|
Name |
Accession |
Description |
Interval |
E-value |
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
30-438 |
0e+00 |
|
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: 539.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSMSPVLF-PNSTKG 108
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGpPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 109 LHPDEVTIADMLSEAGYATTCIGKWHLGHLPPCLPTYQGFDSYYGIPYSNDMWidPanrladdlvlregvtiEQLKTGQK 188
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMW--P----------------FPLYRNDP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 189 LKNRVPLMLDEEVIEYPVDQSTVTKRYTERAVHYIQEQKDRPFFIYLPHTMVHVPLAVSDAFKNRTGELIW-DAIEEVDW 267
Cdd:cd16026 143 PGPLPPLMENEEVIEQPADQSSLTQRYTDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYgDVVEELDW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 268 SVGQILQALKDNKIDEKTLVIFTSDNGAAV------GSSLPLRAKKGSVYDGGIREPTVMRWPSQIPAGTICHEVSASID 341
Cdd:cd16026 223 SVGRILDALKELGLEENTLVIFTSDNGPWLeygghgGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 342 ILPTLSHLCNGKLPS-RQIDGRNIWPLMNGQPNaaSPHNT---YCLAHGPGTVRSGQWKYYPWKEGQSGRRKQNSTaiSD 417
Cdd:cd16026 303 LLPTLAALAGAPLPEdRVIDGKDISPLLLGGSK--SPPHPffyYYDGGDLQAVRSGRWKLHLPTTYRTGTDPGGLD--PT 378
|
410 420
....*....|....*....|.
gi 1712519934 418 PQSEVQLYDTVNDIGETKNVA 438
Cdd:cd16026 379 KLEPPLLYDLEEDPGETYNVA 399
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-451 |
1.14e-123 |
|
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: 373.03 E-value: 1.14e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSM------------- 97
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGItdvipgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 98 SPVLFPNSTKGLHPDEVTIADMLSEAGYATTCIGKWHLGHLPPCLPTYQGFDSYY-----GIPYSNDmwiDPANRLADDL 172
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIggtgnGGPPSYY---FPPGKPNPDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 173 vlregvtiEQLKTGQKLknrvplmldeevieypvdqstvTKRYTERAVHYIQEQKDRPFFIYLPHTMVHVPLAVSDAF-- 250
Cdd:cd16144 158 --------EDGPEGEYL----------------------TDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELie 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 251 -----KNRTGELIWDA-----IEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVG------SSLPLRAKKGSVYDGG 314
Cdd:cd16144 208 kyekkKKGLRKGQKNPvyaamIESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTrggpptSNAPLRGGKGSLYEGG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 315 IREPTVMRWPSQIPAGTICHEVSASIDILPTLSHLCNGKLPSRQ-IDGRNIWPLMNGQPNAA--------SPHNTYCLAH 385
Cdd:cd16144 288 IRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQhLDGVSLVPLLKGGEADLprralfwhFPHYHGQGGR 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712519934 386 GPGTVRSGQWKYYPWKEGQsgrrkqnstaisdpqsEVQLYDTVNDIGETKNVAAHYPEVVSRLQKA 451
Cdd:cd16144 368 PASAIRKGDWKLIEFYEDG----------------RVELYNLKNDIGETNNLAAEMPEKAAELKKK 417
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-461 |
3.19e-116 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 353.03 E-value: 3.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 1 MARKLVALLFTccfvlqsFADPPAKTTSVQPNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCS 80
Cdd:COG3119 1 MKRLLLLLLAL-------LAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 81 GSRTALMTGTHYQRLSMSPVlFPNSTKGLHPDEVTIADMLSEAGYATTCIGKWHLghlppclptyqgfdsyygipysndm 160
Cdd:COG3119 74 PSRASLLTGRYPHRTGVTDN-GEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 161 widpanrladdlvlregvtieqlktgqklknrvplmldeevieypvdqsTVTKRYTERAVHYIQEQ--KDRPFFIYLPHT 238
Cdd:COG3119 128 -------------------------------------------------YLTDLLTDKAIDFLERQadKDKPFFLYLAFN 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 239 MVHVPLAVSDAFKNR-TGELI-----------------------WDAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNG 294
Cdd:COG3119 159 APHAPYQAPEEYLDKyDGKDIplppnlaprdlteeelrraraayAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNG 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 295 AAVGSSLpLRAKKGSVYDGGIREPTVMRWPSQIPAGTICHEVSASIDILPTLSHLCNGKLPSrQIDGRNIWPLMNGQPNA 374
Cdd:COG3119 239 PSLGEHG-LRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPE-DLDGRSLLPLLTGEKAE 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 375 ASPHNTYCLAHGPG--TVRSGQWKYYPWKegqsgrrkqnstaisDPQSEVQLYDTVNDIGETKNVAAHYPEVVSRLQKAW 452
Cdd:COG3119 317 WRDYLYWEYPRGGGnrAIRTGRWKLIRYY---------------DDDGPWELYDLKNDPGETNNLAADYPEVVAELRALL 381
|
....*....
gi 1712519934 453 EEHLVELNA 461
Cdd:COG3119 382 EAWLKELGD 390
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
31-454 |
4.22e-112 |
|
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: 342.99 E-value: 4.22e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVgCAVCSGSRTALMTGTHYQRLSMSPVLFPNSTkgLH 110
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHV-SPVCAPTRAALLTGRYPFRTGVWHTILGRER--MR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 111 PDEVTIADMLSEAGYATTCIGKWHLGHLPPCLPTYQGFDSYYGIPYSndmWI----DPANRLADDLVLREGVTIEQlktg 186
Cdd:cd16146 78 LDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGG---GIgqypDYWGNDYFDDTYYHNGKFVK---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 187 qklknrvplmldeevieypvDQSTVTKRYTERAVHYIQEQKDRPFFIYLPHTMVHVPLAVSDAFKNR---TGELIWDA-- 261
Cdd:cd16146 151 --------------------TEGYCTDVFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYLDPykdMGLDDKLAaf 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 262 ---IEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVGSSLP----LRAKKGSVYDGGIREPTVMRWPSQIPAGTICH 334
Cdd:cd16146 211 ygmIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRfnagMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 335 EVSASIDILPTLSHLCNGKLP-SRQIDGRNIWPLMNGqPNAASPHNTYcLAHgpgtvrSGQWKYYPWKEGQSGRRKQNST 413
Cdd:cd16146 291 TLTAHIDLLPTLLDLCGVKLPeGIKLDGRSLLPLLKG-ESDPWPERTL-FTH------SGRWPPPPKKKRNAAVRTGRWR 362
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1712519934 414 AISDPQSEVQLYDTVNDIGETKNVAAHYPEVVSRLQKAWEE 454
Cdd:cd16146 363 LVSPKGFQPELYDIENDPGEENDVADEHPEVVKRLKAAYEA 403
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-442 |
8.90e-104 |
|
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: 321.47 E-value: 8.90e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRlsmSPVLFPNSTKG-- 108
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGH---TRVRGNSEPGGqd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 109 -LHPDEVTIADMLSEAGYATTCIGKWHLG-HLPPCLPTYQGFDSYYGIP--------YSNDMWidpanrladdlvlREGV 178
Cdd:cd16145 78 pLPPDDVTLAEVLKKAGYATAAFGKWGLGgPGTPGHPTKQGFDYFYGYLdqvhahnyYPEYLW-------------RNGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 179 TIEqlktgqkLKNRVPLMLDEEVIEYPVDQSTVTKRYTERAVHYIQEQKDRPFFIYLPHTMVHVPLAVSDA--------F 250
Cdd:cd16145 145 KVP-------LPNNVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDDgpykykpkD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 251 KNRTGELIWD--------AIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAV-----------GSSLPLRAKKGSVY 311
Cdd:cd16145 218 PGIYAYLPWPqpekayaaMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdpdffDSNGPLRGYKRSLY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 312 DGGIREPTVMRWPSQIPAGTICHEVSASIDILPTLSHLCNGKLPSRqIDGRNIWPLMNGQPNAASPHNTYCLAHGPGT-- 389
Cdd:cd16145 298 EGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPED-IDGISLLPTLLGKPQQQQHDYLYWEFYEGGGaq 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1712519934 390 -VRSGQWKYYpwkegqsgRRKQNstaisdpQSEVQLYDTVNDIGETKNVAAHYP 442
Cdd:cd16145 377 aVRMGGWKAV--------RHGKK-------DGPFELYDLSTDPGETNNLAAQHP 415
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-438 |
1.26e-102 |
|
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: 317.99 E-value: 1.26e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGP-RTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSMSP-VLFPNSTKG 108
