|
Name |
Accession |
Description |
Interval |
E-value |
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-465 |
0e+00 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 591.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMGHCRIRANSSVRGQDHLL 109
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 110 SEDITVAEVLKGAGYTTGFIGKWGIGLPGTEGAPDKQGFDFSYGYYDQARAHGFFPHYLMRNGKPEPIPENYGFnmkrvs 189
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHPTKQGFDYFYGYLDQVHAHNYYPEYLWRNGEKVPLPNNVIP------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 190 tyngrpvdrlddvknvydengNLVPDGVPVAAAAKYSEDLFQDEALSFIKKNRDKPFFLYYATQLPHGPCITPDLGAYKD 269
Cdd:cd16145 155 ---------------------PLDEGNNAGGGGGTYSHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDDGPYKY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 270 K----------PWDLKHKEWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGYSQWGYFgrsrnEDDYLFKNKGPW 339
Cdd:cd16145 214 KpkdpgiyaylPWPQPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSEGGS-----EHDPDFFDSNGP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 340 PKGKFTSTHEGGVRVPFFVYWKDKIKAG-ENDHICALYDVLATLADLASITPPKN-DGISFAPILLGKPDEQeTHQYLYW 417
Cdd:cd16145 289 LRGYKRSLYEGGIRVPFIARWPGKIPAGsVSDHPSAFWDFMPTLADLAGAEPPEDiDGISLLPTLLGKPQQQ-QHDYLYW 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 149137229 418 ENGTMsRHAQSIRLNQWWAYRDHPSK-PIELYDITEDFACKNDLAKSNP 465
Cdd:cd16145 368 EFYEG-GGAQAVRMGGWKAVRHGKKDgPFELYDLSTDPGETNNLAAQHP 415
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-477 |
2.80e-110 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 333.77 E-value: 2.80e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 1 MKKISSLKYLFVVAAMTGSAvfgqghMAKPNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAP 80
Cdd:COG3119 1 MKRLLLLLLALLAAAAAAAA------AKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 81 SRGSLMTGMHMGHCRIRANSSvRGQDHLLSEDITVAEVLKGAGYTTGFIGKWGIglpgtegapdkqgfdfsygyydqara 160
Cdd:COG3119 75 SRASLLTGRYPHRTGVTDNGE-GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL-------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 161 hgffphylmrngkpepipenygfnmkrvstyngrpvdrlddvknvydengnlvpdgvpvaaaakYSEDLFQDEALSFIKK 240
Cdd:COG3119 128 ----------------------------------------------------------------YLTDLLTDKAIDFLER 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 241 NR--DKPFFLYYATQLPHGPCITPD--LGAYKDK---------PWDLKHKEW-------AAMLGHLDRGVGRMLDLMEQL 300
Cdd:COG3119 144 QAdkDKPFFLYLAFNAPHAPYQAPEeyLDKYDGKdiplppnlaPRDLTEEELrraraayAAMIEEVDDQVGRLLDALEEL 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 301 EILDNTIIFFAGDNGYS--QWGYFGRsrneddylfknKGpwpkgkftSTHEGGVRVPFFVYWKDKIKAGE-NDHICALYD 377
Cdd:COG3119 224 GLADNTIVVFTSDNGPSlgEHGLRGG-----------KG--------TLYEGGIRVPLIVRWPGKIKAGSvSDALVSLID 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 378 VLATLADLASITPPKN-DGISFAPILLGKpdEQETHQYLYWENGTMSRHaQSIRLNQWWAYRDHPSK-PIELYDITEDFA 455
Cdd:COG3119 285 LLPTLLDLAGVPIPEDlDGRSLLPLLTGE--KAEWRDYLYWEYPRGGGN-RAIRTGRWKLIRYYDDDgPWELYDLKNDPG 361
|
490 500
....*....|....*....|..
gi 149137229 456 CKNDLAKSNPELIDRIRQIFTE 477
Cdd:COG3119 362 ETNNLAADYPEVVAELRALLEA 383
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-473 |
8.95e-105 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 320.64 E-value: 8.95e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMH-------------MGHCRI 96
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYparlgitdvipgrRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 97 RANSSVRGQDHLLSEDITVAEVLKGAGYTTGFIGKWGIGLPGTEGaPDKQGFDFSYGYYDQARAHGFFPHYLMRNGKPEP 176
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYG-PEDQGFDVNIGGTGNGGPPSYYFPPGKPNPDLED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 177 IPENygfnmkrvstynGRPVDRLddvknvydengnlvpdgvpvaaaakysedlfQDEALSFIKKNRDKPFFLYYATQLPH 256
Cdd:cd16144 160 GPEG------------EYLTDRL-------------------------------TDEAIDFIEQNKDKPFFLYLSHYAVH 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 257 GPCIT-PDLGAY---KDKPWDLKHK--EWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGysqwgyfGRSRNEDD 330
Cdd:cd16144 197 TPIQArPELIEKyekKKKGLRKGQKnpVYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNG-------GLSTRGGP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 331 YLfkNKGPWPKGKfTSTHEGGVRVPFFVYWKDKIKAG-ENDHICALYDVLATLADLASITPPKN---DGISFAPILLGkP 406
Cdd:cd16144 270 PT--SNAPLRGGK-GSLYEGGIRVPLIVRWPGVIKPGsVSDVPVIGTDLYPTFLELAGGPLPPPqhlDGVSLVPLLKG-G 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149137229 407 DEQETHQYLYW----ENGTMSRHAQSIRLNQWWAYRDHPSKPIELYDITEDFACKNDLAKSNPELIDRIRQ 473
Cdd:cd16144 346 EADLPRRALFWhfphYHGQGGRPASAIRKGDWKLIEFYEDGRVELYNLKNDIGETNNLAAEMPEKAAELKK 416
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
30-475 |
6.71e-103 |
|
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: 315.26 E-value: 6.71e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSgSSECAPSRGSLMTGMHmgHCRIRANSSVRGQDHLL 109
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHV-SPVCAPTRAALLTGRY--PFRTGVWHTILGRERMR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 110 SEDITVAEVLKGAGYTTGFIGKWGIGLPgTEGAPDKQGFDFSYGYYDQAraHGFFPHYlmrngkpepiPENYGFNmkrvs 189
Cdd:cd16146 78 LDETTLAEVFKDAGYRTGIFGKWHLGDN-YPYRPQDRGFDEVLGHGGGG--IGQYPDY----------WGNDYFD----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 190 tyngrpvdrlddvkNVYDENGNLVPDGvpvaaaaKYSEDLFQDEALSFIKKNRDKPFFLYYATQLPHGPCITPD--LGAY 267
Cdd:cd16146 140 --------------DTYYHNGKFVKTE-------GYCTDVFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDkyLDPY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 268 KDKPWDLKHKEWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGySQWGYFGRsrneddylFkNKGpwPKGKFTST 347
Cdd:cd16146 199 KDMGLDDKLAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNG-PAGGVPKR--------F-NAG--MRGKKGSV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 348 HEGGVRVPFFVYWKDKIKAG-ENDHICALYDVLATLADLASITPPKN---DGISFAPILLGKPDEQETHQYLY----WEN 419
Cdd:cd16146 267 YEGGHRVPFFIRWPGKILAGkDVDTLTAHIDLLPTLLDLCGVKLPEGiklDGRSLLPLLKGESDPWPERTLFThsgrWPP 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 149137229 420 GTMSRHAQSIRLNQwWAYRDHPSKPIELYDITEDFACKNDLAKSNPELIDRIRQIF 475
Cdd:cd16146 347 PPKKKRNAAVRTGR-WRLVSPKGFQPELYDIENDPGEENDVADEHPEVVKRLKAAY 401
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
29-461 |
3.78e-92 |
|
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: 287.15 E-value: 3.78e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMGHCRIRANSSVRGQDHL 108
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 109 LSED-ITVAEVLKGAGYTTGFIGKWGIG-LPGTegAPDKQGFDFSYGyydqarahgffphylmrngkpepIPenYGFNMK 186
Cdd:cd16026 81 LPPDeITIAEVLKKAGYRTALVGKWHLGhQPEF--LPTRHGFDEYFG-----------------------IP--YSNDMW 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 187 RVSTYNGRPvdRLDDVKNVYDENgnlvpdgvPVAAAAKYSE--DLFQDEALSFIKKNRDKPFFLYYATQLPHGPCITPDL 264
Cdd:cd16026 134 PFPLYRNDP--PGPLPPLMENEE--------VIEQPADQSSltQRYTDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 265 -------GAYKDkpwdlkhkewaaMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNG-YSQWGYFGRSRneddylfknk 336
Cdd:cd16026 204 fkgrsgaGLYGD------------VVEELDWSVGRILDALKELGLEENTLVIFTSDNGpWLEYGGHGGSA---------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 337 GPWPKGKFTsTHEGGVRVPFFVYWKDKIKAGE-NDHICALYDVLATLADLASITPPKN---DGISFAPILLGKPDEqETH 412
Cdd:cd16026 262 GPLRGGKGT-TWEGGVRVPFIAWWPGVIPAGTvSDELASTMDLLPTLAALAGAPLPEDrviDGKDISPLLLGGSKS-PPH 339
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149137229 413 QYLYWENGTmsrHAQSIRLNQW-----WAYRDHPS---------KPIELYDITEDFACKNDLA 461
Cdd:cd16026 340 PFFYYYDGG---DLQAVRSGRWklhlpTTYRTGTDpggldptklEPPLLYDLEEDPGETYNVA 399
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-460 |
7.23e-86 |
|
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: 270.24 E-value: 7.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSgSSECAPSRGSLMTGMHmghcRIRaNSSVRGQDHll 109
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKY----NFR-NYVVFGYLD-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 110 SEDITVAEVLKGAGYTTGFIGKWGIG-LPGTEGAPDKQGFD----FSYGYYDQARAHGFFPHYLMRNGKPepipenygfn 184
