLTGLSQWHHGrVGYG-------DV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 122 VPLDEK-LLPQLLKEAGYTTHMVGKWHLGMYRKEClptrrGFDTYF---GYlLGSEDYYSHERCTLID-----------A 186
Cdd:PRK13759 80 VPWNYKnTLPQEFRDAGYYTQCIGKMHVFPQRNLL-----GFHNVLlhdGY-LHSGRNEDKSQFDFVSdylawlrekapG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 187 LNVTRCALDFRDGEEVATGYK---NMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLK---------- 253
Cdd:PRK13759 154 KDPDLTDIGWDCNSWVARPWDleeRLHPTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSPYDPPKRYFDmykdadipdp 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 254 -----PYDFIQDKN-------------------RHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQtLAGG 309
Cdd:PRK13759 234 higdwEYAEDQDPEggsidalrgnlgeeyarraRAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDM-LGDH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 310 NNWplrgRKWSLWEGGVRGVGFVASP---LLKQKGVKNRELIHISDWLPTLVKLARGHTngTKPLDGFDVWKTISEGSPS 386
Cdd:PRK13759 313 YLF----RKGYPYEGSAHIPFIIYDPgglLAGNRGTVIDQVVELRDIMPTLLDLAGGTI--PDDVDGRSLKNLIFGQYEG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 387 PR--IELLHnidpnfvdsSPCprnsmapakddsslpeYSAFNTsvhaaIRHGNWKLLtgypgcgyWFpppsqynvseips 464
Cdd:PRK13759 387 WRpyLHGEH---------ALG----------------YSSDNY-----LTDGKWKYI--------WF------------- 415
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 38569405 465 sdPPTKTLWLFDIDRDPEERHDLS--REYPHIVTKLLSRL 502
Cdd:PRK13759 416 --SQTGEEQLFDLKKDPHELHNLSpsEKYQPRLREMRKKL 453
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
45-373 |
1.12e-29 |
|
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: 118.84 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGSRI-RTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTGlqhqiIW--PCQ-P 119
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVvKTPNLDRLAARGVVFDNAYCNsPLCAPSRASMMTGRLPSRIG-----AYdnAAEfP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 120 SCVPLdeklLPQLLKEAGYTTHMVGKWHLgmyrkeCLPtrrgfDTYFGYllgseDYysherctlidalnvtrcaldfrDg 199
Cdd:cd16032 76 ADIPT----FAHYLRAAGYRTALSGKMHF------VGP-----DQLHGF-----DY----------------------D- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 200 EEVAtgYKnmystnifTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYlkpYDFIQDKNRHHYAGMVSLMDEAVGN 279
Cdd:cd16032 113 EEVA--FK--------AVQKLYDLARGEDGRPFFLTVSFTHPHDPYVIPQEY---WDLYVRRARRAYYGMVSYVDDKVGQ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 280 VTAALKSSGLWNNTVFIFSTDNG---GQtlaggnnwplRGR--KWSLWEGGVRGVGFVASPLLKQkGVKNRELIHISDWL 354
Cdd:cd16032 180 LLDTLERTGLADDTIVIFTSDHGdmlGE----------RGLwyKMSFFEGSARVPLIISAPGRFA-PRRVAEPVSLVDLL 248
|
330 340
....*....|....*....|
gi 38569405 355 PTLVKLARG-HTNGTKPLDG 373
Cdd:cd16032 249 PTLVDLAGGgTAPHVPPLDG 268
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-361 |
3.78e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 116.11 E-value: 3.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGS-RIRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYqirtGLQHQIIWPcqpscv 122
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYdRVTTPNLDRLAAEGVVFDNHYSGsNPTLPSRFSLFTGLY----PFYHGVWGG------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 123 PLDEK--LLPQLLKEAGYTTHMVGKWHLgmyrkecLPTRRGFDTYFgyllgseDYYsherctlidalnvtrcalDFRDGE 200
Cdd:cd16148 71 PLEPDdpTLAEILRKAGYYTAAVSSNPH-------LFGGPGFDRGF-------DTF------------------EDFRGQ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 201 EVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPlqvpeeYLkpydfiqdknrhhYAGMVSLMDEAVGNV 280
Cdd:cd16148 119 EGDPGEEGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPHEP------YL-------------YDAEVRYVDEQIGRL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 281 TAALKSSGLWNNTVFIFSTDNgGQTLA-GGNNWplrGRKWSLWEGGVRgVGFVASPLLKQKGVKNRELIHISDWLPTLVK 359
Cdd:cd16148 180 LDKLKELGLLEDTLVIVTSDH-GEEFGeHGLYW---GHGSNLYDEQLH-VPLIIRWPGKEPGKRVDALVSHIDIAPTLLD 254
|
..
