|
Name |
Accession |
Description |
Interval |
E-value |
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
30-494 |
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: 992.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 30 PPNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 109
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 110 PQEIVGGIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKARPNIPVYRDWEMVGR 189
Cdd:cd16157 81 PQNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCHFGPYDNKAYPNIPVYRDWEMIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 190 YYEEFPINLKTGEANLTQIYLQEALDFIKRQA-RHHPFFLYWAVDATHAPVYASKPFLGTSQRGRYGDAVREIDDSIGKI 268
Cdd:cd16157 161 YYEEFKIDKKTGESNLTQIYLQEALEFIEKQHdAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 269 LELLQDLHVADNTFVFFTSDNGAALISAPEQGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTT 348
Cdd:cd16157 241 LESLKSLGIENNTFVFFSSDNGAALISAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 349 SLALAGLTPPSDRAIDGLNLLPTLLQGRLMDRPIFYYRGDTLMAATLGQHKAHFWTWTNSWENFRQGIDFCPGQNVSGVT 428
Cdd:cd16157 321 SLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGDELMAVRLGQYKAHFWTWSNSWEEFRKGINFCPGQNVPGVT 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530424707 429 THNLEDHTKLPLIFHLGRDPGERFPLSFASAEYQEALSRITSVVQQHQEALVPAQPQLNVCNWAVM 494
Cdd:cd16157 401 THNQTDHTKLPLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVVQQHQKTLVPGEPQLNVCDLAVM 466
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
30-455 |
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: 544.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 30 PPNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharnayt 109
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVG------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 110 PQEIVGGIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKARPNIPVYRDwemvGR 189
Cdd:cd16026 74 PPGSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP----PL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 190 YYEEFPINLKTGEANLTQIYLQEALDFIKRQaRHHPFFLYWAVDATHAPVYASKPFLGTSQRGRYGDAVREIDDSIGKIL 269
Cdd:cd16026 150 MENEEVIEQPADQSSLTQRYTDEAVDFIERN-KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRIL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 270 ELLQDLHVADNTFVFFTSDNGAALISaPEQGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTS 349
Cdd:cd16026 229 DALKELGLEENTLVIFTSDNGPWLEY-GGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 350 LALAGLTPPSDRAIDGLNLLPTLLQGRLMDRP--IFYYRGDTLMAATLGQHKAHFWTWTNSWENFRqgidfcpgqnvsgv 427
Cdd:cd16026 308 AALAGAPLPEDRVIDGKDISPLLLGGSKSPPHpfFYYYDGGDLQAVRSGRWKLHLPTTYRTGTDPG-------------- 373
|
410 420
....*....|....*....|....*...
gi 530424707 428 ttHNLEDHTKLPLIFHLGRDPGERFPLS 455
Cdd:cd16026 374 --GLDPTKLEPPLLYDLEEDPGETYNVA 399
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
31-460 |
2.86e-120 |
|
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: 362.52 E-value: 2.86e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTnahaRNAYTP 110
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGG----TRVFLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 QEIvGGIPDSEQLLPELLKKAGYVSKIVGKWHLG-----HRPQFH-PLKHGFD----------EWFGSPncHFGPYDNKA 174
Cdd:cd16160 78 WDI-GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDfvgtnlpftnSWACDD--TGRHVDFPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 175 RPNIPVYRDWEMVgryyeEFPINLKtgeaNLTQIYLQEALDFIKRQArHHPFFLYWAVDATHAPVYASKPFLGTSQRGRY 254
Cdd:cd16160 155 RSACFLYYNDTIV-----EQPIQHE----HLTETLVGDAKSFIEDNQ-ENPFFLYFSFPQTHTPLFASKRFKGKSKRGRY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 255 GDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALiSAPEQGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTaGQ 334
Cdd:cd16160 225 GDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHV-EYCLEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIK-PR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 335 VSHQLGSIMDLFTTSLALAGLTPPSDRAIDGLNLLPTLLQGRLMD-RPIFYYRGDTLMAATLGQHKAHFWTWTNSWENFr 413
Cdd:cd16160 303 VSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPhDDILYYCCSRLMAVRYGSYKIHFKTQPLPSQES- 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 530424707 414 QGIDFCPGQNVS-----------GVTTHNledhtkLPLIFHLGRDPGERFPLSFASAE 460
