|
Name |
Accession |
Description |
Interval |
E-value |
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
27-408 |
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: 539.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPAMCTPSRGALLSGRYPIHTGTQHFVISNEEPWALT 106
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEPYGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 107 LNATLMPEIFKEAGYSTNLVGKWHLGFSRPEYTPTRRGFDYHFGYWGAYIDYFQRRSKMPVANYslGYDFRRNMELECRD 186
Cdd:cd16029 81 LNETLLPQYLKELGYATHLVGKWHLGFYTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGGANDYG--NDDLRDNEEPAWDY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 187 RGVYVTDLLTAEAERLIKDHaDKEQPLFLMLSHLAAHTANEDDPLQAPEEEiQKFSYIKDPNRRKYAAMISKLDQSVGRI 266
Cdd:cd16029 159 NGTYSTDLFTDRAVDIIENH-DPSKPLFLYLAFQAVHAPLQVPPEYADPYE-DKFAHIKDEDRRTYAAMVSALDESVGNV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 267 ITALSSTDQLENSIVIFYSDNGAPSvgMFSNTGSNFPLRGQKNTPWEGGVRVAGAIWSSGLQA-RGSIFRQPLYVADWLP 345
Cdd:cd16029 237 VDALKAKGMLDNTLIVFTSDNGGPT--GGGDGGSNYPLRGGKNTLWEGGVRVPAFVWSPLLPPkRGTVSDGLMHVTDWLP 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386771363 346 TLSRAADIELDSSLKLDGIDLWPELSGSADAPHvpREILHILDDVWRL---SALQMGQWKYVNGTT 408
Cdd:cd16029 315 TLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPR--TEILLNIDDITRTtggAAIRVGDWKLIVGKP 378
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
27-404 |
7.86e-105 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 321.80 E-value: 7.86e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTGTQHFV--------- 96
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAApVCSPSRASILTGQYPARLGITDVIpgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 97 ---ISNEEPWALTLNATLMPEIFKEAGYSTNLVGKWHLGfSRPEYTPTRRGFDYHFGYWGAyidyfqrrsKMPVANYSLG 173
Cdd:cd16144 81 tklIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLG-GEGGYGPEDQGFDVNIGGTGN---------GGPPSYYFPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 174 YDFRRNMELEcrDRGVYVTDLLTAEAERLIKDHADKeqPLFLMLSHLAAHTaneddPLQAPEEEIQKFSYIKDPNRRK-- 251
Cdd:cd16144 151 GKPNPDLEDG--PEGEYLTDRLTDEAIDFIEQNKDK--PFFLYLSHYAVHT-----PIQARPELIEKYEKKKKGLRKGqk 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 252 ---YAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNGAPSVGMFSNTgSNFPLRGQKNTPWEGGVRVAGAIWSSGLQ 328
Cdd:cd16144 222 npvYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPT-SNAPLRGGKGSLYEGGIRVPLIVRWPGVI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 329 ARGSIFRQPLYVADWLPTLSRAADIELDSSLKLDGIDLWPELSGSADAPHvPREIL----HILDDVWRL-SALQMGQWKY 403
Cdd:cd16144 301 KPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLP-RRALFwhfpHYHGQGGRPaSAIRKGDWKL 379
|
.
gi 386771363 404 V 404
Cdd:cd16144 380 I 380
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
26-426 |
6.76e-99 |
|
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: 305.64 E-value: 6.76e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 26 RPNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTGTQHFVISNEEPWA 104
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAApVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 105 LTLNATLMPEIFKEAGYSTNLVGKWHLGFsRPEYTPTRRGFDYHFGywgayIDYFQRRSKMPVANYSLGYDFRRNMELEC 184
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGH-QPEFLPTRHGFDEYFG-----IPYSNDMWPFPLYRNDPPGPLPPLMENEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 185 RDRGV----YVTDLLTAEAERLIKDHADkeQPLFLMLSHLAAHTaneddPLQAPEeeiqKFsyiKDPNRR-KYAAMISKL 259
Cdd:cd16026 155 VIEQPadqsSLTQRYTDEAVDFIERNKD--QPFFLYLAHTMPHV-----PLFASE----KF---KGRSGAgLYGDVVEEL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 260 DQSVGRIITALSSTDQLENSIVIFYSDNGaPSVGMFSNTGSNFPLRGQKNTPWEGGVRVAGAIWSSGLQARGSIFRQPLY 339
Cdd:cd16026 221 DWSVGRILDALKELGLEENTLVIFTSDNG-PWLEYGGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELAS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 340 VADWLPTLSRAADIELDSSLKLDGIDLWPELSGSADAPHvpREILHILDDvWRLSALQMGQWKYV------NGTTASGRY 413
Cdd:cd16026 300 TMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPP--HPFFYYYDG-GDLQAVRSGRWKLHlpttyrTGTDPGGLD 376
|
410
....*....|...
gi 386771363 414 DSVLTYRELDDLD 426
Cdd:cd16026 377 PTKLEPPLLYDLE 389
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
27-414 |
1.09e-94 |
|
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: 295.23 E-value: 1.09e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPAMCTPSRGALLSGRYPIHTGTQHFVISNEEpwaLT 106
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTGVWHTILGRER---MR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 107 LNATLMPEIFKEAGYSTNLVGKWHLGFSRPeYTPTRRGFD---YHFGY-WGAYIDYFQRRSKMPVanyslgydFRRNMEL 182
Cdd:cd16146 78 LDETTLAEVFKDAGYRTGIFGKWHLGDNYP-YRPQDRGFDevlGHGGGgIGQYPDYWGNDYFDDT--------YYHNGKF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 183 EcRDRGvYVTDLLTAEAERLIKDHadKEQPLFLMLSHLAAHTaneddPLQAPEEEIQKFSYIK-DPNRRKYAAMISKLDQ 261
Cdd:cd16146 149 V-KTEG-YCTDVFFDEAIDFIEEN--KDKPFFAYLATNAPHG-----PLQVPDKYLDPYKDMGlDDKLAAFYGMIENIDD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 262 SVGRIITALSSTDQLENSIVIFYSDNGaPSVGmfSNTGSNFPLRGQKNTPWEGGVRVAGAI-WSSGLQARGSIFrQPLYV 340
Cdd:cd16146 220 NVGRLLAKLKELGLEENTIVIFMSDNG-PAGG--VPKRFNAGMRGKKGSVYEGGHRVPFFIrWPGKILAGKDVD-TLTAH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 341 ADWLPTLSRAADIELDSSLKLDGIDLWPELSGSADAPHVPREILHI-----LDDVWRLSALQMGQWKYVNGTTASGR-YD 414
Cdd:cd16146 296 IDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLFTHSgrwppPPKKKRNAAVRTGRWRLVSPKGFQPElYD 375
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
16-524 |
3.06e-92 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 288.32 E-value: 3.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 16 VKSDESAAARRPNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAP-AMCTPSRGALLSGRYPIHTGTQH 94
Cdd:COG3119 13 AAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTsPVCSPSRASLLTGRYPHRTGVTD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 95 fvISNEEPWALTLNATLMPEIFKEAGYSTNLVGKWHLgfsrpeytptrrgfdyhfgywgayidyfqrrskmpvanyslgy 174
Cdd:COG3119 93 --NGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 175 dfrrnmelecrdrgvYVTDLLTAEAERLIKDHADKEQPLFLMLSHLAAHtanedDPLQAPEEEIQKF---------SYIK 245
Cdd:COG3119 128 ---------------YLTDLLTDKAIDFLERQADKDKPFFLYLAFNAPH-----APYQAPEEYLDKYdgkdiplppNLAP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 246 DPN--------RRKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNGapsvGMFSNTGsnfpLRGQKNTPWEGGVR 317
Cdd:COG3119 188 RDLteeelrraRAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNG----PSLGEHG----LRGGKGTLYEGGIR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 318 VAGAIWSSGLQARGSIFRQPLYVADWLPTLSRAADIELDSslKLDGIDLWPELSGsaDAPHVPREILHILDDVWRLSALQ 397
Cdd:COG3119 260 VPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPE--DLDGRSLLPLLTG--EKAEWRDYLYWEYPRGGGNRAIR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 398 MGQWKYVngttasgRYDSVLTYRElddldprdsryavtvrnsatsralsrydlrrltqqrisltrrlaavrcgdlqrscn 477
Cdd:COG3119 336 TGRWKLI-------RYYDDDGPWE-------------------------------------------------------- 352
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 386771363 478 plleecLYDILSDPCEQNNLvySERHSDVLTALRRRVQELRASASRP 524
Cdd:COG3119 353 ------LYDLKNDPGETNNL--AADYPEVVAELRALLEAWLKELGDP 391
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
27-404 |
8.06e-84 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 267.15 E-value: 8.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPAM-CTPSRGALLSGRypiHTGtqH-FVISNEEP-- 102
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPvCAPSRASLLTGL---HTG--HtRVRGNSEPgg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 103 -WALTLNATLMPEIFKEAGYSTNLVGKWHLGFSRPEYTPTRRGFDYHFGYW------GAYIDYFQRRS-KMPVANYSLGY 174
Cdd:cd16145 76 qDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHPTKQGFDYFYGYLdqvhahNYYPEYLWRNGeKVPLPNNVIPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 175 DFRRNMELEcrDRGVYVTDLLTAEAERLIKDHADKeqPLFLMLSHLAAHTANE---DDPLQAPEEEIQKFSYIKDPN-RR 250
Cdd:cd16145 156 LDEGNNAGG--GGGTYSHDLFTDEALDFIRENKDK--PFFLYLAYTLPHAPLQvpdDGPYKYKPKDPGIYAYLPWPQpEK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 251 KYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNGAPSVGMFSNTGSNF----PLRGQKNTPWEGGVRVAGAIWSSG 326
Cdd:cd16145 232 AYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSEGGSEHDPDFFdsngPLRGYKRSLYEGGIRVPFIARWPG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 327 LQARGSIFRQPLYVADWLPTLSRAADIELDSslKLDGIDLWPELSGSADAPhvPREILhilddVWRLS------ALQMGQ 400
Cdd:cd16145 312 KIPAGSVSDHPSAFWDFMPTLADLAGAEPPE--DIDGISLLPTLLGKPQQQ--QHDYL-----YWEFYegggaqAVRMGG 382
|
....
