|
Name |
Accession |
Description |
Interval |
E-value |
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
8-507 |
0e+00 |
|
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: 623.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 8 RNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWNAVPLPLEELT 87
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGTPLDARHLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 88 LGDYLRAAGVRTALVGKTHATANLEGMRRLGIDPasaRGAALAEAGFEPYDRNDGVypddpafadkrerapythylrrlg 167
Cdd:cd16028 81 LALELRKAGYDPALFGYTDTSPDPRGLAPLDPRL---LSYELAMPGFDPVDRLDEY------------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 168 ftgdnpwhdwanaaagadgeilsgwrmrhaglptrlPEAHSETAYTTRRAMDFIDEQGERPWCLHLSYIKPHWPYIAPAP 247
Cdd:cd16028 134 ------------------------------------PAEDSDTAFLTDRAIEYLDERQDEPWFLHLSYIRPHPPFVAPAP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 248 YHALYRADQVLPALRAA--PGEESDHPVYRAFREHRESLNFS---------REDVRRQVIPTYMGLIRQVDDQLGRLFQH 316
Cdd:cd16028 178 YHALYDPADVPPPIRAEslAAEAAQHPLLAAFLERIESLSFSpgaanaadlDDEEVAQMRATYLGLIAEVDDHLGRLFDY 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 317 MRASGRWDDTLIVFTSDHGDFLGDHGLGEKEFLLESAVGVPLLIRDPRPEADATRGRVEEALVQSIDVLPSILEAFAVeP 396
Cdd:cd16028 258 LKETGQWDDTLIVFTSDHGEQLGDHWLWGKDGFFDQAYRVPLIVRDPRREADATRGQVVDAFTESVDVMPTILDWLGG-E 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 397 ASHRIEGRSLLPFVHGAPPADWRRYAIAEYDYA--FQAPARERLGRPIDACRMYMVRSERWKYIAYDGFRAQLFDLASDP 474
Cdd:cd16028 337 IPHQCDGRSLLPLLAGAQPSDWRDAVHYEYDFRdvSTRRPQEALGLSPDECSLAVIRDERWKYVHFAALPPLLFDLKNDP 416
|
490 500 510
....*....|....*....|....*....|...
gi 15597529 475 GELRDLGADPAHAAVREAHAGMLFDWLRGLKRR 507
Cdd:cd16028 417 GELRDLAADPAYAAVVLRYAQKLLSWRMRHADR 449
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-505 |
1.17e-114 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 344.94 E-value: 1.17e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 1 MSQPKPirNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWNA-- 78
Cdd:COG3119 19 AAAKRP--NILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGeg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 79 --VPLPLEELTLGDYLRAAGVRTALVGKTHatanlegmrrlgidpasargaalaeagfepydrndgvypddpafadkrer 156
Cdd:COG3119 97 ynGGLPPDEPTLAELLKEAGYRTALFGKWH-------------------------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 157 apytHYLrrlgftgdnpwhdwanaaagadgeilsgwrmrhaglptrlpeahseTAYTTRRAMDFIDEQ--GERPWCLHLS 234
Cdd:COG3119 127 ----LYL----------------------------------------------TDLLTDKAIDFLERQadKDKPFFLYLA 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 235 YIKPHWPYIAPAPYHALYRadqvlpalraapGEESDHPVYRAFREhreslnfSREDVRRQVIPTYMGLIRQVDDQLGRLF 314
Cdd:COG3119 157 FNAPHAPYQAPEEYLDKYD------------GKDIPLPPNLAPRD-------LTEEELRRARAAYAAMIEEVDDQVGRLL 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 315 QHMRASGRWDDTLIVFTSDHGDFLGDHGL-GEKEFLLESAVGVPLLIRDPrpeADATRGRVEEALVQSIDVLPSILEAFA 393
Cdd:COG3119 218 DALEELGLADNTIVVFTSDNGPSLGEHGLrGGKGTLYEGGIRVPLIVRWP---GKIKAGSVSDALVSLIDLLPTLLDLAG 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 394 VEPASHrIEGRSLLPFVHGaPPADWRRYAIAEYDYafqaparerlgrpidACRMYMVRSERWKYIAY--DGFRAQLFDLA 471
Cdd:COG3119 295 VPIPED-LDGRSLLPLLTG-EKAEWRDYLYWEYPR---------------GGGNRAIRTGRWKLIRYydDDGPWELYDLK 357
|
490 500 510
....*....|....*....|....*....|....
gi 15597529 472 SDPGELRDLGADpaHAAVREAHAGMLFDWLRGLK 505
Cdd:COG3119 358 NDPGETNNLAAD--YPEVVAELRALLEAWLKELG 389
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
9-502 |
7.57e-92 |
|
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: 286.81 E-value: 7.57e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWN-------AVPL 81
Cdd:cd16033 2 NILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNvenagaySRGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 82 PLEELTLGDYLRAAGVRTALVGKTHATANlegmrrlgidpasaRGAAlaEAGFEPYdrndgvypddpafadkrerapyth 161
Cdd:cd16033 82 PPGVETFSEDLREAGYRNGYVGKWHVGPE--------------ETPL--DYGFDEY------------------------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 162 ylrrlgftgdnpwhdwanaaagadgeilsgwrmrhaglptrLPEAHSETAYTTRRAMDFIDE--QGERPWCLHLSYIKPH 239
Cdd:cd16033 122 -----------------------------------------LPVETTIEYFLADRAIEMLEElaADDKPFFLRVNFWGPH 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 240 WPYIAPAPYHALYRADQV-LPALRAAPGEesDHP-VYRAFREHRESLNFSREDVRrQVIPTYMGLIRQVDDQLGRLFQHM 317
Cdd:cd16033 161 DPYIPPEPYLDMYDPEDIpLPESFADDFE--DKPyIYRRERKRWGVDTEDEEDWK-EIIAHYWGYITLIDDAIGRILDAL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 318 RASGRWDDTLIVFTSDHGDFLGDHGLGEK-EFLLESAVGVPLLIRDPrpeADATRGRVEEALVQSIDVLPSILEAFAVEP 396
Cdd:cd16033 238 EELGLADDTLVIFTSDHGDALGAHRLWDKgPFMYEETYRIPLIIKWP---GVIAAGQVVDEFVSLLDLAPTILDLAGVDV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 397 aSHRIEGRSLLPFVHGAPPADWRRYAIAEYD----YAFQaparerlgrpidacrmYMVRSERWKYIaYDGF-RAQLFDLA 471
Cdd:cd16033 315 -PPKVDGRSLLPLLRGEQPEDWRDEVVTEYNghefYLPQ----------------RMVRTDRYKYV-FNGFdIDELYDLE 376
|
490 500 510
....*....|....*....|....*....|.
gi 15597529 472 SDPGELRDLGADPAHAAVREAHAGMLFDWLR 502
Cdd:cd16033 377 SDPYELNNLIDDPEYEEILREMRTRLYEWME 407
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
8-492 |
2.52e-90 |
|
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: 283.65 E-value: 2.52e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 8 RNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWNAVPL-PLEEL 86
Cdd:cd16031 3 PNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLfDASQP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 87 TLGDYLRAAGVRTALVGKTHatanlegmrrLGIDPASARgaalaeAGFEPYD--RNDGVYpDDPAFADKRERAPYTHYLr 164
Cdd:cd16031 83 TYPKLLRKAGYQTAFIGKWH----------LGSGGDLPP------PGFDYWVsfPGQGSY-YDPEFIENGKRVGQKGYV- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 165 rlgftgdnpwhdwanaaagadgeilsgwrmrhaglptrlpeahseTAYTTRRAMDFIDEQ-GERPWCLHLSYIKPHWPYI 243
Cdd:cd16031 145 ---------------------------------------------TDIITDKALDFLKERdKDKPFCLSLSFKAPHRPFT 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 244 APAPYHALYRADQV-LPAL-----------RAAPGEESDHPVYRaFREHreslnfSREDVRRQVIpTYMGLIRQVDDQLG 311
Cdd:cd16031 180 PAPRHRGLYEDVTIpEPETfddddyagrpeWAREQRNRIRGVLD-GRFD------TPEKYQRYMK-DYLRTVTGVDDNVG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 312 RLFQHMRASGRWDDTLIVFTSDHGDFLGDHGLGEKEFLLESAVGVPLLIRDPRPEAdatRGRVEEALVQSIDVLPSILEA 391
Cdd:cd16031 252 RILDYLEEQGLADNTIIIYTSDNGFFLGEHGLFDKRLMYEESIRVPLIIRDPRLIK---AGTVVDALVLNIDFAPTILDL 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 392 FAVEPASHrIEGRSLLPFVHGAPPADWRRYAIAEYDYAFQAPARErlgrpidacRMYMVRSERWKYIAYDGFRA--QLFD 469
Cdd:cd16031 329 AGVPIPED-MQGRSLLPLLEGEKPVDWRKEFYYEYYEEPNFHNVP---------THEGVRTERYKYIYYYGVWDeeELYD 398
|
490 500
....*....|....*....|...
