|
Name |
Accession |
Description |
Interval |
E-value |
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
105-616 |
0e+00 |
|
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: 602.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 105 GAPNILFVLYDDTGLAAWSPYGGGINMPTLDKLAANGLTYTQWHTVALCSPTRSTLLTGRNHTLNGMAAITEASNGFPGW 184
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTMAELATGKPGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 185 AGRIPPQAATIAQVLQDNGYSTFWLGKNHNVPEqdvaeggdrktwplgqgferyygfiggetnqwypdlvednhfvepps 264
Cdd:cd16025 81 EGYLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 265 spenGYHLSKDLADQAISMIQNQKAtsPSKPWFMFYNPGANHAPHQAPQEYIAKYKGKFDGGYDAYRSWVLARMIEKGVM 344
Cdd:cd16025 114 ----DYYSTDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAPLQAPKEWIDKYKGKYDAGWDALREERLERQKELGLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 345 PKGTQLTEINPipesqanpadAVRPWDTLTPDERKLFSRMAEVFAGFSEYTDAQVGRVVDYLEQSGQLDNTIVLYAADNG 424
Cdd:cd16025 188 PADTKLTPRPP----------GVPAWDSLSPEEKKLEARRMEVYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 425 TSGEgspngsvnenkffngypddiaenmklidqlggpntyehfpTGWATAFSTPFRMFKRYAqYSGGTADPLVISWPKGI 504
Cdd:cd16025 258 ASAE----------------------------------------PGWANASNTPFRLYKQAS-HEGGIRTPLIVSWPKGI 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 505 KARGELRDQYHHSVDIVPTLLDIVGIEMPKVYHGVEQFPLSGVSMKYTFEAsPDAPTQKKRQFYSMLGTRGIWEDGWLAA 584
Cdd:cd16025 297 KAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNGVPQLPLDGVSLLPTLDG-AAAPSRRRTQYFELFGNRAIRKGGWKAV 375
|
490 500 510
....*....|....*....|....*....|..
gi 2024616551 585 TVHAPFTgrghfDQDQWQLFHVDADRSESTDL 616
Cdd:cd16025 376 ALHPPPG-----WGDQWELYDLAKDPSETHDL 402
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
98-642 |
7.96e-96 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 305.26 E-value: 7.96e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 98 TPKKAPEGAPNILFVLYDDTGLAAWSPYGGG-INMPTLDKLAANGLTYTQWH-TVALCSPTRSTLLTGRNHTLNGMAAIT 175
Cdd:COG3119 15 AAAAAAAKRPNILFILADDLGYGDLGCYGNPlIKTPNIDRLAAEGVRFTNAYvTSPVCSPSRASLLTGRYPHRTGVTDNG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 176 EasngfpGWAGRIPPQAATIAQVLQDNGYSTFWLGKNHNvpeqdvaeggdrktwplgqgferyygfiggetnqwypdlve 255
Cdd:COG3119 95 E------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL----------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 256 dnhfveppsspengyHLSKDLADQAISMIQNQKAtsPSKPWFMFYNPGANHAPHQAPQEYIAKYKGKFDggydayrswvl 335
Cdd:COG3119 128 ---------------YLTDLLTDKAIDFLERQAD--KDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDI----------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 336 armiekgvmpkgtqlteinPIPESQANPadavrpwdtltPDERKLFSRMAEVFAGFSEYTDAQVGRVVDYLEQSGQLDNT 415
Cdd:COG3119 180 -------------------PLPPNLAPR-----------DLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNT 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 416 IVLYAADNGTSGEgspngsvnenkffngypddiaenmklidqlggpntyEHFptgwatafstpFRMFKRYAqYSGGTADP 495
Cdd:COG3119 230 IVVFTSDNGPSLG------------------------------------EHG-----------LRGGKGTL-YEGGIRVP 261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 496 LVISWPKGIKArGELRDQYHHSVDIVPTLLDIVGIEMPKvyhgveqfPLSGVSMKYTFEaspdAPTQKKR-----QFYSM 570
Cdd:COG3119 262 LIVRWPGKIKA-GSVSDALVSLIDLLPTLLDLAGVPIPE--------DLDGRSLLPLLT----GEKAEWRdylywEYPRG 328
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024616551 571 LGTRGIWEDGWLAAtvhapftgRGHFDQDQWQLFHVDADRSESTDLAKQYPEKLEALKKAWLEEAKANLALP 642
Cdd:COG3119 329 GGNRAIRTGRWKLI--------RYYDDDGPWELYDLKNDPGETNNLAADYPEVVAELRALLEAWLKELGDPP 392
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
107-630 |
3.05e-61 |
|
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: 213.17 E-value: 3.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGG-INMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGR--------NHTLNGMAAITE 176
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKfYETPNIDRLAKEGMRFTQAYAAApVCSPSRASILTGQyparlgitDVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 177 ASNGFPGWAGRIPPQAATIAQVLQDNGYSTFWLGKNHnvpeqdvaEGGDRKTWPLGQGFERYYGfiGGETNQWYPDLVED 256
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWH--------LGGEGGYGPEDQGFDVNIG--GTGNGGPPSYYFPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 257 NHFVEPPSSPENGYHLSKDLADQAISMIQNQKatspSKPWFMFYNPGANHAPHQAPQEYIAKYKGKFDGGYDayrswvla 336
Cdd:cd16144 151 GKPNPDLEDGPEGEYLTDRLTDEAIDFIEQNK----DKPFFLYLSHYAVHTPIQARPELIEKYEKKKKGLRK-------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 337 rmiekgvmpkgtqlteinpipeSQANPadavrpwdtltpderklfsrmaeVFAGFSEYTDAQVGRVVDYLEQSGQLDNTI 416
Cdd:cd16144 219 ----------------------GQKNP-----------------------VYAAMIESLDESVGRILDALEELGLADNTL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 417 VLYAADNgtsgegspngsvnenkffngypddiaenmklidqlGGPNTYEHFPTGwatafSTPFRMFKRYAqYSGGTADPL 496
Cdd:cd16144 254 VIFTSDN-----------------------------------GGLSTRGGPPTS-----NAPLRGGKGSL-YEGGIRVPL 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 497 VISWPkGIKARGELRDQYHHSVDIVPTLLDIVGIEMPKVYHgveqfpLSGVSMKYTFEaSPDAPTQKKRQF-----YSML 571
Cdd:cd16144 293 IVRWP-GVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQH------LDGVSLVPLLK-GGEADLPRRALFwhfphYHGQ 364
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024616551 572 GTRgiwedgwLAATVHapftgRGH------FDQDQWQLFHVDADRSESTDLAKQYPEKLEALKKA 630
Cdd:cd16144 365 GGR-------PASAIR-----KGDwkliefYEDGRVELYNLKNDIGETNNLAAEMPEKAAELKKK 417
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
107-636 |
6.23e-57 |
|
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: 201.24 E-value: 6.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTG---LAAW-SPYgggINMPTLDKLAANGLTYTQWHTVALCSPTRSTLLTGRNHTLNGmaaiteASNGFP 182
Cdd:cd16146 1 PNVILILTDDQGygdLGFHgNPI---LKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTG------VWHTIL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 183 GWAgRIPPQAATIAQVLQDNGYSTFWLGKNHNvpeqdvaegGDRKTW-PLGQGFERYYGFIGGETNQ----WYPDLVEDN 257
Cdd:cd16146 72 GRE-RMRLDETTLAEVFKDAGYRTGIFGKWHL---------GDNYPYrPQDRGFDEVLGHGGGGIGQypdyWGNDYFDDT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 258 HFVEPPSSPENGYhLSKDLADQAISMIQNQKatspSKPWFMFYNPGANHAPHQAPQEYIAKYKgkfdggydayrswvlar 337
Cdd:cd16146 142 YYHNGKFVKTEGY-CTDVFFDEAIDFIEENK----DKPFFAYLATNAPHGPLQVPDKYLDPYK----------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 338 miEKGVmpkgtqlteinpipesqanpadavrpwdtltPDERKLFSRMAEVFagfseytDAQVGRVVDYLEQSGQLDNTIV 417
Cdd:cd16146 200 --DMGL-------------------------------DDKLAAFYGMIENI-------DDNVGRLLAKLKELGLEENTIV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 418 LYAADNGTSGegspngsvNENKFFNGypddiaeNMKlidqlGgpntyehfptgwatafstpfrmfKRYAQYSGGTADPLV 497
Cdd:cd16146 240 IFMSDNGPAG--------GVPKRFNA-------GMR-----G-----------------------KKGSVYEGGHRVPFF 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 498 ISWPKGIKARGElRDQYHHSVDIVPTLLDIVGIEMPKVyhgveqFPLSGVSMKYTFEaSPDAPtQKKRQFYSMLGTRGIW 577
Cdd:cd16146 277 IRWPGKILAGKD-VDTLTAHIDLLPTLLDLCGVKLPEG------IKLDGRSLLPLLK-GESDP-WPERTLFTHSGRWPPP 347
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024616551 578 EDGWLAATVHapfTGRGHFDQD---QWQLFHVDADRSESTDLAKQYPEKLEALKKA---WLEEAK 636
Cdd:cd16146 348 PKKKRNAAVR---TGRWRLVSPkgfQPELYDIENDPGEENDVADEHPEVVKRLKAAyeaWWDDVK 409
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
107-621 |
1.13e-52 |
|
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: 189.34 E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGG-INMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRnHTlnGMAAITeaSNGFPGW 184
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKkIKTPNLDRLAAEGMRFTQHYAGApVCAPSRASLLTGL-HT--GHTRVR--GNSEPGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 185 AGRIPPQAATIAQVLQDNGYSTFWLGKNHNVPEQDVAEggdrktwPLGQGFERYYGFIG-GETNQWYP----------DL 253
Cdd:cd16145 76 QDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGH-------PTKQGFDYFYGYLDqVHAHNYYPeylwrngekvPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 254 VEDNHFVEPPSSPENGYH--LSKDL-ADQAISMIQNQKAtspsKPWFMFYNPGANHAPHQAPQEYIAKYKGKFDGGYdAY 330
Cdd:cd16145 149 PNNVIPPLDEGNNAGGGGgtYSHDLfTDEALDFIRENKD----KPFFLYLAYTLPHAPLQVPDDGPYKYKPKDPGIY-AY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 331 RSWvlaRMIEKGvmpkgtqlteinpipesqanpadavrpwdtltpderklfsrmaevFAGFSEYTDAQVGRVVDYLEQSG 410
Cdd:cd16145 224 LPW---PQPEKA---------------------------------------------YAAMVTRLDRDVGRILALLKELG 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 411 QLDNTIVLYAADNGTSGEGspnGSVNENKFFNGYPddiaenmklidqlggpntyehfptgwatafstPFRMFKRyAQYSG 490
Cdd:cd16145 256 IDENTLVVFTSDNGPHSEG---GSEHDPDFFDSNG--------------------------------PLRGYKR-SLYEG 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 491 GTADPLVISWPKGIKARGElRDQYHHSVDIVPTLLDIVGIEMPKvyhgveqfPLSGVSMKYTFEASPDAptQKKR----Q 566
Cdd:cd16145 300 GIRVPFIARWPGKIPAGSV-SDHPSAFWDFMPTLADLAGAEPPE--------DIDGISLLPTLLGKPQQ--QQHDylywE 368
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2024616551 567 FYSMLGTRGIWEDGWlAATVHAPFTGRghfdqdqWQLFHVDADRSESTDLAKQYP 621
Cdd:cd16145 369 FYEGGGAQAVRMGGW-KAVRHGKKDGP-------FELYDLSTDPGETNNLAAQHP 415
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
107-530 |
1.55e-50 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 179.54 E-value: 1.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGGI-NMPTLDKLAANGLTYTQWH-TVALCSPTRSTLLTGRNHTLNGMAAITEASngfpgw 184
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRpTTPFLDRLAEEGLLFSNFYsGGTLTAPSRFALLTGLPPHNFGSYVSTPVG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 185 agrIPPQAATIAQVLQDNGYSTFWLGKNHNvpeqdvaeGGDRKTWPLGQGFERYYGFIGGETNQWYPDLVEDNhfvepps 264
Cdd:pfam00884 75 ---LPRTEPSLPDLLKRAGYNTGAIGKWHL--------GWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYN------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 265 sPENGYHLSKDLADQAISMIQNqkatsPSKPWFMFYNPGANHAPHQAPQEYIAKYKGKFDGGYDAyrswvlarmiekgvm 344
Cdd:pfam00884 137 -CSGGGVSDEALLDEALEFLDN-----NDKPFFLVLHTLGSHGPPYYPDRYPEKYATFKPSSCSE--------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 345 pkgtqlteinpipesqanpadavrpwdtltpderklfSRMAEVFAGFSEYTDAQVGRVVDYLEQSGQLDNTIVLYAADNG 424
Cdd:pfam00884 196 -------------------------------------EQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHG 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 425 tsgegspnGSVNENKffngypddiaenmklidqlggpntyehfptgwatafsTPFRMFKRYAQYSGGTADPLVISWPkGI 504
Cdd:pfam00884 239 --------ESLGEGG-------------------------------------GYLHGGKYDNAPEGGYRVPLLIWSP-GG 272
|
410 420
....*....|....*....|....*.