gi 386771363 401 WKYV 404
Cdd:cd16145 383 WKAV 386
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
26-402 |
2.79e-74 |
|
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: 241.96 E-value: 2.79e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 26 RPNIIIIMADDMGFDDVSFRGGrEFLTPNIDALAYHGRLLDRLYAPAMCTPSRGALLSGRYPIHTGTQHFV-ISNEEPW- 103
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGG-EIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTMAeLATGKPGy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 104 --ALTLNATLMPEIFKEAGYSTNLVGKWHLGFSrpeytptrrgfDYHFgywgayidyfqrrskmpvanyslgydfrrnme 181
Cdd:cd16025 81 egYLPDSAATIAEVLKDAGYHTYMSGKWHLGPD-----------DYYS-------------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 182 lecrdrgvyvTDLLTAEAERLIKDHADKEQPLFLMLSHLAAHtanedDPLQAPEEEIQKF-------------------- 241
Cdd:cd16025 118 ----------TDDLTDKAIEYIDEQKAPDKPFFLYLAFGAPH-----APLQAPKEWIDKYkgkydagwdalreerlerqk 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 242 ---------------SYIK-----DPNRRK--------YAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNGA-PSV 292
Cdd:cd16025 183 elglipadtkltprpPGVPawdslSPEEKKlearrmevYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGAsAEP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 293 G--MFSNTgsnfPLRGQKNTPWEGGVRVAGAI-WSSGLQARGSIFRQPLYVADWLPTLSRAADIELDSSLK------LDG 363
Cdd:cd16025 263 GwaNASNT----PFRLYKQASHEGGIRTPLIVsWPKGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDG 338
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 386771363 364 IDLWPELSGsADAPHVPREIlhilddVWRLS---ALQMGQWK 402
Cdd:cd16025 339 VSLLPTLDG-AAAPSRRRTQ------YFELFgnrAIRKGGWK 373
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
27-435 |
1.58e-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: 233.58 E-value: 1.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFL---TPNIDALAYHGRLLDRLYAPAMCTPSRGALLSGRYPIHTGTQHFVI----SN 99
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGLTTVGLpgspGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 100 EEPWALTLnatlmPEIFKEAGYSTNLVGKWHLGfSRPEYTPTRRGFDYHFGYWGAYID-YFQRRSKmpvanyslgyDFrr 178
Cdd:cd16142 81 LPPWEPTL-----AELLKDAGYATAQFGKWHLG-DEDGRLPTDHGFDEFYGNLYHTIDeEIVDKAI----------DF-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 179 nmelecrdrgvyvtdlltaeaerlIKDHADKEQPLFLMLSHLAAHTANeddpLQAPEeeiqkFSYiKDPNRRKYAAMISK 258
Cdd:cd16142 143 ------------------------IKRNAKADKPFFLYVNFTKMHFPT----LPSPE-----FEG-KSSGKGKYADSMVE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 259 LDQSVGRIITALSSTDQLENSIVIFYSDNGApsvGMFSNTGSNF-PLRGQKNTPWEGGVRVAGAIWSSGLQARGSIFRQP 337
Cdd:cd16142 189 LDDHVGQILDALDELGIADNTIVIFTTDNGP---EQDVWPDGGYtPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 338 LYVADWLPTLSRAADIELDSSLK------LDGIDLWPELSGsaDAPHVPREILHILDDVwRLSALQMGQWKYV------N 405
Cdd:cd16142 266 VSHLDWFPTLAALAGAPDPKDKLlgkdrhIDGVDQSPFLLG--KSEKSRRSEFFYFGEG-ELGAVRWKNWKVHfkaqedT 342
|
410 420 430
....*....|....*....|....*....|..
gi 386771363 406 GTTASGRYDsVLTYRELDDL--DPRDsRYAVT 435
Cdd:cd16142 343 GGPTGEPFY-VLTFPLIFNLrrDPKE-RYDVT 372
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
27-427 |
4.27e-69 |
|
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: 227.85 E-value: 4.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVS-FRGGREFLTPNIDALAYHG-RLLDRlYAP-AMCTPSRGALLSGRYPIHTGTQHFVISNEEPW 103
Cdd:cd16143 1 PNIVIILADDLGYGDIScYNPDSKIPTPNIDRLAAEGmRFTDA-HSPsSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 104 ALTLNATLMPEIFKEAGYSTNLVGKWHLGFsrpeyTPTRRGFDYHFGYWGAYIDYFQRRSKMPVAN---YSLGydfrrnm 180
Cdd:cd16143 80 LIEPDRVTLAKMLKQAGYRTAMVGKWHLGL-----DWKKKDGKKAATGTGKDVDYSKPIKGGPLDHgfdYYFG------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 181 elecrDRGVYVTDLLTAEAERLIKDHADKEQPLFLMLSHLAAHTaneddPLqAPEEEIQKFSyikDPNrrKYAAMISKLD 260
Cdd:cd16143 148 -----IPASEVLPTLTDKAVEFIDQHAKKDKPFFLYFALPAPHT-----PI-VPSPEFQGKS---GAG--PYGDFVYELD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 261 QSVGRIITALSSTDQLENSIVIFYSDNGA---PSVGMFSNTG--SNFPLRGQKNTPWEGGVRVAGAIWSSGLQARGSIFR 335
Cdd:cd16143 212 WVVGRILDALKELGLAENTLVIFTSDNGPspyADYKELEKFGhdPSGPLRGMKADIYEGGHRVPFIVRWPGKIPAGSVSD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 336 QPLYVADWLPTLSRAADIELDSSLKLDGIDLWPELSGSADAPHVPREILHILDDVwrlSALQMGQWKYVNGT------TA 409
Cdd:cd16143 292 QLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGS---FAIRKGDWKLIDGTgsggfsYP 368
|
410 420
....*....|....*....|
gi 386771363 410 SGRYDSVLTYRELDDL--DP 427
Cdd:cd16143 369 RGKEKLGLPPGQLYNLstDP 388
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
27-365 |
1.47e-67 |
|
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: 218.46 E-value: 1.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTGTQHFVISNEEPWal 105
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASpVCSPSRASLLTGRYPHRHGVRGNVGNGGGLP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 106 tLNATLMPEIFKEAGYSTNLVGKWHlgfsrpeytptrrgfdyhfgywgayidyfqrrskmpvanyslgydfrrnmelecr 185
Cdd:cd16022 79 -PDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 186 drgvyvtdlltAEAERLIKDHaDKEQPLFLMLSHLAAHTaneddPLqapeeeiqkfsyikdpnrrKYAAMISKLDQSVGR 265
Cdd:cd16022 103 -----------DEAIDFIERR-DKDKPFFLYVSFNAPHP-----PF-------------------AYYAMVSAIDDQIGR 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 266 IITALSSTDQLENSIVIFYSDNGapsvGMFSNTGsnfpLRGQKNTPWEGGVRVAGAIWSSGLQARGSIFRQPLYVADWLP 345
Cdd:cd16022 147 ILDALEELGLLDNTLIVFTSDHG----DMLGDHG----LRGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLP 218
|
330 340
....*....|....*....|
gi 386771363 346 TLSRAADIELDSslKLDGID 365
Cdd:cd16022 219 TLLDLAGIEPPE--GLDGRS 236
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-406 |
4.35e-63 |
|