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGKWQLGgGRGDGDYPHEFGFDeyclWQLTETGEKYSRPATPTFNIRNGKL---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 185 mkrVSTYNGrpvdrlddvknvydengnlvpdgvpvaaaaKYSEDLFQDEALSFIKKNRDKPFFLYYATQLPHGP-CITPD 263
Cdd:cd16151 143 ---LETTEG------------------------------DYGPDLFADFLIDFIERNKDQPFFAYYPMVLVHDPfVPTPD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 264 LG--AYKDKPWDLKHKEWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGYsqwgyfgrsrNEDDYLFKNKGPWPK 341
Cdd:cd16151 190 SPdwDPDDKRKKDDPEYFPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGT----------HRPITSRTNGREVRG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 342 GKFTSThEGGVRVPFFVYWKDKIKAG-ENDHICALYDVLATLADLASITPPKN---DGISFAPILLGKPDEQEtHQYLYW 417
Cdd:cd16151 260 GKGKTT-DAGTHVPLIVNWPGLIPAGgVSDDLVDFSDFLPTLAELAGAPLPEDyplDGRSFAPQLLGKTGSPR-REWIYW 337
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 149137229 418 --ENGTMSRHAQSIRLNQWWAYRDHpskpiELYDITEDFACKNDL 460
Cdd:cd16151 338 yyRNPHKKFGSRFVRTKRYKLYADG-----RFFDLREDPLEKNPL 377
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-461 |
4.51e-84 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 266.37 E-value: 4.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQE-QFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHmgHCRIRANSSVRG--QD 106
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRY--PWRSRLKGGVLGgfSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 107 HLLSED-ITVAEVLKGAGYTTGFIGKWGIGL------PGTEGAPDKQGFDFSYGYYDQARAHGFfphylmrngkpepipe 179
Cdd:cd16143 79 PLIEPDrVTLAKMLKQAGYRTAMVGKWHLGLdwkkkdGKKAATGTGKDVDYSKPIKGGPLDHGF---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 180 NYGFnmkrvstyngrpvdrlddvknvydengnlvpdGVPVAAAAkyseDLFQDEALSFIKKNR--DKPFFLYYATQLPHG 257
Cdd:cd16143 143 DYYF--------------------------------GIPASEVL----PTLTDKAVEFIDQHAkkDKPFFLYFALPAPHT 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 258 PCITPD-------LGAYKDkpwdlkhkewaaMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGYSqwgYFGRSRNEDD 330
Cdd:cd16143 187 PIVPSPefqgksgAGPYGD------------FVYELDWVVGRILDALKELGLAENTLVIFTSDNGPS---PYADYKELEK 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 331 YLFKNKGPWpKGKFTSTHEGGVRVPFFVYWKDKIKAG-ENDHICALYDVLATLADLASITPPKN---DGISFAPILLGkP 406
Cdd:cd16143 252 FGHDPSGPL-RGMKADIYEGGHRVPFIVRWPGKIPAGsVSDQLVSLTDLFATLAAIVGQKLPDNaaeDSFSFLPALLG-P 329
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149137229 407 DEQETHQYLyWENGTMSRhaQSIRLNQWWAYRDHPSK--------------PIELYDITEDFACKNDLA 461
Cdd:cd16143 330 KKQEVRESL-VHHSGNGS--FAIRKGDWKLIDGTGSGgfsyprgkeklglpPGQLYNLSTDPGESNNLY 395
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
29-460 |
1.65e-73 |
|
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: 238.88 E-value: 1.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSSYGQEqFRTPNLDQLAMNGIRFTQAYSgSSECAPSRGSLMTGMH-----MGHCRIRANSSVR 103
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNFHT-TALCSPTRAALLTGRNhhqvgMGTMAELATGKPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 104 GQDHLLSEDITVAEVLKGAGYTTGFIGKWGIGlpgtegapdkqgfdfsygyydqarahgffphylmrngkpepiPENYgf 183
Cdd:cd16025 80 YEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG------------------------------------------PDDY-- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 184 nmkrvstyngrpvdrlddvknvydengnlvpdgvpvaaaakYSEDLFQDEALSFIKKNR--DKPFFLYYATQLPHGPCIT 261
Cdd:cd16025 116 -----------------------------------------YSTDDLTDKAIEYIDEQKapDKPFFLYLAFGAPHAPLQA 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 262 PD------LGAYKD--------------------------------KPWD---LKHKEW--------AAMLGHLDRGVGR 292
Cdd:cd16025 155 PKewidkyKGKYDAgwdalreerlerqkelglipadtkltprppgvPAWDslsPEEKKLearrmevyAAMVEHMDQQIGR 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 293 MLDLMEQLEILDNTIIFFAGDNGYS---QWGYFGRSrneddylfknkgPWPKGKFTsTHEGGVRVPFFVYWKDKIKAGE- 368
Cdd:cd16025 235 LIDYLKELGELDNTLIIFLSDNGASaepGWANASNT------------PFRLYKQA-SHEGGIRTPLIVSWPKGIKAKGg 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 369 -NDHICALYDVLATLADLASITPPKN---------DGISFAPILLGkPDEQETHQYLYWEngtMSRHAqSIRLNQWWAYR 438
Cdd:cd16025 302 iRHQFAHVIDIAPTILELAGVEYPKTvngvpqlplDGVSLLPTLDG-AAAPSRRRTQYFE---LFGNR-AIRKGGWKAVA 376
|
490 500
....*....|....*....|....*.
gi 149137229 439 DHPSKPI----ELYDITEDFACKNDL 460
Cdd:cd16025 377 LHPPPGWgdqwELYDLAKDPSETHDL 402
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
30-397 |
1.40e-71 |
|
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: 228.48 E-value: 1.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMGHCRIRANssVRGQDHLL 109
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 110 SEDITVAEVLKGAGYTTGFIGKWgiglpgtegapdkqgfdfsygyydqaraHgffphylmrngkpepipenygfnmkrvs 189
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIGKW----------------------------H---------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 190 tyngrpvdrlddvknvydengnlvpdgvpvaaaakysedlfqDEALSFIKKN-RDKPFFLYYATQLPHGPCitpdlgAYk 268
Cdd:cd16022 103 ------------------------------------------DEAIDFIERRdKDKPFFLYVSFNAPHPPF------AY- 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 269 dkpwdlkhkewAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGysqwGYFGRSRNeddylfknkgpwpKGKFTSTH 348
Cdd:cd16022 134 -----------YAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHG----DMLGDHGL-------------RGKKGSLY 185
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 149137229 349 EGGVRVPFFVYWKDKIKAG-ENDHICALYDVLATLADLASITPPKN-DGIS 397
Cdd:cd16022 186 EGGIRVPFIVRWPGKIPAGqVSDALVSLLDLLPTLLDLAGIEPPEGlDGRS 236
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
30-473 |
1.07e-70 |
|
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: 230.86 E-value: 1.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYrDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMH-----MGHCRIRANssvrg 104
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYphqngAHGLRSRGF----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 105 qdHLLSEDITVAEVLKGAGYTTGFIGKWGiglpgtegapdkqgfdfsygyydqarahgffphylmrngkpepipenygfn 184
Cdd:cd16027 75 --PLPDGVKTLPELLREAGYYTGLIGKTH--------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 185 mkrvstYNGRPVDRLDDVKNVYDENGNLVPDGVPVAAAakysedlfqdealsFIK-KNRDKPFFLYYATQLPHGPCITPD 263
Cdd:cd16027 102 ------YNPDAVFPFDDEMRGPDDGGRNAWDYASNAAD--------------FLNrAKKGQPFFLWFGFHDPHRPYPPGD 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 264 LGAYKDKPWDLK-----------HKEWAAMLG---HLDRGVGRMLDLMEQLEILDNTIIFFAGDNGysqwgyfgrsrned 329
Cdd:cd16027 162 GEEPGYDPEKVKvppylpdtpevREDLADYYDeieRLDQQVGEILDELEEDGLLDNTIVIFTSDHG-------------- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 330 dylfknkGPWPKGKfTSTHEGGVRVPFFVYWKDKIKAGE-NDHICALYDVLATLADLASITPPKN-DGISFAPILLGKPD 407
Cdd:cd16027 228 -------MPFPRAK-GTLYDSGLRVPLIVRWPGKIKPGSvSDALVSFIDLAPTLLDLAGIEPPEYlQGRSFLPLLKGEKD 299
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149137229 408 eqETHQYLYwenGTMSRHAQS---IRlnqwwAYRD------HPSKPIELYDITEDFACKNDLAkSNPELIDRIRQ 473
Cdd:cd16027 300 --PGRDYVF---AERDRHDETydpIR-----SVRTgrykyiRNYMPEELYDLKNDPDELNNLA-DDPEYAEVLEE 363
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
29-477 |
3.44e-70 |
|
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: 231.26 E-value: 3.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMghcriRANSSVRGQDHL 108
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYS-----HRHGVTDNNGPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 109 LSEDI-TVAEVLKGAGYTTGFIGKWGIglpGTEGAPDKQGFDFSYGYYDQaraHGFFPHYLMRNGKPEPIPenygfnmkr 187
Cdd:cd16031 77 FDASQpTYPKLLRKAGYQTAFIGKWHL---GSGGDLPPPGFDYWVSFPGQ---GSYYDPEFIENGKRVGQK--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 188 vstyngrpvdrlddvknvydengnlvpdgvpvaaaaKYSEDLFQDEALSFIKKNR-DKPFFLYYATQLPHGPCITPD--L 264
Cdd:cd16031 142 ------------------------------------GYVTDIITDKALDFLKERDkDKPFCLSLSFKAPHRPFTPAPrhR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 265 GAYKDKPW---------DLKHK-EWA-----------------------------AMLGHLDRGVGRMLDLMEQLEILDN 305
Cdd:cd16031 186 GLYEDVTIpepetfdddDYAGRpEWAreqrnrirgvldgrfdtpekyqrymkdylRTVTGVDDNVGRILDYLEEQGLADN 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 306 TIIFFAGDNGYS--QWGYFGRSrneddylfknkgpWPkgkftstHEGGVRVPFFVYWKDKIKAG-ENDHICALYDVLATL 382