gi 38569405 360 LA 361
Cdd:cd16148 255 LL 256
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
44-304 |
2.78e-28 |
|
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: 116.50 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 44 PPHLVFLLADDLGWNDVGFHGSRirtPHLDALAAGGVLLDNYY-TQPLCTPSRSQLLTGRYQIRTGLQHQIIwPCqpSCV 122
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMP---KTKKLLADQGTTFTNAFvTTPLCCPSRASILTGQYAHNHGVTNNSP-PG--GGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 123 P------LDEKLLPQLLKEAGYTTHMVGKwHLGMYRKECLPTR--RGFDTYFGYLLGSEDYYSHerctlidalnvtrcaL 194
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRTAYAGK-YLNGYGVPGGVSYvpPGWDEWDGLVGNSTYYNYT---------------L 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 195 DFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPE-KPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNR---------- 263
Cdd:cd16147 139 SNGGNGKHGVSYPGDYLTDVIANKALDFLRRAAADdKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPPRpppnnpdvsd 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38569405 264 -HHY--------AGMV------------SLM--DEAVGNVTAALKSSGLWNNTVFIFSTDNG---GQ 304
Cdd:cd16147 219 kPHWlrrlpplnPTQIayidelyrkrlrTLQsvDDLVERLVNTLEATGQLDNTYIIYTSDNGyhlGQ 285
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-305 |
8.17e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 112.71 E-value: 8.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVG-FHGSRIRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTG--LQHQIIWPCQPS 120
Cdd:cd16150 1 PNIVIFVADQLRADSLGhLGNPAAVTPNLDALAAEGVRFSNAYCQnPVCSPSRCSFLTGWYPHVNGhrTLHHLLRPDEPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 121 cvpldeklLPQLLKEAGYTTHMVGKWHlgmyrkeCLPTRRGFDTYfgyllgsedyysherCTLIDAlnvtrcaldfrdge 200
Cdd:cd16150 81 --------LLKTLKDAGYHVAWAGKND-------DLPGEFAAEAY---------------CDSDEA-------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 201 evatgyknmystniFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYD-------------------FIQDK 261
Cdd:cd16150 117 --------------CVRTAIDWLRNRRPDKPFCLYLPLIFPHPPYGVEEPWFSMIDreklpprrppglrakgkpsMLEGI 182
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 38569405 262 NRHH---------------YAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQT 305
Cdd:cd16150 183 EKQGldrwseerwrelratYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYT 241
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
49-502 |
3.45e-26 |
|
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: 111.20 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 49 FLLADDLGWNDVGFHG-SRIRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRtglqHQIIWpcqpSCVPLD- 125
Cdd:cd16028 5 FITADQWRADCLSCLGhPLVKTPNLDRLAAEGVRFRNHYTQaAPCGPSRASLYTGRYLMN----HRSVW----NGTPLDa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 126 -EKLLPQLLKEAGYTTHMVGKWHL-----GMYRKeclptrrgfDTYFGYLLGSEDYYSHerctlidalnvtRCALDFRDG 199
Cdd:cd16028 77 rHLTLALELRKAGYDPALFGYTDTspdprGLAPL---------DPRLLSYELAMPGFDP------------VDRLDEYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 200 EEVATGYknmystniFTKRAIALITNHpPEKPLFLYLALQSVHEPLQVPEEYLKPYD-----------FIQDKNRHH--- 265
