|
Name |
Accession |
Description |
Interval |
E-value |
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
1-350 |
1.78e-98 |
|
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: 297.54 E-value: 1.78e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 1 MKAIILLFDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHREW-GPLEPFDDSMP 79
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWgGPLEPDDPTLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 80 ELLKKAGIYTHLISDHLHYWedGGGNYHNRYSSWDVVRGQEGDHwkasvgeppipevlrvpqkqtgggvsglwrhdwanr 159
Cdd:cd16148 81 EILRKAGYYTAAVSSNPHLF--GGPGFDRGFDTFEDFRGQEGDP------------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 160 eyiQQEADFPQTKVFDAGCDFIHKNHAEDNWLLQVETFDPHEPFytteeylslyddewqgphydwprgkvseseeaiahi 239
Cdd:cd16148 123 ---GEEGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPHEPY------------------------------------ 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 240 rcRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKNQMPYYNEVANNPLFIWDPRSAVcGARRQ 319
Cdd:cd16148 164 --LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNLYDEQLHVPLIIRWPGKEP-GKRVD 240
|
330 340 350
....*....|....*....|....*....|.
gi 446566675 320 SLVQMIDWAPTLLDYFQQPIPADMQGQPLAK 350
Cdd:cd16148 241 ALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
4-483 |
1.36e-58 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 198.56 E-value: 1.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLFDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHR-------EWGPLEPFDD 76
Cdd:COG3119 27 LFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGvtdngegYNGGLPPDEP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 77 SMPELLKKAGIYTHLIsdhlhywedggGNYHnrysswdvvrgqegdhwkasvgeppipevlrvpqkqtgggvsgLWRHDW 156
Cdd:COG3119 107 TLAELLKEAGYRTALF-----------GKWH-------------------------------------------LYLTDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 157 anreyiqqeadfpqtkVFDAGCDFIHKNHAEDN-WLLQVETFDPHEPFYTTEEYLSLYDD-EWQGPHYDWPRGkvsESEE 234
Cdd:COG3119 133 ----------------LTDKAIDFLERQADKDKpFFLYLAFNAPHAPYQAPEEYLDKYDGkDIPLPPNLAPRD---LTEE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 235 AIAHIRCRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGW-WAKNQMpyYNEVANNPLFIWDPRSAV 313
Cdd:COG3119 194 ELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLrGGKGTL--YEGGIRVPLIVRWPGKIK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 314 CGARRQSLVQMIDWAPTLLDYFQQPIPADMQGQPLAKVIASDEPVREGALFGVFSGHVN---VTDGRYVYMRAAQPGREh 390
Cdd:COG3119 272 AGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTGEKAEWRDYLYWEYPRGGGnraIRTGRWKLIRYYDDDGP- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 391 dianytlmpikmnarydvdelgklslappfnftkglqvlriparekykgvnsfgHLLFDLRDDPQQQHPIHDE--AIEAR 468
Cdd:COG3119 351 ------------------------------------------------------WELYDLKNDPGETNNLAADypEVVAE 376
|
490
....*....|....*
gi 446566675 469 MISLLIRLMKENDAP 483
Cdd:COG3119 377 LRALLEAWLKELGDP 391
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-380 |
3.15e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 157.77 E-value: 3.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLFDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHrewgplepfddsmpellk 83
Cdd:cd16033 4 LFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEH------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 84 kaGIYThlisdhlhywedgggNYHNRYSswdVVRGQEGDHWKAsvgeppiPEVLRVPQKQTGggVSGLWrH--------D 155
Cdd:cd16033 66 --GVLN---------------NVENAGA---YSRGLPPGVETF-------SEDLREAGYRNG--YVGKW-HvgpeetplD 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 156 WANREYIQQEADFPQTKVfDAGCDFIhKNHAEDN--WLLQVETFDPHEPFYTTEEYLSLYDDE-------WQGPHYDWPR 226
Cdd:cd16033 116 YGFDEYLPVETTIEYFLA-DRAIEML-EELAADDkpFFLRVNFWGPHDPYIPPEPYLDMYDPEdiplpesFADDFEDKPY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 227 ---------GKVSESEEAIAHIRCRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKNqMPYYN 297
Cdd:cd16033 194 iyrrerkrwGVDTEDEEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKG-PFMYE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 298 EVANNPLFIWDPRSAVCGARRQSLVQMIDWAPTLLDYFQQPIPADMQGQPLAKVIASDEPV--REGALF---GVFSGHVN 372
Cdd:cd16033 273 ETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPEdwRDEVVTeynGHEFYLPQ 352
|
410
....*....|
gi 446566675 373 --VTDGRYVY 380
Cdd:cd16033 353 rmVRTDRYKY 362
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
5-357 |
1.06e-42 |
|
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: 157.42 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 5 ILL--FDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHRE-WG--PLEPFDDSMP 79
Cdd:cd16028 3 VLFitADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSvWNgtPLDARHLTLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 80 ELLKKAGIYTHLISdhlhywedgggnyhnrYSswDVVRGQEGDHwkasvgePPIPEVLRVPQKQTGggvsglWRHDWANR 159
Cdd:cd16028 83 LELRKAGYDPALFG----------------YT--DTSPDPRGLA-------PLDPRLLSYELAMPG------FDPVDRLD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 160 EYiqQEADFPQTKVFDAGCDFIhKNHAEDNWLLQVETFDPHEPFYTTEEYLSLYD-------------DEWQGPH----- 221
Cdd:cd16028 132 EY--PAEDSDTAFLTDRAIEYL-DERQDEPWFLHLSYIRPHPPFVAPAPYHALYDpadvpppiraeslAAEAAQHpllaa 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 222 ----------YDWPRGKVSESEEAIAHIRCRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKN 291
Cdd:cd16028 209 flerieslsfSPGAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLWGKD 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446566675 292 QmpYYNEVANNPLFIWDPR---SAVCGARRQSLVQMIDWAPTLLDYFQQPIPADMQGQPLAKVIASDEP 357
Cdd:cd16028 289 G--FFDQAYRVPLIVRDPRreaDATRGQVVDAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQP 355
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
19-382 |
5.71e-41 |
|
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: 152.30 E-value: 5.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 19 YGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHREW---GPLEPFDD-SMPELLKKAGIYTHLIsd 94
Cdd:cd16031 21 YGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTdnnGPLFDASQpTYPKLLRKAGYQTAFI-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 95 hlhywedggGNYHNRYSSWDVVRGQegDHWKASVG----EPPIPEVLRVPQKQTGggvsglwrhdWANREYIqqeadfpq 170