Cdd:cd16031 266 TIIIYTSDNGFFlgEHGLFDKR-------------LM-------YEESIRVPLIIRDPRLIKAGtVVDALVLNIDFAPTI 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 383 ADLASITPPKN-DGISFAPILLGKPDEQETHQ--YLYWENGTMSRHAQS--IR-----LNQWWAYRDHPskpiELYDITE 452
Cdd:cd16031 326 LDLAGVPIPEDmQGRSLLPLLEGEKPVDWRKEfyYEYYEEPNFHNVPTHegVRterykYIYYYGVWDEE----ELYDLKK 401
|
490 500
....*....|....*....|....*
gi 149137229 453 DFACKNDLAkSNPELIDRIRQIFTE 477
Cdd:cd16031 402 DPLELNNLA-NDPEYAEVLKELRKR 425
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
30-461 |
3.23e-68 |
|
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: 224.74 E-value: 3.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSeCAPSRGSLMTG---MH--MGHCRIRANSSvrg 104
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGrypIHtgMQHGVILAGEP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 105 qDHLLSEDITVAEVLKGAGYTTGFIGKWGIGLPGTEGAPDKQGFDFSYGYYDQArahgffphylmrngkpepipENYgFN 184
Cdd:cd16029 77 -YGLPLNETLLPQYLKELGYATHLVGKWHLGFYTWEYTPTNRGFDSFYGYYGGA--------------------EDY-YT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 185 MKRVSTYNGRPVDRLDDVKNVYDENGnlvpdgvpvaaaaKYSEDLFQDEALSFIKK-NRDKPFFLYYATQLPHGPCITPD 263
Cdd:cd16029 135 HTSGGANDYGNDDLRDNEEPAWDYNG-------------TYSTDLFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLQVPP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 264 lgAYKDKP-------WDLKHKEWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGYSQWGYFGRSrNeddylfknk 336
Cdd:cd16029 202 --EYADPYedkfahiKDEDRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGGS-N--------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 337 gpWPK--GKFTsTHEGGVRVPFFVY---WKDKiKAGEND---HICalyDVLATLADLASITP---PKNDGISFAPILLGK 405
Cdd:cd16029 270 --YPLrgGKNT-LWEGGVRVPAFVWsplLPPK-RGTVSDglmHVT---DWLPTLLSLAGGDPddlPPLDGVDQWDALSGG 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149137229 406 PDEQET---HQYLYWenGTMSRHAqSIRLNQWwayrdhpsKPIE---LYDITEDFACKNDLA 461
Cdd:cd16029 343 APSPRTeilLNIDDI--TRTTGGA-AIRVGDW--------KLIVgkpLFNIENDPCERNDLA 393
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-453 |
8.45e-67 |
|
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: 221.29 E-value: 8.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMGHCRIRANssvrgqDHL 108
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGN------DVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 109 LSED-ITVAEVLKGAGYTTGFIGKW---GIGLPGTEGA------PDKQGFDFSYGYYdqARAHGFFPHYlmrngkpepip 178
Cdd:cd16034 75 LPPDaPTIADVLKDAGYRTGYIGKWhldGPERNDGRADdytpppERRHGFDYWKGYE--CNHDHNNPHY----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 179 enygfnmkrvstyngrpvdrlddvknvYDENGNLVpdgvpvaAAAKYSEDLFQDEALSFIK--KNRDKPFFLYYATQLPH 256
Cdd:cd16034 142 ---------------------------YDDDGKRI-------YIKGYSPDAETDLAIEYLEnqADKDKPFALVLSWNPPH 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 257 GPCIT---PDLGAYKDK--------PWDLKHKEWA--------AMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGys 317
Cdd:cd16034 188 DPYTTapeEYLDMYDPKklllrpnvPEDKKEEAGLredlrgyyAMITALDDNIGRLLDALKELGLLENTIVVFTSDHG-- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 318 qwgyfgrsrnedDYLFKNkGPWPKGKFtstHEGGVRVPFFVYWKDKIKAGENDHICA-LYDVLATLADLASITPPKN-DG 395
Cdd:cd16034 266 ------------DMLGSH-GLMNKQVP---YEESIRVPFIIRYPGKIKAGRVVDLLInTVDIMPTLLGLCGLPIPDTvEG 329
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149137229 396 ISFAPILLGKPDEQETHQYLYWENGTmsrHAQSIRLNQWW-AYRDH-------PSKPIELYDITED 453
Cdd:cd16034 330 RDLSPLLLGGKDDEPDSVLLQCFVPF---GGGSARDGGEWrGVRTDrytyvrdKNGPWLLFDNEKD 392
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
30-437 |
3.16e-64 |
|
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: 213.93 E-value: 3.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFR---TPNLDQLAMNGIRFTQAYSGSSeCAPSRGSLMTGMHMghcrIR-ANSSV--R 103
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHP----IRtGLTTVglP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 104 GQDH-LLSEDITVAEVLKGAGYTTGFIGKWGIGlpGTEGA-PDKQGFDFSYGYYdqarahgffPHylmrngkpepipeny 181
Cdd:cd16142 76 GSPGgLPPWEPTLAELLKDAGYATAQFGKWHLG--DEDGRlPTDHGFDEFYGNL---------YH--------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 182 gfnmkrvstyngrpvdRLDDVknvydengnlvpdgvpvaaaakysedlFQDEALSFIKKNR--DKPFFLYYATQLPHGPC 259
Cdd:cd16142 130 ----------------TIDEE---------------------------IVDKAIDFIKRNAkaDKPFFLYVNFTKMHFPT 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 260 ITPDLGAYKDKPWDlkhkEWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNG--YSQW---GYfgrsrneddylfk 334
Cdd:cd16142 167 LPSPEFEGKSSGKG----KYADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeQDVWpdgGY------------- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 335 nkGPWPKGKFTsTHEGGVRVPFFVYWKDKIKAG-ENDHICALYDVLATLADLASITPPKN---------DGISFAPILLG 404
Cdd:cd16142 230 --TPFRGEKGT-TWEGGVRVPAIVRWPGKIKPGrVSNEIVSHLDWFPTLAALAGAPDPKDkllgkdrhiDGVDQSPFLLG 306
|
410 420 430
....*....|....*....|....*....|...
gi 149137229 405 KPDEQETHQYLYWENGTMSrhaqSIRLNQWWAY 437
Cdd:cd16142 307 KSEKSRRSEFFYFGEGELG----AVRWKNWKVH 335
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
29-468 |
1.82e-57 |
|
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: 198.04 E-value: 1.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSSYGQ-EQFRTPnLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMH------MGHCRIRANSS 101
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHpTQERGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLpirsgmYGGTRVFLPWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 102 VRGqdhLLSEDITVAEVLKGAGYTTGFIGKWGIGL---PGTEGA--PDKQGFDFsYGYydqarahgFFPhylmrngkpep 176
Cdd:cd16160 80 IGG---LPKTEVTMAEALKEAGYTTGMVGKWHLGInenNHSDGAhlPSHHGFDF-VGT--------NLP----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 177 ipenYGFNMKRVSTynGRPVDRLDDVKNVYDENGNLVPDgvPVaaAAKYSEDLFQDEALSFIKKNRDKPFFLYYATQLPH 256
Cdd:cd16160 137 ----FTNSWACDDT--GRHVDFPDRSACFLYYNDTIVEQ--PI--QHEHLTETLVGDAKSFIEDNQENPFFLYFSFPQTH 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 257 GP-------CITPDLGAYKDkpwDLKHKEWAamlghldrgVGRMLDLMEQLEILDNTIIFFAGDNG-YSQWGYFGRSrne 328
Cdd:cd16160 207 TPlfaskrfKGKSKRGRYGD---NINEMSWA---------VGEVLDTLVDTGLDQNTLVFFLSDHGpHVEYCLEGGS--- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 329 ddylfknKGPWPKGKfTSTHEGGVRVPFFVYWKDKIKAGENDHICALYDVLATLADLASITPPKN---DGISFAPILLGK 405
Cdd:cd16160 272 -------TGGLKGGK-GNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriyDGLSITDLLLGE 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149137229 406 PDEqETHQYLYWENGTMSR----------HAQSIRLNQWWAYRDHPSKPieLYDITEDFACKND-LAKSNPELI 468
Cdd:cd16160 344 ADS-PHDDILYYCCSRLMAvrygsykihfKTQPLPSQESLDPNCDGGGP--LSDYIVCYDCEDEcVTKHNPPLI 414
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-475 |
1.99e-56 |
|
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: 193.16 E-value: 1.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAY-----SGSSeCAPSRGSLMTGMHMGHcriranSSVR 103
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYnmggwSGAV-CVPSRAMLMTGRTLFH------APEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 104 GQDHLLSEDITVAEVLKGAGYTTGFIGKWGiglpgtegapdkqgfdfsygyydqarahgffphylmrNGkpepipenygf 183
Cdd:cd16155 75 GKAAIPSDDKTWPETFKKAGYRTFATGKWH-------------------------------------NG----------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 184 nmkrvstyngrpvdrlddvknvydengnlvpdgvpvaaaakysedlFQDEALSFIK--KNRDKPFFLYYATQLPHGPCIT 261
Cdd:cd16155 107 ----------------------------------------------FADAAIEFLEeyKDGDKPFFMYVAFTAPHDPRQA 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 262 PDlgAYKDK-------------------------------PWDLKHK-------EWAAMLGHLDRGVGRMLDLMEQLEIL 303
Cdd:cd16155 141 PP--EYLDMyppetiplpenflpqhpfdngegtvrdeqlaPFPRTPEavrqhlaEYYAMITHLDAQIGRILDALEASGEL 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 304 DNTIIFFAGDNGYS--QWGYFGRSrneddylfknkgpwpkgkftSTHEGGVRVPFFVYWKDkIKAGE-NDHICALYDVLA 380
Cdd:cd16155 219 DNTIIVFTSDHGLAvgSHGLMGKQ--------------------NLYEHSMRVPLIISGPG-IPKGKrRDALVYLQDVFP 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 381 TLADLASITPPK-NDGISFAPILLGKPDEQETHQYLYWENGTmsrhaQSIRLNQW-WAYRDHPSKPIELYDITEDFACKN 458
Cdd:cd16155 278 TLCELAGIEIPEsVEGKSLLPVIRGEKKAVRDTLYGAYRDGQ-----RAIRDDRWkLIIYVPGVKRTQLFDLKKDPDELN 352
|
490
....*....|....*..