Cdd:cd16028 136 EDSDTAF--------LTDRAIEYLDER-QDEPWFLHLSYIRPHPPFVAPAPYHALYDpadvpppiraeSLAAEAAQHpll 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 266 ---------------------------------YAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQtlaGGNNW 312
Cdd:cd16028 207 aaflerieslsfspgaanaadlddeevaqmratYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQ---LGDHW 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 313 plrgrkwsLWEggvrgvgfvaspllkqKGVKNRELIHIsdwlPTLVKLAR---GHTNGTKpLDGF----DVWKTISE--- 382
Cdd:cd16028 284 --------LWG----------------KDGFFDQAYRV----PLIVRDPRreaDATRGQV-VDAFtesvDVMPTILDwlg 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 383 GSPSPRIE------LLHNIDPNfvdsspcPRNSMAPAKDDSSLPEYS----AFNTSVH----AAIRHGNWKLLTgYPGcg 448
Cdd:cd16028 335 GEIPHQCDgrsllpLLAGAQPS-------DWRDAVHYEYDFRDVSTRrpqeALGLSPDecslAVIRDERWKYVH-FAA-- 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 38569405 449 ywFPPpsqynvseipssdpptktlWLFDIDRDPEERHDLSR--EYPHIVTKLLSRL 502
Cdd:cd16028 405 --LPP-------------------LLFDLKNDPGELRDLAAdpAYAAVVLRYAQKL 439
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-375 |
5.85e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 104.38 E-value: 5.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGS-----------RIRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYQIRTGL-QH 111
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNahtgksesrlgYVESPNIDALAAEGVLFTNAYCNsPVCVPSRTSMLTGRYPHRTGVyGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 112 QIIWPcQPSCVPLdekLLPQLLKEAGYTTHMVGKWHLGMYRKeclptrrgfdtyfgYLlgsedyysherctliDALNVTr 191
Cdd:cd16153 82 EAAHP-ALDHGLP---TFPEVLKKAGYQTASFGKSHLEAFQR--------------YL---------------KNANQS- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 192 caldfrdgeevatgYKNMYSTNIFTKRaialitnhpPEKPLFLYLALQSVHEPLQVPEEYlkpydfiqdKNRHHYAGMVS 271
Cdd:cd16153 128 --------------YKSFWGKIAKGAD---------SDKPFFVRLSFLQPHTPVLPPKEF---------RDRFDYYAFCA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 272 LMDEAVGNVTAALKSSGLWN---NTVFIFSTDNGGQTlagGNNWPLrgRKWSLWEGGVRGVGFVASP--LLKQKGVKNRE 346
Cdd:cd16153 176 YGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHL---GEQGIL--AKFTFWPQSHRVPLIVVSSdkLKAPAGKVRHD 250
|
330 340
....*....|....*....|....*....
gi 38569405 347 LIHISDWLPTLVKLARGHTNGTKPLDGFD 375
Cdd:cd16153 251 FVEFVDLAPTLLAAAGVDVDAPDYLDGRD 279
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
45-266 |
3.28e-23 |
|
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: 102.46 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVG-FHGSRIRTPHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYqirtglqhqiiwPCQ---- 118
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGcYGNKAMKTPNLDRLAAEGVRFDSAYTtQPVCGPARSGLFTGLY------------PHTngsw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 119 PSCVPLDE--KLLPQLLKEAGYTTHMVGKWHLGmyrkeclptrrGFDtYFGYllG------SEDYYSHERCTLiDALN-- 188
Cdd:cd16156 69 TNCMALGDnvKTIGQRLSDNGIHTAYIGKWHLD-----------GGD-YFGN--GicpqgwDPDYWYDMRNYL-DELTee 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 189 ---VTRCALDFRDGEEVATGYknMYSTNIfTKRAIALITNHpPEKPLFLYLALQSVHEPLQVPEEYLKPY-DFIQDKNRH 264
Cdd:cd16156 134 errKSRRGLTSLEAEGIKEEF--TYGHRC-TNRALDFIEKH-KDEDFFLVVSYDEPHHPFLCPKPYASMYkDFEFPKGEN 209
|
..