gi 2024616551 505 KARGELRDQYHHSVDIVPTLLDIVGI 530
Cdd:pfam00884 273 KAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
107-534 |
5.87e-48 |
|
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: 175.47 E-value: 5.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGG--GINMPTLDKLAANGLTYTQWHT-VALCSPTRSTLLTGRNH--TLNGmaaiteaSNGF 181
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPdsKIPTPNIDRLAAEGMRFTDAHSpSSVCTPSRYGLLTGRYPwrSRLK-------GGVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 182 PGWAG-RIPPQAATIAQVLQDNGYSTFWLGKNH-------NVPEQDVAEGGDRKTW-------PLGQGFERYYGFIGGEt 246
Cdd:cd16143 74 GGFSPpLIEPDRVTLAKMLKQAGYRTAMVGKWHlgldwkkKDGKKAATGTGKDVDYskpikggPLDHGFDYYFGIPASE- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 247 nqwypdlvednhfveppsspengyhLSKDLADQAISMIQNQKAtsPSKPWFMFYNPGANHAPHQAPQEyiakYKGKfdgg 326
Cdd:cd16143 153 -------------------------VLPTLTDKAVEFIDQHAK--KDKPFFLYFALPAPHTPIVPSPE----FQGK---- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 327 ydayrswvlarmiekgvmpkgtqlteinpipeSQANP-ADAVrpwdtltpderklfsrmAEVfagfseytDAQVGRVVDY 405
Cdd:cd16143 198 --------------------------------SGAGPyGDFV-----------------YEL--------DWVVGRILDA 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 406 LEQSGQLDNTIVLYAADNGTSgegspngsvnenkffngYPDDIAENMKlidqlggpntYEHFPTGwatafstPFRMFKRY 485
Cdd:cd16143 221 LKELGLAENTLVIFTSDNGPS-----------------PYADYKELEK----------FGHDPSG-------PLRGMKAD 266
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2024616551 486 AqYSGGTADPLVISWPKGIKArGELRDQYHHSVDIVPTLLDIVGIEMPK 534
Cdd:cd16143 267 I-YEGGHRVPFIVRWPGKIPA-GSVSDQLVSLTDLFATLAAIVGQKLPD 313
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
107-629 |
6.09e-47 |
|
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.
Pssm-ID: 293755 [Multi-domain] Cd Length: 429 Bit Score: 173.48 E-value: 6.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGGINM-PTLDKLAANGLTYTQWH-TVALCSPTRSTLLTGR-NHTlNGMaaITEASNGFPG 183
Cdd:cd16031 3 PNIIFILTDDHRYDALGCYGNPIVKtPNIDRLAKEGVRFDNAFvTTSICAPSRASILTGQySHR-HGV--TDNNGPLFDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 184 WAgrippqaATIAQVLQDNGYSTFWLGKNHnvpeqdVAEGGDrktwPLGQGFERYYGFIgGETNQWYPDLVEDNHFVEPP 263
Cdd:cd16031 80 SQ-------PTYPKLLRKAGYQTAFIGKWH------LGSGGD----LPPPGFDYWVSFP-GQGSYYDPEFIENGKRVGQK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 264 sspenGYhlSKD-LADQAISMIQNQKAtspSKPWFMFYNPGANHAPHQAPQEYIAKYKGK--------FDGGYDAYRSWV 334
Cdd:cd16031 142 -----GY--VTDiITDKALDFLKERDK---DKPFCLSLSFKAPHRPFTPAPRHRGLYEDVtipepetfDDDDYAGRPEWA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 335 -LARMIEKGVMpkgtqlteinpipesqanpadavrPWDTLTPDE-----RKLFSRMAEVfagfseytDAQVGRVVDYLEQ 408
Cdd:cd16031 212 rEQRNRIRGVL------------------------DGRFDTPEKyqrymKDYLRTVTGV--------DDNVGRILDYLEE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 409 SGQLDNTIVLYAADNGtsgegspngsvnenkFFNGypddiaenmklidqlggpntyEHfptGWATafstpfrmfKRYAqY 488
Cdd:cd16031 260 QGLADNTIIIYTSDNG---------------FFLG---------------------EH---GLFD---------KRLM-Y 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 489 SGGTADPLVISWPKGIKArGELRDQYHHSVDIVPTLLDIVGIEMPKVYHgveqfplsGVSMKYTFEASPDAPTqkkRQ-- 566
Cdd:cd16031 291 EESIRVPLIIRDPRLIKA-GTVVDALVLNIDFAPTILDLAGVPIPEDMQ--------GRSLLPLLEGEKPVDW---RKef 358
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024616551 567 FYSMLgtrgiWEDGWLAATVHapFTGRG--------HFDQDQWQLFHVDADRSESTDLA--KQYPEKLEALKK 629
Cdd:cd16031 359 YYEYY-----EEPNFHNVPTH--EGVRTerykyiyyYGVWDEEELYDLKKDPLELNNLAndPEYAEVLKELRK 424
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
107-538 |
2.47e-46 |
|
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: 170.00 E-value: 2.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGGINMPTLDKLAANGLTYTQWH-TVALCSPTRSTLLTGRNHTLNGMAAIteASNGFPgwa 185
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFtTAPVCSPSRSALLTGLYPHQNGAHGL--RSRGFP--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 186 grIPPQAATIAQVLQDNGYSTFWLGKNHNVPEqdvaeggdrktWPLGQGFERYYGFIGGETNQWYPDLVEDnhFVeppss 265
Cdd:cd16027 76 --LPDGVKTLPELLREAGYYTGLIGKTHYNPD-----------AVFPFDDEMRGPDDGGRNAWDYASNAAD--FL----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 266 pengyhlskdladqaismiqnqKATSPSKPWFMFYNPganHAPHqapqeyiakykgkfdggydayRSWvlarmiekgvmp 345
Cdd:cd16027 136 ----------------------NRAKKGQPFFLWFGF---HDPH---------------------RPY------------ 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 346 kgtqltEINPIPESQANPADAVRPW---DtlTPDERKLFSRM-AEVfagfsEYTDAQVGRVVDYLEQSGQLDNTIVLYAA 421
Cdd:cd16027 158 ------PPGDGEEPGYDPEKVKVPPylpD--TPEVREDLADYyDEI-----ERLDQQVGEILDELEEDGLLDNTIVIFTS 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 422 DNGTSgegspngsvnenkffngypddiaenmklidqlggpntyehFPtgwatafstpfRMfKRYAqYSGGTADPLVISWP 501
Cdd:cd16027 225 DHGMP----------------------------------------FP-----------RA-KGTL-YDSGLRVPLIVRWP 251
|
410 420 430
....*....|....*....|....*....|....*..
gi 2024616551 502 KGIKArGELRDQYHHSVDIVPTLLDIVGIEMPKVYHG 538
Cdd:cd16027 252 GKIKP-GSVSDALVSFIDLAPTLLDLAGIEPPEYLQG 287
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
107-534 |
1.07e-43 |
|
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: 162.70 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGGINM----PTLDKLAANGLTYTQWHTVALCSPTRSTLLTGRNHTLNGMAAIteasnGFP 182
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgaptPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGLTTV-----GLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 183 GWAGRIPPQAATIAQVLQDNGYSTFWLGKNHnVPEQDvaeggdrKTWPLGQGFERYYGFIggetnqwypdlvedNHFVEp 262
Cdd:cd16142 76 GSPGGLPPWEPTLAELLKDAGYATAQFGKWH-LGDED-------GRLPTDHGFDEFYGNL--------------YHTID- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 263 psspengyhlsKDLADQAISMIQNQKATspSKPWFMFYNPGANHAPHQAPQEYIAKYKGKfdGGYdayrswvlarmiekg 342
Cdd:cd16142 133 -----------EEIVDKAIDFIKRNAKA--DKPFFLYVNFTKMHFPTLPSPEFEGKSSGK--GKY--------------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 343 vmpkgtqlteinpipesqanpADAvrpwdtltpderklfsrMAEVfagfseytDAQVGRVVDYLEQSGQLDNTIVLYAAD 422
Cdd:cd16142 183 ---------------------ADS-----------------MVEL--------DDHVGQILDALDELGIADNTIVIFTTD 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 423 NGtsgegsPNGSVnenkffngYPDdiaenmklidqlGGpntyehfptgwatafSTPFRMFKRYAqYSGGTADPLVISWPK 502
Cdd:cd16142 217 NG------PEQDV--------WPD------------GG---------------YTPFRGEKGTT-WEGGVRVPAIVRWPG 254
|
410 420 430
....*....|....*....|....*....|..
