|
Name |
Accession |
Description |
Interval |
E-value |
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
46-500 |
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: 293776 [Multi-domain] Cd Length: 466 Bit Score: 967.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 46 EMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTPQEIVGGIPD 125
Cdd:cd16157 11 DMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTPQNIVGGIPD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 126 SEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKARPNIPVYRDWEMVGRYYEEFPINLK 205
Cdd:cd16157 91 SEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCHFGPYDNKAYPNIPVYRDWEMIGRYYEEFKIDKK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 206 TGEANLTQIYLQEALDFIKRQA-RHHPFFLYWAVDATHAPVYASKPFLGTSQRGRYGDAVREIDDSIGKILELLQDLHVA 284
Cdd:cd16157 171 TGESNLTQIYLQEALEFIEKQHdAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 285 DNTFVFFTSDNGAALISAPEQGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPP 364
Cdd:cd16157 251 NNTFVFFSSDNGAALISAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 365 SDRAIDGLNLLPTLLQGRLMDRPIFYYRGDTLMAATLGQHKAHFWTWTNSWENFRQGIDFCPGQNVSGVTTHNLEDHTKL 444
Cdd:cd16157 331 SDRAIDGIDLLPVLLNGKEKDRPIFYYRGDELMAVRLGQYKAHFWTWSNSWEEFRKGINFCPGQNVPGVTTHNQTDHTKL 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217305387 445 PLIFHLGRDPGERFPLSFASAEYQEALSRITSVVQQHQEALVPAQPQLNVCNWAVM 500
Cdd:cd16157 411 PLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVVQQHQKTLVPGEPQLNVCDLAVM 466
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
47-461 |
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: 522.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharnaytPQEIVGGIPDS 126
Cdd:cd16026 12 LGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVG-------PPGSKGGLPPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 127 EQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKARPNIPVYRDwemvGRYYEEFPINLKT 206
Cdd:cd16026 85 EITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP----PLMENEEVIEQPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 207 GEANLTQIYLQEALDFIKRQaRHHPFFLYWAVDATHAPVYASKPFLGTSQRGRYGDAVREIDDSIGKILELLQDLHVADN 286
Cdd:cd16026 161 DQSSLTQRYTDEAVDFIERN-KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEEN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 287 TFVFFTSDNGAALISaPEQGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSD 366
Cdd:cd16026 240 TLVIFTSDNGPWLEY-GGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPED 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 367 RAIDGLNLLPTLLQGRLMDRP--IFYYRGDTLMAATLGQHKAHFWTWTNSWENFRqgidfcpgqnvsgvttHNLEDHTKL 444
Cdd:cd16026 319 RVIDGKDISPLLLGGSKSPPHpfFYYYDGGDLQAVRSGRWKLHLPTTYRTGTDPG----------------GLDPTKLEP 382
|
410
....*....|....*..
gi 2217305387 445 PLIFHLGRDPGERFPLS 461
Cdd:cd16026 383 PLLYDLEEDPGETYNVA 399
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
46-466 |
5.49e-114 |
|
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: 344.80 E-value: 5.49e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 46 EMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTnahaRNAYTPQEIvGGIPD 125
Cdd:cd16160 11 DMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGG----TRVFLPWDI-GGLPK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 126 SEQLLPELLKKAGYVSKIVGKWHLG-----HRPQFH-PLKHGFD----------EWFGSPncHFGPYDNKARPNIPVYRD 189
Cdd:cd16160 86 TEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDfvgtnlpftnSWACDD--TGRHVDFPDRSACFLYYN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 190 WEMVgryyeEFPINLKtgeaNLTQIYLQEALDFIKRQArHHPFFLYWAVDATHAPVYASKPFLGTSQRGRYGDAVREIDD 269
Cdd:cd16160 164 DTIV-----EQPIQHE----HLTETLVGDAKSFIEDNQ-ENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSW 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 270 SIGKILELLQDLHVADNTFVFFTSDNGAALiSAPEQGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTaGQVSHQLGSIM 349
Cdd:cd16160 234 AVGEVLDTLVDTGLDQNTLVFFLSDHGPHV-EYCLEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIK-PRVSHEVVSTM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 350 DLFTTSLALAGLTPPSDRAIDGLNLLPTLLQGRLMD-RPIFYYRGDTLMAATLGQHKAHFWTWTNSWENFrQGIDFCPGQ 428
Cdd:cd16160 312 DIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPhDDILYYCCSRLMAVRYGSYKIHFKTQPLPSQES-LDPNCDGGG 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2217305387 429 NVS-----------GVTTHNledhtkLPLIFHLGRDPGERFPLSFASAE 466
Cdd:cd16160 391 PLSdyivcydcedeCVTKHN------PPLIFDVEKDPGEQYPLQPSVYE 433
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
47-492 |
2.09e-108 |
|
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: 333.10 E-value: 2.09e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTPQEivGGIPDS 126
Cdd:cd16159 12 LGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFTASS--GGLPPN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 127 EQLLPELLKKAGYVSKIVGKWHLG-HRPQ-----FHPLKHGFDEWFGSP-----NCHFGP---YDNKARPNIPVYRDWEM 192
Cdd:cd16159 90 ETTFAEVLKQQGYSTALIGKWHLGlHCESrndfcHHPLNHGFDYFYGLPltnlkDCGDGSngeYDLSFDPLFPLLTAFVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 193 VG-----------------------------------------------RYYE--EFPINLKtgeaNLTQIYLQEALDFI 223
Cdd:cd16159 170 ITaltiflllylgavskrffvfllilsllfislfflllitnryfncilmRNHEvvEQPMSLE----NLTQRLTKEAISFL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 224 KRQaRHHPFFLYWAVDATHAPVYASKPFLGTSQRGRYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAAL--IS 301
Cdd:cd16159 246 ERN-KERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeIS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 302 A-PEQGGSNGPFLCGK-QTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDRAIDGLNLLPtLL 379
Cdd:cd16159 325 VgGEYGGGNGGIYGGKkMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLMP-LL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 380 QGRLMDRP---IFYYRGDTLMAATLGQH------KAHFWTwtnswENFRQGIDFCPGQNV-----SGVTTHNledhtkLP 445
Cdd:cd16159 404 TGQEKRSPhefLFHYCGAELHAVRYRPRdggavwKAHYFT-----PNFYPGTEGCCGTLLcrcfgDSVTHHD------PP 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2217305387 446 LIFHLGRDPGERFPLSFASAEYQEALSRITSVVQQHQEALVPAQPQL 492
Cdd:cd16159 473 LLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIEPVESQL 519
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
47-460 |
2.39e-106 |
|
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: 322.56 E-value: 2.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLGVYG---EPSRETPNLDRMAAEGLLFPNFYsANPLCSPSRAALLTGRLPIRNGFYTTnaharnayTPQEIVGGI 123
Cdd:cd16142 11 IGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFY-VEPSCTPGRAAFITGRHPIRTGLTTV--------GLPGSPGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 124 PDSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGspnchfgpydnkarpNIPVYRDWEMVGRyyeefpin 203
Cdd:cd16142 82 PPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYG---------------NLYHTIDEEIVDK-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 204 lktgeanltqiylqeALDFIKRQAR-HHPFFLYWAVDATHAPVYASKPFLGTSQR-GRYGDAVREIDDSIGKILELLQDL 281
Cdd:cd16142 139 ---------------AIDFIKRNAKaDKPFFLYVNFTKMHFPTLPSPEFEGKSSGkGKYADSMVELDDHVGQILDALDEL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 282 HVADNTFVFFTSDNGAALISAPeqGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGL 361
Cdd:cd16142 204 GIADNTIVIFTTDNGPEQDVWP--DGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 362 TPP------SDRAIDGLNLLPTLL--QGRLMDRPIFYYRGDTLMAATLGQHKAHFwTWtnswenfrqgidfcpgQNVSGV 433
Cdd:cd16142 282 PDPkdkllgKDRHIDGVDQSPFLLgkSEKSRRSEFFYFGEGELGAVRWKNWKVHF-KA----------------QEDTGG 344
|
410 420
....*....|....*....|....*..
