|
Name |
Accession |
Description |
Interval |
E-value |
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
27-505 |
0e+00 |
|
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: 658.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 27 KRPNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNA-STFDGN 105
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNgPLFDAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 106 QQTFPKLLQAAGYQTSIVGKWHL----ITEPQGFDYWCILTGQheqGDYYNPDFNENGKQIVEQGYTTDVITDKAIEYLE 181
Cdd:cd16031 81 QPTYPKLLRKAGYQTAFIGKWHLgsggDLPPPGFDYWVSFPGQ---GSYYDPEFIENGKRVGQKGYVTDIITDKALDFLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 182 HRDKSKPFCMMYHQKAPHRNWMPAPRHLGMFNNTVFPEPATLF-DTYEGRGSAAIEQDMSIEHTLTNDWDLKlltreeml 260
Cdd:cd16031 158 ERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPETFDdDDYAGRPEWAREQRNRIRGVLDGRFDTP-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 261 kdttnrlyqvykrmpadvqdkwdsvyaqriseyrsgnlrgkelisWKYQQYMRDYLATIVAVDENIGRLLGYLEKNGELD 340
Cdd:cd16031 230 ---------------------------------------------EKYQRYMKDYLRTVTGVDDNVGRILDYLEEQGLAD 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 341 NTIIIYTSDQGFFLGEHGWFDKRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMNVDFAPTLLDFAGVDIPADIQGQSLRT 420
Cdd:cd16031 265 NTIIIYTSDNGFFLGEHGLFDKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 421 ILEngGKTPADWRKAAYYHYYEYPAEHSVKRHYGIRTADFKLIHFYNDVDEWEMYDLKNDPSELNSVFGKPEYADKQAEL 500
Cdd:cd16031 345 LLE--GEKPVDWRKEFYYEYYEEPNFHNVPTHEGVRTERYKYIYYYGVWDEEELYDLKKDPLELNNLANDPEYAEVLKEL 422
|
....*
gi 949759693 501 ISLLK 505
Cdd:cd16031 423 RKRLE 427
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-513 |
1.06e-149 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 434.31 E-value: 1.06e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 1 MNRLSYIFLPLTAigmsaCSSGKEEVKRPNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPS 80
Cdd:COG3119 1 MKRLLLLLLALLA-----AAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 81 RACILTGKFSHINGFTDNAS----TFDGNQQTFPKLLQAAGYQTSIVGKWHLitepqgfdywciltgqheqgdyynpdfn 156
Cdd:COG3119 76 RASLLTGRYPHRTGVTDNGEgyngGLPPDEPTLAELLKEAGYRTALFGKWHL---------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 157 engkqiveqgYTTDVITDKAIEYLE-HRDKSKPFCMMYHQKAPHRNWMPAPRHLGMFNNTVFPEPATLfdtyegrgsaai 235
Cdd:COG3119 128 ----------YLTDLLTDKAIDFLErQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPLPPNL------------ 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 236 eqdmsiehtltndwdlklltreemlkdttnrlyqvykrMPADVQDkwdsvyaqriseyrsgnlrgkelisWKYQQYMRDY 315
Cdd:COG3119 186 --------------------------------------APRDLTE-------------------------EELRRARAAY 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 316 LATIVAVDENIGRLLGYLEKNGELDNTIIIYTSDQGFFLGEHGW-FDKRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMN 394
Cdd:COG3119 203 AAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLrGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSL 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 395 VDFAPTLLDFAGVDIPADIQGQSLRTILENGgktPADWRKAAYYHYYEYPaehsvkRHYGIRTADFKLIHFYNDVDEWEM 474
Cdd:COG3119 283 IDLLPTLLDLAGVPIPEDLDGRSLLPLLTGE---KAEWRDYLYWEYPRGG------GNRAIRTGRWKLIRYYDDDGPWEL 353
|
490 500 510
....*....|....*....|....*....|....*....
gi 949759693 475 YDLKNDPSELNSVFGkpEYADKQAELISLLKKIQKQYKD 513
Cdd:COG3119 354 YDLKNDPGETNNLAA--DYPEVVAELRALLEAWLKELGD 390
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-485 |
1.43e-99 |
|
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: 306.42 E-value: 1.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 28 RPNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFDGNQQ 107
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVPLPPDAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 108 TFPKLLQAAGYQTSIVGKWHL-------------ITEP---QGFDYWCILTGQHeqgDYYNP-DFNENGKQIVEQGYTTD 170
Cdd:cd16034 81 TIADVLKDAGYRTGYIGKWHLdgperndgraddyTPPPerrHGFDYWKGYECNH---DHNNPhYYDDDGKRIYIKGYSPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 171 VITDKAIEYLE-HRDKSKPFCMM--YHQkaPHRNWMPAP-RHLGMFNntvfpepatlfdtyegrgsaaieqdmsiehtlt 246
Cdd:cd16034 158 AETDLAIEYLEnQADKDKPFALVlsWNP--PHDPYTTAPeEYLDMYD--------------------------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 247 ndwDLKLLTREEmlkdttnrlyqvykrMPADVQDKwdsvyaqriseyrsgnlrgkelisWKYQQYMRDYLATIVAVDENI 326
Cdd:cd16034 203 ---PKKLLLRPN---------------VPEDKKEE------------------------AGLREDLRGYYAMITALDDNI 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 327 GRLLGYLEKNGELDNTIIIYTSDQGFFLGEHGWFDKRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMNVDFAPTLLDFAG 406
Cdd:cd16034 241 GRLLDALKELGLLENTIVVFTSDHGDMLGSHGLMNKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCG 320
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949759693 407 VDIPADIQGQSLRTILENGGKTPADWRKAAYYHYYEYPAEHSVKRHYGIRTADFKLIHFYNdvDEWEMYDLKNDPSELN 485
Cdd:cd16034 321 LPIPDTVEGRDLSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVRTDRYTYVRDKN--GPWLLFDNEKDPYQLN 397
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-513 |
2.12e-98 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 303.76 E-value: 2.12e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFDGNQQ- 107
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 108 ------TFPKLLQAAGYQTSIVGKWHLITE--PQ--GFDYWCiltGQHEQGDYYnpdfnengkqiveqgyttdvITDKAI 177
Cdd:cd16033 81 lppgveTFSEDLREAGYRNGYVGKWHVGPEetPLdyGFDEYL---PVETTIEYF--------------------LADRAI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 178 EYLE-HRDKSKPFCMMYHQKAPHRNWMPAPRHLGMFNNTVFPEPATLFDTYEGRgsaaieqdmsiehtltndwdlklltr 256
Cdd:cd16033 138 EMLEeLAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDK-------------------------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 257 eemlkdttNRLYQVYKRMPADVQDKWDsvyaqriseyrsgnlrgkeliswKYQQYMRDYLATIVAVDENIGRLLGYLEKN 336
Cdd:cd16033 192 --------PYIYRRERKRWGVDTEDEE-----------------------DWKEIIAHYWGYITLIDDAIGRILDALEEL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 337 GELDNTIIIYTSDQGFFLGEHGWFDKR-FMYEECQRMPLVIRYPKAIKAGSVSSAIAMNVDFAPTLLDFAGVDIPADIQG 415
Cdd:cd16033 241 GLADDTLVIFTSDHGDALGAHRLWDKGpFMYEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDG 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 416 QSLRTILEngGKTPADWRKAAY--YHYYEYPAEHSVkrhygIRTADFKLIhfYNDVDEWEMYDLKNDPSELNSVFGKPEY 493
Cdd:cd16033 321 RSLLPLLR--GEQPEDWRDEVVteYNGHEFYLPQRM-----VRTDRYKYV--FNGFDIDELYDLESDPYELNNLIDDPEY 391
|
490 500
....*....|....*....|
gi 949759693 494 ADKQAELISLLKKIQKQYKD 513
Cdd:cd16033 392 EEILREMRTRLYEWMEETGD 411
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
29-509 |
3.50e-96 |
|
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: 296.73 E-value: 3.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQaMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNAS---TFDGN 105
Cdd:cd16027 1 PNILWIIADDLSPD-LGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSrgfPLPDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 106 QQTFPKLLQAAGYQTSIVGKWHLitepqgfdywciltgqheqGDYYNPDFNENGKQIVEQGYTTDVITDKAIEYLEHRDK 185
Cdd:cd16027 80 VKTLPELLREAGYYTGLIGKTHY-------------------NPDAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRAKK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 186 SKPFCMMYHQKAPHRNWMPAPRHLGMFNNTVFPEPATLFDTYEgrgsaaieqdmsiehtltndwdlkllTREEMLkdttn 265
Cdd:cd16027 141 GQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPYLPDTPE--------------------------VREDLA----- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 266 rlyqvykrmpadvqdkwdsvyaqriseyrsgnlrgkeliswkyqqymrDYLATIVAVDENIGRLLGYLEKNGELDNTIII 345
Cdd:cd16027 190 ------------------------------------------------DYYDEIERLDQQVGEILDELEEDGLLDNTIVI 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 346 YTSDqgfflgeHGW---FDKRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMNVDFAPTLLDFAGVDIPADIQGQSLRTIL 422
Cdd:cd16027 222 FTSD-------HGMpfpRAKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLL 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 423 ENGgktPADWRKAAYyhyyeypAEHSvkRH----Y---GIRTADFKLIHFYNdvdEWEMYDLKNDPSELNSVFGKPEYAD 495
Cdd:cd16027 295 KGE---KDPGRDYVF-------AERD--RHdetyDpirSVRTGRYKYIRNYM---PEELYDLKNDPDELNNLADDPEYAE 359
|
490
....*....|....