gi 15597529 470 LASDPGELRDLGADPAHAAVREA 492
Cdd:cd16031 399 LKKDPLELNNLANDPEYAEVLKE 421
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
8-475 |
2.54e-90 |
|
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: 279.81 E-value: 2.54e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 8 RNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWNAVPLPLEELT 87
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDGDVPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 88 LGDYLRAAGVRTALVGKTHAtanlegmrrLGIDPasargaalaEAGFEpYDRNdgvypddpafadkrerapythylrrlg 167
Cdd:cd16037 81 WGHALRAAGYETVLIGKLHF---------RGEDQ---------RHGFR-YDRD--------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 168 ftgdnpwhdwanaaagadgeilsgwrmrhaglptrlpeahsetayTTRRAMDFIDEQG--ERPWCLHLSYIKPHWPYIAP 245
Cdd:cd16037 115 ---------------------------------------------VTEAAVDWLREEAadDKPWFLFVGFVAPHFPLIAP 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 246 APYHALYRADqvlpaLRAApgeesdhpvyrafrehreslnfsredvrrqviptYMGLIRQVDDQLGRLFQHMRASGRWDD 325
Cdd:cd16037 150 QEFYDLYVRR-----ARAA----------------------------------YYGLVEFLDENIGRVLDALEELGLLDN 190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 326 TLIVFTSDHGDFLGDHGLGEKEFLLESAVGVPLLIRDPrpeaDATRGRVEEALVQSIDVLPSILEAFAVEPASHRiEGRS 405
Cdd:cd16037 191 TLIIYTSDHGDMLGERGLWGKSTMYEESVRVPMIISGP----GIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL-DGRS 265
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 406 LLPFVHGapPADWRRYAIAEYdYAFQAParerlgrpidaCRMYMVRSERWKYIAYDGFRAQLFDLASDPG 475
Cdd:cd16037 266 LLPLAEG--PDDPDRVVFSEY-HAHGSP-----------SGAFMLRKGRWKYIYYVGYPPQLFDLENDPE 321
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
5-480 |
2.43e-80 |
|
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: 256.73 E-value: 2.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 5 KPirNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWNAVPLPLE 84
Cdd:cd16034 1 KP--NILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVPLPPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 85 ELTLGDYLRAAGVRTALVGKTHatanLEGMRRLgidpasargaalaeagfepydrndgvypddpafaDKRERAPYTHYLR 164
Cdd:cd16034 79 APTIADVLKDAGYRTGYIGKWH----LDGPERN----------------------------------DGRADDYTPPPER 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 165 RLGF-------TGDNPW--HDWANaaaGADGEILSGWrmrhaglptrlpeahsETAYTTRRAMDFIDEQG--ERPWCLHL 233
Cdd:cd16034 121 RHGFdywkgyeCNHDHNnpHYYDD---DGKRIYIKGY----------------SPDAETDLAIEYLENQAdkDKPFALVL 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 234 SYIKPHWPY-IAPAPYHALYRADQVLpaLRaaPGEESDHPVYRAFREHreslnfsredvrrqvIPTYMGLIRQVDDQLGR 312
Cdd:cd16034 182 SWNPPHDPYtTAPEEYLDMYDPKKLL--LR--PNVPEDKKEEAGLRED---------------LRGYYAMITALDDNIGR 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 313 LFQHMRASGRWDDTLIVFTSDHGDFLGDHGLGEKEFLLESAVGVPLLIRDPRPEADatrGRVEEALVQSIDVLPSILEAF 392
Cdd:cd16034 243 LLDALKELGLLENTIVVFTSDHGDMLGSHGLMNKQVPYEESIRVPFIIRYPGKIKA---GRVVDLLINTVDIMPTLLGLC 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 393 AVEPASHrIEGRSLLPFVHG---APPADWRRYAIAEYDYAFQAPARERLGrpidacrmymVRSERWKYIAYDGFRAQLFD 469
Cdd:cd16034 320 GLPIPDT-VEGRDLSPLLLGgkdDEPDSVLLQCFVPFGGGSARDGGEWRG----------VRTDRYTYVRDKNGPWLLFD 388
|
490
....*....|.
gi 15597529 470 LASDPGELRDL 480
Cdd:cd16034 389 NEKDPYQLNNL 399
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
8-501 |
1.25e-74 |
|
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: 242.53 E-value: 1.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 8 RNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRY--VSSHQVAWNAvpLPLEE 85
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLHHL--LRPDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 86 LTLGDYLRAAGVRTALVGKTHATanlegmrrlgidpasargaalaeagfePYDRNDGVYPDDpafadkrerapythylrr 165
Cdd:cd16150 79 PNLLKTLKDAGYHVAWAGKNDDL---------------------------PGEFAAEAYCDS------------------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 166 lgftgdnpwhDWANAaagadgeilsgwrmrhaglptrlpeahsetayttRRAMDFIDE-QGERPWCLHLSYIKPHWPYIA 244
Cdd:cd16150 114 ----------DEACV----------------------------------RTAIDWLRNrRPDKPFCLYLPLIFPHPPYGV 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 245 PAPYHALYRADQvLPALRAAPGeesDHPVYRAFREHRESLNFSR--EDVRRQVIPTYMGLIRQVDDQLGRLFQHMRASGR 322
Cdd:cd16150 150 EEPWFSMIDREK-LPPRRPPGL---RAKGKPSMLEGIEKQGLDRwsEERWRELRATYLGMVSRLDHQFGRLLEALKETGL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 323 WDDTLIVFTSDHGDFLGDHGLGEK--EFLLESAVGVPLLIRDPRpeadATRGRVEEALVQSIDVLPSILEAFAVePASHR 400
Cdd:cd16150 226 YDDTAVFFFSDHGDYTGDYGLVEKwpNTFEDCLTRVPLIIKPPG----GPAGGVSDALVELVDIPPTLLDLAGI-PLSHT 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 401 IEGRSLLPFVHGaPPADWRRYAIAE---------------YDYAFQAPARERLGRPIDACRMYMVRSERWKYIA--YDGf 463
Cdd:cd16150 301 HFGRSLLPVLAG-ETEEHRDAVFSEggrlhgeeqamegghGPYDLKWPRLLQQEEPPEHTKAVMIRTRRYKYVYrlYEP- 378
|
490 500 510
....*....|....*....|....*....|....*...
gi 15597529 464 rAQLFDLASDPGELRDLGADPAHAAVREAHAGMLFDWL 501
Cdd:cd16150 379 -DELYDLEADPLELHNLIGDPAYAEIIAEMKQRLLRWM 415
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
9-502 |
4.16e-74 |
|
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: 239.72 E-value: 4.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRdYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWNA---VPLPLEE 85
Cdd:cd16027 2 NILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRsrgFPLPDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 86 LTLGDYLRAAGVRTALVGKTHatanlegmrrlgidpasargaalaEAGFEPYDRNDGVYPDDPafadkrerapythylrr 165
Cdd:cd16027 81 KTLPELLREAGYYTGLIGKTH------------------------YNPDAVFPFDDEMRGPDD----------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 166 lgfTGDNPWHDWANAAAgadgeilsgWRMRHAGlptrlpeahsetayttrramdfideqgERPWCLHLSYIKPHWPYIAP 245
Cdd:cd16027 120 ---GGRNAWDYASNAAD---------FLNRAKK---------------------------GQPFFLWFGFHDPHRPYPPG 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 246 APYHALYRADQV-----LPalraapgeesDHPVYRafrehreslnfsrEDVRRqviptYMGLIRQVDDQLGRLFQHMRAS 320
Cdd:cd16027 161 DGEEPGYDPEKVkvppyLP----------DTPEVR-------------EDLAD-----YYDEIERLDQQVGEILDELEED 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 321 GRWDDTLIVFTSDHGD-FLGDhglgeKEFLLESAVGVPLLIRDPrpeADATRGRVEEALVQSIDVLPSILEAFAVEPASH 399
Cdd:cd16027 213 GLLDNTIVIFTSDHGMpFPRA-----KGTLYDSGLRVPLIVRWP---GKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 400 rIEGRSLLPfVHGAPPADWRRYAIAEydyafqapaRERLGRPIDACRmyMVRSERWKYIaYDGFRAQLFDLASDPGELRD 479
Cdd:cd16027 285 -LQGRSFLP-LLKGEKDPGRDYVFAE---------RDRHDETYDPIR--SVRTGRYKYI-RNYMPEELYDLKNDPDELNN 350
|
490 500
....*....|....*....|...
gi 15597529 480 LGADPAHAAVREAHAGMLFDWLR 502
Cdd:cd16027 351 LADDPEYAEVLEELRAALDAWMK 373
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
9-405 |
2.38e-73 |
|
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: 233.10 E-value: 2.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQV---AWNAVPLPLEE 85
Cdd:cd16022 2 NILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVrgnVGNGGGLPPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 86 LTLGDYLRAAGVRTALVGKthatanlegmrrlgidpasargaalaeagfepydrndgvypddpafadkrerapythylrr 165
Cdd:cd16022 82 PTLAELLKEAGYRTALIGK------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 166 lgftgdnpWHDwanaaagadgeilsgwrmrhaglptrlpeahsetayttrRAMDFIDEQ-GERPWCLHLSYIKPHWPYia 244
Cdd:cd16022 101 --------WHD---------------------------------------EAIDFIERRdKDKPFFLYVSFNAPHPPF-- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 245 papyhalyradqvlpalraapgeesdhpvyrafrehreslnfsredvrrqvipTYMGLIRQVDDQLGRLFQHMRASGRWD 324
Cdd:cd16022 132 -----------------------------------------------------AYYAMVSAIDDQIGRILDALEELGLLD 158
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 325 DTLIVFTSDHGDFLGDHGL-GEKEFLLESAVGVPLLIRDPrpeADATRGRVEEALVQSIDVLPSILEAFAVEPaSHRIEG 403
Cdd:cd16022 159 NTLIVFTSDHGDMLGDHGLrGKKGSLYEGGIRVPFIVRWP---GKIPAGQVSDALVSLLDLLPTLLDLAGIEP-PEGLDG 234
|
..
gi 15597529 404 RS 405
Cdd:cd16022 235 RS 236
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
9-474 |
3.14e-73 |
|
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: 235.94 E-value: 3.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWNAVPLPLEELTL 88
Cdd:cd16032 2 NILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPADIPTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 89 GDYLRAAGVRTALVGKTHatanlegmrrlgidpasargaalaeagFepydrndgVYPDDpafadkrerapyTHylrrlGF 168
Cdd:cd16032 82 AHYLRAAGYRTALSGKMH---------------------------F--------VGPDQ------------LH-----GF 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 169 TGDNpwhdwanaaagadgeilsgwrmrhaglptrlpeahsETAYTTRRAM-DFIDEQGERPWCLHLSYIKPHWPYIAPAP 247
Cdd:cd16032 110 DYDE------------------------------------EVAFKAVQKLyDLARGEDGRPFFLTVSFTHPHDPYVIPQE 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 248 YHALYradqvlpalraapgeesdhpVYRAfrehreslnfsredvRRqvipTYMGLIRQVDDQLGRLFQHMRASGRWDDTL 327
Cdd:cd16032 154 YWDLY--------------------VRRA---------------RR----AYYGMVSYVDDKVGQLLDTLERTGLADDTI 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 328 IVFTSDHGDFLGDHGLGEKEFLLESAVGVPLLIRDPrpeaDATRGRVEEALVQSIDVLPSILEAFAVEPASHR--IEGRS 405
Cdd:cd16032 195 VIFTSDHGDMLGERGLWYKMSFFEGSARVPLIISAP----GRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVppLDGRS 270
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597529 406 LLPFVHGaPPADWRRYAIAEYdYAFQAPArerlgrPIdacrmYMVRSERWKYIAYDGFRAQLFDLASDP 474
Cdd:cd16032 271 LLPLLEG-GDSGGEDEVISEY-LAEGAVA------PC-----VMIRRGRWKFIYCPGDPDQLFDLEADP 326
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
9-486 |
1.08e-69 |
|
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: 230.15 E-value: 1.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRrDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWNAVP----LPlE 84
Cdd:cd16030 4 NVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYfrkvAP-D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 85 ELTLGDYLRAAGVRTALVGKThatanlegmrrlgidpasargaalaeagFEPYDRNDGVYP---DDPAFADKRERAPYTH 161
Cdd:cd16030 82 AVTLPQYFKENGYTTAGVGKI----------------------------FHPGIPDGDDDPaswDEPPNPPGPEKYPPGK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 162 YLRRLGFTGDNPWHDWANAAAGADGEilsgwrmrhaglptrLPEAHsetayTTRRAMDFIDE--QGERPWCLHLSYIKPH 239
Cdd:cd16030 134 LCPGKKGGKGGGGGPAWEAADVPDEA---------------YPDGK-----VADEAIEQLRKlkDSDKPFFLAVGFYKPH 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 240 WPYIAPAPYHALYRADQVLPALRAAPgeeSDHPVYR-------AFREHRESLNFSR------EDVRRQVIPTYMGLIRQV 306
Cdd:cd16030 194 LPFVAPKKYFDLYPLESIPLPNPFDP---IDLPEVAwndlddlPKYGDIPALNPGDpkgplpDEQARELRQAYYASVSYV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 307 DDQLGRLFQHMRASGRWDDTLIVFTSDHGDFLGDHGLGEKEFLLESAVGVPLLIRDPRPEAdatRGRVEEALVQSIDVLP 386
Cdd:cd16030 271 DAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTK---PGKVTDALVELVDIYP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 387 SILEAFAVEPASHrIEGRSLLPFVHGaPPADWRRYAIAEYdyafqaPARERLGrpidacrmYMVRSERWKYIAYDGFRAQ 466
Cdd:cd16030 348 TLAELAGLPAPPC-LEGKSLVPLLKN-PSAKWKDAAFSQY------PRPSIMG--------YSIRTERYRYTEWVDFDKV 411
|
490 500
....*....|....*....|....