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGgVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 109 LHPDEVTIADMLSEAGYATTCIGKWHLG-------------HLPPCL---------PTYQGFDSYYGIPysndmwidpan 166
Cdd:cd16143 81 IEPDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkaatGTGKDVdyskpikggPLDHGFDYYFGIP----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 167 rladdlvlregvtieqlktgqklknrvplmldeevieypvdQSTVTKRYTERAVHYIQEQ--KDRPFFIYLPHTMVHVPL 244
Cdd:cd16143 150 -----------------------------------------ASEVLPTLTDKAVEFIDQHakKDKPFFLYFALPAPHTPI 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 245 AVSDAFKNRTGELIW-DAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVG------------SSLPLRAKKGSVY 311
Cdd:cd16143 189 VPSPEFQGKSGAGPYgDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPYadykelekfghdPSGPLRGMKADIY 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 312 DGGIREPTVMRWPSQIPAGTICHEVSASIDILPTLSHLCNGKLP-SRQIDGRNIWPLMNGQPNAASPHNTYCLAHGPG-T 389
Cdd:cd16143 269 EGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPdNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGSfA 348
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1712519934 390 VRSGQWKYYPwkEGQSGRRKQNSTAISDPQSEVQLYDTVNDIGETKNVA 438
Cdd:cd16143 349 IRKGDWKLID--GTGSGGFSYPRGKEKLGLPPGQLYNLSTDPGESNNLY 395
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
30-459 |
2.87e-98 |
|
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: 310.76 E-value: 2.87e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSMSPV------LFP 103
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASShgmrviLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 104 NSTKGLHPDEVTIADMLSEAGYATTCIGKWHLG-----------HlppclPTYQGFDSYYGIPYSN------------DM 160
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGlhcesrndfchH-----PLNHGFDYFYGLPLTNlkdcgdgsngeyDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 161 WIDPANRLADDLVLREGVTIEQLKTGQKLKNRVP---------------------------LMLDEEVIEYPVDQSTVTK 213
Cdd:cd16159 156 SFDPLFPLLTAFVLITALTIFLLLYLGAVSKRFFvfllilsllfislfflllitnryfnciLMRNHEVVEQPMSLENLTQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 214 RYTERAVHYIQEQKDRPFFIYLPHTMVHVPLAVSDAFKNRTGELIW-DAIEEVDWSVGQILQALKDNKIDEKTLVIFTSD 292
Cdd:cd16159 236 RLTKEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYgDNVEEMDWSVGQILDALDELGLKDNTFVYFTSD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 293 NGAAV-----------GSSLPLRAKKGSVYDGGIREPTVMRWPSQIPAGTICHEVSASIDILPTLSHLCNGKLPS-RQID 360
Cdd:cd16159 316 NGGHLeeisvggeyggGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSdRIID 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 361 GRNIWPLMNGQpNAASPHN---TYCLAHGPG---TVRSGQ--WK-------YYPWKEGQSGR---RKQNSTAIS-DPQse 421
Cdd:cd16159 396 GRDLMPLLTGQ-EKRSPHEflfHYCGAELHAvryRPRDGGavWKahyftpnFYPGTEGCCGTllcRCFGDSVTHhDPP-- 472
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1712519934 422 vQLYDTVNDIGETKNVAA---HYPEVVSRLQKAWEEHLVEL 459
Cdd:cd16159 473 -LLFDLSADPSESNPLDPtdePYQEIIKKILEAVAEHQSSI 512
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
31-482 |
1.39e-97 |
|
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: 307.83 E-value: 1.39e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSMSP-VLFPNSTKGL 109
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPgVFYPGSRGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 110 HPDEVTIADMLSEAGYATTCIGKWHLGHLP--PCLPTYQGFDSYYGIPYSND------MWIDPANRLADDLVlregvtie 181
Cdd:cd16158 82 PLNETTIAEVLKTVGYQTAMVGKWHLGVGLngTYLPTHQGFDHYLGIPYSHDqgpcqnLTCFPPNIPCFGGC-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 182 qlKTGQKLknrVPLMLDEEVIEYPVDQSTVTKRYTERAVHYIQE--QKDRPFFIYLPHTMVHVPLAVSDAFKNRTGELIW 259
Cdd:cd16158 154 --DQGEVP---CPLFYNESIVQQPVDLLTLEERYAKFAKDFIADnaKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 260 -DAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAV------GSSLPLRAKKGSVYDGGIREPTVMRWPSQIPAGtI 332
Cdd:cd16158 229 gDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPG-V 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 333 CHEVSASIDILPTLSHLCNGKLPSRQIDGRNIWPLMNGQpnAASPHNTYCL-------AHGPGTVRSGQWK--YYPWKEG 403
Cdd:cd16158 308 THELASTLDILPTIAKLAGAPLPNVTLDGVDMSPILFEQ--GKSPRQTFFYyptspdpDKGVFAVRWGKYKahFYTQGAA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 404 QSGRRKQNSTAISDPQSEVQ---LYDTVNDIGETKNV--AAHYPEVVSRLQKAWEEHLVELnanKRPTAELQRPEGSL-- 476
Cdd:cd16158 386 HSGTTPDKDCHPSAELTSHDpplLFDLSQDPSENYNLlgLPEYNQVLKQIQQVKERFEASM---KFGESEINKGEDPAle 462
|
....*.
gi 1712519934 477 PATRPG 482
Cdd:cd16158 463 PCCKPG 468
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-438 |
3.26e-96 |
|
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: 300.60 E-value: 3.26e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNG---AQGPRTPHLDQMAKEGMQFRDFYVGcAVCSGSRTALMTGTHYQRLSMSPVLFPNSTK 107
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVE-PSCTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 108 GLHPDEVTIADMLSEAGYATTCIGKWHLGHLPPCLPTYQGFDSYYGIPYSNdmwidpanrladdlvlregvtieqlktgq 187
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYHT----------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 188 klknrvplmLDEEVieypvdqstvtkryTERAVHYIQEQK--DRPFFIYLPHTMVHVPLAVSDAFKNR-TGELIW-DAIE 263
Cdd:cd16142 131 ---------IDEEI--------------VDKAIDFIKRNAkaDKPFFLYVNFTKMHFPTLPSPEFEGKsSGKGKYaDSMV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 264 EVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAV-----GSSLPLRAKKGSVYDGGIREPTVMRWPSQIPAGTICHEVSA 338
Cdd:cd16142 188 ELDDHVGQILDALDELGIADNTIVIFTTDNGPEQdvwpdGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVS 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 339 SIDILPTLSHLCNGKLPS-------RQIDGRNIWPLMNGQpNAASPHNT--YCLAHGPGTVRSGQWKYYP-WKEGQSGRR 408
Cdd:cd16142 268 HLDWFPTLAALAGAPDPKdkllgkdRHIDGVDQSPFLLGK-SEKSRRSEffYFGEGELGAVRWKNWKVHFkAQEDTGGPT 346
|
410 420 430
....*....|....*....|....*....|
gi 1712519934 409 KQNSTAISDPqsevQLYDTVNDIGETKNVA 438
Cdd:cd16142 347 GEPFYVLTFP----LIFNLRRDPKERYDVT 372
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
30-435 |
3.46e-96 |
|
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: 300.93 E-value: 3.46e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDMGFGDVGFNGAQGPR-TPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSMSPVLFPNSTKG 108
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 109 LHPDEVTIADMLSEAGYATTCIGKWHLGHLPPCLPTYQGFDSYYGIPYSNDmwidpanrladdlvlregvtieqlktgqk 188
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 189 lknrvplmldeevieypvdqSTVTKRYTERAVHYIQE--QKDRPFFIYLPHTMVHVPLAVSDAFKNRTGE--LIWDAIEE 264
Cdd:cd16161 132 --------------------SSLADRYAQFATDFIQRasAKDRPFFLYAALAHVHVPLANLPRFQSPTSGrgPYGDALQE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 265 VDWSVGQILQALKDNKIDEKTLVIFTSDNGA-------AVG-------SSLPLRAKKGSVYDGGIREPTVMRWPSQIPAG 330
Cdd:cd16161 192 MDDLVGQIMDAVKHAGLKDNTLTWFTSDNGPwevkcelAVGpgtgdwqGNLGGSVAKASTWEGGHREPAIVYWPGRIPAN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 331 TICHEVSASIDILPTLSHLCNGKLPS-RQIDGRNIWPLMNGQpnAASPHNtyCLAH---------GPGTVRSGQWKYYpW 400
Cdd:cd16161 272 STSAALVSTLDIFPTVVALAGASLPPgRIYDGKDLSPVLFGG--SKTGHR--CLFHpnsgaagagALSAVRCGDYKAH-Y 346
|
410 420 430
....*....|....*....|....*....|....*
gi 1712519934 401 KEGqSGRRKQNSTAISDPQSEVQLYDTVNDIGETK 435
Cdd:cd16161 347 ATG-GALACCGSTGPKLYHDPPLLFDLEVDPAESF 380
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
31-438 |
9.60e-84 |
|
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: 268.65 E-value: 9.60e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCaVCSGSRTALMTGTHYQRLSM-SPVLFPNSTKGL 109
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGRYPIHTGMqHGVILAGEPYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 110 HPDEVTIADMLSEAGYATTCIGKWHLGHL-PPCLPTYQGFDSYYGipY---SNDMW---IDPANRLADDlVLREGVTIEQ 182