Cdd:cd16031 99 ---------GKWHLGSGGDLPPPGF--DYWVSFPGqgsyYDPEFIENGKRVGQKG----------YVTDIIT-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 171 tkvfDAGCDFIHKNHAEDNWLLQVETFDPHEPFYTTEEYLSLYDDE-------WQGPHYDwPRGK-VSESEEAIAH---- 238
Cdd:cd16031 150 ----DKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVtipepetFDDDDYA-GRPEwAREQRNRIRGvldg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 239 -----------IRCRYRALVSMcDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKNQMpyYNEVANNPLFIW 307
Cdd:cd16031 225 rfdtpekyqryMKDYLRTVTGV-DDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLFDKRLM--YEESIRVPLIIR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 308 DPRSAVCGARRQSLVQMIDWAPTLLDYFQQPIPADMQGQPLAKVIASDEPV--REGALFGVFSG--------HVNVTDGR 377
Cdd:cd16031 302 DPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEGEKPVdwRKEFYYEYYEEpnfhnvptHEGVRTER 381
|
....*
gi 446566675 378 YVYMR 382
Cdd:cd16031 382 YKYIY 386
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-381 |
1.22e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 143.07 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLFDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHREW---GPLEPFDDSMPE 80
Cdd:cd16037 4 LIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWdnaDPYDGDVPSWGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 81 LLKKAGIYTHLISdHLHYwedgggnyhnrysswdvvRGQEGDHwkasvgeppipevlrvpqkqtgggvsgLWRHDwanRE 160
Cdd:cd16037 84 ALRAAGYETVLIG-KLHF------------------RGEDQRH---------------------------GFRYD---RD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 161 yiqqeadfpqtkVFDAGCDFIHKN-HAEDNWLLQVETFDPHEPFYTTEEYLSLYddewqgphydwprgkvseseeaiaHI 239
Cdd:cd16037 115 ------------VTEAAVDWLREEaADDKPWFLFVGFVAPHFPLIAPQEFYDLY------------------------VR 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 240 RCR--YRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKNQMpyYNEVANNPLFIWDPRSAVcGAR 317
Cdd:cd16037 159 RARaaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTM--YEESVRVPMIISGPGIPA-GKR 235
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446566675 318 RQSLVQMIDWAPTLLDYFQQPIPADMQGQPLAKVIASDEPVREGAL-----FGVFSGHVNVTDGRYVYM 381
Cdd:cd16037 236 VKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEGPDDPDRVVFseyhaHGSPSGAFMLRKGRWKYI 304
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
4-346 |
4.56e-36 |
|
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: 133.72 E-value: 4.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLF-DSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHR------EWGPLEPFDD 76
Cdd:cd16022 3 ILLIMtDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGvrgnvgNGGGLPPDEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 77 SMPELLKKAGIYTHLIsdhlhywedggGNYHNRysswdvvrgqegdhwkasvgeppipevlrvpqkqtgggvsglwrhdw 156
Cdd:cd16022 83 TLAELLKEAGYRTALI-----------GKWHDE----------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 157 anreyiqqeadfpqtkvfdaGCDFIHKNHAEDNWLLQVETFDPHEPFYtteeylslyddewqgphydwprgkvseseeai 236
Cdd:cd16022 105 --------------------AIDFIERRDKDKPFFLYVSFNAPHPPFA-------------------------------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 237 ahircrYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGW-WAKNQMpyYNEVANNPLFIWDPRSAVCG 315
Cdd:cd16022 133 ------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKKGSL--YEGGIRVPFIVRWPGKIPAG 204
|
330 340 350
....*....|....*....|....*....|.
gi 446566675 316 ARRQSLVQMIDWAPTLLDYFQQPIPADMQGQ 346
Cdd:cd16022 205 QVSDALVSLLDLLPTLLDLAGIEPPEGLDGR 235
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
15-382 |
2.08e-35 |
|
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: 135.71 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 15 YLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNF------LHREWGPLEPFDDSMPELLKKAGIY 88
Cdd:cd16027 14 DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHqngahgLRSRGFPLPDGVKTLPELLREAGYY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 89 THLISDHlHYwedgggNYHNRYSSWDVVRGQEGDHwkasvgeppipevlrvpqkqtgggvsglwRHDWANreyiqqeadf 168
Cdd:cd16027 94 TGLIGKT-HY------NPDAVFPFDDEMRGPDDGG-----------------------------RNAWDY---------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 169 pqtkvFDAGCDFIHKNHAEDNWLLQVETFDPHEPFYTTEEYLSLYDDEWQGPHYDWPrgKVSESEEAIAhircRYRALVS 248
Cdd:cd16027 128 -----ASNAADFLNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPYLP--DTPEVREDLA----DYYDEIE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 249 MCDRNLGRILDLMDEHDLWRDTMLIVGTDHG--FLlgehgwWAKnQMPYYN--EVannPLFIWDPRSAVCGARRQSLVQM 324
Cdd:cd16027 197 RLDQQVGEILDELEEDGLLDNTIVIFTSDHGmpFP------RAK-GTLYDSglRV---PLIVRWPGKIKPGSVSDALVSF 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446566675 325 IDWAPTLLDYFQQPIPADMQGQPLAKVIASDE-PVREgALFGVFSGHVN-------VTDGRYVYMR 382
Cdd:cd16027 267 IDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKdPGRD-YVFAERDRHDEtydpirsVRTGRYKYIR 331
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
5-352 |
8.82e-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: 135.01 E-value: 8.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 5 ILLF--DSLNkNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVgSMP-CMPARRELHTGR-------YNFLHReWGPLEPF 74
Cdd:cd16030 5 VLFIavDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYC-QQPvCGPSRASLLTGRrpdttgvYDNNSY-FRKVAPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 75 DDSMPELLKKAGIYTHLISDHLHYWEDGGGNYHNrysSWDVVRGQEGDHWKASvgeppipevlRVPQKQTGGGVSGLWRH 154
Cdd:cd16030 82 AVTLPQYFKENGYTTAGVGKIFHPGIPDGDDDPA---SWDEPPNPPGPEKYPP----------GKLCPGKKGGKGGGGGP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 155 DWANREyiQQEADFPQTKVFDAGCDFIHKNHAED-NWLLQVETFDPHEPFYTTEEYLSLYD-DEWQGPHYDWPRG----- 227
Cdd:cd16030 149 AWEAAD--VPDEAYPDGKVADEAIEQLRKLKDSDkPFFLAVGFYKPHLPFVAPKKYFDLYPlESIPLPNPFDPIDlpeva 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 228 ---------------------KVSESEEAIAHIRCRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHG 286
Cdd:cd16030 227 wndlddlpkygdipalnpgdpKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHG 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446566675 287 WWAKNQMpyYNEVANNPLFIWDPRSAVCGARRQSLVQMIDWAPTLLDYFQQPIPADMQGQPLAKVI 352
Cdd:cd16030 307 HWGKHTL--FEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLL 370
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
2-487 |
7.28e-32 |
|