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: 211.69 E-value: 4.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPAMCTPSRGALLSGRYPIHTGTQHFVISNEEP-WAl 105
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQKtFG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 106 tlnatlmpEIFKEAGYSTNLVGKWHLG-FSRPEYTPTRRGFDYHFGYWGAyidyfqrRSKMPVANYSLGYDFRRNMELEC 184
Cdd:cd16151 80 --------HLLKDAGYATAIAGKWQLGgGRGDGDYPHEFGFDEYCLWQLT-------ETGEKYSRPATPTFNIRNGKLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 185 RDRGVYVTDLLTAEAERLIKDHadKEQPLFLMLSHLAAHTANEDDPlqaPEEEIQKFSYIKDPNRRKYAAMISKLDQSVG 264
Cdd:cd16151 145 TTEGDYGPDLFADFLIDFIERN--KDQPFFAYYPMVLVHDPFVPTP---DSPDWDPDDKRKKDDPEYFPDMVAYMDKLVG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 265 RIITALSSTDQLENSIVIFYSDNGAPSVgMFSNTGSNfPLRGQKNTPWEGGVRV-AGAIWSSGLQARGSIfRQPLYVADW 343
Cdd:cd16151 220 KLVDKLEELGLRENTIIIFTGDNGTHRP-ITSRTNGR-EVRGGKGKTTDAGTHVpLIVNWPGLIPAGGVS-DDLVDFSDF 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386771363 344 LPTLSRAADIELDSSLKLDGIDLWPELSGSADAPHvpREILHI----LDDVWRLSALQMGQWK-YVNG 406
Cdd:cd16151 297 LPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPR--REWIYWyyrnPHKKFGSRFVRTKRYKlYADG 362
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
26-404 |
4.21e-61 |
|
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: 207.04 E-value: 4.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 26 RPNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAP-AMCTPSRGALLSGRYPIHTGtqhfVISNEEPwa 104
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNyPVCSPYRASLLTGQYPLTNG----VFGNDVP-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 105 LTLNATLMPEIFKEAGYSTNLVGKWHLGFSRPEY--------TPTRR-GFDYHFGYwGAYIDYFQrrskmpvanyslGYD 175
Cdd:cd16034 75 LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDgraddytpPPERRhGFDYWKGY-ECNHDHNN------------PHY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 176 FRRNMELECRDRgvYVTDLLTAEAERLIKDHADKEQPLFLMLSHLAAHTANEddplQAPEEEIQKFSYIKDPNR------ 249
Cdd:cd16034 142 YDDDGKRIYIKG--YSPDAETDLAIEYLENQADKDKPFALVLSWNPPHDPYT----TAPEEYLDMYDPKKLLLRpnvped 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 250 -----------RKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNGApsvgMFsntGSNfplrGQ--KNTPWEGGV 316
Cdd:cd16034 216 kkeeaglredlRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGD----ML---GSH----GLmnKQVPYEESI 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 317 RVAGAIWSSGLQARGSIFRQPLYVADWLPTLSRAADIELDSSlkLDGIDLWPELSGSADAPHVPREILHIL--------- 387
Cdd:cd16034 285 RVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLLQCFVpfgggsard 362
|
410
....*....|....*..
gi 386771363 388 DDVWRlsALQMGQWKYV 404
Cdd:cd16034 363 GGEWR--GVRTDRYTYV 377
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
26-410 |
5.17e-58 |
|
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: 198.46 E-value: 5.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 26 RPNIIIIMADDMGFDDVSFRGG-REFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTGTQHfVISNEEPW 103
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAAsVCSPSRASLMTGRLGLRNGVGH-NFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 104 ALTLNATLMPEIFKEAGYSTNLVGKWHLGfSRPEYTPTRRGFDYHFGywgayidyfqrrskMPvanyslgydFRRNMELe 183
Cdd:cd16161 80 GLPLNETTLAEVLRQAGYATGMIGKWHLG-QREAYLPNSRGFDYYFG--------------IP---------FSHDSSL- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 184 crdrgvyvTDLLTAEAERLIKDHADKEQPLFLMLSHLAAHTANEDDPLQAPEEEIqkfsyikdpnRRKYAAMISKLDQSV 263
Cdd:cd16161 135 --------ADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSG----------RGPYGDALQEMDDLV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 264 GRIITALSSTDQLENSIVIFYSDNGAPSV----GMFSNTG---SNFPLRGQKNTPWEGGVRVAGAIWSSGLQARGSIFRQ 336
Cdd:cd16161 197 GQIMDAVKHAGLKDNTLTWFTSDNGPWEVkcelAVGPGTGdwqGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 337 PLYVADWLPTLSRAADIELDSSLKLDGIDLWPELSGSADAPHvpREILHILDDVW---RLSALQMGQWK---YVNGTTAS 410
Cdd:cd16161 277 LVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGH--RCLFHPNSGAAgagALSAVRCGDYKahyATGGALAC 354
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
27-516 |
2.60e-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: 196.19 E-value: 2.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFrGGREFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTGTQHFVISNeepWAL 105
Cdd:cd16027 1 PNILWIIADDLSPDLGGY-GGNVVKTPNLDRLAAEGVRFTNAFTTApVCSPSRSALLTGLYPHQNGAHGLRSRG---FPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 106 TLNATLMPEIFKEAGYSTNLVGKWHLGFSRPEYTPTRRGFDYHFGYWGAYidyfqrrskmpvaNYSLGYDFRrnmelecr 185
Cdd:cd16027 77 PDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAWD-------------YASNAADFL-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 186 drgvyvtdlltaeaerlikDHADKEQPLFLMLSHLAAH---TANEDDPLQAPEEEIQKFSYIKD--PNRR---KYAAMIS 257
Cdd:cd16027 136 -------------------NRAKKGQPFFLWFGFHDPHrpyPPGDGEEPGYDPEKVKVPPYLPDtpEVREdlaDYYDEIE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 258 KLDQSVGRIITALSSTDQLENSIVIFYSDNGAPsvgmfsntgsnFPlRGqKNTPWEGGVRVAGAIWSSGLQARGSIFRQP 337
Cdd:cd16027 197 RLDQQVGEILDELEEDGLLDNTIVIFTSDHGMP-----------FP-RA-KGTLYDSGLRVPLIVRWPGKIKPGSVSDAL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 338 LYVADWLPTLSRAADIELDSSlkLDGIDLWPELSGSADAPHvpreilhilddvwrlsalqmgqwkyvngttasgryDSVL 417
Cdd:cd16027 264 VSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGR-----------------------------------DYVF 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 418 TYRELDDldprdsryavtvrnsatsralSRYDLRRltqqrisltrrlaAVRCGD--LQRscNPLLEEcLYDILSDPCEQN 495
Cdd:cd16027 307 AERDRHD---------------------ETYDPIR-------------SVRTGRykYIR--NYMPEE-LYDLKNDPDELN 349
|
490 500
....*....|....*....|.