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYtWEYTPTNRGFDSFYG--YyggAEDYYthtSGGANDYGND-DLRDNEEPAW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 183 LKTGQklknrvplmldeevieYpvdqstVTKRYTERAVHYIQEQ-KDRPFFIYLPHTMVHVPLAVSDAFKNR---TGELI 258
Cdd:cd16029 157 DYNGT----------------Y------STDLFTDRAVDIIENHdPSKPLFLYLAFQAVHAPLQVPPEYADPyedKFAHI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 259 WD--------AIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAV-----GSSLPLRAKKGSVYDGGIREPTVMrWPS 325
Cdd:cd16029 215 KDedrrtyaaMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTgggdgGSNYPLRGGKNTLWEGGVRVPAFV-WSP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 326 QIP--AGTICHEVSASIDILPTLSHLCNGKLPS-RQIDGRNIWPLMNGqpNAASPHNT-------YCLAHGPGTVRSGQW 395
Cdd:cd16029 294 LLPpkRGTVSDGLMHVTDWLPTLLSLAGGDPDDlPPLDGVDQWDALSG--GAPSPRTEillniddITRTTGGAAIRVGDW 371
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1712519934 396 KYYpwkEGQsgrrkqnstaisdpqsevQLYDTVNDIGETKNVA 438
Cdd:cd16029 372 KLI---VGK------------------PLFNIENDPCERNDLA 393
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
30-396 |
2.67e-83 |
|
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: 269.30 E-value: 2.67e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSM-SP--VLFPNST 106
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyGGtrVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 107 KGLHPDEVTIADMLSEAGYATTCIGKWHLG----------HlppcLPTYQGFDsYYG--IPYSNDMWIDPANRLADDlvl 174
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennhsdgaH----LPSHHGFD-FVGtnLPFTNSWACDDTGRHVDF--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 175 regvtieqlktgqKLKNRVPLMLDEEVIEYPVDQSTVTKRYTERAVHYIQEQKDRPFFIYLPHTMVHVPLAVSDAFKNRT 254
Cdd:cd16160 153 -------------PDRSACFLYYNDTIVEQPIQHEHLTETLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 255 GELIW-DAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAV------GSSLPLRAKKGSVYDGGIREPTVMRWPSQI 327
Cdd:cd16160 220 KRGRYgDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVeyclegGSTGGLKGGKGNSWEGGIRVPFIAYWPGTI 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712519934 328 PAGtICHEVSASIDILPTLSHLCNGKLPS-RQIDGRNIWPLMngQPNAASPHNT---YCLAHgPGTVRSGQWK 396
Cdd:cd16160 300 KPR-VSHEVVSTMDIFPTFVDLAGGTLPTdRIYDGLSITDLL--LGEADSPHDDilyYCCSR-LMAVRYGSYK 368
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
31-363 |
1.82e-79 |
|
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: 251.97 E-value: 1.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSMspVLFPNSTKGLH 110
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGV--RGNVGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 111 PDEVTIADMLSEAGYATTCIGKWHlghlppclptyqgfdsyygipysndmwidpanrladdlvlregvtieqlktgqklk 190
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 191 nrvplmldeevieypvdqstvtkrytERAVHYIQEQ-KDRPFFIYLPHTMVHVPLAvsdafknrtgelIWDAIEEVDWSV 269
Cdd:cd16022 103 --------------------------DEAIDFIERRdKDKPFFLYVSFNAPHPPFA------------YYAMVSAIDDQI 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 270 GQILQALKDNKIDEKTLVIFTSDNGAAVGSSlPLRAKKGSVYDGGIREPTVMRWPSQIPAGTICHEVSASIDILPTLSHL 349
Cdd:cd16022 145 GRILDALEELGLLDNTLIVFTSDHGDMLGDH-GLRGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDL 223
|
330
....*....|....
gi 1712519934 350 CNGKLPsRQIDGRN 363
Cdd:cd16022 224 AGIEPP-EGLDGRS 236
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
30-459 |
1.15e-76 |
|
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: 252.39 E-value: 1.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTG-----------THYQRLSMS 98
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGrlpirngfyttNAHARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 99 PvlfPNSTKGLHPDEVTIADMLSEAGYATTCIGKWHLGHLPPCLPTYQGFDSYYGIPysNDMWIDPANrladdlvlregv 178
Cdd:cd16157 81 P---QNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAP--NCHFGPYDN------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 179 tieqlktgqKLKNRVPLMLDEEVI-----EYPVD----QSTVTKRYTERAVHYIQEQ--KDRPFFIYLPHTMVHVPLAVS 247
Cdd:cd16157 144 ---------KAYPNIPVYRDWEMIgryyeEFKIDkktgESNLTQIYLQEALEFIEKQhdAQKPFFLYWAPDATHAPVYAS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 248 DAF--KNRTGeLIWDAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAA-------VGSSLPLRAKKGSVYDGGIREP 318
Cdd:cd16157 215 KPFlgTSQRG-LYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAAlisapeqGGSNGPFLCGKQTTFEGGMREP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 319 TVMRWPSQIPAGTICHEVSASIDILPTLSHLCNGKLPS-RQIDGRNIWPLMNGQPNAASPHNTYcLAHGPGTVRSGQWK- 396
Cdd:cd16157 294 AIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSdRAIDGIDLLPVLLNGKEKDRPIFYY-RGDELMAVRLGQYKa 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712519934 397 -YYPWKEGQSGRRK-------QNSTAIS-----DPQSEVQLYDTVNDIGETKNV---AAHYPEVVSRLQKAWEEHLVEL 459
Cdd:cd16157 373 hFWTWSNSWEEFRKginfcpgQNVPGVTthnqtDHTKLPLLFHLGRDPGEKYPIsfkSAEYKQAMPRISKVVQQHQKTL 451
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
30-437 |
2.87e-72 |
|
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293749 [Multi-domain] Cd Length: 402 Bit Score: 238.88 E-value: 2.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDMGFGDVGFNGaqGP-RTPHLDQMAKEGMQFRDFYVgCAVCSGSRTALMTGTHYQRL---SMSPVL--FP 103
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFG--GEiPTPNLDALAAEGLRFTNFHT-TALCSPTRAALLTGRNHHQVgmgTMAELAtgKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 104 NSTKGLHPDEVTIADMLSEAGYATTCIGKWHLGHlppclptyqgfDSYYgipYSNDmwidpanrladdlvlregvtieql 183
Cdd:cd16025 79 GYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGP-----------DDYY---STDD------------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 184 ktgqklknrvplmldeevieypvdqstvtkrYTERAVHYIQEQK--DRPFFIYLPHTMVHVPLAVSDA----FKNR---- 253
Cdd:cd16025 121 -------------------------------LTDKAIEYIDEQKapDKPFFLYLAFGAPHAPLQAPKEwidkYKGKydag 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 254 --------------------------TGELI--WDA-------------------IEEVDWSVGQILQALKDNKIDEKTL 286
Cdd:cd16025 170 wdalreerlerqkelglipadtkltpRPPGVpaWDSlspeekklearrmevyaamVEHMDQQIGRLIDYLKELGELDNTL 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 287 VIFTSDNGA------AVGSSLPLRAKKGSVYDGGIREPTVMRWPSQIPA-GTICHEVSASIDILPTLSHLCNGKLPS--- 356
Cdd:cd16025 250 IIFLSDNGAsaepgwANASNTPFRLYKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHVIDIAPTILELAGVEYPKtvn 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 357 ----RQIDGRNIWPLMNGqPNAASPHNTYCLAH-GPGTVRSGQWK----YYPWKEGQsgrrkqnstaisdpqsEVQLYDT 427
Cdd:cd16025 330 gvpqLPLDGVSLLPTLDG-AAAPSRRRTQYFELfGNRAIRKGGWKavalHPPPGWGD----------------QWELYDL 392
|
490
....*....|
gi 1712519934 428 VNDIGETKNV 437
Cdd:cd16025 393 AKDPSETHDL 402
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-436 |
5.09e-65 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 219.01 E-value: 5.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYvGCAVCSGSRTALMTG----THYQRlsmspvlfpnsT 106
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAY-AQPLCTPSRVQLMTGkynfRNYVV-----------F 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 107 KGLHPDEVTIADMLSEAGYATtCI-GKWHLGHLPPCLPTYQ--GFDSYYgipysndMW-----IDPANRLAddLVLREGV 178
Cdd:cd16151 69 GYLDPKQKTFGHLLKDAGYAT-AIaGKWQLGGGRGDGDYPHefGFDEYC-------LWqltetGEKYSRPA--TPTFNIR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 179 TIEQLKTGQKlknrvplmldeeviEYPVDQstvtkrYTERAVHYIQEQKDRPFFIYLPHTMVHVPL----------AVSD 248
Cdd:cd16151 139 NGKLLETTEG--------------DYGPDL------FADFLIDFIERNKDQPFFAYYPMVLVHDPFvptpdspdwdPDDK 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 249 AFKNRTGELIwDAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNG-AAVGSSLP----LRAKKGSVYDGGIREPTVMRW 323
Cdd:cd16151 199 RKKDDPEYFP-DMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGtHRPITSRTngreVRGGKGKTTDAGTHVPLIVNW 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 324 PSQIPAGTICHEVSASIDILPTLSHLCNGKLPS-RQIDGRNIWPLMNGQPNAASPHNTYCLAHGPGT------VRSGQWK 396