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: 127.50 E-value: 7.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 2 KAIILLFDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHREWGPLEPFDD---SM 78
Cdd:cd16156 2 QFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDnvkTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 79 PELLKKAGIYTHLISD-HL-----------------HYWEDGGgNYHN------RYSSWDVVRGQEGDHWKASVgeppip 134
Cdd:cd16156 82 GQRLSDNGIHTAYIGKwHLdggdyfgngicpqgwdpDYWYDMR-NYLDelteeeRRKSRRGLTSLEAEGIKEEF------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 135 evlrvpqkqtgggvsglwrhDWANReyiqqeadfpqtkVFDAGCDFIhKNHAEDNWLLQVETFDPHEPFYTTEEYLSLYD 214
Cdd:cd16156 155 --------------------TYGHR-------------CTNRALDFI-EKHKDEDFFLVVSYDEPHHPFLCPKPYASMYK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 215 D-EW-QGP-HYD-----------WPRGKVSESEEAIAHIRCRYRALVSMCDRNLGRILDLMDEhdLWRDTMLIVGTDHGF 280
Cdd:cd16156 201 DfEFpKGEnAYDdlenkplhqrlWAGAKPHEDGDKGTIKHPLYFGCNSFVDYEIGRVLDAADE--IAEDAWVIYTSDHGD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 281 LLGEHGWWAKNQMpYYNEVANNPLFIWDPRSAVCGARRQSLVQMIDWAPTLLDYFQQPIPADMQGQPLAKVIASDepvre 360
Cdd:cd16156 279 MLGAHKLWAKGPA-VYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIEDP----- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 361 galfgvfsghvNVTDGRYVYMRAaqpgrehdianytlmpikmnARYDVDELGklslappFNftkGLQVLRIPAREKYKGV 440
Cdd:cd16156 353 -----------EIPENRGVFVEF--------------------GRYEVDHDG-------FG---GFQPVRCVVDGRYKLV 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446566675 441 -NSFGH-LLFDLRDDPQQQHP-IHDE---AIEARMISLLIRLMKENDAPAEQY 487
Cdd:cd16156 392 iNLLSTdELYDLEKDPYEMHNlIDDPdyaDVRDQLHDELLDYMNETRDPFRGY 444
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-382 |
4.55e-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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 121.14 E-value: 4.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLFDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYvGSMP-CMPARRELHTGRYNFLHREWG---PLEPFDDSMP 79
Cdd:cd16034 5 LFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAV-SNYPvCSPYRASLLTGQYPLTNGVFGndvPLPPDAPTIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 80 ELLKKAGIYTHLISD-HLhyweDGGGNYHNRYSS--WDVVRGQEGDHWKASvgeppipevlrvpqkqtGGGVSGLWRHDW 156
Cdd:cd16034 84 DVLKDAGYRTGYIGKwHL----DGPERNDGRADDytPPPERRHGFDYWKGY-----------------ECNHDHNNPHYY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 157 AN---REYIQQEADFPQTkvfDAGCDFIHKNHAEDN-WLLQVETFDPHEPFYTT-EEYLSLYDDE--WQGPHYDWPRGKV 229
Cdd:cd16034 143 DDdgkRIYIKGYSPDAET---DLAIEYLENQADKDKpFALVLSWNPPHDPYTTApEEYLDMYDPKklLLRPNVPEDKKEE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 230 SESEEAIAHircrYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKNQmpYYNEVANNPLFIWDP 309
Cdd:cd16034 220 AGLREDLRG----YYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLMNKQV--PYEESIRVPFIIRYP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 310 RSAVCGARRQSLVQMIDWAPTLLDYFQQPIPADMQGQPLAKVIASDEPVREGA----LFGVFSGHVN--------VTDGR 377
Cdd:cd16034 294 GKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKDDEPDSvllqCFVPFGGGSArdggewrgVRTDR 373
|
....*
gi 446566675 378 YVYMR 382
Cdd:cd16034 374 YTYVR 378
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
20-389 |
4.09e-29 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 119.77 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 20 GDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTG----RYNFLHREWGPLEPFDDSMPELLKKAGIYTHLISDh 95
Cdd:PRK13759 26 GNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGlsqwHHGRVGYGDVVPWNYKNTLPQEFRDAGYYTQCIGK- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 96 LHYW-EDGGGNYHNrysswdvVRGQEGDHWKASVGEPPIPEV---------LRVPQKQTGGGVSGLWRHDWANREYIQQE 165
Cdd:PRK13759 105 MHVFpQRNLLGFHN-------VLLHDGYLHSGRNEDKSQFDFvsdylawlrEKAPGKDPDLTDIGWDCNSWVARPWDLEE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 166 ADFPQTKVFDAGCDFIHKNHAEDNWLLQVETFDPHEPFYTTEEYLSLYDD---------EW--------QGPHYDWPRGK 228
Cdd:PRK13759 178 RLHPTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDadipdphigDWeyaedqdpEGGSIDALRGN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 229 VSEseEAIAHIRCRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKNqMPYYNEvANNPLFIWD 308
Cdd:PRK13759 258 LGE--EYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKG-YPYEGS-AHIPFIIYD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 309 PRSAVCGAR---RQSLVQMIDWAPTLLDYFQQPIPADMQGQPLAKVIASDEP-VR-----EGALFGVFSGHvnVTDGRYV 379
Cdd:PRK13759 334 PGGLLAGNRgtvIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFGQYEgWRpylhgEHALGYSSDNY--LTDGKWK 411
|
410
....*....|
gi 446566675 380 YMRAAQPGRE 389
Cdd:PRK13759 412 YIWFSQTGEE 421
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
5-479 |
1.27e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 111.56 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 5 ILLF--DSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFL--HREWGPL-EPFDDSMP 79
Cdd:cd16150 3 IVIFvaDQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVngHRTLHHLlRPDEPNLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 80 ELLKKAGIYThlisdhlhYWedGGGNyhnrysswDVVrgqEGDHWKASVGEPpipevlrvpqkqtgggvsglwrhDWAnr 159
Cdd:cd16150 83 KTLKDAGYHV--------AW--AGKN--------DDL---PGEFAAEAYCDS-----------------------DEA-- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 160 eyiqqeadfpqtkVFDAGCDFIhKNHAEDN-WLLQVETFDPHEPFYTTEEYLSLYDDEWQGPHydWPRGK---------- 228
Cdd:cd16150 117 -------------CVRTAIDWL-RNRRPDKpFCLYLPLIFPHPPYGVEEPWFSMIDREKLPPR--RPPGLrakgkpsmle 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 229 -------VSESEEAIAHIRCRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKNQMPYYNEVAN 301
Cdd:cd16150 181 giekqglDRWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNTFEDCLTR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 302 NPLFIWDPRSAVCGaRRQSLVQMIDWAPTLLDYFQQPIPADMQGQPLAKVIA-SDEPVREgalfGVFS-GhvnvtdGRYV 379
Cdd:cd16150 261 VPLIIKPPGGPAGG-VSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLPVLAgETEEHRD----AVFSeG------GRLH 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 380 YMRAAQPGREhdiANYTLMPIKMNARYDVDELGKlslappfnftkgLQVLRIparEKYKGVN--SFGHLLFDLRDDPQQQ 457
Cdd:cd16150 330 GEEQAMEGGH---GPYDLKWPRLLQQEEPPEHTK------------AVMIRT---RRYKYVYrlYEPDELYDLEADPLEL 391
|
490 500
....*....|....*....|....*.