gi 386771363 496 NLVYSERHSDVLTALRRRVQE 516
Cdd:cd16027 350 NLADDPEYAEVLEELRAALDA 370
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
27-353 |
5.12e-57 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 193.02 E-value: 5.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTGTQHFVisneePWAL 105
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGtLTAPSRFALLTGLPPHNFGSYVST-----PVGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 106 TLNATLMPEIFKEAGYSTNLVGKWHLGFsRPEYTPTRRGFDyHFGYWGAYIDYFQRRSKMPVaNYSLGYDFrrnmelecr 185
Cdd:pfam00884 76 PRTEPSLPDLLKRAGYNTGAIGKWHLGW-YNNQSPCNLGFD-KFFGRNTGSDLYADPPDVPY-NCSGGGVS--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 186 drgvyvTDLLTAEAERLIKDHadkEQPLFLMLSHLAAHTANE-DDPLQAPEEEIQKFSYIKDPNRRKYAAMISKLDQSVG 264
Cdd:pfam00884 144 ------DEALLDEALEFLDNN---DKPFFLVLHTLGSHGPPYyPDRYPEKYATFKPSSCSEEQLLNSYDNTLLYTDDAIG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 265 RIITALSSTDQLENSIVIFYSDNGaPSVGmfsntGSNFPLRGQK-NTPWEGGVRVAGAIWSSGLQARGSIFRQPLYVADW 343
Cdd:pfam00884 215 RVLDKLEENGLLDNTLVVYTSDHG-ESLG-----EGGGYLHGGKyDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDL 288
|
330
....*....|
gi 386771363 344 LPTLSRAADI 353
Cdd:pfam00884 289 FPTILDLAGI 298
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
26-370 |
7.66e-56 |
|
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: 194.99 E-value: 7.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 26 RPNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTG------------- 91
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANpLCSPSRAALLTGRLPIRNGfyttnaharnayt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 92 TQHFV--ISNEEpwaltlnaTLMPEIFKEAGYSTNLVGKWHLGfSRPEYTPTRRGFDYHFG----YWGAYIDyfQRRSKM 165
Cdd:cd16157 81 PQNIVggIPDSE--------ILLPELLKKAGYRNKIVGKWHLG-HRPQYHPLKHGFDEWFGapncHFGPYDN--KAYPNI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 166 PV-ANYSLGYDFRRNMELECRDRGVYVTDLLTAEAERLIKDHADKEQPLFLMLSHLAAHTaneddPLQAPEeeiqkfSYI 244
Cdd:cd16157 150 PVyRDWEMIGRYYEEFKIDKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHA-----PVYASK------PFL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 245 KDPNRRKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNGAPSVGMFSNTGSNFPLRGQKNTPWEGGVRVAGAIWS 324
Cdd:cd16157 219 GTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALISAPEQGGSNGPFLCGKQTTFEGGMREPAIAWW 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 386771363 325 SGLQARGSIFRQPLYVADWLPTLSRAADIELDSSLKLDGIDLWPEL 370
Cdd:cd16157 299 PGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVL 344
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
25-517 |
4.30e-55 |
|
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: 191.97 E-value: 4.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 25 RRPNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAP-AMCTPSRGALLSGRYPIHTGTQHFVISNEEPW 103
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTtSICAPSRASILTGQYSHRHGVTDNNGPLFDAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 104 ALTLnatlmPEIFKEAGYSTNLVGKWHLGFSrpEYTPtRRGFDYHFGY--WGAYIDyfqrrskmPVANYSLGYDFRRnme 181
Cdd:cd16031 81 QPTY-----PKLLRKAGYQTAFIGKWHLGSG--GDLP-PPGFDYWVSFpgQGSYYD--------PEFIENGKRVGQK--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 182 lecrdrgVYVTDLLTAEAERLIKdHADKEQPLFLMLSHLAAH----------------------TANEDDPLQAPE---- 235
Cdd:cd16031 142 -------GYVTDIITDKALDFLK-ERDKDKPFCLSLSFKAPHrpftpaprhrglyedvtipepeTFDDDDYAGRPEware 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 236 -------EEIQKFSYIKDPNR--RKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNGApsvgMFSNTGsnfplRG 306
Cdd:cd16031 214 qrnrirgVLDGRFDTPEKYQRymKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGF----FLGEHG-----LF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 307 QKNTPWEGGVRVAGAIWSSGLQARGSIFRQPLYVADWLPTLSRAADIELDSSlkLDGIDLWPELSGsaDAPHVPREIL-- 384
Cdd:cd16031 285 DKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEG--EKPVDWRKEFyy 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 385 -----HILDDVWRLSALQMGQWKYVngttasgRYdsvltYRELDdldprdsryavtvrnsatsralsrydlrrltqqris 459
Cdd:cd16031 361 eyyeePNFHNVPTHEGVRTERYKYI-------YY-----YGVWD------------------------------------ 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 386771363 460 ltrrlaavrcgdlqrscnpllEECLYDILSDPCEQNNLVYSERHSDVLTALRRRVQEL 517
Cdd:cd16031 393 ---------------------EEELYDLKKDPLELNNLANDPEYAEVLKELRKRLEEL 429
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
26-402 |
4.54e-53 |
|
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: 186.87 E-value: 4.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 26 RPNIIIIMADDMGFDDVSFRG--GREFlTPnIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTG----TQHFVis 98
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGhpTQER-GP-IDDMAAEGIRFTQAYSADsVCTPSRAALLTGRLPIRSGmyggTRVFL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 99 neePW---ALTLNATLMPEIFKEAGYSTNLVGKWHLGFSrpEYT-------PTRRGFDY--HF---------GYWGAYID 157
Cdd:cd16160 77 ---PWdigGLPKTEVTMAEALKEAGYTTGMVGKWHLGIN--ENNhsdgahlPSHHGFDFvgTNlpftnswacDDTGRHVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 158 YfqrrskmpvANYSLGYDFRRNMELECRDRGVYVTDLLTAEAERLIKDHADKeqPLFLMLSHLAAHTaneddPLQAPEEe 237
Cdd:cd16160 152 F---------PDRSACFLYYNDTIVEQPIQHEHLTETLVGDAKSFIEDNQEN--PFFLYFSFPQTHT-----PLFASKR- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 238 iqkfsyIKDPNRR-KYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNGaPSVGMFSNTGSNFPLRGQKNTPWEGGV 316
Cdd:cd16160 215 ------FKGKSKRgRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHG-PHVEYCLEGGSTGGLKGGKGNSWEGGI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 317 RV-AGAIWSSGLQARGSifRQPLYVADWLPTLSRAADIELDSSLKLDGIDLWPELSGSADAPHvpREILHILDDvwRLSA 395
Cdd:cd16160 288 RVpFIAYWPGTIKPRVS--HEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPH--DDILYYCCS--RLMA 361
|
....*..
gi 386771363 396 LQMGQWK 402
Cdd:cd16160 362 VRYGSYK 368
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
26-378 |
5.67e-49 |
|
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: 177.48 E-value: 5.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 26 RPNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHG-RLLDRLYAPAMCTPSRGALLSGRYPIHTGTQHFVISNEEPWA 104
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGvKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 105 -----LTLNATLMPEIFKEAGYSTNLVGKWHLGFSRPE-----YTPTRRGFDYHFG----------------YWGAYIDY 158
Cdd:cd16159 81 assggLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESrndfcHHPLNHGFDYFYGlpltnlkdcgdgsngeYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 159 FQRRSKM--------------------------------PVANYSLGYDFR-------RN-------MELEcrdrgvYVT 192
Cdd:cd16159 161 FPLLTAFvlitaltiflllylgavskrffvfllilsllfISLFFLLLITNRyfncilmRNhevveqpMSLE------NLT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 193 DLLTAEAERLIKDHadKEQPLFLMLSHLAAHTAneddplqapeeeiqKFSYIKDPNRRK---YAAMISKLDQSVGRIITA 269
Cdd:cd16159 235 QRLTKEAISFLERN--KERPFLLVMSFLHVHTA--------------LFTSKKFKGRSKhgrYGDNVEEMDWSVGQILDA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 270 LsstDQLE---NSIVIFYSDNGAP----SVGMFSNTGSNFPLRGQKNTPWEGGVRVAGAI-WSSGLQArGSIFRQPLYVA 341
Cdd:cd16159 299 L---DELGlkdNTFVYFTSDNGGHleeiSVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVrWPGVIPP-GSVIDEPTSLM 374
|
410 420 430
....*....|....*....|....*....|....*...
gi 386771363 342 DWLPTLSRAADIELDSSLKLDGIDLWPELSG-SADAPH 378
Cdd:cd16159 375 DIFPTVAALAGAPLPSDRIIDGRDLMPLLTGqEKRSPH 412
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
27-411 |
4.13e-45 |
|
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: 166.08 E-value: 4.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTGTQHFVISNEEPWAL 105
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSpVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 106 TLNATLMPEIFKEAGYSTNLVGKWHLGFS-RPEYTPTRRGFDYHFGywgayIDYFQrrSKMPVANYSL------GYDFRR 178
Cdd:cd16158 82 PLNETTIAEVLKTVGYQTAMVGKWHLGVGlNGTYLPTHQGFDHYLG-----IPYSH--DQGPCQNLTCfppnipCFGGCD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 179 NMELEC--------RDRGVYVTDL---LTAEAERLIKDHADKEQPLFLML-SHlaaHTaneddplQAPEEEIQKFSyiKD 246
Cdd:cd16158 155 QGEVPCplfynesiVQQPVDLLTLeerYAKFAKDFIADNAKEGKPFFLYYaSH---HT-------HYPQFAGQKFA--GR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 247 PNRRKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNGaPSVGMFSNTGSNFPLRGQKNTPWEGGVRVAGAIWSSG 326
Cdd:cd16158 223 SSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNG-PSTMRKSRGGNAGLLKCGKGTTYEGGVREPAIAYWPG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 327 LQARGsIFRQPLYVADWLPTLSRAADIELdSSLKLDGIDLWPELSGSADAphvPREILHIL----DDVWRLSALQMGQWK 402
Cdd:cd16158 302 RIKPG-VTHELASTLDILPTIAKLAGAPL-PNVTLDGVDMSPILFEQGKS---PRQTFFYYptspDPDKGVFAVRWGKYK 376
|
410
....*....|..