gi 2217305387 434 TTHNLEDHTKLPLIFHLGRDPGERFPL 460
Cdd:cd16142 345 PTGEPFYVLTFPLIFNLRRDPKERYDV 371
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
46-493 |
1.38e-104 |
|
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: 321.70 E-value: 1.38e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 46 EMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAytpqeivGGIPD 125
Cdd:cd16158 11 DLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSR-------GGLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 126 SEQLLPELLKKAGYVSKIVGKWHLGHRPQ--FHPLKHGFDEWFGSPNCH-FGPYDNKA--RPNIPVYRDWE--------M 192
Cdd:cd16158 84 NETTIAEVLKTVGYQTAMVGKWHLGVGLNgtYLPTHQGFDHYLGIPYSHdQGPCQNLTcfPPNIPCFGGCDqgevpcplF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 193 VGRYYEEFPINLktgeANLTQIYLQEALDFI-KRQARHHPFFLYWAVDATHAPVYASKPFLGTSQRGRYGDAVREIDDSI 271
Cdd:cd16158 164 YNESIVQQPVDL----LTLEERYAKFAKDFIaDNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 272 GKILELLQDLHVADNTFVFFTSDNGAALISApEQGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTAGqVSHQLGSIMDL 351
Cdd:cd16158 240 GELLQTLKENGIDNNTLVFFTSDNGPSTMRK-SRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPG-VTHELASTLDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 352 FTTSLALAGLTPPsDRAIDGLNLLPTLL-QGRLMDRPIFYYRGDT-----LMAATLGQHKAHFWTwtnswenfrqgidfc 425
Cdd:cd16158 318 LPTIAKLAGAPLP-NVTLDGVDMSPILFeQGKSPRQTFFYYPTSPdpdkgVFAVRWGKYKAHFYT--------------- 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217305387 426 PGQNVSGVTTHN-------LEDHTKlPLIFHLGRDPGERFPLSfASAEYQEALSRITSVVQQHQEALVPAQPQLN 493
Cdd:cd16158 382 QGAAHSGTTPDKdchpsaeLTSHDP-PLLFDLSQDPSENYNLL-GLPEYNQVLKQIQQVKERFEASMKFGESEIN 454
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
46-460 |
2.52e-101 |
|
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: 310.17 E-value: 2.52e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 46 EMGWGDLGVYGEPSR-ETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFyTTNAHARNaytpqeiVGGIP 124
Cdd:cd16161 11 DLGWGDLGANWAPNAiLTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTS-------VGGLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 125 DSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHfgpydnkarpnipvyrdwemvgryyeefpinl 204
Cdd:cd16161 83 LNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSH-------------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 205 ktgEANLTQIYLQEALDFIKR-QARHHPFFLYWAVDATHAPV-YASKPFLGTSQRGRYGDAVREIDDSIGKILELLQDLH 282
Cdd:cd16161 131 ---DSSLADRYAQFATDFIQRaSAKDRPFFLYAALAHVHVPLaNLPRFQSPTSGRGPYGDALQEMDDLVGQIMDAVKHAG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 283 VADNTFVFFTSDNGAALISAPEQGG-------SNGPFLCGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTS 355
Cdd:cd16161 208 LKDNTLTWFTSDNGPWEVKCELAVGpgtgdwqGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 356 LALAGLTPPSDRAIDGLNLLPTLLQGRLMDRPIFYY------RGDTLMAATLGQHKAHFWTwtnswenfrQGI-----DF 424
Cdd:cd16161 288 VALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHpnsgaaGAGALSAVRCGDYKAHYAT---------GGAlaccgST 358
|
410 420 430
....*....|....*....|....*....|....*.
gi 2217305387 425 CPGQnvsgvtthnledHTKLPLIFHLGRDPGERFPL 460
Cdd:cd16161 359 GPKL------------YHDPPLLFDLEVDPAESFPL 382
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
47-416 |
2.08e-97 |
|
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: 301.38 E-value: 2.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAY-----TPQEIVG 121
Cdd:cd16144 11 LGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPdntklIPPPSTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 122 GIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSpnCHFGPYDNKARPNIPVYRDWEmvgryyeefp 201
Cdd:cd16144 91 RLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIGG--TGNGGPPSYYFPPGKPNPDLE---------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 202 iNLKTGEaNLTQIYLQEALDFIKRQARhHPFFLYWAVDATHAPV----------YASKPFLGTSQRG-RYGDAVREIDDS 270
Cdd:cd16144 159 -DGPEGE-YLTDRLTDEAIDFIEQNKD-KPFFLYLSHYAVHTPIqarpeliekyEKKKKGLRKGQKNpVYAAMIESLDES 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 271 IGKILELLQDLHVADNTFVFFTSDNGaALISAPEQGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMD 350
Cdd:cd16144 236 VGRILDALEELGLADNTLVIFTSDNG-GLSTRGGPPTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTD 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217305387 351 LFTTSLALAGLTPPSDRAIDGLNLLPTLLQG--RLMDRPIF----YYRGDTLMAAT---LGQHKAHFWTWTNSWE 416
Cdd:cd16144 315 LYPTFLELAGGPLPPPQHLDGVSLVPLLKGGeaDLPRRALFwhfpHYHGQGGRPASairKGDWKLIEFYEDGRVE 389
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
47-485 |
4.09e-92 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 286.77 E-value: 4.09e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARnaytpqeivGGIPDS 126
Cdd:COG3119 34 LGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYN---------GGLPPD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 127 EQLLPELLKKAGYVSKIVGKWHLghrpqfhplkhgfdewfgspnchfgpydnkarpnipvyrdwemvgryyeefpinlkt 206
Cdd:COG3119 105 EPTLAELLKEAGYRTALFGKWHL--------------------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 207 geaNLTQIYLQEALDFIKRQARH-HPFFLYWAVDATHAPVYASKPFLG-----------------------TSQRGRYGD 262
Cdd:COG3119 128 ---YLTDLLTDKAIDFLERQADKdKPFFLYLAFNAPHAPYQAPEEYLDkydgkdiplppnlaprdlteeelRRARAAYAA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 263 AVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALisaPEQGgsngpFLCGKQTTFEGGMREPALAWWPGHVTAGQVS 342
Cdd:COG3119 205 MIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSL---GEHG-----LRGGKGTLYEGGIRVPLIVRWPGKIKAGSVS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 343 HQLGSIMDLFTTSLALAGLTPPSDraIDGLNLLPTLLQGRLMDRPIFYY---RGDTLMAATLGQHKAHFWtwtnswenfr 419
Cdd:COG3119 277 DALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWeypRGGGNRAIRTGRWKLIRY---------- 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217305387 420 qgidfcpgqnvsgvttHNLEDHTKLpliFHLGRDPGERFPLsfaSAEYQEALSRITSVVQQHQEAL 485
Cdd:COG3119 345 ----------------YDDDGPWEL---YDLKNDPGETNNL---AADYPEVVAELRALLEAWLKEL 388
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
46-416 |
2.78e-91 |
|
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: 285.26 E-value: 2.78e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 46 EMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTG----RLPIRngfyttnaharnAYTPQEIVG 121
Cdd:cd16145 10 DLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGlhtgHTRVR------------GNSEPGGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 122 GIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQF-HPLKHGFDEWFGSPN---CHFG--PY--DNKARPNIPvyrdwEMV 193
Cdd:cd16145 78 PLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYGYLDqvhAHNYypEYlwRNGEKVPLP-----NNV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 194 GRYYEEFPINLKTGEANLTQIYLQEALDFIKRQaRHHPFFLYWAVDATHAPV------YASKPFLGTSQRG--------- 258
Cdd:cd16145 153 IPPLDEGNNAGGGGGTYSHDLFTDEALDFIREN-KDKPFFLYLAYTLPHAPLqvpddgPYKYKPKDPGIYAylpwpqpek 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 259 RYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALISAPEQGG----SNGPFLCGKQTTFEGGMREPALAWWPG 334
Cdd:cd16145 232 AYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSEGGSEHDPdffdSNGPLRGYKRSLYEGGIRVPFIARWPG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 335 HVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDraIDGLNLLPTLLQGRL--MDRPIFY--YRGDTLMAATLGQHKA-HFW 409
Cdd:cd16145 312 KIPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQqqQHDYLYWefYEGGGAQAVRMGGWKAvRHG 389
|
....*..