gi 38569405 265 HY 266
Cdd:cd16156 210 AY 211
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
70-361 |
1.27e-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: 77.63 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 70 PHLDALAAGGVLLDNYYT-QPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPscvPLDEKL--LPQLLKEAGYTTHMVGKW 146
Cdd:cd16035 27 PARERLAANGLSFENHYTaACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQP---LLSPDVptLGHMLRAAGYYTAYKGKW 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 147 HLGmyrkeclptrrgfdtyfGYLLGSEDYysherctlidalnvtrcaldfrDGeevatgyknmystnIFTKRAIALITNH 226
Cdd:cd16035 104 HLS-----------------GAAGGGYKR----------------------DP--------------GIAAQAVEWLRER 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 227 PPE----KPLFLYLAL---QSVHEPLQVPEEYLKPYDFiqdknrhhYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFST 299
Cdd:cd16035 131 GAKnadgKPWFLVVSLvnpHDIMFPPDDEERWRRFRNF--------YYNLIRDVDRQIGRVLDALDASGLADNTIVVFTS 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38569405 300 DNGGQTLAGGnnwpLRGRKWSLWEGGVRgVGFVAS-PLLKQKGVKNRELI-HIsDWLPTLVKLA 361
Cdd:cd16035 203 DHGEMGGAHG----LRGKGFNAYEEALH-VPLIIShPDLFGTGQTTDALTsHI-DLLPTLLGLA 260
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
69-300 |
7.01e-15 |
|
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: 75.03 E-value: 7.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 69 TPHLDALAAGGVLLDNYYTQPLCTP-SRSQ--LLTGRYQI--RTGLQHQIIWPCQPScvpldeklLPQLLKEAGYTTHMV 143
Cdd:cd16015 26 TPNLNKLAKEGLYFGNFYSPGFGGGtANGEfeVLTGLPPLplGSGSYTLYKLNPLPS--------LPSILKEQGYETIFI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 144 GKWHLGMYRkeclptRRGFDTYFGYllgsEDYYSHErctlidalnvtrcalDFRDGEEVATGYknMYSTNIFTKRAIALI 223
Cdd:cd16015 98 HGGDASFYN------RDSVYPNLGF----DEFYDLE---------------DFPDDEKETNGW--GVSDESLFDQALEEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 224 TNHPpEKPLFLYLA-LQSvHEPLQVPEEYLKPYDFIQDKNRH--HYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTD 300
Cdd:cd16015 151 EELK-KKPFFIFLVtMSN-HGPYDLPEEKKDEPLKVEEDKTEleNYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGD 228
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
37-361 |
1.89e-14 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 75.85 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 37 SGAGASRPPHLVFLLADDLGWNDVGFHGSRIR-TPHLDALAAGGVLLDNYYTQplcTP--SRSQ--LLTGRYQ------I 105
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDvTPFLDSLAKESLYFGNFYSQ---GGrtSRGEfaVLTGLPPlpggspY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 106 RTGLQHQiiwpcQPScvpldeklLPQLLKEAGYTTHMvgkWH---LGMYRkeclptRRGFDTYFGYllgsEDYYSHErct 182
Cdd:COG1368 304 KRPGQNN-----FPS--------LPSILKKQGYETSF---FHggdGSFWN------RDSFYKNLGF----DEFYDRE--- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 183 lidalnvtrcalDFRDGEEVATGYKNMYstniFTKRAIALITNHPpeKPLFLYLALQSVHEPLQVPEEYLKPYDFiQDKN 262
Cdd:COG1368 355 ------------DFDDPFDGGWGVSDED----LFDKALEELEKLK--KPFFAFLITLSNHGPYTLPEEDKKIPDY-GKTT 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 263 RHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGqtlaggnnwPLRGRKWSLWEGGVRGV-GFVASPLLKQKG 341
Cdd:COG1368 416 LNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGP---------RSPGKTDYENPLERYRVpLLIYSPGLKKPK 486
|
330 340
....*....|....*....|
gi 38569405 342 VKNRELIHIsDWLPTLVKLA 361
Cdd:COG1368 487 VIDTVGSQI-DIAPTLLDLL 505
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
45-361 |
2.27e-14 |
|
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: 72.84 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVG-FHGSRIRTPHLDALAAGGVLLD--NYYTQPLCTPSRSQLLTGRYQIRTGL-QHQIIWPCQPS 120
Cdd:cd00016 1 KHVVLIVLDGLGADDLGkAGNPAPTTPNLKRLASEGATFNfrSVSPPTSSAPNHAALLTGAYPTLHGYtGNGSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 121 CV---PLDEKLLPQLLKEAGYTTHMVGkwhlgmyrkeclptrrgfdtyfgyllgsedyysherctlidalnvtrcALDFr 197
Cdd:cd00016 81 RAagkDEDGPTIPELLKQAGYRTGVIG------------------------------------------------LLKA- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 198 dgeevatgyknmystniftkraialITNHPPEKPLFLYLALQSVHEPLQvpeeylkpydfiqDKNRHH--YAGMVSLMDE 275
Cdd:cd00016 112 -------------------------IDETSKEKPFVLFLHFDGPDGPGH-------------AYGPNTpeYYDAVEEIDE 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 276 AVGNVTAALKSSGLWNNTVFIFSTDNGGqTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHIsDWLP 355
Cdd:cd00016 154 RIGKVLDALKKAGDADDTVIIVTADHGG-IDKGHGGDPKADGKADKSHTGMRVPFIAYGPGVKKGGVKHELISQY-DIAP 231
|
....*.
