|
Name |
Accession |
Description |
Interval |
E-value |
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
32-447 |
0e+00 |
|
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: 745.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNFKGLDPNYTT 111
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPNYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 112 WMDVMERHGYRTQKFGKLDYTSGHHSISNRVEAWTRDVAFLLRQEGRPMVNLIRNRTKVRVMERDWQNTDKAVNWLRKEA 191
Cdd:cd16171 81 WMDRLEKHGYHTQKYGKLDYTSGHHSVSNRVEAWTRDVPFLLRQEGRPTVNLVGDRSTVRVMLKDWQNTDKAVHWIRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 192 INYTEPFVIYLGLNLPHPYPSPSSGENFGSstfhtslywlekvshdaikipkwsplsemhpvdyyssytknctgrftkke 271
Cdd:cd16171 161 PNLTQPFALYLGLNLPHPYPSPSMGENFGS-------------------------------------------------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 272 IKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFYKMSMYEASAHVPLLMMGPGIKAGLQV 351
Cdd:cd16171 191 IRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMYEGSSHVPLLIMGPGIKAGQQV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 352 SNVVSLVDIYPTMLDIAGIPLPQNLSGYSLLPLSSETFKNEHKVKNLHPPWILSEFHGCNVNASTYMLRTNHWKYIAYSD 431
Cdd:cd16171 271 SDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLLSESSIKESPSRVPHPDWVLSEFHGCNVNASTYMLRTNSWKYIAYAD 350
|
410
....*....|....*.
gi 39930577 432 GASILPQLFDLSSDPD 447
Cdd:cd16171 351 GNSVPPQLFDLSKDPD 366
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-447 |
7.44e-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: 278.66 E-value: 7.44e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNFKGLDPNYTT 111
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDGDVPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 112 WMDVMERHGYRTQKFGKLDYTSGhhsisnrveawTRDVAFllrqegrpmvnlirnrtkvrvmERDWQNTDKAVNWLRKEA 191
Cdd:cd16037 81 WGHALRAAGYETVLIGKLHFRGE-----------DQRHGF----------------------RYDRDVTEAAVDWLREEA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 192 iNYTEPFVIYLGLNLPHPypspssgenfgsstfhtslywlekvshdaikipkwsPLseMHPVDYYSSYTKNCtgrftkke 271
Cdd:cd16037 128 -ADDKPWFLFVGFVAPHF------------------------------------PL--IAPQEFYDLYVRRA-------- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 272 ikniRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFYKMSMYEASAHVPLLMMGPGIKAGLQV 351
Cdd:cd16037 161 ----RAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMYEESVRVPMIISGPGIPAGKRV 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 352 SNVVSLVDIYPTMLDIAGIPLPQNLSGYSLLPLSSETFKNEHKVknlhppwiLSEFHGCNVNASTYMLRTNHWKYIAYSD 431
Cdd:cd16037 237 KTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEGPDDPDRVV--------FSEYHAHGSPSGAFMLRKGRWKYIYYVG 308
|
410
....*....|....*.
gi 39930577 432 GAsilPQLFDLSSDPD 447
Cdd:cd16037 309 YP---PQLFDLENDPE 321
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
21-471 |
2.12e-88 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 277.53 E-value: 2.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 21 AGEQRRRAAKAPNVVLVVSDsfD---GRLTFHpGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTE 97
Cdd:COG3119 13 AAAAAAAAAKRPNILFILAD--DlgyGDLGCY-GNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 98 SWNNFKG----LDPNYTTWMDVMERHGYRTQKFGKLdytsgHHSISNRVeawtrdvafllrqegrpmvnlirnrtkvrvm 173
Cdd:COG3119 90 VTDNGEGynggLPPDEPTLAELLKEAGYRTALFGKW-----HLYLTDLL------------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 174 erdwqnTDKAVNWLRKEAiNYTEPFVIYLGLNLPH-PYPSPSSgenfgsstfhtslyWLEKVSHDAIKIPKWSPLSEMhp 252
Cdd:COG3119 134 ------TDKAIDFLERQA-DKDKPFFLYLAFNAPHaPYQAPEE--------------YLDKYDGKDIPLPPNLAPRDL-- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 253 vdyyssytknctgrfTKKEIKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHR-QFYKMSMYE 331
Cdd:COG3119 191 ---------------TEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGlRGGKGTLYE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 332 ASAHVPLLMMGPG-IKAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLSGYSLLPLssetFKNEHKVknlHPPWILSEFHGc 410
Cdd:COG3119 256 GGIRVPLIVRWPGkIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPL----LTGEKAE---WRDYLYWEYPR- 327
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39930577 411 nvNASTYMLRTNHWKYIAYSDGASIlPQLFDLSSDPDELTNVAVKFPEITYSLDQKLHSII 471
Cdd:COG3119 328 --GGGNRAIRTGRWKLIRYYDDDGP-WELYDLKNDPGETNNLAADYPEVVAELRALLEAWL 385
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
30-453 |
5.01e-64 |
|
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: 215.13 E-value: 5.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 30 KAPNVVLVVSDsfDGR--LTFHpGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLF---THLTESWNNFKG 104
Cdd:cd16030 1 KKPNVLFIAVD--DLRpwLGCY-GGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRpdtTGVYDNNSYFRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 105 LDPNYTTWMDVMERHGYRTQKFGKLdYTSGHHSISNRVEAWTrDVAFLLRQEGRPMVNLIRNRTKVRVMER--------- 175
Cdd:cd16030 78 VAPDAVTLPQYFKENGYTTAGVGKI-FHPGIPDGDDDPASWD-EPPNPPGPEKYPPGKLCPGKKGGKGGGGgpaweaadv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 176 ------DWQNTDKAVNWLRKEAiNYTEPFVIYLGLNLPH-PYPSPSSgenfgsstfhtslYW----LEKVS----HDAIK 240
Cdd:cd16030 156 pdeaypDGKVADEAIEQLRKLK-DSDKPFFLAVGFYKPHlPFVAPKK-------------YFdlypLESIPlpnpFDPID 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 241 IPK--WSPLSEMHP-VDYYSSYTKNCTGRFTKKEIKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHG-E 316
Cdd:cd16030 222 LPEvaWNDLDDLPKyGDIPALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGwH 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 317 LAmEHRQFYKMSMYEASAHVPLLMMGPGIKAGLQVSN-VVSLVDIYPTMLDIAGIPLPQNLSGYSLLPLssetfknehkV 395
Cdd:cd16030 302 LG-EHGHWGKHTLFEEATRVPLIIRAPGVTKPGKVTDaLVELVDIYPTLAELAGLPAPPCLEGKSLVPL----------L 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930577 396 KNLHPPW---ILSEFHGCNVNAstYMLRTNHWKYIAYSDGASILPQ-LFDLSSDPDELTNVA 453
Cdd:cd16030 371 KNPSAKWkdaAFSQYPRPSIMG--YSIRTERYRYTEWVDFDKVGAEeLYDHKNDPNEWKNLA 430
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
32-380 |
2.22e-61 |
|
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: 201.90 E-value: 2.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDsfDGR---LTFHpGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNFK---GL 105
Cdd:cd16022 1 PNILLIMTD--DLGyddLGCY-GNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGnggGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 106 DPNYTTWMDVMERHGYRTQKFGKLdytsghHsisnrveawtrdvafllrqegrpmvnlirnrtkvrvmerdwqntDKAVN 185
Cdd:cd16022 78 PPDEPTLAELLKEAGYRTALIGKW------H--------------------------------------------DEAID 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 186 WLRKEAinYTEPFVIYLGLNLPHPypspssgenfgsstfhtslywlekvshdaikipkwsPLSemhpvdyyssytknctg 265
Cdd:cd16022 108 FIERRD--KDKPFFLYVSFNAPHP------------------------------------PFA----------------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 266 rftkkeiknirafYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHR-QFYKMSMYEASAHVPLLMMGPG 344
Cdd:cd16022 133 -------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGlRGKKGSLYEGGIRVPFIVRWPG 199
|
330 340 350
....*....|....*....|....*....|....*..