Cdd:cd16151 278 PGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEdYPLDGRSFAPQLLGKTGSPRREWIYWYYRNPHKkfgsrfVRTKRYK 357
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1712519934 397 YYpwkegqsgrrkqnstaisdpqSEVQLYDTVNDIGETKN 436
Cdd:cd16151 358 LY---------------------ADGRFFDLREDPLEKNP 376
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
31-456 |
1.40e-64 |
|
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: 217.38 E-value: 1.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGpRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSMspvlFPNSTKG-- 108
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVV-KTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA----HGLRSRGfp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 109 LHPDEVTIADMLSEAGYATTCIGKWHLGhlPPclPTYQGFDSYYGIPYSNDMWIDPANRLADDLvlregvtiEQLKTGQk 188
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTHYN--PD--AVFPFDDEMRGPDDGGRNAWDYASNAADFL--------NRAKKGQ- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 189 lknrvPLMLdeeVIeypvdQSTVTKR--YTERAVHYIQEQKDRPFFIYLPHTmvhvPLAVSDAFKNrtgeliWDAIEEVD 266
Cdd:cd16027 143 -----PFFL---WF-----GFHDPHRpyPPGDGEEPGYDPEKVKVPPYLPDT----PEVREDLADY------YDEIERLD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 267 WSVGQILQALKDNKIDEKTLVIFTSDNGAAvgssLPlRAKkGSVYDGGIREPTVMRWPSQIPAGTICHE-VSaSIDILPT 345
Cdd:cd16027 200 QQVGEILDELEEDGLLDNTIVIFTSDHGMP----FP-RAK-GTLYDSGLRVPLIVRWPGKIKPGSVSDAlVS-FIDLAPT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 346 LSHLCNGKLPSrQIDGRNIWPLMNGQPnaaSPHNTYCLA----HGPG-----TVRSGQWKY----YPWkegqsgrrkqns 412
Cdd:cd16027 273 LLDLAGIEPPE-YLQGRSFLPLLKGEK---DPGRDYVFAerdrHDETydpirSVRTGRYKYirnyMPE------------ 336
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1712519934 413 taisdpqsevQLYDTVNDIGETKNVAAH--YPEVVSRLQKAWEEHL 456
Cdd:cd16027 337 ----------ELYDLKNDPDELNNLADDpeYAEVLEELRAALDAWM 372
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
31-349 |
1.99e-61 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 206.89 E-value: 1.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSMSpvlfPNSTKGLH 110
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSY----VSTPVGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 111 PDEVTIADMLSEAGYATTCIGKWHLGHLPPCLPTYQGFDSYYGIPYSNDMWIDPANRladdlvlregvtieqlktgqKLK 190
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDV--------------------PYN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 191 NRVPLMLDEevieypvdqstvtkRYTERAVHYIQeQKDRPFFIYLpHTM-VHVPLAVSDAFKNRTG-------------E 256
Cdd:pfam00884 137 CSGGGVSDE--------------ALLDEALEFLD-NNDKPFFLVL-HTLgSHGPPYYPDRYPEKYAtfkpsscseeqllN 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 257 LIWDAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVGSS-LPLRA-KKGSVYDGGIREPTVMRWPSQIPAGTICH 334
Cdd:pfam00884 201 SYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGgGYLHGgKYDNAPEGGYRVPLLIWSPGGKAKGQKSE 280
|
330
....*....|....*
gi 1712519934 335 EVSASIDILPTLSHL 349
Cdd:pfam00884 281 ALVSHVDLFPTILDL 295
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
30-454 |
2.28e-58 |
|
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: 202.76 E-value: 2.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRlsmSPVLFpNSTKGL 109
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHR---HGVTD-NNGPLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 110 HPDEVTIADMLSEAGYATTCIGKWHLGHLPPCLPTyqGFDSYYGIPYSNDMWiDPANRLADDLVLREGvtieqlktgqkl 189
Cdd:cd16031 78 DASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--GFDYWVSFPGQGSYY-DPEFIENGKRVGQKG------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 190 knrvplmldeevieYpvdqstVTKRYTERAVHYIQEQ-KDRPFFIYL----PH----------------TMVHVPLAVSD 248
Cdd:cd16031 143 --------------Y------VTDIITDKALDFLKERdKDKPFCLSLsfkaPHrpftpaprhrglyedvTIPEPETFDDD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 249 AFKNR-----------TGELIWD----------------AIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVGSsl 301
Cdd:cd16031 203 DYAGRpewareqrnriRGVLDGRfdtpekyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGE-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 302 plR--AKKGSVYDGGIREPTVMRWPSQIPAGTICHEVSASIDILPTLSHLCNGKLPSRqIDGRNIWPLMNGQPNAASPHN 379
Cdd:cd16031 281 --HglFDKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED-MQGRSLLPLLEGEKPVDWRKE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 380 TYC-------LAHGPGT--VRSGQWKY--YPwkegqsgrrkqnstaiSDPQSEvQLYDTVNDIGETKNVAAH--YPEVVS 446
Cdd:cd16031 358 FYYeyyeepnFHNVPTHegVRTERYKYiyYY----------------GVWDEE-ELYDLKKDPLELNNLANDpeYAEVLK 420
|
....*...
gi 1712519934 447 RLQKAWEE 454
Cdd:cd16031 421 ELRKRLEE 428
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-436 |
2.96e-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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 193.17 E-value: 2.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSMspvlFPNSTKgL 109
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGV----FGNDVP-L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 110 HPDEVTIADMLSEAGYATTCIGKWHLG-----------HLPPclPTY-QGFDSYYGipYSNdmWIDPANRLADDlvlreg 177
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGKWHLDgperndgraddYTPP--PERrHGFDYWKG--YEC--NHDHNNPHYYD------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 178 vtieqlktgqklknrvplmlDEEVIEYPvdqstvtKRY-----TERAVHYIQEQ--KDRPFFIYL----PHTMVH----- 241
Cdd:cd16034 144 --------------------DDGKRIYI-------KGYspdaeTDLAIEYLENQadKDKPFALVLswnpPHDPYTtapee 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 242 ---------------VPLAVSDAFKNRtgELIWD---AIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVGSSlpL 303
Cdd:cd16034 197 yldmydpkklllrpnVPEDKKEEAGLR--EDLRGyyaMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSH--G 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 304 RAKKGSVYDGGIREPTVMRWPSQIPAGTICHEVSASIDILPTLSHLCNGKLPSrQIDGRNIWPLMNGQPNaASPHNTYCL 383
Cdd:cd16034 273 LMNKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPD-TVEGRDLSPLLLGGKD-DEPDSVLLQ 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1712519934 384 AhgpgTVRSGQWKYYPWKEGQSGRRKQNSTAISDPQSEVqLYDTVNDIGETKN 436
Cdd:cd16034 351 C----FVPFGGGSARDGGEWRGVRTDRYTYVRDKNGPWL-LFDNEKDPYQLNN 398
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-454 |
2.44e-48 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 174.72 E-value: 2.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGthyQRLSMSPVL-----FPNS 105
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTG---LYPHEHGVLnnvenAGAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 106 TKGLHPDEVTIADMLSEAGYATTCIGKWHLGhlPPCLPTYQGFDSYygipysndmwidpanrladdlvlregvtieqlkt 185
Cdd:cd16033 78 SRGLPPGVETFSEDLREAGYRNGYVGKWHVG--PEETPLDYGFDEY---------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 186 gqklknrvplmLDEEvieypvdqSTVTKRYTERAVHYIQE--QKDRPFFIYL----PHTMVHVP---------------- 243
Cdd:cd16033 122 -----------LPVE--------TTIEYFLADRAIEMLEElaADDKPFFLRVnfwgPHDPYIPPepyldmydpediplpe 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 244 -------------------LAVSDAFKNRTGELI---WDAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVGSSl 301
Cdd:cd16033 183 sfaddfedkpyiyrrerkrWGVDTEDEEDWKEIIahyWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAH- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 302 PLRAKKGSVYDGGIREPTVMRWPSQIPAGTICHEVSASIDILPTLSHLCnGKLPSRQIDGRNIWPLMNGQPNAASPHNTY 381
Cdd:cd16033 262 RLWDKGPFMYEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLA-GVDVPPKVDGRSLLPLLRGEQPEDWRDEVV 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 382 CLAHGPGT------VRSGQWKYypwkegqsgrrkqnstaISDPQSEVQLYDTVNDIGETKNVAAH--YPEVVSRLQKA-W 452
Cdd:cd16033 341 TEYNGHEFylpqrmVRTDRYKY-----------------VFNGFDIDELYDLESDPYELNNLIDDpeYEEILREMRTRlY 403
|
..