gi 149137229 459 DLAkSNPELIDRIRQIF 475
Cdd:cd16155 353 NLA-DEPEYQERLKKLL 368
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
29-416 |
1.15e-51 |
|
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: 183.42 E-value: 1.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGmhmghcRIRANSSV------ 102
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTG------RYQVRSGVypgvfy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 103 ---RGQdhLLSEDITVAEVLKGAGYTTGFIGKWGIGLpGTEGA--PDKQGFDFSYGY---YDQARAHG---FFPHY---- 167
Cdd:cd16158 75 pgsRGG--LPLNETTIAEVLKTVGYQTAMVGKWHLGV-GLNGTylPTHQGFDHYLGIpysHDQGPCQNltcFPPNIpcfg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 168 LMRNGKPePIPENYGFNMKRvstyngRPVDRLddvknvydengNLVPdgvpvaaaakysedLFQDEALSFIKKN--RDKP 245
Cdd:cd16158 152 GCDQGEV-PCPLFYNESIVQ------QPVDLL-----------TLEE--------------RYAKFAKDFIADNakEGKP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 246 FFLYYATQLPHGPCItpdlgAYKDKPWDLKHKEWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGYS-QWgyfgR 324
Cdd:cd16158 200 FFLYYASHHTHYPQF-----AGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPStMR----K 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 325 SRNEDDYLFKNkgpwpkGKFTsTHEGGVRVPFFVYWKDKIKAGENDHICALYDVLATLADLASITPPKN--DGISFAPIL 402
Cdd:cd16158 271 SRGGNAGLLKC------GKGT-TYEGGVREPAIAYWPGRIKPGVTHELASTLDILPTIAKLAGAPLPNVtlDGVDMSPIL 343
|
410
....*....|....*
gi 149137229 403 LGK-PDEQETHQYLY 416
Cdd:cd16158 344 FEQgKSPRQTFFYYP 358
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
30-388 |
1.60e-48 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 169.91 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHmghcRIRANSSVRGQDHLL 109
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLP----PHNFGSYVSTPVGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 110 SEDITVAEVLKGAGYTTGFIGKWGIGlPGTEGAPDKQGFDFSYGYydqarahgffphylmrngkpEPIPENYgfnmkrvs 189
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLG-WYNNQSPCNLGFDKFFGR--------------------NTGSDLY-------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 190 tyngrpvdrlddvKNVYDENGNLVPDGVpvaaaakYSEDLFqDEALSFIKKNrDKPFFLYYATQLPHGP--CITPDLGAY 267
Cdd:pfam00884 128 -------------ADPPDVPYNCSGGGV-------SDEALL-DEALEFLDNN-DKPFFLVLHTLGSHGPpyYPDRYPEKY 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 268 KDKPWDLKHKE-----WAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGYSqwgyfgrsrneddyLFKNKGPWPKG 342
Cdd:pfam00884 186 ATFKPSSCSEEqllnsYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGES--------------LGEGGGYLHGG 251
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 149137229 343 KFTSTHEGGVRVPFFVYWKDKIKAGENDHicALY---DVLATLADLASI 388
Cdd:pfam00884 252 KYDNAPEGGYRVPLLIWSPGGKAKGQKSE--ALVshvDLFPTILDLAGI 298
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
29-437 |
5.00e-48 |
|
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: 171.11 E-value: 5.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSSYGQEQFR-TPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMGHCRIRANSSVRGQDH 107
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 108 LLSEDITVAEVLKGAGYTTGFIGKWGIGLPGTEgAPDKQGFDFSYGyydqarahgffphylmrngkpepIPenygfnmkr 187
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAY-LPNSRGFDYYFG-----------------------IP--------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 188 vstyngrpvdrlddvknvYDENGNLvpdgvpvaaAAKYSEdlfqdEALSFIK--KNRDKPFFLYYATQLPHGPcitpdLG 265
Cdd:cd16161 128 ------------------FSHDSSL---------ADRYAQ-----FATDFIQraSAKDRPFFLYAALAHVHVP-----LA 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 266 AYKDKPWDLKHK-EWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGysQWGYFGRSRNEDDYLFKNK-GPWPKGK 343
Cdd:cd16161 171 NLPRFQSPTSGRgPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNG--PWEVKCELAVGPGTGDWQGnLGGSVAK 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 344 fTSTHEGGVRVPFFVYWKDKIKAG-ENDHICALYDVLATLADLASITPPKN---DGISFAPILLGKpdEQETHQYLYWEN 419
Cdd:cd16161 249 -ASTWEGGHREPAIVYWPGRIPANsTSAALVSTLDIFPTVVALAGASLPPGriyDGKDLSPVLFGG--SKTGHRCLFHPN 325
|
410 420
....*....|....*....|
gi 149137229 420 GTM--SRHAQSIRLNQWWAY 437
Cdd:cd16161 326 SGAagAGALSAVRCGDYKAH 345
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-400 |
1.38e-46 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 163.56 E-value: 1.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTG----MHMGHCRIR--ANSSVR 103
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGrmpsQHGIHDWIVegSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 104 GQDHLLSEDITVAEVLKGAGYTTGFIGKWGIGlpgtegapdkqgfdfsygyyDQArahgffphylmrngkpepipenygf 183
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG--------------------DDA------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 184 nmkrvstyngrpVDRLDDVknvydengnlvpdgvpvaaaakysedlfqdealsfikKNRDKPFFLYYATQLPHGpcitpd 263
Cdd:cd16149 116 ------------ADFLRRR-------------------------------------AEAEKPFFLSVNYTAPHS------ 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 264 lgaykdkPWdlkhkEWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGYS--QWGYFGrsrneddylfKNKGPWPK 341
Cdd:cd16149 141 -------PW-----GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNmgHHGIWG----------KGNGTFPL 198
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149137229 342 GKFTSTheggVRVPFFVYWKDKIKAGE--NDHICAlYDVLATLADLASITPPKND---GISFAP 400
Cdd:cd16149 199 NMYDNS----VKVPFIIRWPGVVPAGRvvDSLVSA-YDFFPTLLELAGVDPPADPrlpGRSFAD 257
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
29-416 |
3.53e-46 |
|
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: 169.39 E-value: 3.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTG-----MHMG-HCRIRANSSV 102
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGrypirSGMAsSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 103 RGQDHLLSEDITVAEVLKGAGYTTGFIGKWGIGLPGTEGA-----PDKQGFDFSYGYydqarahgffPHYLMRNGKPEPI 177
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNdfchhPLNHGFDYFYGL----------PLTNLKDCGDGSN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 178 PENYGFNMKRVSTY--------------------NGRPV------------------DRLDDVKNVYDENGNLVPDgvPV 219
Cdd:cd16159 151 GEYDLSFDPLFPLLtafvlitaltiflllylgavSKRFFvfllilsllfislfflllITNRYFNCILMRNHEVVEQ--PM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 220 AaaakySEDLFQ---DEALSFIKKNRDKPFFLYYATQLPHGPCITPDLgaYKDKPwdlKHKEWAAMLGHLDRGVGRMLDL 296
Cdd:cd16159 229 S-----LENLTQrltKEAISFLERNKERPFLLVMSFLHVHTALFTSKK--FKGRS---KHGRYGDNVEEMDWSVGQILDA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 297 MEQLEILDNTIIFFAGDNGysqwGYFGRSRNEDDYLFKNKGpWPKGKFTSTHEGGVRVPFFVYWKDKIKAG-ENDHICAL 375
Cdd:cd16159 299 LDELGLKDNTFVYFTSDNG----GHLEEISVGGEYGGGNGG-IYGGKKMGGWEGGIRVPTIVRWPGVIPPGsVIDEPTSL 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 149137229 376 YDVLATLADLASITPPKN---DGISFAPILLGKpDEQETHQYLY 416
Cdd:cd16159 374 MDIFPTVAALAGAPLPSDriiDGRDLMPLLTGQ-EKRSPHEFLF 416
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
29-427 |
2.49e-45 |
|
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: 165.72 E-value: 2.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGmhmgHCRIR---------AN 99