gi 949759693 496 KQAELISLLKKIQK 509
Cdd:cd16027 360 VLEELRAALDAWMK 373
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
28-491 |
2.55e-89 |
|
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: 279.82 E-value: 2.55e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 28 RPNIIFMMTDDHTTQAMScyggrflQTPNM---DRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFDG 104
Cdd:cd16147 1 RPNIVLILTDDQDVELGS-------MDPMPktkKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPPGGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 105 ---------NQQTFPKLLQAAGYQTSIVGK----WHLITE----PQGFDYWCILTGQHeQGDYYNPDFNENGKQIV--EQ 165
Cdd:cd16147 74 ypkfwqnglERSTLPVWLQEAGYRTAYAGKylngYGVPGGvsyvPPGWDEWDGLVGNS-TYYNYTLSNGGNGKHGVsyPG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 166 GYTTDVITDKAIEYLE-HRDKSKPFCMMYHQKAPHRNWMPAPRHLGMFNNTVFPEPATLFDTYEGRGSAaieqdmsieht 244
Cdd:cd16147 153 DYLTDVIANKALDFLRrAAADDKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPPRPPPNNPDVSDKPH----------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 245 ltndWDLKLltreemlkdttnrlyqvyKRMPADVQDKWDSVYAQRiseyrsgnlrgkeliswkyqqymrdyLATIVAVDE 324
Cdd:cd16147 222 ----WLRRL------------------PPLNPTQIAYIDELYRKR--------------------------LRTLQSVDD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 325 NIGRLLGYLEKNGELDNTIIIYTSDQGFFLGEHGW-FDKRFMYEECQRMPLVIRYPkAIKAGSVSSAIAMNVDFAPTLLD 403
Cdd:cd16147 254 LVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLpPGKRTPYEEDIRVPLLVRGP-GIPAGVTVDQLVSNIDLAPTILD 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 404 FAGVDIPADIQGQSlrtilenggktPADWRKAAYyhyyeypaehsvkrhYGIRTADFKLIHFYN--DVDEWEMYDLKNDP 481
Cdd:cd16147 333 LAGAPPPSDMDGRS-----------CGDSNNNTY---------------KCVRTVDDTYNLLYFewCTGFRELYDLTTDP 386
|
490
....*....|
gi 949759693 482 SELNSVFGKP 491
Cdd:cd16147 387 YQLTNLAGDL 396
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
29-506 |
3.65e-86 |
|
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: 272.49 E-value: 3.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFS---HINGFTDNASTFDGN 105
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYParlGITDVIPGRRGPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 106 Q---------------QTFPKLLQAAGYQTSIVGKWHLITEP------QGFDYWCILTGQHEQGDYYNPDFNENG--KQI 162
Cdd:cd16144 81 TklipppsttrlpleeVTIAEALKDAGYATAHFGKWHLGGEGgygpedQGFDVNIGGTGNGGPPSYYFPPGKPNPdlEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 163 VEQGYTTDVITDKAIEYLEhRDKSKPFCMMYHQKAPHrnwmpAPrhlgmfnntvfpepatlfdtyegrgsaaieqdmsie 242
Cdd:cd16144 161 PEGEYLTDRLTDEAIDFIE-QNKDKPFFLYLSHYAVH-----TP------------------------------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 243 htltndwdlkLLTREEMLKDttnrlyqvYKRMPADvqdkwdsvyaqriseyrsgnlrgkelisWKYQQYMRDYLATIVAV 322
Cdd:cd16144 199 ----------IQARPELIEK--------YEKKKKG----------------------------LRKGQKNPVYAAMIESL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 323 DENIGRLLGYLEKNGELDNTIIIYTSDQGFFLGEHGWFD--------KRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMN 394
Cdd:cd16144 233 DESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTsnaplrggKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 395 VDFAPTLLDFAGVDIPA--DIQGQSLRTILENGGKTPAdwRKAAYYHyyeYPAEHSVKRHYG--IRTADFKLIHFYNDvD 470
Cdd:cd16144 313 TDLYPTFLELAGGPLPPpqHLDGVSLVPLLKGGEADLP--RRALFWH---FPHYHGQGGRPAsaIRKGDWKLIEFYED-G 386
|
490 500 510
....*....|....*....|....*....|....*.
gi 949759693 471 EWEMYDLKNDPSELNSVFGkpEYADKQAELISLLKK 506
Cdd:cd16144 387 RVELYNLKNDIGETNNLAA--EMPEKAAELKKKLDA 420
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
29-417 |
3.42e-81 |
|
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: 253.13 E-value: 3.42e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFDG---N 105
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGlppD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 106 QQTFPKLLQAAGYQTSIVGKWHlitepqgfdywciltgqheqgdyynpdfnengkqiveqgyttdvitDKAIEYLEHRDK 185
Cdd:cd16022 81 EPTLAELLKEAGYRTALIGKWH----------------------------------------------DEAIDFIERRDK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 186 SKPFCMMYHQKAPHRNWMpaprhlgmfnntvfpepatlfdtyegrgsaaieqdmsiehtltndwdlklltreemlkdttn 265
Cdd:cd16022 115 DKPFFLYVSFNAPHPPFA-------------------------------------------------------------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 266 rlyqvykrmpadvqdkwdsvyaqriseyrsgnlrgkeliswkyqqymrdYLATIVAVDENIGRLLGYLEKNGELDNTIII 345
Cdd:cd16022 133 -------------------------------------------------YYAMVSAIDDQIGRILDALEELGLLDNTLIV 163
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949759693 346 YTSDQGFFLGEHGW-FDKRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMNVDFAPTLLDFAGVDIPADIQGQS 417
Cdd:cd16022 164 FTSDHGDMLGDHGLrGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
29-514 |
7.78e-81 |
|
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: 258.25 E-value: 7.78e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDhttQA---MSCYGGRFLQTPNMDRIANEGVRMDNCYaVNALSGPSRACILTGKFSHINGFTDNA---STF 102
Cdd:cd16146 1 PNVILILTDD---QGygdLGFHGNPILKTPNLDRLAAESVRFTNFH-VSPVCAPTRAALLTGRYPFRTGVWHTIlgrERM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 103 DGNQQTFPKLLQAAGYQTSIVGKWHLITEP------QGFDYWCILTGQHeQGDYYNPDFNE--------NGKQIVEQGYT 168
Cdd:cd16146 77 RLDETTLAEVFKDAGYRTGIFGKWHLGDNYpyrpqdRGFDEVLGHGGGG-IGQYPDYWGNDyfddtyyhNGKFVKTEGYC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 169 TDVITDKAIEYLEhRDKSKPFCMMYHQKAPHRnwmpaprhlgmfnntvfpepatlfdtyegrgsaaieqdmsiehtltnd 248
Cdd:cd16146 156 TDVFFDEAIDFIE-ENKDKPFFAYLATNAPHG------------------------------------------------ 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 249 wdlklltreemlkdttnrlyqvykrmPADVQDK-WDSVYAQRISEYRSGnlrgkeliswkyqqymrdYLATIVAVDENIG 327
Cdd:cd16146 187 --------------------------PLQVPDKyLDPYKDMGLDDKLAA------------------FYGMIENIDDNVG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 328 RLLGYLEKNGELDNTIIIYTSDQGFflgeHGWFDKRF---M-------YEECQRMPLVIRYPKAIKAGSVSSAIAMNVDF 397
Cdd:cd16146 223 RLLAKLKELGLEENTIVIFMSDNGP----AGGVPKRFnagMrgkkgsvYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDL 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 398 APTLLDFAGVDIPADIQ--GQSLRTILENGgkTPADWRKAAYYHYYEYPAEHSVKRHYGIRTADFKLIHfyNDVDEWEMY 475
Cdd:cd16146 299 LPTLLDLCGVKLPEGIKldGRSLLPLLKGE--SDPWPERTLFTHSGRWPPPPKKKRNAAVRTGRWRLVS--PKGFQPELY 374
|
490 500 510
....*....|....*....|....*....|....*....
gi 949759693 476 DLKNDPSELNSVfgkpeyADKQAELISLLKKIQKQYKDD 514
Cdd:cd16146 375 DIENDPGEENDV------ADEHPEVVKRLKAAYEAWWDD 407
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
27-485 |
9.32e-79 |
|
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: 252.75 E-value: 9.32e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 27 KRPNIIFMMTDDhttqaM-----SCYGGRfLQTPNMDRIANEGVRMDNCYaVNALSGPSRACILTGKFSHINGF---TDN 98
Cdd:cd16025 1 GRPNILLILADD-----LgfsdlGCFGGE-IPTPNLDALAAEGLRFTNFH-TTALCSPTRAALLTGRNHHQVGMgtmAEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 99 ASTFDGNQ-------QTFPKLLQAAGYQTSIVGKWHLItePQGFdywciltgqheqgdyynpdfnengkqiveqgYTTDV 171
Cdd:cd16025 74 ATGKPGYEgylpdsaATIAEVLKDAGYHTYMSGKWHLG--PDDY-------------------------------YSTDD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 172 ITDKAIEYL-EHRDKSKPFcMMY--HQkAPHrnwmpAPRHLgmfnntvfpePATLFDTYEGR---Gsaaieqdmsiehtl 245
Cdd:cd16025 121 LTDKAIEYIdEQKAPDKPF-FLYlaFG-APH-----APLQA----------PKEWIDKYKGKydaG-------------- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 246 tndWDlKLltREemlkdttnrlyQVYKRM------PADVQ--------DKWDSVYAQRiseyrsgnlrgKELiswkYQQY 311
Cdd:cd16025 170 ---WD-AL--RE-----------ERLERQkelgliPADTKltprppgvPAWDSLSPEE-----------KKL----EARR 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 312 MRDYLATIVAVDENIGRLLGYLEKNGELDNTIIIYTSDQGfFLGEHGW---------FDKRFMYEECQRMPLVIRYPKAI 382
Cdd:cd16025 218 MEVYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNG-ASAEPGWanasntpfrLYKQASHEGGIRTPLIVSWPKGI 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 383 KA-GSVSSAIAMNVDFAPTLLDFAGVDIPAD--------IQGQSLRTILeNGGKTPADwRKAAYYhyyeypaEHSvkRHY 453
Cdd:cd16025 297 KAkGGIRHQFAHVIDIAPTILELAGVEYPKTvngvpqlpLDGVSLLPTL-DGAAAPSR-RRTQYF-------ELF--GNR 365
|
490 500 510
....*....|....*....|....*....|....*
gi 949759693 454 GIRTADFKLIHFYN---DVDEWEMYDLKNDPSELN 485
Cdd:cd16025 366 AIRKGGWKAVALHPppgWGDQWELYDLAKDPSETH 400
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-505 |
2.71e-77 |
|
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: 247.86 E-value: 2.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 27 KRPNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSG----PSRACILTGKF----SHINGFTDN 98
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWSGavcvPSRAMLMTGRTlfhaPEGGKAAIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 99 AstfdgNQQTFPKLLQAAGYQTSIVGKWHlitepqgfdywciltgqheqgdyynpdfneNGkqiveqgyttdvITDKAIE 178
Cdd:cd16155 81 S-----DDKTWPETFKKAGYRTFATGKWH------------------------------NG------------FADAAIE 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 179 YLEHRDKS-KPFCMMYHQKAPHRNWMPAPRHLGMFNNTVFPEPATLFDtyegrgsaaieqdmsiEHTLTNDWdlkLLTRE 257
Cdd:cd16155 114 FLEEYKDGdKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPLPENFLP----------------QHPFDNGE---GTVRD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 258 EMLKDttnrlyqvYKRMPADVQdkwdsvyaqriseyrsgnlrgKELiswkyqqymRDYLATIVAVDENIGRLLGYLEKNG 337
Cdd:cd16155 175 EQLAP--------FPRTPEAVR---------------------QHL---------AEYYAMITHLDAQIGRILDALEASG 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 338 ELDNTIIIYTSDQGFFLGEHGWFDKRFMYEECQRMPLVIRYPkAIKAGSVSSAIAMNVDFAPTLLDFAGVDIPADIQGQS 417
Cdd:cd16155 217 ELDNTIIVFTSDHGLAVGSHGLMGKQNLYEHSMRVPLIISGP-GIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKS 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 418 LRTILENGGKTpadWRKAAYYHYyeypaehsVKRHYGIRTADFKLIHFYNDVDEWEMYDLKNDPSELNSVFGKPEYADKQ 497
Cdd:cd16155 296 LLPVIRGEKKA---VRDTLYGAY--------RDGQRAIRDDRWKLIIYVPGVKRTQLFDLKKDPDELNNLADEPEYQERL 364
|
....*...