gi 1712519934 453 EE 454
Cdd:cd16033 404 EW 405
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-450 |
8.16e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 161.19 E-value: 8.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYV-GC---AVCSGSRTALMTGTHYQRLSMSPvlfPNS 105
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNmGGwsgAVCVPSRAMLMTGRTLFHAPEGG---KAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 106 TKglhPDEVTIADMLSEAGYATTCIGKWHLGHlppclptyqgfdsyygipysndmwidpanrlADDlvlregvtieqlkt 185
Cdd:cd16155 79 IP---SDDKTWPETFKKAGYRTFATGKWHNGF-------------------------------ADA-------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 186 gqklknrvplmldeevieypvdqstvtkryterAVHYIQEQK--DRPFFIYLPHTMVHVPLAVSDAF------------K 251
Cdd:cd16155 111 ---------------------------------AIEFLEEYKdgDKPFFMYVAFTAPHDPRQAPPEYldmyppetiplpE 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 252 N-----------------------RTGELI-------WDAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVGSSl 301
Cdd:cd16155 158 NflpqhpfdngegtvrdeqlapfpRTPEAVrqhlaeyYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSH- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 302 PLRAKKgSVYDGGIREPTVMRWPSqIPAGTICHEVSASIDILPTLSHLCNGKLPSRqIDGRNIWPLMNGQPNAASPHNTY 381
Cdd:cd16155 237 GLMGKQ-NLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES-VEGKSLLPVIRGEKKAVRDTLYG 313
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712519934 382 CLAHGPGTVRSGQWKYYpWKEGQSGRrkqnstaisdpqseVQLYDTVNDIGETKNVAAHyPEVVSRLQK 450
Cdd:cd16155 314 AYRDGQRAIRDDRWKLI-IYVPGVKR--------------TQLFDLKKDPDELNNLADE-PEYQERLKK 366
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-398 |
1.33e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 141.96 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSMSPVLFPNSTKGLH 110
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 111 PDEVTIADMLSEAGYATTCIGKWHLGHLppclpTYQGFDSyygipysndmwiDPanrladdlvlregvtieqlktgqklk 190
Cdd:cd16035 81 PDVPTLGHMLRAAGYYTAYKGKWHLSGA-----AGGGYKR------------DP-------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 191 nrvplmldeevieypvdqstvtkRYTERAVHYIQEQK-----DRPFFIYL----PHTMVHVPLAVSDAFKNRT--GELiw 259
Cdd:cd16035 118 -----------------------GIAAQAVEWLRERGaknadGKPWFLVVslvnPHDIMFPPDDEERWRRFRNfyYNL-- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 260 daIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVGSSLpLRAKKGSVYDGGIREPTVMRWPSQIPAGTICHEVSAS 339
Cdd:cd16035 173 --IRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHG-LRGKGFNAYEEALHVPLIISHPDLFGTGQTTDALTSH 249
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712519934 340 IDILPTLSHLCNGKLPSRQID-----GRNIWPLMNGQPNAA---SPHNTYclahgpgtvrsGQWKYY 398
Cdd:cd16035 250 IDLLPTLLGLAGVDAEARATEapplpGRDLSPLLTDADADAvrdGILFTY-----------DRYKFA 305
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-366 |
2.20e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 140.38 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFID----DMgfgdVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTH--YQRlsmsPVLFPn 104
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYpfYHG----VWGGP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 105 stkgLHPDEVTIADMLSEAGYATTCIGKWHLGHLPPCLptYQGFDSYYGIPYSNDMWIDPANRLADDLvlregvtieqlk 184
Cdd:cd16148 72 ----LEPDDPTLAEILRKAGYYTAAVSSNPHLFGGPGF--DRGFDTFEDFRGQEGDPGEEGDERAERV------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 185 tgqklknrvplmldeevieypvdqstvtkryTERAVHYIQEQK-DRPFFIYLpHTM-VHVPlavsDAFKNrtgeliwdAI 262
Cdd:cd16148 134 -------------------------------TDRALEWLDRNAdDDPFFLFL-HYFdPHEP----YLYDA--------EV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 263 EEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVGSSLPLRAKKGSVYDGGIREPTVMRWPSQIPAGTICHEVSaSIDI 342
Cdd:cd16148 170 RYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNLYDEQLHVPLIIRWPGKEPGKRVDALVS-HIDI 248
|
330 340
....*....|....*....|....
gi 1712519934 343 LPTLSHLCNGKLPSRqIDGRNIWP 366
Cdd:cd16148 249 APTLLDLLGVEPPDY-SDGRSLLP 271
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
30-456 |
4.19e-37 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 144.81 E-value: 4.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTG----TH----YQRlsMSPVL 101
Cdd:PRK13759 6 KPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGlsqwHHgrvgYGD--VVPWN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 102 FPNstkglhpdevTIADMLSEAGYATTCIGKWHLghlppcLPTYQ--GFDsyygipysndmwidpaNRLADDLVLREGVT 179
Cdd:PRK13759 84 YKN----------TLPQEFRDAGYYTQCIGKMHV------FPQRNllGFH----------------NVLLHDGYLHSGRN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 180 IEQLKTGQK------LKNRVPlMLDEEVIEYPVDQSTVTKR---YTER----------AVHYIQE-QKDRPFFIYL---- 235
Cdd:PRK13759 132 EDKSQFDFVsdylawLREKAP-GKDPDLTDIGWDCNSWVARpwdLEERlhptnwvgseSIEFLRRrDPTKPFFLKMsfar 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 236 PHTMVHVPLAVSDAFKNR------TGEliWDAIEE---------------------------------VDWSVGQILQAL 276
Cdd:PRK13759 211 PHSPYDPPKRYFDMYKDAdipdphIGD--WEYAEDqdpeggsidalrgnlgeeyarraraayyglithIDHQIGRFLQAL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 277 KDNKIDEKTLVIFTSDNGAAVGSSLPLRakKGSVYDGGIREPTVMRWPS---QIPAGTICHEVSASIDILPTLSHLCNGK 353
Cdd:PRK13759 289 KEFGLLDNTIILFVSDHGDMLGDHYLFR--KGYPYEGSAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 354 LPsRQIDGRNIWPLMNGQPNAASPHntYCLAHGPGT-----VRSGQWKYYPWKegQSGRRkqnstaisdpqsevQLYDTV 428
Cdd:PRK13759 367 IP-DDVDGRSLKNLIFGQYEGWRPY--LHGEHALGYssdnyLTDGKWKYIWFS--QTGEE--------------QLFDLK 427
|
490 500 510
....*....|....*....|....*....|
gi 1712519934 429 NDIGETKNVA--AHYPEVVSRLQKAWEEHL 456
Cdd:PRK13759 428 KDPHELHNLSpsEKYQPRLREMRKKLVDHL 457
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-346 |
6.77e-33 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 127.35 E-value: 6.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGT-------------HYQRLSM 97
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRmpsqhgihdwiveGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 98 SPVLFPnstkglhPDEVTIADMLSEAGYATTCIGKWHLGhlppclptyqgfdsyygipysndmwidpanrladdlvlreg 177
Cdd:cd16149 81 KPEGYL-------EGQTTLPEVLQDAGYRCGLSGKWHLG----------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 178 vtieqlktgqklknrvplmldeevieypvdqstvtkryTERAVHYI-QEQKDRPFFIYLPHTMVHVPlavsdafknrtge 256
Cdd:cd16149 113 --------------------------------------DDAADFLRrRAEAEKPFFLSVNYTAPHSP------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 257 liWD---AIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVG---------SSLPLrakkgSVYDGGIREPTVMRWP 324
Cdd:cd16149 142 --WGyfaAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGhhgiwgkgnGTFPL-----NMYDNSVKVPFIIRWP 214
|
330 340
....*....|....*....|..
gi 1712519934 325 SQIPAGTICHEVSASIDILPTL 346
Cdd:cd16149 215 GVVPAGRVVDSLVSAYDFFPTL 236
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
30-439 |
9.72e-33 |
|
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: 131.16 E-value: 9.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDMGfGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHyqrlsmspvlfPNSTK-- 107
Cdd:cd16030 2 KPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRR-----------PDTTGvy 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 108 -------GLHPDEVTIADMLSEAGYATTCIGK-WHlghlppclptyQGFDSYYGIPYSndmWIDPANRLADDlvLREGVT 179
Cdd:cd16030 70 dnnsyfrKVAPDAVTLPQYFKENGYTTAGVGKiFH-----------PGIPDGDDDPAS---WDEPPNPPGPE--KYPPGK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 180 IEQLKTGQKLKNRVPlmlDEEVIEYPvDQSTVTKRYTERAVHYIQEQKDR--PFF----IYLPHTMVHVP---------- 243
Cdd:cd16030 134 LCPGKKGGKGGGGGP---AWEAADVP-DEAYPDGKVADEAIEQLRKLKDSdkPFFlavgFYKPHLPFVAPkkyfdlyple 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 244 ---------------LAVSDAFKNRTGELIWD------------------------AIEEVDWSVGQILQALKDNKIDEK 284
Cdd:cd16030 210 siplpnpfdpidlpeVAWNDLDDLPKYGDIPAlnpgdpkgplpdeqarelrqayyaSVSYVDAQVGRVLDALEELGLADN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 285 TLVIFTSDNGAAVGsslplrAK----KGSVYDGGIREPTVMRWPSQIPAGTICHEVSASIDILPTLSHLCNGKLPSrQID 360
Cdd:cd16030 290 TIVVLWSDHGWHLG------EHghwgKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPP-CLE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 361 GRNIWPLMNGqPNAASPHNTYCLAHGPG----TVRSGQWKYYPWKEGQsgrrkqnstaisDPQSEvQLYDTVNDIGETKN 436
Cdd:cd16030 363 GKSLVPLLKN-PSAKWKDAAFSQYPRPSimgySIRTERYRYTEWVDFD------------KVGAE-ELYDHKNDPNEWKN 428
|
...