gi 39930577 345 IKAGLQVSN-VVSLVDIYPTMLDIAGIPLPQNLSGYS 380
Cdd:cd16022 200 KIPAGQVSDaLVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-451 |
4.63e-60 |
|
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: 203.57 E-value: 4.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFDGR-LTFHpGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNFKGLDPNYT 110
Cdd:cd16034 2 PNILFIFADQHRAQaLGCA-GDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVPLPPDAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 111 TWMDVMERHGYRTQKFGK--LDytsGHHSISNRVEA--WTRDvafllRQEG--------------RPMVNliRNRTKVRV 172
Cdd:cd16034 81 TIADVLKDAGYRTGYIGKwhLD---GPERNDGRADDytPPPE-----RRHGfdywkgyecnhdhnNPHYY--DDDGKRIY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 173 MER---DWQnTDKAVNWLRKEAINyTEPFVIYLGLNLPH-PY---PSPssgenfgsstfhtslyWLEKVSHDAIKIPKWS 245
Cdd:cd16034 151 IKGyspDAE-TDLAIEYLENQADK-DKPFALVLSWNPPHdPYttaPEE----------------YLDMYDPKKLLLRPNV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 246 PLSEMhpvdyyssytkncTGRFTKKEIKNirafYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFY 325
Cdd:cd16034 213 PEDKK-------------EEAGLREDLRG----YYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLMN 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 326 KMSMYEASAHVPLLMMGPG-IKAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLSGYSLlplsSETFKNEhKVKNLHPPWIL 404
Cdd:cd16034 276 KQVPYEESIRVPFIIRYPGkIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDL----SPLLLGG-KDDEPDSVLLQ 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 39930577 405 S--EFHGCNVNASTYM--LRTNHWKYIAYSDGAsilPQLFDLSSDPDELTN 451
Cdd:cd16034 351 CfvPFGGGSARDGGEWrgVRTDRYTYVRDKNGP---WLLFDNEKDPYQLNN 398
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
32-453 |
7.76e-60 |
|
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: 202.35 E-value: 7.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDsfD-GRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNFKG---LDP 107
Cdd:cd16027 1 PNILWIIAD--DlSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRgfpLPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 108 NYTTWMDVMERHGYRTQKFGKldytsGHHSISNRVEAWTRdvafllrqegrpmvnlirNRTKVRVMERDWQNTDKAVNWL 187
Cdd:cd16027 79 GVKTLPELLREAGYYTGLIGK-----THYNPDAVFPFDDE------------------MRGPDDGGRNAWDYASNAADFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 188 RKEAINytEPFVIYLGLNLPH-PYPSPSSGENfgsstfhtslywleKVSHDAIKIPKWSPLSEmhpvdyyssytknctgr 266
Cdd:cd16027 136 NRAKKG--QPFFLWFGFHDPHrPYPPGDGEEP--------------GYDPEKVKVPPYLPDTP----------------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 267 ftkkEIKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGeLAMehrQFYKMSMYEASAHVPLLMMGPG-I 345
Cdd:cd16027 183 ----EVREDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG-MPF---PRAKGTLYDSGLRVPLIVRWPGkI 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 346 KAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLSGYSLLPLssetFKNEhkvKNLHPPWILSEFHGCnvnASTY----MLRT 421
Cdd:cd16027 255 KPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPL----LKGE---KDPGRDYVFAERDRH---DETYdpirSVRT 324
|
410 420 430
....*....|....*....|....*....|..
gi 39930577 422 NHWKYIAYSDGasilPQLFDLSSDPDELTNVA 453
Cdd:cd16027 325 GRYKYIRNYMP----EELYDLKNDPDELNNLA 352
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-453 |
8.00e-59 |
|
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: 200.52 E-value: 8.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNFK-------G 104
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVEnagaysrG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 105 LDPNYTTWMDVMERHGYRTQKFGK---------LDYTSGHHsisNRVEAwTRDvAFLlrqegrpmvnlirnrtkvrvmer 175
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKwhvgpeetpLDYGFDEY---LPVET-TIE-YFL----------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 176 dwqnTDKAVNWLRKEAiNYTEPFVIYLGLNLPH-PY--PSPssgenfgsstfHTSLYwlekvshDAIKIPKW----SPLS 248
Cdd:cd16033 133 ----ADRAIEMLEELA-ADDKPFFLRVNFWGPHdPYipPEP-----------YLDMY-------DPEDIPLPesfaDDFE 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 249 EMHPVdyYSSYTKNCTGR-FTKKEIKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFYK- 326
Cdd:cd16033 190 DKPYI--YRRERKRWGVDtEDEEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKg 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 327 MSMYEASAHVPLLMMGPG-IKAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLSGYSLLPLssetFKNEHKvknlhPPW--- 402
Cdd:cd16033 268 PFMYEETYRIPLIIKWPGvIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPL----LRGEQP-----EDWrde 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 39930577 403 ILSEFHGCNVNASTYMLRTNHWKYIAysDGASIlPQLFDLSSDPDELTNVA 453
Cdd:cd16033 339 VVTEYNGHEFYLPQRMVRTDRYKYVF--NGFDI-DELYDLESDPYELNNLI 386
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-453 |
2.46e-58 |
|
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: 198.17 E-value: 2.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSD--SFDgrlTFHP-GSQVVKLPFINFMKTRGTSFLNAY----TNSPICCPSRAAMWSG--LFtHLTEswNNF 102
Cdd:cd16155 3 PNILFILADdqRAD---TIGAlGNPEIQTPNLDRLARRGTSFTNAYnmggWSGAVCVPSRAMLMTGrtLF-HAPE--GGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 103 KGLDPNYTTWMDVMERHGYRTQKFGKldytsghhsisnrveaWTRDVAfllrqegrpmvnlirnrtkvrvmerdwqntDK 182
Cdd:cd16155 77 AAIPSDDKTWPETFKKAGYRTFATGK----------------WHNGFA------------------------------DA 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 183 AVNWLRKEAINyTEPFVIYLGLNLPH-PYPSPSSgenfgsstfhtslyWLEKVSHDAIKIPKwSPLSEmHPVDYyssytK 261
Cdd:cd16155 111 AIEFLEEYKDG-DKPFFMYVAFTAPHdPRQAPPE--------------YLDMYPPETIPLPE-NFLPQ-HPFDN-----G 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 262 NCTGRF--------TKKEIKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGeLAM-EHRQFYKMSMYEA 332
Cdd:cd16155 169 EGTVRDeqlapfprTPEAVRQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHG-LAVgSHGLMGKQNLYEH 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 333 SAHVPLLMMGPGIKAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLSGYSLLPLSSETFKNEHKVknlhppwILSEFHGCnv 412
Cdd:cd16155 248 SMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVRDT-------LYGAYRDG-- 318
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 39930577 413 nasTYMLRTNHWKYIAYSDGASILpQLFDLSSDPDELTNVA 453
Cdd:cd16155 319 ---QRAIRDDRWKLIIYVPGVKRT-QLFDLKKDPDELNNLA 355
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
32-447 |
1.29e-56 |
|
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: 192.41 E-value: 1.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNN---FKGLDPn 108
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNaaeFPADIP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 109 ytTWMDVMERHGYRTQKFGKLDYTSG--HHSISnrveaWTRDVAFLLRQegrpmvnlirnrtKVRvmerdwqntDKAvnw 186
Cdd:cd16032 80 --TFAHYLRAAGYRTALSGKMHFVGPdqLHGFD-----YDEEVAFKAVQ-------------KLY---------DLA--- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 187 lRKEAinyTEPFVIYLGLNLPH-PYPSPSSgenfgsstfhtslYWlekvshdaikipkwsplsemhpvDYYssytknctg 265
Cdd:cd16032 128 -RGED---GRPFFLTVSFTHPHdPYVIPQE-------------YW-----------------------DLY--------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 266 rftkkeIKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFYKMSMYEASAHVPLLMMGPGI 345
Cdd:cd16032 159 ------VRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSFFEGSARVPLIISAPGR 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 346 KAGLQVSNVVSLVDIYPTMLDIAGIPLPQN---LSGYSLLPLSSETFKNEHKVknlhppwILSEFHGCNVNASTYMLRTN 422
Cdd:cd16032 233 FAPRRVAEPVSLVDLLPTLVDLAGGGTAPHvppLDGRSLLPLLEGGDSGGEDE-------VISEYLAEGAVAPCVMIRRG 305
|
410 420
....*....|....*....|....*
gi 39930577 423 HWKYIaYSDGASilPQLFDLSSDPD 447
Cdd:cd16032 306 RWKFI-YCPGDP--DQLFDLEADPL 327
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
30-453 |
3.75e-55 |
|
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.