gi 949759693 498 AELISLLK 505
Cdd:cd16155 365 KKLLAELK 372
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
27-493 |
6.70e-75 |
|
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: 243.63 E-value: 6.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 27 KRPNIIFMMTDDHTTQaMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFD--- 103
Cdd:cd16030 1 KKPNVLFIAVDDLRPW-LGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRkva 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 104 GNQQTFPKLLQAAGYQTSIVGK------WHLITEPQGFDYWCILTGQHEqgdYYNPDFNENGKQIVEQGYTTDV------ 171
Cdd:cd16030 80 PDAVTLPQYFKENGYTTAGVGKifhpgiPDGDDDPASWDEPPNPPGPEK---YPPGKLCPGKKGGKGGGGGPAWeaadvp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 172 --------ITDKAIEYL-EHRDKSKPFCMM--YHQkaPHRNWmpaprhlgmfnntVFPEpaTLFDTYEgrgsaaieqdms 240
Cdd:cd16030 157 deaypdgkVADEAIEQLrKLKDSDKPFFLAvgFYK--PHLPF-------------VAPK--KYFDLYP------------ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 241 iehtltndwdlklltreemLKDTTNRLYQVYKRMPADVQDKWDSVYAQRISEYRSGNLRGKELISWKYQQYMRDYLATIV 320
Cdd:cd16030 208 -------------------LESIPLPNPFDPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPDEQARELRQAYYASVS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 321 AVDENIGRLLGYLEKNGELDNTIIIYTSDQGFFLGEHGWFDKRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMNVDFAPT 400
Cdd:cd16030 269 YVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPT 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 401 LLDFAGVDIPADIQGQSLRTILENGGktpADWRKAAyYHYYEYPAehsvKRHYGIRTADFKLIHFYNDVDEW--EMYDLK 478
Cdd:cd16030 349 LAELAGLPAPPCLEGKSLVPLLKNPS---AKWKDAA-FSQYPRPS----IMGYSIRTERYRYTEWVDFDKVGaeELYDHK 420
|
490
....*....|....*
gi 949759693 479 NDPSELNSVFGKPEY 493
Cdd:cd16030 421 NDPNEWKNLANDPEY 435
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-481 |
1.94e-73 |
|
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: 235.90 E-value: 1.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFDGNQQT 108
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDGDVPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 109 FPKLLQAAGYQTSIVGKWHLITEPQ--GFDYwciltgqheqgdyynpdfnengkqiveqgytTDVITDKAIEYL-EHRDK 185
Cdd:cd16037 81 WGHALRAAGYETVLIGKLHFRGEDQrhGFRY-------------------------------DRDVTEAAVDWLrEEAAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 186 SKPFCMMYHQKAPHrnwmpaprhlgmfnntvFPepatlfdtyegrgsaaieqdmsiehtltndwdlkLLTREEMlkdttn 265
Cdd:cd16037 130 DKPWFLFVGFVAPH-----------------FP----------------------------------LIAPQEF------ 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 266 rlyqvykrmpadvqdkwdsvyaqriseyrsgnlrgkeliswkYQQYMRD----YLATIVAVDENIGRLLGYLEKNGELDN 341
Cdd:cd16037 153 ------------------------------------------YDLYVRRaraaYYGLVEFLDENIGRVLDALEELGLLDN 190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 342 TIIIYTSDQGFFLGEHGWFDKRFMYEECQRMPLVIRYPKaIKAGSVSSAIAMNVDFAPTLLDFAGVDIPADIQGQSLRTI 421
Cdd:cd16037 191 TLIIYTSDHGDMLGERGLWGKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPL 269
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 422 LENggktPADWRKAAyyhYYEYPAEHSVKRHYGIRTADFKLIHFYNDVDewEMYDLKNDP 481
Cdd:cd16037 270 AEG----PDDPDRVV---FSEYHAHGSPSGAFMLRKGRWKYIYYVGYPP--QLFDLENDP 320
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
29-504 |
5.73e-71 |
|
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: 233.69 E-value: 5.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTD----DHttqaMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFDG 104
Cdd:cd16028 1 RNVLFITADqwraDC----LSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGTPLDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 105 NQQTFPKLLQAAGYQTSIVGKWHLITEPQG--------FDYWCILTGqheqgdyYNPDFNENGkqIVEQGYTTDVITDKA 176
Cdd:cd16028 77 RHLTLALELRKAGYDPALFGYTDTSPDPRGlapldprlLSYELAMPG-------FDPVDRLDE--YPAEDSDTAFLTDRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 177 IEYLEHRDKsKPFCMMYHQKAPHRNWM-PAPRHlGMFNNTVFPEPatlfdtyEGRGSAAIEQDmsiEHTLtndwdLKLLt 255
Cdd:cd16028 148 IEYLDERQD-EPWFLHLSYIRPHPPFVaPAPYH-ALYDPADVPPP-------IRAESLAAEAA---QHPL-----LAAF- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 256 REEMLKDTTNRLYQVYKRMPADVQDKWDSVYAQRISEyrsgnlrgkeliswkyqqymrdylativaVDENIGRLLGYLEK 335
Cdd:cd16028 210 LERIESLSFSPGAANAADLDDEEVAQMRATYLGLIAE-----------------------------VDDHLGRLFDYLKE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 336 NGELDNTIIIYTSDQGFFLGEHGWFDKRFMYEECQRMPLVIRYPKA---IKAGSVSSAIAMNVDFAPTLLDFAGVDIPAD 412
Cdd:cd16028 261 TGQWDDTLIVFTSDHGEQLGDHWLWGKDGFFDQAYRVPLIVRDPRReadATRGQVVDAFTESVDVMPTILDWLGGEIPHQ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 413 IQGQSLRTILEngGKTPADWRKAAYYHYYEYPAEHS-VKRHYG----------IRTADFKLIHFyNDVDEwEMYDLKNDP 481
Cdd:cd16028 341 CDGRSLLPLLA--GAQPSDWRDAVHYEYDFRDVSTRrPQEALGlspdecslavIRDERWKYVHF-AALPP-LLFDLKNDP 416
|
490 500
....*....|....*....|...
gi 949759693 482 SELNSVFGKPEYADKQAELISLL 504
Cdd:cd16028 417 GELRDLAADPAYAAVVLRYAQKL 439
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-509 |
9.02e-69 |
|
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: 225.57 E-value: 9.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 28 RPNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFDGNQQ 107
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNGIPLPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 108 TFPKLLQAAGYQTSIVGKWHLitepqgfdywciltgqheqgdyynpdfnengkqiveQGYTTDVITDKAIEYLEHRDKSK 187
Cdd:cd16152 81 TLAHYFRDAGYETGYVGKWHL------------------------------------AGYRVDALTDFAIDYLDNRQKDK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 188 PFCMMYHQKAPHrnwmpaprhlgMFNNTvfpepatlfDTYEG-RGSAAIEQDMSIehtltndwdlklltreemlkdttnr 266
Cdd:cd16152 125 PFFLFLSYLEPH-----------HQNDR---------DRYVApEGSAERFANFWV------------------------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 267 lyqvykrmPADVQDkwdsvyaqriseyRSGNlrgkeliswkYQQYMRDYLATIVAVDENIGRLLGYLEKNGELDNTIIIY 346
Cdd:cd16152 160 --------PPDLAA-------------LPGD----------WAEELPDYLGCCERLDENVGRIRDALKELGLYDNTIIVF 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 347 TSDQG-FFL---GEHgwfdKRFMYEECQRMPLVIRYPkAIKAGSVSSAIAMNVDFAPTLLDFAGVDIPADIQGQSLRTIL 422
Cdd:cd16152 209 TSDHGcHFRtrnAEY----KRSCHESSIRVPLVIYGP-GFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLV 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 423 ENggkTPADWRKAAYYHYyeypAEHSVKRhyGIRTADFKLI------HFYNDVD-----EWEMYDLKNDPSELNSVFGKP 491
Cdd:cd16152 284 DG---KVEDWRNEVFIQI----SESQVGR--AIRTDRWKYSvaapdkDGWKDSGsdvyvEDYLYDLEADPYELVNLIGRP 354
|
490
....*....|....*....