gi 15597529 467 ----LFDLASDPGELRDLGADPAH 486
Cdd:cd16030 412 gaeeLYDHKNDPNEWKNLANDPEY 435
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
3-534 |
9.49e-69 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 229.17 E-value: 9.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 3 QPKPirNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSH-------QVA 75
Cdd:PRK13759 4 TKKP--NIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHgrvgygdVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 76 WNAvplpleELTLGDYLRAAGVRTALVGKTHATANlegMRRLGIDpasargAALAEAGFEPYDRNDGvyPDDPAFADKre 155
Cdd:PRK13759 82 WNY------KNTLPQEFRDAGYYTQCIGKMHVFPQ---RNLLGFH------NVLLHDGYLHSGRNED--KSQFDFVSD-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 156 rapYTHYLRR--LGFTGDNPWHDWANaaagadgeilSGWRMRhaglPTRLPEAHSETAYTTRRAMDFIDE-QGERPWCLH 232
Cdd:PRK13759 143 ---YLAWLREkaPGKDPDLTDIGWDC----------NSWVAR----PWDLEERLHPTNWVGSESIEFLRRrDPTKPFFLK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 233 LSYIKPHWPYIAPAPYHALYRADQVLPALraapgeESDHPVyrAFREHRESL-------NFSREDVRRQVIpTYMGLIRQ 305
Cdd:PRK13759 206 MSFARPHSPYDPPKRYFDMYKDADIPDPH------IGDWEY--AEDQDPEGGsidalrgNLGEEYARRARA-AYYGLITH 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 306 VDDQLGRLFQHMRASGRWDDTLIVFTSDHGDFLGDHGLGEKEFLLESAVGVPLLIRDPRPEADATRGRVEEALVQSIDVL 385
Cdd:PRK13759 277 IDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGNRGTVIDQVVELRDIM 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 386 PSILEAFAVEPAShRIEGRSLLPFVHGAPPAdWRRYAIAEYDYAFQAparerlgrpidacRMYMVrSERWKYI--AYDGf 463
Cdd:PRK13759 357 PTLLDLAGGTIPD-DVDGRSLKNLIFGQYEG-WRPYLHGEHALGYSS-------------DNYLT-DGKWKYIwfSQTG- 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597529 464 RAQLFDLASDPGELRDLGADPAHAAVREAHAGMLFDWLRGlkrrttisnaeidlRGQAFrygePEGGRLVP 534
Cdd:PRK13759 420 EEQLFDLKKDPHELHNLSPSEKYQPRLREMRKKLVDHLRG--------------REEGF----VKDGKLVV 472
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
5-501 |
1.22e-65 |
|
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: 217.43 E-value: 1.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 5 KPirNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICG----PSRMSSYTGRYVSSHQVAwNAVP 80
Cdd:cd16155 2 KP--NILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWSGavcvPSRAMLMTGRTLFHAPEG-GKAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 81 LPLEELTLGDYLRAAGVRTALVGKthatanlegmrrlgidpasargaalaeagfepydrndgvypddpafadkrerapyt 160
Cdd:cd16155 79 IPSDDKTWPETFKKAGYRTFATGK-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 161 hylrrlgftgdnpWH-DWANAAagadgeilsgwrmrhaglptrlpeahsetayttrraMDFIDEQ--GERPWCLHLSYIK 237
Cdd:cd16155 103 -------------WHnGFADAA------------------------------------IEFLEEYkdGDKPFFMYVAFTA 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 238 PHWPYIAPAPYHALYRADQVLPALRAAPGeesdHPVYRAFREHRES--LNFSR-EDVRRQVIPTYMGLIRQVDDQLGRLF 314
Cdd:cd16155 134 PHDPRQAPPEYLDMYPPETIPLPENFLPQ----HPFDNGEGTVRDEqlAPFPRtPEAVRQHLAEYYAMITHLDAQIGRIL 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 315 QHMRASGRWDDTLIVFTSDHGDFLGDHGLGEKEFLLESAVGVPLLIRDPrpeaDATRGRVEEALVQSIDVLPSILEAFAV 394
Cdd:cd16155 210 DALEASGELDNTIIVFTSDHGLAVGSHGLMGKQNLYEHSMRVPLIISGP----GIPKGKRRDALVYLQDVFPTLCELAGI 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 395 EPASHrIEGRSLLPFVHGapPADWRRYAIAeydYAFQAPARerlgrpidacrmyMVRSERWKYIAYDG--FRAQLFDLAS 472
Cdd:cd16155 286 EIPES-VEGKSLLPVIRG--EKKAVRDTLY---GAYRDGQR-------------AIRDDRWKLIIYVPgvKRTQLFDLKK 346
|
490 500
....*....|....*....|....*....
gi 15597529 473 DPGELRDLGADPAHAAVREAhagmLFDWL 501
Cdd:cd16155 347 DPDELNNLADEPEYQERLKK----LLAEL 371
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
9-408 |
2.35e-63 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 208.17 E-value: 2.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWnaVPLPLEELTL 88
Cdd:cd16148 2 NVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWG--GPLEPDDPTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 89 GDYLRAAGVRTALVGKTHATANLEGMRRlgidpasargaalaeaGFEPYDRNDGVYPDDPAFADKRERApythylrrlgf 168
Cdd:cd16148 80 AEILRKAGYYTAAVSSNPHLFGGPGFDR----------------GFDTFEDFRGQEGDPGEEGDERAER----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 169 tgdnpwhdwanaaagadgeilsgwrmrhaglptrlpeahsetayTTRRAMDFIDEQ-GERPWCLHLSYIKPHWPYiapap 247
Cdd:cd16148 133 --------------------------------------------VTDRALEWLDRNaDDDPFFLFLHYFDPHEPY----- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 248 yhalyradqvlpalraapgeesdhpvyrafrehreslnfsredvrrqvipTYMGLIRQVDDQLGRLFQHMRASGRWDDTL 327
Cdd:cd16148 164 --------------------------------------------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTL 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 328 IVFTSDHGDFLGDHGLGEKE--FLLESAVGVPLLIRDPrpeaDATRGRVEEALVQSIDVLPSILEAFAVEPaSHRIEGRS 405
Cdd:cd16148 194 VIVTSDHGEEFGEHGLYWGHgsNLYDEQLHVPLIIRWP----GKEPGKRVDALVSHIDIAPTLLDLLGVEP-PDYSDGRS 268
|
...
gi 15597529 406 LLP 408
Cdd:cd16148 269 LLP 271
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
5-502 |
3.99e-62 |
|
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: 208.24 E-value: 3.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 5 KPirNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWNAVPLPLE 84
Cdd:cd16152 1 KP--NVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNGIPLPAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 85 ELTLGDYLRAAGVRTALVGKthatanlegmrrlgidpasargaalaeagfepydrndgvypddpafadkrerapythylr 164
Cdd:cd16152 79 EKTLAHYFRDAGYETGYVGK------------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 165 rlgftgdnpWHdwanaaagadgeiLSGWRmrhaglptrlpeahseTAYTTRRAMDFIDE-QGERPWCLHLSYIKPH---- 239
Cdd:cd16152 99 ---------WH-------------LAGYR----------------VDALTDFAIDYLDNrQKDKPFFLFLSYLEPHhqnd 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 240 -WPYIAPAPYHALYRADQVLPALRAAPGEESDHpvyrafrehreslnfsredvrrqvIPTYMGLIRQVDDQLGRLFQHMR 318
Cdd:cd16152 141 rDRYVAPEGSAERFANFWVPPDLAALPGDWAEE------------------------LPDYLGCCERLDENVGRIRDALK 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 319 ASGRWDDTLIVFTSDHG-DFL---GDHglgeKEFLLESAVGVPLLIRDPrpeaDATRGRVEEALVQSIDVLPSILEAFAV 394
Cdd:cd16152 197 ELGLYDNTIIVFTSDHGcHFRtrnAEY----KRSCHESSIRVPLVIYGP----GFNGGGRVEELVSLIDLPPTLLDAAGI 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 395 EPaSHRIEGRSLLPFVHGAPPaDWRryaiaeyDYAFQAPARERLGRPIdacrmymvRSERWKYIAY----DGFR------ 464
Cdd:cd16152 269 DV-PEEMQGRSLLPLVDGKVE-DWR-------NEVFIQISESQVGRAI--------RTDRWKYSVAapdkDGWKdsgsdv 331
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15597529 465 ---AQLFDLASDPGELRDLGADPAHAAVREAHAGMLFDWLR 502
Cdd:cd16152 332 yveDYLYDLEADPYELVNLIGRPEYREVAAELRERLLARMA 372
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
9-480 |
1.71e-60 |
|
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: 205.47 E-value: 1.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQL-RRDyLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQV------------- 74
Cdd:cd16144 2 NIVLILVDDLgWAD-LGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdvipgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 75 -----AWNAVPLPLEELTLGDYLRAAGVRTALVGKTHatanlegmrrLGIDPasarGAALAEAGFepyDRNDGVYPDDPA 149
Cdd:cd16144 81 tklipPPSTTRLPLEEVTIAEALKDAGYATAHFGKWH----------LGGEG----GYGPEDQGF---DVNIGGTGNGGP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 150 fadKRERAPYTHYLRRLGFTGDNPWhdwanaaagadgeilsgwrmrhagLPTRLpeahsetaytTRRAMDFIDEQGERPW 229
Cdd:cd16144 144 ---PSYYFPPGKPNPDLEDGPEGEY------------------------LTDRL----------TDEAIDFIEQNKDKPF 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 230 CLHLSYIKPHWPYIAPAPYHALYRADQvlpalraapgeesdhpvyrafrehreslnfsREDVRRQVIPTYMGLIRQVDDQ 309
Cdd:cd16144 187 FLYLSHYAVHTPIQARPELIEKYEKKK-------------------------------KGLRKGQKNPVYAAMIESLDES 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 310 LGRLFQHMRASGRWDDTLIVFTSDHGDFLGDHGL--------GEKEFLLESAVGVPLLIRDPRPEADatrGRVEEALVQS 381
Cdd:cd16144 236 VGRILDALEELGLADNTLVIFTSDNGGLSTRGGPptsnaplrGGKGSLYEGGIRVPLIVRWPGVIKP---GSVSDVPVIG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 382 IDVLPSILEAFAVE-PASHRIEGRSLLPFVHGaPPADWRRYAIaeydYAFQAPARERLGRPIDAcrmymVRSERWKYIA- 459
Cdd:cd16144 313 TDLYPTFLELAGGPlPPPQHLDGVSLVPLLKG-GEADLPRRAL----FWHFPHYHGQGGRPASA-----IRKGDWKLIEf 382
|
490 500
....*....|....*....|.