gi 2217305387 410 TWTNSWE 416
Cdd:cd16145 390 KKDGPFE 396
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
47-457 |
1.76e-82 |
|
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: 261.75 E-value: 1.76e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLGVYGEPSR-ETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIR--NGFYTTNAHARNAytpqeivggI 123
Cdd:cd16143 11 LGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRsrLKGGVLGGFSPPL---------I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 124 PDSEQLLPELLKKAGYVSKIVGKWHLG---------HRPQFH-------------PLKHGFDEWFGSPNCHFGPYdnkar 181
Cdd:cd16143 82 EPDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkKAATGTgkdvdyskpikggPLDHGFDYYFGIPASEVLPT----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 182 pnipvyrdwemvgryyeefpinlktgeanLTQiylqEALDFIKRQARH-HPFFLYWAVDATHAPVYASKPFLGTSQRGRY 260
Cdd:cd16143 157 -----------------------------LTD----KAVEFIDQHAKKdKPFFLYFALPAPHTPIVPSPEFQGKSGAGPY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 261 GDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGA---ALISAPEQGG--SNGPFLCGKQTTFEGGMREPALAWWPGH 335
Cdd:cd16143 204 GDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPspyADYKELEKFGhdPSGPLRGMKADIYEGGHRVPFIVRWPGK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 336 VTAGQVSHQLGSIMDLFTTSLALAGLTPPSDRAIDGLNLLPTLL-QGRLMDRP-IFYYRGDTLMAATLGQHKahfwtwtn 413
Cdd:cd16143 284 IPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLgPKKQEVREsLVHHSGNGSFAIRKGDWK-------- 355
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2217305387 414 swenfrqgidFCPGQNVSGVTTHNLEDHTKLPLI--FHLGRDPGER 457
Cdd:cd16143 356 ----------LIDGTGSGGFSYPRGKEKLGLPPGqlYNLSTDPGES 391
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
47-476 |
1.83e-82 |
|
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: 262.49 E-value: 1.83e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYsANPLCSPSRAALLTGRLPIRNGFYTTnaharnaytpqeIVGG--IP 124
Cdd:cd16146 11 QGYGDLGFHGNPILKTPNLDRLAAESVRFTNFH-VSPVCAPTRAALLTGRYPFRTGVWHT------------ILGRerMR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 125 DSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFG---PYDNKARPNIPVYRDWEMVGryYEEFp 201
Cdd:cd16146 78 LDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGGGIGqypDYWGNDYFDDTYYHNGKFVK--TEGY- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 202 inlktgeanLTQIYLQEALDFIKRQaRHHPFFLYWAVDATHAPVYA----SKPF----LGTSQRGRYGdAVREIDDSIGK 273
Cdd:cd16146 155 ---------CTDVFFDEAIDFIEEN-KDKPFFAYLATNAPHGPLQVpdkyLDPYkdmgLDDKLAAFYG-MIENIDDNVGR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 274 ILELLQDLHVADNTFVFFTSDNGAAlisapeqGGSNGPFLCG----KQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIM 349
Cdd:cd16146 224 LLAKLKELGLEENTIVIFMSDNGPA-------GGVPKRFNAGmrgkKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 350 DLFTTSLALAGLTPPSDRAIDGLNLLPTLLQGRLM--DRPIFYYRGDTLMAAtlgQHKAHFWTWTNSWenfrqgidfcpg 427
Cdd:cd16146 297 DLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPwpERTLFTHSGRWPPPP---KKKRNAAVRTGRW------------ 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2217305387 428 qnvsgvttHNLEDHTKLPLIFHLGRDPGERFPLsfaSAEYQEALSRITS 476
Cdd:cd16146 362 --------RLVSPKGFQPELYDIENDPGEENDV---ADEHPEVVKRLKA 399
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
47-361 |
1.14e-80 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 253.88 E-value: 1.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTnaharnaytpqeIVGGIPDS 126
Cdd:pfam00884 11 LRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS------------TPVGLPRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 127 EQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKARPNIPVyrdwemVGRYYeefpinlkt 206
Cdd:pfam00884 79 EPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNCS------GGGVS--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 207 geanlTQIYLQEALDFIKRQARhhPFFLYWAVDATHAPVYASKPFLGT------------SQRGRYGDAVREIDDSIGKI 274
Cdd:pfam00884 144 -----DEALLDEALEFLDNNDK--PFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscseeQLLNSYDNTLLYTDDAIGRV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 275 LELLQDLHVADNTFVFFTSDNGAALisapeqGGSNGPFLCGKQ-TTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFT 353
Cdd:pfam00884 217 LDKLEENGLLDNTLVVYTSDHGESL------GEGGGYLHGGKYdNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFP 290
|
....*...
gi 2217305387 354 TSLALAGL 361
Cdd:pfam00884 291 TILDLAGI 298
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
47-373 |
1.20e-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: 248.89 E-value: 1.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHArnaytpqeivGGIPDS 126
Cdd:cd16022 11 LGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNG----------GGLPPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 127 EQLLPELLKKAGYVSKIVGKWHlghrpqfhplkhgfdewfgspnchfgpydnkarpnipvyrdwemvgryyeefpinlkt 206
Cdd:cd16022 81 EPTLAELLKEAGYRTALIGKWH---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 207 geanltqiylQEALDFIKRQARHHPFFLYWAVDATHAPVYaskpflgtsqrgrYGDAVREIDDSIGKILELLQDLHVADN 286
Cdd:cd16022 103 ----------DEAIDFIERRDKDKPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDN 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 287 TFVFFTSDNGAALisapEQGGSNGpflcGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPsd 366
Cdd:cd16022 160 TLIVFTSDHGDML----GDHGLRG----KKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPP-- 229
|
....*..
gi 2217305387 367 RAIDGLN 373
Cdd:cd16022 230 EGLDGRS 236
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
47-382 |
1.45e-78 |
|
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: 251.70 E-value: 1.45e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSaNPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYtpqeivgGIPDS 126
Cdd:cd16029 11 LGWNDVGFHGSDQIKTPNLDALAADGVILNNYYV-QPICTPSRAALMTGRYPIHTGMQHGVILAGEPY-------GLPLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 127 EQLLPELLKKAGYVSKIVGKWHLGH-RPQFHPLKHGFDEWFGSPNCHFGPYDNKARPnipvYRDWEMVGRYYEEFPINLK 205
Cdd:cd16029 83 ETLLPQYLKELGYATHLVGKWHLGFyTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGG----ANDYGNDDLRDNEEPAWDY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 206 TGEaNLTQIYLQEALDFIKRQARHHPFFLYWAVDATHAPVYASKPFLG----------TSQRGRYGDAVREIDDSIGKIL 275
Cdd:cd16029 159 NGT-YSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADpyedkfahikDEDRRTYAAMVSALDESVGNVV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 276 ELLQDLHVADNTFVFFTSDNGAALISAPeqGGSNGPFLCGKQTTFEGGMREPALAWWPG-HVTAGQVSHQLGSIMDLFTT 354
Cdd:cd16029 238 DALKAKGMLDNTLIVFTSDNGGPTGGGD--GGSNYPLRGGKNTLWEGGVRVPAFVWSPLlPPKRGTVSDGLMHVTDWLPT 315
|
330 340
....*....|....*....|....*...
gi 2217305387 355 SLALAGLTPPSDRAIDGLNLLPTLLQGR 382
Cdd:cd16029 316 LLSLAGGDPDDLPPLDGVDQWDALSGGA 343
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
47-460 |
4.61e-69 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 226.33 E-value: 4.61e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYsANPLCSPSRAALLTGRLPIRNGfyttnaharnaytpqeIVGGIPDS 126
Cdd:cd16151 11 LGYECIGCYGGESYKTPNIDALAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNY----------------VVFGYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 127 EQL-LPELLKKAGYVSKIVGKWHLGHRPQF--HPLKHGFDEWfgspnCHFGPYDNKARPNIPVYRDWEMvgryyeefpIN 203
Cdd:cd16151 74 KQKtFGHLLKDAGYATAIAGKWQLGGGRGDgdYPHEFGFDEY-----CLWQLTETGEKYSRPATPTFNI---------RN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 204 LKTGEANLTQ----IYLQEALDFIKRQaRHHPFFLYWAVDATHAPVYA------SKPFLGTSQR--GRYGDAVREIDDSI 271
Cdd:cd16151 140 GKLLETTEGDygpdLFADFLIDFIERN-KDQPFFAYYPMVLVHDPFVPtpdspdWDPDDKRKKDdpEYFPDMVAYMDKLV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 272 GKILELLQDLHVADNTFVFFTSDNG-AALISAPEQGGS-NGpflcGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIM 349
Cdd:cd16151 219 GKLVDKLEELGLRENTIIIFTGDNGtHRPITSRTNGREvRG----GKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 350 DLFTTSLALAGLTPPSDRAIDGLNLLPTLL--QGRLMDRPIFYYrgdtlmAATLGQHKAHFWTWTNSWenfrqgidfcpg 427
Cdd:cd16151 295 DFLPTLAELAGAPLPEDYPLDGRSFAPQLLgkTGSPRREWIYWY------YRNPHKKFGSRFVRTKRY------------ 356
|
410 420 430
....*....|....*....|....*....|...