gi 2024616551 503 GIKARGELRDQYHHsVDIVPTLLDIVGIEMPK 534
Cdd:cd16142 255 KIKPGRVSNEIVSH-LDWFPTLAALAGAPDPK 285
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
107-617 |
1.30e-42 |
|
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: 160.04 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGG-GINMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRNHTLNGMAAIteasNGFPGW 184
Cdd:cd16026 2 PNIVVILADDLGYGDLGCYGSpLIKTPNIDRLAAEGVRFTDFYAAApVCSPSRAALLTGRYPVRVGLPGV----VGPPGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 185 AGRIPPQAATIAQVLQDNGYSTFWLGKNH--NVPEqdvaeggdrkTWPLGQGFERYYGfIGGETNQWYPDLVEDNH---- 258
Cdd:cd16026 78 KGGLPPDEITIAEVLKKAGYRTALVGKWHlgHQPE----------FLPTRHGFDEYFG-IPYSNDMWPFPLYRNDPpgpl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 259 -----FVEPPSSPENGYHLSKDLADQAISMIQNQKatspSKPWFMFYNPGANHAPHQAPQeyiaKYKGKFDGGydAYrsw 333
Cdd:cd16026 147 pplmeNEEVIEQPADQSSLTQRYTDEAVDFIERNK----DQPFFLYLAHTMPHVPLFASE----KFKGRSGAG--LY--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 334 vlarmiekgvmpkgtqlteinpipesqanpADAVrpwdtltpderklfsrmaevfagfsEYTDAQVGRVVDYLEQSGQLD 413
Cdd:cd16026 214 ------------------------------GDVV-------------------------EELDWSVGRILDALKELGLEE 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 414 NTIVLYAADNG-TSGEGSPNGSvnenkffngypddiaenmklidqlggpntyehfptgwatafSTPFRMFKrYAQYSGGT 492
Cdd:cd16026 239 NTLVIFTSDNGpWLEYGGHGGS-----------------------------------------AGPLRGGK-GTTWEGGV 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 493 ADPLVISWPKGIKArGELRDQYHHSVDIVPTLLDIVGIEMPkvyhgvEQFPLSGVSMKYTFEASPDAPTQKKRQFYSMLG 572
Cdd:cd16026 277 RVPFIAWWPGVIPA-GTVSDELASTMDLLPTLAALAGAPLP------EDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGD 349
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2024616551 573 TRGIWEDGWLAATVHAPFTGRG-----HFDQDQWQLFHVDADRSESTDLA 617
Cdd:cd16026 350 LQAVRSGRWKLHLPTTYRTGTDpggldPTKLEPPLLYDLEEDPGETYNVA 399
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
107-632 |
6.60e-41 |
|
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: 154.64 E-value: 6.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDD---TGLAAwspYGG-GINMPTLDKLAANGLTYTQ------WHTvALCSPTRSTLLTGRNhtLNGmaaiTE 176
Cdd:cd16155 3 PNILFILADDqraDTIGA---LGNpEIQTPNLDRLARRGTSFTNaynmggWSG-AVCVPSRAMLMTGRT--LFH----AP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 177 ASNGFPgwagrIPPQAATIAQVLQDNGYSTFWLGKNHNvpeqdvaeggdrktwplgqgferyygfiggetnqwypdlved 256
Cdd:cd16155 73 EGGKAA-----IPSDDKTWPETFKKAGYRTFATGKWHN------------------------------------------ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 257 nhfveppsspengyhlskDLADQAISMIQNQKATspSKPWFMFYNPGANHAPHQAPQEYIAKYKgkfdggydayrswvla 336
Cdd:cd16155 106 ------------------GFADAAIEFLEEYKDG--DKPFFMYVAFTAPHDPRQAPPEYLDMYP---------------- 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 337 rmiekgvmPKGTQLTEiNPIPESQANPAD-AVR-----PWDtLTPDERKlfSRMAEVFAgFSEYTDAQVGRVVDYLEQSG 410
Cdd:cd16155 150 --------PETIPLPE-NFLPQHPFDNGEgTVRdeqlaPFP-RTPEAVR--QHLAEYYA-MITHLDAQIGRILDALEASG 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 411 QLDNTIVLYAADNGTS-GEgspngsvnenkffNGYpddiaenmklidqLGGPNTYEHfptgwatafstPFRMfkryaqys 489
Cdd:cd16155 217 ELDNTIIVFTSDHGLAvGS-------------HGL-------------MGKQNLYEH-----------SMRV-------- 251
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 490 ggtadPLVISWPkGIKArGELRDQ--YHHsvDIVPTLLDIVGIEMPKvyhGVEqfplsGVSMKytfeasP--DAPTQKKR 565
Cdd:cd16155 252 -----PLIISGP-GIPK-GKRRDAlvYLQ--DVFPTLCELAGIEIPE---SVE-----GKSLL------PviRGEKKAVR 308
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024616551 566 Q--FYSMLG-TRGIWEDGW-LAATVHApftgrghfdQDQWQLFHVDADRSESTDLAKQ--YPEKLEALKKAWL 632
Cdd:cd16155 309 DtlYGAYRDgQRAIRDDRWkLIIYVPG---------VKRTQLFDLKKDPDELNNLADEpeYQERLKKLLAELK 372
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
107-617 |
3.01e-38 |
|
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: 147.31 E-value: 3.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGlaaWSPYG----GGINMPTLDKLAANGLTYTQWHTVALCSPTRSTLLTGRNHTLNGMaaiteasNGFP 182
Cdd:cd16029 1 PHIVFILADDLG---WNDVGfhgsDQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGM-------QHGV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 183 GWAGR---IPPQAATIAQVLQDNGYSTFWLGKNHNvpeqdvaeGGDRKTW-PLGQGFERYYGFIGGETN-------QWYP 251
Cdd:cd16029 71 ILAGEpygLPLNETLLPQYLKELGYATHLVGKWHL--------GFYTWEYtPTNRGFDSFYGYYGGAEDyythtsgGAND 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 252 DLVEDNHFVEPPSSPENGYHLSKDLADQAISMIQNQKatsPSKPWFMFYNPGANHAPHQAPQEYIAKYKGKFDGGYDayr 331
Cdd:cd16029 143 YGNDDLRDNEEPAWDYNGTYSTDLFTDRAVDIIENHD---PSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKD--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 332 swvlarmiekgvmpkgtqlteinpipesqanpadavrpwdtltpDERKLFSRMAEVFagfseytDAQVGRVVDYLEQSGQ 411
Cdd:cd16029 217 --------------------------------------------EDRRTYAAMVSAL-------DESVGNVVDALKAKGM 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 412 LDNTIVLYAADNGtsgeGSPNGSvnenkffngypddiaenmklidqLGGPNtyehfptgWatafstPFRMFKrYAQYSGG 491
Cdd:cd16029 246 LDNTLIVFTSDNG----GPTGGG-----------------------DGGSN--------Y------PLRGGK-NTLWEGG 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 492 TADPLVISWPKGIKARGELRDQYHHSVDIVPTLLDIVGIEMPkvyhgvEQFPLSGVSMKYTFEASPDAPtqkkRQfySML 571
Cdd:cd16029 284 VRVPAFVWSPLLPPKRGTVSDGLMHVTDWLPTLLSLAGGDPD------DLPPLDGVDQWDALSGGAPSP----RT--EIL 351
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2024616551 572 gtrgiwedgwLAATVHAPFTGRGHFDQDQW------QLFHVDADRSESTDLA 617
Cdd:cd16029 352 ----------LNIDDITRTTGGAAIRVGDWklivgkPLFNIENDPCERNDLA 393
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
107-538 |
3.69e-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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 147.33 E-value: 3.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVL-----YDDTGLAAWSPygggINMPTLDKLAANGLTYTQ-WHTVALCSPTRSTLLTGRNHTLNGMAAiteasNG 180
Cdd:cd16034 2 PNILFIFadqhrAQALGCAGDDP----VKTPNLDRLAKEGVVFTNaVSNYPVCSPYRASLLTGQYPLTNGVFG-----ND 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 181 FPgwagrIPPQAATIAQVLQDNGYSTFWLGKNH-NVPEQDvAEGGDRKTWP--LGQGFERYYGFiggETNQWYPD-LVED 256
Cdd:cd16034 73 VP-----LPPDAPTIADVLKDAGYRTGYIGKWHlDGPERN-DGRADDYTPPpeRRHGFDYWKGY---ECNHDHNNpHYYD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 257 NhfvEPPSSPENGYHlSKDLADQAISMIQNQKatSPSKPWFMFYNPGANHAPHQ-APQEYIAKYKgkfdggydayrswvl 335
Cdd:cd16034 144 D---DGKRIYIKGYS-PDAETDLAIEYLENQA--DKDKPFALVLSWNPPHDPYTtAPEEYLDMYD--------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 336 armiekgvmpkgtqlteinpiPESQANPADAvrpwdtltPDERKLFSRMAEVFAGFseYT-----DAQVGRVVDYLEQSG 410
Cdd:cd16034 203 ---------------------PKKLLLRPNV--------PEDKKEEAGLREDLRGY--YAmitalDDNIGRLLDALKELG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 411 QLDNTIVLYAADNGTSGeGSpNGSVNENKFFNgypddiaENMKLidqlggpntyehfptgwatafstpfrmfkryaqysg 490
Cdd:cd16034 252 LLENTIVVFTSDHGDML-GS-HGLMNKQVPYE-------ESIRV------------------------------------ 286
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2024616551 491 gtadPLVISWPKGIKARGElRDQYHHSVDIVPTLLDIVGIEMPKVYHG 538
Cdd:cd16034 287 ----PFIIRYPGKIKAGRV-VDLLINTVDIMPTLLGLCGLPIPDTVEG 329
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
107-539 |
2.10e-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: 137.18 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGG-INMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRNHTLNGMAaiteasnGFPGW 184
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPdIKTPNLDRLAAEGVRFTNAYVASpVCSPSRASLLTGRYPHRHGVR-------GNVGN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 185 AGRIPPQAATIAQVLQDNGYSTFWLGKNHnvpeqdvaeggdrktwplgqgferyygfiggetnqwypdlvednhfvepps 264
Cdd:cd16022 74 GGGLPPDEPTLAELLKEAGYRTALIGKWH--------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 265 spengyhlskdlaDQAISMIQNQKatsPSKPWFMFYNPganHAPHqAPqeyiakykgkfdggydayrsWVLARMIekgvm 344