gi 1712519934 437 VAA 439
Cdd:cd16030 429 LAN 431
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
31-448 |
1.34e-32 |
|
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: 131.23 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGthyqRLSMSPVLFPNSTKgLH 110
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTG----RYLMNHRSVWNGTP-LD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 111 PDEVTIADMLSEAGYATTCIGKwhlghlppclptyqgfdsyygipysNDMWIDPANRLADDLVLRegvTIEQLKTGQklk 190
Cdd:cd16028 76 ARHLTLALELRKAGYDPALFGY-------------------------TDTSPDPRGLAPLDPRLL---SYELAMPGF--- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 191 nRVPLMLDEevieYPVDQSTvTKRYTERAVHYIQEQKDRPFFIYLPHTMVHVPLAVSD---------------------- 248
Cdd:cd16028 125 -DPVDRLDE----YPAEDSD-TAFLTDRAIEYLDERQDEPWFLHLSYIRPHPPFVAPApyhalydpadvpppiraeslaa 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 249 ---------AFKNRTGELIWDA-----------------------IEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAA 296
Cdd:cd16028 199 eaaqhpllaAFLERIESLSFSPgaanaadlddeevaqmratylglIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 297 VGSSLpLRAKKGsVYDGGIREPTVMRWPSQiPA----GTICHEVSASIDILPTLSHLCNGKLPSrQIDGRNIWPLMNGQP 372
Cdd:cd16028 279 LGDHW-LWGKDG-FFDQAYRVPLIVRDPRR-EAdatrGQVVDAFTESVDVMPTILDWLGGEIPH-QCDGRSLLPLLAGAQ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 373 NAA-------------------------SPHNtyCLAHgpgTVRSGQWKYYPWkegqsgrrkqnsTAIsDPqsevQLYDT 427
Cdd:cd16028 355 PSDwrdavhyeydfrdvstrrpqealglSPDE--CSLA---VIRDERWKYVHF------------AAL-PP----LLFDL 412
|
490 500
....*....|....*....|...
gi 1712519934 428 VNDIGETKNVAAH--YPEVVSRL 448
Cdd:cd16028 413 KNDPGELRDLAADpaYAAVVLRY 435
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-397 |
6.73e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 126.12 E-value: 6.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSmspvlFPNSTKGLH 110
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETG-----VWDNADPYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 111 PDEVTIADMLSEAGYATTCIGKWHlghlppclptYQGFDSYYGIPYsndmwidpanrladdlvlregvtieqlktgqklk 190
Cdd:cd16037 76 GDVPSWGHALRAAGYETVLIGKLH----------FRGEDQRHGFRY---------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 191 nrvplmlDEEVieypvdqstvtkryTERAVHYIQEQ--KDRPFFI----YLPHTMVHVPLAVSDAFKNRTGELIWDAIEE 264
Cdd:cd16037 112 -------DRDV--------------TEAAVDWLREEaaDDKPWFLfvgfVAPHFPLIAPQEFYDLYVRRARAAYYGLVEF 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 265 VDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVGSslplRA--KKGSVYDGGIREPTVMRWPSqIPAGTICHEVSASIDI 342
Cdd:cd16037 171 LDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGE----RGlwGKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDL 245
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712519934 343 LPTLSHLCNGKLPSRQiDGRNIWPLMNGqpNAASPHNTYC--LAHGPGT----VRSGQWKY 397
Cdd:cd16037 246 APTILEAAGAPPPPDL-DGRSLLPLAEG--PDDPDRVVFSeyHAHGSPSgafmLRKGRWKY 303
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
30-440 |
1.45e-31 |
|
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: 126.90 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDMgfgDVGFNGAQgPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTG--------THYQRLSMSPVL 101
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMD-PMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGqyahnhgvTNNSPPGGGYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 102 FpnSTKGLHPDevTIADMLSEAGYATTCIGKWHLGHLPPCLPTY--QGFDSYYGI--PYSNDMWIDPANRladdlvlreg 177
Cdd:cd16147 77 F--WQNGLERS--TLPVWLQEAGYRTAYAGKYLNGYGVPGGVSYvpPGWDEWDGLvgNSTYYNYTLSNGG---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 178 vtieqlktgqklkNRVPlmldeeVIEYPVDQST-VtkrYTERAVHYIQE--QKDRPFFIYLPHTMVHVPLAV----SDAF 250
Cdd:cd16147 143 -------------NGKH------GVSYPGDYLTdV---IANKALDFLRRaaADDKPFFLVVAPPAPHGPFTPapryANLF 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 251 KN----------------------RTGELIWDAIEE--------------VDWSVGQILQALKDNKIDEKTLVIFTSDNG 294
Cdd:cd16147 201 PNvtapprpppnnpdvsdkphwlrRLPPLNPTQIAYidelyrkrlrtlqsVDDLVERLVNTLEATGQLDNTYIIYTSDNG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 295 AAVGS-SLPLRakKGSVYDGGIREPTVMRWPSqIPAGTICHEVSASIDILPTLSHLCNGKLPSRqidgrniwplMNGQPN 373
Cdd:cd16147 281 YHLGQhRLPPG--KRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPSD----------MDGRSC 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712519934 374 AASPHNTY-CL-AHGPGTVrsgqWKYYPWKEGqsgrrkqnstaisdpqsEVQLYDTVNDIGETKNVAAH 440
Cdd:cd16147 348 GDSNNNTYkCVrTVDDTYN----LLYFEWCTG-----------------FRELYDLTTDPYQLTNLAGD 395
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-458 |
1.90e-31 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 126.19 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGthyqrlsmspvLFPNST--- 106
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTG-----------LYPTETgcf 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 107 ---KGLHPDEVTIADMLSEAGYATTCIGKWHLGhlppclptyqgfdsyygipysndmwidpanrladdlvlregvtieql 183
Cdd:cd16152 70 rngIPLPADEKTLAHYFRDAGYETGYVGKWHLA----------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 184 ktgqklknrvplmldeeviEYPVDQstvtkrYTERAVHYIQE-QKDRPFFIYLPHTMVH---------VPLAVSDAFKNR 253
Cdd:cd16152 103 -------------------GYRVDA------LTDFAIDYLDNrQKDKPFFLFLSYLEPHhqndrdryvAPEGSAERFANF 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 254 T--GELI-----WD--------AIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNgaavGSSLPLRAK--KGSVYDGGIR 316
Cdd:cd16152 158 WvpPDLAalpgdWAeelpdylgCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHFRTRNAeyKRSCHESSIR 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 317 EPTVMRWPSQIPAGTICHEVSAsIDILPTLSHLCNGKLPSrQIDGRNIWPLMNGQPnAASPHNTY----------CLahg 386
Cdd:cd16152 234 VPLVIYGPGFNGGGRVEELVSL-IDLPPTLLDAAGIDVPE-EMQGRSLLPLVDGKV-EDWRNEVFiqisesqvgrAI--- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 387 pgtvRSGQWKY-------YPWKEgqsgrrkqnstAISDPQSEVQLYDTVNDIGETKNVAAH--YPEVVSRLQKAWEEHLV 457
Cdd:cd16152 308 ----RTDRWKYsvaapdkDGWKD-----------SGSDVYVEDYLYDLEADPYELVNLIGRpeYREVAAELRERLLARMA 372
|
.
gi 1712519934 458 E 458
Cdd:cd16152 373 E 373
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
31-458 |
1.84e-30 |
|
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: 125.19 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGthyqrlsmspvLFPNSTKGLH 110
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTG-----------LYPHTNGSWT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 111 -----PDEV-TIADMLSEAGYATTCIGKWHL-GH----LPPClPtyQGFDSYYgipysndmWIDPANRLaDDLVLREgvt 179
Cdd:cd16156 70 ncmalGDNVkTIGQRLSDNGIHTAYIGKWHLdGGdyfgNGIC-P--QGWDPDY--------WYDMRNYL-DELTEEE--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 180 ieqlktgQKLKNRVPLMLDEEVIEypvDQSTVTKRYTERAVHYIQEQKDRPFFIYL----PHTMVHVPLAVSDAFKN--- 252
Cdd:cd16156 135 -------RRKSRRGLTSLEAEGIK---EEFTYGHRCTNRALDFIEKHKDEDFFLVVsydePHHPFLCPKPYASMYKDfef 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 253 RTGELIWDAIEE---------------------------------VDWSVGQILQALKDNKIDekTLVIFTSDNGAAVGS 299
Cdd:cd16156 205 PKGENAYDDLENkplhqrlwagakphedgdkgtikhplyfgcnsfVDYEIGRVLDAADEIAED--AWVIYTSDHGDMLGA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 300 SlPLRAKKGSVYDGGIREPTVMRWPSQIPAGTICHEVSASIDILPTLSHLCNGKLPsRQIDGRNIWPLMngQPNAASPHN 379
Cdd:cd16156 283 H-KLWAKGPAVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQP-KVLEGESILATI--EDPEIPENR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 380 TYCLAHGPGTVRSGQW-KYYPWKEGQSGRRKQNSTAISDPqsevQLYDTVNDIGETKNVAAH--YPEVVSRLQKAWEEHL 456
Cdd:cd16156 359 GVFVEFGRYEVDHDGFgGFQPVRCVVDGRYKLVINLLSTD----ELYDLEKDPYEMHNLIDDpdYADVRDQLHDELLDYM 434
|
..