Pssm-ID: 293755 [Multi-domain] Cd Length: 429 Bit Score: 191.20 E-value: 3.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 30 KAPNVVLVVSD--SFDGrLTFHpGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNFKGL-D 106
Cdd:cd16031 1 KRPNIIFILTDdhRYDA-LGCY-GNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLfD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 107 PNYTTWMDVMERHGYRTQKFGKLDYTSGHHSISNRVEAWtrdVAFLLRQEGRPMVNLIRNRTKVRVMERDWQNTDKAVNW 186
Cdd:cd16031 79 ASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYW---VSFPGQGSYYDPEFIENGKRVGQKGYVTDIITDKALDF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 187 LRKEAINytEPFVIYLGLNLPHpypspssgENFGSSTFHTSLYwlekvshDAIKIPKWSPLSEmhpvDYYSS-------Y 259
Cdd:cd16031 156 LKERDKD--KPFCLSLSFKAPH--------RPFTPAPRHRGLY-------EDVTIPEPETFDD----DDYAGrpewareQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 260 TKNCTGRFTKKEI------KNIRAfYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFYKMSMYEAS 333
Cdd:cd16031 215 RNRIRGVLDGRFDtpekyqRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLFDKRLMYEES 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 334 AHVPLLMMGPG-IKAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLSGYSLLPLssetFKNEHKvknlhPPW---ILSEFHG 409
Cdd:cd16031 294 IRVPLIIRDPRlIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPL----LEGEKP-----VDWrkeFYYEYYE 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 39930577 410 ---CNVNASTYMLRTNHWKYIAYSDGASILpQLFDLSSDPDELTNVA 453
Cdd:cd16031 365 epnFHNVPTHEGVRTERYKYIYYYGVWDEE-ELYDLKKDPLELNNLA 410
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-467 |
3.83e-52 |
|
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: 183.20 E-value: 3.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLteswNNFKGL------ 105
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHV----NGHRTLhhllrp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 106 -DPNYttwMDVMERHGYRTQKFGKLDYTSGHHSISNrVEAWtrdvafllrqegrpmvnlirnrtkvrvmerDWQNTDKAV 184
Cdd:cd16150 77 dEPNL---LKTLKDAGYHVAWAGKNDDLPGEFAAEA-YCDS------------------------------DEACVRTAI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 185 NWLRkeaiNYT--EPFVIYLGLNLPHPY---PSPssgenfgsstFHTSlywlekvsHDAIKIPKWSPLSEMHPvdYYSSY 259
Cdd:cd16150 123 DWLR----NRRpdKPFCLYLPLIFPHPPygvEEP----------WFSM--------IDREKLPPRRPPGLRAK--GKPSM 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 260 TKNC----TGRFTKKEIKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFYKM--SMYEAS 333
Cdd:cd16150 179 LEGIekqgLDRWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWpnTFEDCL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 334 AHVPLLMMGPGIKAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLSGYSLLP-------------------LSSET--FKNE 392
Cdd:cd16150 259 TRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLPvlageteehrdavfseggrLHGEEqaMEGG 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930577 393 HKVKNLHPPWILSEFHGCNVNASTyMLRTNHWKYIAYSDGAsilPQLFDLSSDPDELTNVA--VKFPEITYSLDQKL 467
Cdd:cd16150 339 HGPYDLKWPRLLQQEEPPEHTKAV-MIRTRRYKYVYRLYEP---DELYDLEADPLELHNLIgdPAYAEIIAEMKQRL 411
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
32-453 |
7.50e-52 |
|
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: 183.23 E-value: 7.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNFKGLDPNYTT 111
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGTPLDARHLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 112 WMDVMERHGYRTQKFGKLDYTS---GHHSisNRVEAWTRDVAfllrQEG-RPMVNLirNRTKVRVMERDWQnTDKAVNWL 187
Cdd:cd16028 81 LALELRKAGYDPALFGYTDTSPdprGLAP--LDPRLLSYELA----MPGfDPVDRL--DEYPAEDSDTAFL-TDRAIEYL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 188 RkeaINYTEPFVIYLGLNLPHP---YPSPssgenfgsstFHtSLYWLEKVShDAIKIPKWSPLSEMHPV----------- 253
Cdd:cd16028 152 D---ERQDEPWFLHLSYIRPHPpfvAPAP----------YH-ALYDPADVP-PPIRAESLAAEAAQHPLlaafleriesl 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 254 DYYSSYTKNCTgrFTKKEIKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFYKMSMYEAS 333
Cdd:cd16028 217 SFSPGAANAAD--LDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLWGKDGFFDQA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 334 AHVPLLMMGPGIKA----GLQVSNVVSLVDIYPTMLDIAGIPLPQNLSGYSLLP-LSSETFKNE----------HKVKNL 398
Cdd:cd16028 295 YRVPLIVRDPRREAdatrGQVVDAFTESVDVMPTILDWLGGEIPHQCDGRSLLPlLAGAQPSDWrdavhyeydfRDVSTR 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 39930577 399 HPPWILS-EFHGCNVNastyMLRTNHWKYIAYSDGAsilPQLFDLSSDPDELTNVA 453
Cdd:cd16028 375 RPQEALGlSPDECSLA----VIRDERWKYVHFAALP---PLLFDLKNDPGELRDLA 423
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
32-467 |
5.12e-50 |
|
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: 176.97 E-value: 5.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDsfD---GRLTFHpGSQVVKLPFINFMKTRGTSFLNAYTnSPICCPSRAAMWSGLFTHLTESWNNFKG---L 105
Cdd:cd16146 1 PNVILILTD--DqgyGDLGFH-GNPILKTPNLDRLAAESVRFTNFHV-SPVCAPTRAALLTGRYPFRTGVWHTILGrerM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 106 DPNYTTWMDVMERHGYRTQKFGK---------------LDYTSGHHS--ISNRVEAWTRDvafllrqegRPMVNLIRNRT 168
Cdd:cd16146 77 RLDETTLAEVFKDAGYRTGIFGKwhlgdnypyrpqdrgFDEVLGHGGggIGQYPDYWGND---------YFDDTYYHNGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 169 KVRV---MERDWqnTDKAVNWLRKeaiNYTEPFVIYLGLNLPH-PYPSPSSgenfgsstfhtslYWlekvshdaikipkw 244
Cdd:cd16146 148 FVKTegyCTDVF--FDEAIDFIEE---NKDKPFFAYLATNAPHgPLQVPDK-------------YL-------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 245 splsemhpvdyyssytknctGRFTKKEIKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQF 324
Cdd:cd16146 196 --------------------DPYKDMGLDDKLAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRF 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 325 ------YKMSMYEASAHVPLLMMGPG-IKAGLQVSNVVSLVDIYPTMLDIAGIPLPQN--LSGYSLLP-LSSETFKNEHK 394
Cdd:cd16146 256 nagmrgKKGSVYEGGHRVPFFIRWPGkILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGikLDGRSLLPlLKGESDPWPER 335
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930577 395 VKNLH---PPWILSEFHGCNVnastymlRTNHWKYIAYSDGAsilPQLFDLSSDPDELTNVAVKFPEITYSLDQKL 467
Cdd:cd16146 336 TLFTHsgrWPPPPKKKRNAAV-------RTGRWRLVSPKGFQ---PELYDIENDPGEENDVADEHPEVVKRLKAAY 401
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
28-453 |
1.17e-48 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 175.24 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 28 AAKAPNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLfthltESWNN-----F 102
Cdd:PRK13759 3 QTKKPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGL-----SQWHHgrvgyG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 103 KGLDPNYTTWM-DVMERHGYRTQKFGKLDYTS-----GHHSI--------SNRVEawtrdvafllRQEGRPMVNLIRNRT 168
Cdd:PRK13759 78 DVVPWNYKNTLpQEFRDAGYYTQCIGKMHVFPqrnllGFHNVllhdgylhSGRNE----------DKSQFDFVSDYLAWL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 169 KVRVMERDWQNTDKAVN-------------------WLRKEAINY------TEPFVIYLGLNLPH-PYPSPSsgenfgss 222
Cdd:PRK13759 148 REKAPGKDPDLTDIGWDcnswvarpwdleerlhptnWVGSESIEFlrrrdpTKPFFLKMSFARPHsPYDPPK-------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 223 tFHTSLYwlEKVSHDAIKIPKWSPLSEMHPvdyySSYTKNCT-GRFTKKEIKNIRAFYYAMCAETDAMLGEIILALHQLD 301
Cdd:PRK13759 220 -RYFDMY--KDADIPDPHIGDWEYAEDQDP----EGGSIDALrGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 302 LLQKTIVIYSSDHGELAMEHRQFYKMSMYEASAHVPLLMMGPG----IKAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLS 377
Cdd:PRK13759 293 LLDNTIILFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVD 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930577 378 GYSLLPLSSETfknehkvKNLHPPWILSEfHGCNVNASTYmLRTNHWKYIAYS-DGASilpQLFDLSSDPDELTNVA 453
Cdd:PRK13759 373 GRSLKNLIFGQ-------YEGWRPYLHGE-HALGYSSDNY-LTDGKWKYIWFSqTGEE---QLFDLKKDPHELHNLS 437
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-453 |
1.31e-46 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 167.02 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSF--D-----GR---LTfhpgsqvvklPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNN 101
Cdd:cd16152 2 PNVIVFFTDQQrwDtlgcyGQpldLT----------PNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 102 FKGLDPNYTTWMDVMERHGYRTQKFGKLdytsghHSISNRVEAWTrdvafllrqegrpmvnlirnrtkvrvmerdwqntD 181
Cdd:cd16152 72 GIPLPADEKTLAHYFRDAGYETGYVGKW------HLAGYRVDALT----------------------------------D 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 182 KAVNWLRKeaINYTEPFVIYLGLNLPH------PYPSP-SSGENFGSstfhtslYWlekVSHDAIKIPKwsplsemhpvD 254
Cdd:cd16152 112 FAIDYLDN--RQKDKPFFLFLSYLEPHhqndrdRYVAPeGSAERFAN-------FW---VPPDLAALPG----------D 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 255 YYSSYtknctgrftkkeiknirAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFYKMSMYEASA 334
Cdd:cd16152 170 WAEEL-----------------PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCHFRTRNAEYKRSCHESSI 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 335 HVPLLMMGPGIKAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLSGYSLLPL---SSETFKNEHKVKnlhppwiLSEFHgcn 411
Cdd:cd16152 233 RVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLvdgKVEDWRNEVFIQ-------ISESQ--- 302
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 39930577 412 VNAStymLRTNHWKYIAYSDGASILP----------QLFDLSSDPDELTNVA 453
Cdd:cd16152 303 VGRA---IRTDRWKYSVAAPDKDGWKdsgsdvyvedYLYDLEADPYELVNLI 351
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
32-453 |
1.34e-45 |
|
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: 164.65 E-value: 1.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFD---GRLTFHPgsQVVKLpfinfMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNF------ 102
Cdd:cd16147 2 PNIVLILTDDQDvelGSMDPMP--KTKKL-----LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSppgggy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 103 -----KGLDPNY-TTWMDvmeRHGYRTQKFGKL----DYTSGHHSIsnrVEAWTRDVAFLL--RQEGRPMVNLIRNRTKV 170
Cdd:cd16147 75 pkfwqNGLERSTlPVWLQ---EAGYRTAYAGKYlngyGVPGGVSYV---PPGWDEWDGLVGnsTYYNYTLSNGGNGKHGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 171 RvmERDWQNTD----KAVNWLRkEAINYTEPFVIYLGLNLPH-PY----------------PSPSSGENFGSSTFHtsly 229
Cdd:cd16147 149 S--YPGDYLTDvianKALDFLR-RAAADDKPFFLVVAPPAPHgPFtpapryanlfpnvtapPRPPPNNPDVSDKPH---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 230 WLekvshdaikipKWSPLSemhpvdyyssytknctgrfTKKEIKNIRAFYYAMCaET----DAMLGEIILALHQLDLLQK 305
Cdd:cd16147 222 WL-----------RRLPPL-------------------NPTQIAYIDELYRKRL-RTlqsvDDLVERLVNTLEATGQLDN 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 306 TIVIYSSDHGELAMEHRQFY-KMSMYEASAHVPLLMMGPGIKAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLSGYSllpl 384
Cdd:cd16147 271 TYIIYTSDNGYHLGQHRLPPgKRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGAPPPSDMDGRS---- 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39930577 385 ssetfknehkvknlhppwilsefhGCNVNASTYM-LRT----NHWKYIAYSDGASilpQLFDLSSDPDELTNVA 453
Cdd:cd16147 347 ------------------------CGDSNNNTYKcVRTvddtYNLLYFEWCTGFR---ELYDLTTDPYQLTNLA 393
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-383 |
8.98e-45 |
|
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: 158.87 E-value: 8.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSF--DgRLTFHpGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNFkgLDPNY 109
Cdd:cd16148 1 MNVILIVIDSLraD-HLGCY-GYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGP--LEPDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 110 TTWMDVMERHGYRTQKFGKLDYTSGHHSISNRVEAWTrdvaFLLRQEGRPmvnlirnrtKVRVMERDWQNTDKAVNWLRK 189
Cdd:cd16148 77 PTLAEILRKAGYYTAAVSSNPHLFGGPGFDRGFDTFE----DFRGQEGDP---------GEEGDERAERVTDRALEWLDR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 190 EAINytEPFVIYLGLNLPH-PYPspssgenfgsstfhtslywlekvshdaikipkwsplsemhpvdyyssytknctgrft 268
Cdd:cd16148 144 NADD--DPFFLFLHYFDPHePYL--------------------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 269 kkeiknirafYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFYK--MSMYEASAHVPLLMMGPGIK 346
Cdd:cd16148 165 ----------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGhgSNLYDEQLHVPLIIRWPGKE 234
|
330 340 350
....*....|....*....|....*....|....*..