gi 386771363 403 ---YVNGTTASG 411
Cdd:cd16158 377 ahfYTQGAAHSG 388
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-393 |
9.87e-43 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 156.96 E-value: 9.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 25 RRPNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLY-----APAMCTPSRGALLSGRYPIHtgtqhfvISN 99
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYnmggwSGAVCVPSRAMLMTGRTLFH-------APE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 100 EEPWALTLNATLMPEIFKEAGYSTNLVGKWHLGFsrpeytptrrgfdyhfgywgayidyfqrrskmpvANyslgydfrrn 179
Cdd:cd16155 74 GGKAAIPSDDKTWPETFKKAGYRTFATGKWHNGF----------------------------------AD---------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 180 melecrdrgvyvtdlltaEAERLIKDHADKEQPLFLMLSHLAAHtanedDPLQAPEEEIQK--FSYIKDPN--------- 248
Cdd:cd16155 110 ------------------AAIEFLEEYKDGDKPFFMYVAFTAPH-----DPRQAPPEYLDMypPETIPLPEnflpqhpfd 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 249 ------------------------RRKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNGApSVGmfsNTGsnfpL 304
Cdd:cd16155 167 ngegtvrdeqlapfprtpeavrqhLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGL-AVG---SHG----L 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 305 RGQKNtPWEGGVRV----AGAiwssGLQARGSIfRQPLYVADWLPTLSRAADIELDSSlkLDGIDLWPELSGSADAphvP 380
Cdd:cd16155 239 MGKQN-LYEHSMRVpliiSGP----GIPKGKRR-DALVYLQDVFPTLCELAGIEIPES--VEGKSLLPVIRGEKKA---V 307
|
410 420
....*....|....*....|..
gi 386771363 381 REILH---------ILDDVWRL 393
Cdd:cd16155 308 RDTLYgayrdgqraIRDDRWKL 329
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
26-517 |
4.32e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 146.99 E-value: 4.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 26 RPNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAP-AMCTPSRGALLSGRYPihtgTQHFVISNEEPwa 104
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPqPVCGPARACLQTGLYP----TETGCFRNGIP-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 105 LTLNATLMPEIFKEAGYSTNLVGKWHLGfsrpeytptrrgfdyhfgywgayidyfqrrskmpvanyslgydfrrnmelec 184
Cdd:cd16152 75 LPADEKTLAHYFRDAGYETGYVGKWHLA---------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 185 rdrgVYVTDLLTAEAERLIKDHaDKEQPLFLMLSHLAAHTANEDDPLQAPE---EEIQKFSYIKDPNRRK---------Y 252
Cdd:cd16152 103 ----GYRVDALTDFAIDYLDNR-QKDKPFFLFLSYLEPHHQNDRDRYVAPEgsaERFANFWVPPDLAALPgdwaeelpdY 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 253 AAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNgapsvgmfsntGSNFPLRGQ--KNTPWEGGVRVAGAIWSSGLQaR 330
Cdd:cd16152 178 LGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH-----------GCHFRTRNAeyKRSCHESSIRVPLVIYGPGFN-G 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 331 GSIFRQPLYVADWLPTLSRAADIELDSSlkLDGIDLWPELSGsaDAPHVPREILHILDDVWRLSALQMGQWKY-VNGTTA 409
Cdd:cd16152 246 GGRVEELVSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDG--KVEDWRNEVFIQISESQVGRAIRTDRWKYsVAAPDK 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 410 SGRydsvltyrelddLDPRDSRYAvtvrnsatsralsrydlrrltqqrisltrrlaavrcgdlqrscnpllEECLYDILS 489
Cdd:cd16152 322 DGW------------KDSGSDVYV-----------------------------------------------EDYLYDLEA 342
|
490 500
....*....|....*....|....*...
gi 386771363 490 DPCEQNNLVYSERHSDVLTALRRRVQEL 517
Cdd:cd16152 343 DPYELVNLIGRPEYREVAAELRERLLAR 370
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-407 |
5.31e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 141.97 E-value: 5.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAP-AMCTPSRGALLSGRYPihtgTQHFVISNEE---- 101
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPsPVCCPARASLLTGLYP----HEHGVLNNVEnaga 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 102 -PWALTLNATLMPEIFKEAGYSTNLVGKWHLGfsrPEYTPTRRGFDYHFGYwGAYIDYFqrrskmpvanyslgydfrrnm 180
Cdd:cd16033 77 ySRGLPPGVETFSEDLREAGYRNGYVGKWHVG---PEETPLDYGFDEYLPV-ETTIEYF--------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 181 elecrdrgvyvtdlLTAEAERLIKDHADKEQPLFLMLSHLAAHT--------------------ANEDDPLQA-P----- 234
Cdd:cd16033 132 --------------LADRAIEMLEELAADDKPFFLRVNFWGPHDpyippepyldmydpediplpESFADDFEDkPyiyrr 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 235 ----------EEEIQKfsyikdPNRRKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNG--APSVGMFsNTGSNF 302
Cdd:cd16033 198 erkrwgvdteDEEDWK------EIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGdaLGAHRLW-DKGPFM 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 303 PlrgqkntpwEGGVRVAGAIWSSGLQARGSIFRQPLYVADWLPTLSRAAdiELDSSLKLDGIDLWPELSGSADAPHvPRE 382
Cdd:cd16033 271 Y---------EETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLA--GVDVPPKVDGRSLLPLLRGEQPEDW-RDE 338
|
410 420
....*....|....*....|....*....
gi 386771363 383 ILHILDDVWRLSALQM---GQWKYV-NGT 407
Cdd:cd16033 339 VVTEYNGHEFYLPQRMvrtDRYKYVfNGF 367
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-318 |
9.94e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 140.18 E-value: 9.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVS-FRGGREF-LTPNIDALAYHGRLLDRLYAPAMCTPSRGALLSGRYPIHTGtqhfVISNEEPWA 104
Cdd:cd16154 1 PNILLIIADDQGLDSSAqYSLSSDLpVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTG----VLAVPDELL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 105 LTLNATLMPEIFKE--AGYSTNLVGKWHLGFSrpEYTPTRRG-FDYHFGYWGAYI-DYFQrrskmpvanyslgYDFRRNM 180
Cdd:cd16154 77 LSEETLLQLLIKDAttAGYSSAVIGKWHLGGN--DNSPNNPGgIPYYAGILGGGVqDYYN-------------WNLTNNG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 181 ELEcrDRGVYVTDLLTAEAERLIkdhADKEQPLFLMLSHLAAHTaneddPLQAPEEEIQ------KFSYIKDPNRRKYAA 254
Cdd:cd16154 142 QTT--NSTEYATTKLTNLAIDWI---DQQTKPWFLWLAYNAPHT-----PFHLPPAELHsrsllgDSADIEANPRPYYLA 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386771363 255 MISKLDQSVGRIITALSStDQLENSIVIFYSDNGAPSvgmfSNTGSNFPLRGQKNTPWEGGVRV 318
Cdd:cd16154 212 AIEAMDTEIGRLLASIDE-EERENTIIIFIGDNGTPG----QVVDLPYTRNHAKGSLYEGGINV 270
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-404 |
2.80e-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: 137.67 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTGTqhfvisneepW-- 103
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSpICVPSRASFLTGRYVHETGV----------Wdn 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 104 ALTLNATL--MPEIFKEAGYSTNLVGKWHlgFSRPEYtptRRGFDYhfgywgayidyfqrrskmpvanyslgydfrrnme 181
Cdd:cd16037 71 ADPYDGDVpsWGHALRAAGYETVLIGKLH--FRGEDQ---RHGFRY---------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 182 lecrDRGVyvtdllTAEAERLIKDHADKEQPLFLMLSHLAAHTaneddPLQAPEEEIQKfsYIKDPnRRKYAAMISKLDQ 261
Cdd:cd16037 112 ----DRDV------TEAAVDWLREEAADDKPWFLFVGFVAPHF-----PLIAPQEFYDL--YVRRA-RAAYYGLVEFLDE 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 262 SVGRIITALSSTDQLENSIVIFYSDNGApsvgmfsNTGSnfplRG--QKNTPWEGGVRVAGAIWSSGLQArGSIFRQPLY 339
Cdd:cd16037 174 NIGRVLDALEELGLLDNTLIIYTSDHGD-------MLGE----RGlwGKSTMYEESVRVPMIISGPGIPA-GKRVKTPVS 241
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386771363 340 VADWLPTLSRAADIELDSslKLDGIDLWPELSGSADAphvPREILHILDDVWRLSALQM---GQWKYV 404
Cdd:cd16037 242 LVDLAPTILEAAGAPPPP--DLDGRSLLPLAEGPDDP---DRVVFSEYHAHGSPSGAFMlrkGRWKYI 304
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
22-437 |
9.85e-36 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 139.80 E-value: 9.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 22 AAARRPNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTGTQHFviSNE 100
Cdd:PRK13759 2 VQTKKPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVpSCTPARAALLTGLSQWHHGRVGY--GDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 101 EPWALTlnaTLMPEIFKEAGYSTNLVGKWHLGFSRpeytpTRRGFD-----------------YHFGYWGAYIDYFQRRS 163
Cdd:PRK13759 80 VPWNYK---NTLPQEFRDAGYYTQCIGKMHVFPQR-----NLLGFHnvllhdgylhsgrnedkSQFDFVSDYLAWLREKA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 164 KMPVANYS-LGYD----FRRNMELECRdrgVYVTDLLTAEAERLIKDHaDKEQPLFLMLSHLAAHTANedDP-------- 230
Cdd:PRK13759 152 PGKDPDLTdIGWDcnswVARPWDLEER---LHPTNWVGSESIEFLRRR-DPTKPFFLKMSFARPHSPY--DPpkryfdmy 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 231 --LQAPEEEIQKFSYIKDPN---------------------RRKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDN 287
Cdd:PRK13759 226 kdADIPDPHIGDWEYAEDQDpeggsidalrgnlgeeyarraRAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 288 GApsvgMFsntGSNFPLRgqKNTPWEGGVRVAGAI-WSSGLQA--RGSIFRQPLYVADWLPTLSRAADIELDSSlkLDGI 364
Cdd:PRK13759 306 GD----ML---GDHYLFR--KGYPYEGSAHIPFIIyDPGGLLAgnRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 365 DLWPELSGSADAphvPREILH------ILDDVWrlsaLQMGQWKYV--NGTTASGRYDSVLTYRELDDLDPrDSRYAVTV 436
Cdd:PRK13759 375 SLKNLIFGQYEG---WRPYLHgehalgYSSDNY----LTDGKWKYIwfSQTGEEQLFDLKKDPHELHNLSP-SEKYQPRL 446
|
.