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTG----RLPIRngfyttnahAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 100 SSVRGQD---HLLSEDITVAEVLKGAGYTTGFIGKWGIGlPGTEGAPDKQGFDFSYGYYDqarahgffPHYLMRNGKPEP 176
Cdd:cd16157 77 NAYTPQNivgGIPDSEILLPELLKKAGYRNKIVGKWHLG-HRPQYHPLKHGFDEWFGAPN--------CHFGPYDNKAYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 177 -IPENYGFNMKrvstynGRPVDRLD-DVKNvydENGNLVpdgvpvaaaakyseDLFQDEALSFIKK--NRDKPFFLYYAT 252
Cdd:cd16157 148 nIPVYRDWEMI------GRYYEEFKiDKKT---GESNLT--------------QIYLQEALEFIEKqhDAQKPFFLYWAP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 253 QLPHGPCI-------TPDLGAYKDkpwdlkhkewAAMlgHLDRGVGRMLDLMEQLEILDNTIIFFAGDNG---YSQWGYF 322
Cdd:cd16157 205 DATHAPVYaskpflgTSQRGLYGD----------AVM--ELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 323 GrsrneddylfkNKGPWPKGKFTsTHEGGVRVPFFVYWKDKIKAGENDH-ICALYDVLATLADLASITPPKN---DGISF 398
Cdd:cd16157 273 G-----------SNGPFLCGKQT-TFEGGMREPAIAWWPGHIKPGQVSHqLGSLMDLFTTSLALAGLPIPSDraiDGIDL 340
|
410 420 430
....*....|....*....|....*....|
gi 149137229 399 APILLGKPDEQETHQYlYWENGTMS-RHAQ 427
Cdd:cd16157 341 LPVLLNGKEKDRPIFY-YRGDELMAvRLGQ 369
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-400 |
9.68e-44 |
|
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: 156.17 E-value: 9.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMGHcriraNSSVRGQdhLL 109
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFY-----HGVWGGP--LE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 110 SEDITVAEVLKGAGYTTGFIGKWgiglpgtegapdkqGFDFSYGYYDQarahGFFpHYLMRNGKPEPIPENYGFNMKRVS 189
Cdd:cd16148 74 PDDPTLAEILRKAGYYTAAVSSN--------------PHLFGGPGFDR----GFD-TFEDFRGQEGDPGEEGDERAERVT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 190 tyngrpvdrlddvknvydengnlvpdgvpvaaaakysedlfqDEALSFIKKN-RDKPFFLYYATQLPHGPCitpdlgAYK 268
Cdd:cd16148 135 ------------------------------------------DRALEWLDRNaDDDPFFLFLHYFDPHEPY------LYD 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 269 dkpwdlkhkewaAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGYSQwgyfgrsrNEDDYLFKNKGPWpkgkftstH 348
Cdd:cd16148 167 ------------AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEF--------GEHGLYWGHGSNL--------Y 218
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 149137229 349 EGGVRVPFFVYWKDKIKAGENDHICALYDVLATLADLASI-TPPKNDGISFAP 400
Cdd:cd16148 219 DEQLHVPLIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVePPDYSDGRSLLP 271
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-453 |
4.78e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 151.73 E-value: 4.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSyRDLS---SYGQEQFRTPNLDQLAMNGIRFTQAYSGSSeCAPSRGSLMTGMHmghcRIRANSSVRGQD 106
Cdd:cd16154 1 PNILLIIADDQG-LDSSaqySLSSDLPVTPTLDSLANSGIVFDNLWATPA-CSPTRATILTGKY----GFRTGVLAVPDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 107 HLLSEDITVAEVLKGA---GYTTGFIGKWGIGlpGTEGAPDkqgfdfsygyydqarAHGFFPHYlmrngkpepipenYGF 183
Cdd:cd16154 75 LLLSEETLLQLLIKDAttaGYSSAVIGKWHLG--GNDNSPN---------------NPGGIPYY-------------AGI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 184 NMKRVSTYNgrpvdrlddvknvydeNGNLVPDGVpVAAAAKYSEDLFQDEALSFIKkNRDKPFFLYYATQLPHGPCITP- 262
Cdd:cd16154 125 LGGGVQDYY----------------NWNLTNNGQ-TTNSTEYATTKLTNLAIDWID-QQTKPWFLWLAYNAPHTPFHLPp 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 263 -------DLGAYKD-----KPWDLkhkewaAMLGHLDRGVGRMLDLMEQlEILDNTIIFFAGDNGYSqwgyfGRSRNEDD 330
Cdd:cd16154 187 aelhsrsLLGDSADieanpRPYYL------AAIEAMDTEIGRLLASIDE-EERENTIIIFIGDNGTP-----GQVVDLPY 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 331 YLFKNKGpwpkgkftSTHEGGVRVPFFVYWKDKIKAGEN-DHICALYDVLATLADLASITPPK-NDGISFAPILLGKPde 408
Cdd:cd16154 255 TRNHAKG--------SLYEGGINVPLIVSGAGVERANEReSALVNATDLYATIAELAGVDAAEiHDSVSFKPLLSDVN-- 324
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 149137229 409 QETHQYLYWENGTMSRhaqsirlnQWWAYRDHPSKPI-------ELYDITED 453
Cdd:cd16154 325 ASTRQYNYTEYESPTT--------TGWATRNQYYKLIesengqeELYDLIND 368
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-453 |
2.26e-40 |
|
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: 150.83 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTG-MHMGHcRIRANSSV-RGQDH 107
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGlYPHEH-GVLNNVENaGAYSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 108 LLSEDITVA-EVLKGAGYTTGFIGKWGIglpGTEGAPDKQGFDfsyGYYDQaraHGFFPHYLMrngkpepipenygfnmk 186
Cdd:cd16033 80 GLPPGVETFsEDLREAGYRNGYVGKWHV---GPEETPLDYGFD---EYLPV---ETTIEYFLA----------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 187 rvstyngrpvdrlddvknvydengnlvpdgvpvaaaakysedlfqDEALSFIKK--NRDKPFFLYYATQLPHGPCITPD- 263
Cdd:cd16033 134 ---------------------------------------------DRAIEMLEElaADDKPFFLRVNFWGPHDPYIPPEp 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 264 -LGAYK---------------DKP------------WDLKHKEWAAMLGH-------LDRGVGRMLDLMEQLEILDNTII 308
Cdd:cd16033 169 yLDMYDpediplpesfaddfeDKPyiyrrerkrwgvDTEDEEDWKEIIAHywgyitlIDDAIGRILDALEELGLADDTLV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 309 FFAGDNGysqwgyfgrsrnedDYLfKNKGPWPKGKFtsTHEGGVRVPFFVYWKDKIKAGE-NDHICALYDVLATLADLAS 387
Cdd:cd16033 249 IFTSDHG--------------DAL-GAHRLWDKGPF--MYEETYRIPLIIKWPGVIAAGQvVDEFVSLLDLAPTILDLAG 311
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149137229 388 ITPP-KNDGISFAPILLGKPdEQETHQYLYWE-NGTMSRHAQSIRLNQWWAYRDHPSKPIELYDITED 453
Cdd:cd16033 312 VDVPpKVDGRSLLPLLRGEQ-PEDWRDEVVTEyNGHEFYLPQRMVRTDRYKYVFNGFDIDELYDLESD 378
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
29-453 |
2.04e-39 |
|
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: 148.87 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLsyRD-LSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMGHCRIRANSSVRgqDH 107
Cdd:cd16030 2 KPNVLFIAVDDL--RPwLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYF--RK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 108 LLSEDITVAEVLKGAGYTTGFIGK---WGIGlpgtEGAPDKQGFDFsygyydqarahgFFPHYLMRNGKPEPIPENYGFN 184
Cdd:cd16030 78 VAPDAVTLPQYFKENGYTTAGVGKifhPGIP----DGDDDPASWDE------------PPNPPGPEKYPPGKLCPGKKGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 185 MKRVSTYNGRPVDrlddvknvydengnlVPDGvpvaaaaKYSEDLFQDEALSFIK--KNRDKPFFL---YYAtqlPHGPC 259
Cdd:cd16030 142 KGGGGGPAWEAAD---------------VPDE-------AYPDGKVADEAIEQLRklKDSDKPFFLavgFYK---PHLPF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 260 ITP--------------------------------DLGAYKDKP--------WDLKHKEWAAML-GHL------DRGVGR 292
Cdd:cd16030 197 VAPkkyfdlyplesiplpnpfdpidlpevawndldDLPKYGDIPalnpgdpkGPLPDEQARELRqAYYasvsyvDAQVGR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 293 MLDLMEQLEILDNTIIFFAGDNGYSqwgyFGrsrneddylfkNKGPWpkGKFTsTHEGGVRVPFFVYWKDKIKAGEN-DH 371
Cdd:cd16030 277 VLDALEELGLADNTIVVLWSDHGWH----LG-----------EHGHW--GKHT-LFEEATRVPLIIRAPGVTKPGKVtDA 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 372 ICALYDVLATLADLASITPPKN-DGISFAPILLGKPDEQETHQYLYWENGTMSRHaqSIRLNQW----WAYRDHPsKPIE 446
Cdd:cd16030 339 LVELVDIYPTLAELAGLPAPPClEGKSLVPLLKNPSAKWKDAAFSQYPRPSIMGY--SIRTERYryteWVDFDKV-GAEE 415
|
....*..