Cdd:cd16022 103 -------------DEAIDFIERRD---KDKPFFLYVSF---NAPH-PP--------------------FAYYAMV----- 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 345 pkgtqlteinpipesqanpadavrpwdtltpderklfsrmaevfagfsEYTDAQVGRVVDYLEQSGQLDNTIVLYAADNG 424
Cdd:cd16022 138 ------------------------------------------------SAIDDQIGRILDALEELGLLDNTLIVFTSDHG 169
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 425 tsgegspngsvnenkffngypddiaenmkliDQLGGPNTyehfptgwatafstpfrMFKRYAQYSGGTADPLVISWPKGI 504
Cdd:cd16022 170 -------------------------------DMLGDHGL-----------------RGKKGSLYEGGIRVPFIVRWPGKI 201
|
410 420 430
....*....|....*....|....*....|....*
gi 2024616551 505 KArGELRDQYHHSVDIVPTLLDIVGIEMPKVYHGV 539
Cdd:cd16022 202 PA-GQVSDALVSLLDLLPTLLDLAGIEPPEGLDGR 235
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
107-638 |
3.18e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 135.81 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGGI-NMPTLDKLAANGLTYTQWHTV-ALCSPTRSTLLTGRNHTLNGMAAITEASNGFpgw 184
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIvKTPNIDRLAAEGVRFTNAYTPsPVCCPARASLLTGLYPHEHGVLNNVENAGAY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 185 AGRIPPQAATIAQVLQDNGYSTFWLGKNHNVPEQdvaeggdrktWPLGQGFEryygfiggetnqwypDLVEDNHFVEpps 264
Cdd:cd16033 78 SRGLPPGVETFSEDLREAGYRNGYVGKWHVGPEE----------TPLDYGFD---------------EYLPVETTIE--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 265 spengyhlsKDLADQAISMIqnQKATSPSKPWFM---FYNPganHAPHQAPQEYIAKYKG---KFDGGYDAYrswvlarM 338
Cdd:cd16033 130 ---------YFLADRAIEML--EELAADDKPFFLrvnFWGP---HDPYIPPEPYLDMYDPediPLPESFADD-------F 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 339 IEKgvmpkgtqlteinpiPESQANPAdavRPWDTLTPDERKlFSRMAEVFAGFSEYTDAQVGRVVDYLEQSGQLDNTIVL 418
Cdd:cd16033 189 EDK---------------PYIYRRER---KRWGVDTEDEED-WKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVI 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 419 YAADNGtsgegspngsvnenkffngypddiaenmkliDQLGgpntyEHfptgwatafstpfRMF-KRYAQYSGGTADPLV 497
Cdd:cd16033 250 FTSDHG-------------------------------DALG-----AH-------------RLWdKGPFMYEETYRIPLI 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 498 ISWPKGIKArGELRDQYHHSVDIVPTLLDIVGIEMPKVYHGVEQFPLsgvsmkYTFEASPDAPTQKKRQFY---SMLGTR 574
Cdd:cd16033 281 IKWPGVIAA-GQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPL------LRGEQPEDWRDEVVTEYNgheFYLPQR 353
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024616551 575 GIWEDGWlaatvHAPFTGrghFDQDqwQLFHVDADRSESTDLA--KQYPEKLEALKKAWLEEAKAN 638
Cdd:cd16033 354 MVRTDRY-----KYVFNG---FDID--ELYDLESDPYELNNLIddPEYEEILREMRTRLYEWMEET 409
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
107-538 |
8.48e-34 |
|
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: 134.21 E-value: 8.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDD--TGLAAWSPYggginMPTLDKLAANGLTYTQWH-TVALCSPTRSTLLTGR---NHtlnGMAAITEASNG 180
Cdd:cd16147 2 PNIVLILTDDqdVELGSMDPM-----PKTKKLLADQGTTFTNAFvTTPLCCPSRASILTGQyahNH---GVTNNSPPGGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 181 FPGWAGRIPPQaATIAQVLQDNGYSTFWLGK---NHNVPeqdvaegGDRKTWPlgQGFERYYGFIGGETNQWYpdLVEDN 257
Cdd:cd16147 74 YPKFWQNGLER-STLPVWLQEAGYRTAYAGKylnGYGVP-------GGVSYVP--PGWDEWDGLVGNSTYYNY--TLSNG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 258 HFVEPPSSPENGYhlSKD-LADQAISMIQNQKATspSKPWFMFYNPGANHAPHQ-APQeyiakYKGKFDGGYDAYR---- 331
Cdd:cd16147 142 GNGKHGVSYPGDY--LTDvIANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTpAPR-----YANLFPNVTAPPRpppn 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 332 --------SWVLARMiekgvmpkgtqlteinPIPESQANPADAVRpwdtltpdeRK-LFSRMAevfagfseyTDAQVGRV 402
Cdd:cd16147 213 npdvsdkpHWLRRLP----------------PLNPTQIAYIDELY---------RKrLRTLQS---------VDDLVERL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 403 VDYLEQSGQLDNTIVLYAADNGtsgegspngsvnenkfFNgypddiaenmklidqLGgpntyEH-FPTGWATAFSTPFRM 481
Cdd:cd16147 259 VNTLEATGQLDNTYIIYTSDNG----------------YH---------------LG-----QHrLPPGKRTPYEEDIRV 302
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024616551 482 fkryaqysggtadPLVISWPkGIKARGELRDQYHHsVDIVPTLLDIVGIEMPKVYHG 538
Cdd:cd16147 303 -------------PLLVRGP-GIPAGVTVDQLVSN-IDLAPTILDLAGAPPPSDMDG 344
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
107-550 |
3.63e-31 |
|
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.
Pssm-ID: 293754 [Multi-domain] Cd Length: 435 Bit Score: 127.30 E-value: 3.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDtgLAAW-SPYGG-GINMPTLDKLAANGLTYTQWHT-VALCSPTRSTLLTGRNHTLNGMAaiteasnGFPG 183
Cdd:cd16030 3 PNVLFIAVDD--LRPWlGCYGGhPAKTPNIDRLAARGVLFTNAYCqQPVCGPSRASLLTGRRPDTTGVY-------DNNS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 184 WAGRIPPQAATIAQVLQDNGYSTFWLGK---NHNVPEQDVAEGGDRKTW-PLGQGFERYYGFIGGETNQWYpdlvEDNHF 259
Cdd:cd16030 74 YFRKVAPDAVTLPQYFKENGYTTAGVGKifhPGIPDGDDDPASWDEPPNpPGPEKYPPGKLCPGKKGGKGG----GGGPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 260 VEPPSSPENGYhlsKD--LADQAISMIQNQKATSpsKPWFM---FYNPganHAPHQAPQEYiakykgkfdggYDAY--RS 332
Cdd:cd16030 150 WEAADVPDEAY---PDgkVADEAIEQLRKLKDSD--KPFFLavgFYKP---HLPFVAPKKY-----------FDLYplES 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 333 WVLARMIEKGVMPKgTQLTEINPIPESQANPADAVRPWDTLTPDE-RKLFSR--MAEVfagfsEYTDAQVGRVVDYLEQS 409
Cdd:cd16030 211 IPLPNPFDPIDLPE-VAWNDLDDLPKYGDIPALNPGDPKGPLPDEqARELRQayYASV-----SYVDAQVGRVLDALEEL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 410 GQLDNTIVLYAADNGTsgegspngsvnenkffngypddiaenmklidQLGgpntyEHfpTGWAtafstpfrmfKrYAQYS 489
Cdd:cd16030 285 GLADNTIVVLWSDHGW-------------------------------HLG-----EH--GHWG----------K-HTLFE 315
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024616551 490 GGTADPLVISWPkGIKARGELRDQYHHSVDIVPTLLDIVGIEMPKvyhgveqfPLSGVSMK 550
Cdd:cd16030 316 EATRVPLIIRAP-GVTKPGKVTDALVELVDIYPTLAELAGLPAPP--------CLEGKSLV 367
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
107-616 |
4.40e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 123.09 E-value: 4.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGG-GINMPTLDKLAANGLTYTQWHTVALCSPTRSTLLTGRNHTLNGMaaiteasngfpgWA 185
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGeSYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYV------------VF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 186 GRIPPQAATIAQVLQDNGYSTF----W-LGKNHNVPEQ------------DVAEGGDRKTWPLGQGFERYYGFIGGETNQ 248
Cdd:cd16151 69 GYLDPKQKTFGHLLKDAGYATAiagkWqLGGGRGDGDYphefgfdeyclwQLTETGEKYSRPATPTFNIRNGKLLETTEG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 249 WY-PDLVednhfveppsspengyhlskdlADQAISMIQNQKAtspsKPWFMFYNPGANHAPHQapqeyiakykgkfdggy 327
Cdd:cd16151 149 DYgPDLF----------------------ADFLIDFIERNKD----QPFFAYYPMVLVHDPFV----------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 328 dayrswvlarmiekgvmpkgtqlteinPIPESqanpadavRPWDtltPDERKLFSRMaEVFAGFSEYTDAQVGRVVDYLE 407
Cdd:cd16151 186 ---------------------------PTPDS--------PDWD---PDDKRKKDDP-EYFPDMVAYMDKLVGKLVDKLE 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 408 QSGQLDNTIVLYAADNGTSGEGS--PNGS-VNENKffngypddiaenMKLIDQlggpntyehfptgwatafstpfrmfkr 484
Cdd:cd16151 227 ELGLRENTIIIFTGDNGTHRPITsrTNGReVRGGK------------GKTTDA--------------------------- 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 485 yaqysgGTADPLVISWPKGIKARGELrDQYHHSVDIVPTLLDIVGIEMPKVYH--GVEQFP-LSGVSmkytfeaspdaPT 561
Cdd:cd16151 268 ------GTHVPLIVNWPGLIPAGGVS-DDLVDFSDFLPTLAELAGAPLPEDYPldGRSFAPqLLGKT-----------GS 329
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024616551 562 QKKRQFYsmlgtrgiwedgWLAATVHAPFTGRGHFDQDqW------QLFHVDADRSESTDL 616
Cdd:cd16151 330 PRREWIY------------WYYRNPHKKFGSRFVRTKR-YklyadgRFFDLREDPLEKNPL 377
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
107-539 |
7.09e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 108.02 E-value: 7.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDdtglaAW-----SPYGGGIN-MPTLDKLAANGLTYTQWHTVAL-CSPTRSTLLTGRNHTLNGmaaiteasn 179