gi 15597529 460 YDGFRAQLFDLASDPGELRDL 480
Cdd:cd16144 383 YEDGRVELYNLKNDIGETNNL 403
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
9-483 |
5.31e-57 |
|
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293765 [Multi-domain] Cd Length: 409 Bit Score: 195.85 E-value: 5.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTiCGPSRMSSYTGRYvsSHQV-AWNAVP----LPL 83
Cdd:cd16146 2 NVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVSPV-CAPTRAALLTGRY--PFRTgVWHTILgrerMRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 84 EELTLGDYLRAAGVRTALVGKTHatanlegmrrLGidpasargaalAEAGFEPYDRndGvypddpafadkrerapYTHYL 163
Cdd:cd16146 79 DETTLAEVFKDAGYRTGIFGKWH----------LG-----------DNYPYRPQDR--G----------------FDEVL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 164 R-RLGFTGDNPwhDWANAAAGADGEILSGWRMRHAGLPTRLpeahsetayTTRRAMDFIDEQGERPWCLHLSYIKPHWPY 242
Cdd:cd16146 120 GhGGGGIGQYP--DYWGNDYFDDTYYHNGKFVKTEGYCTDV---------FFDEAIDFIEENKDKPFFAYLATNAPHGPL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 243 IAPAPYHALYRaDQVLPALRAapgeesdhpvyrafrehreslnfsredvrrqvipTYMGLIRQVDDQLGRLFQHMRASGR 322
Cdd:cd16146 189 QVPDKYLDPYK-DMGLDDKLA----------------------------------AFYGMIENIDDNVGRLLAKLKELGL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 323 WDDTLIVFTSDHGDFLGDHGL------GEKEFLLESAVGVPLLIRDPRPEADatrGRVEEALVQSIDVLPSILEAFAVE- 395
Cdd:cd16146 234 EENTIVIFMSDNGPAGGVPKRfnagmrGKKGSVYEGGHRVPFFIRWPGKILA---GKDVDTLTAHIDLLPTLLDLCGVKl 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 396 PASHRIEGRSLLPFVHGAPPADWRRYAIAEYDYAFQAPARErlgrpidacRMYMVRSERWKYIAYDGFRAQLFDLASDPG 475
Cdd:cd16146 311 PEGIKLDGRSLLPLLKGESDPWPERTLFTHSGRWPPPPKKK---------RNAAVRTGRWRLVSPKGFQPELYDIENDPG 381
|
....*...
gi 15597529 476 ELRDLGAD 483
Cdd:cd16146 382 EENDVADE 389
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
8-501 |
9.69e-55 |
|
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: 191.44 E-value: 9.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 8 RNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWNAVPLPLEELT 87
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 88 LGDYLRAAGVRTALVGKTHatanLEGMRRLGidpasargaalaeagfepydrnDGVYPD--DPA-FADKR----ERAPYT 160
Cdd:cd16156 81 IGQRLSDNGIHTAYIGKWH----LDGGDYFG----------------------NGICPQgwDPDyWYDMRnyldELTEEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 161 HYLRRLGFTGDNpwhdwanaAAGADGEILSGWRMrhaglptrlpeahsetaytTRRAMDFIDEQGERPWCLHLSYIKPHW 240
Cdd:cd16156 135 RRKSRRGLTSLE--------AEGIKEEFTYGHRC-------------------TNRALDFIEKHKDEDFFLVVSYDEPHH 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 241 PYIAPAPYHALYrADQVLPALRAAPGEESDHPVY-RAFREHRESLNFSREDVRRqviPTYMGLIRQVDDQLGRLFQHMRA 319
Cdd:cd16156 188 PFLCPKPYASMY-KDFEFPKGENAYDDLENKPLHqRLWAGAKPHEDGDKGTIKH---PLYFGCNSFVDYEIGRVLDAADE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 320 SGrwDDTLIVFTSDHGDFLGDHGLGEK-EFLLESAVGVPLLIRDPrpeADATRGRVEEALVQSIDVLPSILEAFAVePAS 398
Cdd:cd16156 264 IA--EDAWVIYTSDHGDMLGAHKLWAKgPAVYDEITNIPLIIRGK---GGEKAGTVTDTPVSHIDLAPTILDYAGI-PQP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 399 HRIEGRSLLPFVH--GAPPAD-----WRRYAIaEYDY--AFQaPARerlgrpidacrmyMVRSERWKYIAYDGFRAQLFD 469
Cdd:cd16156 338 KVLEGESILATIEdpEIPENRgvfveFGRYEV-DHDGfgGFQ-PVR-------------CVVDGRYKLVINLLSTDELYD 402
|
490 500 510
....*....|....*....|....*....|..
gi 15597529 470 LASDPGELRDLGADPAHAAVREAHAGMLFDWL 501
Cdd:cd16156 403 LEKDPYEMHNLIDDPDYADVRDQLHDELLDYM 434
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
9-483 |
3.14e-48 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 172.39 E-value: 3.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGR-----YVSSHQVAWNAVPLPL 83
Cdd:cd16145 2 NIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLhtghtRVRGNSEPGGQDPLPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 84 EELTLGDYLRAAGVRTALVGKthatanlegmrrLGIDPASARGAALAEaGFepyDRNDGVYpdDPAFAdkreRAPYTHYL 163
Cdd:cd16145 82 DDVTLAEVLKKAGYATAAFGK------------WGLGGPGTPGHPTKQ-GF---DYFYGYL--DQVHA----HNYYPEYL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 164 RRLG--FTGDNPWHDWANAAAGADGEilsgwrmrhaglptrlPEAHSETAYTTrRAMDFIDEQGERPWCLHLSYIKPHWP 241
Cdd:cd16145 140 WRNGekVPLPNNVIPPLDEGNNAGGG----------------GGTYSHDLFTD-EALDFIRENKDKPFFLYLAYTLPHAP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 242 YIAPAPYHALYRADQvlpalraaPGEESDHPVYRAFREhreslnfsredvrrqviptYMGLIRQVDDQLGRLFQHMRASG 321
Cdd:cd16145 203 LQVPDDGPYKYKPKD--------PGIYAYLPWPQPEKA-------------------YAAMVTRLDRDVGRILALLKELG 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 322 RWDDTLIVFTSDHG-----------DFLGDHG--LGEKEFLLESAVGVPLLIRDP-RPEAdatrGRVEEALVQSIDVLPS 387
Cdd:cd16145 256 IDENTLVVFTSDNGphseggsehdpDFFDSNGplRGYKRSLYEGGIRVPFIARWPgKIPA----GSVSDHPSAFWDFMPT 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 388 ILEAFAVEPAShRIEGRSLLPFVHGAPPADWRRYAIAEYDYAFQAPArerlgrpidacrmymVRSERWKYIAYDGFRA-- 465
Cdd:cd16145 332 LADLAGAEPPE-DIDGISLLPTLLGKPQQQQHDYLYWEFYEGGGAQA---------------VRMGGWKAVRHGKKDGpf 395
|
490
....*....|....*...
gi 15597529 466 QLFDLASDPGELRDLGAD 483
Cdd:cd16145 396 ELYDLSTDPGETNNLAAQ 413
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
9-480 |
4.86e-48 |
|
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: 170.86 E-value: 4.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQgTICGPSRMSSYTGRYVSSHQVAWNavPLPLEELTL 88
Cdd:cd16151 2 NIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNYVVFG--YLDPKQKTF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 89 GDYLRAAGVRTALVGKTHatanLEGMRRLGIdpasargaALAEAGFEPYDRNDGVYPDDPAFadkrerapythylrrlgf 168
Cdd:cd16151 79 GHLLKDAGYATAIAGKWQ----LGGGRGDGD--------YPHEFGFDEYCLWQLTETGEKYS------------------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 169 tgdNPWHDWANAAAGADGEILSGWrmrhaglptrlpeahsetaY----TTRRAMDFIDEQGERPWCLHLSYIKPHWPYia 244
Cdd:cd16151 129 ---RPATPTFNIRNGKLLETTEGD-------------------YgpdlFADFLIDFIERNKDQPFFAYYPMVLVHDPF-- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 245 papyhalyradqvlpalraAPGEESDHPVYRAFREHRESLNFsREDVrrqvipTYMglirqvDDQLGRLFQHMRASGRWD 324
Cdd:cd16151 185 -------------------VPTPDSPDWDPDDKRKKDDPEYF-PDMV------AYM------DKLVGKLVDKLEELGLRE 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 325 DTLIVFTSDHGDFLGDHGL-------GEKEFLLESAVGVPLLIRDPR--PeadatRGRVEEALVQSIDVLPSILEAFAVE 395
Cdd:cd16151 233 NTIIIFTGDNGTHRPITSRtngrevrGGKGKTTDAGTHVPLIVNWPGliP-----AGGVSDDLVDFSDFLPTLAELAGAP 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 396 -PASHRIEGRSLLPFVHGAPPADWRRYaiaeydYAFQAPARERLGRPidacrmYMVRSERWKYIAYDGFraqlFDLASDP 474
Cdd:cd16151 308 lPEDYPLDGRSFAPQLLGKTGSPRREW------IYWYYRNPHKKFGS------RFVRTKRYKLYADGRF----FDLREDP 371
|
....*.