gi 386771363 437 R 437
Cdd:PRK13759 447 R 447
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
26-380 |
2.51e-35 |
|
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: 137.70 E-value: 2.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 26 RPNIIIIMADDMGfDDVSFRGGREFLTPNIDALAYHGRLLDRLYAP-AMCTPSRGALLSGRYPIHTGtqhfVISNEEPWA 104
Cdd:cd16030 2 KPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQqPVCGPSRASLLTGRRPDTTG----VYDNNSYFR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 105 LTL-NATLMPEIFKEAGYSTNLVGK-WHLGFSRPEYTPtrRGFDYHfgYWGAYIDYFQRRSKMPVANYSLGYDFRRNME- 181
Cdd:cd16030 77 KVApDAVTLPQYFKENGYTTAGVGKiFHPGIPDGDDDP--ASWDEP--PNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 182 LECRDrGVYVTDLLTAEAERLIKDHADKEQPLFL-------------------MLSHLAAHTANEDDPLQAPE------E 236
Cdd:cd16030 153 ADVPD-EAYPDGKVADEAIEQLRKLKDSDKPFFLavgfykphlpfvapkkyfdLYPLESIPLPNPFDPIDLPEvawndlD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 237 EIQKFSYIKDPN----------------RRKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNGapsvgmFSNtgs 300
Cdd:cd16030 232 DLPKYGDIPALNpgdpkgplpdeqarelRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHG------WHL--- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 301 nfplrG-----QKNTPWEGGVRVAGAIWSSGLQARGSIFRQP-----LYvadwlPTLSRAADIELDSslKLDGIDLWPEL 370
Cdd:cd16030 303 -----GehghwGKHTLFEEATRVPLIIRAPGVTKPGKVTDALvelvdIY-----PTLAELAGLPAPP--CLEGKSLVPLL 370
|
410
....*....|
gi 386771363 371 SGSADAPHVP 380
Cdd:cd16030 371 KNPSAKWKDA 380
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-368 |
2.88e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 130.75 E-value: 2.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPAM-CTPSRGALLSGRYPIHTGTQHFVISNEEPwal 105
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNpTLPSRFSLFTGLYPFYHGVWGGPLEPDDP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 106 tlnatLMPEIFKEAGYSTNLVGKWHLGFSRPEYtptRRGFDYhfgywgayidyfqrrskmpvanyslgYDFRRNMELECR 185
Cdd:cd16148 78 -----TLAEILRKAGYYTAAVSSNPHLFGGPGF---DRGFDT--------------------------FEDFRGQEGDPG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 186 DRGVYVTDLLTAEAERLIKDHADkEQPLFLMLSHLAAHTaneddPLQapeeeiqkfsyikdpnrrkYAAMISKLDQSVGR 265
Cdd:cd16148 124 EEGDERAERVTDRALEWLDRNAD-DDPFFLFLHYFDPHE-----PYL-------------------YDAEVRYVDEQIGR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 266 IITALSSTDQLENSIVIFYSDNGApsvgMFS----NTGSNFPLrgqkntpWEGGVRVAGAIWSSGLQARGSIfRQPLYVA 341
Cdd:cd16148 179 LLDKLKELGLLEDTLVIVTSDHGE----EFGehglYWGHGSNL-------YDEQLHVPLIIRWPGKEPGKRV-DALVSHI 246
|
330 340
....*....|....*....|....*..
gi 386771363 342 DWLPTLSRAADIELDSSlkLDGIDLWP 368
Cdd:cd16148 247 DIAPTLLDLLGVEPPDY--SDGRSLLP 271
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
27-404 |
1.57e-32 |
|
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: 127.31 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTGTQHfvisneepwal 105
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSpLCAPSRASMMTGRLPSRIGAYD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 106 tlNATLMP-EI------FKEAGYSTNLVGKWHlgFSRPEytptrrgfDYHfgywgayidyfqrrskmpvanyslGYDFrr 178
Cdd:cd16032 70 --NAAEFPaDIptfahyLRAAGYRTALSGKMH--FVGPD--------QLH------------------------GFDY-- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 179 nmelecrDrgvyvtDLLTAEAERLIKDHA--DKEQPLFLMLSHLAAHtanedDPLQAPEEEIQKfsYIKDPnRRKYAAMI 256
Cdd:cd16032 112 -------D------EEVAFKAVQKLYDLArgEDGRPFFLTVSFTHPH-----DPYVIPQEYWDL--YVRRA-RRAYYGMV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 257 SKLDQSVGRIITALSSTDQLENSIVIFYSDNGApsvgMFSNtgsnfplRG--QKNTPWEGGVRVAGAIWSSGLQARGSIf 334
Cdd:cd16032 171 SYVDDKVGQLLDTLERTGLADDTIVIFTSDHGD----MLGE-------RGlwYKMSFFEGSARVPLIISAPGRFAPRRV- 238
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386771363 335 RQPLYVADWLPTLSRAADIEL-DSSLKLDGIDLWPELSGSADAPHvpRE-ILHILDD--VWRLSALQMGQWKYV 404
Cdd:cd16032 239 AEPVSLVDLLPTLVDLAGGGTaPHVPPLDGRSLLPLLEGGDSGGE--DEvISEYLAEgaVAPCVMIRRGRWKFI 310
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
26-318 |
4.14e-32 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 127.67 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 26 RPNIIIIMADDMGFDDVSFrggrEFLTPNIDALAYHGRLLDRLYAP-AMCTPSRGALLSGRYPiHtgtQHFVISNEEP-- 102
Cdd:cd16147 1 RPNIVLILTDDQDVELGSM----DPMPKTKKLLADQGTTFTNAFVTtPLCCPSRASILTGQYA-H---NHGVTNNSPPgg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 103 -----WALTLNATLMPEIFKEAGYSTNLVGKW---HLGFSRPEYTPtrRGFDYHFGYWGAYIDYfqrrskmpvaNYSlgY 174
Cdd:cd16147 73 gypkfWQNGLERSTLPVWLQEAGYRTAYAGKYlngYGVPGGVSYVP--PGWDEWDGLVGNSTYY----------NYT--L 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 175 DFRRNMELECRDRGVYVTDLLTAEAERLIKDHADKEQPLFLMLSHLAAHT----ANEDDPLQAPEEEI-----------Q 239
Cdd:cd16147 139 SNGGNGKHGVSYPGDYLTDVIANKALDFLRRAAADDKPFFLVVAPPAPHGpftpAPRYANLFPNVTAPprpppnnpdvsD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 240 KFSYIK-------------DPNRRKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNGapsvgmFsNTGsNFPLRG 306
Cdd:cd16147 219 KPHWLRrlpplnptqiayiDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNG------Y-HLG-QHRLPP 290
|
330
....*....|..