gi 446566675 458 HPIHDE----AIEARMISLLIRLMKE 479
Cdd:cd16150 392 HNLIGDpayaEIIAEMKQRLLRWMVE 417
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
4-335 |
3.38e-26 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 108.28 E-value: 3.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLFDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHREWGPLEP----FDDSMP 79
Cdd:pfam00884 4 VLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVglprTEPSLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 80 ELLKKAGIYTHLIsdhlhywedggGNYHNRYSSWDVVRGQEGDHWkasVGEPPIPEVLRvpqkqtgggvsglwrhDWANR 159
Cdd:pfam00884 84 DLLKRAGYNTGAI-----------GKWHLGWYNNQSPCNLGFDKF---FGRNTGSDLYA----------------DPPDV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 160 EYIQQEADFPQTKVFDAGCDFIHKNHaeDNWLLQVETFDPHEPFYtteeylslYDDEWQGPHYDWPRGKVSESEeaiaHI 239
Cdd:pfam00884 134 PYNCSGGGVSDEALLDEALEFLDNND--KPFFLVLHTLGSHGPPY--------YPDRYPEKYATFKPSSCSEEQ----LL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 240 RCRYRALVSMcDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAK--NQMPYYNEVANNPLFIWDPRSAVCGAR 317
Cdd:pfam00884 200 NSYDNTLLYT-DDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHggKYDNAPEGGYRVPLLIWSPGGKAKGQK 278
|
330
....*....|....*...
gi 446566675 318 RQSLVQMIDWAPTLLDYF 335
Cdd:pfam00884 279 SEALVSHVDLFPTILDLA 296
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
4-369 |
2.72e-24 |
|
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: 103.43 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLFDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHREWGPLEPFDDSMPEL-- 81
Cdd:cd16032 4 LLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPADIPTFah 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 82 -LKKAGIYT------HLIS-DHLHYWE-DGGGNYHNRYSSWDVVRGQEGdhwkasvgePPipevlrvpqkqtgggvsglw 152
Cdd:cd16032 84 yLRAAGYRTalsgkmHFVGpDQLHGFDyDEEVAFKAVQKLYDLARGEDG---------RP-------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 153 rhdwanreyiqqeadfpqtkvfdagcdfihknhaednWLLQVETFDPHEPFYTTEEYLSLYddewqgphydwprgkvses 232
Cdd:cd16032 135 -------------------------------------FFLTVSFTHPHDPYVIPQEYWDLY------------------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 233 eeaIAHIRCRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKnqMPYYNEVANNPLFIWDPRSA 312
Cdd:cd16032 159 ---VRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYK--MSFFEGSARVPLIISAPGRF 233
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 313 VcGARRQSLVQMIDWAPTLLDYF---QQPIPADMQGQPLAKVIASDEPVREGALFGVFSG 369
Cdd:cd16032 234 A-PRRVAEPVSLVDLLPTLVDLAgggTAPHVPPLDGRSLLPLLEGGDSGGEDEVISEYLA 292
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
19-477 |
5.35e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 103.41 E-value: 5.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 19 YGDLLTKAPNFQRLAAHAATFDNSYV-GSMP---CMPARRELHTGRYNF-LHREWGPLEPFDD-SMPELLKKAGIYTHLI 92
Cdd:cd16155 21 LGNPEIQTPNLDRLARRGTSFTNAYNmGGWSgavCVPSRAMLMTGRTLFhAPEGGKAAIPSDDkTWPETFKKAGYRTFAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 93 sdhlhywedggGNYHNRYsswdvvrgqegdhwkasvgeppipevlrvpqkqtgggvsglwrhdwanreyiqqeadfpqtk 172
Cdd:cd16155 101 -----------GKWHNGF-------------------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 173 vFDAGCDFIH-KNHAEDNWLLQVETFDPHEPFYTTEEYLSLYDDE-------WQGPH-YD-------------WPRgkvs 230
Cdd:cd16155 108 -ADAAIEFLEeYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPEtiplpenFLPQHpFDngegtvrdeqlapFPR---- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 231 eSEEAIAHIRCRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKNQMpyYNEVANNPLFIWDPr 310
Cdd:cd16155 183 -TPEAVRQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLMGKQNL--YEHSMRVPLIISGP- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 311 SAVCGARRQSLVQMIDWAPTLLDYFQQPIPADMQGQPLAKVIASDEPVREGALFGvfsghvnvtdgryVYMRAAQPGReh 390
Cdd:cd16155 259 GIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVRDTLYG-------------AYRDGQRAIR-- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 391 dianytlmpikmnarydvDELGKLslappfnftkglqVLRIPAREKYkgvnsfghLLFDLRDDPQQQHPIHDE-AIEARM 469
Cdd:cd16155 324 ------------------DDRWKL-------------IIYVPGVKRT--------QLFDLKKDPDELNNLADEpEYQERL 364
|
....*...
gi 446566675 470 ISLLIRLM 477
Cdd:cd16155 365 KKLLAELK 372
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
16-342 |
3.02e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 98.85 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 16 LPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHrewgplepfddsmpellkkaGIythlisdh 95
Cdd:cd16149 16 LGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQH--------------------GI-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 96 lHYWEDGGGnyHNRYsswdvvrgQEGDHWkaSVGEPPIPEVLrvpqKQTG--GGVSGLWrHdwanreyiqqeadfpqtkV 173
Cdd:cd16149 68 -HDWIVEGS--HGKT--------KKPEGY--LEGQTTLPEVL----QDAGyrCGLSGKW-H------------------L 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 174 FDAGCDFIHKNHAEDN-WLLQVETFDPHEPfytteeylslyddeWQgphydwprgkvseseeaiahircrYRALVSMCDR 252
Cdd:cd16149 112 GDDAADFLRRRAEAEKpFFLSVNYTAPHSP--------------WG------------------------YFAAVTGVDR 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 253 NLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAK----NQMPYYNEVANNPLFIWDPRSAVCGARRQSLVQMIDWA 328
Cdd:cd16149 154 NVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKgngtFPLNMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFF 233
|
330
....*....|....