gi 949759693 492 EYADKQAELIS-LLKKIQK 509
Cdd:cd16152 355 EYREVAAELRErLLARMAE 373
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
29-487 |
9.04e-69 |
|
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: 227.09 E-value: 9.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKfsHI-------NGFTDNAST 101
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGL--HTghtrvrgNSEPGGQDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 102 FDGNQQTFPKLLQAAGYQTSIVGKWHL-------ITEPQGFDYWcilTGQHEQGD---YYNPDFNENGKQI--------- 162
Cdd:cd16145 79 LPPDDVTLAEVLKKAGYATAAFGKWGLggpgtpgHPTKQGFDYF---YGYLDQVHahnYYPEYLWRNGEKVplpnnvipp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 163 ---------VEQGYTTDVITDKAIEYL-EHRDksKPFCMMYHQKAPHRNWmpaprhlgmfnntvfpepatlfdtyegrgs 232
Cdd:cd16145 156 ldegnnaggGGGTYSHDLFTDEALDFIrENKD--KPFFLYLAYTLPHAPL------------------------------ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 233 aaieqdmsiehtltndwdlklltreemlkdttnrlyQVYKRMPADVQDKWDSVYAQRiseyrsgnlrgkeliSWKYQQym 312
Cdd:cd16145 204 ------------------------------------QVPDDGPYKYKPKDPGIYAYL---------------PWPQPE-- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 313 RDYLATIVAVDENIGRLLGYLEKNGELDNTIIIYTSDQG------------FFLGeHGWFD--KRFMYEECQRMPLVIRY 378
Cdd:cd16145 231 KAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGphseggsehdpdFFDS-NGPLRgyKRSLYEGGIRVPFIARW 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 379 PKAIKAGSVSSAIAMNVDFAPTLLDFAGVDIPADIQGQS-LRTILENGGKTPADwrkaayYHYYEypaEHSVKRHYGIRT 457
Cdd:cd16145 310 PGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISlLPTLLGKPQQQQHD------YLYWE---FYEGGGAQAVRM 380
|
490 500 510
....*....|....*....|....*....|
gi 949759693 458 ADFKLIHFYNDVDEWEMYDLKNDPSELNSV 487
Cdd:cd16145 381 GGWKAVRHGKKDGPFELYDLSTDPGETNNL 410
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-485 |
9.27e-64 |
|
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: 212.46 E-value: 9.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAvNALSGPSRACILTGKFSHING---FTDNAStfdgn 105
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRNYvvfGYLDPK----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 106 QQTFPKLLQAAGYQTSIVGKWHLITEPQ--------GFDYWCILTGQHEQGDYYNPD----FNENGKQI--VEQGYTTDV 171
Cdd:cd16151 75 QKTFGHLLKDAGYATAIAGKWQLGGGRGdgdyphefGFDEYCLWQLTETGEKYSRPAtptfNIRNGKLLetTEGDYGPDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 172 ITDKAIEYLEhRDKSKPFCMMYHQKAPHRNWMPAPrhlgmfnntvfpepatlfdtyegrgsaaieqdmsiehtLTNDWDL 251
Cdd:cd16151 155 FADFLIDFIE-RNKDQPFFAYYPMVLVHDPFVPTP--------------------------------------DSPDWDP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 252 KlltreemlKDTTNRLYQVYKRMpadvqdkwdsvyaqriseyrsgnlrgkeliswkyQQYMrdylativavDENIGRLLG 331
Cdd:cd16151 196 D--------DKRKKDDPEYFPDM----------------------------------VAYM----------DKLVGKLVD 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 332 YLEKNGELDNTIIIYTSDQGFFLGEHGWFD-------KRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMNVDFAPTLLDF 404
Cdd:cd16151 224 KLEELGLRENTIIIFTGDNGTHRPITSRTNgrevrggKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAEL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 405 AGVDIPADIQ--GQSLRTILEngGKTPADWRkaaYYHYYEYPAEHSVKRHYGIRTADFKLihfYNDvdeWEMYDLKNDPS 482
Cdd:cd16151 304 AGAPLPEDYPldGRSFAPQLL--GKTGSPRR---EWIYWYYRNPHKKFGSRFVRTKRYKL---YAD---GRFFDLREDPL 372
|
...
gi 949759693 483 ELN 485
Cdd:cd16151 373 EKN 375
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
29-516 |
1.61e-62 |
|
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: 211.86 E-value: 1.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFDGNQQT 108
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 109 FPKLLQAAGYQTSIVGKWHLITE--------PQGFD--YW----CILTGQHEQGDYY--NPDFNENGKQIVEQGYTTDVI 172
Cdd:cd16156 81 IGQRLSDNGIHTAYIGKWHLDGGdyfgngicPQGWDpdYWydmrNYLDELTEEERRKsrRGLTSLEAEGIKEEFTYGHRC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 173 TDKAIEYLEHRdKSKPFCMMYHQKAPHRNWMPAPRHLGMFNNTVFPEPATLFDTYEGRGSaaieqdmsiehtltndwdlk 252
Cdd:cd16156 161 TNRALDFIEKH-KDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAYDDLENKPL-------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 253 lltreemlkdttnrlyqvYKRMpadvqdkWdsvyaqriSEYRSGNLRGKELISWKYqqymrdYLATIVAVDENIGRLLGY 332
Cdd:cd16156 220 ------------------HQRL-------W--------AGAKPHEDGDKGTIKHPL------YFGCNSFVDYEIGRVLDA 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 333 LEKNGEldNTIIIYTSDQGFFLGEHGWFDK-RFMYEECQRMPLVIRYPKAIKAGSVSSAIAMNVDFAPTLLDFAGVDIPA 411
Cdd:cd16156 261 ADEIAE--DAWVIYTSDHGDMLGAHKLWAKgPAVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 412 DIQGQSLRTILENGGKTPadwRKAAYYHYYEYPAEHSvkrHYG-------IRTADFKLIhfYNDVDEWEMYDLKNDPSEL 484
Cdd:cd16156 339 VLEGESILATIEDPEIPE---NRGVFVEFGRYEVDHD---GFGgfqpvrcVVDGRYKLV--INLLSTDELYDLEKDPYEM 410
|
490 500 510
....*....|....*....|....*....|..
gi 949759693 485 NSVFGKPEYADKQAELISLLkkIQKQYKDDDP 516
Cdd:cd16156 411 HNLIDDPDYADVRDQLHDEL--LDYMNETRDP 440
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
25-514 |
8.24e-61 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 207.98 E-value: 8.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 25 EVKRPNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTG--KFSH-INGFTDNAST 101
Cdd:PRK13759 3 QTKKPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGlsQWHHgRVGYGDVVPW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 102 FDGNqqTFPKLLQAAGYQTSIVGKWHLITEPQ--GFDYWCILTGQHEQG------------DY----------YNPDF-- 155
Cdd:PRK13759 83 NYKN--TLPQEFRDAGYYTQCIGKMHVFPQRNllGFHNVLLHDGYLHSGrnedksqfdfvsDYlawlrekapgKDPDLtd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 156 ---NENGKQ-----IVEQGYTTDVITDKAIEYLEHRDKSKPFCMMYHQKAPHRNWMPAPRHLGMFNNTVFPEPATlfdty 227
Cdd:PRK13759 161 igwDCNSWVarpwdLEERLHPTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADIPDPHI----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 228 egrgsaaieqdmsiehtltNDWdlklltreemlkdttnrlyqvykrmpADVQDKWDSVYAQRISEyrsGNLrGKELIswk 307
Cdd:PRK13759 236 -------------------GDW--------------------------EYAEDQDPEGGSIDALR---GNL-GEEYA--- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 308 yQQYMRDYLATIVAVDENIGRLLGYLEKNGELDNTIIIYTSDQGFFLGEHGWFDKRFMYEECQRMPLVIRYPKAIKAGSV 387
Cdd:PRK13759 264 -RRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGNR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 388 SSAIAMNV---DFAPTLLDFAGVDIPADIQGQSLRTILEngGKTPAdWRKaaYYHyyeypAEHSV---KRHYgIRTADFK 461
Cdd:PRK13759 343 GTVIDQVVelrDIMPTLLDLAGGTIPDDVDGRSLKNLIF--GQYEG-WRP--YLH-----GEHALgysSDNY-LTDGKWK 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 949759693 462 LIHFYNDVDEwEMYDLKNDPSELNSVFGKPEYADK----QAELISLLKKIQKQYKDD 514
Cdd:PRK13759 412 YIWFSQTGEE-QLFDLKKDPHELHNLSPSEKYQPRlremRKKLVDHLRGREEGFVKD 467
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
29-481 |
1.11e-59 |
|
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: 200.50 E-value: 1.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFDGNQQT 108
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPADIPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 109 FPKLLQAAGYQTSIVGKWHLITEPQ--GFDYwciltgqheqgdyynpDfnengkqiveqgyttDVITDKAIEYL---EHR 183
Cdd:cd16032 81 FAHYLRAAGYRTALSGKMHFVGPDQlhGFDY----------------D---------------EEVAFKAVQKLydlARG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 184 DKSKPFCMMYHQKAPHrnwmpaprhlgmfnntvfpepatlfDTYegrgsaAIEQdmsiEHtltndWDLklltreemlkdt 263
Cdd:cd16032 130 EDGRPFFLTVSFTHPH-------------------------DPY------VIPQ----EY-----WDL------------ 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 264 tnrlyqvYkrmpadvqdkwdsVYAQRiseyrsgnlrgkeliswkyqqymRDYLATIVAVDENIGRLLGYLEKNGELDNTI 343
Cdd:cd16032 158 -------Y-------------VRRAR-----------------------RAYYGMVSYVDDKVGQLLDTLERTGLADDTI 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 344 IIYTSDQGFFLGEHG-WFdKRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMnVDFAPTLLDFAGV---DIPADIQGQSLR 419
Cdd:cd16032 195 VIFTSDHGDMLGERGlWY-KMSFFEGSARVPLIISAPGRFAPRRVAEPVSL-VDLLPTLVDLAGGgtaPHVPPLDGRSLL 272
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949759693 420 TILENGGktpADWRKAAyyhYYEYPAEHSVKRHYGIRTADFKLIHFYNDVDewEMYDLKNDP 481
Cdd:cd16032 273 PLLEGGD---SGGEDEV---ISEYLAEGAVAPCVMIRRGRWKFIYCPGDPD--QLFDLEADP 326
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
28-487 |
1.50e-58 |
|
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: 199.71 E-value: 1.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 28 RPNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFDG--- 104
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSkgg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 105 ---NQQTFPKLLQAAGYQTSIVGKWHLITEP------QGFDYWCILTGQHEQG--DYYNPD------FNENGKQIVE--- 164
Cdd:cd16026 81 lppDEITIAEVLKKAGYRTALVGKWHLGHQPeflptrHGFDEYFGIPYSNDMWpfPLYRNDppgplpPLMENEEVIEqpa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 165 -QGYTTDVITDKAIEYLEhRDKSKPFCMMYHQKAPHRNWMPAPRHLGMfnntvfpepatlfdtyEGRGsaaieqdmsieh 243
Cdd:cd16026 161 dQSSLTQRYTDEAVDFIE-RNKDQPFFLYLAHTMPHVPLFASEKFKGR----------------SGAG------------ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 244 tltndwdlklltreemlkdttnrLYqvykrmpADVqdkwdsvyaqrISEyrsgnlrgkeliswkyqqymrdylativaVD 323
Cdd:cd16026 212 -----------------------LY-------GDV-----------VEE-----------------------------LD 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 324 ENIGRLLGYLEKNGELDNTIIIYTSDQG------FFLGEHGWFD--KRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMNV 395
Cdd:cd16026 222 WSVGRILDALKELGLEENTLVIFTSDNGpwleygGHGGSAGPLRggKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTM 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 396 DFAPTLLDFAGVDIPAD--IQGQSLRTILENGGKTPAdwRKAAYYHYYEYPAehsvkrhyGIRTADFKLI--HFYNDV-- 469
Cdd:cd16026 302 DLLPTLAALAGAPLPEDrvIDGKDISPLLLGGSKSPP--HPFFYYYDGGDLQ--------AVRSGRWKLHlpTTYRTGtd 371
|
490 500
....*....|....*....|....*..