gi 15597529 475 GELRDL 480
Cdd:cd16151 372 LEKNPL 377
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
5-480 |
4.09e-46 |
|
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: 166.20 E-value: 4.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 5 KPirNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRY------VSSHQVAWNA 78
Cdd:cd16026 1 KP--NIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvglPGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 79 VPLPLEELTLGDYLRAAGVRTALVGKTHatanlegmrrLGIdpasargaalaEAGFEPYDRN-DGVYPddpafadkrerA 157
Cdd:cd16026 79 GGLPPDEITIAEVLKKAGYRTALVGKWH----------LGH-----------QPEFLPTRHGfDEYFG-----------I 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 158 PYTHYLRRLGFTGDNPWHDWANAAAgadGEILSGWRMRHAGLPTRLpeahsetaytTRRAMDFIDEQGERPWCLHLSYIK 237
Cdd:cd16026 127 PYSNDMWPFPLYRNDPPGPLPPLME---NEEVIEQPADQSSLTQRY----------TDEAVDFIERNKDQPFFLYLAHTM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 238 PHWPYIAPAPYHalyradqvlpalraapgEESDHPVYRafrehreslnfsreDVrrqviptymglIRQVDDQLGRLFQHM 317
Cdd:cd16026 194 PHVPLFASEKFK-----------------GRSGAGLYG--------------DV-----------VEELDWSVGRILDAL 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 318 RASGRWDDTLIVFTSDHG------DFLGDHGL--GEKEFLLESAVGVPLLIRDPR--PEadatrGRVEEALVQSIDVLPS 387
Cdd:cd16026 232 KELGLEENTLVIFTSDNGpwleygGHGGSAGPlrGGKGTTWEGGVRVPFIAWWPGviPA-----GTVSDELASTMDLLPT 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 388 ILEAFAVE-PASHRIEGRSLLPFVHGAPPADWRRYAIAEYDYAFQAparerlgrpidacrmymVRSERWKYIAYDGFRA- 465
Cdd:cd16026 307 LAALAGAPlPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQA-----------------VRSGRWKLHLPTTYRTg 369
|
490 500
....*....|....*....|....*....
gi 15597529 466 --------------QLFDLASDPGELRDL 480
Cdd:cd16026 370 tdpggldptkleppLLYDLEEDPGETYNV 398
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
8-392 |
4.17e-44 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 157.97 E-value: 4.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 8 RNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWN-AVPLPLEEL 86
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVStPVGLPRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 87 TLGDYLRAAGVRTALVGKTHATanlegmrrlgidpasargaalaeagfePYDRNDGvypddpafadkrerapythylRRL 166
Cdd:pfam00884 81 SLPDLLKRAGYNTGAIGKWHLG---------------------------WYNNQSP---------------------CNL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 167 GFTGdnpWHDWANAAAGADGEILSGWRMRHAGLPTRLpeahsetayTTRRAMDFIDEQGeRPWCLHLSYIKPHWPYIAPA 246
Cdd:pfam00884 113 GFDK---FFGRNTGSDLYADPPDVPYNCSGGGVSDEA---------LLDEALEFLDNND-KPFFLVLHTLGSHGPPYYPD 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 247 PYHALYRAdqvlpalraapgeesdhpvyrafrehreslNFSREDVRRQVIPTYMGLIRQVDDQLGRLFQHMRASGRWDDT 326
Cdd:pfam00884 180 RYPEKYAT------------------------------FKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNT 229
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 327 LIVFTSDHGDFLGD---HGLGEKEFLL-ESAVGVPLLIRDPRpeaDATRGRVEEALVQSIDVLPSILEAF 392
Cdd:pfam00884 230 LVVYTSDHGESLGEgggYLHGGKYDNApEGGYRVPLLIWSPG---GKAKGQKSEALVSHVDLFPTILDLA 296
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
9-480 |
4.25e-39 |
|
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: 146.93 E-value: 4.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQgTICGPSRMSSYTGRYVS----SHQVAWNAVP--LP 82
Cdd:cd16029 2 HIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIhtgmQHGVILAGEPygLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 83 LEELTLGDYLRAAGVRTALVGKTHAtanleGMRRLGIDPAsARGaalaeagfepYDRNDGVYPDDPAFadkrerapYTHY 162
Cdd:cd16029 81 LNETLLPQYLKELGYATHLVGKWHL-----GFYTWEYTPT-NRG----------FDSFYGYYGGAEDY--------YTHT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 163 LRRLGFTGDNPWHDWANAAAGADGEilsgwrmrhaglptrlpeaHSETAYtTRRAMDFIDEQ-GERPWCLHLSYIKPHWP 241
Cdd:cd16029 137 SGGANDYGNDDLRDNEEPAWDYNGT-------------------YSTDLF-TDRAVDIIENHdPSKPLFLYLAFQAVHAP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 242 YIAPAPYHALYradqvlpalraaPGEESDHPvyrafrehreslnfsreDVRRQvipTYMGLIRQVDDQLGRLFQHMRASG 321
Cdd:cd16029 197 LQVPPEYADPY------------EDKFAHIK-----------------DEDRR---TYAAMVSALDESVGNVVDALKAKG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 322 RWDDTLIVFTSDHG-DFLGDHG-----L-GEKEFLLESAVGVPLLIRDPRPEadATRGRVEEALVQSIDVLPSILEAFAV 394
Cdd:cd16029 245 MLDNTLIVFTSDNGgPTGGGDGgsnypLrGGKNTLWEGGVRVPAFVWSPLLP--PKRGTVSDGLMHVTDWLPTLLSLAGG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 395 EPASHR-IEGRSLLP-FVHGAPPAdwRR---YAIAEYDYAFQAPArerlgrpidacrmymVRSERWKYIAydGFraQLFD 469
Cdd:cd16029 323 DPDDLPpLDGVDQWDaLSGGAPSP--RTeilLNIDDITRTTGGAA---------------IRVGDWKLIV--GK--PLFN 381
|
490
....*....|.
gi 15597529 470 LASDPGELRDL 480
Cdd:cd16029 382 IENDPCERNDL 392
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
5-406 |
5.81e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 143.67 E-value: 5.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 5 KPirNVLYIMCDQLRRDYLSCYGHP----------YLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQV 74
Cdd:cd16153 1 KP--NILWIITDDQRVDSLSCYNNAhtgksesrlgYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 75 -----AWNAVPLPLEelTLGDYLRAAGVRTALVGKTHAtanlegmrrlgidpasargaalaeagfepydrndgvypddpa 149
Cdd:cd16153 79 ygfeaAHPALDHGLP--TFPEVLKKAGYQTASFGKSHL------------------------------------------ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 150 fadkrerAPYTHYLRRLGFTGDNPWHdwaNAAAGADgeilsgwrmrhaglptrlpeahsetayttrramdfideqGERPW 229
Cdd:cd16153 115 -------EAFQRYLKNANQSYKSFWG---KIAKGAD---------------------------------------SDKPF 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 230 CLHLSYIKPHWPYIAPAPYHALYRadqvlpalraapgeesdhpvyrafrehreslnfsredvrrqviptYMGLIRQVDDQ 309
Cdd:cd16153 146 FVRLSFLQPHTPVLPPKEFRDRFD---------------------------------------------YYAFCAYGDAQ 180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 310 LGRLFQHMRASGRW---DDTLIVFTSDHGDFLGDHGLGEKEFLLESAVGVPLLIRDPRPEAdATRGRVEEALVQSIDVLP 386
Cdd:cd16153 181 VGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGILAKFTFWPQSHRVPLIVVSSDKLK-APAGKVRHDFVEFVDLAP 259
|
410 420
....*....|....*....|.
gi 15597529 387 SILEAFAVEPASHR-IEGRSL 406
Cdd:cd16153 260 TLLAAAGVDVDAPDyLDGRDL 280
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
9-427 |
9.47e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 143.89 E-value: 9.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLR--RDYLScyGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWNAVPLPLEEL 86
Cdd:cd16035 2 NILLILTDQERypPPWPA--GWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 87 -----TLGDYLRAAGVRTALVGKTHATanlegmrrlgidpasarGAALaeagfepydrndGVYPDDPAFADkrerapyth 161
Cdd:cd16035 80 spdvpTLGHMLRAAGYYTAYKGKWHLS-----------------GAAG------------GGYKRDPGIAA--------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 162 ylrrlgftgdnpwhdwanaaagadgeilsgwrmrhaglptrlpeahsetayttrRAMDFIDEQGER-----PWCLHLSYI 236
Cdd:cd16035 122 ------------------------------------------------------QAVEWLRERGAKnadgkPWFLVVSLV 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 237 KPHwpyiapapyhalyraDQVLPalraaPGEEsdhpvyrafREHRESLNFsredvrrqviptYMGLIRQVDDQLGRLFQH 316
Cdd:cd16035 148 NPH---------------DIMFP-----PDDE---------ERWRRFRNF------------YYNLIRDVDRQIGRVLDA 186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 317 MRASGRWDDTLIVFTSDHGDFLGDHGLGEKEFLL-ESAVGVPLLIRDPRPeadATRGRVEEALVQSIDVLPSILE----- 390
Cdd:cd16035 187 LDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAyEEALHVPLIISHPDL---FGTGQTTDALTSHIDLLPTLLGlagvd 263
|
410 420 430
....*....|....*....|....*....|....*..