gi 39930577 347 AGLQVSNVVSLVDIYPTMLDIAGIPLPQNLSGYSLLP 383
Cdd:cd16148 235 PGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
32-469 |
4.24e-44 |
|
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: 161.17 E-value: 4.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGL------FTH----------- 94
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQyparlgITDvipgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 95 --LTESWNNfKGLDPNYTTWMDVMERHGYRTQKFGK-------------------LDYTSGHHSISNRVEAWTRDVAFLL 153
Cdd:cd16144 81 tkLIPPPST-TRLPLEEVTIAEALKDAGYATAHFGKwhlggeggygpedqgfdvnIGGTGNGGPPSYYFPPGKPNPDLED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 154 RQEGRpmvnlirnrtkvRVMERdwqNTDKAVNWLRKeaiNYTEPFVIYLglnlphpypspssgenfgsstfhtslywlek 233
Cdd:cd16144 160 GPEGE------------YLTDR---LTDEAIDFIEQ---NKDKPFFLYL------------------------------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 234 vSHDAIKIPkWSPLSEMhpVDYYSSYTKNctgrfTKKEIKNirAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSD 313
Cdd:cd16144 191 -SHYAVHTP-IQARPEL--IEKYEKKKKG-----LRKGQKN--PVYAAMIESLDESVGRILDALEELGLADNTLVIFTSD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 314 HGELAMEHRQF--------YKMSMYEASAHVPLLMMGPGIKAGLQVSNV-VSLVDIYPTMLDIAGIPLP--QNLSGYSLL 382
Cdd:cd16144 260 NGGLSTRGGPPtsnaplrgGKGSLYEGGIRVPLIVRWPGVIKPGSVSDVpVIGTDLYPTFLELAGGPLPppQHLDGVSLV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 383 PLssetFKNEHKVKNLHP-----PWILSEFHGCnvnASTYmlRTNHWKYIA-YSDGAsilPQLFDLSSDPDELTNVAVKF 456
Cdd:cd16144 340 PL----LKGGEADLPRRAlfwhfPHYHGQGGRP---ASAI--RKGDWKLIEfYEDGR---VELYNLKNDIGETNNLAAEM 407
|
490
....*....|...
gi 39930577 457 PEITYSLDQKLHS 469
Cdd:cd16144 408 PEKAAELKKKLDA 420
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
32-457 |
1.56e-40 |
|
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: 151.59 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDsfD---GRLTFHpGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNFKG---- 104
Cdd:cd16145 1 PNIIFILAD--DlgyGDLGCY-GQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPggqd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 105 -LDPNYTTWMDVMERHGYRTQKFGKLDYTSGHHSIS-------------NRVEAWTRDVAFLLRQEGRpmvNLIRNRTKV 170
Cdd:cd16145 78 pLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHptkqgfdyfygylDQVHAHNYYPEYLWRNGEK---VPLPNNVIP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 171 RVMERDWQN-----------TDKAVNWLRKeaiNYTEPFVIYLGLNLPH-PYPSPSSGENFGSstfhtslywlekvshda 238
Cdd:cd16145 155 PLDEGNNAGggggtyshdlfTDEALDFIRE---NKDKPFFLYLAYTLPHaPLQVPDDGPYKYK----------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 239 ikiPKWSPLSEMHPVDyyssytknctgrftkkeikNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHG--- 315
Cdd:cd16145 215 ---PKDPGIYAYLPWP-------------------QPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGphs 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 316 ELAMEHR-QF---------YKMSMYEASAHVPLLMMGPG-IKAGlQVSNVVS-LVDIYPTMLDIAGIPLPQNLSGYSLLP 383
Cdd:cd16145 273 EGGSEHDpDFfdsngplrgYKRSLYEGGIRVPFIARWPGkIPAG-SVSDHPSaFWDFMPTLADLAGAEPPEDIDGISLLP 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930577 384 -LSSETFKNEHkvKNLHppWilsEFHGCNvnaSTYMLRTNHWKYIAYSDGASILpQLFDLSSDPDELTNVAVKFP 457
Cdd:cd16145 352 tLLGKPQQQQH--DYLY--W---EFYEGG---GAQAVRMGGWKAVRHGKKDGPF-ELYDLSTDPGETNNLAAQHP 415
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-384 |
5.70e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 138.88 E-value: 5.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNN-----FKGLD 106
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTlgspmQPLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 107 PNYTTWMDVMERHGYRTQKFGK--LdytSGHHSisnrvEAWTRDVAFllrqegrpmvnlirnrtkvrvmerdwqnTDKAV 184
Cdd:cd16035 81 PDVPTLGHMLRAAGYYTAYKGKwhL---SGAAG-----GGYKRDPGI----------------------------AAQAV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 185 NWLRKEAINYTE--PFviYLGLNLPHPypspssgenfgsstfhtslywlekvsHDAIKIPKwsplsemhpvdyyssytkn 262
Cdd:cd16035 125 EWLRERGAKNADgkPW--FLVVSLVNP--------------------------HDIMFPPD------------------- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 263 ctgrfTKKEIKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEH---RQFYkmSMYEASAHVPLL 339
Cdd:cd16035 158 -----DEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHglrGKGF--NAYEEALHVPLI 230
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 39930577 340 MMGPGIKAGLQVSN-VVSLVDIYPTMLDIAGIPLPQ------NLSGYSLLPL 384
Cdd:cd16035 231 ISHPDLFGTGQTTDaLTSHIDLLPTLLGLAGVDAEArateapPLPGRDLSPL 282
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
32-453 |
1.51e-33 |
|
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: 131.53 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDsfD---GRLTFHpGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMW-------SGLFTHLTESWNN 101
Cdd:cd16026 2 PNIVVILAD--DlgyGDLGCY-GSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLtgrypvrVGLPGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 102 fKGLDPNYTTWMDVMERHGYRTQKFGK--LDYTSGHHSI------------SNrveawtrD-VAFLLRQEGRPMVNLIRN 166
Cdd:cd16026 79 -GGLPPDEITIAEVLKKAGYRTALVGKwhLGHQPEFLPTrhgfdeyfgipySN-------DmWPFPLYRNDPPGPLPPLM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 167 RTKVRVMERDWQN------TDKAVNWLRKEAinyTEPFVIYLGLNLPH-PYPSPssgENF-GSSTfhTSLYwlekvsHDA 238
Cdd:cd16026 151 ENEEVIEQPADQSsltqryTDEAVDFIERNK---DQPFFLYLAHTMPHvPLFAS---EKFkGRSG--AGLY------GDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 239 IKipkwsplsemhpvdyyssytknctgrftkkeiknirafyyamcaETDAMLGEIILALHQLDLLQKTIVIYSSDHG-EL 317
Cdd:cd16026 217 VE--------------------------------------------ELDWSVGRILDALKELGLEENTLVIFTSDNGpWL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 318 AMEHRQFY-------KMSMYEASAHVPLLMMGPG-IKAGLQVSNVVSLVDIYPTMLDIAGIPLPQN--LSGYSLLPLsse 387
Cdd:cd16026 253 EYGGHGGSagplrggKGTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDrvIDGKDISPL--- 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930577 388 tFKNEHKVKnlHPPWILSeFHGCNVNAstymLRTNHWKYIAYSDGAS------------ILPQLFDLSSDPDELTNVA 453
Cdd:cd16026 330 -LLGGSKSP--PHPFFYY-YDGGDLQA----VRSGRWKLHLPTTYRTgtdpggldptklEPPLLYDLEEDPGETYNVA 399
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
32-453 |
3.72e-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: 130.40 E-value: 3.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDsfD---GRLT-FHPGSQVvKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTES----WNNFK 103
Cdd:cd16143 1 PNIVIILAD--DlgyGDIScYNPDSKI-PTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLkggvLGGFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 104 G--LDPNYTTWMDVMERHGYRTQKFGK----LDYTSGHhsISNRVEAWTRDVAFLlrqegRPMVN-----------LIRN 166
Cdd:cd16143 78 PplIEPDRVTLAKMLKQAGYRTAMVGKwhlgLDWKKKD--GKKAATGTGKDVDYS-----KPIKGgpldhgfdyyfGIPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 167 RTKVRVMerdwqnTDKAVNWLRKEAiNYTEPFVIYLGLNLPH-PY-PSPSsgenF-GSSTfhTSLYwlekvshdaikipk 243
Cdd:cd16143 151 SEVLPTL------TDKAVEFIDQHA-KKDKPFFLYFALPAPHtPIvPSPE----FqGKSG--AGPY-------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 244 wsplsemhpvdyyssytknctGRFTkkeiknirafyyamcAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAM---- 319
Cdd:cd16143 204 ---------------------GDFV---------------YELDWVVGRILDALKELGLAENTLVIFTSDNGPSPYadyk 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 320 EHRQF----------YKMSMYEASAHVPLLMMGPG-IKAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLS--GYSLLPLss 386