gi 446566675 329 PTLLDYFQQPIPAD 342
Cdd:cd16149 234 PTLLELAGVDPPAD 247
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
15-364 |
6.55e-22 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 96.12 E-value: 6.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 15 YLPPY--GDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHREW-----GPLEPFDDSMPEL---LKK 84
Cdd:cd16035 13 YPPPWpaGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTdtlgsPMQPLLSPDVPTLghmLRA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 85 AGIYThlisdhlhYWedgggnyhnrysswdvvRGQegdhWKASvgeppipevlrvpqkqtgGGVSGLWRHDwanREYIQQ 164
Cdd:cd16035 93 AGYYT--------AY-----------------KGK----WHLS------------------GAAGGGYKRD---PGIAAQ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 165 EADFPQTKvfdagcdfIHKNHAEDNWLLQVETFDPHEPFYTTEEylslyDDEWQgPHYDWprgkvseseeaiahircrYR 244
Cdd:cd16035 123 AVEWLRER--------GAKNADGKPWFLVVSLVNPHDIMFPPDD-----EERWR-RFRNF------------------YY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 245 ALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKNQMPyYNEVANNPLFIWDPRSAVCGARRQSLVQM 324
Cdd:cd16035 171 NLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNA-YEEALHVPLIISHPDLFGTGQTTDALTSH 249
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446566675 325 IDWAPTLLDY------FQQPIPADMQGQPLAKVI--ASDEPVREGALF 364
Cdd:cd16035 250 IDLLPTLLGLagvdaeARATEAPPLPGRDLSPLLtdADADAVRDGILF 297
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
30-347 |
9.92e-20 |
|
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: 91.07 E-value: 9.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 30 QRLAAHAATFDNSYVgSMP-CMPARRELHTGRY----NFLH--REWGPLEPF------DDSMPELLKKAGIYTHLISDHL 96
Cdd:cd16147 27 KLLADQGTTFTNAFV-TTPlCCPSRASILTGQYahnhGVTNnsPPGGGYPKFwqngleRSTLPVWLQEAGYRTAYAGKYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 97 H-YWEDGGGNYhnrysswdVVRGqeGDHWKASVGepPIPEVLRVPQKQTGGGvsglwRHDWANREYiqqeadfpQTKVF- 174
Cdd:cd16147 106 NgYGVPGGVSY--------VPPG--WDEWDGLVG--NSTYYNYTLSNGGNGK-----HGVSYPGDY--------LTDVIa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 175 DAGCDFIHKNHAEDN-WLLQVETFDPHEPFYTTEEYLSLYDDEW-------------QGPHydWPRGKVSESEEAIAHI- 239
Cdd:cd16147 161 NKALDFLRRAAADDKpFFLVVAPPAPHGPFTPAPRYANLFPNVTapprpppnnpdvsDKPH--WLRRLPPLNPTQIAYId 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 240 ---RCRYRALVSMcDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKNQMPYYNEVaNNPLFIWDPrSAVCGA 316
Cdd:cd16147 239 elyRKRLRTLQSV-DDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDI-RVPLLVRGP-GIPAGV 315
|
330 340 350
....*....|....*....|....*....|.
gi 446566675 317 RRQSLVQMIDWAPTLLDYFQQPIPADMQGQP 347
Cdd:cd16147 316 TVDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
25-332 |
6.16e-17 |
|
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: 80.88 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 25 KAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHrewgplepfddsmpellkkagiythlisdhlhywedggG 104
Cdd:cd16153 36 ESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRT--------------------------------------G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 105 NYHNRYSSwdvvrgQEGDHwkasvGEPPIPEVLRVPQKQTGggVSGLWRHDWANReYIQQEADFPQTKVFDA--GCDfih 182
Cdd:cd16153 78 VYGFEAAH------PALDH-----GLPTFPEVLKKAGYQTA--SFGKSHLEAFQR-YLKNANQSYKSFWGKIakGAD--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 183 knhAEDNWLLQVETFDPHEPFYTTEEYLSLYDdewqgphydwprgkvseseeaiahircrYRALVSMCDRNLGRILDLMD 262
Cdd:cd16153 141 ---SDKPFFVRLSFLQPHTPVLPPKEFRDRFD----------------------------YYAFCAYGDAQVGRAVEAFK 189
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446566675 263 EHDLWRD---TMLIVGTDHGFLLGEHGWWAKnQMPYYNEVANNPLFIW-DPRSAVCGARRQSLVQMIDWAPTLL 332
Cdd:cd16153 190 AYSLKQDrdyTIVYVTGDHGWHLGEQGILAK-FTFWPQSHRVPLIVVSsDKLKAPAGKVRHDFVEFVDLAPTLL 262
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
19-407 |
7.96e-17 |
|
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: 82.21 E-value: 7.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 19 YGDL------LTKAPNFQRLAAHAATFDNSYVGSMpCMPARRELHTGRYNF---LHREWGPLEPFDDS---MPELLKKAG 86
Cdd:cd16146 13 YGDLgfhgnpILKTPNLDRLAAESVRFTNFHVSPV-CAPTRAALLTGRYPFrtgVWHTILGRERMRLDettLAEVFKDAG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 87 IYTHLISD-HLhywedgGGNYhnRYSSWDvvRGQEgdhwkasvgeppipEVLRvpqkQTGGGVSGLWrhDWANREY---- 161
Cdd:cd16146 92 YRTGIFGKwHL------GDNY--PYRPQD--RGFD--------------EVLG----HGGGGIGQYP--DYWGNDYfddt 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 162 IQQEADFPQTK------VFDAGCDFIHKNHaEDNWLLQVETFDPHEPFYTTEEYLSLYDDEWQGPHydwprgkvseseea 235
Cdd:cd16146 142 YYHNGKFVKTEgyctdvFFDEAIDFIEENK-DKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDK-------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 236 iahiRCRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWW------AKNQmPYYNEVaNNPLFIWDP 309
Cdd:cd16146 207 ----LAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRFnagmrgKKGS-VYEGGH-RVPFFIRWP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 310 RSAVCGARRQSLVQMIDWAPTLLDYFQQPIPA--DMQGQPLAKVIASDE-PVREGALFgVFSGHVNVTDGRYVY--MRAA 384
Cdd:cd16146 281 GKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEgiKLDGRSLLPLLKGESdPWPERTLF-THSGRWPPPPKKKRNaaVRTG 359
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446566675 385 Q-------------------PGREHDIAN-YTLMPIKMNARYD 407
Cdd:cd16146 360 RwrlvspkgfqpelydiendPGEENDVADeHPEVVKRLKAAYE 402
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
27-364 |
8.04e-16 |
|
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: 79.51 E-value: 8.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 27 PNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRY-------NFLHREWGP--------------LEPFDDSMPELLKKA 85
Cdd:cd16144 27 PNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYparlgitDVIPGRRGPpdntklipppsttrLPLEEVTIAEALKDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 86 GIYT------HLISDHLHYWEDGGgnyhnryssWDVVRGQEGDHWKASVGEPPIPEVLRVPQKQTGggvsglwrhdwanr 159
Cdd:cd16144 107 GYATahfgkwHLGGEGGYGPEDQG---------FDVNIGGTGNGGPPSYYFPPGKPNPDLEDGPEG-------------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 160 eyiqqeaDFPQTKVFDAGCDFIhKNHAEDNWLLQVETFDPHEPFYTTEEYLSLYDDewqgphydwpRGKVSESEEAIAHi 239
Cdd:cd16144 164 -------EYLTDRLTDEAIDFI-EQNKDKPFFLYLSHYAVHTPIQARPELIEKYEK----------KKKGLRKGQKNPV- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 240 rcrYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKNQmPY------YNE----VannPLFIWDP 309
Cdd:cd16144 225 ---YAAMIESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTSNA-PLrggkgsLYEggirV---PLIVRWP 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446566675 310 RSAVCGARRQSLVQMIDWAPTLLDYFQQPIPA--DMQGQPLAKVIASDEPVR-EGALF 364