gi 2217305387 428 qnvsgvtthNLEDHTKLpliFHLGRDPGERFPL 460
Cdd:cd16151 357 ---------KLYADGRF---FDLREDPLEKNPL 377
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
47-386 |
2.68e-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: 213.91 E-value: 2.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWgDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGfytTNAHARNAYTPqeivggiPDS 126
Cdd:cd16027 11 LSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNG---AHGLRSRGFPL-------PDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 127 EQLLPELLKKAGYVSKIVGKWHlghrpqfhplkHGFDEwfgspncHFGPYDNKARPNIPVYRDWEmvgryyeefpinlkt 206
Cdd:cd16027 80 VKTLPELLREAGYYTGLIGKTH-----------YNPDA-------VFPFDDEMRGPDDGGRNAWD--------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 207 geanltqiYLQEALDFIKRQARHHPFFLYWAVDATHAPVYASKPFLGT-------------------SQRGRYGDAVREI 267
Cdd:cd16027 127 --------YASNAADFLNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGydpekvkvppylpdtpevrEDLADYYDEIERL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 268 DDSIGKILELLQDLHVADNTFVFFTSDNGAALisapeqggsngPFlcGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGS 347
Cdd:cd16027 199 DQQVGEILDELEEDGLLDNTIVIFTSDHGMPF-----------PR--AKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVS 265
|
330 340 350
....*....|....*....|....*....|....*....
gi 2217305387 348 IMDLFTTSLALAGLTPPSDraIDGLNLLPTLLQGRLMDR 386
Cdd:cd16027 266 FIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGR 302
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
47-416 |
4.50e-64 |
|
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: 213.84 E-value: 4.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLGVYGEPSReTPNLDRMAAEGLLFPNFYsANPLCSPSRAALLTGRLPIRNGF--YTTNAHARNAYTpqeivGGIP 124
Cdd:cd16025 13 LGFSDLGCFGGEIP-TPNLDALAAEGLRFTNFH-TTALCSPTRAALLTGRNHHQVGMgtMAELATGKPGYE-----GYLP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 125 DSEQLLPELLKKAGYVSKIVGKWHLGHrPQFHplkhgfdewfgspnchfgpydnkarpnipvyrdwemvgryyeefpinl 204
Cdd:cd16025 86 DSAATIAEVLKDAGYHTYMSGKWHLGP-DDYY------------------------------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 205 ktgeanLTQIYLQEALDFIKRQARHH-PFFLYWAVDATHAPVYASKPFLgTSQRGRYG---DAVRE-------------- 266
Cdd:cd16025 117 ------STDDLTDKAIEYIDEQKAPDkPFFLYLAFGAPHAPLQAPKEWI-DKYKGKYDagwDALREerlerqkelglipa 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 267 --------------------------------------IDDSIGKILELLQDLHVADNTFVFFTSDNGAalisAPEQG-- 306
Cdd:cd16025 190 dtkltprppgvpawdslspeekklearrmevyaamvehMDQQIGRLIDYLKELGELDNTLIIFLSDNGA----SAEPGwa 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 307 -GSNGPFLCGKQTTFEGGMREPALAWWPGHVTA-GQVSHQLGSIMDLFTTSLALAGLTPPSDR------AIDGLNLLPTL 378
Cdd:cd16025 266 nASNTPFRLYKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHVIDIAPTILELAGVEYPKTVngvpqlPLDGVSLLPTL 345
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2217305387 379 L--QGRLMDRPIFY--------YRGDtLMAATLGQhkahFWTWTNSWE 416
Cdd:cd16025 346 DgaAAPSRRRTQYFelfgnraiRKGG-WKAVALHP----PPGWGDQWE 388
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
49-392 |
1.37e-60 |
|
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: 205.46 E-value: 1.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 49 WGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGfYTTNAHarnaytpqeivGGIPDSEQ 128
Cdd:cd16031 15 YDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHG-VTDNNG-----------PLFDASQP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 129 LLPELLKKAGYVSKIVGKWHLGHRPQFHPlkHGFDEWFGSP-NCHFGPYDNKarpnipvyrdwEMVGRYYEEFPInlktg 207
Cdd:cd16031 83 TYPKLLRKAGYQTAFIGKWHLGSGGDLPP--PGFDYWVSFPgQGSYYDPEFI-----------ENGKRVGQKGYV----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 208 eanlTQIYLQEALDFIKRQARHHPFFLYWAVDATHAP-------------------------VYASKPFLGTSQRGR--- 259
Cdd:cd16031 145 ----TDIITDKALDFLKERDKDKPFCLSLSFKAPHRPftpaprhrglyedvtipepetfdddDYAGRPEWAREQRNRirg 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 260 ------------------YGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALisapeqgGSNGpfLCGKQTTFE 321
Cdd:cd16031 221 vldgrfdtpekyqrymkdYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL-------GEHG--LFDKRLMYE 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217305387 322 GGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDraIDGLNLLPtLLQGRLMD--RPIFYYR 392
Cdd:cd16031 292 ESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLP-LLEGEKPVdwRKEFYYE 361
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
51-382 |
9.29e-57 |
|
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: 194.71 E-value: 9.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 51 DLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHarnaytpqeivggIPDSEQLL 130
Cdd:cd16034 16 ALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-------------LPPDAPTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 131 PELLKKAGYVSKIVGKWHL-GHRPQFH---------PLKHGFDEWFGSPNC--HFGPYDNKARPNIPVYRDWEmvgryye 198
Cdd:cd16034 83 ADVLKDAGYRTGYIGKWHLdGPERNDGraddytpppERRHGFDYWKGYECNhdHNNPHYYDDDGKRIYIKGYS------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 199 efPInlktGEANLtqiylqeALDFIKRQA-RHHPFFLYWAVDATHAPvYASKP--------------------------F 251
Cdd:cd16034 156 --PD----AETDL-------AIEYLENQAdKDKPFALVLSWNPPHDP-YTTAPeeyldmydpkklllrpnvpedkkeeaG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 252 LGTSQRGRYGdAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGaalisapEQGGSNGpfLCGKQTTFEGGMREPALAW 331
Cdd:cd16034 222 LREDLRGYYA-MITALDDNIGRLLDALKELGLLENTIVVFTSDHG-------DMLGSHG--LMNKQVPYEESIRVPFIIR 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2217305387 332 WPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDraIDGLNLLPTLLQGR 382
Cdd:cd16034 292 YPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGK 340
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
47-359 |
6.16e-52 |
|
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: 176.84 E-value: 6.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLGVYGEPSRETPNLDRMAAEGLLFpNFYSANPLCS--PSRAALLTGRLPIRNGFYTTNAHARnayTPQEIVGGIP 124
Cdd:cd00016 11 LGADDLGKAGNPAPTTPNLKRLASEGATF-NFRSVSPPTSsaPNHAALLTGAYPTLHGYTGNGSADP---ELPSRAAGKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 125 DSEQLLPELLKKAGYVSKIVGkwhlghrpqfhplkhgfdewfgspnchfgpydnkarpnipvyrdwemvgryyeefpinl 204
Cdd:cd00016 87 EDGPTIPELLKQAGYRTGVIG----------------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 205 ktgeanltqiylqeALDFIKRQARHHPFFLYWAVDATHAPVYASKPflgtsQRGRYGDAVREIDDSIGKILELLQDLHVA 284
Cdd:cd00016 108 --------------LLKAIDETSKEKPFVLFLHFDGPDGPGHAYGP-----NTPEYYDAVEEIDERIGKVLDALKKAGDA 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217305387 285 DNTFVFFTSDNGAALISAPEQggsngPFLCGKQTTFEGGMREPALAWWPGHVtAGQVSHQLGSIMDLFTTSLALA 359
Cdd:cd00016 169 DDTVIIVTADHGGIDKGHGGD-----PKADGKADKSHTGMRVPFIAYGPGVK-KGGVKHELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
52-404 |
9.22e-49 |
|
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: 173.56 E-value: 9.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 52 LGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTtnaharNAYTPQEIVGGIPDSEQLLP 131
Cdd:cd16033 16 LGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLN------NVENAGAYSRGLPPGVETFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 132 ELLKKAGYVSKIVGKWHLGhrPQFHPLKHGFDEWFgsPNCHFGPYDnkarpnipvyrdwemvgryyeefpinlktgeanl 211
Cdd:cd16033 90 EDLREAGYRNGYVGKWHVG--PEETPLDYGFDEYL--PVETTIEYF---------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 212 tqiYLQEALDFIKR-QARHHPFFLYWAVDATHAPVYASKPFL----------------------GTSQRGR--------- 259