Cdd:cd16148 1 MNVILIVID-----SLradhlGCYGYDRVtTPNLDRLAAEGVVFDNHYSGSNpTLPSRFSLFTGLYPFYHG--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 180 gfpGWAGRIPPQAATIAQVLQDNGYSTFWLGKNHNVPEQdvaeggdrktWPLGQGFERYYGFIGGETnqwypdlvednhf 259
Cdd:cd16148 67 ---VWGGPLEPDDPTLAEILRKAGYYTAAVSSNPHLFGG----------PGFDRGFDTFEDFRGQEG------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 260 veppSSPENGYHLSKDLADQAISMIQNQKAtspSKPWFMFYNPGANHAPHQapqeyiakykgkfdggYDAyrswvlarmi 339
Cdd:cd16148 121 ----DPGEEGDERAERVTDRALEWLDRNAD---DDPFFLFLHYFDPHEPYL----------------YDA---------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 340 ekgvmpkgtqlteinpipesqanpadAVRpwdtltpderklfsrmaevfagfseYTDAQVGRVVDYLEQSGQLDNTIVLY 419
Cdd:cd16148 168 --------------------------EVR-------------------------YVDEQIGRLLDKLKELGLLEDTLVIV 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 420 AADNGTsgegspngSVNENKFFNGypddiaENMKLIDQLggpntyehfptgwatafstpfrmfkryaqysggTADPLVIS 499
Cdd:cd16148 197 TSDHGE--------EFGEHGLYWG------HGSNLYDEQ---------------------------------LHVPLIIR 229
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2024616551 500 WPKgiKARGELRDQYHHSVDIVPTLLDIVGIEMPKVYHGV 539
Cdd:cd16148 230 WPG--KEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGR 267
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
105-634 |
3.03e-25 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 110.53 E-value: 3.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 105 GAPNILFVLYD----DTGLAAWSPYgggINMPTLDKLAANGLTYTQWHT-VALCSPTRSTLLTG---RNHTLNGMAaiTE 176
Cdd:PRK13759 5 KKPNIILIMVDqmrgDCLGCNGNKA---VETPNLDMLASEGYNFENAYSaVPSCTPARAALLTGlsqWHHGRVGYG--DV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 177 ASNGFPgwagrippqaATIAQVLQDNGYSTFWLGKNHNVPEQ-----------DVAEGGDRKTWPLGQGF-ERYYGFIGG 244
Cdd:PRK13759 80 VPWNYK----------NTLPQEFRDAGYYTQCIGKMHVFPQRnllgfhnvllhDGYLHSGRNEDKSQFDFvSDYLAWLRE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 245 ETNQWYPDL----VEDNHFVEPPSSPENGYHLSKDLADQAISMIQNQkatSPSKPWFMFYNPGANHAPHQAPQEYIAKYK 320
Cdd:PRK13759 150 KAPGKDPDLtdigWDCNSWVARPWDLEERLHPTNWVGSESIEFLRRR---DPTKPFFLKMSFARPHSPYDPPKRYFDMYK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 321 GkfdggydayrswvlaRMIEKGVMPKGTQLTEinPIPEsQANPaDAVRpwdTLTPDERKLFSRMAevFAGFSEYTDAQVG 400
Cdd:PRK13759 227 D---------------ADIPDPHIGDWEYAED--QDPE-GGSI-DALR---GNLGEEYARRARAA--YYGLITHIDHQIG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 401 RVVDYLEQSGQLDNTIVLYAADNGtsgegspngsvnenkffngypddiaenmkliDQLGgpntyEHFptgwatafstpfr 480
Cdd:PRK13759 283 RFLQALKEFGLLDNTIILFVSDHG-------------------------------DMLG-----DHY------------- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 481 MFKRYAQYSGGTADPLVISWPKGIKA--RGELRDQYHHSVDIVPTLLDIVGIEMPKvyhgveqfPLSGVSMKYTFEASPD 558
Cdd:PRK13759 314 LFRKGYPYEGSAHIPFIIYDPGGLLAgnRGTVIDQVVELRDIMPTLLDLAGGTIPD--------DVDGRSLKNLIFGQYE 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 559 APtqkkRQFYSMLGTRGIWEDGWLAATVHAP--FTGRGHFdqdqwQLFHVDADRSESTDLA--KQYPEKLEALKKAWLEE 634
Cdd:PRK13759 386 GW----RPYLHGEHALGYSSDNYLTDGKWKYiwFSQTGEE-----QLFDLKKDPHELHNLSpsEKYQPRLREMRKKLVDH 456
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
107-538 |
4.13e-25 |
|
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: 109.27 E-value: 4.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDtglaaW-----SPYGGG-INMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGR---NHtlnGMAAite 176
Cdd:cd16028 1 RNVLFITADQ-----WradclSCLGHPlVKTPNLDRLAAEGVRFRNHYTQAaPCGPSRASLYTGRylmNH---RSVW--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 177 asNGFPGWAGRippqaATIAQVLQDNGYSTFWLGKNHNVPEQD-VAEGGDRKTWPLG--QGFeRYYGFIGGetnqwYPDL 253
Cdd:cd16028 70 --NGTPLDARH-----LTLALELRKAGYDPALFGYTDTSPDPRgLAPLDPRLLSYELamPGF-DPVDRLDE-----YPAE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 254 VEDNHFveppsspengyhlskdLADQAISMIQNQkatsPSKPWFM---FYNPganHAPHQAPQEYiakykgkfdggyday 330
Cdd:cd16028 137 DSDTAF----------------LTDRAIEYLDER----QDEPWFLhlsYIRP---HPPFVAPAPY--------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 331 rswvlARMIEKGVMP----KGTQLTEINPIP--------ESQANPADAVRPWDTLTPDERKlfsRMAEVFAGFSEYTDAQ 398
Cdd:cd16028 179 -----HALYDPADVPppirAESLAAEAAQHPllaaflerIESLSFSPGAANAADLDDEEVA---QMRATYLGLIAEVDDH 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 399 VGRVVDYLEQSGQLDNTIVLYAADNGtsgegspngsvnenkffngypddiaenmkliDQLGgpntyEHFPTGWATAFSTP 478
Cdd:cd16028 251 LGRLFDYLKETGQWDDTLIVFTSDHG-------------------------------EQLG-----DHWLWGKDGFFDQA 294
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024616551 479 FRMfkryaqysggtadPLVISWPKGI--KARGELRDQYHHSVDIVPTLLDIVGIEMPKVYHG 538
Cdd:cd16028 295 YRV-------------PLIVRDPRREadATRGQVVDAFTESVDVMPTILDWLGGEIPHQCDG 343
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
107-549 |
4.29e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 106.91 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTglAAWSPYGGG---INMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRNHTLNGMAaiteaSNGFP 182
Cdd:cd16035 1 PNILLILTDQE--RYPPPWPAGwaaLNLPARERLAANGLSFENHYTAAcMCSPSRSTLYTGLHPQQTGVT-----DTLGS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 183 GWAGRIPPQAATIAQVLQDNGYSTFWLGKNHnvpeqdvaeggdrktwplgqgferyygfIGGETNQwypdlvednhfvep 262
Cdd:cd16035 74 PMQPLLSPDVPTLGHMLRAAGYYTAYKGKWH----------------------------LSGAAGG-------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 263 psspenGYHLSKDLADQAISMIQNQKATSPS-KPWFMFYNpganhaphqapqeyiakykgkFdggydayrswvlarmiek 341
Cdd:cd16035 112 ------GYKRDPGIAAQAVEWLRERGAKNADgKPWFLVVS---------------------L------------------ 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 342 gvmpkgtqlteinpipesqANPADAVrpwdtLTPDERKLFSRMAEVFAGFSEYTDAQVGRVVDYLEQSGQLDNTIVLYAA 421
Cdd:cd16035 147 -------------------VNPHDIM-----FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTS 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 422 DNGTSGeGSPNGSVnenKFFNGYpddiAENMKLidqlggpntyehfptgwatafstpfrmfkryaqysggtadPLVISWP 501
Cdd:cd16035 203 DHGEMG-GAHGLRG---KGFNAY----EEALHV----------------------------------------PLIISHP 234
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2024616551 502 kGIKARGELRDQYHHSVDIVPTLLDIVGIemPKVYHGVEQFPLSGVSM 549
Cdd:cd16035 235 -DLFGTGQTTDALTSHIDLLPTLLGLAGV--DAEARATEAPPLPGRDL 279
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
107-593 |
1.21e-24 |
|
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: 108.24 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGG-GINMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRNHTLNGMaaiteasngfpgW 184
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNkAMKTPNLDRLAAEGVRFDSAYTTQpVCGPARSGLFTGLYPHTNGS------------W 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 185 AGRIPP--QAATIAQVLQDNGYSTFWLGKNHnvpeqdvAEGGDrktwplgqgferYYGF----IGGETNQWY------PD 252
Cdd:cd16156 69 TNCMALgdNVKTIGQRLSDNGIHTAYIGKWH-------LDGGD------------YFGNgicpQGWDPDYWYdmrnylDE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 253 LVEDNHFV--EPPSSPEnGYHLSKD------LADQAISMIQNQKatspSKPWFMFYNPGANHAPHQAPQEYIAKYKG-KF 323
Cdd:cd16156 130 LTEEERRKsrRGLTSLE-AEGIKEEftyghrCTNRALDFIEKHK----DEDFFLVVSYDEPHHPFLCPKPYASMYKDfEF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 324 DGGYDAYRSwvlarmIEKGvmpkgtqlteinpiPESQanpadavRPW--DTLTPDERKLFSRMAEVFaGFSEYTDAQVGR 401
Cdd:cd16156 205 PKGENAYDD------LENK--------------PLHQ-------RLWagAKPHEDGDKGTIKHPLYF-GCNSFVDYEIGR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 402 VVDYLEQsgQLDNTIVLYAADNGtsgegspngsvnenkffngypdDIAENMKLidQLGGPNTYEHFptgwatafstpfrm 481
Cdd:cd16156 257 VLDAADE--IAEDAWVIYTSDHG----------------------DMLGAHKL--WAKGPAVYDEI-------------- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 482 fkryaqysggTADPLVISWPKGIKArgELRDQYHHS-VDIVPTLLDIVGIEMPKVyhgveqfpLSGVSMKYTFEaspDAP 560
Cdd:cd16156 297 ----------TNIPLIIRGKGGEKA--GTVTDTPVShIDLAPTILDYAGIPQPKV--------LEGESILATIE---DPE 353
|
490 500 510
....*....|....*....|....*....|....