gi 1712519934 457 VE 458
Cdd:cd16156 435 NE 436
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-434 |
7.38e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 121.69 E-value: 7.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFgDV--GFN-GAQGPRTPHLDQMAKEGMQFRDFYVGcAVCSGSRTALMTGTHYQRlsmSPVLFPNSTK 107
Cdd:cd16154 1 PNILLIIADDQGL-DSsaQYSlSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFR---TGVLAVPDEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 108 GLHPDEVTIADMLSE--AGYATTCIGKWHLGHLPPCLPTYQGFDSYYGI------PYSNdmWidpanrladDLVLREGVT 179
Cdd:cd16154 76 LLSEETLLQLLIKDAttAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGIlgggvqDYYN--W---------NLTNNGQTT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 180 ieqlktgqklknrvplmldeEVIEYpvdqstVTKRYTERAVHYIQEQkDRPFFIYLPHTMVHVPLAVSDAFKNRTGEL-- 257
Cdd:cd16154 145 --------------------NSTEY------ATTKLTNLAIDWIDQQ-TKPWFLWLAYNAPHTPFHLPPAELHSRSLLgd 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 258 ---IWD--------AIEEVDWSVGQILQALKDNKIdEKTLVIFTSDNG---AAVGSSLPLRAKKGSVYDGGIREP----- 318
Cdd:cd16154 198 sadIEAnprpyylaAIEAMDTEIGRLLASIDEEER-ENTIIIFIGDNGtpgQVVDLPYTRNHAKGSLYEGGINVPlivsg 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 319 -TVMRwpsqipAGTICHEVSASIDILPTLSHLCNGKLPSrQIDGRNIWPLMNGQPNAASPHNTYCLAHGPGTVRSGQWKY 397
Cdd:cd16154 277 aGVER------ANERESALVNATDLYATIAELAGVDAAE-IHDSVSFKPLLSDVNASTRQYNYTEYESPTTTGWATRNQY 349
|
410 420 430
....*....|....*....|....*....|....*..
gi 1712519934 398 YPWKEGQSGRRkqnstaisdpqsevQLYDTVNDIGET 434
Cdd:cd16154 350 YKLIESENGQE--------------ELYDLINDPSEQ 372
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
31-430 |
2.50e-29 |
|
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: 118.84 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGthyqRLSMSPVLFPNSTKgLH 110
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTG----RLPSRIGAYDNAAE-FP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 111 PDEVTIADMLSEAGYATTCIGKWHlghlppclptYQGFDSYYGIPYsndmwidpanrladdlvlregvtieqlktgqklk 190
Cdd:cd16032 76 ADIPTFAHYLRAAGYRTALSGKMH----------FVGPDQLHGFDY---------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 191 nrvplmlDEEVieypvdqstvtkryTERAVHYI----QEQKDRPFFIYLPHTMVHVPLAVSDAFknrtgeliWD------ 260
Cdd:cd16032 112 -------DEEV--------------AFKAVQKLydlaRGEDGRPFFLTVSFTHPHDPYVIPQEY--------WDlyvrra 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 261 ------AIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVGSslplRAK--KGSVYDGGIREPTVMRWPSQIPAGTI 332
Cdd:cd16032 163 rrayygMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGE----RGLwyKMSFFEGSARVPLIISAPGRFAPRRV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 333 CHEVSaSIDILPTLSHLCNGKLPS--RQIDGRNIWPLMNGQPNAASPH--NTYCL--AHGPG-TVRSGQWKYypwkegqs 405
Cdd:cd16032 239 AEPVS-LVDLLPTLVDLAGGGTAPhvPPLDGRSLLPLLEGGDSGGEDEviSEYLAegAVAPCvMIRRGRWKF-------- 309
|
410 420
....*....|....*....|....*
gi 1712519934 406 grrkqnstaISDPQSEVQLYDTVND 430
Cdd:cd16032 310 ---------IYCPGDPDQLFDLEAD 325
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-458 |
3.90e-28 |
|
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: 117.34 E-value: 3.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGthyqrlsmspvLFPnSTKG-- 108
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTG-----------WYP-HVNGhr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 109 -----LHPDEVTIADMLSEAGYATTCIGKwhlghlppclptyqgfdsyygipysNDMWidPANRLADDLVLRegvtieql 183
Cdd:cd16150 69 tlhhlLRPDEPNLLKTLKDAGYHVAWAGK-------------------------NDDL--PGEFAAEAYCDS-------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 184 ktgqklknrvplmlDEEVIEYpvdqstvtkryterAVHYIQE-QKDRPFFIYLPHTMVHVPLAVSDAF----------KN 252
Cdd:cd16150 114 --------------DEACVRT--------------AIDWLRNrRPDKPFCLYLPLIFPHPPYGVEEPWfsmidreklpPR 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 253 RTGELIWDA-------------------------------IEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVGS-S 300
Cdd:cd16150 166 RPPGLRAKGkpsmlegiekqgldrwseerwrelratylgmVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDyG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 301 LplrAKK--GSVYDGGIREPTVMRWPSQIPAGTICHEVSAsIDILPTLSHLCNGKLPSRQIdGRNIWPLMNGQPNAAS-- 376
Cdd:cd16150 246 L---VEKwpNTFEDCLTRVPLIIKPPGGPAGGVSDALVEL-VDIPPTLLDLAGIPLSHTHF-GRSLLPVLAGETEEHRda 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 377 --------PHNTYCLAHGPGtVRSGQWKYYPWKEGQSGR------RKQNSTAISDPQSEVQLYDTVNDIGETKNVA--AH 440
Cdd:cd16150 321 vfseggrlHGEEQAMEGGHG-PYDLKWPRLLQQEEPPEHtkavmiRTRRYKYVYRLYEPDELYDLEADPLELHNLIgdPA 399
|
490
....*....|....*...
gi 1712519934 441 YPEVVSRLQKAWEEHLVE 458
Cdd:cd16150 400 YAEIIAEMKQRLLRWMVE 417
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
31-349 |
1.62e-24 |
|
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: 102.50 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGcAVCSG--SRTALMTGTH-----YQRLSMSPVLFP 103
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVS-PPTSSapNHAALLTGAYptlhgYTGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 104 NSTKGLHPDEVTIADMLSEAGYATTCIGkwhlghlppclptyqgfdsyygipysndmwidpanrLADDLVlregvtieql 183
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG------------------------------------LLKAID---------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 184 ktgqklknrvplmldeevieypvdqstvtkryteravhyiQEQKDRPFFIYL----PHTMVHvplavsdAFKNRTGELIw 259
Cdd:cd00016 114 ----------------------------------------ETSKEKPFVLFLhfdgPDGPGH-------AYGPNTPEYY- 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 260 DAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVG--SSLPLRAKKGSVYDGGIREPTVMRWPSqIPAGTICHEVS 337
Cdd:cd00016 146 DAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKghGGDPKADGKADKSHTGMRVPFIAYGPG-VKKGGVKHELI 224
|
330
....*....|..
gi 1712519934 338 ASIDILPTLSHL 349
Cdd:cd00016 225 SQYDIAPTLADL 236
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
31-405 |
1.00e-22 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 100.31 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDDMGFGDVGFNGAQGPRTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQrLSMSPvlfpNSTKGLH 110
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTH-LTESW----NNYKGLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 111 PDEVTIADMLSEAGYATTCIGK--WHLGHlppclptyqgfdsyygipYSNDMWIDPANRLADDLVLREGVTIEQLkTGQK 188
Cdd:cd16171 76 PNYPTWMDRLEKHGYHTQKYGKldYTSGH------------------HSVSNRVEAWTRDVPFLLRQEGRPTVNL-VGDR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 189 LKNRVpLMLDEEVieypvdqstvtkryTERAVHYIQEQK---DRPFFIYLPHTMVHvPLAVSDAFKNRTG-----ELIWD 260
Cdd:cd16171 137 STVRV-MLKDWQN--------------TDKAVHWIRKEApnlTQPFALYLGLNLPH-PYPSPSMGENFGSirnirAFYYA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 261 AIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGaavgsSLPLRAK---KGSVYDGGIREPTVMRWPsQIPAGTICHEVS 337
Cdd:cd16171 201 MCAETDAMLGEIISALKDTGLLDKTYVFFTSDHG-----ELAMEHRqfyKMSMYEGSSHVPLLIMGP-GIKAGQQVSDVV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 338 ASIDILPTLSHLCNGKLPsRQIDGRNIWPLM----NGQPNAASPHNTYCLA--HGPGT------VRSGQWKYYPWKEGQS 405
Cdd:cd16171 275 SLVDIYPTMLDIAGVPQP-QNLSGYSLLPLLsessIKESPSRVPHPDWVLSefHGCNVnastymLRTNSWKYIAYADGNS 353
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
31-351 |
5.15e-18 |
|
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: 84.66 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 31 PNVIIIFIDdmGFGD---VGFNGAQGPrTPHLDQMAKEGMQFRDFYvgcAVCSGSRT-----ALMTGthyqrLSMSPVLF 102
Cdd:cd16015 1 PNVIVILLE--SFSDpyiDKDVGGEDL-TPNLNKLAKEGLYFGNFY---SPGFGGGTangefEVLTG-----LPPLPLGS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 103 PNSTKGLHPDEVTIADMLSEAGYATTCIgkwHLGH---------LPpclptYQGFDSYYGIpysNDMwidpanRLADDLV 173
Cdd:cd16015 70 GSYTLYKLNPLPSLPSILKEQGYETIFI---HGGDasfynrdsvYP-----NLGFDEFYDL---EDF------PDDEKET 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 174 LREGVTieqlktgqklknrvplmlDEEVieypvdqstvtkryTERAVHYIQEQKDRPFFIYLpHTMV-HVP--------- 243
Cdd:cd16015 133 NGWGVS------------------DESL--------------FDQALEELEELKKKPFFIFL-VTMSnHGPydlpeekkd 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 244 -LAVSDAFKNRTGELIwDAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVGSSLPLRAKKGSVYDggiREPTVMR 322
Cdd:cd16015 180 ePLKVEEDKTELENYL-NAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY---RTPLLIY 255
|
330 340
....*....|....*....|....*....