Cdd:cd16033 132 ---LADRAIEMLEElAADDKPFFLRVNFWGPHDPYIPPEPYLdmydpediplpesfaddfedkpYIYRRERkrwgvdted 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 260 ----------YGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALISapeQGGSN-GPFLcgkqttFEGGMREPA 328
Cdd:cd16033 209 eedwkeiiahYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGA---HRLWDkGPFM------YEETYRIPL 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217305387 329 LAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPsdRAIDGLNLLPTLLQGRLMDRPifyyrgDTLMAATLGQH 404
Cdd:cd16033 280 IIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVP--PKVDGRSLLPLLRGEQPEDWR------DEVVTEYNGHE 347
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
52-376 |
5.09e-47 |
|
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: 164.33 E-value: 5.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 52 LGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTPQEIvgGIPDSEQLLP 131
Cdd:cd16149 16 LGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTKKPE--GYLEGQTTLP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 132 ELLKKAGYVSKIVGKWHLGhrpqfhplkhgfdewfgspnchfgpydnkarpnipvyrdwemvgryyeefpinlktgeanl 211
Cdd:cd16149 94 EVLQDAGYRCGLSGKWHLG------------------------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 212 tqiylQEALDF-IKRQARHHPFFLYWAVDATHAPvyaskpflgtsqrGRYGDAVREIDDSIGKILELLQDLHVADNTFVF 290
Cdd:cd16149 113 -----DDAADFlRRRAEAEKPFFLSVNYTAPHSP-------------WGYFAAVTGVDRNVGRLLDELEELGLTENTLVI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 291 FTSDNGAALisapeqgGSNGPFLCGKQTT----FEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSD 366
Cdd:cd16149 175 FTSDNGFNM-------GHHGIWGKGNGTFplnmYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPAD 247
|
330
....*....|
gi 2217305387 367 RAIDGLNLLP 376
Cdd:cd16149 248 PRLPGRSFAD 257
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
52-389 |
2.93e-45 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 161.56 E-value: 2.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 52 LGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTtNAHArnaytpqeivggIPDSEQLLP 131
Cdd:cd16037 16 MGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWD-NADP------------YDGDVPSWG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 132 ELLKKAGYVSKIVGKWHLGHRPQFHplkhGFDewfgspnchfgpYDnkarpnipvyrdwEMVgryyeefpinlktgeanl 211
Cdd:cd16037 83 HALRAAGYETVLIGKLHFRGEDQRH----GFR------------YD-------------RDV------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 212 tqiyLQEALDFIKRQARH-HPFFLYWAVDATHAPVYASKPFLG----TSQRGRYGdAVREIDDSIGKILELLQDLHVADN 286
Cdd:cd16037 116 ----TEAAVDWLREEAADdKPWFLFVGFVAPHFPLIAPQEFYDlyvrRARAAYYG-LVEFLDENIGRVLDALEELGLLDN 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 287 TFVFFTSDNGaalisapEQGGSNGpfLCGKQTTFEGGMREPALAWWPGhVTAGQVSHQLGSIMDLFTTSLALAGLTPPSD 366
Cdd:cd16037 191 TLIIYTSDHG-------DMLGERG--LWGKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPD 260
|
330 340
....*....|....*....|...
gi 2217305387 367 RaiDGLNLLPTLLQGRLMDRPIF 389
Cdd:cd16037 261 L--DGRSLLPLAEGPDDPDRVVF 281
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
52-376 |
6.65e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 148.46 E-value: 6.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 52 LGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYttnaharnaytpqeiVGGIPDSEQLLP 131
Cdd:cd16148 16 LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW---------------GGPLEPDDPTLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 132 ELLKKAGYVSKIVGKW-HLGHRPQFHplkHGFDEWfgspncHFGPYDNKARPNIPVYRDWEMVgryyeefpinlktgean 210
Cdd:cd16148 81 EILRKAGYYTAAVSSNpHLFGGPGFD---RGFDTF------EDFRGQEGDPGEEGDERAERVT----------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 211 ltqiylQEALDFIKRQARHHPFFLYWAVDATHAPvYaskpflgtsqrgRYGDAVREIDDSIGKILELLQDLHVADNTFVF 290
Cdd:cd16148 135 ------DRALEWLDRNADDDPFFLFLHYFDPHEP-Y------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 291 FTSDNGAALisapeqgGSNGpFLCGKQTTF-EGGMREPALAWWPGhVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDraI 369
Cdd:cd16148 196 VTSDHGEEF-------GEHG-LYWGHGSNLyDEQLHVPLIIRWPG-KEPGKRVDALVSHIDIAPTLLDLLGVEPPDY--S 264
|
....*..
gi 2217305387 370 DGLNLLP 376
Cdd:cd16148 265 DGRSLLP 271
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-476 |
5.56e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 148.87 E-value: 5.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 49 WGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANP----LCSPSRAALLTGRlpirNGFYTTNAHARNaytpqeivggIP 124
Cdd:cd16155 15 ADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGwsgaVCVPSRAMLMTGR----TLFHAPEGGKAA----------IP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 125 DSEQLLPELLKKAGYVSKIVGKWHLGHrpqfhplkhgfdewfgspnchfgpydnkarpnipvyrdwemvgryyeefpinl 204
Cdd:cd16155 81 SDDKTWPETFKKAGYRTFATGKWHNGF----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 205 ktgeANltqiylqEALDFIKRQARH-HPFFLYWAVDATHAPVYASKPFL------------------------------- 252
Cdd:cd16155 108 ----AD-------AAIEFLEEYKDGdKPFFMYVAFTAPHDPRQAPPEYLdmyppetiplpenflpqhpfdngegtvrdeq 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 253 -----GTS-----QRGRYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALisapeqgGSNGpfLCGKQTTFEG 322
Cdd:cd16155 177 lapfpRTPeavrqHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAV-------GSHG--LMGKQNLYEH 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 323 GMREPALAWWPGhVTAGQVSHQLGSIMDLFTTSLALAGLTPPSdrAIDGLNLLPtLLQG---RLMDRPIFYYRGDTLMAA 399
Cdd:cd16155 248 SMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPE--SVEGKSLLP-VIRGekkAVRDTLYGAYRDGQRAIR 323
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217305387 400 TlGQHKahfwtwtnswenfrqGIDFCPGQnvsgvtthnleDHTKLpliFHLGRDPGERFPLSfASAEYQEALSRITS 476
Cdd:cd16155 324 D-DRWK---------------LIIYVPGV-----------KRTQL---FDLKKDPDELNNLA-DEPEYQERLKKLLA 369
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
386-514 |
6.20e-40 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 140.91 E-value: 6.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 386 RPIFYYRGDTLMAATLGQHKAHFWTwtNSWenFRQGIDFCPGQNVsGVTTHNLedhtklPLIFHLGRDPGERFPLSFASA 465
Cdd:pfam14707 4 EFLFHYCGAALHAVRWGPYKAHFFT--PSF--DPPGAEGCYGSKV-PVTHHDP------PLLFDLERDPSEKYPLSPDSP 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217305387 466 EYQEALSRITSVVQQHQEALVPAQPQLNVCNWAVMNWAPPGCEKLGKCL 514
Cdd:pfam14707 73 EYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACT 121
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
52-387 |
2.35e-36 |
|
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: 137.71 E-value: 2.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 52 LGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYtTNAHARNAYTPQeivggipdseqlLP 131
Cdd:cd16032 16 LPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAY-DNAAEFPADIPT------------FA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 132 ELLKKAGYVSKIVGKWHL-GhrPQFHplkHGFDewfgspnchfgpYDnkarpnipvyrdwEMVGRyyeefpinlktgean 210
Cdd:cd16032 83 HYLRAAGYRTALSGKMHFvG--PDQL---HGFD------------YD-------------EEVAF--------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 211 ltqiylqEALDFIKRQARHH---PFFLywAVDAT--HAPVYASKPFLG----TSQRGRYGdAVREIDDSIGKILELLQDL 281
Cdd:cd16032 118 -------KAVQKLYDLARGEdgrPFFL--TVSFThpHDPYVIPQEYWDlyvrRARRAYYG-MVSYVDDKVGQLLDTLERT 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 282 HVADNTFVFFTSDNGAALisapeqgGSNGpfLCGKQTTFEGGMREPALAWWPGHVTAGQVShQLGSIMDLFTTSLALAGL 361
Cdd:cd16032 188 GLADDTIVIFTSDHGDML-------GERG--LWYKMSFFEGSARVPLIISAPGRFAPRRVA-EPVSLVDLLPTLVDLAGG 257
|
330 340
....*....|....*....|....*..