gi 2024616551 561 TQKKRQFYSMLGTRGIWEDGWLA-ATVHAPFTGR 593
Cdd:cd16156 354 IPENRGVFVEFGRYEVDHDGFGGfQPVRCVVDGR 387
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
107-544 |
1.19e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 100.89 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGGI---NMPTLDKLAANGLTYTQ-WHTVAlCSPTRSTLLTGRNHTLNGMAAIteasngfp 182
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSdlpVTPTLDSLANSGIVFDNlWATPA-CSPTRATILTGKYGFRTGVLAV-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 183 gwAGRIPPQAATIAQVLQDN----GYSTFWLGKNHnvpeqdvaEGGDRKTWPLGQGFERYYGFIGGETNQWYP-DLVEDN 257
Cdd:cd16154 72 --PDELLLSEETLLQLLIKDattaGYSSAVIGKWH--------LGGNDNSPNNPGGIPYYAGILGGGVQDYYNwNLTNNG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 258 HfveppSSPENGYHLSKdLADQAISMIQNQkatspSKPWFMF--YNpgANHAPHQAPqeyiakykgkfdggydayrswvl 335
Cdd:cd16154 142 Q-----TTNSTEYATTK-LTNLAIDWIDQQ-----TKPWFLWlaYN--APHTPFHLP----------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 336 armiekgvmpkgtqlteinpipesqanPADAVRPwdTLTPDER-----KLFSRMAEVfagfsEYTDAQVGRVVDYLEQSg 410
Cdd:cd16154 186 ---------------------------PAELHSR--SLLGDSAdieanPRPYYLAAI-----EAMDTEIGRLLASIDEE- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 411 QLDNTIVLYAADNGTsgegsPNGSVNENKFFNGypddiAENmklidqlggpntyehfptgwatafstpfrmfkryAQYSG 490
Cdd:cd16154 231 ERENTIIIFIGDNGT-----PGQVVDLPYTRNH-----AKG----------------------------------SLYEG 266
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2024616551 491 GTADPLVISwPKGIKARGELRDQYHHSVDIVPTLLDIVGIEMPKVYHGVEQFPL 544
Cdd:cd16154 267 GINVPLIVS-GAGVERANERESALVNATDLYATIAELAGVDAAEIHDSVSFKPL 319
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
107-677 |
1.25e-22 |
|
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: 102.14 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGGINM-PTLDKLAANGLTYTQWH-TVALCSPTRSTLLTGRNHTLNGMAAiteasnG--FP 182
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSStPNLDRLAANGLRFTDFYsSSPVCSPSRAALLTGRYQVRSGVYP------GvfYP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 183 GWAGRIPPQAATIAQVLQDNGYSTFWLGKNHnvpeqdVAEGGDRKTWPLGQGFERYYGfIGGETNQ--------WYPD-- 252
Cdd:cd16158 76 GSRGGLPLNETTIAEVLKTVGYQTAMVGKWH------LGVGLNGTYLPTHQGFDHYLG-IPYSHDQgpcqnltcFPPNip 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 253 -------------LVEDNHFVEPPSSPENGYHLSKDLADQAISmiqnqKATSPSKPWFMFYnpgANHAPHQaPQEYIAKY 319
Cdd:cd16158 149 cfggcdqgevpcpLFYNESIVQQPVDLLTLEERYAKFAKDFIA-----DNAKEGKPFFLYY---ASHHTHY-PQFAGQKF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 320 KGKFDGGydayrswvlarmiekgvmPKGTQLTEInpipesqanpadavrpwdtltpderklfsrmaevfagfseytDAQV 399
Cdd:cd16158 220 AGRSSRG------------------PFGDALAEL------------------------------------------DGSV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 400 GRVVDYLEQSGQLDNTIVLYAADNGTSGEGSPNGSVnenkffngypddiAENMKlidqLGGPNTYEhfptgwatafstpf 479
Cdd:cd16158 240 GELLQTLKENGIDNNTLVFFTSDNGPSTMRKSRGGN-------------AGLLK----CGKGTTYE-------------- 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 480 rmfkryaqysGGTADPLVISWPKGIK--ARGELRDqyhhSVDIVPTLLDIVGIEMPKV-YHGVEQFPL---SGVSMKYTF 553
Cdd:cd16158 289 ----------GGVREPAIAYWPGRIKpgVTHELAS----TLDILPTIAKLAGAPLPNVtLDGVDMSPIlfeQGKSPRQTF 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 554 EASPDAPTQKKRQFYSMLG-------TRGIWEDGWLAATVHAPFTGRGHFDQDqwQLFHVDADRSESTDLAKQyPEKLEA 626
Cdd:cd16158 355 FYYPTSPDPDKGVFAVRWGkykahfyTQGAAHSGTTPDKDCHPSAELTSHDPP--LLFDLSQDPSENYNLLGL-PEYNQV 431
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2024616551 627 LKKAWLEEAKANLALPVddrPAPEILGVERPSGEPVRDryvyyPGTSPVPE 677
Cdd:cd16158 432 LKQIQQVKERFEASMKF---GESEINKGEDPALEPCCK-----PGCTPKPS 474
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
106-544 |
7.79e-22 |
|
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: 98.70 E-value: 7.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 106 APNILFVLYDDTGL----AAWSPygGGINMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRNHTLNGMAaiteaSNG 180
Cdd:cd16161 1 KPNFLLLFADDLGWgdlgANWAP--NAILTPNLDKLAAEGTRFVDWYSAAsVCSPSRASLMTGRLGLRNGVG-----HNF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 181 FPGWAGRIPPQAATIAQVLQDNGYSTFWLGKNHNvpeqdvaegGDRKTW-PLGQGFERYYGFiggetnqwypdlvednhf 259
Cdd:cd16161 74 LPTSVGGLPLNETTLAEVLRQAGYATGMIGKWHL---------GQREAYlPNSRGFDYYFGI------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 260 vepPSSpeNGYHLSKDLADQAISMIQNqkATSPSKPWFMFYNPGANHAPHQAPQEYIAKYKGkfDGGYdayrswvlarmi 339
Cdd:cd16161 127 ---PFS--HDSSLADRYAQFATDFIQR--ASAKDRPFFLYAALAHVHVPLANLPRFQSPTSG--RGPY------------ 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 340 ekgvmpkgtqlteinpipesqanpADAVRPWDTLtpderklfsrmaevfagfseytdaqVGRVVDYLEQSGQLDNTIVLY 419
Cdd:cd16161 186 ------------------------GDALQEMDDL-------------------------VGQIMDAVKHAGLKDNTLTWF 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 420 AADNGTsgegspngsvnenkffngyPDDIAEnmklidqlggpntYEHFPTGWATAFSTPFRMFKRyAQYSGGTADPLVIS 499
Cdd:cd16161 217 TSDNGP-------------------WEVKCE-------------LAVGPGTGDWQGNLGGSVAKA-STWEGGHREPAIVY 263
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2024616551 500 WPKGIKArGELRDQYHHSVDIVPTLLDIVGIEMP--KVYHGVEQFPL 544
Cdd:cd16161 264 WPGRIPA-NSTSAALVSTLDIFPTVVALAGASLPpgRIYDGKDLSPV 309
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
107-544 |
1.24e-20 |
|
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: 93.76 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGG-INMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRnhtlngMAAITEASNGFPGW 184
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPvVRTPNLDRLAARGTRFENAYTPSpICVPSRASFLTGR------YVHETGVWDNADPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 185 AGRIPpqaaTIAQVLQDNGYSTFWLGKNHnvpeqdvaeggdrktwplgqgferyygFIGGetnqwypdlvEDNHfvepps 264
Cdd:cd16037 75 DGDVP----SWGHALRAAGYETVLIGKLH---------------------------FRGE----------DQRH------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 265 spenGYHLSKDLADQAISMIQNQKATspSKPWFM---FYNPganHAPHQAPQEYiakykgkfdggYDAYrswvlarmiek 341
Cdd:cd16037 108 ----GFRYDRDVTEAAVDWLREEAAD--DKPWFLfvgFVAP---HFPLIAPQEF-----------YDLY----------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 342 gvmpkgtqlteinpipesqanpadaVRpwdtltpderklfsrmaEVFAGFS---EYTDAQVGRVVDYLEQSGQLDNTIVL 418
Cdd:cd16037 157 -------------------------VR-----------------RARAAYYglvEFLDENIGRVLDALEELGLLDNTLII 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 419 YAADNGtsgegspngsvnenkffngypddiaenmkliDQLGgpntyEHfptG--WATAFstpfrmfkryaqYSGGTADPL 496
Cdd:cd16037 195 YTSDHG-------------------------------DMLG-----ER---GlwGKSTM------------YEESVRVPM 223
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2024616551 497 VISWPkGIKArGELRDQYHHSVDIVPTLLDIVGIEMPKVYHGVEQFPL 544
Cdd:cd16037 224 IISGP-GIPA-GKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPL 269
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
132-538 |
6.60e-20 |
|
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: 93.07 E-value: 6.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 132 PTLDKLAANGL----TYTQwHTValCSPTRSTLLTGR-NHTlngmaaiteasNGFPGWAGRIPPQAATIAQVLQDNGYST 206
Cdd:cd16150 27 PNLDALAAEGVrfsnAYCQ-NPV--CSPSRCSFLTGWyPHV-----------NGHRTLHHLLRPDEPNLLKTLKDAGYHV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 207 FWLGKNHNVPEQDVAEGgdrktwplgqgferyygfiggetnqwYPDlvEDNHFVEppsspengyhlskdladQAISMIQN 286
Cdd:cd16150 93 AWAGKNDDLPGEFAAEA--------------------------YCD--SDEACVR-----------------TAIDWLRN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 287 qkaTSPSKPWFMFYNPGANHAPHQAPQEYiakykgkFDggydayrswvlarMIEKGVMPKGTqlteinPIPESQANPADA 366
Cdd:cd16150 128 ---RRPDKPFCLYLPLIFPHPPYGVEEPW-------FS-------------MIDREKLPPRR------PPGLRAKGKPSM 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 367 VRP-----WDTLTpDERklFSRMAEVFAGFSEYTDAQVGRVVDYLEQSGQLDNTIVLYAADNGtsgegspngsvnenkff 441
Cdd:cd16150 179 LEGiekqgLDRWS-EER--WRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHG----------------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 442 nGYPDD--IAENmklidqlggpntyehfptgWATAFSTPFrmfkryaqysggTADPLVISWPKGIKARgeLRDQYHHSVD 519
Cdd:cd16150 239 -DYTGDygLVEK-------------------WPNTFEDCL------------TRVPLIIKPPGGPAGG--VSDALVELVD 284
|
410
....*....|....*....