Cdd:cd16144 298 GVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPpqHLDGVSLVPLLKGGEADLpRRALF 355
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
20-333 |
8.24e-15 |
|
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: 76.05 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 20 GDLLTKAPNFQRLAAHAATFDNSYVGSMpCMPARRELHTGRYNFLH----------REWGpLEPFDDSMPELLKKAGIYT 89
Cdd:cd16029 20 GSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTgmqhgvilagEPYG-LPLNETLLPQYLKELGYAT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 90 HLIsdhlhywedggGNYHNRYSSWDVV---RG---------QEGDHWKASVGEPPipevlrvpqkqtGGGVSGLWRHDWA 157
Cdd:cd16029 98 HLV-----------GKWHLGFYTWEYTptnRGfdsfygyygGAEDYYTHTSGGAN------------DYGNDDLRDNEEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 158 NREYIQQEAdfpqTKVF-DAGCDFIHkNHaednwllqvetfDPHEPFYtteEYLSlyddeWQGPHY--DWPRGKVSESEE 234
Cdd:cd16029 155 AWDYNGTYS----TDLFtDRAVDIIE-NH------------DPSKPLF---LYLA-----FQAVHAplQVPPEYADPYED 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 235 AIAHIRCRYR----ALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGfllgehGWwaknqmPYYNEVANN-PL----- 304
Cdd:cd16029 210 KFAHIKDEDRrtyaAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG------GP------TGGGDGGSNyPLrggkn 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446566675 305 -----------FIWdprSAVCGARRQS----LVQMIDWAPTLLD 333
Cdd:cd16029 278 tlweggvrvpaFVW---SPLLPPKRGTvsdgLMHVTDWLPTLLS 318
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
4-394 |
4.09e-13 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 70.71 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IIL-LFDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYvgSMP-CMPARRELHTGRYNFLHREW-GPLEPFDDSMPE 80
Cdd:cd16151 3 IILiMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAY--AQPlCTPSRVQLMTGKYNFRNYVVfGYLDPKQKTFGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 81 LLKKAGiYTHLISDHlhyWEDGGGNYHN---------RYSSWDVVRGQEgdhwKASVGEPPIPEVlrvpqkQTGGGvsgl 151
Cdd:cd16151 81 LLKDAG-YATAIAGK---WQLGGGRGDGdyphefgfdEYCLWQLTETGE----KYSRPATPTFNI------RNGKL---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 152 wrhdwanREYIQQE------ADFpqtkvfdaGCDFIHKNHAEDnWLLQVETFDPHEPFYTTEeylslyDDEwqgPHYDWP 225
Cdd:cd16151 143 -------LETTEGDygpdlfADF--------LIDFIERNKDQP-FFAYYPMVLVHDPFVPTP------DSP---DWDPDD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 226 RGKVSESEeaiahircRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWW-------AKNQMpyyNE 298
Cdd:cd16151 198 KRKKDDPE--------YFPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTngrevrgGKGKT---TD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 299 VANN-PLFIWDPRSAVCGARRQSLVQMIDWAPTLLDYFQQPIPAD--MQGQPLAKVI--ASDEPVRE-----GALFGVFS 368
Cdd:cd16151 267 AGTHvPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQLlgKTGSPRREwiywyYRNPHKKF 346
|
410 420
....*....|....*....|....*.
gi 446566675 369 GHVNVTDGRYVYMRaaqPGREHDIAN 394
Cdd:cd16151 347 GSRFVRTKRYKLYA---DGRFFDLRE 369
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
20-348 |
1.29e-12 |
|
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: 69.11 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 20 GDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNFLHREWGPLEPFDDSMP---ELLKKAGIYTHLISDhL 96
Cdd:cd16171 20 GNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPNYPtwmDRLEKHGYHTQKYGK-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 97 HYwEDGGGNYHNRYSSW--DV--VRGQEGDHWKASVGEPpipEVLRVPQKqtgggvsglwrhDWANREyiqqeadfpqtk 172
Cdd:cd16171 99 DY-TSGHHSVSNRVEAWtrDVpfLLRQEGRPTVNLVGDR---STVRVMLK------------DWQNTD------------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 173 vfdagcdfihknhAEDNWLLQvETFDPHEPFYTteeYLSLyddewQGPHyDWPRGKVSESEEAIAHIRCRYRALVSMCDR 252
Cdd:cd16171 151 -------------KAVHWIRK-EAPNLTQPFAL---YLGL-----NLPH-PYPSPSMGENFGSIRNIRAFYYAMCAETDA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 253 NLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKnqMPYYNEVANNPLFIWDPRSAVcGARRQSLVQMIDWAPTLL 332
Cdd:cd16171 208 MLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYK--MSMYEGSSHVPLLIMGPGIKA-GQQVSDVVSLVDIYPTML 284
|
330
....*....|....*.
gi 446566675 333 DYFQQPIPADMQGQPL 348
Cdd:cd16171 285 DIAGVPQPQNLSGYSL 300
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
19-279 |
5.85e-12 |
|
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: 67.23 E-value: 5.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 19 YGDL------LTKAPNFQRLAAHAATFDNSYVGSMPCMPARREL----HTG----RYNFLHREWGPLEPFDDSMPELLKK 84
Cdd:cd16145 13 YGDLgcygqkKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLltglHTGhtrvRGNSEPGGQDPLPPDDVTLAEVLKK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 85 AGIYTHLISDhlhyWEDGG----GNYHNRysSWDVVRGQEgDHWKASVGEPpiPEVLRVPQKQTGGGVSGLWRHDWANRE 160
Cdd:cd16145 93 AGYATAAFGK----WGLGGpgtpGHPTKQ--GFDYFYGYL-DQVHAHNYYP--EYLWRNGEKVPLPNNVIPPLDEGNNAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 161 YiqQEADFPQTKVFDAGCDFIhKNHAEDNWLLQVETFDPHEPFYTTEEYLSLYDDEWQGPHY--DWPRGKVseseeaiah 238
Cdd:cd16145 164 G--GGGTYSHDLFTDEALDFI-RENKDKPFFLYLAYTLPHAPLQVPDDGPYKYKPKDPGIYAylPWPQPEK--------- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446566675 239 ircRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHG 279
Cdd:cd16145 232 ---AYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNG 269
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
4-335 |
5.93e-10 |
|
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: 60.00 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLFDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYV-----GSMPCMParrELHTGRYNFLHREWGPLEPFD--- 75
Cdd:cd16015 4 IVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSpgfggGTANGEF---EVLTGLPPLPLGSGSYTLYKLnpl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 76 DSMPELLKKAGIYTH-LISDHLHYWedgggnyhNR---YSSW--DVVRGQEgdhwkasvgEPPIPEVLRVpqkqtGGGVS 149
Cdd:cd16015 81 PSLPSILKEQGYETIfIHGGDASFY--------NRdsvYPNLgfDEFYDLE---------DFPDDEKETN-----GWGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 150 glwrhDWANREYIQQEAdfpqtkvfdagcdfihKNHAEDNWLLQVETFDPHEPFYTTEEYlslyddewqGPHYDWPRGKV 229
Cdd:cd16015 139 -----DESLFDQALEEL----------------EELKKKPFFIFLVTMSNHGPYDLPEEK---------KDEPLKVEEDK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 230 SESEEAIAHIRCryralvsmCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKNQMPYYNEVannPLFIWDP 309
Cdd:cd16015 189 TELENYLNAIHY--------TDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLYRT---PLLIYSP 257
|
330 340
....*....|....*....|....*.