gi 2217305387 362 -TPPSDRAIDGLNLLPtLLQGRLMDRP 387
Cdd:cd16032 258 gTAPHVPPLDGRSLLP-LLEGGDSGGE 283
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
50-481 |
6.07e-36 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 139.80 E-value: 6.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 50 GD-LGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTPQeivggipdseq 128
Cdd:PRK13759 19 GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVPWNYKNT----------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 129 lLPELLKKAGYVSKIVGKWHlghrpqFHP--LKHGFDE-WFGSPNCHFGPYDNKARPN-IPVYRDW---EMVGRYYEEFP 201
Cdd:PRK13759 88 -LPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHNvLLHDGYLHSGRNEDKSQFDfVSDYLAWlreKAPGKDPDLTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 202 INLK---------TGEANL--TQIYLQEALDFIKRQARHHPFFLYWAVDATHAP---------VY----ASKPFLGT--- 254
Cdd:PRK13759 161 IGWDcnswvarpwDLEERLhpTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSPydppkryfdMYkdadIPDPHIGDwey 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 255 -------------------------SQRGRYGDaVREIDDSIGKILELLQDLHVADNTFVFFTSDNGaalisapEQGGSN 309
Cdd:PRK13759 241 aedqdpeggsidalrgnlgeeyarrARAAYYGL-ITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG-------DMLGDH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 310 GPFLcgKQTTFEGGMREPALAWWPGHVTA---GQVSHQLGSIMDLFTTSLALAGLTPPSDraIDGLNLLPTLLQGRLMDR 386
Cdd:PRK13759 313 YLFR--KGYPYEGSAHIPFIIYDPGGLLAgnrGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQYEGWR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 387 PIFY----YRGDTLMAATLGQHKAHFWTWTNSWEnfrqgidfcpgqnvsgvtthnledhtklplIFHLGRDPGERFPLSf 462
Cdd:PRK13759 389 PYLHgehaLGYSSDNYLTDGKWKYIWFSQTGEEQ------------------------------LFDLKKDPHELHNLS- 437
|
490
....*....|....*....
gi 2217305387 463 ASAEYQEALSRITSVVQQH 481
Cdd:PRK13759 438 PSEKYQPRLREMRKKLVDH 456
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
51-378 |
2.49e-35 |
|
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: 137.32 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 51 DLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAytpqeivggIPDSeQLL 130
Cdd:cd16030 16 WLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKV---------APDA-VTL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 131 PELLKKAGYVSKIVGK-WHlGHRPQFHPLKHGFDEWFGSPncHFGPYDNKARPNIPVYRDWEMVGRYYEEFPInlkTGEA 209
Cdd:cd16030 86 PQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPP--GPEKYPPGKLCPGKKGGKGGGGGPAWEAADV---PDEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 210 NLTQIYLQEALDFIKRQARHH-PFFL----------------YW------------AVDATHAPVYASKPFLGTSQRGRY 260
Cdd:cd16030 160 YPDGKVADEAIEQLRKLKDSDkPFFLavgfykphlpfvapkkYFdlyplesiplpnPFDPIDLPEVAWNDLDDLPKYGDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 261 GD------------------------AVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALisapeqgGSNGPFlcGK 316
Cdd:cd16030 240 PAlnpgdpkgplpdeqarelrqayyaSVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHL-------GEHGHW--GK 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217305387 317 QTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDraIDGLNLLPTL 378
Cdd:cd16030 311 HTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPPC--LEGKSLVPLL 370
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
67-371 |
9.29e-35 |
|
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: 134.99 E-value: 9.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 67 RMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFyTTNAHARNAYTPQEIVGGIPDSeqlLPELLKKAGYVSKIVGK 146
Cdd:cd16147 28 LLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGV-TNNSPPGGGYPKFWQNGLERST---LPVWLQEAGYRTAYAGK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 147 ----WHLGHRPQFHPLkhGFDEWFGSpnchFGPYdnkarpnipVYRDWEMVGRYYEEFPINLKtgEANLTQIYLQEALDF 222
Cdd:cd16147 104 ylngYGVPGGVSYVPP--GWDEWDGL----VGNS---------TYYNYTLSNGGNGKHGVSYP--GDYLTDVIANKALDF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 223 IKRQARHH-PFFLYWAVDATHAPV-------------------------YASKP---------------FLGTSQRGRYG 261
Cdd:cd16147 167 LRRAAADDkPFFLVVAPPAPHGPFtpapryanlfpnvtapprpppnnpdVSDKPhwlrrlpplnptqiaYIDELYRKRLR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 262 dAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALisapeqgGSNG-PFlcGKQTTFEGGMREPALAWWPGhVTAGQ 340
Cdd:cd16147 247 -TLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHL-------GQHRlPP--GKRTPYEEDIRVPLLVRGPG-IPAGV 315
|
330 340 350
....*....|....*....|....*....|.
gi 2217305387 341 VSHQLGSIMDLFTTSLALAGLTPPSDraIDG 371
Cdd:cd16147 316 TVDQLVSNIDLAPTILDLAGAPPPSD--MDG 344
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
49-387 |
1.24e-34 |
|
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: 133.89 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 49 WGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYttnahaRNAytpqeivGGIPDSEQ 128
Cdd:cd16152 14 WDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCF------RNG-------IPLPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 129 LLPELLKKAGYVSKIVGKWHL-GHRPQFhplkhgfdewfgspnchfgpydnkarpnipvyrdwemvgryyeefpinlktg 207
Cdd:cd16152 81 TLAHYFRDAGYETGYVGKWHLaGYRVDA---------------------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 208 eanLTQIylqeALDFIKRQARHHPFFLYWA---------VDATHAPV-YASK-----------PFLGTSQRGrYGD---A 263
Cdd:cd16152 109 ---LTDF----AIDYLDNRQKDKPFFLFLSylephhqndRDRYVAPEgSAERfanfwvppdlaALPGDWAEE-LPDylgC 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 264 VREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALISapeqggSNGPFlcgKQTTFEGGMREPALAWWPGhVTAGQVSH 343
Cdd:cd16152 181 CERLDENVGRIRDALKELGLYDNTIIVFTSDHGCHFRT------RNAEY---KRSCHESSIRVPLVIYGPG-FNGGGRVE 250
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2217305387 344 QLGSIMDLFTTSLALAGLTPPSdrAIDGLNLLPtLLQGRLMDRP 387
Cdd:cd16152 251 ELVSLIDLPPTLLDAAGIDVPE--EMQGRSLLP-LVDGKVEDWR 291
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
61-374 |
2.97e-34 |
|
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: 130.57 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 61 ETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTtnaharNAYTPQEivggIPDSEQLLPELLKKAGYV 140
Cdd:cd16153 36 ESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG------FEAAHPA----LDHGLPTFPEVLKKAGYQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 141 SKIVGKWHlghrpqfhplkhgfdewfgspnchfgpydnkarpnipvyrdwemvgryYEEFPINLKtgeaNLTQIYLQEAL 220
Cdd:cd16153 106 TASFGKSH------------------------------------------------LEAFQRYLK----NANQSYKSFWG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 221 DFIKRQARHHPFFLYWAVDATHAPVYASKPFlgtSQRGRYGDAVREIDDSIGKILELLQDLHVA---DNTFVFFTSDNGA 297
Cdd:cd16153 134 KIAKGADSDKPFFVRLSFLQPHTPVLPPKEF---RDRFDYYAFCAYGDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGW 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217305387 298 ALisapeqgGSNGpfLCGKQTTFEGGMREPALAWWPGH--VTAGQVSHQLGSIMDLFTTSLALAGLTPPSDRAIDGLNL 374
Cdd:cd16153 211 HL-------GEQG--ILAKFTFWPQSHRVPLIVVSSDKlkAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
62-365 |
5.01e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 129.39 E-value: 5.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 62 TPNLDRMAAEGLLFPNFYsANPLCSPSRAALLTGRLPIRNGFyttnaharnaytpQEIVGGIPDSEQLLPELLKK----A 137
Cdd:cd16154 28 TPTLDSLANSGIVFDNLW-ATPACSPTRATILTGKYGFRTGV-------------LAVPDELLLSEETLLQLLIKdattA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 138 GYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNchfgpydnkarPNIPVYRDWEMVgryyeefpINLKTGEAN--LTQIY 215
Cdd:cd16154 94 GYSSAVIGKWHLGGNDNSPNNPGGIPYYAGILG-----------GGVQDYYNWNLT--------NNGQTTNSTeyATTKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 216 LQEALDFIKRQarHHPFFLYWAVDATHAPVYA------SKPFLGTSQ------RGRYGDAVREIDDSIGKILELLqDLHV 283
Cdd:cd16154 155 TNLAIDWIDQQ--TKPWFLWLAYNAPHTPFHLppaelhSRSLLGDSAdieanpRPYYLAAIEAMDTEIGRLLASI-DEEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 284 ADNTFVFFTSDNGAALISAPEQGGSNGpflcGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTP 363
Cdd:cd16154 232 RENTIIIFIGDNGTPGQVVDLPYTRNH----AKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDA 307
|
..