gi 949759693 470 ---------DEWEMYDLKNDPSELNSV 487
Cdd:cd16026 372 pggldptklEPPLLYDLEEDPGETYNV 398
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-419 |
5.44e-55 |
|
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: 186.21 E-value: 5.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTD----DHttqaMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGftDNASTFDG 104
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHG--VWGGPLEP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 105 NQQTFPKLLQAAGYQTSIVGKWHLITEPQGFDywciltgqheQG-DYYNPDFNENGKQIVEQGYTTDVITDKAIEYLEHR 183
Cdd:cd16148 75 DDPTLAEILRKAGYYTAAVSSNPHLFGGPGFD----------RGfDTFEDFRGQEGDPGEEGDERAERVTDRALEWLDRN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 184 DKSKPFCMMYHQKAPHrnwmpaprhlgmfnntvfpEPatlfdtyegrgsaaieqdmsiehtltndwdlklltreemlkdt 263
Cdd:cd16148 145 ADDDPFFLFLHYFDPH-------------------EP------------------------------------------- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 264 tnrlyqvykrmpadvqdkwdsvyaqriseYRsgnlrgkeliswkyqqymrdYLATIVAVDENIGRLLGYLEKNGELDNTI 343
Cdd:cd16148 163 -----------------------------YL--------------------YDAEVRYVDEQIGRLLDKLKELGLLEDTL 193
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949759693 344 IIYTSDQGFFLGEHGWFDK--RFMYEECQRMPLVIRYPKAiKAGSVSSAIAMNVDFAPTLLDFAGVDIPADIQGQSLR 419
Cdd:cd16148 194 VIVTSDHGEEFGEHGLYWGhgSNLYDEQLHVPLIIRWPGK-EPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLL 270
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-418 |
1.44e-54 |
|
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: 184.36 E-value: 1.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKF-----------SHINGFTD 97
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMpsqhgihdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 98 NASTFDGNQQTFPKLLQAAGYQTSIVGKWHLitepqgfdywciltgqheqGDyynpdfnengkqiveqgyttdvitDKAI 177
Cdd:cd16149 81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHL-------------------GD------------------------DAAD 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 178 EYLEHRDKSKPFCMMYHQKAPHRNWmpaprhlgmfnntvfpepatlfdtyegrgsaaieqdmsiehtltndwdlklltre 257
Cdd:cd16149 118 FLRRRAEAEKPFFLSVNYTAPHSPW------------------------------------------------------- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 258 emlkdttnrlyqvykrmpadvqdkwdsvyaqriseyrsgnlrgkeliswkyqqymrDYLATIVAVDENIGRLLGYLEKNG 337
Cdd:cd16149 143 --------------------------------------------------------GYFAAVTGVDRNVGRLLDELEELG 166
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 338 ELDNTIIIYTSDQGFFLGEHGWFDK-----RF-MYEECQRMPLVIRYPKAIKAGSVSSAIAMNVDFAPTLLDFAGVDIPA 411
Cdd:cd16149 167 LTENTLVIFTSDNGFNMGHHGIWGKgngtfPLnMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPA 246
|
....*....
gi 949759693 412 DIQ--GQSL 418
Cdd:cd16149 247 DPRlpGRSF 255
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
29-487 |
2.67e-53 |
|
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: 185.48 E-value: 2.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDhttqaM-----SCYGG-RFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSH------INGFT 96
Cdd:cd16143 1 PNIVIILADD-----LgygdiSCYNPdSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWrsrlkgGVLGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 97 DNASTFDGNQQTFPKLLQAAGYQTSIVGKWHLitepqGFDyWCILTGQHE-QGDYYNPDFNengKQI----VEQG----Y 167
Cdd:cd16143 76 FSPPLIEPDRVTLAKMLKQAGYRTAMVGKWHL-----GLD-WKKKDGKKAaTGTGKDVDYS---KPIkggpLDHGfdyyF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 168 TT------DVITDKAIEYL-EHRDKSKPFCMMYHQKAPHRNWMPAPRhlgmfnntvfpepatlfdtYEGRGSAaieqdms 240
Cdd:cd16143 147 GIpasevlPTLTDKAVEFIdQHAKKDKPFFLYFALPAPHTPIVPSPE-------------------FQGKSGA------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 241 iehtltndwdlklltreemlkdttnrlyqvykrmpadvqdkwdsvyaqriseyrsgNLRGkeliswkyqqymrDYlatIV 320
Cdd:cd16143 201 --------------------------------------------------------GPYG-------------DF---VY 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 321 AVDENIGRLLGYLEKNGELDNTIIIYTSDQGfflGEHGWFD-----------------KRFMYEECQRMPLVIRYPKAIK 383
Cdd:cd16143 209 ELDWVVGRILDALKELGLAENTLVIFTSDNG---PSPYADYkelekfghdpsgplrgmKADIYEGGHRVPFIVRWPGKIP 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 384 AGSVSSAIAMNVDFAPTLLDFAGVDIPADIQ--GQSLRTILenGGKTPADWRKAAYYhyyeypaeHSVKRHYGIRTADFK 461
Cdd:cd16143 286 AGSVSDQLVSLTDLFATLAAIVGQKLPDNAAedSFSFLPAL--LGPKKQEVRESLVH--------HSGNGSFAIRKGDWK 355
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 949759693 462 LIhFYNDVDEW--------------EMYDLKNDPSELNSV 487
Cdd:cd16143 356 LI-DGTGSGGFsyprgkeklglppgQLYNLSTDPGESNNL 394
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
409-513 |
2.33e-52 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 173.20 E-value: 2.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 409 IPADIQGQSLRTILEngGKTPADWRKAAYYHYYEYPAEHSVKRHYGIRTADFKLIHFYNDVDEWEMYDLKNDPSELNSVF 488
Cdd:pfam16347 1 IPADMQGKSFLPLLK--GKKPKNWRDALYYHYYEYPAEHAVKRHYGVRTERYKLIHFYNDIDEWELYDLQKDPKEMNNVY 78
|
90 100
....*....|....*....|....*
gi 949759693 489 GKPEYADKQAELISLLKKIQKQYKD 513
Cdd:pfam16347 79 GDPEYAEVQAELKEELEELRKQYKD 103
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-500 |
1.33e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 168.18 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFDGNQQT 108
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPDEPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 109 FPKLLQAAGYQTSIVGKWHLitepqgfdywciLTGQHEQGDYYNPDfnengkqiveqgyttDVITDKAIEYLEHRDKSKP 188
Cdd:cd16150 81 LLKTLKDAGYHVAWAGKNDD------------LPGEFAAEAYCDSD---------------EACVRTAIDWLRNRRPDKP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 189 FCMMYHQKAPHRNW-MPAPRHlGMFNNTVFPEPATLFDTYEGRGSAAIeqdmsiehtltndwdlklltreemlkdttNRL 267
Cdd:cd16150 134 FCLYLPLIFPHPPYgVEEPWF-SMIDREKLPPRRPPGLRAKGKPSMLE-----------------------------GIE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 268 YQVYKRMPadvQDKWDSVYAQriseyrsgnlrgkeliswkyqqymrdYLATIVAVDENIGRLLGYLEKNGELDNTIIIYT 347
Cdd:cd16150 184 KQGLDRWS---EERWRELRAT--------------------------YLGMVSRLDHQFGRLLEALKETGLYDDTAVFFF 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 348 SDQGFFLGEHGWFDK---RFmyEECQ-RMPLVIRYPKAIKaGSVSSAIAMNVDFAPTLLDFAGVDIPADIQGQSLRTILE 423
Cdd:cd16150 235 SDHGDYTGDYGLVEKwpnTF--EDCLtRVPLIIKPPGGPA-GGVSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLPVLA 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 424 NGGKTPadwRKAAY-------------------YHYY-------EYPAEHSvkRHYGIRTADFKLIHFYNDVDewEMYDL 477
Cdd:cd16150 312 GETEEH---RDAVFseggrlhgeeqamegghgpYDLKwprllqqEEPPEHT--KAVMIRTRRYKYVYRLYEPD--ELYDL 384
|
490 500
....*....|....*....|...