gi 386771363 307 QKNTPWEGGVRV 318
Cdd:cd16147 291 GKRTPYEEDIRV 302
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
26-366 |
6.43e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 121.71 E-value: 6.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 26 RPNIIIIMADDMGFDDVSFRGG----------REFLTPNIDALAYHGRLLDRLYAPAM-CTPSRGALLSGRYPIHTGtqh 94
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPvCVPSRTSMLTGRYPHRTG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 95 fVISNEEPWALTLNATLM-PEIFKEAGYSTNLVGKWHLgfsrpeytptrrgfdyhfgywGAYIDYFQRrskmpvANYSLG 173
Cdd:cd16153 78 -VYGFEAAHPALDHGLPTfPEVLKKAGYQTASFGKSHL---------------------EAFQRYLKN------ANQSYK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 174 YDFRRNMELecrdrgvyvtdlltaeaerlikdhADKEQPLFLMLSHLAAHTaneddPLQAPEEEIQKFSYikdpnrrkYa 253
Cdd:cd16153 130 SFWGKIAKG------------------------ADSDKPFFVRLSFLQPHT-----PVLPPKEFRDRFDY--------Y- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 254 AMISKLDQSVGRIITAL---SSTDQLENSIVIFYSDNGApsvgmfsNTGSNFPLrgQKNTPWEGGVRVAG-AIWSSGLQA 329
Cdd:cd16153 172 AFCAYGDAQVGRAVEAFkaySLKQDRDYTIVYVTGDHGW-------HLGEQGIL--AKFTFWPQSHRVPLiVVSSDKLKA 242
|
330 340 350
....*....|....*....|....*....|....*....
gi 386771363 330 RGSIFRQPL--YVaDWLPTLSRAADIELDSSLKLDGIDL 366
Cdd:cd16153 243 PAGKVRHDFveFV-DLAPTLLAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-363 |
1.15e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 120.42 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYP----IH---TGTQHFVIS 98
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSpVCSPARASLLTGRMPsqhgIHdwiVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 99 NEEPWALtlNATLMPEIFKEAGYSTNLVGKWHLGfsrpeytptrrgfDYHfgywgayIDYFQRRskmpvanyslgydfrr 178
Cdd:cd16149 81 KPEGYLE--GQTTLPEVLQDAGYRCGLSGKWHLG-------------DDA-------ADFLRRR---------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 179 nmelecrdrgvyvtdlltaeaerlikdhADKEQPLFLMLSHLAAHtanedDPLQapeeeiqkfsyikdpnrrkYAAMISK 258
Cdd:cd16149 123 ----------------------------AEAEKPFFLSVNYTAPH-----SPWG-------------------YFAAVTG 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 259 LDQSVGRIITALSSTDQLENSIVIFYSDNG--APSVGMFSNTGSNFPLrgqkNTpWEGGVRVAGAIWSSGLQARGSIFRQ 336
Cdd:cd16149 151 VDRNVGRLLDELEELGLTENTLVIFTSDNGfnMGHHGIWGKGNGTFPL----NM-YDNSVKVPFIIRWPGVVPAGRVVDS 225
|
330 340
....*....|....*....|....*..
gi 386771363 337 PLYVADWLPTLSRAADIELDSSLKLDG 363
Cdd:cd16149 226 LVSAYDFFPTLLELAGVDPPADPRLPG 252
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-394 |
7.03e-23 |
|
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: 99.20 E-value: 7.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTGtqhfVISNEEPWAL 105
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAAcMCSPSRSTLYTGLHPQQTG----VTDTLGSPMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 106 TLNATLMPEI---FKEAGYSTNLVGKWHLGfsrpeytptrrGFDyhfgyWGAYIdyfqrrskmpvanyslgydfrrnmel 182
Cdd:cd16035 77 PLLSPDVPTLghmLRAAGYYTAYKGKWHLS-----------GAA-----GGGYK-------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 183 ecRDRGVyvtdllTAEAERLIKDHA---DKEQPLFLMLSHLAAHtanedDPLQAPEEEIQkfsYIKDPNRrkYAAMISKL 259
Cdd:cd16035 115 --RDPGI------AAQAVEWLRERGaknADGKPWFLVVSLVNPH-----DIMFPPDDEER---WRRFRNF--YYNLIRDV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 260 DQSVGRIITALSSTDQLENSIVIFYSDNG--APSVGMfsntgsnfplRGQKNTPWEGGVRVAGAIWSSGLQARGSIFRQP 337
Cdd:cd16035 177 DRQIGRVLDALDASGLADNTIVVFTSDHGemGGAHGL----------RGKGFNAYEEALHVPLIISHPDLFGTGQTTDAL 246
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386771363 338 LYVADWLPTLSRAADIELDSSLK----LDGIDLWPELSGsADAPHVPREILHILDDvWRLS 394
Cdd:cd16035 247 TSHIDLLPTLLGLAGVDAEARATeappLPGRDLSPLLTD-ADADAVRDGILFTYDR-YKFA 305
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
27-452 |
1.09e-18 |
|
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: 88.98 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPIHTGtqhfvisneePW-- 103
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQpVCGPARSGLFTGLYPHTNG----------SWtn 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 104 --ALTLNATLMPEIFKEAGYSTNLVGKWHLGfsrpeytptrrGFDYhFG-----------YW---GAYID-------YFQ 160
Cdd:cd16156 71 cmALGDNVKTIGQRLSDNGIHTAYIGKWHLD-----------GGDY-FGngicpqgwdpdYWydmRNYLDelteeerRKS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 161 RRSKMPVANYSLGYDFrrNMELECRDRGVyvtdlltaeaeRLIKDHADKeqPLFLMLSHLAAHtanedDPLQAPEEEIQK 240
Cdd:cd16156 139 RRGLTSLEAEGIKEEF--TYGHRCTNRAL-----------DFIEKHKDE--DFFLVVSYDEPH-----HPFLCPKPYASM 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 241 ---FSYIKDPN------------------------------RRKYAAMISKLDQSVGRIITALssTDQLENSIVIFYSDN 287
Cdd:cd16156 199 ykdFEFPKGENayddlenkplhqrlwagakphedgdkgtikHPLYFGCNSFVDYEIGRVLDAA--DEIAEDAWVIYTSDH 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 288 GaPSVGMFSntgsnfpLRGQKNTPWEGGVRVAGAIWSSGLQARGSIFRQPLYVADWLPTLSRAADIELDSSlkLDGIDLW 367
Cdd:cd16156 277 G-DMLGAHK-------LWAKGPAVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKV--LEGESIL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 368 PELSGSADAPHVP-------REILHildDVWrlSALQM------GQWKYV-NGTTASGRYDSVLTYRELDDLdPRDSRYA 433
Cdd:cd16156 347 ATIEDPEIPENRGvfvefgrYEVDH---DGF--GGFQPvrcvvdGRYKLViNLLSTDELYDLEKDPYEMHNL-IDDPDYA 420
|
490
....*....|....*....