Cdd:cd16143 248 ELEKFghdpsgplrgMKADIYEGGHRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAedSFSFLPA-- 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39930577 387 etFKNEhKVKNLHPPWILSEFHGcnvnasTYMLRTNHWKYIAYSDGASILP------------QLFDLSSDPDELTNVA 453
Cdd:cd16143 326 --LLGP-KKQEVRESLVHHSGNG------SFAIRKGDWKLIDGTGSGGFSYprgkeklglppgQLYNLSTDPGESNNLY 395
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
32-370 |
5.15e-33 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 127.54 E-value: 5.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSF-DGRLTFHPGSQVVkLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESW-NNFKGLDPNY 109
Cdd:pfam00884 1 PNVVLVLGESLrAPDLGLYGYPRPT-TPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYvSTPVGLPRTE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 110 TTWMDVMERHGYRTQKFGKldYTSGHHSiSNRVEAWTRDVAFllrqEGRPMVNLIRNRTKVRVMERDW-----QNTDKAV 184
Cdd:pfam00884 80 PSLPDLLKRAGYNTGAIGK--WHLGWYN-NQSPCNLGFDKFF----GRNTGSDLYADPPDVPYNCSGGgvsdeALLDEAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 185 NWLRKEainyTEPFVIYLGLNLPHPypspssgenfgsstfhtslywlekvshdaikiPKWSPlsEMHPVDYYSSYTKNCT 264
Cdd:pfam00884 153 EFLDNN----DKPFFLVLHTLGSHG--------------------------------PPYYP--DRYPEKYATFKPSSCS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 265 GRftkkeikNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAME----HRQFYKMSMYEASAHVPLLM 340
Cdd:pfam00884 195 EE-------QLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEgggyLHGGKYDNAPEGGYRVPLLI 267
|
330 340 350
....*....|....*....|....*....|.
gi 39930577 341 MGPG-IKAGLQVSNVVSLVDIYPTMLDIAGI 370
Cdd:pfam00884 268 WSPGgKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-451 |
8.16e-33 |
|
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: 128.87 E-value: 8.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFdGRLTF-HPGSQVVKLPFINFMKTRGTSFLNAYTNsPICCPSRAAMWSGLFTHLTesWNNFKGLDPNYT 110
Cdd:cd16151 1 PNIILIMADDL-GYECIgCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRN--YVVFGYLDPKQK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 111 TWMDVMERHGYRTQKFGKLDYTSGhhsisNRVEAWTRDVAF---LLRQ-------EGRPMVNLIRNRT-KVRVMERDW-- 177
Cdd:cd16151 77 TFGHLLKDAGYATAIAGKWQLGGG-----RGDGDYPHEFGFdeyCLWQltetgekYSRPATPTFNIRNgKLLETTEGDyg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 178 --QNTDKAVNWLRKeaiNYTEPFVIYLGLNLPH-PY-PSPSSgenfgsstfhtslywlekvshdaikiPKWSPLSemhpv 253
Cdd:cd16151 152 pdLFADFLIDFIER---NKDQPFFAYYPMVLVHdPFvPTPDS--------------------------PDWDPDD----- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 254 dyyssytknctgrftkKEIKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGElameHRQF--------- 324
Cdd:cd16151 198 ----------------KRKKDDPEYFPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGT----HRPItsrtngrev 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 325 --YKMSMYEASAHVPLLMMGPG-IKAGLQVSNVVSLVDIYPTMLDIAGIPLPQN--LSGYSLLP-LSSETfknehkvKNL 398
Cdd:cd16151 258 rgGKGKTTDAGTHVPLIVNWPGlIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPqLLGKT-------GSP 330
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 39930577 399 HPPWILseFHGCNVNAST--YMLRTNHWKYiaYSDGasilpQLFDLSSDPDELTN 451
Cdd:cd16151 331 RREWIY--WYYRNPHKKFgsRFVRTKRYKL--YADG-----RFFDLREDPLEKNP 376
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
32-451 |
1.81e-29 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293775 [Multi-domain] Cd Length: 468 Bit Score: 120.95 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNFKGLDPNYTT 111
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 112 WMDVMERHGYRTQKFGK--LDytsGHHSISNRV--EAWTRDVAFllrqegrPMVNLI-----RNRTKVR----VMERD-- 176
Cdd:cd16156 81 IGQRLSDNGIHTAYIGKwhLD---GGDYFGNGIcpQGWDPDYWY-------DMRNYLdelteEERRKSRrgltSLEAEgi 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 177 -------WQNTDKAVNWLRKEAinyTEPFVIYLGLNLPH-PYPSPSSgenfgsstfHTSLYwlekvshDAIKIPK----W 244
Cdd:cd16156 151 keeftygHRCTNRALDFIEKHK---DEDFFLVVSYDEPHhPFLCPKP---------YASMY-------KDFEFPKgenaY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 245 SPLSEMHPVDYYSSYTKnctgRFTKKEIKNIRAFYYAMCAE-TDAMLGEIILALHQLdlLQKTIVIYSSDHGELAMEHRQ 323
Cdd:cd16156 212 DDLENKPLHQRLWAGAK----PHEDGDKGTIKHPLYFGCNSfVDYEIGRVLDAADEI--AEDAWVIYTSDHGDMLGAHKL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 324 FYK-MSMYEASAHVPLLMMGPG-IKAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLSGYSLLPLSSETFKNEHKvknlhpp 401
Cdd:cd16156 286 WAKgPAVYDEITNIPLIIRGKGgEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIEDPEIPENR------- 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 402 WILSEFHGCNVNASTY----MLR---TNHWKYIAY---SDgasilpQLFDLSSDPDELTN 451
Cdd:cd16156 359 GVFVEFGRYEVDHDGFggfqPVRcvvDGRYKLVINllsTD------ELYDLEKDPYEMHN 412
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-381 |
8.48e-27 |
|
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: 109.77 E-value: 8.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSD--------SFDGRLTFHPGSQV--VKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNN 101
Cdd:cd16153 2 PNILWIITDdqrvdslsCYNNAHTGKSESRLgyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 102 FK---GLDPNYTTWMDVMERHGYRTQKFGKLDYtsghhsisnrveawtrdvafllrqegRPMVNLIRNRtkvrvmerdwQ 178
Cdd:cd16153 82 EAahpALDHGLPTFPEVLKKAGYQTASFGKSHL--------------------------EAFQRYLKNA----------N 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 179 NTDKAVNWLRKEAINYTEPFVIYLGLNLPHPYPSPSsgENFGSstfhtslywlekvshdaikipkwsplsemhpvdyyss 258
Cdd:cd16153 126 QSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPP--KEFRD------------------------------------- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 259 ytknctgRFTkkeiknirafYYAMCAETDAMLGEIILALHQLDLLQK---TIVIYSSDHGELAMEHRQFYKMSMYEASAH 335
Cdd:cd16153 167 -------RFD----------YYAFCAYGDAQVGRAVEAFKAYSLKQDrdyTIVYVTGDHGWHLGEQGILAKFTFWPQSHR 229
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 39930577 336 VPLLMMGPGIK---AGLQVSNVVSLVDIYPTMLDIAGIPL--PQNLSGYSL 381
Cdd:cd16153 230 VPLIVVSSDKLkapAGKVRHDFVEFVDLAPTLLAAAGVDVdaPDYLDGRDL 280
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
30-452 |
1.31e-26 |
|
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: 111.77 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 30 KAPNVVLVVSD--------SFDGRltfhpgsqvVKLPFINFMKTRGTSFLNAYTnSPICCPSRAAMWSGLFTH------L 95
Cdd:cd16025 1 GRPNILLILADdlgfsdlgCFGGE---------IPTPNLDALAAEGLRFTNFHT-TALCSPTRAALLTGRNHHqvgmgtM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 96 TESWNNFkgldPNYTTWM--------DVMERHGYRTQKFGKLDYTS-GHHSisnrveawTRDVafllrqegrpmvnlirn 166
Cdd:cd16025 71 AELATGK----PGYEGYLpdsaatiaEVLKDAGYHTYMSGKWHLGPdDYYS--------TDDL----------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 167 rtkvrvmerdwqnTDKAVNWLRkEAINYTEPFVIYLGLNLPH-PYPSPSSgenfgsstfhtslyWLEK------VSHDAI 239
Cdd:cd16025 122 -------------TDKAIEYID-EQKAPDKPFFLYLAFGAPHaPLQAPKE--------------WIDKykgkydAGWDAL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 240 K------------IPKWSPLSEMHP-VDYYSSYTKNCTGRFTKK-EIknirafYYAMCAETDAMLGEIILALHQLDLLQK 305
Cdd:cd16025 174 ReerlerqkelglIPADTKLTPRPPgVPAWDSLSPEEKKLEARRmEV------YAAMVEHMDQQIGRLIDYLKELGELDN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 306 TIVIYSSDHG--------ELAMEHRQFYKMSMYEASAHVPLLMMGP-GIKAGLQVSN-VVSLVDIYPTMLDIAGIPLPQN 375
Cdd:cd16025 248 TLIIFLSDNGasaepgwaNASNTPFRLYKQASHEGGIRTPLIVSWPkGIKAKGGIRHqFAHVIDIAPTILELAGVEYPKT 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 376 --------LSGYSLLPlsseTFKNehkvKNLHPP--WILSEFHGcnvNAStymLRTNHWKYIAYSDGASILP--QLFDLS 443
Cdd:cd16025 328 vngvpqlpLDGVSLLP----TLDG----AAAPSRrrTQYFELFG---NRA---IRKGGWKAVALHPPPGWGDqwELYDLA 393
|
....*....