gi 149137229 447 LYDITED 453
Cdd:cd16030 416 LYDHKND 422
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
27-473 |
2.45e-39 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 149.43 E-value: 2.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 27 MAKPNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMhmghcRIRANSSVRGQD 106
Cdd:PRK13759 4 TKKPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGL-----SQWHHGRVGYGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 107 HLLSE-DITVAEVLKGAGYTTGFIGKwgiglpgtegapdkqgfdfsYGYYDQARAHGFfPHYLMRNGKPEPIPENYGFNM 185
Cdd:PRK13759 79 VVPWNyKNTLPQEFRDAGYYTQCIGK--------------------MHVFPQRNLLGF-HNVLLHDGYLHSGRNEDKSQF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 186 KRVSTYngRPVDRLDDVKNVYDENGNLVPDGVPVAAAAKYSEDLFQ-----DEALSFIK-KNRDKPFFLYYATQLPHGPC 259
Cdd:PRK13759 138 DFVSDY--LAWLREKAPGKDPDLTDIGWDCNSWVARPWDLEERLHPtnwvgSESIEFLRrRDPTKPFFLKMSFARPHSPY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 260 ITPD--LGAYKDKP--------WDLKHKEW----------------------AAMLG---HLDRGVGRMLDLMEQLEILD 304
Cdd:PRK13759 216 DPPKryFDMYKDADipdphigdWEYAEDQDpeggsidalrgnlgeeyarrarAAYYGlitHIDHQIGRFLQALKEFGLLD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 305 NTIIFFAGDNGySQWGyfgrsrneDDYLFKNKGPWpkgkftsthEGGVRVPFFVYWKDKIKAG----ENDHICALYDVLA 380
Cdd:PRK13759 296 NTIILFVSDHG-DMLG--------DHYLFRKGYPY---------EGSAHIPFIIYDPGGLLAGnrgtVIDQVVELRDIMP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 381 TLADLASITPPKN-DGISFAPILLGKPDEQEThqYLYWEngtmsrHAQSIRLNQ----------WWAYRDHPskpiELYD 449
Cdd:PRK13759 358 TLLDLAGGTIPDDvDGRSLKNLIFGQYEGWRP--YLHGE------HALGYSSDNyltdgkwkyiWFSQTGEE----QLFD 425
|
490 500
....*....|....*....|....
gi 149137229 450 ITEDFACKNDLAKSnPELIDRIRQ 473
Cdd:PRK13759 426 LKKDPHELHNLSPS-EKYQPRLRE 448
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-453 |
3.87e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 142.30 E-value: 3.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMGHCRIRANSSVrgqdhlL 109
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP------Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 110 SEDI-TVAEVLKGAGYTTGFIGKwgiglpgtegapdkqgfdFSYGYYDQAraHGFFphylmrngkpepipenygfnmkrv 188
Cdd:cd16037 75 DGDVpSWGHALRAAGYETVLIGK------------------LHFRGEDQR--HGFR------------------------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 189 styngrpvdrlddvknvYDENgnlvpdgvpVAAAAkysEDLFQDEAlsfikkNRDKPFFLYYATQLPHGPCITP-DLgay 267
Cdd:cd16037 111 -----------------YDRD---------VTEAA---VDWLREEA------ADDKPWFLFVGFVAPHFPLIAPqEF--- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 268 kdkpWDLKHKE----WAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGySQWGYFGRsrneddylfknkgpWPKGK 343
Cdd:cd16037 153 ----YDLYVRRaraaYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHG-DMLGERGL--------------WGKST 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 344 FtstHEGGVRVPFFVYWKDKIKAGENDHICALYDVLATLADLASITPPKN-DGISFAPILLGKPDEQETHQYLYWENGTM 422
Cdd:cd16037 214 M---YEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDlDGRSLLPLAEGPDDPDRVVFSEYHAHGSP 290
|
410 420 430
....*....|....*....|....*....|.
gi 149137229 423 SRHAQsIRLNQwWAYRDHPSKPIELYDITED 453
Cdd:cd16037 291 SGAFM-LRKGR-WKYIYYVGYPPQLFDLEND 319
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
29-453 |
1.32e-37 |
|
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: 142.69 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSsygqEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHmGHC-RIRANS----SVR 103
Cdd:cd16147 1 RPNIVLILTDDQDVELGS----MDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQY-AHNhGVTNNSppggGYP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 104 GQDHLLSEDITVAEVLKGAGYTTGFIGKW--GIGLPGTEGAPDKqGFDFSYGyydqarAHGFFPHYlmrngkpepipeNY 181
Cdd:cd16147 76 KFWQNGLERSTLPVWLQEAGYRTAYAGKYlnGYGVPGGVSYVPP-GWDEWDG------LVGNSTYY------------NY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 182 GFNMkrvSTYNGRPVDRLDDvknvydengnlvpdgvpvaaaakYSEDLFQDEALSFIK--KNRDKPFFLYYATQLPHGPC 259
Cdd:cd16147 137 TLSN---GGNGKHGVSYPGD-----------------------YLTDVIANKALDFLRraAADDKPFFLVVAPPAPHGPF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 260 I--TPDLGAYKD------------KPWDLKH---------------------KEWAAMLGhLDRGVGRMLDLMEQLEILD 304
Cdd:cd16147 191 TpaPRYANLFPNvtapprpppnnpDVSDKPHwlrrlpplnptqiayidelyrKRLRTLQS-VDDLVERLVNTLEATGQLD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 305 NTIIFFAGDNGYSqWGYFGrsrneddylfknkgpWPKGKFTStHEGGVRVPFFVYWkDKIKAGE-NDHICALYDVLATLA 383
Cdd:cd16147 270 NTYIIYTSDNGYH-LGQHR---------------LPPGKRTP-YEEDIRVPLLVRG-PGIPAGVtVDQLVSNIDLAPTIL 331
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149137229 384 DLASITPPKN-DGISFAPILLGkpdeqeTHQYLYWENGTmsrhaqSIRLNQWWAYRDHpskpiELYDITED 453
Cdd:cd16147 332 DLAGAPPPSDmDGRSCGDSNNN------TYKCVRTVDDT------YNLLYFEWCTGFR-----ELYDLTTD 385
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
30-453 |
6.00e-34 |
|
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: 131.16 E-value: 6.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMGhcRIRA--NSSvrgqdH 107
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPS--RIGAydNAA-----E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 108 LLSEDITVAEVLKGAGYTTGFIGKWG-IGlpgtegaPDK-QGFDfsygyydqarahgffphylmrngkpepipenygfnm 185
Cdd:cd16032 74 FPADIPTFAHYLRAAGYRTALSGKMHfVG-------PDQlHGFD------------------------------------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 186 krvstyngrpvdrlddvknvYDENgnlvpdgvpVAAAAKysEDLFqDEAlsfiKKNRDKPFFLYYATQLPHGPCITPdlg 265
Cdd:cd16032 111 --------------------YDEE---------VAFKAV--QKLY-DLA----RGEDGRPFFLTVSFTHPHDPYVIP--- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 266 aykDKPWDL-----KHKeWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGysqwgyfgrsrnedDYLfKNKGPWP 340
Cdd:cd16032 152 ---QEYWDLyvrraRRA-YYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHG--------------DML-GERGLWY 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 341 KGKFtstHEGGVRVPFFVYWKDKIKAGENDHICALYDVLATLADLASITPPKN----DGISFAPILLGKPDEQETHQYL- 415
Cdd:cd16032 213 KMSF---FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHvpplDGRSLLPLLEGGDSGGEDEVISe 289
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 149137229 416 YWENGT-----MSRHAqsirlnqWWAYRDHPSKPIELYDITED 453
Cdd:cd16032 290 YLAEGAvapcvMIRRG-------RWKFIYCPGDPDQLFDLEAD 325
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-453 |
3.54e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 128.12 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTG--MHM-GHcriranssvRGQD 106
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGwyPHVnGH---------RTLH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 107 HLLSED-ITVAEVLKGAGYTTGFIGKwgiglpgtegapdkqgfdfsygyydqarahgffphylmrngkpepipenygfnm 185
Cdd:cd16150 72 HLLRPDePNLLKTLKDAGYHVAWAGK------------------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 186 krvstyngrpvdrlddvknvydeNGNLVPDGVPVAAAAkySEDLFQDEALSFIK-KNRDKPFFLYYATQLPHGP------ 258
Cdd:cd16150 98 -----------------------NDDLPGEFAAEAYCD--SDEACVRTAIDWLRnRRPDKPFCLYLPLIFPHPPygveep 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 259 ---CITPDL--------GAYKDKPWDLKHKE-----------WA-------AMLGHLDRGVGRMLDLMEQLEILDNTIIF 309
Cdd:cd16150 153 wfsMIDREKlpprrppgLRAKGKPSMLEGIEkqgldrwseerWRelratylGMVSRLDHQFGRLLEALKETGLYDDTAVF 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 310 FAGDNGysqwGYFGrsrnedDYLFKNKgpWPkgkfTSTHEGGVRVPFFVYWKDKIKAGENDHICALYDVLATLADLASIT 389
Cdd:cd16150 233 FFSDHG----DYTG------DYGLVEK--WP----NTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 390 PP-KNDGISFAPILLGKPDE-------------QETHQY--------LYWENGTMSRH------AQSIRLNQW-WAYRdh 440
Cdd:cd16150 297 LShTHFGRSLLPVLAGETEEhrdavfseggrlhGEEQAMegghgpydLKWPRLLQQEEppehtkAVMIRTRRYkYVYR-- 374
|
490
....*....|...