gi 15597529 391 AFAVEPASHRIEGRSLLPFVHGAPPADWRRYAIAEYD 427
Cdd:cd16035 264 AEARATEAPPLPGRDLSPLLTDADADAVRDGILFTYD 300
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
9-480 |
6.94e-35 |
|
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: 135.26 E-value: 6.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLrrDY--LSCYGHPyLHTPNIDRLAAEGVRFARAYTQGtICGPSRMSSYTGRYvsSHQV-----AWNAVP- 80
Cdd:cd16025 4 NILLILADDL--GFsdLGCFGGE-IPTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRN--HHQVgmgtmAELATGk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 81 ------LPLEELTLGDYLRAAGVRTALVGKthatanlegmrrlgidpasargaalaeagfepydrndgvypddpafadkr 154
Cdd:cd16025 78 pgyegyLPDSAATIAEVLKDAGYHTYMSGK-------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 155 erapythylrrlgftgdnpWHdwanaaAGADGEilsgwrmrhaglptrlpeaHSETAYTTrRAMDFIDEQ--GERPWCLH 232
Cdd:cd16025 108 -------------------WH------LGPDDY-------------------YSTDDLTD-KAIEYIDEQkaPDKPFFLY 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 233 LSYIKPHWPYIAPAPYHALYRA--DQ-----------------VLPALRAAPGEESDHPVYrafrehrESLNFSREDV-- 291
Cdd:cd16025 143 LAFGAPHAPLQAPKEWIDKYKGkyDAgwdalreerlerqkelgLIPADTKLTPRPPGVPAW-------DSLSPEEKKLea 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 292 RRQVIptYMGLIRQVDDQLGRLFQHMRASGRWDDTLIVFTSDHGdflgdhGLGE--------------KEFLLESAVGVP 357
Cdd:cd16025 216 RRMEV--YAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNG------ASAEpgwanasntpfrlyKQASHEGGIRTP 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 358 LLIRdpRPEADATRGRVEEALVQSIDVLPSILEAFAVEPASHR-------IEGRSLLPFVHGAPPADWRRYaiaeydYAF 430
Cdd:cd16025 288 LIVS--WPKGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVngvpqlpLDGVSLLPTLDGAAAPSRRRT------QYF 359
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15597529 431 qaparERLGRpidacrmYMVRSERWKYIAY-----DGFRAQLFDLASDPGELRDL 480
Cdd:cd16025 360 -----ELFGN-------RAIRKGGWKAVALhpppgWGDQWELYDLAKDPSETHDL 402
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
9-480 |
1.21e-33 |
|
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: 131.94 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLrrDY--LSCYG-HPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYV----SSHQVAWNAVPL 81
Cdd:cd16143 2 NIVIILADDL--GYgdISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPwrsrLKGGVLGGFSPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 82 PLEE--LTLGDYLRAAGVRTALVGKTHatanlegmrrLGIDpasargaalaeagfepYDRNDGvypdDPAFADKRERAPY 159
Cdd:cd16143 80 LIEPdrVTLAKMLKQAGYRTAMVGKWH----------LGLD----------------WKKKDG----KKAATGTGKDVDY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 160 THYLRR----LGFtgDnpwHDWANAAagadGEIlsgwrmrhagLPTrlpeahsetayTTRRAMDFIDEQ--GERPWCLHL 233
Cdd:cd16143 130 SKPIKGgpldHGF--D---YYFGIPA----SEV----------LPT-----------LTDKAVEFIDQHakKDKPFFLYF 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 234 SYIKPHWPyIAPAPYhalYRAdqvlpalRAAPGEESDHpvyrafrehreslnfsredvrrqviptymglIRQVDDQLGRL 313
Cdd:cd16143 180 ALPAPHTP-IVPSPE---FQG-------KSGAGPYGDF-------------------------------VYELDWVVGRI 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 314 FQHMRASGRWDDTLIVFTSDHG-------DFLGDHGL-------GEKEFLLESAVGVPLLIRDPrpeaDATR-GRVEEAL 378
Cdd:cd16143 218 LDALKELGLAENTLVIFTSDNGpspyadyKELEKFGHdpsgplrGMKADIYEGGHRVPFIVRWP----GKIPaGSVSDQL 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 379 VQSIDVLPSILEAFAVE-PASHRIEGRSLLPFVHGAPPADWRRYAIAEydyafqaparerlgrpiDACRMYMVRSERWKY 457
Cdd:cd16143 294 VSLTDLFATLAAIVGQKlPDNAAEDSFSFLPALLGPKKQEVRESLVHH-----------------SGNGSFAIRKGDWKL 356
|
490 500 510
....*....|....*....|....*....|....*...
gi 15597529 458 IAYDGF---------------RAQLFDLASDPGELRDL 480
Cdd:cd16143 357 IDGTGSggfsyprgkeklglpPGQLYNLSTDPGESNNL 394
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
5-484 |
6.10e-33 |
|
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: 129.98 E-value: 6.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 5 KPirNVLYIMCDQLRRDYLSCYGHPYLHtpniDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWNAVPLP-- 82
Cdd:cd16147 1 RP--NIVLILTDDQDVELGSMDPMPKTK----KLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPPGGgy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 83 -------LEELTLGDYLRAAGVRTALVGKThatanLEGMRRLGidpasarGAALAEAGFepyDRNDGVYPddpafadkre 155
Cdd:cd16147 75 pkfwqngLERSTLPVWLQEAGYRTAYAGKY-----LNGYGVPG-------GVSYVPPGW---DEWDGLVG---------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 156 raPYTHYLRRLGFTGDNpwhdwanaaagadgeilsgwrmrhaGLPTRLPEAHSeTAYTTRRAMDFIDE--QGERPWCLHL 233
Cdd:cd16147 130 --NSTYYNYTLSNGGNG-------------------------KHGVSYPGDYL-TDVIANKALDFLRRaaADDKPFFLVV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 234 SYIKPHWPYiAPAPYHALYRADQVLPALRAAPgeESDHP-----VYRAFREHRESLNFSREDVRRQviptyMGLIRQVDD 308
Cdd:cd16147 182 APPAPHGPF-TPAPRYANLFPNVTAPPRPPPN--NPDVSdkphwLRRLPPLNPTQIAYIDELYRKR-----LRTLQSVDD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 309 QLGRLFQHMRASGRWDDTLIVFTSDHGDFLGDHGLG-EKEFLLESAVGVPLLIRDPrpeaDATRGRVEEALVQSIDVLPS 387
Cdd:cd16147 254 LVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPpGKRTPYEEDIRVPLLVRGP----GIPAGVTVDQLVSNIDLAPT 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 388 ILEAFAVEPASHrIEGRSllpfvhgAPPADWRRYaiaeydyafqaparerlgrpidACrmymVRSERWKYIAY-----DG 462
Cdd:cd16147 330 ILDLAGAPPPSD-MDGRS-------CGDSNNNTY----------------------KC----VRTVDDTYNLLyfewcTG 375
|
490 500
....*....|....*....|..
gi 15597529 463 FRaQLFDLASDPGELRDLGADP 484
Cdd:cd16147 376 FR-ELYDLTTDPYQLTNLAGDL 396
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
9-408 |
2.24e-31 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 121.96 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQV-----------AWN 77
Cdd:cd16149 2 NILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivegshgkTKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 78 AVPLPLEELTLGDYLRAAGVRTALVGKthatanlegmrrlgidpasargaalaeagfepydrndgvypddpafadkrera 157
Cdd:cd16149 82 PEGYLEGQTTLPEVLQDAGYRCGLSGK----------------------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 158 pythylrrlgftgdnpWHdwanaaAGADgeilsgwrmrhaglptrlpeahsetayttrrAMDFIDEQ--GERPWCLHLSY 235
Cdd:cd16149 109 ----------------WH------LGDD-------------------------------AADFLRRRaeAEKPFFLSVNY 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 236 IKPH--WPYIApapyhalyradqvlpALRAapgeesdhpvyrafrehreslnfsredvrrqviptymglirqVDDQLGRL 313
Cdd:cd16149 136 TAPHspWGYFA---------------AVTG------------------------------------------VDRNVGRL 158
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 314 FQHMRASGRWDDTLIVFTSDHGDFLGDHGLGEK------EFLLESAVGVPLLIRDPrpeADATRGRVEEALVQSIDVLPS 387
Cdd:cd16149 159 LDELEELGLTENTLVIFTSDNGFNMGHHGIWGKgngtfpLNMYDNSVKVPFIIRWP---GVVPAGRVVDSLVSAYDFFPT 235
|
410 420
....*....|....*....|..
gi 15597529 388 ILEAFAVEPASH-RIEGRSLLP 408
Cdd:cd16149 236 LLELAGVDPPADpRLPGRSFAD 257
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
9-476 |
1.47e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 111.29 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYG----HPylHTPNIDRLAAEGVRFARAYTQGTiCGPSRMSSYTGRYVSSHQVAWNAVPLPLE 84
Cdd:cd16154 2 NILLIIADDQGLDSSAQYSlssdLP--VTPTLDSLANSGIVFDNLWATPA-CSPTRATILTGKYGFRTGVLAVPDELLLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 85 ELTLGDYL----RAAGVRTALVGKTHATANLEGMRRLGIDPasargaalaeagfepydrndgvypddpafadkrerapyt 160
Cdd:cd16154 79 EETLLQLLikdaTTAGYSSAVIGKWHLGGNDNSPNNPGGIP--------------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 161 HYLRRLGFTGDNPWHdwanaaagadgeilsgWRMRHAGLPTRLPEAHseTAYTTRRAMDFIDEQGErPWCLHLSYIKPHW 240
Cdd:cd16154 120 YYAGILGGGVQDYYN----------------WNLTNNGQTTNSTEYA--TTKLTNLAIDWIDQQTK-PWFLWLAYNAPHT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 241 PYIAPaPyHALyradqvlpalraapgeesdhpvyrafreHRESLNFSREDVRRQVIPTYMGLIRQVDDQLGRLFQHMRAS 320
Cdd:cd16154 181 PFHLP-P-AEL----------------------------HSRSLLGDSADIEANPRPYYLAAIEAMDTEIGRLLASIDEE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 321 GRwDDTLIVFTSDHG--------DFLGDHGlgeKEFLLESAVGVPLLIRDprpeADATR-GRVEEALVQSIDVLPSILEA 391
Cdd:cd16154 231 ER-ENTIIIFIGDNGtpgqvvdlPYTRNHA---KGSLYEGGINVPLIVSG----AGVERaNERESALVNATDLYATIAEL 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 392 FAVEPA----SHRIegRSLLPFVhgapPADWRRYAIAEYDYAFQAparerlgrpidacrMYMVRSERWKYIAYDGFRAQL 467
Cdd:cd16154 303 AGVDAAeihdSVSF--KPLLSDV----NASTRQYNYTEYESPTTT--------------GWATRNQYYKLIESENGQEEL 362
|
....*....