gi 2217305387 364 PS 365
Cdd:cd16154 308 AE 309
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
52-381 |
5.41e-26 |
|
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: 110.43 E-value: 5.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 52 LGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGfyttnaHARNAyTPqeivggIPDSEQLLP 131
Cdd:cd16028 16 LSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHR------SVWNG-TP------LDARHLTLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 132 ELLKKAGYVSKIVGKWH----LGHRPQFHPLKH-------GFDewfgsPNCHFGPYdnKARPNIPVY------------- 187
Cdd:cd16028 83 LELRKAGYDPALFGYTDtspdPRGLAPLDPRLLsyelampGFD-----PVDRLDEY--PAEDSDTAFltdraieylderq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 188 -RDWEMVGRYYEEFPINLKTGEANL----TQIYLQEALDFIKRQARHHPFFlywavdATHAPVYASKPFLGTSQRGRYGD 262
Cdd:cd16028 156 dEPWFLHLSYIRPHPPFVAPAPYHAlydpADVPPPIRAESLAAEAAQHPLL------AAFLERIESLSFSPGAANAADLD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 263 A-------------VREIDDSIGKILELLQDLHVADNTFVFFTSDNGaalisapEQGGSNgpFLCGKQTTFEGGMREPAL 329
Cdd:cd16028 230 DeevaqmratylglIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG-------EQLGDH--WLWGKDGFFDQAYRVPLI 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2217305387 330 AWWPG---HVTAGQVSHQLGSIMDLFTTSLALAGLTPPSdrAIDGLNLLPtLLQG 381
Cdd:cd16028 301 VRDPRreaDATRGQVVDAFTESVDVMPTILDWLGGEIPH--QCDGRSLLP-LLAG 352
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
48-389 |
2.78e-25 |
|
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: 108.62 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 48 GWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharnaytpqeivgGIPDSE 127
Cdd:cd16156 12 RWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCM-------------ALGDNV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 128 QLLPELLKKAGYVSKIVGKWHL-GHrpqfhplkhgfdEWFGSPNCHFGpYDnkarpniPVYrdWEMVGRYYEEFP---IN 203
Cdd:cd16156 79 KTIGQRLSDNGIHTAYIGKWHLdGG------------DYFGNGICPQG-WD-------PDY--WYDMRNYLDELTeeeRR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 204 LKTGEANLTQIY------------LQEALDFIkRQARHHPFFLYWAVDATHAPVYASKPF----------LGTS------ 255
Cdd:cd16156 137 KSRRGLTSLEAEgikeeftyghrcTNRALDFI-EKHKDEDFFLVVSYDEPHHPFLCPKPYasmykdfefpKGENayddle 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 256 -----QR---GRYGDAVRE---------------IDDSIGKILELLQDLhvADNTFVFFTSDNGAALisapeqgGSNGPF 312
Cdd:cd16156 216 nkplhQRlwaGAKPHEDGDkgtikhplyfgcnsfVDYEIGRVLDAADEI--AEDAWVIYTSDHGDML-------GAHKLW 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217305387 313 LCGKqTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPsdRAIDGLNLLPTLLQGRL-MDRPIF 389
Cdd:cd16156 287 AKGP-AVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQP--KVLEGESILATIEDPEIpENRGVF 361
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
52-378 |
1.11e-22 |
|
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: 100.39 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 52 LGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTtnaharnaytpqeIVGGIPDSEQLLP 131
Cdd:cd16150 16 LGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRT-------------LHHLLRPDEPNLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 132 ELLKKAGYVSKIVGKWHLghrpqfhpLKHGFDewfgspnchFGPYdnkarpnipVYRDWEMVgryyeefpinlktgeanl 211
Cdd:cd16150 83 KTLKDAGYHVAWAGKNDD--------LPGEFA---------AEAY---------CDSDEACV------------------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 212 tqiylQEALDFIKRQARHHPFFLYWAVDATHAPVYASKPF----------------------------LGTSQRGRYGDA 263
Cdd:cd16150 119 -----RTAIDWLRNRRPDKPFCLYLPLIFPHPPYGVEEPWfsmidreklpprrppglrakgkpsmlegIEKQGLDRWSEE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 264 V-REI-----------DDSIGKILELLQDLHVADNTFVFFTSDNGaalisapEQGGSNGpfLCGK-QTTFEGGM-REPAL 329
Cdd:cd16150 194 RwRELratylgmvsrlDHQFGRLLEALKETGLYDDTAVFFFSDHG-------DYTGDYG--LVEKwPNTFEDCLtRVPLI 264
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2217305387 330 AWWPGhVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDRAidGLNLLPTL 378
Cdd:cd16150 265 IKPPG-GPAGGVSDALVELVDIPPTLLDLAGIPLSHTHF--GRSLLPVL 310
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
63-454 |
1.13e-17 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 84.52 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 63 PNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGrlpirngFYTTNAHARNAYTpqeivgGIPDSEQLLPELLKKAGYVSK 142
Cdd:cd16171 27 PYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG-------LFTHLTESWNNYK------GLDPNYPTWMDRLEKHGYHTQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 143 IVGKwhLGHRPQFHPLKHGFDEWfgspnchfgpydnkarpnipvYRDWEMVGRYyEEFPINLKTGEANLTQIYLQE---- 218
Cdd:cd16171 94 KYGK--LDYTSGHHSVSNRVEAW---------------------TRDVPFLLRQ-EGRPTVNLVGDRSTVRVMLKDwqnt 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 219 --ALDFIKRQARHH--PFFLYWAVDATHA-PVYASKPFLGTSQRGR--YGDAVREIDDSIGKILELLQDLHVADNTFVFF 291
Cdd:cd16171 150 dkAVHWIRKEAPNLtqPFALYLGLNLPHPyPSPSMGENFGSIRNIRafYYAMCAETDAMLGEIISALKDTGLLDKTYVFF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 292 TSDNGaalisapEQGGSNGPFLcgKQTTFEGGMREPALAWWPGhVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDraIDG 371
Cdd:cd16171 230 TSDHG-------ELAMEHRQFY--KMSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 372 LNLLPTLLQGRLMDRPIFYYRGDTLMAATLG--QHKAHFWTWTNSWENfrqgIDFCPGQNVSgvtthnledhtklPLIFH 449
Cdd:cd16171 298 YSLLPLLSESSIKESPSRVPHPDWVLSEFHGcnVNASTYMLRTNSWKY----IAYADGNSVP-------------PQLFD 360
|
....*
gi 2217305387 450 LGRDP 454
Cdd:cd16171 361 LSKDP 365
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
56-381 |
1.41e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 83.41 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 56 GEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTnaharnaytpqeivGGIPDSEQLLPEL-- 133
Cdd:cd16035 20 GWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDT--------------LGSPMQPLLSPDVpt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 134 ----LKKAGYVSKIVGKWHLGhrpqfhplkhgfdewfGSPNchfGPYDNKARpnipvyrdwemvgryyeefpinlktgea 209
Cdd:cd16035 86 lghmLRAAGYYTAYKGKWHLS----------------GAAG---GGYKRDPG---------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 210 nltqiYLQEALDFIKRQAR----HHPFFLywAV------DathapVYASKPFLGTSQRGR--YGDAVREIDDSIGKILEL 277
Cdd:cd16035 119 -----IAAQAVEWLRERGAknadGKPWFL--VVslvnphD-----IMFPPDDEERWRRFRnfYYNLIRDVDRQIGRVLDA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 278 LQDLHVADNTFVFFTSDNGaalisapEQGGSNGpflcGKQ---TTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTT 354
Cdd:cd16035 187 LDASGLADNTIVVFTSDHG-------EMGGAHG----LRGkgfNAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLLPT 255
|
330 340 350
....*....|....*....|....*....|.