gi 149137229 441 PSKPIELYDITED 453
Cdd:cd16150 375 LYEPDELYDLEAD 387
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-415 |
1.06e-31 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 125.80 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHmghcriRANSSVRGQDHL 108
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLY------PTETGCFRNGIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 109 LSEDI-TVAEVLKGAGYTTGFIGKWGIglpgtegapdkqgfdfsygyydqarahgffphylmrngkpepipenygfnmkr 187
Cdd:cd16152 75 LPADEkTLAHYFRDAGYETGYVGKWHL----------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 188 vstyngrpvdrlddvknvydengnlvpdgvpvaaaAKYSEDLFQDEALSFI-KKNRDKPFFLYYATQLPH-----GPCIT 261
Cdd:cd16152 102 -----------------------------------AGYRVDALTDFAIDYLdNRQKDKPFFLFLSYLEPHhqndrDRYVA 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 262 PDLGA--YKDK--PWDLKHKE--WAAMLG-------HLDRGVGRMLDLMEQLEILDNTIIFFAGDNGysqwGYFgRSRNE 328
Cdd:cd16152 147 PEGSAerFANFwvPPDLAALPgdWAEELPdylgcceRLDENVGRIRDALKELGLYDNTIIVFTSDHG----CHF-RTRNA 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 329 DdylFKNkgpwpkgkftSTHEGGVRVPFFVYWKDKIKAGENDHICALYDVLATLADLASITPPKN-DGISFAPILLGKPD 407
Cdd:cd16152 222 E---YKR----------SCHESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEmQGRSLLPLVDGKVE 288
|
....*...
gi 149137229 408 EQETHQYL 415
Cdd:cd16152 289 DWRNEVFI 296
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
30-392 |
4.94e-29 |
|
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: 119.79 E-value: 4.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMGHCRIRANSSVrgqdhlL 109
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMA------L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 110 SEDI-TVAEVLKGAGYTTGFIGKW---GIGLPGTEGAPdkQGFDFSYgYYDQARahgffphYL------MRNGKPEPIPE 179
Cdd:cd16156 75 GDNVkTIGQRLSDNGIHTAYIGKWhldGGDYFGNGICP--QGWDPDY-WYDMRN-------YLdelteeERRKSRRGLTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 180 NYGFNMKRVSTYNGRPVDRlddvknvydengnlvpdgvpvaaaakysedlfqdeALSFIKKNRDKPFFLYYATQLPHGPC 259
Cdd:cd16156 145 LEAEGIKEEFTYGHRCTNR-----------------------------------ALDFIEKHKDEDFFLVVSYDEPHHPF 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 260 ITPDLGA--YKDKPWDLK-------------HKEWAAMLGHLDRG-------------------VGRMLDLMEqlEILDN 305
Cdd:cd16156 190 LCPKPYAsmYKDFEFPKGenayddlenkplhQRLWAGAKPHEDGDkgtikhplyfgcnsfvdyeIGRVLDAAD--EIAED 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 306 TIIFFAGDNGYSQWGyfgrsrneddYLFKNKGPwpkgkftSTHEGGVRVPFFVYWKDKIKAG-ENDHICALYDVLATLAD 384
Cdd:cd16156 268 AWVIYTSDHGDMLGA----------HKLWAKGP-------AVYDEITNIPLIIRGKGGEKAGtVTDTPVSHIDLAPTILD 330
|
....*...
gi 149137229 385 LASITPPK 392
Cdd:cd16156 331 YAGIPQPK 338
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
30-466 |
8.35e-29 |
|
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: 118.90 E-value: 8.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMH-MGHcRIRANSSVRGQDHL 108
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYlMNH-RSVWNGTPLDARHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 109 lsediTVAEVLKGAGYTTGFIGKwgiglpgTEGAPDKQGFdfsygyydqARAHGFFPHYLmrngkpepiPENYGFnmkrv 188
Cdd:cd16028 80 -----TLALELRKAGYDPALFGY-------TDTSPDPRGL---------APLDPRLLSYE---------LAMPGF----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 189 styngRPVDRLDDVKnvydengnlvpdgvpvaaaAKYSEDLF-QDEALSFIKKNRDKPFFLYYATQLPHGPCITPD---- 263
Cdd:cd16028 125 -----DPVDRLDEYP-------------------AEDSDTAFlTDRAIEYLDERQDEPWFLHLSYIRPHPPFVAPApyha 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 264 ----------------LGAYKDKPW---------------------DLKHKEWAAM----LG---HLDRGVGRMLDLMEQ 299
Cdd:cd16028 181 lydpadvpppiraeslAAEAAQHPLlaaflerieslsfspgaanaaDLDDEEVAQMratyLGliaEVDDHLGRLFDYLKE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 300 LEILDNTIIFFAGDNGySQWGyfgrsrneDDYLFknkgpwpkGKFTsTHEGGVRVPFFVYW----KDKIKAGENDHICAL 375
Cdd:cd16028 261 TGQWDDTLIVFTSDHG-EQLG--------DHWLW--------GKDG-FFDQAYRVPLIVRDprreADATRGQVVDAFTES 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 376 YDVLATLADLASITPPKN-DGISFAPILLGKPDE---QETHQYLYWENGT---------MSRHAQS--IRLNQWWAYRDH 440
Cdd:cd16028 323 VDVMPTILDWLGGEIPHQcDGRSLLPLLAGAQPSdwrDAVHYEYDFRDVStrrpqealgLSPDECSlaVIRDERWKYVHF 402
|
490 500
....*....|....*....|....*.
gi 149137229 441 PSKPIELYDITEDFACKNDLAkSNPE 466
Cdd:cd16028 403 AALPPLLFDLKNDPGELRDLA-ADPA 427
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-425 |
8.40e-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: 104.60 E-value: 8.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMGHCRIRANSSVRGQdHLL 109
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQ-PLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 110 SEDI-TVAEVLKGAGYTTGFIGKWGIGlpgtegapdkqgfDFSYGYYDQarahgffphylmrngkpepipenygfnmkrv 188
Cdd:cd16035 80 SPDVpTLGHMLRAAGYYTAYKGKWHLS-------------GAAGGGYKR------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 189 styngrpvdrlddvknvydengnlvpDGVpvaaaakysedlFQDEALSFIKK-----NRDKPFFLyyATQL--PHGPCIT 261
Cdd:cd16035 116 --------------------------DPG------------IAAQAVEWLRErgaknADGKPWFL--VVSLvnPHDIMFP 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 262 PDlgayKDKPWDLKHKEWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGysqwgyfgrsrnedDYLFKNKGpwpK 341
Cdd:cd16035 156 PD----DEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG--------------EMGGAHGL---R 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 342 GKFTSTHEGGVRVPFFVYWKD-KIKAGENDHICALYDVLATLADLASITPPKND-------GISFAPILLGKPDEQETHQ 413
Cdd:cd16035 215 GKGFNAYEEALHVPLIISHPDlFGTGQTTDALTSHIDLLPTLLGLAGVDAEARAteapplpGRDLSPLLTDADADAVRDG 294
|
410
....*....|..
gi 149137229 414 YLYwengTMSRH 425
Cdd:cd16035 295 ILF----TYDRY 302
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-399 |
3.93e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 102.07 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSSYGQEQF----------RTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMGHCRIRA 98
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNAHTgksesrlgyvESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 99 NS-SVRGQDHLLsedITVAEVLKGAGYTTGFIGKWGiglpgtegapdkqgfdfsygyydqaraHGFFPHYLMRNGKPEPI 177
Cdd:cd16153 81 FEaAHPALDHGL---PTFPEVLKKAGYQTASFGKSH---------------------------LEAFQRYLKNANQSYKS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 178 PenYGFNMKRVSTyngrpvdrlddvknvydengnlvpdgvpvaaaakysedlfqdealsfikknrDKPFFLYYATQLPHG 257
Cdd:cd16153 131 F--WGKIAKGADS----------------------------------------------------DKPFFVRLSFLQPHT 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 258 PCITPdlgaykdKPWdLKHKEWAAMLGHLDRGVGRMLDLMEQL---EILDNTIIFFAGDNGysqWgyfgrSRNEDDYLFK 334
Cdd:cd16153 157 PVLPP-------KEF-RDRFDYYAFCAYGDAQVGRAVEAFKAYslkQDRDYTIVYVTGDHG---W-----HLGEQGILAK 220
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149137229 335 NkGPWPKgkftsthegGVRVPFFVYWKDKIKAGENDH---ICALYDVLATLADLASI---TPPKNDGISFA 399
Cdd:cd16153 221 F-TFWPQ---------SHRVPLIVVSSDKLKAPAGKVrhdFVEFVDLAPTLLAAAGVdvdAPDYLDGRDLF 281
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
30-386 |
1.53e-23 |
|
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: 100.45 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYSGSSECAPSRG--SLMTGMHMghcriRANSSVRGQDH 107
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPP-----LPLGSGSYTLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 108 LLSEDITVAEVLKGAGYTTGFIgkwgiglpgtegapdkqgfdfsygyydqaraHGFFPHYlmrngkpepipenygFNMKR 187
Cdd:cd16015 76 KLNPLPSLPSILKEQGYETIFI-------------------------------HGGDASF---------------YNRDS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 188 VSTYNGrpVDRLDDVKN----VYDENGNLVPDgvpvaaaakysEDLFqDEALSFIKKNRDKPFFLYYATQLPHGPCITPD 263
Cdd:cd16015 110 VYPNLG--FDEFYDLEDfpddEKETNGWGVSD-----------ESLF-DQALEELEELKKKPFFIFLVTMSNHGPYDLPE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 264 LGAYKDKPWDLKHKEWAAMLGHL---DRGVGRMLDLMEQLEILDNTIIFFAGDNGYSQWGYFGRSRNEDDYLFknkgpwp 340
Cdd:cd16015 176 EKKDEPLKVEEDKTELENYLNAIhytDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY------- 248
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 149137229 341 kgkftstheggvRVPFFVYWKDKIKAGENDHICALYDVLATLADLA 386
Cdd:cd16015 249 ------------RTPLLIYSPGLKKPKKIDRVGSQIDIAPTLLDLL 282
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
23-430 |
2.43e-19 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 91.25 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 23 GQGHMAKPNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRFTQAYS--GSSecapSRG--SLMTGMHMghcriRA 98
Cdd:COG1368 228 PFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSqgGRT----SRGefAVLTGLPP-----LP 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 99 NSSV--RGQDHLLSediTVAEVLKGAGYTTGFIgkwgiglpgtegapdkqgfdfsygyydqaraHGFFPHYlmrngkpep 176
Cdd:COG1368 299 GGSPykRPGQNNFP---SLPSILKKQGYETSFF-------------------------------HGGDGSF--------- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 177 ipenygFNMKRVSTYNGrpVDRLDDVKN-VYDENGNL-VPDgvpvaaaakysEDLFqDEALSFIKKNrDKPFFLYYATQL 254
Cdd:COG1368 336 ------WNRDSFYKNLG--FDEFYDREDfDDPFDGGWgVSD-----------EDLF-DKALEELEKL-KKPFFAFLITLS 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 255 PHGPCITPDLGAYKDkpwDLKHKEWAAMLGHL---DRGVGRMLDLMEQLEILDNTIIFFAGDNGysqwgyfGRSRNEDDY 331
Cdd:COG1368 395 NHGPYTLPEEDKKIP---DYGKTTLNNYLNAVryaDQALGEFIEKLKKSGWYDNTIFVIYGDHG-------PRSPGKTDY 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 332 LfknkgpWPKGKFtstheggvRVPFFVYWKDKIKAGENDHICALYDVLATLADLASItpPKNDGISFAPILLGKPDEQE- 410
Cdd:COG1368 465 E------NPLERY--------RVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGI--DYPSYYAFGRDLLSPDTDPFa 528
|
410 420
....*....|....*....|....*...