gi 15597529 468 FDLASDPGE 476
Cdd:cd16154 363 YDLINDPSE 371
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
9-474 |
5.18e-22 |
|
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: 97.61 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQvAWNAVP-LPLEELT 87
Cdd:cd16171 2 NVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTE-SWNNYKgLDPNYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 88 LGDYLRAAGVRTALVGKTHATAnlegmrrlGIDPASARgaalaeagFEPYDRndgvypdDPAFADKRERAPYTHylrrlg 167
Cdd:cd16171 81 WMDRLEKHGYHTQKYGKLDYTS--------GHHSVSNR--------VEAWTR-------DVPFLLRQEGRPTVN------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 168 FTGDNPW-----HDWANAAAGadgeilSGWrMRHaglptrlpEAHSETayttrramdfideqgeRPWCLHLSYIKPHwPY 242
Cdd:cd16171 132 LVGDRSTvrvmlKDWQNTDKA------VHW-IRK--------EAPNLT----------------QPFALYLGLNLPH-PY 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 243 iaPAPYHalyradqvlpalraapGEesdhpvyrafrehreslNF-SREDVRrqviPTYMGLIRQVDDQLGRLFQHMRASG 321
Cdd:cd16171 180 --PSPSM----------------GE-----------------NFgSIRNIR----AFYYAMCAETDAMLGEIISALKDTG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 322 RWDDTLIVFTSDHGDFLGDHGLGEKEFLLESAVGVPLLIRDPRPEAdatrGRVEEALVQSIDVLPSILEaFAVEPASHRI 401
Cdd:cd16171 221 LLDKTYVFFTSDHGELAMEHRQFYKMSMYEGSSHVPLLIMGPGIKA----GQQVSDVVSLVDIYPTMLD-IAGVPQPQNL 295
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597529 402 EGRSLLPFVhgappadwRRYAIAEYDYAFQAPA---RERLGRPIDAcRMYMVRSERWKYIAY-DGFR--AQLFDLASDP 474
Cdd:cd16171 296 SGYSLLPLL--------SESSIKESPSRVPHPDwvlSEFHGCNVNA-STYMLRTNSWKYIAYaDGNSvpPQLFDLSKDP 365
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
5-485 |
5.56e-22 |
|
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: 98.66 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 5 KPirNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRY------VSSHQV--AW 76
Cdd:cd16160 1 KP--NIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLpirsgmYGGTRVflPW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 77 NAVPLPLEELTLGDYLRAAGVRTALVGKTHatanlegmrrLGIDpasargaalaeagfePYDRNDGVY-PDDPAFADKRE 155
Cdd:cd16160 79 DIGGLPKTEVTMAEALKEAGYTTGMVGKWH----------LGIN---------------ENNHSDGAHlPSHHGFDFVGT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 156 RAPYTHYLrRLGFTGDNPWHDWANAAAGADGEILSGWRMRHAGLPTRLPEAhsetayttrrAMDFIDEQGERPWCLHLSY 235
Cdd:cd16160 134 NLPFTNSW-ACDDTGRHVDFPDRSACFLYYNDTIVEQPIQHEHLTETLVGD----------AKSFIEDNQENPFFLYFSF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 236 IKPHWPYIApapyhalyradqvlpalraapgeeSDHpvyrafrehreslnFSREDVRRQviptYMGLIRQVDDQLGRLFQ 315
Cdd:cd16160 203 PQTHTPLFA------------------------SKR--------------FKGKSKRGR----YGDNINEMSWAVGEVLD 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 316 HMRASGRWDDTLIVFTSDHGDFL------GDHGL--GEKEFLLESAVGVPLLIRDPrpeaDATRGRVEEALVQSIDVLPS 387
Cdd:cd16160 241 TLVDTGLDQNTLVFFLSDHGPHVeyclegGSTGGlkGGKGNSWEGGIRVPFIAYWP----GTIKPRVSHEVVSTMDIFPT 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 388 ILE-AFAVEPASHRIEGRSLLPFV---HGAPPAD-------------WRRYAIAEYDYAFqaPARERLGrpIDACRMYMV 450
Cdd:cd16160 317 FVDlAGGTLPTDRIYDGLSITDLLlgeADSPHDDilyyccsrlmavrYGSYKIHFKTQPL--PSQESLD--PNCDGGGPL 392
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15597529 451 RSERWKYIAYDGFRAQL-----FDLASDPGELRDLGADPA 485
Cdd:cd16160 393 SDYIVCYDCEDECVTKHnppliFDVEKDPGEQYPLQPSVY 432
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
8-392 |
1.87e-20 |
|
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: 91.59 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 8 RNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRM--SSYTGRYvSSHQVAWNAVPLPLEE 85
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLP-PLPLGSGSYTLYKLNP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 86 L-TLGDYLRAAGVRTAlvgkthatanlegmrrlgidpasargaalaeagfepydrndGVYPDDPAFADKRErapythYLR 164
Cdd:cd16015 80 LpSLPSILKEQGYETI-----------------------------------------FIHGGDASFYNRDS------VYP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 165 RLGFTgdnpwHDWANAAAGADGEILSGWrmrhaGLPTrlpeahsetAYTTRRAMDFIDEQGERPWCLHLSYIKPHWPYIA 244
Cdd:cd16015 113 NLGFD-----EFYDLEDFPDDEKETNGW-----GVSD---------ESLFDQALEELEELKKKPFFIFLVTMSNHGPYDL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 245 PapyhalyradqvlpalraapgeesdhpvyrafrEHRESLNFSREDVRRQVIpTYMGLIRQVDDQLGRLFQHMRASGRWD 324
Cdd:cd16015 174 P---------------------------------EEKKDEPLKVEEDKTELE-NYLNAIHYTDKALGEFIEKLKKSGLYE 219
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597529 325 DTLIVFTSDHGDFLGDHGLGEKEFLLESAVgVPLLIRDPrpeaDATRGRVEEALVQSIDVLPSILEAF 392
Cdd:cd16015 220 NTIIVIYGDHLPSLGSDYDETDEDPLDLYR-TPLLIYSP----GLKKPKKIDRVGSQIDIAPTLLDLL 282
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
9-142 |
6.18e-20 |
|
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: 92.89 E-value: 6.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYvsshQVAWNAVP-------- 80
Cdd:cd16158 3 NIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRY----QVRSGVYPgvfypgsr 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597529 81 --LPLEELTLGDYLRAAGVRTALVGKTHATANLEGM---------RRLGIDPASARGAALAEAGFEPYDRNDG 142
Cdd:cd16158 79 ggLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGTylpthqgfdHYLGIPYSHDQGPCQNLTCFPPNIPCFG 151
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
9-481 |
2.52e-18 |
|
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: 86.82 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGH------PylhTPNIDRLAAEGVRFARAYTQGTiCGPSRMSSYTGRYV---SSHQVAWNAV 79
Cdd:cd16142 2 NILVILGDDIGWGDLGCYGGgigrgaP---TPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPirtGLTTVGLPGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 80 P--LPLEELTLGDYLRAAGVRTALVGKTHatanlegmrrLGidpasargaalaeagfepydrndgvypddpafaDKRERA 157
Cdd:cd16142 78 PggLPPWEPTLAELLKDAGYATAQFGKWH----------LG---------------------------------DEDGRL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 158 PYTHylrrlGFtgdnpwhD--WANAAAGADGEIlsgwrmrhaglptrlpeahsetaytTRRAMDFIDEQ--GERPWCLHL 233
Cdd:cd16142 115 PTDH-----GF-------DefYGNLYHTIDEEI-------------------------VDKAIDFIKRNakADKPFFLYV 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 234 SYIKPHWPYIaPAPYHAlyradqvlpalraapGEESDHPVYRAfrehreslnfsredvrrqviptymGLIrQVDDQLGRL 313
Cdd:cd16142 158 NFTKMHFPTL-PSPEFE---------------GKSSGKGKYAD------------------------SMV-ELDDHVGQI 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 314 FQHMRASGRWDDTLIVFTSDHG---DFLGDHGL----GEKEFLLESAVGVPLLIRDP-RPEAdatrGRVEEALVQSIDVL 385
Cdd:cd16142 197 LDALDELGIADNTIVIFTTDNGpeqDVWPDGGYtpfrGEKGTTWEGGVRVPAIVRWPgKIKP----GRVSNEIVSHLDWF 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 386 PSILEAFAVEPASHR-------IEGRSLLPFVHGAPPADWRRYAIAEYDYAFQAparerlgrpidacrmymVRSERWKYI 458
Cdd:cd16142 273 PTLAALAGAPDPKDKllgkdrhIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGA-----------------VRWKNWKVH 335
|
490 500 510
....*....|....*....|....*....|....*..
gi 15597529 459 --------------AYDGFRAQLFDLASDPGELRDLG 481
Cdd:cd16142 336 fkaqedtggptgepFYVLTFPLIFNLRRDPKERYDVT 372
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
5-412 |
1.53e-17 |
|
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: 85.42 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 5 KPirNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRY------VSSHQVA--- 75
Cdd:cd16159 1 KP--NIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmASSHGMRvil 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 76 WNAVP--LPLEELTLGDYLRAAGVRTALVGKTHatanlegmrrLGIDPASargaalaeagfepydRNDGVY-PDDPAFaD 152
Cdd:cd16159 79 FTASSggLPPNETTFAEVLKQQGYSTALIGKWH----------LGLHCES---------------RNDFCHhPLNHGF-D 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 153 KRERAPYTHYL-------RRLGFTGDNPWHDWANAAAGADGEILSGWRMRHAG--------------------LPTRLP- 204
Cdd:cd16159 133 YFYGLPLTNLKdcgdgsnGEYDLSFDPLFPLLTAFVLITALTIFLLLYLGAVSkrffvfllilsllfislfflLLITNRy 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 205 ------------EAHSETAYTTRR----AMDFIDEQGERPWCLHLSYIKPHWPYIAPAPY-----HALYrADQVlpalra 263
Cdd:cd16159 213 fncilmrnhevvEQPMSLENLTQRltkeAISFLERNKERPFLLVMSFLHVHTALFTSKKFkgrskHGRY-GDNV------ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 264 apgEESDHPVyrafrehreslnfsredvrrqviptymGLIRQVDDQLGRLfqhmrasgrwDDTLIVFTSDHGDFL----- 338
Cdd:cd16159 286 ---EEMDWSV---------------------------GQILDALDELGLK----------DNTFVYFTSDNGGHLeeisv 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 339 -GDHGLGEKEFL-------LESAVGVPLLIRDPRpeaDATRGRVEEALVQSIDVLPSILE-AFAVEPASHRIEGRSLLPF 409
Cdd:cd16159 326 gGEYGGGNGGIYggkkmggWEGGIRVPTIVRWPG---VIPPGSVIDEPTSLMDIFPTVAAlAGAPLPSDRIIDGRDLMPL 402
|
...
gi 15597529 410 VHG 412
Cdd:cd16159 403 LTG 405
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
8-407 |
4.67e-17 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 84.32 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 8 RNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTicgpsrMSSYTgryvsshqvawnavplpLEELT 87
Cdd:COG1368 235 PNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGG------RTSRG-----------------EFAVL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 88 LGDYLRAAGVrtalVGKTHATANLEGMrrlgidpasarGAALAEAGFEPYdrndGVYPDDPAFaDKRERapythYLRRLG 167
Cdd:COG1368 292 TGLPPLPGGS----PYKRPGQNNFPSL-----------PSILKKQGYETS----FFHGGDGSF-WNRDS-----FYKNLG 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 168 FT---GDNpwhDWANAAAGadgeilsGWRMrhaglptrlpeaHSETAYttRRAMDFIDEQGErPWCLHLSYIKPHWPYIA 244
Cdd:COG1368 347 FDefyDRE---DFDDPFDG-------GWGV------------SDEDLF--DKALEELEKLKK-PFFAFLITLSNHGPYTL 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 245 PAPYHALYradqvlpalrAAPGEESDhpvyrafrehreslnfsredvrrqvipTYMGLIRQVDDQLGRLFQHMRASGRWD 324
Cdd:COG1368 402 PEEDKKIP----------DYGKTTLN---------------------------NYLNAVRYADQALGEFIEKLKKSGWYD 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 325 DTLIVFTSDHGDFLGDHglgEKEFLLESAVGVPLLIRDPrpeaDATRGRVEEALVQSIDVLPSILEAFAVEPASHRIEGR 404
Cdd:COG1368 445 NTIFVIYGDHGPRSPGK---TDYENPLERYRVPLLIYSP----GLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGR 517
|
...