gi 1712519934 323 WPSQIPAGTIcHEVSASIDILPTLSHLCN 351
Cdd:cd16015 256 SPGLKKPKKI-DRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
14-371 |
7.49e-17 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 84.32 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 14 FVLQSFADPPAKTTSVQPNVIIIFIDdmGFGD--VGFNGAQGPRTPHLDQMAKEGMQFRDFYVgcavcSGSRT-----AL 86
Cdd:COG1368 218 YLKSNRPTPNPFGPAKKPNVVVILLE--SFSDffIGALGNGKDVTPFLDSLAKESLYFGNFYS-----QGGRTsrgefAV 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 87 MTGthyqrLSMSP---VLFPNSTKGLHpdevTIADMLSEAGYATTCIgkwHLGH---------LPpclptYQGFDSYYGI 154
Cdd:COG1368 291 LTG-----LPPLPggsPYKRPGQNNFP----SLPSILKKQGYETSFF---HGGDgsfwnrdsfYK-----NLGFDEFYDR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 155 pysNDMWIDPAN--RLADDLVLREgvTIEQLKTGQKlknrvplmldeevieypvdqstvtkryteravhyiqeqkdrPFF 232
Cdd:COG1368 354 ---EDFDDPFDGgwGVSDEDLFDK--ALEELEKLKK-----------------------------------------PFF 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 233 IYLpHTMV-HVPLAVSD------AFKNRTGELIWDAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAAVGSSLPLRA 305
Cdd:COG1368 388 AFL-ITLSnHGPYTLPEedkkipDYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYEN 466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712519934 306 KKGS------VYDGGIREPTVMrwpsqipagticHEVSASIDILPTLSHLCNGKLPSRQIDGRNI-------WPLMNGQ 371
Cdd:COG1368 467 PLERyrvpllIYSPGLKKPKVI------------DTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLlspdtdpFAFRNGG 533
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-364 |
9.18e-17 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 80.88 E-value: 9.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 30 QPNVIIIFIDDM------GFGDVGFNGAQGP----RTPHLDQMAKEGMQFRDFYVGCAVCSGSRTALMTGTHYQRLSMsp 99
Cdd:cd16153 1 KPNILWIITDDQrvdslsCYNNAHTGKSESRlgyvESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 100 VLFPNSTKGLHPDEVTIADMLSEAGYATTCIGKWHlghlppclptyqgfdsyygipysndmwIDPANRladdlvlregvt 179
Cdd:cd16153 79 YGFEAAHPALDHGLPTFPEVLKKAGYQTASFGKSH---------------------------LEAFQR------------ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 180 ieqlktgqKLKNrvplmldeeviEYPVDQSTVTKRYTERAvhyiqeqKDRPFFIYL----PHTMVHVPLAVSDAFknrtg 255
Cdd:cd16153 120 --------YLKN-----------ANQSYKSFWGKIAKGAD-------SDKPFFVRLsflqPHTPVLPPKEFRDRF----- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 256 eLIWDAIEEVDWSVGQILQALKD---NKIDEKTLVIFTSDNGAAVGSSlPLRAKKGSvYDGGIREPTVMRWPSQI--PAG 330
Cdd:cd16153 169 -DYYAFCAYGDAQVGRAVEAFKAyslKQDRDYTIVYVTGDHGWHLGEQ-GILAKFTF-WPQSHRVPLIVVSSDKLkaPAG 245
|
330 340 350
....*....|....*....|....*....|....*
gi 1712519934 331 TICHEVSASIDILPTLSHLCNGKLPS-RQIDGRNI 364
Cdd:cd16153 246 KVRHDFVEFVDLAPTLLAAAGVDVDApDYLDGRDL 280
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
13-294 |
5.89e-10 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 61.69 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 13 CFVLQSFADPPAKTTSVQPNVIIIFIDdmGFG-DVgfngAQGPRTPHLDQMAKEGMQFRDFYvgCAVCSGSRTA---LMT 88
Cdd:COG1524 6 SLLLASLLAAAAAAAPPAKKVVLILVD--GLRaDL----LERAHAPNLAALAARGVYARPLT--SVFPSTTAPAhttLLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 89 GTH-----------YQR-LSMSPVLFPNSTKGLHPDEV----TIADMLSEAGYATTCIGKWHL-------GHLPPclpTY 145
Cdd:COG1524 78 GLYpgehgivgngwYDPeLGRVVNSLSWVEDGFGSNSLlpvpTIFERARAAGLTTAAVFWPSFegsglidAARPY---PY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 146 QGFDSYYGIPYSnDMWIdpanrladdlvlregvtieqlktgqklknrvplmldeevieypvdqstvtkryTERAVHYIQE 225
Cdd:COG1524 155 DGRKPLLGNPAA-DRWI-----------------------------------------------------AAAALELLRE 180
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1712519934 226 QKDRPFFIYLPHTmvhvplavsDAFKNRTG---ELIWDAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNG 294
Cdd:COG1524 181 GRPDLLLVYLPDL---------DYAGHRYGpdsPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| DUF4994 |
pfam16385 |
Domain of unknown function; This family around 100 residues locates in the C-terminal of some ... |
389-449 |
1.56e-09 |
|
Domain of unknown function; This family around 100 residues locates in the C-terminal of some uncharacterized proteins in various Bacteroides and Prevotella species. The function of this family remains unknown.
Pssm-ID: 406720 [Multi-domain] Cd Length: 98 Bit Score: 55.37 E-value: 1.56e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1712519934 389 TVRSGQWKYYpwkEGQSGRRKQNSTAISDPQS-EVQLYDTVNDIGETKNVAAHYPEVVSRLQ 449
Cdd:pfam16385 37 SVRTGDWKYI---EPSDGPAYIKWTKIETGNSpEPQLYDLKADPGEQENVAKKHPEKVKELQ 95
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
216-299 |
2.29e-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: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 216 TERAVHYIQE--QKDRPFFI--YLPHTmvhvplavsDAFKNRTG---ELIWDAIEEVDWSVGQILQALKDNKIDEKTLVI 288
Cdd:cd16018 141 FEERVDTILEwlDLERPDLIllYFEEP---------DSAGHKYGpdsPEVNEALKRVDRRLGYLIEALKERGLLDDTNII 211
|
90
....*....|..
gi 1712519934 289 FTSDNG-AAVGS 299
Cdd:cd16018 212 VVSDHGmTDVGT 223
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
33-296 |
5.59e-06 |
|
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: 48.96 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 33 VIIIFIDDMGFGDVGFNGaqgpRTPHLDQMAKEGMQFRdfYVGCAV----CSGsRTALMTG-----------THYQRLSM 97
Cdd:pfam01663 1 LLVISLDGFRADYLDRFE----LTPNLAALAKEGVSAP--NLTPVFptltFPN-HYTLVTGlypgshgivgnTFYDPKTG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 98 SPVLFPNSTKGLHP--DEVTIADMLSEAGYATTCIGkWhlghlPPCLPTYqgfDSYYGIPysNDMWIDPanrLADDLVLR 175
Cdd:pfam01663 74 EYLVFVISDPEDPRwwQGEPIWDTAAKAGVRAAALF-W-----PGSEVDY---STYYGTP--PRYLKDD---YNNSVPFE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 176 EGVTieqlktgqklknrvplmldeevieypvdqSTVTKRYTERAVHYIQEQKDRPFFIYLPHTmvhvplavsDAFKNRTG 255
Cdd:pfam01663 140 DRVD-----------------------------TAVLQTWLDLPFADVAAERPDLLLVYLEEP---------DYAGHRYG 181
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1712519934 256 ---ELIWDAIEEVDWSVGQILQALKDNKIDEKTLVIFTSDNGAA 296
Cdd:pfam01663 182 pdsPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMT 225
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
376-456 |
9.47e-06 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 45.38 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519934 376 SPHNT---YCLAHgPGTVRSGQWK--YYpwkegQSGRRKQNSTAISDPQSEVQ------LYDTVNDIGETKNVAA---HY 441
Cdd:pfam14707 1 SPHEFlfhYCGAA-LHAVRWGPYKahFF-----TPSFDPPGAEGCYGSKVPVThhdpplLFDLERDPSEKYPLSPdspEY 74
|
90
....*....|....*
gi 1712519934 442 PEVVSRLQKAWEEHL 456
Cdd:pfam14707 75 PEVLAEIKAAVEEHK 89
|
|
| |