gi 39930577 444 SDPDELTNV 452
Cdd:cd16025 394 KDPSETHDL 402
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-383 |
9.01e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 97.69 E-value: 9.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDsfD-GRLTFH-PGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGL--FTH----LTESWNNFK 103
Cdd:cd16149 1 PNILFILTD--DqGPWALGcYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRmpSQHgihdWIVEGSHGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 104 -----GLDPNYTTWMDVMERHGYRTQKFGKldytsghhsisnrveawtrdvafllrqegrpmvnlirnrtkvrvmerdWQ 178
Cdd:cd16149 79 tkkpeGYLEGQTTLPEVLQDAGYRCGLSGK------------------------------------------------WH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 179 NTDKAVNWLRKEAiNYTEPFviYLGLNlphpYPSPssgenfgsstfhtslywlekvsHDaikipkwsplsemhPVDYYSS 258
Cdd:cd16149 111 LGDDAADFLRRRA-EAEKPF--FLSVN----YTAP----------------------HS--------------PWGYFAA 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 259 YTknctgrftkkeiknirafyyAMcaetDAMLGEIILALHQLDLLQKTIVIYSSDHGeLAMEHRQFY-------KMSMYE 331
Cdd:cd16149 148 VT--------------------GV----DRNVGRLLDELEELGLTENTLVIFTSDNG-FNMGHHGIWgkgngtfPLNMYD 202
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 39930577 332 ASAHVPLLMMGPG-IKAGLQVSNVVSLVDIYPTMLDIAGIPLP--QNLSGYSLLP 383
Cdd:cd16149 203 NSVKVPFIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPadPRLPGRSFAD 257
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
32-453 |
8.24e-19 |
|
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: 88.38 E-value: 8.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFD-GRLTFHpGSQVVKLPFINFMKTRGTSFLNAYTNsPICCPSRAAMWSGLFTHLTE------SWNNFKG 104
Cdd:cd16029 1 PHIVFILADDLGwNDVGFH-GSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGmqhgviLAGEPYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 105 LDPNYTTWMDVMERHGYRTQKFGKLDytSGHHSIS----NR------------VEAWTRDVAfllrqeGRPMVNLIRNRT 168
Cdd:cd16029 79 LPLNETLLPQYLKELGYATHLVGKWH--LGFYTWEytptNRgfdsfygyyggaEDYYTHTSG------GANDYGNDDLRD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 169 KVRVMERDWQN------TDKAVNWLRKEaiNYTEPFVIYLGLNLPHpypspssgenfgsstfhtslywlekvshdaikip 242
Cdd:cd16029 151 NEEPAWDYNGTystdlfTDRAVDIIENH--DPSKPLFLYLAFQAVH---------------------------------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 243 kwSPLSEmhPVDYYSSYTKNCTGrftkkeIKNI-RAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGelAMEH 321
Cdd:cd16029 195 --APLQV--PPEYADPYEDKFAH------IKDEdRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG--GPTG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 322 RQFY---------KMSMYEASAHVPLLMMGPGIKAG-LQVSN-VVSLVDIYPTMLDIAG--IPLPQNLSGYSLLP--LSS 386
Cdd:cd16029 263 GGDGgsnyplrggKNTLWEGGVRVPAFVWSPLLPPKrGTVSDgLMHVTDWLPTLLSLAGgdPDDLPPLDGVDQWDalSGG 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930577 387 ETFKNEHKVKNLHPPWILsefhgcNVNAStymLRTNHWKYIAysdGAsilpQLFDLSSDPDELTNVA 453
Cdd:cd16029 343 APSPRTEILLNIDDITRT------TGGAA---IRVGDWKLIV---GK----PLFNIENDPCERNDLA 393
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
32-459 |
9.04e-19 |
|
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.
Pssm-ID: 293778 [Multi-domain] Cd Length: 521 Bit Score: 89.27 E-value: 9.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSD--------SFdgrltfhpGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLT--ESWNN 101
Cdd:cd16159 2 PNIVLFMADdlgigdvgCF--------GNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSgmASSHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 102 FK---------GLDPNYTTWMDVMERHGYRTQKFGK----------LDYTsgHHSISNRVEAWTrdvafllrqeGRPMVN 162
Cdd:cd16159 74 MRvilftassgGLPPNETTFAEVLKQQGYSTALIGKwhlglhcesrNDFC--HHPLNHGFDYFY----------GLPLTN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 163 L-----IRNRTKVRVMERDWQ----------------NTDKAVNWLRKEAINYTEPFVIYLGLNLPHPYP---------- 211
Cdd:cd16159 142 LkdcgdGSNGEYDLSFDPLFPlltafvlitaltifllLYLGAVSKRFFVFLLILSLLFISLFFLLLITNRyfncilmrnh 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 212 ----SPSSGENFGSSTFHTSLYWLEKVSHDaikipkwsplsemhPVDYYSSYTKNCTGRFTKKEI--KNIRAFYYAMCAE 285
Cdd:cd16159 222 evveQPMSLENLTQRLTKEAISFLERNKER--------------PFLLVMSFLHVHTALFTSKKFkgRSKHGRYGDNVEE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 286 TDAMLGEIILALHQLDLLQKTIVIYSSDHG---ELAMEHRQ-------FY---KMSMYEASAHVPLLMMGPG-IKAGLQV 351
Cdd:cd16159 288 MDWSVGQILDALDELGLKDNTFVYFTSDNGghlEEISVGGEygggnggIYggkKMGGWEGGIRVPTIVRWPGvIPPGSVI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 352 SNVVSLVDIYPTMLDIAGIPLPQN--LSGYSLLPLSSETFKN-EHKVKnlhppwilseFHGCN--VNASTYMLRTNH--W 424
Cdd:cd16159 368 DEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLLTGQEKRsPHEFL----------FHYCGaeLHAVRYRPRDGGavW 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 425 K-------YIAYSDGASIL---------------PQLFDLSSDPDELTNVAVK---FPEI 459
Cdd:cd16159 438 KahyftpnFYPGTEGCCGTllcrcfgdsvthhdpPLLFDLSADPSESNPLDPTdepYQEI 497
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
32-494 |
1.23e-17 |
|
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: 85.57 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSF---DGRLTFHPGSQVvklPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESW------NNF 102
Cdd:cd16158 2 PNIVLLFADDLgygDLGCYGHPSSST---PNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYpgvfypGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 103 KGLDPNYTTWMDVMERHGYRTQKFGK-----------LDYTSGHHSI------------SNRVEAWTRDVAFLLRQEGRP 159
Cdd:cd16158 79 GGLPLNETTIAEVLKTVGYQTAMVGKwhlgvglngtyLPTHQGFDHYlgipyshdqgpcQNLTCFPPNIPCFGGCDQGEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 160 MVNLIRNrTKVRVMERDWQNTDKAVNWLRKEAI--NYTE--PFVIYlglnlphpYPSpssgenfgsstFHTslywlekvs 235
Cdd:cd16158 159 PCPLFYN-ESIVQQPVDLLTLEERYAKFAKDFIadNAKEgkPFFLY--------YAS-----------HHT--------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 236 HdaikipkwsplsemHPvdyyssytknctgRFTKKEIKN--IRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSD 313
Cdd:cd16158 210 H--------------YP-------------QFAGQKFAGrsSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 314 HG-ELAMEHR-------QFYKMSMYEASAHVPLLMMGPG-IKAGLqVSNVVSLVDIYPTMLDIAGIPLPQ-NLSGYSLLP 383
Cdd:cd16158 263 NGpSTMRKSRggnagllKCGKGTTYEGGVREPAIAYWPGrIKPGV-THELASTLDILPTIAKLAGAPLPNvTLDGVDMSP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 384 LSSETFKNEHKVKNLHPPWIlsefhgcNVNASTYMLRTNHWKYIAYSDGASIL-------------------PQLFDLSS 444
Cdd:cd16158 342 ILFEQGKSPRQTFFYYPTSP-------DPDKGVFAVRWGKYKAHFYTQGAAHSgttpdkdchpsaeltshdpPLLFDLSQ 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 39930577 445 DPDELTNvavkfpeitysldqkLHSIINYPKVSASVHQYnKEQF---IKWKQS 494
Cdd:cd16158 415 DPSENYN---------------LLGLPEYNQVLKQIQQV-KERFeasMKFGES 451
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
31-448 |
1.62e-16 |
|
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: 81.36 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 31 APNVVLVVSDSF---DGRLTFHPGSQVVklPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNF----- 102
Cdd:cd16161 1 KPNFLLLFADDLgwgDLGANWAPNAILT--PNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFlptsv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 103 KGLDPNYTTWMDVMERHGYRTQKFGK--LDYTSGHHSISNRVEAWTrdvafllrqeGRPMVNlirnrtKVRVMERdwqNT 180
Cdd:cd16161 79 GGLPLNETTLAEVLRQAGYATGMIGKwhLGQREAYLPNSRGFDYYF----------GIPFSH------DSSLADR---YA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 181 DKAVNWLRKeAINYTEPFVIYLGLN---LPHPYPSPssgenFGSSTFHTSLYwlekvsHDAikipkwspLSEMhpvdyys 257
Cdd:cd16161 140 QFATDFIQR-ASAKDRPFFLYAALAhvhVPLANLPR-----FQSPTSGRGPY------GDA--------LQEM------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 258 sytknctgrftkkeiknirafyyamcaetDAMLGEIILALHQLDLLQKTIVIYSSDHG-------------ELAMEHRQF 324
Cdd:cd16161 193 -----------------------------DDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcelavgpgTGDWQGNLG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 325 ---YKMSMYEASAHVPLLMMGPG-IKAGLQVSNVVSLVDIYPTMLDIAGIPLPQN--LSGYSLLPLSSETFKNEHKVKnL 398