gi 386771363 434 VtVRNSATSRALSRYDLRR 452
Cdd:cd16156 421 D-VRDQLHDELLDYMNETR 438
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-288 |
1.42e-18 |
|
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: 88.06 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLY--APaMCTPSRGALLSGRYPiHTG---TQHFVISNEE 101
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYcqNP-VCSPSRCSFLTGWYP-HVNghrTLHHLLRPDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 102 PwaltlnaTLMpEIFKEAGYSTNLVGKWHLgfsrpeytpTRRGFDyhfgyWGAYIDyfqrrskmpvanyslgydfrrnme 181
Cdd:cd16150 79 P-------NLL-KTLKDAGYHVAWAGKNDD---------LPGEFA-----AEAYCD------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 182 lecrdrgvyvTDLLTAE-AERLIKDHADkEQPLFLMLSHLAAHT---ANED-----DPLQAPEE---------------- 236
Cdd:cd16150 113 ----------SDEACVRtAIDWLRNRRP-DKPFCLYLPLIFPHPpygVEEPwfsmiDREKLPPRrppglrakgkpsmleg 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 386771363 237 -EIQKFSYIKDPN----RRKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNG 288
Cdd:cd16150 182 iEKQGLDRWSEERwrelRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHG 238
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
27-329 |
1.50e-18 |
|
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: 86.20 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPAMCTP-SRG--ALLSGRYPIHTGTQHFVISNEEPw 103
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGtANGefEVLTGLPPLPLGSGSYTLYKLNP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 104 altLNAtlMPEIFKEAGYSTNLvgkwhlgfsrpeytptrrgfdYHfgywGAYIDYFQRRSKMPvanySLGYD---FRRNM 180
Cdd:cd16015 80 ---LPS--LPSILKEQGYETIF---------------------IH----GGDASFYNRDSVYP----NLGFDefyDLEDF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 181 EL-ECRDRGVYVTD-LLTAEAERLIKDHadKEQPLFLMLSHLAAHTANEDDPlqaPEEEIQKFSYIKDPNRRKYAAMISK 258
Cdd:cd16015 126 PDdEKETNGWGVSDeSLFDQALEELEEL--KKKPFFIFLVTMSNHGPYDLPE---EKKDEPLKVEEDKTELENYLNAIHY 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386771363 259 LDQSVGRIITALSSTDQLENSIVIFYSDNGAPSVGMFSNTGSNFPLRgqKNTPWeggvrvagAIWSSGLQA 329
Cdd:cd16015 201 TDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDL--YRTPL--------LIYSPGLKK 261
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
27-404 |
1.75e-18 |
|
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: 88.08 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPAM-CTPSRGALLSGRYPIhtgtQHFVISNEEPwaL 105
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAApCGPSRASLYTGRYLM----NHRSVWNGTP--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 106 TLNATLMPEIFKEAGYSTNLVGKWHlgfsrpeYTPTRRGFD----YHFGYWGAyidyfqrrskMPvanyslGYDFRRNME 181
Cdd:cd16028 75 DARHLTLALELRKAGYDPALFGYTD-------TSPDPRGLApldpRLLSYELA----------MP------GFDPVDRLD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 182 L------ECRdrgvYVTDlltaEAERLIKDHADKeqPLFLMLSHLAAHTaneddPLQAPE-------------------- 235
Cdd:cd16028 132 EypaedsDTA----FLTD----RAIEYLDERQDE--PWFLHLSYIRPHP-----PFVAPApyhalydpadvpppiraesl 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 236 -EEIQK---------------FSYIKDPN-----------RRKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNG 288
Cdd:cd16028 197 aAEAAQhpllaaflerieslsFSPGAANAadlddeevaqmRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 289 apsvgmfSNTGSNFpLRGqKNTPWEGGVRVAGAIWSSGLQA---RGSIFRQPLYVADWLPTLSRAADIELDSSlkLDGID 365
Cdd:cd16028 277 -------EQLGDHW-LWG-KDGFFDQAYRVPLIVRDPRREAdatRGQVVDAFTESVDVMPTILDWLGGEIPHQ--CDGRS 345
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 386771363 366 LWPELSGsaDAPHVPREILHILDDVW------------------RLSALQMGQWKYV 404
Cdd:cd16028 346 LLPLLAG--AQPSDWRDAVHYEYDFRdvstrrpqealglspdecSLAVIRDERWKYV 400
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
27-351 |
2.61e-18 |
|
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: 84.39 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPAMC--TPSRGALLSGRYPIHTGTQHFVISNEEPWA 104
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 105 LTLNATLM----PEIFKEAGYSTNLVGKWhlgfsrpeytptrrgfdyhfgywgAYIDYFQrrskmpvanyslgydfrrnm 180
Cdd:cd00016 81 RAAGKDEDgptiPELLKQAGYRTGVIGLL------------------------KAIDETS-------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 181 elecrdrgvyvtdlltaeaerlikdhadKEQPLFLMLshlaaHTANEDDPLQAPeeeiqkfsyikDPNRRKYAAMISKLD 260
Cdd:cd00016 117 ----------------------------KEKPFVLFL-----HFDGPDGPGHAY-----------GPNTPEYYDAVEEID 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 261 QSVGRIITALSSTDQLENSIVIFYSDNGAPSVGMfsntgSNFPLRGQKNTPWEGGVRVAGAIWSSGLQARGSIfRQPLYV 340
Cdd:cd00016 153 ERIGKVLDALKKAGDADDTVIIVTADHGGIDKGH-----GGDPKADGKADKSHTGMRVPFIAYGPGVKKGGVK-HELISQ 226
|
330
....*....|.
gi 386771363 341 ADWLPTLSRAA 351
Cdd:cd00016 227 YDIAPTLADLL 237
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
14-293 |
1.15e-17 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 86.25 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 14 QRVKSDESAAARRPNIIIIMADDMGFDDVSFRGGREFLTPNIDALAYHGRLLDRLYAPAMCTpSRG--ALLSGRYPihTG 91
Cdd:COG1368 222 NRPTPNPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRT-SRGefAVLTGLPP--LP 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 92 TQHFVISNEEPWALTLnatlmPEIFKEAGYSTNLvgkWHlgfsrpeytptrrGFDYHFgyWGayidyfqRRSKMPvanyS 171
Cdd:COG1368 299 GGSPYKRPGQNNFPSL-----PSILKKQGYETSF---FH-------------GGDGSF--WN-------RDSFYK----N 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 172 LGYD---FRRNMELEcrDRGVY-VTD-LLTAEAERLIKdhaDKEQPLFLMLSHLAAHTaneddPLQAPEEEiQKFSYIKD 246
Cdd:COG1368 345 LGFDefyDREDFDDP--FDGGWgVSDeDLFDKALEELE---KLKKPFFAFLITLSNHG-----PYTLPEED-KKIPDYGK 413
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 386771363 247 PNRRKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNGAPSVG 293
Cdd:COG1368 414 TTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPG 460
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
27-404 |
1.32e-13 |
|
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: 72.57 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 27 PNIIIIMADdmGFDD-VSFRGGREFLT-PNIDALAYHGRLLDRLYAPA-MCTPSRGALLSGRYPihtgtqHFVISNEEPW 103
Cdd:cd16171 1 PNVVMVMSD--SFDGrLTFRPGNQVVDlPYINFMKQHGSVFLNAYTNSpICCPSRAAMWSGLFT------HLTESWNNYK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 104 ALTLNATLMPEIFKEAGYSTNLVGKWhlgfsrpEYTPTRRGFDYHFGYWGAYIDYFQRRSKMPVANYSLGYDFRRNMELE 183
Cdd:cd16171 73 GLDPNYPTWMDRLEKHGYHTQKYGKL-------DYTSGHHSVSNRVEAWTRDVPFLLRQEGRPTVNLVGDRSTVRVMLKD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 184 CRdrgvyVTDLLTAeaeRLIKDHADKEQPLFLMLSHLAAHtaneddPLQAPEEEiQKFSYIKDPnRRKYAAMISKLDQSV 263
Cdd:cd16171 146 WQ-----NTDKAVH---WIRKEAPNLTQPFALYLGLNLPH------PYPSPSMG-ENFGSIRNI-RAFYYAMCAETDAML 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 264 GRIITALSSTDQLENSIVIFYSDNGapSVGMfsnTGSNFplrgQKNTPWEGGVRVAGAIWSSGLQArGSIFRQPLYVADW 343
Cdd:cd16171 210 GEIISALKDTGLLDKTYVFFTSDHG--ELAM---EHRQF----YKMSMYEGSSHVPLLIMGPGIKA-GQQVSDVVSLVDI 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386771363 344 LPTLSRAADIELDSSlkLDGIDLWPELSGSADAPHvPREILHildDVWRLSA------------LQMGQWKYV 404
Cdd:cd16171 280 YPTMLDIAGVPQPQN--LSGYSLLPLLSESSIKES-PSRVPH---PDWVLSEfhgcnvnastymLRTNSWKYI 346
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
18-288 |
1.65e-10 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 62.84 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 18 SDESAAARRPNIIIIMADDMGFDDVsfrggREFLTPNIDALAYHGRLLDRLYA--PAMCTPSRGALLSGRYPIHTGtqhf 95
Cdd:COG1524 15 AAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSvfPSTTAPAHTTLLTGLYPGEHG---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 96 VISNEepWaltlnatlmpeIFKEAGYSTNLVGKWHLGFSRPEY--TPT------RRGFDYHFGYWGAYIDYfqrrskmPV 167
Cdd:COG1524 86 IVGNG--W-----------YDPELGRVVNSLSWVEDGFGSNSLlpVPTiferarAAGLTTAAVFWPSFEGS-------GL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771363 168 ANYSLGYDFRRNMELecrdRGVYVTDLLTAE-AERLIKDHadkeQPLFLM--LSHL--AAHtaneddplqapeeeiqKFS 242
Cdd:COG1524 146 IDAARPYPYDGRKPL----LGNPAADRWIAAaALELLREG----RPDLLLvyLPDLdyAGH----------------RYG 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 386771363 243 yikdPNRRKYAAMISKLDQSVGRIITALSSTDQLENSIVIFYSDNG 288
Cdd:COG1524 202 ----PDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| |