gi 949759693 478 KNDPSELNSVFGKPEYADKQAEL 500
Cdd:cd16150 385 EADPLELHNLIGDPAYAEIIAEM 407
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
29-407 |
2.23e-45 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 161.44 E-value: 2.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFDGN-QQ 107
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVGLPRtEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 108 TFPKLLQAAGYQTSIVGKWHLI------TEPQGFDYWCilTGQHEQGDYYNPDFNENgkQIVEQGYTTDVITDKAIEYLE 181
Cdd:pfam00884 81 SLPDLLKRAGYNTGAIGKWHLGwynnqsPCNLGFDKFF--GRNTGSDLYADPPDVPY--NCSGGGVSDEALLDEALEFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 182 HRDksKPFCMMYHQKAPHrnwmpaprhlgmfnntvfpepatlfdtyegrgsaaieqdmsiehtltndwdlklltreemlk 261
Cdd:pfam00884 157 NND--KPFFLVLHTLGSH-------------------------------------------------------------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 262 dttnrlyqvykrMPADVQDKWDSVYAQRISEYRSGNlrgkeliswkyqQYMRDYLATIVAVDENIGRLLGYLEKNGELDN 341
Cdd:pfam00884 173 ------------GPPYYPDRYPEKYATFKPSSCSEE------------QLLNSYDNTLLYTDDAIGRVLDKLEENGLLDN 228
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 342 TIIIYTSDQGFFLGEHG----WFDKRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMNVDFAPTLLDFAGV 407
Cdd:pfam00884 229 TLVVYTSDHGESLGEGGgylhGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
29-488 |
1.00e-42 |
|
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: 156.15 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGG---RFLQTPNMDRIANEGVRMDNCYAVNALSgPSRACILTGKFSHINGFTdnASTFDGN 105
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGgigRGAPTPNIDRLAKEGLRFTSFYVEPSCT-PGRAAFITGRHPIRTGLT--TVGLPGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 106 QQ-------TFPKLLQAAGYQTSIVGKWHLITEP------QGFDYWciltgqheqgdYYNPdfnengkqiveqgYTT--D 170
Cdd:cd16142 78 PGglppwepTLAELLKDAGYATAQFGKWHLGDEDgrlptdHGFDEF-----------YGNL-------------YHTidE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 171 VITDKAIEYLEHRDKS-KPFcMMYHqkaphrNWMPAprHlgmFNNTVFPEpatlfdtYEGRGSAAieqdmsiehtltndw 249
Cdd:cd16142 134 EIVDKAIDFIKRNAKAdKPF-FLYV------NFTKM--H---FPTLPSPE-------FEGKSSGK--------------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 250 dlklltreemlkdttnrlyqvykrmpadvqdkwdSVYAqriseyrsgnlrgkeliswkyqqymrdylATIVAVDENIGRL 329
Cdd:cd16142 180 ----------------------------------GKYA-----------------------------DSMVELDDHVGQI 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 330 LGYLEKNGELDNTIIIYTSDQG-----FFLGEHGWF--DKRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMNVDFAPTLL 402
Cdd:cd16142 197 LDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFrgEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLA 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 403 DFAGVDIPADIQGQSLRTI---------LENGGKTPADWrkaAYYHYYEYPAehsvkrhyGIRTADFKlIHFYNDVDEWE 473
Cdd:cd16142 277 ALAGAPDPKDKLLGKDRHIdgvdqspflLGKSEKSRRSE---FFYFGEGELG--------AVRWKNWK-VHFKAQEDTGG 344
|
490 500
....*....|....*....|....*...
gi 949759693 474 -------------MYDLKNDPSELNSVF 488
Cdd:cd16142 345 ptgepfyvltfplIFNLRRDPKERYDVT 372
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-443 |
2.90e-42 |
|
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: 153.52 E-value: 2.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHttQAMSCY--GGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNAS-----T 101
Cdd:cd16035 1 PNILLILTDQE--RYPPPWpaGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGspmqpL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 102 FDGNQQTFPKLLQAAGYQTSIVGKWHLITEPQGfdywciltgqheqgdyynpdfnengkqiveqGYTTD-VITDKAIEYL 180
Cdd:cd16035 79 LSPDVPTLGHMLRAAGYYTAYKGKWHLSGAAGG-------------------------------GYKRDpGIAAQAVEWL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 181 EHRDKS----KPFCMMYHQKAPHrnwmpaprhlgmfnntvfpepatlfdtyegrgsaaieqDMsiehtltndwdlklltr 256
Cdd:cd16035 128 RERGAKnadgKPWFLVVSLVNPH--------------------------------------DI----------------- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 257 eeMLkdttnrlyqvykrMPADvQDKWdsvyaqriseyrsgnlrgkeliswkyqQYMRD-YLATIVAVDENIGRLLGYLEK 335
Cdd:cd16035 153 --MF-------------PPDD-EERW---------------------------RRFRNfYYNLIRDVDRQIGRVLDALDA 189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 336 NGELDNTIIIYTSDQGFFLGEHGWFDKRF-MYEECQRMPLVIRYPKAIKAGSVSSAIAMNVDFAPTLLDFAGVDIPA--- 411
Cdd:cd16035 190 SGLADNTIVVFTSDHGEMGGAHGLRGKGFnAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEArat 269
|
410 420 430
....*....|....*....|....*....|....*
gi 949759693 412 ---DIQGQSLRTILENGGKTPAdwRKAAYYHYYEY 443
Cdd:cd16035 270 eapPLPGRDLSPLLTDADADAV--RDGILFTYDRY 302
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-483 |
2.71e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 149.81 E-value: 2.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFL--QTPNMDRIANEGVRMDNCYAVNALSgPSRACILTGKFSHINGFTDNASTFDGNQ 106
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFDNLWATPACS-PTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 107 QTFPKLL----QAAGYQTSIVGKWHL------ITEPQGFDYWC-ILTGQHEqgDYYNPDFNENGKQIVEQGYTTDVITDK 175
Cdd:cd16154 80 ETLLQLLikdaTTAGYSSAVIGKWHLggndnsPNNPGGIPYYAgILGGGVQ--DYYNWNLTNNGQTTNSTEYATTKLTNL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 176 AIEYLEhrDKSKPFCMMYHQKAPHrnwmpAPRHLgmfnntvfPePATLFDTYEGRGSAAIEQDmsiehtltndwdlkllt 255
Cdd:cd16154 158 AIDWID--QQTKPWFLWLAYNAPH-----TPFHL--------P-PAELHSRSLLGDSADIEAN----------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 256 reemlkdttNRLYqvykrmpadvqdkwdsvyaqriseyrsgnlrgkeliswkyqqymrdYLATIVAVDENIGRLLGYLEK 335
Cdd:cd16154 205 ---------PRPY----------------------------------------------YLAAIEAMDTEIGRLLASIDE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 336 NgELDNTIIIYTSDQG--------FFLGEHGwfdKRFMYEECQRMPLVIrYPKAI-KAGSVSSAIAMNVDFAPTLLDFAG 406
Cdd:cd16154 230 E-ERENTIIIFIGDNGtpgqvvdlPYTRNHA---KGSLYEGGINVPLIV-SGAGVeRANERESALVNATDLYATIAELAG 304
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949759693 407 VDIPADIQGQSLRTILENGGKTPADwrkaayYHYYEYpaEHSVKRHYGIRTADFKLIHFYNDVDewEMYDLKNDPSE 483
Cdd:cd16154 305 VDAAEIHDSVSFKPLLSDVNASTRQ------YNYTEY--ESPTTTGWATRNQYYKLIESENGQE--ELYDLINDPSE 371
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
29-485 |
1.91e-39 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 147.70 E-value: 1.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYaVNALSGPSRACILTGKFSHINGFTD---NASTFDG- 104
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYY-VQPICTPSRAALMTGRYPIHTGMQHgviLAGEPYGl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 105 --NQQTFPKLLQAAGYQTSIVGKWHL------ITEPQ-GFD----YWcilTGQ-----HEQG---DYYNPDFNENGKQIV 163
Cdd:cd16029 80 plNETLLPQYLKELGYATHLVGKWHLgfytweYTPTNrGFDsfygYY---GGAedyytHTSGganDYGNDDLRDNEEPAW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 164 EQG--YTTDVITDKAIEYLEHRDKSKPFCMMYHQKAPHrnwmpAPrhlgmfnntvFPEPATLFDTYEGRGSaaieqdmsi 241
Cdd:cd16029 157 DYNgtYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVH-----AP----------LQVPPEYADPYEDKFA--------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 242 ehtltNDWDlklltreemlkdtTNRlyqvykrmpadvqdkwdsvyaqriseyrsgnlrgkeliswkyqqymRDYLATIVA 321
Cdd:cd16029 213 -----HIKD-------------EDR----------------------------------------------RTYAAMVSA 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 322 VDENIGRLLGYLEKNGELDNTIIIYTSDQGfflGEHGWFD----------KRFMYEECQRMPLVIRYPK-AIKAGSVSSA 390
Cdd:cd16029 229 LDESVGNVVDALKAKGMLDNTLIVFTSDNG---GPTGGGDggsnyplrggKNTLWEGGVRVPAFVWSPLlPPKRGTVSDG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 391 IAMNVDFAPTLLDFAGVDIPA--DIQGQSLRTILENGGKTPadwRKAAYYHYYEYPaehSVKRHYGIRTADFKLIHFYNd 468
Cdd:cd16029 306 LMHVTDWLPTLLSLAGGDPDDlpPLDGVDQWDALSGGAPSP---RTEILLNIDDIT---RTTGGAAIRVGDWKLIVGKP- 378
|
490
....*....|....*..