Cdd:cd16161 244 gsvAKASTWEGGHREPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVLFGGSKTGHRCL-F 322
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930577 399 HPPwilsefHGCNVNASTYMLRTNHWK--YIAYSDGASIL----------PQLFDLSSDPDE 448
Cdd:cd16161 323 HPN------SGAAGAGALSAVRCGDYKahYATGGALACCGstgpklyhdpPLLFDLEVDPAE 378
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
279-453 |
3.84e-15 |
|
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: 77.19 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 279 YYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHG-ELAMEHRQFY------KMSMYEASAHVPLLMMGPG-IKAGlQ 350
Cdd:cd16142 182 YADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGpEQDVWPDGGYtpfrgeKGTTWEGGVRVPAIVRWPGkIKPG-R 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 351 VSN-VVSLVDIYPTMLDIAGIPLPQN--------LSGYSLLP-LSSETFKNEHKVknlhppWILseFHGCNVNAstymLR 420
Cdd:cd16142 261 VSNeIVSHLDWFPTLAALAGAPDPKDkllgkdrhIDGVDQSPfLLGKSEKSRRSE------FFY--FGEGELGA----VR 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 39930577 421 TNHWKY---IAYSDGASIL--------PQLFDLSSDPDELTNVA 453
Cdd:cd16142 329 WKNWKVhfkAQEDTGGPTGepfyvltfPLIFNLRRDPKERYDVT 372
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
32-369 |
4.65e-15 |
|
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: 75.80 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRA--AMWSGLFTHLTESWNNFKGLDPNY 109
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLNPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 110 TTWMDVMERHGYRTQkfgkldYTSGHHSisnrvEAWTRDVAF-------LLRQEGRPMVNLIRNRTKVRvmerDWQNTDK 182
Cdd:cd16015 81 PSLPSILKEQGYETI------FIHGGDA-----SFYNRDSVYpnlgfdeFYDLEDFPDDEKETNGWGVS----DESLFDQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 183 AVNWLRKEAinyTEPFVIYLgLNL-PH-PYPSPSSGENfgsstfhtslywlekvshdaikipkwsplsEMHPVDYYSSYT 260
Cdd:cd16015 146 ALEELEELK---KKPFFIFL-VTMsNHgPYDLPEEKKD------------------------------EPLKVEEDKTEL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 261 KNctgrftkkeiknirafYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHrQFYKMSMYEASAHVPLLM 340
Cdd:cd16015 192 EN----------------YLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSD-YDETDEDPLDLYRTPLLI 254
|
330 340
....*....|....*....|....*....
gi 39930577 341 MGPGIKAGLQVSNVVSLVDIYPTMLDIAG 369
Cdd:cd16015 255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-448 |
6.37e-15 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 76.23 E-value: 6.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSF--DGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNsPICCPSRAAMWSGLF-THLTESWNNFKGLDPN 108
Cdd:cd16154 1 PNILLIIADDQglDSSAQYSLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYgFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 109 YTTWMDVMER---HGYRTQKFGKL-----DYTSGHHSISNRVEA-----------WTrdvaflLRQEGRPMVNLIRNRTK 169
Cdd:cd16154 80 ETLLQLLIKDattAGYSSAVIGKWhlggnDNSPNNPGGIPYYAGilgggvqdyynWN------LTNNGQTTNSTEYATTK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 170 VrvmerdwqnTDKAVNWLRKEainyTEPFVIYLGLNLPHpypSPssgenfgsstFHTslywlekvshdaikipkwsPLSE 249
Cdd:cd16154 154 L---------TNLAIDWIDQQ----TKPWFLWLAYNAPH---TP----------FHL-------------------PPAE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 250 MHpvDYYSSYTKNCTGrftkkeiKNIRAFYYAMCAETDAMLGEIILALHQlDLLQKTIVIYSSDHGELAMEHRQFY---- 325
Cdd:cd16154 189 LH--SRSLLGDSADIE-------ANPRPYYLAAIEAMDTEIGRLLASIDE-EERENTIIIFIGDNGTPGQVVDLPYtrnh 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 326 -KMSMYEASAHVPLLMMGPGI-KAGLQVSNVVSLVDIYPTMLDIAGIPLPQ---NLSGYSLLPLSSETFKNEHKVKNLHP 400
Cdd:cd16154 259 aKGSLYEGGINVPLIVSGAGVeRANERESALVNATDLYATIAELAGVDAAEihdSVSFKPLLSDVNASTRQYNYTEYESP 338
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 39930577 401 PWIlsefhgcnvnasTYMLRTNHWKYIAYSDGASilpQLFDLSSDPDE 448
Cdd:cd16154 339 TTT------------GWATRNQYYKLIESENGQE---ELYDLINDPSE 371
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
32-368 |
5.05e-14 |
|
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: 71.68 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFlNAYTNSPIC--CPSRAAMWSGL----------FTHLTESW 99
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATF-NFRSVSPPTssAPNHAALLTGAyptlhgytgnGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 100 NNFKGLDPNYTTWMDVMERHGYRTQKFGkldytsghhsisnrveawtrdvafllrqegrpmvnlirnrtkvrvmerdwqn 179
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG---------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 180 TDKAVNWLRKEainytEPFVIYLGLNLPHpypspssgenfgsstfhtslywlekvshdaikipkwsplsemHPVDYYSSY 259
Cdd:cd00016 108 LLKAIDETSKE-----KPFVLFLHFDGPD------------------------------------------GPGHAYGPN 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 260 TKNctgrftkkeiknirafYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFYKMSMYEASAH---- 335
Cdd:cd00016 141 TPE----------------YYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADGKADKSHtgmr 204
|
330 340 350
....*....|....*....|....*....|...
gi 39930577 336 VPLLMMGPGIKAGLQVSNVVSLVDIYPTMLDIA 368
Cdd:cd00016 205 VPFIAYGPGVKKGGVKHELISQYDIAPTLADLL 237
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
32-395 |
7.37e-14 |
|
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: 73.62 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSFD-------GRLTFHPGsqvvklpFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESW----- 99
Cdd:cd16160 2 PNIVLFFADDMGygdlasyGHPTQERG-------PIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYggtrv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 100 ---NNFKGLDPNYTTWMDVMERHGYRTQKFGK-------LDYTSGHHSISNR----------------VEAWTRDVAFll 153
Cdd:cd16160 75 flpWDIGGLPKTEVTMAEALKEAGYTTGMVGKwhlgineNNHSDGAHLPSHHgfdfvgtnlpftnswaCDDTGRHVDF-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 154 rqegrPMVNLIRNRTKVRVMERDWQN---TDKAVN-WLRKEAINYTEPFVIYLglNLPHPypspssgenfgsstfHTSLY 229
Cdd:cd16160 153 -----PDRSACFLYYNDTIVEQPIQHehlTETLVGdAKSFIEDNQENPFFLYF--SFPQT---------------HTPLF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 230 wlekvshdaikipkwsplsemhpvdyyssytknCTGRFTKKeikNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVI 309
Cdd:cd16160 211 ---------------------------------ASKRFKGK---SKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVF 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 310 YSSDHGElameHRQF------------YKMSMYEASAHVPLLMMGPGIKAGLQVSNVVSLVDIYPTMLDIAGIPLPQ--N 375
Cdd:cd16160 255 FLSDHGP----HVEYcleggstgglkgGKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTdrI 330
|
410 420
....*....|....*....|
gi 39930577 376 LSGYSLLPLSSETFKNEHKV 395
Cdd:cd16160 331 YDGLSITDLLLGEADSPHDD 350
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
28-382 |
1.49e-13 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 73.15 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 28 AAKAPNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFThLTESWNNFKGLDP 107
Cdd:COG1368 231 PAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPP-LPGGSPYKRPGQN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 108 NYTTWMDVMERHGYRTQkfgkldYTSGHHSISnrveaWTRDVAFllRQEGrpmVNLIRNRTKVRVMERD-WQNTDKAV-N 185
Cdd:COG1368 310 NFPSLPSILKKQGYETS------FFHGGDGSF-----WNRDSFY--KNLG---FDEFYDREDFDDPFDGgWGVSDEDLfD 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 186 WLRKEAINYTEPFVIYLglnlphpypspssgenfgsstFHTSlywlekvSHDAIKIPKwsplsEMHPVDYYSSYTKNctg 265
Cdd:COG1368 374 KALEELEKLKKPFFAFL---------------------ITLS-------NHGPYTLPE-----EDKKIPDYGKTTLN--- 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 266 rftkkeiKNIRAFYYamcaeTDAMLGEIILALHQLDLLQKTIVIYSSDHGE-LAMEHRQFYKMSMYeasaHVPLLMMGPG 344
Cdd:COG1368 418 -------NYLNAVRY-----ADQALGEFIEKLKKSGWYDNTIFVIYGDHGPrSPGKTDYENPLERY----RVPLLIYSPG 481
|
330 340 350
....*....|....*....|....*....|....*....