gi 149137229 411 -------THQYLY-WENGTMSRHAQSIR 430
Cdd:COG1368 529 frnggfiTDDYVYvLKTGELTEEDKELE 556
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
30-386 |
5.32e-17 |
|
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: 80.54 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRDLSSYGQEQFRTPNLDQLAMNGIRF-TQAYSGSSECAPSRGSLMTG----MHMGHCRIRANSSVRG 104
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGayptLHGYTGNGSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 105 QD-HLLSEDITVAEVLKGAGYTTGFIGkwgiglpgtegapdkqgfdfsygyydqarahgffphylmrngkpepipenygf 183
Cdd:cd00016 81 RAaGKDEDGPTIPELLKQAGYRTGVIG----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 184 nmkrvstyngrpvdrlddvknvydengnlvpdgvpvaaaakysedlfqdeALSFIK-KNRDKPFFLYYATQLPHGPcitp 262
Cdd:cd00016 108 --------------------------------------------------LLKAIDeTSKEKPFVLFLHFDGPDGP---- 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 263 dlgAYKDKPwdlKHKEWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGYSqwgyfgrsrneddylFKNKGPWPKG 342
Cdd:cd00016 134 ---GHAYGP---NTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGI---------------DKGHGGDPKA 192
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 149137229 343 KFT-STHEGGVRVPFFVYWKDKIKAGENDHICALYDVLATLADLA 386
Cdd:cd00016 193 DGKaDKSHTGMRVPFIAYGPGVKKGGVKHELISQYDIAPTLADLL 237
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
30-453 |
1.02e-14 |
|
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: 75.66 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 30 PNILFIFSDDLSYRdLSSYGQEQF-RTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHmghcrIRANSSVRGQDHL 108
Cdd:cd16171 1 PNVVMVMSDSFDGR-LTFRPGNQVvDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLF-----THLTESWNNYKGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 109 LSEDITVAEVLKGAGYTTGFIGKwgiglpgtegapdkqgFDFSYGyydqarahgffpHYLMRNgKPEPIPENYGFNMKRv 188
Cdd:cd16171 75 DPNYPTWMDRLEKHGYHTQKYGK----------------LDYTSG------------HHSVSN-RVEAWTRDVPFLLRQ- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 189 styNGRPVdrlddvknvydenGNLVPDGVPVAAAAKYSEDLfqDEALSFIKK---NRDKPFFLYYATQLPHgPCITPDLG 265
Cdd:cd16171 125 ---EGRPT-------------VNLVGDRSTVRVMLKDWQNT--DKAVHWIRKeapNLTQPFALYLGLNLPH-PYPSPSMG 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 266 AYKDKPWDLKhKEWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGysqwgyfgRSRNEDDYLFKnkgpwpkgkfT 345
Cdd:cd16171 186 ENFGSIRNIR-AFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHG--------ELAMEHRQFYK----------M 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 346 STHEGGVRVPFFVYwKDKIKAG-ENDHICALYDVLATLADLASITPPKN-DGISFAPILLGK-----PDEQETHQYLYWE 418
Cdd:cd16171 247 SMYEGSSHVPLLIM-GPGIKAGqQVSDVVSLVDIYPTMLDIAGVPQPQNlSGYSLLPLLSESsikesPSRVPHPDWVLSE 325
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 149137229 419 ----NGTMSRHAqsIRLNQW--WAYRDHPSKPIELYDITED 453
Cdd:cd16171 326 fhgcNVNASTYM--LRTNSWkyIAYADGNSVPPQLFDLSKD 364
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
29-382 |
1.29e-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: 57.61 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 29 KPNILFIFSDDLSYRDLSsygQEQfrTPNLDQLAMNGIRFTQAYSGSSECAPSRGSLMTGMHMGHcriranssvrgQDHL 108
Cdd:COG3083 244 PPNILLIVVDSLRADMLD---PEV--MPNLYAFAQRSLRFTNHYSSGNSTRAGLFGLFYGLPGNY-----------WDSI 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 109 LSEDITVA--EVLKGAGYTTGFIGkwgiglpgteGAPdkqgfdFSYGYYDQArahgFFphylmrNGKPEPIPENYGFNMK 186
Cdd:COG3083 308 LAERTPPVliDALQQQGYQFGLFS----------SAG------FNSPLFRQT----IF------SDVSLPRLHTPGGPAQ 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 187 RvstyngrpvdrldDVKNVydengnlvpdgvpvaaaakysedlfqDEALSFI-KKNRDKPFFLYYATQLPHGPCITPD-- 263
Cdd:COG3083 362 R-------------DRQIT--------------------------AQWLQWLdQRDSDRPWFSYLFLDAPHAYSFPADyp 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 264 -----------LGAYKDKPWDLKHKEWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNGY----SQWGYFGRSRNE 328
Cdd:COG3083 403 kpfqpsedcnyLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEefneNGQNYWGHNSNF 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 149137229 329 DDYLfknkgpwpkgkftstheggVRVPFFVYWKDKiKAGENDHICALYDVLATL 382
Cdd:COG3083 483 SRYQ-------------------LQVPLVIHWPGT-PPQVISKLTSHLDIVPTL 516
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
1-371 |
9.51e-06 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 47.82 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 1 MKKISSLKYLFVVAAMTGSAvfgqghMAKPNILFIFSDDLSYRDLssygqEQFRTPNLDQLAMNGIRFTQAYSGS-SECA 79
Cdd:COG1524 1 MKRGLSLLLASLLAAAAAAA------PPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 80 PSRGSLMTGMHMGHCRIRANS-------------SVRGQDHLLSEDI---TVAEVLKGAGYTTGFIGkWgiglPGTEGap 143
Cdd:COG1524 70 PAHTTLLTGLYPGEHGIVGNGwydpelgrvvnslSWVEDGFGSNSLLpvpTIFERARAAGLTTAAVF-W----PSFEG-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 144 dkqgfdfsYGYYDQARAHGFfphylmrngkpepipenygfnmkrvstyngrpvdrlddvknvydeNGNLVPDGVPVAaaa 223
Cdd:COG1524 143 --------SGLIDAARPYPY---------------------------------------------DGRKPLLGNPAA--- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 224 kyseDLFQ-DEALSFIKKNRdkPFFLY-YatqLPHgpcitPDlgaykdkpwDLKHK------EWAAMLGHLDRGVGRMLD 295
Cdd:COG1524 167 ----DRWIaAAALELLREGR--PDLLLvY---LPD-----LD---------YAGHRygpdspEYRAALREVDAALGRLLD 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 296 LMEQLEILDNTIIFFAGDNG---YSQWGYFGRSRnEDDYLFKNKGP----WPKGKFTSTHEGGVRVPFFVYWKDKIKAGE 368
Cdd:COG1524 224 ALKARGLYEGTLVIVTADHGmvdVPPDIDLNRLR-LAGLLAVRAGEsahlYLKDGADAEVRALLGLPARVLTREELAAGH 302
|
...
gi 149137229 369 NDH 371
Cdd:COG1524 303 FGP 305
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
237-327 |
4.98e-03 |
|
uncharacterized Alkaline phosphatase subfamily; 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.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 39.04 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149137229 237 FIKKNRDKPFF-LYYATQLPHgpcitpdlgaykdkpwdlkhkEWAAMLGHLDRGVGRMLDLMEQLEILDNTIIFFAGDNG 315
Cdd:cd16021 156 FIEAYKDRPKFsFFWLSELTH---------------------DYLNGLSLADEDLLEFLKRLKENGLLDNTFVIFMSDHG 214
|
90
....*....|..
gi 149137229 316 YSqwgyFGRSRN 327
Cdd:cd16021 215 LR----FGKIRE 222
|
|
| |