gi 2024616551 520 IVPTLLDIVGIEMPKVYHG 538
Cdd:cd16150 285 IPPTLLDLAGIPLSHTHFG 303
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
107-534 |
5.83e-19 |
|
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: 90.99 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGG-GINMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRNHTLNGMAAITE-ASNGF-- 181
Cdd:cd16157 2 PNIILMLMDDMGWGDLGVFGEpSRETPNLDRMAAEGMLFTDFYSANpLCSPSRAALLTGRLPIRNGFYTTNAhARNAYtp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 182 PGWAGRIPPQAATIAQVLQDNGYSTFWLGKNHnvpeqdvaEGGDRKTWPLGQGFERYYG----FIGGETNQWYP------ 251
Cdd:cd16157 82 QNIVGGIPDSEILLPELLKKAGYRNKIVGKWH--------LGHRPQYHPLKHGFDEWFGapncHFGPYDNKAYPnipvyr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 252 -DLVEDNHFVEPPSSPENG-YHLSKDLADQAISMIQNQKATSpsKPWFMFYNPGANHAPHQAPQEYIAKY-KGKFdggyd 328
Cdd:cd16157 154 dWEMIGRYYEEFKIDKKTGeSNLTQIYLQEALEFIEKQHDAQ--KPFFLYWAPDATHAPVYASKPFLGTSqRGLY----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 329 ayrswvlarmiekgvmpkgtqlteinpipesqanpADAVRPwdtltpderklfsrmaevfagfseyTDAQVGRVVDYLEQ 408
Cdd:cd16157 227 -----------------------------------GDAVME-------------------------LDSSVGKILESLKS 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 409 SGQLDNTIVLYAADNGTSGEGSPngsvnenkffngypddiaenmklidQLGGPNtyehfptgwatafsTPFRMFKRyAQY 488
Cdd:cd16157 247 LGIENNTFVFFSSDNGAALISAP-------------------------EQGGSN--------------GPFLCGKQ-TTF 286
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2024616551 489 SGGTADPLVISWPKGIKArGELRDQYHHSVDIVPTLLDIVGIEMPK 534
Cdd:cd16157 287 EGGMREPAIAWWPGHIKP-GQVSHQLGSLMDLFTTSLALAGLPIPS 331
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
107-534 |
5.84e-19 |
|
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: 91.20 E-value: 5.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGG-INMPTLDKLAANGLTYTQwHTVA--LCSPTRSTLLTGRNHTLNGMAA-ITEASNGFP 182
Cdd:cd16159 2 PNIVLFMADDLGIGDVGCFGNDtIRTPNIDRLAKEGVKLTH-HLAAapLCTPSRAAFLTGRYPIRSGMASsHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 183 GWAGRIPPQAATIAQVLQDNGYSTFWLGKNHnvPEQDVAEGGDRKTWPLGQGFERYYGF-------IGGETNQ------- 248
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWH--LGLHCESRNDFCHHPLNHGFDYFYGLpltnlkdCGDGSNGeydlsfd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 249 -WYPD-----------------------------------------------------LVEDNHFVEPPSSPENgyhLSK 274
Cdd:cd16159 159 pLFPLltafvlitaltiflllylgavskrffvfllilsllfislfflllitnryfnciLMRNHEVVEQPMSLEN---LTQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 275 DLADQAISMIQNQKatspSKPWFMFYNPGANHAP-HQAPqeyiaKYKGKfdggydayrswvlarmiekgvmpkgtqltei 353
Cdd:cd16159 236 RLTKEAISFLERNK----ERPFLLVMSFLHVHTAlFTSK-----KFKGR------------------------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 354 npipeSQANP-ADAVrpwdtltpderklfsrmaevfagfsEYTDAQVGRVVDYLEQSGQLDNTIVLYAADNGtsgegspn 432
Cdd:cd16159 276 -----SKHGRyGDNV-------------------------EEMDWSVGQILDALDELGLKDNTFVYFTSDNG-------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 433 gsvnenkffnGYPDDIAENmkliDQLGGpntyehfptGWATafstpFRMFKRYAQYSGGTADPLVISWPKGIKARGELrD 512
Cdd:cd16159 318 ----------GHLEEISVG----GEYGG---------GNGG-----IYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVI-D 368
|
490 500
....*....|....*....|..
gi 2024616551 513 QYHHSVDIVPTLLDIVGIEMPK 534
Cdd:cd16159 369 EPTSLMDIFPTVAALAGAPLPS 390
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
107-533 |
2.34e-18 |
|
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: 88.64 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGgginMPT-----LDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRNHTLNGMAAITEASng 180
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYG----HPTqergpIDDMAAEGIRFTQAYSADsVCTPSRAALLTGRLPIRSGMYGGTRVF-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 181 FPGWAGRIPPQAATIAQVLQDNGYSTFWLGKNH---NVPEQDvaeggDRKTWPLGQGFErYYGFIGGETNQWYPD----- 252
Cdd:cd16160 76 LPWDIGGLPKTEVTMAEALKEAGYTTGMVGKWHlgiNENNHS-----DGAHLPSHHGFD-FVGTNLPFTNSWACDdtgrh 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 253 ----------LVEDNHFVEPPSSPEngyHLSKDLADQAISMIQnqkaTSPSKPWFMFYNPGANHAPHQAPQEYIAKYKgk 322
Cdd:cd16160 150 vdfpdrsacfLYYNDTIVEQPIQHE---HLTETLVGDAKSFIE----DNQENPFFLYFSFPQTHTPLFASKRFKGKSK-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 323 fDGGYdayrswvlarmiekgvmpkGTQLTEInpipeSQAnpadavrpwdtltpderklfsrmaevfagfseytdaqVGRV 402
Cdd:cd16160 221 -RGRY-------------------GDNINEM-----SWA-------------------------------------VGEV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 403 VDYLEQSGQLDNTIVLYAADNGTSGE-----GSPNGsvnenkfFNGypddiaenmklidqlGGPNTYEhfptgwatafst 477
Cdd:cd16160 239 LDTLVDTGLDQNTLVFFLSDHGPHVEyclegGSTGG-------LKG---------------GKGNSWE------------ 284
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024616551 478 pfrmfkryaqysGGTADPLVISWPKGIKARgeLRDQYHHSVDIVPTLLDIVGIEMP 533
Cdd:cd16160 285 ------------GGIRVPFIAYWPGTIKPR--VSHEVVSTMDIFPTFVDLAGGTLP 326
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
107-533 |
3.45e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 82.29 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGG-INMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRnhtlngMAA-------ITEA 177
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSeAVTPNLDRLAAEGVRFENFFCTSpVCSPARASLLTGR------MPSqhgihdwIVEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 178 SNGFPGWAGRIPPQAATIAQVLQDNGYSTFWLGKnhnvpeqdvaeggdrktWPLGQgferyygfiggetnqwypdlvedn 257
Cdd:cd16149 75 SHGKTKKPEGYLEGQTTLPEVLQDAGYRCGLSGK-----------------WHLGD------------------------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 258 hfveppsspengyhlskdlaDQAISMIQNQKAtspSKPWFMFYNPGANHAPHQapqeYIAKYKGkfdggydayrswvlar 337
Cdd:cd16149 114 --------------------DAADFLRRRAEA---EKPFFLSVNYTAPHSPWG----YFAAVTG---------------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 338 miekgvmpkgtqlteinpipesqanpadavrpwdtltpderklfsrmaevfagfseyTDAQVGRVVDYLEQSGQLDNTIV 417
Cdd:cd16149 151 ---------------------------------------------------------VDRNVGRLLDELEELGLTENTLV 173
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 418 LYAADNGTS-------GEGspNGSvnenkffngYPddiaenmklidqlggPNTYEhfptgwatafsTPFRMfkryaqysg 490
Cdd:cd16149 174 IFTSDNGFNmghhgiwGKG--NGT---------FP---------------LNMYD-----------NSVKV--------- 207
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2024616551 491 gtadPLVISWPKGIKARGELRDQYHHsVDIVPTLLDIVGIEMP 533
Cdd:cd16149 208 ----PFIIRWPGVVPAGRVVDSLVSA-YDFFPTLLELAGVDPP 245
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
107-549 |
1.20e-15 |
|
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: 78.77 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGGI-NMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRnhtlngMAAITEA-SNgfpg 183
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVvKTPNLDRLAARGVVFDNAYCNSpLCAPSRASMMTGR------LPSRIGAyDN---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 184 wAGRIPPQAATIAQVLQDNGYSTFWLGKNHnvpeqdvaeggdrktwplgqgferyygFIGgetnqwyPDLVednHfvepp 263
Cdd:cd16032 71 -AAEFPADIPTFAHYLRAAGYRTALSGKMH---------------------------FVG-------PDQL---H----- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 264 sspenGYHLSKDLADQAISMIQNQKATSPSKPWFM---FYNPganHAPHQAPQEYiakykgkfdggYDAYrswvlarmie 340
Cdd:cd16032 108 -----GFDYDEEVAFKAVQKLYDLARGEDGRPFFLtvsFTHP---HDPYVIPQEY-----------WDLY---------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 341 kgvmpkgtqlteinpipesqanpadaVRPwdtltpderklfSRMAeVFAGFSeYTDAQVGRVVDYLEQSGQLDNTIVLYA 420
Cdd:cd16032 159 --------------------------VRR------------ARRA-YYGMVS-YVDDKVGQLLDTLERTGLADDTIVIFT 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 421 ADNGtsgegspngsvnenkffngypddiaenmkliDQLGgpntyEHfptG-WatafstpfrmFKRyAQYSGGTADPLVIS 499
Cdd:cd16032 199 SDHG-------------------------------DMLG-----ER---GlW----------YKM-SFFEGSARVPLIIS 228
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2024616551 500 WPkGIKARGELRDQYHHsVDIVPTLLDIVGIEMPkvyHGVEqfPLSGVSM 549
Cdd:cd16032 229 AP-GRFAPRRVAEPVSL-VDLLPTLVDLAGGGTA---PHVP--PLDGRSL 271
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
107-634 |
1.54e-15 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 79.19 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYD----DT-GLaawspYGGGINM-PTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRNHTLNGMAaiteaSN 179
Cdd:cd16152 2 PNVIVFFTDqqrwDTlGC-----YGQPLDLtPNLDALAEEGVLFENAFTPQpVCGPARACLQTGLYPTETGCF-----RN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 180 GFPgwagrIPPQAATIAQVLQDNGYSTfwlgknhnvpeqdvaeggdrktwplgqgferyyGFIGgetnQWypdlvednhf 259
Cdd:cd16152 72 GIP-----LPADEKTLAHYFRDAGYET---------------------------------GYVG----KW---------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 260 veppsspengyHLSK----DLADQAISMIQNQKAtspSKPWFMFynpgANH-APHQ--------APQEYIAKYKGKFdgg 326
Cdd:cd16152 100 -----------HLAGyrvdALTDFAIDYLDNRQK---DKPFFLF----LSYlEPHHqndrdryvAPEGSAERFANFW--- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 327 ydayrswvlarmiekgvmpkgtqlteinpIPES-QANPADavrpWDTLTPDerklfsrmaevFAGFSEYTDAQVGRVVDY 405
Cdd:cd16152 159 -----------------------------VPPDlAALPGD----WAEELPD-----------YLGCCERLDENVGRIRDA 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 406 LEQSGQLDNTIVLYAADNGTsgegspngsvnenkffngypddiaenmklidqlggpntyeHFPTgwatafstpfrmfkRY 485
Cdd:cd16152 195 LKELGLYDNTIIVFTSDHGC----------------------------------------HFRT--------------RN 220
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 486 AQYSGGTAD-----PLVISWPkGIKaRGELRDQYHHSVDIVPTLLDIVGIEMPKVYHGVEQFPLsgvsmkytfeASPDAP 560
Cdd:cd16152 221 AEYKRSCHEssirvPLVIYGP-GFN-GGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPL----------VDGKVE 288
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 561 TQKKRQFY----SMLGtRGIWEDGWLAAtVHAP-FTGRGHFDQD---QWQLFHVDADRSESTDLA--KQYPEKLEALKKA 630
Cdd:cd16152 289 DWRNEVFIqiseSQVG-RAIRTDRWKYS-VAAPdKDGWKDSGSDvyvEDYLYDLEADPYELVNLIgrPEYREVAAELRER 366
|
....