gi 39930577 345 IKAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLS-GYSLL 382
Cdd:COG1368 482 LKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAfGRDLL 520
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
24-365 |
1.85e-13 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 73.02 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 24 QRRRAAKAPNVVLVVSDS--FDgrlTFHPGsqvvKLPFINFMKTRGTSFLNAYTNSpiccpSRAAMwsGLFthlteswNN 101
Cdd:COG3083 237 QFSDPAKPPNILLIVVDSlrAD---MLDPE----VMPNLYAFAQRSLRFTNHYSSG-----NSTRA--GLF-------GL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 102 FKGLDPNYTT----------WMDVMERHGYRTQKFGkldyTSGHHSIsnrveawtrdvafLLRQEGRPMVNLIRNRTKVR 171
Cdd:COG3083 296 FYGLPGNYWDsilaertppvLIDALQQQGYQFGLFS----SAGFNSP-------------LFRQTIFSDVSLPRLHTPGG 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 172 VMERDWQNTDKAVNWLrkEAINYTEPFVIYLGLNLPHPYPSPSSGENFGSStfhtslywlekvshdAIKIPKWSPLSEMH 251
Cdd:COG3083 359 PAQRDRQITAQWLQWL--DQRDSDRPWFSYLFLDAPHAYSFPADYPKPFQP---------------SEDCNYLALDNESD 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 252 PVDYYSSYtKNCtgrftkkeiknirafyyamCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFY-----K 326
Cdd:COG3083 422 PTPFKNRY-RNA-------------------VHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQNYwghnsN 481
|
330 340 350
....*....|....*....|....*....|....*....
gi 39930577 327 MSMYEasAHVPLLMMGPGIKAGlQVSNVVSLVDIYPTML 365
Cdd:COG3083 482 FSRYQ--LQVPLVIHWPGTPPQ-VISKLTSHLDIVPTLM 517
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
32-458 |
7.25e-10 |
|
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: 61.33 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 32 PNVVLVVSDSF---DGRLTFHPGSQVvklPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSG-------LFT---HLTES 98
Cdd:cd16157 2 PNIILMLMDDMgwgDLGVFGEPSRET---PNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGrlpirngFYTtnaHARNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 99 W---NNFKGLDPNYTTWMDVMERHGYRTQKFGK--LDYTSGHHSISNRVEAW--TRDVAFllrqegRPMVNLIRNRTKVR 171
Cdd:cd16157 79 YtpqNIVGGIPDSEILLPELLKKAGYRNKIVGKwhLGHRPQYHPLKHGFDEWfgAPNCHF------GPYDNKAYPNIPVY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 172 vmeRDWQNTDKavnwlrkeainYTEPFVIYLglnlphpypspSSGE-NFGSSTFHTSLYWLEKvSHDAIK--IPKWSPLS 248
Cdd:cd16157 153 ---RDWEMIGR-----------YYEEFKIDK-----------KTGEsNLTQIYLQEALEFIEK-QHDAQKpfFLYWAPDA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 249 EMHPVdyYSSytKNCTGrftkkeiKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFY--- 325
Cdd:cd16157 207 THAPV--YAS--KPFLG-------TSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALISAPEQGgsn 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 326 ------KMSMYEASAHVPLLMMGPG-IKAGlQVSN-VVSLVDIYPTMLDIAGIPLPQN--LSGYSLLPL----------- 384
Cdd:cd16157 276 gpflcgKQTTFEGGMREPAIAWWPGhIKPG-QVSHqLGSLMDLFTTSLALAGLPIPSDraIDGIDLLPVllngkekdrpi 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 385 ----SSETFKNEHKVKNLHP-PWILSE------FHGC---NVNASTYMLRTNHwkyiaysdgaSILPQLFDLSSDPDELT 450
Cdd:cd16157 355 fyyrGDELMAVRLGQYKAHFwTWSNSWeefrkgINFCpgqNVPGVTTHNQTDH----------TKLPLLFHLGRDPGEKY 424
|
....*...
gi 39930577 451 NVAVKFPE 458
Cdd:cd16157 425 PISFKSAE 432
|
|
| DUF4994 |
pfam16385 |
Domain of unknown function; This family around 100 residues locates in the C-terminal of some ... |
401-467 |
1.31e-09 |
|
Domain of unknown function; This family around 100 residues locates in the C-terminal of some uncharacterized proteins in various Bacteroides and Prevotella species. The function of this family remains unknown.
Pssm-ID: 406720 [Multi-domain] Cd Length: 98 Bit Score: 55.37 E-value: 1.31e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39930577 401 PWILSefHGCNvnaSTYMLRTNHWKYIAYSDGASIL------------PQLFDLSSDPDELTNVAVKFPEITYSLDQKL 467
Cdd:pfam16385 25 PYVIE--QALN---GTLSVRTGDWKYIEPSDGPAYIkwtkietgnspePQLYDLKADPGEQENVAKKHPEKVKELQTIL 98
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
281-369 |
4.67e-08 |
|
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: 54.51 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 281 AMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHG--ELAMeHRQF-YKMSMyeasaHVPLLMMGPGIKAGLQVSNVvSL 357
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGmtDVGT-HGYDnELPDM-----RAIFIARGPAFKKGKKLGPF-RN 255
|
90
....*....|..
gi 39930577 358 VDIYPTMLDIAG 369
Cdd:cd16018 256 VDIYPLMCNLLG 267
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
251-370 |
2.81e-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: 52.24 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 251 HPvDYYSSYTKN-------CTGRFTKKEIKNIRAFY-----YamcaeTDAMLGEIILALHQLDllQKTIVIYSSDHGElA 318
Cdd:cd16017 154 HG-PYYDRYPEEfakftpdCDNELQSCSKEELINAYdnsilY-----TDYVLSQIIERLKKKD--KDAALIYFSDHGE-S 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930577 319 MEHRQFYKMSMYEAS---AHVPLLMMG--------PGIKAGLQVSNVVSLVDIYPTMLDIAGI 370
Cdd:cd16017 225 LGENGLYLHGAPYAPkeqYHVPFIIWSsdsykqryPVERLRANKDRPFSHDNLFHTLLGLLGI 287
|
|
| AP-SPAP |
cd16016 |
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
328-373 |
8.63e-06 |
|
SPAP is a subclass of alkaline phosphatase (AP); 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. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.
Pssm-ID: 293740 [Multi-domain] Cd Length: 457 Bit Score: 48.30 E-value: 8.63e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 39930577 328 SMYEASAHVPLLMMGPGIKAGlQVSNVVSLVDIYPTMLDIAGIPLP 373
Cdd:cd16016 403 SPYDYDTHVPLLFYGWGIKPG-EIPRPVEITDIAPTLAALLGIQPP 447
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
328-371 |
2.55e-04 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 43.58 E-value: 2.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 39930577 328 SMYEASAHVPLLMMGPGIKAGlqvsnvVSLVDIYPTMLDIAGIP 371
Cdd:COG1524 331 GLPDEEMRVPLLASGPGFRPG------VRNVDVAPTIARLLGLP 368
|
|
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
286-370 |
8.81e-04 |
|
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441797 [Multi-domain] Cd Length: 537 Bit Score: 42.15 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 286 TDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQF-----YKM---SMYeasaHVPLLM-MGPGIKAGLQV----- 351
Cdd:COG2194 421 TDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYlhgtpYAIapdEQT----HVPMIMwLSDGYAQRYGIdfacl 496
|
90 100
....*....|....*....|...
gi 39930577 352 ----SNVVSLVDIYPTMLDIAGI 370
Cdd:COG2194 497 karaDKPYSHDNLFHTLLGLLDV 519
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
283-382 |
1.34e-03 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 41.25 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 283 CAETDAMLGEIILALHQLDllqkTIVIYSSDHG--ELamehrqfykmsMYEAS------AH----VPLLMMGPGIKAGLQ 350
Cdd:cd16010 409 VEAVDECLGRIVEAVLENG----GTLLITADHGnaEE-----------MIDPEtggphtAHttnpVPFIIVDPGLKRKLL 473
|
90 100 110
....*....|....*....|....*....|..
gi 39930577 351 VSNvvSLVDIYPTMLDIAGIPLPQNLSGYSLL 382
Cdd:cd16010 474 KDG--GLADVAPTILDLLGIEKPKEMTGKSLI 503
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
285-375 |
8.93e-03 |
|
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 38.31 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930577 285 ETDAMLGEIILALHQLDLLQKTIVIYSSDHGelamehrqfykmsMYEASAH---------VPLLMMGPGIKA-------G 348
Cdd:cd16024 175 EMDDVIKRIYESLEEQSSNNPTLLVVCGDHG-------------MTDAGNHggsspgetsVPLLFISPKFSSkpsnadgE 241
|
90 100
....*....|....*....|....*..
gi 39930577 349 LQVSNVVSLVDIYPTMLDIAGIPLPQN 375
Cdd:cd16024 242 LSYYETVQQVDLAPTLALLLGLPIPKN 268
|
|
| |