gi 38569405 356 TLVKLA 361
Cdd:cd00016 232 TLADLL 237
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
39-302 |
1.84e-07 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 53.21 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 39 AGASRPPHLVFLLADDLGWNDVGFHgsriRTPHLDALAAGGVLLDNYYTQ-PLCT-PSRSQLLTGRYQIRTG-------- 108
Cdd:COG1524 18 AAAPPAKKVVLILVDGLRADLLERA----HAPNLAALAARGVYARPLTSVfPSTTaPAHTTLLTGLYPGEHGivgngwyd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 109 --LQHQIIWPCQPSCVPLDEKLLP-----QLLKEAGYTTHMVGKWHLGMYrkeclptrrgfdtyfgyllgsedyysherc 181
Cdd:COG1524 94 peLGRVVNSLSWVEDGFGSNSLLPvptifERARAAGLTTAAVFWPSFEGS------------------------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 182 TLIDAlnvtrcALDFR-DGEEVATGYknmYSTNIFT-KRAIALITNHPPEkplFLYLALQSVheplqvpeeylkpydfiq 259
Cdd:COG1524 144 GLIDA------ARPYPyDGRKPLLGN---PAADRWIaAAALELLREGRPD---LLLVYLPDL------------------ 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 38569405 260 DKNRHHY-------AGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNG 302
Cdd:COG1524 194 DYAGHRYgpdspeyRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
45-362 |
2.38e-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: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 45 PHLVFLLADDLGWNDVGFHGSR-IRTPHLDALAAGGVLLDNYYTQ-PLCTPSRSQLLTGRYqirTGLQHQiiWPcQPSCV 122
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQvVDLPYINFMKQHGSVFLNAYTNsPICCPSRAAMWSGLF---THLTES--WN-NYKGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 123 PLDEKLLPQLLKEAGYTTHMVGKwhlgmyrkeclptrrgfdtyfgyllgsEDYYS--HERCTLIDALNVTRCALDFRDGE 200
Cdd:cd16171 75 DPNYPTWMDRLEKHGYHTQKYGK---------------------------LDYTSghHSVSNRVEAWTRDVPFLLRQEGR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 201 EVATGYKNMYSTNIF------TKRAIALITNHPP--EKPLFLYLALQSVHEplqVPEEYLKPyDFIQDKN-RHHYAGMVS 271
Cdd:cd16171 128 PTVNLVGDRSTVRVMlkdwqnTDKAVHWIRKEAPnlTQPFALYLGLNLPHP---YPSPSMGE-NFGSIRNiRAFYYAMCA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569405 272 LMDEAVGNVTAALKSSGLWNNTVFIFSTDNGgqTLAggnnwpLRGR---KWSLWEGGVRGVGFVASPLLKqKGVKNRELI 348
Cdd:cd16171 204 ETDAMLGEIISALKDTGLLDKTYVFFTSDHG--ELA------MEHRqfyKMSMYEGSSHVPLLIMGPGIK-AGQQVSDVV 274
|
330
....*....|....
gi 38569405 349 HISDWLPTLVKLAR 362
Cdd:cd16171 275 SLVDIYPTMLDIAG 288
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
432-498 |
1.79e-03 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 38.45 E-value: 1.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38569405 432 AIRHGNWKL--------LTGYPGCGYWFPPPSQYnvseipssDPPtktLwLFDIDRDPEERHDL---SREYPHIVTKL 498
Cdd:pfam14707 16 AVRWGPYKAhfftpsfdPPGAEGCYGSKVPVTHH--------DPP---L-LFDLERDPSEKYPLspdSPEYPEVLAEI 81
|
|
| |