gi 949759693 469 vdeweMYDLKNDPSELN 485
Cdd:cd16029 379 -----LFNIENDPCERN 390
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
28-486 |
2.60e-34 |
|
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: 135.88 E-value: 2.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 28 RPNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKF-------SHING----FT 96
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmaSSHGMrvilFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 97 DNASTFDGNQQTFPKLLQAAGYQTSIVGKWHL----------ITEP--QGFDYW--CILTGQHEQGDYYNPDF---NENG 159
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLglhcesrndfCHHPlnHGFDYFygLPLTNLKDCGDGSNGEYdlsFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 160 KQIVEQGYTTDVITDKAIEYLEHRDKSKPFCMMYHQKAPHRNWMPAPRHLGMFNNTVFpepatlfdtyegRGSAAIEQDM 239
Cdd:cd16159 161 FPLLTAFVLITALTIFLLLYLGAVSKRFFVFLLILSLLFISLFFLLLITNRYFNCILM------------RNHEVVEQPM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 240 SIEhTLTndwdlKLLTREemlkdtTNRLYQVYKRMPADVQDKWDSVYAqriSEYRSGNLRGKEliswKYQQYMrdylATI 319
Cdd:cd16159 229 SLE-NLT-----QRLTKE------AISFLERNKERPFLLVMSFLHVHT---ALFTSKKFKGRS----KHGRYG----DNV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 320 VAVDENIGRLLGYLEKNGELDNTIIIYTSDQGFFLGE-------HGWFD------KRFMYEECQRMPLVIRYPKAIKAGS 386
Cdd:cd16159 286 EEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLEEisvggeyGGGNGgiyggkKMGGWEGGIRVPTIVRWPGVIPPGS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 387 VSSAIAMNVDFAPTLLDFAGVDIPAD--IQGQSLRTILENGGK-TPADWrkaaYYHY---------YEYPAEHSV-KRHY 453
Cdd:cd16159 366 VIDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLLTGQEKrSPHEF----LFHYcgaelhavrYRPRDGGAVwKAHY 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 949759693 454 giRTADFK----------LIHFYND----VDEWEMYDLKNDPSELNS 486
Cdd:cd16159 442 --FTPNFYpgtegccgtlLCRCFGDsvthHDPPLLFDLSADPSESNP 486
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
28-425 |
9.32e-32 |
|
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: 127.58 E-value: 9.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 28 RPNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGF-TDNASTFDG-- 104
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFyTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 105 ----------NQQTFPKLLQAAGYQTSIVGKWHLITEPQ------GFDYWciltgqheqgdyynpdFnengkqiveqgyt 168
Cdd:cd16157 81 pqnivggipdSEILLPELLKKAGYRNKIVGKWHLGHRPQyhplkhGFDEW----------------F------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 169 tdvitdkaieylehrdkSKPFCmmyhqkaphrnwmpaprHLGMFNNTVFPE-PATLFDTYEGRgsaaIEQDMSIEHTlTN 247
Cdd:cd16157 132 -----------------GAPNC-----------------HFGPYDNKAYPNiPVYRDWEMIGR----YYEEFKIDKK-TG 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 248 DWDLKLLTREEMLKDTTNrlyQVYKRMPADVQDKWDS----VYAQRisEYRSGNLRGKeliswkyqqymrdYLATIVAVD 323
Cdd:cd16157 173 ESNLTQIYLQEALEFIEK---QHDAQKPFFLYWAPDAthapVYASK--PFLGTSQRGL-------------YGDAVMELD 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 324 ENIGRLLGYLEKNGELDNTIIIYTSDQGFFL-------GEHGWF--DKRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMN 394
Cdd:cd16157 235 SSVGKILESLKSLGIENNTFVFFSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSL 314
|
410 420 430
....*....|....*....|....*....|...
gi 949759693 395 VDFAPTLLDFAGVDIPAD--IQGQSLRTILENG 425
Cdd:cd16157 315 MDLFTTSLALAGLPIPSDraIDGIDLLPVLLNG 347
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
29-511 |
1.17e-31 |
|
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: 127.56 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHING-----FTDNAS-TF 102
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGvypgvFYPGSRgGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 103 DGNQQTFPKLLQAAGYQTSIVGKWHL--------ITEPQGFDYWCILTGQHEQGDYYNpdfnengkqiveqgyttdvitd 174
Cdd:cd16158 82 PLNETTIAEVLKTVGYQTAMVGKWHLgvglngtyLPTHQGFDHYLGIPYSHDQGPCQN---------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 175 kaIEYLEHRDKSKPFCMMYHQKAPhrnwmpaprhlgMFNNTVFPE-PATLFDTYEGRGSAAieqdmsiehtltndwdlKL 253
Cdd:cd16158 140 --LTCFPPNIPCFGGCDQGEVPCP------------LFYNESIVQqPVDLLTLEERYAKFA-----------------KD 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 254 LTREEMLKDTTNRLYQVYKRmpadvqdkwdSVYAQRISE-YRSGNLRGKeliswkyqqyMRDYLATIvavDENIGRLLGY 332
Cdd:cd16158 189 FIADNAKEGKPFFLYYASHH----------THYPQFAGQkFAGRSSRGP----------FGDALAEL---DGSVGELLQT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 333 LEKNGELDNTIIIYTSDQGFFL------GEHGWFD--KRFMYEECQRMPLVIRYPKAIKAGsVSSAIAMNVDFAPTLLDF 404
Cdd:cd16158 246 LKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcgKGTTYEGGVREPAIAYWPGRIKPG-VTHELASTLDILPTIAKL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 405 AGVDIP-ADIQGQSLRTILENGGKTPADwrkaAYYHYYEYPAEhsVKRHYGIRTADFKlIHFY----------NDVD--- 470
Cdd:cd16158 325 AGAPLPnVTLDGVDMSPILFEQGKSPRQ----TFFYYPTSPDP--DKGVFAVRWGKYK-AHFYtqgaahsgttPDKDchp 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 949759693 471 ----EWE----MYDLKNDPSELNSVFGKPEYAdkqaeliSLLKKIQKQY 511
Cdd:cd16158 398 saelTSHdpplLFDLSQDPSENYNLLGLPEYN-------QVLKQIQQVK 439
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-418 |
7.04e-29 |
|
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: 115.55 E-value: 7.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 28 RPNIIFMMTDDHTTQAMSCYGG----------RFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTD 97
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 98 NASTfdgNQQ------TFPKLLQAAGYQTSIVGKWHLitepqgfdywciltgqheqgdyynpdfnengkqiveqgyttdv 171
Cdd:cd16153 81 FEAA---HPAldhglpTFPEVLKKAGYQTASFGKSHL------------------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 172 itDKAIEYLEHRDKSkpFCMMYHQKAphrnWMPAPR-----HLGMfnntVFPepatlfdtyegrgsaaieqdmsieHTlt 246
Cdd:cd16153 115 --EAFQRYLKNANQS--YKSFWGKIA----KGADSDkpffvRLSF----LQP------------------------HT-- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 247 ndwdlklltreemlkdttnrlyqvykrmPADVQDKWDSVYaqriseyrsgnlrgkeliswkyqqymrDYLATIVAVDENI 326
Cdd:cd16153 157 ----------------------------PVLPPKEFRDRF---------------------------DYYAFCAYGDAQV 181
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 327 GRLLGYLEKNGEL---DNTIIIYTSDQGFFLGEHGWFDKRFMYEECQRMPLVIRYPKAIK--AGSVSSAIAMNVDFAPTL 401
Cdd:cd16153 182 GRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGILAKFTFWPQSHRVPLIVVSSDKLKapAGKVRHDFVEFVDLAPTL 261
|
410
....*....|....*....
gi 949759693 402 LDFAGVDI--PADIQGQSL 418
Cdd:cd16153 262 LAAAGVDVdaPDYLDGRDL 280
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
28-475 |
1.13e-24 |
|
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: 106.75 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 28 RPNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGF--------TDNA 99
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggtrvflPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 100 STFDGNQQTFPKLLQAAGYQTSIVGKWHL-ITE---------P--QGFDY----------W-CILTGQHEQGDYYNPDFN 156
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLgINEnnhsdgahlPshHGFDFvgtnlpftnsWaCDDTGRHVDFPDRSACFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 157 ENGKQIVEQ----GYTTDVITDKAIEYLEHRDKsKPFCMmyhqkaphrnWMPAPR-HLGMFNNTVFpepatlfdtyegRG 231
Cdd:cd16160 161 YYNDTIVEQpiqhEHLTETLVGDAKSFIEDNQE-NPFFL----------YFSFPQtHTPLFASKRF------------KG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 232 SAaieqdmsiehtltndwdlklltreemlkdttnrlyqvyKRmpadvqdkwdSVYAQRISEyrsgnlrgkelISWKyqqy 311
Cdd:cd16160 218 KS--------------------------------------KR----------GRYGDNINE-----------MSWA---- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 312 mrdylativavdenIGRLLGYLEKNGELDNTIIIYTSDQGFFL------GEHGWFD--KRFMYEECQRMPLVIRYPKAIK 383
Cdd:cd16160 235 --------------VGEVLDTLVDTGLDQNTLVFFLSDHGPHVeyclegGSTGGLKggKGNSWEGGIRVPFIAYWPGTIK 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 384 AGsVSSAIAMNVDFAPTLLDFAGVDIPAD--IQGQSLRTILENGGKTPADwrkAAYYHYyeypaehsVKRHYGIRTADFK 461
Cdd:cd16160 301 PR-VSHEVVSTMDIFPTFVDLAGGTLPTDriYDGLSITDLLLGEADSPHD---DILYYC--------CSRLMAVRYGSYK 368
|
490
....*....|....