gi 446566675 310 RSAVcGARRQSLVQMIDWAPTLLDYF 335
Cdd:cd16015 258 GLKK-PKKIDRVGSQIDIAPTLLDLL 282
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
4-279 |
7.96e-10 |
|
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: 60.68 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLFDSLNknylppYGDL-------LTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRYNF-LHREWGPLEPFD 75
Cdd:cd16143 4 VIILADDLG------YGDIscynpdsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWrSRLKGGVLGGFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 76 DS--------MPELLKKAGIYTHLISD-HLHY-WEDGGGNYHNRYSSWDVVRGQegdhwkasvgepPIPevlrvpqkqtG 145
Cdd:cd16143 78 PPliepdrvtLAKMLKQAGYRTAMVGKwHLGLdWKKKDGKKAATGTGKDVDYSK------------PIK----------G 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 146 GGVSGLWRHDWAnreyiqqeadFPQTKV----FDAGCDFIHKNHAEDN-WLLQVETFDPHEPFytteeylsLYDDEWQG- 219
Cdd:cd16143 136 GPLDHGFDYYFG----------IPASEVlptlTDKAVEFIDQHAKKDKpFFLYFALPAPHTPI--------VPSPEFQGk 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446566675 220 ----PHYDWprgkvseseeaiahircryralVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHG 279
Cdd:cd16143 198 sgagPYGDF----------------------VYELDWVVGRILDALKELGLAENTLVIFTSDNG 239
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
4-286 |
1.84e-09 |
|
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: 59.50 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLFDSLNknylppYGDL------LTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRY-------NFLHREWGP 70
Cdd:cd16026 5 VVILADDLG------YGDLgcygspLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvglpGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 71 --LEPFDDSMPELLKKAGIYTHLI--------SDHL-------HYWedgGGNYHNrysswdvvrgqegDHWKASVGEPPI 133
Cdd:cd16026 79 ggLPPDEITIAEVLKKAGYRTALVgkwhlghqPEFLptrhgfdEYF---GIPYSN-------------DMWPFPLYRNDP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 134 PEVLRVPQkqtgggvsglwrhdwANREYIQQEADFPQ-TKVF-DAGCDFIHKnHAEDNWLLQVETFDPHEPFYTTEEYls 211
Cdd:cd16026 143 PGPLPPLM---------------ENEEVIEQPADQSSlTQRYtDEAVDFIER-NKDQPFFLYLAHTMPHVPLFASEKF-- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446566675 212 lyddewqgphydwpRGKvSEseeaiahiRCRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHG--FLLGEHG 286
Cdd:cd16026 205 --------------KGR-SG--------AGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHG 258
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
249-364 |
6.89e-09 |
|
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: 57.62 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 249 MC---DRNLGRILDLMDEHDLWRDTMLIVGTDHG--FllgehgwwaKNQMPYYNEVANN-----PLFIWDPRsAVCGARR 318
Cdd:cd16152 180 CCerlDENVGRIRDALKELGLYDNTIIVFTSDHGchF---------RTRNAEYKRSCHEssirvPLVIYGPG-FNGGGRV 249
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446566675 319 QSLVQMIDWAPTLLDYFQQPIPADMQGQPLAKVIASDEPVREGALF 364
Cdd:cd16152 250 EELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVEDWRNEVF 295
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
4-363 |
2.55e-08 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 56.20 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLFDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYV---GSMPCMPArreLHTGRY-----NFLHREWGPlePFD 75
Cdd:COG1368 238 VVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSqggRTSRGEFA---VLTGLPplpggSPYKRPGQN--NFP 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 76 dSMPELLKKAGIYTHLI-SDHLHYWedgggNYHNRYSSW--DVVRGQEGdhwkasvgeppipevlrVPQKQTGG-GVSgl 151
Cdd:COG1368 313 -SLPSILKKQGYETSFFhGGDGSFW-----NRDSFYKNLgfDEFYDRED-----------------FDDPFDGGwGVS-- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 152 wrhDWANREYIQQEADfpqtkvfdagcdfihknHAEDNWLLQVETFDPHEPFYTTEEYLSLYDDewqgphydwPRGKVSE 231
Cdd:COG1368 368 ---DEDLFDKALEELE-----------------KLKKPFFAFLITLSNHGPYTLPEEDKKIPDY---------GKTTLNN 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 232 SEEAIahircRYrAlvsmcDRNLGRILDLMDEHDLWRDTML-IVGtDHGFLLGEHGWWAKNQMPYynevaNNPLFIWDPR 310
Cdd:COG1368 419 YLNAV-----RY-A-----DQALGEFIEKLKKSGWYDNTIFvIYG-DHGPRSPGKTDYENPLERY-----RVPLLIYSPG 481
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446566675 311 SAVcGARRQSLVQMIDWAPTLLDYFQQPIPADMQ-GQPLAKVIASDEPVREGAL 363
Cdd:COG1368 482 LKK-PKVIDTVGSQIDIAPTLLDLLGIDYPSYYAfGRDLLSPDTDPFAFRNGGF 534
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
5-279 |
6.18e-08 |
|
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: 54.66 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 5 ILLF--DSLNKNYLPPY--GDLLTKAPNFQRLAAHAATFDNSYVGSMpCMPARRELHTGRYNFlhR---EWGPLEPFD-- 75
Cdd:cd16154 3 ILLIiaDDQGLDSSAQYslSSDLPVTPTLDSLANSGIVFDNLWATPA-CSPTRATILTGKYGF--RtgvLAVPDELLLse 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 76 DSMPELLKKAGIYTHLISDHLHYWEDGGGNYHNRysswdvvRGQEGDHWKASVGeppipevlrvpqkqtgGGVSGLWRHD 155
Cdd:cd16154 80 ETLLQLLIKDATTAGYSSAVIGKWHLGGNDNSPN-------NPGGIPYYAGILG----------------GGVQDYYNWN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 156 WANREYIQQEADFPQTKVFDAGCDFIHKNHAEdnWLLQVETFDPHEPFYTTEEYLSLYDDewqgphydwprgkvSESEEA 235
Cdd:cd16154 137 LTNNGQTTNSTEYATTKLTNLAIDWIDQQTKP--WFLWLAYNAPHTPFHLPPAELHSRSL--------------LGDSAD 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446566675 236 I-AHIRCRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGtDHG 279
Cdd:cd16154 201 IeANPRPYYLAAIEAMDTEIGRLLASIDEEERENTIIIFIG-DNG 244
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
4-333 |
5.42e-06 |
|
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: 47.80 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLFDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMP-CMPARRELHTGRYNFLHrewgplepfddsmpell 82
Cdd:cd00016 4 VLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTsSAPNHAALLTGAYPTLH----------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 83 kkaGIYTHLISDHLHYWEDGGGNYHnrysswdvvrgqegdhwkasvgEPPIPEVLRvpQKQTGGGVSGLWrhdwanrEYI 162
Cdd:cd00016 67 ---GYTGNGSADPELPSRAAGKDED----------------------GPTIPELLK--QAGYRTGVIGLL-------KAI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 163 QQEAD-FPQtkvfdagcdfihknhaednwLLQVETFDPHEPFYtteeylslyddewqgphydwprgkvseseeAIAHIRC 241
Cdd:cd00016 113 DETSKeKPF--------------------VLFLHFDGPDGPGH------------------------------AYGPNTP 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 242 RYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHGWWAKNQMPYYNEVANN--PLFIWDPRSAVCGARRQ 319
Cdd:cd00016 143 EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADGKADKSHTGMrvPFIAYGPGVKKGGVKHE 222
|
330
....*....|....