gi 2024616551 631 WLEE 634
Cdd:cd16152 367 LLAR 370
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
84-536 |
3.88e-15 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 79.31 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 84 ELDIRQSVPDWGPFTPKKAPEGAPNILFVLYDDTGLAAWSPYGGGIN-MPTLDKLAANGLTYTQwhtvaLCSPTrstllt 162
Cdd:COG1368 212 ALEIKKYLKSNRPTPNPFGPAKKPNVVVILLESFSDFFIGALGNGKDvTPFLDSLAKESLYFGN-----FYSQG------ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 163 grNHTLNGMAAITeasNGFPGWAGRIP------PQAATIAQVLQDNGYST-FWLGknhnvpeqDVAEGGDRKTWPLGQGF 235
Cdd:COG1368 281 --GRTSRGEFAVL---TGLPPLPGGSPykrpgqNNFPSLPSILKKQGYETsFFHG--------GDGSFWNRDSFYKNLGF 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 236 ERYYGfiggetnqwypdlveDNHFVEPpssPENGYHLS-KDLADQAISMIQNQKatspsKPWFMFYNPGANHAPHQAPQE 314
Cdd:COG1368 348 DEFYD---------------REDFDDP---FDGGWGVSdEDLFDKALEELEKLK-----KPFFAFLITLSNHGPYTLPEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 315 Y--IAKYKGKFDGGYdayrswvlarmiekgvmpkgtqlteinpipesqanpADAVRpwdtltpderklfsrmaevfagfs 392
Cdd:COG1368 405 DkkIPDYGKTTLNNY------------------------------------LNAVR------------------------ 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 393 eYTDAQVGRVVDYLEQSGQLDNTIVLYAADNGTSGEGSPNGSVNENKffngypddiaenmklidqlggpntyehfptgwa 472
Cdd:COG1368 425 -YADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENPLER--------------------------------- 470
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024616551 473 taFSTPFrMFkryaqYSGGTADPLVIswpkgikargelrDQYHHSVDIVPTLLDIVGIEMPKVY 536
Cdd:COG1368 471 --YRVPL-LI-----YSPGLKKPKVI-------------DTVGSQIDIAPTLLDLLGIDYPSYY 513
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
107-213 |
3.63e-10 |
|
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: 61.62 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYG-----------GGINMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRNHTLNGM--- 171
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNnahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSpVCVPSRTSMLTGRYPHRTGVygf 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2024616551 172 -AAITEASNGFPgwagrippqaaTIAQVLQDNGYSTFWLGKNH 213
Cdd:cd16153 82 eAAHPALDHGLP-----------TFPEVLKKAGYQTASFGKSH 113
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
107-439 |
9.23e-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: 60.39 E-value: 9.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVL---YDDTglaAWSPYGGGIN-MPTLDKLAANGLTYTqwHTVALCSPTRS-----TLLTGRNHTLNGMAAITEA 177
Cdd:cd16015 1 PNVIVILlesFSDP---YIDKDVGGEDlTPNLNKLAKEGLYFG--NFYSPGFGGGTangefEVLTGLPPLPLGSGSYTLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 178 SNgfpgwagripPQAATIAQVLQDNGYSTFWLgknHNvpeqDVAEGGDRKTWPLGQGFERYYGfiggetnqwYPDLVEDN 257
Cdd:cd16015 76 KL----------NPLPSLPSILKEQGYETIFI---HG----GDASFYNRDSVYPNLGFDEFYD---------LEDFPDDE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 258 HFveppsspENGYHLS-KDLADQAISMIQNQKAtspsKPWFMFYNPGANHAPHQAPQEYIAKYKGKfdggydayrswvla 336
Cdd:cd16015 130 KE-------TNGWGVSdESLFDQALEELEELKK----KPFFIFLVTMSNHGPYDLPEEKKDEPLKV-------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 337 rmiekgvmpkgtqlteinpipesqanpadavrpwdtltPDERKLFSRMAEVFAgfseYTDAQVGRVVDYLEQSGQLDNTI 416
Cdd:cd16015 185 --------------------------------------EEDKTELENYLNAIH----YTDKALGEFIEKLKKSGLYENTI 222
|
330 340
....*....|....*....|...
gi 2024616551 417 VLYAADNGTSGEGSPNGSVNENK 439
Cdd:cd16015 223 IVIYGDHLPSLGSDYDETDEDPL 245
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
107-609 |
3.50e-09 |
|
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: 59.48 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDD-TGLAAWSPYGGGINMPTLDKLAANGLTYTQWHTVA-LCSPTRSTLLTGRnHTlngmaAITEASNGFPGw 184
Cdd:cd16171 1 PNVVMVMSDSfDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSpICCPSRAAMWSGL-FT-----HLTESWNNYKG- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 185 agrIPPQAATIAQVLQDNGYSTFWLGKnhnvpeQDVAEGgDRKTWPLGQGFERYYGFIGGETNQWYPDLVEDNHFVEPps 264
Cdd:cd16171 74 ---LDPNYPTWMDRLEKHGYHTQKYGK------LDYTSG-HHSVSNRVEAWTRDVPFLLRQEGRPTVNLVGDRSTVRV-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 265 spengyhLSKDLA--DQAISMIQNQkATSPSKPWFMFYnpGANhAPHQAPQEYIakykGKFDGGYDAYRSWVLARMIEkg 342
Cdd:cd16171 142 -------MLKDWQntDKAVHWIRKE-APNLTQPFALYL--GLN-LPHPYPSPSM----GENFGSIRNIRAFYYAMCAE-- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 343 vmpkgtqlteinpipesqanpadavrpwdtltpderklfsrmaevfagfseyTDAQVGRVVDYLEQSGQLDNTIVLYAAD 422
Cdd:cd16171 205 ----------------------------------------------------TDAMLGEIISALKDTGLLDKTYVFFTSD 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 423 NGtsgegspngsvnenkffngypdDIAenmklidqlggpntYEHfptgwatafstpfRMFKRYAQYSGGTADPLVISWPk 502
Cdd:cd16171 233 HG----------------------ELA--------------MEH-------------RQFYKMSMYEGSSHVPLLIMGP- 262
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 503 GIKArGELRDQYHHSVDIVPTLLDIVGIEMPKVYHGVEQFPLSGVSMKYTFEASPDAPTQKKRQFYSM---LGTRGIWED 579
Cdd:cd16171 263 GIKA-GQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLLSESSIKESPSRVPHPDWVLSEFHGCnvnASTYMLRTN 341
|
490 500 510
....*....|....*....|....*....|
gi 2024616551 580 GWlaatvhaPFTGRGHFDQDQWQLFHVDAD 609
Cdd:cd16171 342 SW-------KYIAYADGNSVPPQLFDLSKD 364
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
107-210 |
6.92e-09 |
|
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: 57.43 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 107 PNILFVLYDDTGLAAWSPYGGGINM-PTLDKLAANGlTYTQWHTVALCS---PTRSTLLTGRNHTLNGMAAITEASNGFP 182
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTtPNLKRLASEG-ATFNFRSVSPPTssaPNHAALLTGAYPTLHGYTGNGSADPELP 79
|
90 100
....*....|....*....|....*...
gi 2024616551 183 GWAGRIPPQAATIAQVLQDNGYSTFWLG 210
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG 107
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
254-525 |
3.49e-08 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 57.22 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 254 VEDNHFVEPPSSPENgyhlSKDLADQAISMIQNQkatSPSKPWF--MFYNpganhAPH--QAPQEYIAKYKgkfdggyda 329
Cdd:COG3083 348 VSLPRLHTPGGPAQR----DRQITAQWLQWLDQR---DSDRPWFsyLFLD-----APHaySFPADYPKPFQ--------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 330 yrswvlarmiekgvmpkgtqlteinpiPESQANPADAVRPWDTLTPDERKLFSRMaevfagfseYTDAQVGRVVDYLEQS 409
Cdd:COG3083 407 ---------------------------PSEDCNYLALDNESDPTPFKNRYRNAVH---------YVDSQIGRVLDTLEQR 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024616551 410 GQLDNTIVLYAADNGTsgegspngSVNENkffngypddiaenmklidqlgGPNTYEHfptgwATAFStpfrmfkRYaQys 489
Cdd:COG3083 451 GLLENTIVIITADHGE--------EFNEN---------------------GQNYWGH-----NSNFS-------RY-Q-- 486
|
250 260 270
....*....|....*....|....*....|....*....
gi 2024616551 490 ggTADPLVISWPkGIKARgelrdQYHH---SVDIVPTLL 525
Cdd:COG3083 487 --LQVPLVIHWP-GTPPQ-----VISKltsHLDIVPTLM 517
|
|
| DUF4994 |
pfam16385 |
Domain of unknown function; This family around 100 residues locates in the C-terminal of some ... |
602-628 |
7.02e-04 |
|
Domain of unknown function; This family around 100 residues locates in the C-terminal of some uncharacterized proteins in various Bacteroides and Prevotella species. The function of this family remains unknown.
Pssm-ID: 406720 [Multi-domain] Cd Length: 98 Bit Score: 39.58 E-value: 7.02e-04
10 20
....*....|....*....|....*..
gi 2024616551 602 QLFHVDADRSESTDLAKQYPEKLEALK 628
Cdd:pfam16385 69 QLYDLKADPGEQENVAKKHPEKVKELQ 95
|
|
| |