gi 949759693 462 lIHFYNDVDEWEMY 475
Cdd:cd16160 369 -IHFKTQPLPSQES 381
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
54-483 |
4.42e-23 |
|
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: 101.01 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 54 TPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDN-ASTFDG----NQQTFPKLLQAAGYQTSIVGKWHL 128
Cdd:cd16161 28 TPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNfLPTSVGglplNETTLAEVLRQAGYATGMIGKWHL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 129 ----ITEP--QGFDYwciltgqheqgdYYNPDFNENGKqiveqgyTTDVITDKAIEYLE-HRDKSKPFcMMYhqkaphrn 201
Cdd:cd16161 108 gqreAYLPnsRGFDY------------YFGIPFSHDSS-------LADRYAQFATDFIQrASAKDRPF-FLY-------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 202 wmpaprhlgmfnntvfpepatlfdtyegrgsaaieqdMSIEHTLTNDwdlklltreemlkdttnrlyQVYKRMPAdvqdk 281
Cdd:cd16161 160 -------------------------------------AALAHVHVPL--------------------ANLPRFQS----- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 282 wdsvyaqriseyrSGNLRGKeliswkyqqymrdYLATIVAVDENIGRLLGYLEKNGELDNTIIIYTSDQG---------- 351
Cdd:cd16161 178 -------------PTSGRGP-------------YGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcelav 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 352 -----FFLGEHGWFD-KRFMYEECQRMPLVIRYPKAIKAGSVSSAIAMNVDFAPTLLDFAGVDIPAD--IQGQSLRTILE 423
Cdd:cd16161 232 gpgtgDWQGNLGGSVaKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVLF 311
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949759693 424 NGGKTPADwrkaAYYHYYEypAEHSVKRHYGIRTADFKLiHFYN------DVDEWE--------MYDLKNDPSE 483
Cdd:cd16161 312 GGSKTGHR----CLFHPNS--GAAGAGALSAVRCGDYKA-HYATggalacCGSTGPklyhdpplLFDLEVDPAE 378
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
29-482 |
2.25e-17 |
|
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: 83.74 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 29 PNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYAVNALSGPSRACILTGKFSHINGFTDNASTFDGNQQT 108
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPNYPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 109 FPKLLQAAGYQTSIVGKwhlitepqgFDYwciLTGQHEQGDYynpdfnengkqiVEqGYTTDVitdkaieylehrdkskP 188
Cdd:cd16171 81 WMDRLEKHGYHTQKYGK---------LDY---TSGHHSVSNR------------VE-AWTRDV----------------P 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 189 FCMmyhqkaphrnwmpaprhlgmfnntvfpepatlfdTYEGRGSAAIEQDMSIEHTLTNDWDLKLLTREEMLKDTTNRLY 268
Cdd:cd16171 120 FLL----------------------------------RQEGRPTVNLVGDRSTVRVMLKDWQNTDKAVHWIRKEAPNLTQ 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 269 QVYKRMPADVQDKWDSVYA-------QRISEYrsgnlrgkeliswkyqqymrdYLATIVAVDENIGRLLGYLEKNGELDN 341
Cdd:cd16171 166 PFALYLGLNLPHPYPSPSMgenfgsiRNIRAF---------------------YYAMCAETDAMLGEIISALKDTGLLDK 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 342 TIIIYTSDQGFFLGEHGWFDKRFMYEECQRMPLVIRYPKaIKAGSVSSAIAMNVDFAPTLLDFAGVDIPADIQGQSLRTI 421
Cdd:cd16171 225 TYVFFTSDHGELAMEHRQFYKMSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPL 303
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 422 LENGGKTPA-------DWrkaAYYHYYEYPAEHSVkrhYGIRTADFKLIHfYNDVDEW--EMYDLKNDPS 482
Cdd:cd16171 304 LSESSIKESpsrvphpDW---VLSEFHGCNVNAST---YMLRTNSWKYIA-YADGNSVppQLFDLSKDPD 366
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
54-406 |
5.33e-13 |
|
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: 69.63 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 54 TPNMDRIANEGVRMDNCYAVNALSGPSRA--CILTGKFSHINGFTDNASTFDGNQQTFPKLLQAAGYQTSIV-------G 124
Cdd:cd16015 26 TPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLNPLPSLPSILKEQGYETIFIhggdasfY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 125 KWHLITEPQGFDywciltgqheqgDYYNP-DFNENGKQIVEQGYTTDVITDKAIEYLEHRDKsKPFcmmyhqkaphrnwm 203
Cdd:cd16015 106 NRDSVYPNLGFD------------EFYDLeDFPDDEKETNGWGVSDESLFDQALEELEELKK-KPF-------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 204 paprhlgmFNNTVfpepatlfdtyegrgsaaieqdmsiehTLTNdwdlklltreemlkdttnrlyqvykRMPADVQDKWD 283
Cdd:cd16015 159 --------FIFLV---------------------------TMSN-------------------------HGPYDLPEEKK 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 284 svyaqriseyrsgnlrGKELISWKYQQYMRDYLATIVAVDENIGRLLGYLEKNGELDNTIIIYTSDQGFFLGEHGWFDKR 363
Cdd:cd16015 179 ----------------DEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDE 242
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 949759693 364 FMYEEcQRMPLVIRYPKAIKAGSVSSAIAMNvDFAPTLLDFAG 406
Cdd:cd16015 243 DPLDL-YRTPLLIYSPGLKKPKKIDRVGSQI-DIAPTLLDLLG 283
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
315-403 |
3.63e-12 |
|
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: 66.29 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 315 YLATIVAVDENIGRLLGYLEKNGELDNTIIIYTSDQGFFLGEHGWFDK------RFMYEEcqRMPLVIRYPKAiKAGSVS 388
Cdd:cd00016 144 YYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKadgkadKSHTGM--RVPFIAYGPGV-KKGGVK 220
|
90
....*....|....*
gi 949759693 389 SAIAMNVDFAPTLLD 403
Cdd:cd00016 221 HELISQYDIAPTLAD 235
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
27-418 |
1.95e-11 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 66.60 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 27 KRPNIIFMMTDDHTTQAMSCYGGRFLQTPNMDRIANEGVRMDNCYA-----VNALSGpsracILTGkFShingFTDNAST 101
Cdd:COG1368 233 KKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSqggrtSRGEFA-----VLTG-LP----PLPGGSP 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 102 F----DGNQQTFPKLLQAAGYQTSIV----GKW---HLITEPQGFDYwciltgQHEQGDYYNPDFNENGkqiveqgYTTD 170
Cdd:COG1368 303 YkrpgQNNFPSLPSILKKQGYETSFFhggdGSFwnrDSFYKNLGFDE------FYDREDFDDPFDGGWG-------VSDE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 171 VITDKAIEYLEHRDKskPFcmmyhqkaphrnwmpaprhlgmFNNTVfpepatlfdtyegrgsaaieqdmsiehTLTN--D 248
Cdd:COG1368 370 DLFDKALEELEKLKK--PF----------------------FAFLI---------------------------TLSNhgP 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 249 WDLklltreemlkdttnrlyqvykrmPADvqdkwdsvyAQRISEYRSGNLRgkeliswkyqqymrDYLATIVAVDENIGR 328
Cdd:COG1368 399 YTL-----------------------PEE---------DKKIPDYGKTTLN--------------NYLNAVRYADQALGE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 329 LLGYLEKNGELDNTIIIYTSDQGFFLGEHGWFDKRFMYeecQRMPLVIRYPKaIKAGSVSSAIAMNVDFAPTLLDFAGVD 408
Cdd:COG1368 433 FIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENPLER---YRVPLLIYSPG-LKKPKVIDTVGSQIDIAPTLLDLLGID 508
|
410
....*....|.
gi 949759693 409 IPADIQ-GQSL 418
Cdd:COG1368 509 YPSYYAfGRDL 519
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
309-439 |
1.44e-09 |
|
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: 60.69 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 309 QQYMRDYLATIVAVDENIGRLLGYLEKNGELDNTIIIYTSDQGFFLGEHG---WFDKRFMYEECQRMPLVIRYPKAiKAG 385
Cdd:COG3083 423 TPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGqnyWGHNSNFSRYQLQVPLVIHWPGT-PPQ 501
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 949759693 386 SVSSaIAMNVDFAPTLL-DFAGVDIPAD--IQGQSLrtiLENGGKTP----ADWRKAAYYH 439
Cdd:COG3083 502 VISK-LTSHLDIVPTLMqRLLGVQNPASdySQGEDL---FDPQRRRDwvlaGDYRNLAIIT 558
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
317-403 |
1.62e-06 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 49.51 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 317 ATIVAVDENIGRLLGYLEKNGELDNTIIIYTSDQGFF-LGEHGWF-DKRFMYeecqrmPLVIRYPKAIKAGSVSSAIaMN 394
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHGYDnELPDMR------AIFIARGPAFKKGKKLGPF-RN 255
|
....*....
gi 949759693 395 VDFAPTLLD 403
Cdd:cd16018 256 VDIYPLMCN 264
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
313-383 |
2.60e-06 |
|
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 49.06 E-value: 2.60e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 949759693 313 RDYLATIVAVDENIGRLLGYLEKNGELDNTIIIYTSDQGFFLGEhgwFDKRF--MYEEcqRMP-LVIRYPKAIK 383
Cdd:cd16021 176 HDYLNGLSLADEDLLEFLKRLKENGLLDNTFVIFMSDHGLRFGK---IRETLqgKLEE--RLPfLSISLPKWFR 244
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
286-408 |
1.06e-04 |
|
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: 44.15 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 286 YAQRI-SEYRSGNLRGKELISWKYQQYMRD-YLATIVAVDENIGRLLGYLEKNGEldNTIIIYTSDQGFFLGE-----HG 358
Cdd:cd16017 157 YYDRYpEEFAKFTPDCDNELQSCSKEELINaYDNSILYTDYVLSQIIERLKKKDK--DAALIYFSDHGESLGEnglylHG 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 949759693 359 WFDK-RFMYEecqrMPLVI--------RYPKAIKAGSVSSAIaMNVDFAPTLLDFAGVD 408
Cdd:cd16017 235 APYApKEQYH----VPFIIwssdsykqRYPVERLRANKDRPF-SHDNLFHTLLGLLGIK 288
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
50-98 |
1.20e-04 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 44.33 E-value: 1.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 949759693 50 RFLQTPNMDRIANEGVRMDNCYAV-NALSGPSRACILTGKFSHINGFTDN 98
Cdd:pfam01663 16 RFELTPNLAALAKEGVSAPNLTPVfPTLTFPNHYTLVTGLYPGSHGIVGN 65
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
314-384 |
2.34e-03 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 40.41 E-value: 2.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 949759693 314 DYLATIVAVDENIGRLLGYLEKNGELDNTIIIYTSDQGFFLGEHgwfdKRF---MYEEcqRMPL-VIRYPKAIKA 384
Cdd:pfam02995 305 DDFNYASALDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKL----RRTsqgMLEE--RLPLmSIRYPPWFRE 373
|
|
| AP-SPAP |
cd16016 |
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
318-369 |
2.85e-03 |
|
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: 40.21 E-value: 2.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 949759693 318 TIVAVDENIGRLLGYLEKNGELDNTIIIYTSDQGF-----FLGEHGWFDKRFMYEEC 369
Cdd:cd16016 234 TYLRLDRDLARLLDALDKKVGKGNYLVFLTADHGAadnpeFLKDHKIPAGRFDPKRL 290
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
314-418 |
4.48e-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: 39.71 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949759693 314 DYLATIVA---VDENIGRLLGYLEKNGeldNTIIIyTSDqgfflgeHGWFDKrfMYEECQ----------RMPLVIRYPK 380
Cdd:cd16010 401 NLEAAVKAveaVDECLGRIVEAVLENG---GTLLI-TAD-------HGNAEE--MIDPETggphtahttnPVPFIIVDPG 467
|
90 100 110
....*....|....*....|....*....|....*...
gi 949759693 381 AIKAGSVSSAIAmnvDFAPTLLDFAGVDIPADIQGQSL 418
Cdd:cd16010 468 LKRKLLKDGGLA---DVAPTILDLLGIEKPKEMTGKSL 502
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
315-352 |
6.86e-03 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 38.96 E-value: 6.86e-03
10 20 30
....*....|....*....|....*....|....*...
gi 949759693 315 YLATIVAVDENIGRLLGYLEKNGELDNTIIIYTSDQGF 352
Cdd:COG1524 207 YRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGM 244
|
|
| |