gi 446566675 320 SLVQMiDWAPTLLD 333
Cdd:cd00016 223 LISQY-DIAPTLAD 235
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
243-351 |
3.35e-05 |
|
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: 46.28 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 243 YRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGfLLGEHGW-WAKN-------QMPYYNEVAnNPLFI-WDPRSAV 313
Cdd:cd16025 221 YAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNG-ASAEPGWaNASNtpfrlykQASHEGGIR-TPLIVsWPKGIKA 298
|
90 100 110
....*....|....*....|....*....|....*...
gi 446566675 314 CGARRQSLVQMIDWAPTLLDYFQQPIPADMQGQPLAKV 351
Cdd:cd16025 299 KGGIRHQFAHVIDIAPTILELAGVEYPKTVNGVPQLPL 336
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
4-96 |
5.34e-05 |
|
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: 45.54 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLFDSLNKNYLPPYGDLLTKA-PNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRY--------NFLHREWGPLEPF 74
Cdd:cd16161 5 LLLFADDLGWGDLGANWAPNAILtPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLglrngvghNFLPTSVGGLPLN 84
|
90 100
....*....|....*....|...
gi 446566675 75 DDSMPELLKKAGIYTHLISD-HL 96
Cdd:cd16161 85 ETTLAEVLRQAGYATGMIGKwHL 107
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
4-61 |
1.12e-04 |
|
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: 44.74 E-value: 1.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446566675 4 IILLF-DSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRY 61
Cdd:cd16158 4 IVLLFaDDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRY 62
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
2-280 |
1.78e-04 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 43.58 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 2 KAIILLFDSLNKNYLPPYgdlltKAPNFQRLAAHAATFDNSYVG----SMPCMPArreLHTGRYnflhrewgplepfdds 77
Cdd:COG1524 25 KVVLILVDGLRADLLERA-----HAPNLAALAARGVYARPLTSVfpstTAPAHTT---LLTGLY---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 78 mPEllkKAGIYthlisdHLHYWEDGGGNYHNrYSSWDVVRGQEGDHWKAsvgePPIPEVLRvpqkQTGGGVSGLWRHDWA 157
Cdd:COG1524 81 -PG---EHGIV------GNGWYDPELGRVVN-SLSWVEDGFGSNSLLPV----PTIFERAR----AAGLTTAAVFWPSFE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 158 NREYIQQEADFPQTkvfdaGCDFIHKNHAEDNWLLQ--VETFDPHEPFYTTEeYLSLYDDE--WQGPhydwprgkvsESE 233
Cdd:COG1524 142 GSGLIDAARPYPYD-----GRKPLLGNPAADRWIAAaaLELLREGRPDLLLV-YLPDLDYAghRYGP----------DSP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446566675 234 EAIAHIRcryralvsMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGF 280
Cdd:COG1524 206 EYRAALR--------EVDAALGRLLDALKARGLYEGTLVIVTADHGM 244
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
231-287 |
2.49e-04 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 42.96 E-value: 2.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446566675 231 ESEEAIAHIRcryralvsMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFL-LGEHGW 287
Cdd:cd16018 177 DSPEVNEALK--------RVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHGY 226
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
4-232 |
5.44e-04 |
|
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: 42.45 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLFDSLNKNYLPPYGDLLTKAPNFQRLAAHAATFDNSYVGSMPCMPARRELHTGRY----------NFLHREWGPLE- 72
Cdd:cd16157 5 ILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLpirngfyttnAHARNAYTPQNi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 73 --PFDDS---MPELLKKAGIYTHLISD-HLHYWEdgggNYHNRYSSWDVVRGQEGDHWKA--SVGEPPIPevlrvpqkqt 144
Cdd:cd16157 85 vgGIPDSeilLPELLKKAGYRNKIVGKwHLGHRP----QYHPLKHGFDEWFGAPNCHFGPydNKAYPNIP---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 145 gggvsgLWRHDWANREYIQQ--------EADFPQTKVFDAgCDFIHKNHAEDNWLLQVETFDP-HEPFYTTEEYL----- 210
Cdd:cd16157 151 ------VYRDWEMIGRYYEEfkidkktgESNLTQIYLQEA-LEFIEKQHDAQKPFFLYWAPDAtHAPVYASKPFLgtsqr 223
|
250 260
....*....|....*....|..
gi 446566675 211 SLYDDEWQgpHYDWPRGKVSES 232
Cdd:cd16157 224 GLYGDAVM--ELDSSVGKILES 243
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
4-279 |
6.73e-04 |
|
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: 42.03 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 4 IILLF-DSLNknylppYGDLL-----TKAPNF-QRLAAHAATFDNSYVGSMPCMPARRELHTGRYNflHR-----EWGPL 71
Cdd:cd16160 4 IVLFFaDDMG------YGDLAsyghpTQERGPiDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLP--IRsgmygGTRVF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 72 EPFDDS--------MPELLKKAGIYT------HL-ISDHLHywEDGGGNYHNRysSWDVVrGQE---GDHWKASVGEPPI 133
Cdd:cd16160 76 LPWDIGglpktevtMAEALKEAGYTTgmvgkwHLgINENNH--SDGAHLPSHH--GFDFV-GTNlpfTNSWACDDTGRHV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 134 PEVLRvpqkqtggGVSGLWRHDWANREYIQQEaDFPQTKVFDAGcDFIHKNhAEDNWLLQVETFDPHEPFYTTEEYlsly 213
Cdd:cd16160 151 DFPDR--------SACFLYYNDTIVEQPIQHE-HLTETLVGDAK-SFIEDN-QENPFFLYFSFPQTHTPLFASKRF---- 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446566675 214 ddewqgphydwpRGKvseseeaiaHIRCRYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHG 279
Cdd:cd16160 216 ------------KGK---------SKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHG 260
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
242-332 |
3.60e-03 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 39.89 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446566675 242 RYRALVSMCDRNLGRILDLMDEHDLWRDTMLIVGTDHGFLLGEHG--WWAKNQmpYYNE----VannPLFIWDPRSAvcg 315
Cdd:COG3083 428 RYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGqnYWGHNS--NFSRyqlqV---PLVIHWPGTP--- 499
|
90
....*....|....*...
gi 446566675 316 ARRQS-LVQMIDWAPTLL 332
Cdd:COG3083 500 PQVISkLTSHLDIVPTLM 517
|
|
| |