gi 2217305387 355 SLALAGLTPPSDRAID----GLNLLPTLLQG 381
Cdd:cd16035 256 LLGLAGVDAEARATEApplpGRDLSPLLTDA 286
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
62-360 |
2.69e-14 |
|
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: 73.49 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 62 TPNLDRMAAEGLLFPNFYSANPLCSPSRA--ALLTGRLPIRNGFYTTNAHARNAYTpqeivggipdSeqlLPELLKKAGY 139
Cdd:cd16015 26 TPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLNPLP----------S---LPSILKEQGY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 140 VSKIVgkwHLGH-----RPQFHPlKHGFDEWFGspnCHFGPYDNKARPNIPVYrDWEMvgryyeefpinlktgeanltqi 214
Cdd:cd16015 93 ETIFI---HGGDasfynRDSVYP-NLGFDEFYD---LEDFPDDEKETNGWGVS-DESL---------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 215 yLQEALDFIKRQARhHPFFLY---------WAVDATHAPVYASKPFLGTSQrGRYGDAVREIDDSIGKILELLQDLHVAD 285
Cdd:cd16015 143 -FDQALEELEELKK-KPFFIFlvtmsnhgpYDLPEEKKDEPLKVEEDKTEL-ENYLNAIHYTDKALGEFIEKLKKSGLYE 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217305387 286 NTFVFFTSDNGAALISAPEQGGSNgpflcgkqttFEGGMREPALAWWPGhVTAGQVSHQLGSIMDLFTTSLALAG 360
Cdd:cd16015 220 NTIIVIYGDHLPSLGSDYDETDED----------PLDLYRTPLLIYSPG-LKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
62-375 |
1.16e-11 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 66.99 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 62 TPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGrLPIRNGFYTTNAHARNAYtpqeivggipdseQLLPELLKKAGYVS 141
Cdd:COG1368 260 TPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTG-LPPLPGGSPYKRPGQNNF-------------PSLPSILKKQGYET 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 142 KIV--GKWHLGHRPQFHPlKHGFDEWFGSPNchfgpYDNKARPNIPVYrDWEMvgryyeefpinlktgeanltqiyLQEA 219
Cdd:COG1368 326 SFFhgGDGSFWNRDSFYK-NLGFDEFYDRED-----FDDPFDGGWGVS-DEDL-----------------------FDKA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 220 LDFIKRQARhhPFFLYWAVDATHAP-----VYASKPFLGTSQRGRYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSD 294
Cdd:COG1368 376 LEELEKLKK--PFFAFLITLSNHGPytlpeEDKKIPDYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGD 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 295 NGAALisapeQGGSNGPFLCGKQTTfeggmrePALAWWPGHvTAGQVSHQLGSIMDLFTTSLALAGLTPPSDRAIdGLNL 374
Cdd:COG1368 454 HGPRS-----PGKTDYENPLERYRV-------PLLIYSPGL-KKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDL 519
|
.
gi 2217305387 375 L 375
Cdd:COG1368 520 L 520
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
217-375 |
1.60e-09 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 60.30 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 217 QEALDFIKRQARHHPFFLYWAVDATHA---PVYASKPFLGTSQRG---------------RYGDAVREIDDSIGKILELL 278
Cdd:COG3083 368 AQWLQWLDQRDSDRPWFSYLFLDAPHAysfPADYPKPFQPSEDCNylaldnesdptpfknRYRNAVHYVDSQIGRVLDTL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 279 QDLHVADNTFVFFTSDNGAALIsapEQG----GSNGPFlcGKQTTfeggmREPALAWWPGhVTAGQVSHqLGSIMDLFTT 354
Cdd:COG3083 448 EQRGLLENTIVIITADHGEEFN---ENGqnywGHNSNF--SRYQL-----QVPLVIHWPG-TPPQVISK-LTSHLDIVPT 515
|
170 180
....*....|....*....|...
gi 2217305387 355 SL--ALAGLTPPSDRAIdGLNLL 375
Cdd:COG3083 516 LMqrLLGVQNPASDYSQ-GEDLF 537
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
47-301 |
7.10e-09 |
|
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: 57.43 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 47 MGWGDLgvygEPSRETPNLDRMAAEGLLFPNFYSA-NPLCSPSRAALLTGRLPIRNGfyttnaharnaytpqeIVG-GIP 124
Cdd:pfam01663 9 FRADYL----DRFELTPNLAALAKEGVSAPNLTPVfPTLTFPNHYTLVTGLYPGSHG----------------IVGnTFY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 125 DseqllPELLKKAGYV--SKIVGKWHLGHRPQFHPLKHGFdewfgSPNCHFGPYDNKARPNIPVYRDWEMVGRYYEEFPI 202
Cdd:pfam01663 69 D-----PKTGEYLVFVisDPEDPRWWQGEPIWDTAAKAGV-----RAAALFWPGSEVDYSTYYGTPPRYLKDDYNNSVPF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 203 NLKTGEANLTQ-IYLQEALDFIKRqarhhPFFLYWAVDAThapvyaskpflGTSQRgRYG-------DAVREIDDSIGKI 274
Cdd:pfam01663 139 EDRVDTAVLQTwLDLPFADVAAER-----PDLLLVYLEEP-----------DYAGH-RYGpdspeveDALRRVDRAIGDL 201
|
250 260
....*....|....*....|....*..
gi 2217305387 275 LELLQDLHVADNTFVFFTSDNGAALIS 301
Cdd:pfam01663 202 LEALDERGLFEDTNVIVVSDHGMTPVS 228
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
59-296 |
7.97e-08 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 54.37 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 59 SRETPNLDRMAAEGLLFPNFYSANPlcS---PSRAALLTGRLPIR-----NGFYTTNAHARNAYTPQEIVGGIPDSEQLL 130
Cdd:COG1524 41 RAHAPNLAALAARGVYARPLTSVFP--SttaPAHTTLLTGLYPGEhgivgNGWYDPELGRVVNSLSWVEDGFGSNSLLPV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 131 P---ELLKKAGYVSKIVGKWHLGHRPQFhplkhgfdewfgspnchfgpydnkaRPNIPVYRDwemvGRYYeefpinlKTG 207
Cdd:COG1524 119 PtifERARAAGLTTAAVFWPSFEGSGLI-------------------------DAARPYPYD----GRKP-------LLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 208 EANLTQIYLQEALDFIKRQARHhPFFLYW-AVDAT-HapvyaskpflgtsqrgRYG-------DAVREIDDSIGKILELL 278
Cdd:COG1524 163 NPAADRWIAAAALELLREGRPD-LLLVYLpDLDYAgH----------------RYGpdspeyrAALREVDAALGRLLDAL 225
|
250
....*....|....*...
gi 2217305387 279 QDLHVADNTFVFFTSDNG 296
Cdd:COG1524 226 KARGLYEGTLVIVTADHG 243
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
61-296 |
6.39e-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: 47.96 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 61 ETPNLDRMAAEGLLFPNFYSANP-LCSPSRAALLTGRLPIR-----NGFY--TTNA--HARNAYTPQEIVGGIPdseqlL 130
Cdd:cd16018 21 LTPNLKRLAEEGVRAKYVKPVFPtLTFPNHYSIVTGLYPEShgivgNYFYdpKTNEefSDSDWVWDPWWIGGEP-----I 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 131 PELLKKAGYVSKIVgkwhlghrpqfhplkhgFdeWFGSPNCHFGPYdnkarpNIPVYRDWeMVGRYYEEFPInlktgean 210
Cdd:cd16018 96 WVTAEKAGLKTASY-----------------F--WPGSEVAIIGYN------PTPIPLGG-YWQPYNDSFPF-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 211 ltqiylQEALD-FIKRQARHHPFFLYW---AVDAT-HapvyaskpflgtsqrgRYG-------DAVREIDDSIGKILELL 278
Cdd:cd16018 142 ------EERVDtILEWLDLERPDLILLyfeEPDSAgH----------------KYGpdspevnEALKRVDRRLGYLIEAL 199
|
250
....*....|....*...
gi 2217305387 279 QDLHVADNTFVFFTSDNG 296
Cdd:cd16018 200 KERGLLDDTNIIVVSDHG 217
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
125-297 |
2.37e-05 |
|
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 46.36 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 125 DSEQLLPELLKKAGYVskivgkWHLG----HRPQFHPLKHGFDEwfgspnchfGPYDNKARP-NIPVYRDWEMVGRYYEE 199
Cdd:cd16021 76 DNCPFIWKDFKKAGYV------TAFAedwpKIGTFNYRKKGFKK---------PPTDHYLRPfWLAAEKTTSYSTKSYCT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 200 FPINLktgeanlTQIYLQEALDFIKRQaRHHPFF-LYWAVDATHapvyaskpflgtsqrgRYGDAVREIDDSIGKILELL 278
Cdd:cd16021 141 GCRPS-------HKALLDYLEDFIEAY-KDRPKFsFFWLSELTH----------------DYLNGLSLADEDLLEFLKRL 196
|
170
....*....|....*....
gi 2217305387 279 QDLHVADNTFVFFTSDNGA 297
Cdd:cd16021 197 KENGLLDNTFVIFMSDHGL 215
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
52-139 |
7.81e-04 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 41.45 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305387 52 LGVYGEPsRET-PNLDRMAAEGLLFPNFYSANPLCSPSRAALLTgrlpirngfyttnaharnAYTPQEivGGIPDSEQLL 130
Cdd:cd16017 18 MSLYGYP-RDTtPFLSKLKKNLIVFDNVISCGTSTAVSLPCMLS------------------FANREN--YDRAYYQENL 76
|
....*....
gi 2217305387 131 PELLKKAGY 139
Cdd:cd16017 77 IDLAKKAGY 85
|
|
| |