gi 15597529 405 SLL 407
Cdd:COG1368 518 DLL 520
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
9-410 |
1.28e-16 |
|
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: 82.51 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGR------YVSSHQVAWNA-VP- 80
Cdd:cd16157 3 NIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRlpirngFYTTNAHARNAyTPq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 81 -----LPLEELTLGDYLRAAGVRTALVGKTHAtanleGMR------RLGIDpaSARGAalAEAGFEPYDrnDGVYPDDPA 149
Cdd:cd16157 83 nivggIPDSEILLPELLKKAGYRNKIVGKWHL-----GHRpqyhplKHGFD--EWFGA--PNCHFGPYD--NKAYPNIPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 150 FADKRERAPYTHYLRRLGFTGDnpwhdwANAaagadgeilsgwrmrhaglptrlpeahseTAYTTRRAMDFIDEQGERPw 229
Cdd:cd16157 152 YRDWEMIGRYYEEFKIDKKTGE------SNL-----------------------------TQIYLQEALEFIEKQHDAQ- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 230 clhlsyiKPHWPYIAPAPYHAlyradqvlpalraapgeesdhPVY--RAFrehresLNFSREDVrrqviptYMGLIRQVD 307
Cdd:cd16157 196 -------KPFFLYWAPDATHA---------------------PVYasKPF------LGTSQRGL-------YGDAVMELD 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 308 DQLGRLFQHMRASGRWDDTLIVFTSDHGDFL-------GDHG--LGEKEFLLESAVGVPLLIRDPrpeADATRGRVEEAL 378
Cdd:cd16157 235 SSVGKILESLKSLGIENNTFVFFSSDNGAALisapeqgGSNGpfLCGKQTTFEGGMREPAIAWWP---GHIKPGQVSHQL 311
|
410 420 430
....*....|....*....|....*....|...
gi 15597529 379 VQSIDVLPSILEAFAVEPASHR-IEGRSLLPFV 410
Cdd:cd16157 312 GSLMDLFTTSLALAGLPIPSDRaIDGIDLLPVL 344
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
9-412 |
1.38e-14 |
|
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: 75.58 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 9 NVLYIMCDQLRRDYLSCYGHP-YLHTPNIDRLAAEGVRFARAYTQGTICGPSRMSSYTGRYVSSHQVAWNAVP-----LP 82
Cdd:cd16161 3 NFLLLFADDLGWGDLGANWAPnAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPtsvggLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 83 LEELTLGDYLRAAGVRTALVGKTHatanlegmrrLGIdpasaRGAALAEA-GFEPYdrnDGV-YPDDPAFADKrerapyt 160
Cdd:cd16161 83 LNETTLAEVLRQAGYATGMIGKWH----------LGQ-----REAYLPNSrGFDYY---FGIpFSHDSSLADR------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 161 hylrrlgftgdnpwhdWANAAAgadgeilsGWRMRHAglptrlpeahsetayttrramdfideQGERPWCLHLSYIKPHW 240
Cdd:cd16161 138 ----------------YAQFAT--------DFIQRAS--------------------------AKDRPFFLYAALAHVHV 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 241 PyiapapyhalyraDQVLPalRAAPGEESDHPVYRAFREhreslnfsredvrrqviptymglirqVDDQLGRLFQHMRAS 320
Cdd:cd16161 168 P-------------LANLP--RFQSPTSGRGPYGDALQE--------------------------MDDLVGQIMDAVKHA 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 321 GRWDDTLIVFTSD---------------HGDFLGDHGL-GEKEFLLESAVGVPLLIRDPrpeadatrGRVEE-----ALV 379
Cdd:cd16161 207 GLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGsVAKASTWEGGHREPAIVYWP--------GRIPAnstsaALV 278
|
410 420 430
....*....|....*....|....*....|....
gi 15597529 380 QSIDVLPSILE-AFAVEPASHRIEGRSLLPFVHG 412
Cdd:cd16161 279 STLDIFPTVVAlAGASLPPGRIYDGKDLSPVLFG 312
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
8-392 |
2.82e-13 |
|
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: 69.37 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 8 RNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRF-ARAYTQGTICGPSRMSSYTGRYVSSHQVAWN--------- 77
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNgsadpelps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 78 -AVPLPLEELTLGDYLRAAGVRTALVGkthatanlegmrrlgidpasargaalaeagfepydrndgvypddpafadkrer 156
Cdd:cd00016 81 rAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 157 apythylrrlgftgdnpwhdwanaaagadgeilsgwrmrhaglptrlpeahsetayttrrAMDFIDEQ-GERPWCLHLSY 235
Cdd:cd00016 108 ------------------------------------------------------------LLKAIDETsKEKPFVLFLHF 127
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 236 IKPHWPYIAPAPYHALYRADqvlpalraapgeesdhpvyrafrehreslnfsredvrrqviptymglIRQVDDQLGRLFQ 315
Cdd:cd00016 128 DGPDGPGHAYGPNTPEYYDA-----------------------------------------------VEEIDERIGKVLD 160
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 316 HMRASGRWDDTLIVFTSDHGD-FLGDHGLGEKEFLLESAVG---VPLLIRDPRpeadATRGRVEEALVQSIDVLPSILEA 391
Cdd:cd00016 161 ALKKAGDADDTVIIVTADHGGiDKGHGGDPKADGKADKSHTgmrVPFIAYGPG----VKKGGVKHELISQYDIAPTLADL 236
|
.
gi 15597529 392 F 392
Cdd:cd00016 237 L 237
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
401-490 |
7.46e-08 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 50.33 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 401 IEGRSLLPFVHGAPPADWRRyaiAEYDYAFQAPARErlgrpiDACRMYMVRSERWKYIAY--DGFRAQLFDLASDPGELR 478
Cdd:pfam16347 5 MQGKSFLPLLKGKKPKNWRD---ALYYHYYEYPAEH------AVKRHYGVRTERYKLIHFynDIDEWELYDLQKDPKEMN 75
|
90
....*....|..
gi 15597529 479 DLGADPAHAAVR 490
Cdd:pfam16347 76 NVYGDPEYAEVQ 87
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
7-343 |
1.83e-07 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 52.63 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 7 IRNVLYIMCDQLRRDYLSCYGHPYLHTPNIDRLAAEGVRFARAYTQGTICGPS--RMSSYTGRYvssHQVAWNavplplE 84
Cdd:cd16017 2 PKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLKKNLIVFDNVISCGTSTAVSlpCMLSFANRE---NYDRAY------Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 85 ELTLGDYLRAAGVRTALVGkthataNLEGMrRLGIDPASARGAALAEAGFEPYDRNDGVYpddpafadkrerapythylr 164
Cdd:cd16017 73 QENLIDLAKKAGYKTYWIS------NQGGC-GGYDTRISAIAKIETVFTNKGSCNSSNCY-------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 165 rlgftgdnpwhdwanaaagaDGEILsgwrmrhAGLPTRLPEAHSETAYTtrramdfideqgerpwcLHL--SyikpHWPY 242
Cdd:cd16017 126 --------------------DEALL-------PLLDEALADSSKKKLIV-----------------LHLmgS----HGPY 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 243 iapapyhalyradqvlpALRAAPGEESDHPVYrafreHRESLNFSREdvrrQVIPTYMGLIRQVDDQLGRLFQHMRASGR 322
Cdd:cd16017 158 -----------------YDRYPEEFAKFTPDC-----DNELQSCSKE----ELINAYDNSILYTDYVLSQIIERLKKKDK 211
|
330 340
....*....|....*....|.
gi 15597529 323 wdDTLIVFTSDHGDFLGDHGL 343
Cdd:cd16017 212 --DAALIYFSDHGESLGENGL 230
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
303-342 |
1.08e-06 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 50.28 E-value: 1.08e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 15597529 303 IRQVDDQLGRLFQHMRASGRWDDTLIVFTSDHG--DfLGDHG 342
Cdd:cd16018 185 LKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGmtD-VGTHG 225
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
2-335 |
1.90e-06 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 50.13 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 2 SQPKPIRNVLYIMCDQLRRDYLScyghpYLHTPNIDRLAAEGVRFARAYTQG-TICGPSRMSSYTGRYVSSHQVAWNAVP 80
Cdd:COG1524 18 AAAPPAKKVVLILVDGLRADLLE-----RAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGLYPGEHGIVGNGWY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 81 LPlEELTLGDYLRAAGVRTALVGKTHATANLEGMRRLGIDPASArgaalaeagFEPYdrndgvypddpafadkRERAPYT 160
Cdd:COG1524 93 DP-ELGRVVNSLSWVEDGFGSNSLLPVPTIFERARAAGLTTAAV---------FWPS----------------FEGSGLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 161 HYLRRLGFTGDNPWHDWANAAagadgeilsgwrmrhaglptrlpeahsetAYTTRRAMDFIDEqgERPwclHLSYIkpHW 240
Cdd:COG1524 147 DAARPYPYDGRKPLLGNPAAD-----------------------------RWIAAAALELLRE--GRP---DLLLV--YL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 241 PYIapapyhalyraDQVLpalraapgeesdhpvyrafreHRESLNFsredvrrqviPTYMGLIRQVDDQLGRLFQHMRAS 320
Cdd:COG1524 191 PDL-----------DYAG---------------------HRYGPDS----------PEYRAALREVDAALGRLLDALKAR 228
|
330
....*....|....*
gi 15597529 321 GRWDDTLIVFTSDHG 335
Cdd:COG1524 229 GLYEGTLVIVTADHG 243
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
10-74 |
4.83e-05 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 45.49 E-value: 4.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597529 10 VLYIMCDQLRRDYLScyghPYLHTPNIDRLAAEGVRFARAYTQG-TICGPSRMSSYTGRYVSSHQV 74
Cdd:pfam01663 1 LLVISLDGFRADYLD----RFELTPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGI 62
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
303-396 |
2.27e-03 |
|
Metalloenzyme superfamily; This family includes phosphopentomutase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This family is also related to pfam00245. The alignment contains the most conserved residues that are probably involved in metal binding and catalysis.
Pssm-ID: 396305 Cd Length: 410 Bit Score: 40.46 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597529 303 IRQVDDQLGRLFQHMRAsgrwDDTLIVFTSDHG---DFLGDHGLGEKefllesavgVPLLIRDPRPEADATRGRVEEALV 379
Cdd:pfam01676 326 IEAVDERLGELLDALEE----DDGLLIITADHGnpeEMKDTDHTREP---------VPILIYGKGVRPDQVLFGEKFRER 392
|
90
....*....|....*...
gi 15597529 380 QSI-DVLPSILEAFAVEP 396
Cdd:pfam01676 393 GGLaDIAATILMLLGLKK 410
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
306-335 |
9.90e-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: 37.88 E-value: 9.90e-03
10 20 30
....*....|....*....|....*....|
gi 15597529 306 VDDQLGRLFQHMRASGRWDDTLIVFTSDHG 335
Cdd:cd16021 185 ADEDLLEFLKRLKENGLLDNTFVIFMSDHG 214
|
|
| |