Cdd:cd16160 382 LDPNCDGGGPLSdyivcydcedeCVTKHN------PPLIFDVEKDPGEQYPLQPSVYE 433
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
30-486 |
1.68e-116 |
|
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: 355.44 E-value: 1.68e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 30 PPNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 109
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 110 PQEivGGIPDSEQLLPELLKKAGYVSKIVGKWHLG-HRPQ-----FHPLKHGFDEWFGSP-----NCHFGP---YDNKAR 175
Cdd:cd16159 81 ASS--GGLPPNETTFAEVLKQQGYSTALIGKWHLGlHCESrndfcHHPLNHGFDYFYGLPltnlkDCGDGSngeYDLSFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 176 PNIPVYRDWEMVG-----------------------------------------------RYYE--EFPINLKtgeaNLT 206
Cdd:cd16159 159 PLFPLLTAFVLITaltiflllylgavskrffvfllilsllfislfflllitnryfncilmRNHEvvEQPMSLE----NLT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 207 QIYLQEALDFIKRQaRHHPFFLYWAVDATHAPVYASKPFLGTSQRGRYGDAVREIDDSIGKILELLQDLHVADNTFVFFT 286
Cdd:cd16159 235 QRLTKEAISFLERN-KERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 287 SDNGAAL--ISA-PEQGGSNGPFLCGK-QTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDRA 362
Cdd:cd16159 314 SDNGGHLeeISVgGEYGGGNGGIYGGKkMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 363 IDGLNLLPtLLQGRLMDRP---IFYYRGDTLMAATLGQH------KAHFWTwtnswENFRQGIDFCPGQNV-----SGVT 428
Cdd:cd16159 394 IDGRDLMP-LLTGQEKRSPhefLFHYCGAELHAVRYRPRdggavwKAHYFT-----PNFYPGTEGCCGTLLcrcfgDSVT 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 530424707 429 THNledhtkLPLIFHLGRDPGERFPLSFASAEYQEALSRITSVVQQHQEALVPAQPQL 486
Cdd:cd16159 468 HHD------PPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIEPVESQL 519
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-454 |
8.82e-115 |
|
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: 345.67 E-value: 8.82e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYG---EPSRETPNLDRMAAEGLLFPNFYsANPLCSPSRAALLTGRLPIRNGFYTTnaharna 107
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFY-VEPSCTPGRAAFITGRHPIRTGLTTV------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 108 yTPQEIVGGIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGspnchfgpydnkarpNIPVYRDWEMV 187
Cdd:cd16142 73 -GLPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYG---------------NLYHTIDEEIV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 188 GRyyeefpinlktgeanltqiylqeALDFIKRQAR-HHPFFLYWAVDATHAPVYASKPFLGTSQR-GRYGDAVREIDDSI 265
Cdd:cd16142 137 DK-----------------------AIDFIKRNAKaDKPFFLYVNFTKMHFPTLPSPEFEGKSSGkGKYADSMVELDDHV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 266 GKILELLQDLHVADNTFVFFTSDNGAALISAPeqGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDL 345
Cdd:cd16142 194 GQILDALDELGIADNTIVIFTTDNGPEQDVWP--DGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDW 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 346 FTTSLALAGLTPP------SDRAIDGLNLLPTLL--QGRLMDRPIFYYRGDTLMAATLGQHKAHFwTWtnswenfrqgid 417
Cdd:cd16142 272 FPTLAALAGAPDPkdkllgKDRHIDGVDQSPFLLgkSEKSRRSEFFYFGEGELGAVRWKNWKVHF-KA------------ 338
|
410 420 430
....*....|....*....|....*....|....*..
gi 530424707 418 fcpgQNVSGVTTHNLEDHTKLPLIFHLGRDPGERFPL 454
Cdd:cd16142 339 ----QEDTGGPTGEPFYVLTFPLIFNLRRDPKERYDV 371
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
30-487 |
8.81e-111 |
|
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: 339.42 E-value: 8.81e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 30 PPNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAyt 109
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 110 pqeivGGIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQ--FHPLKHGFDEWFGSPNCH-FGPYDNKA--RPNIPVYRDW 184
Cdd:cd16158 79 -----GGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNgtYLPTHQGFDHYLGIPYSHdQGPCQNLTcfPPNIPCFGGC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 185 E--------MVGRYYEEFPINLktgeANLTQIYLQEALDFI-KRQARHHPFFLYWAVDATHAPVYASKPFLGTSQRGRYG 255
Cdd:cd16158 154 DqgevpcplFYNESIVQQPVDL----LTLEERYAKFAKDFIaDNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 256 DAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALISApEQGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTAGqV 335
Cdd:cd16158 230 DALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRK-SRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPG-V 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 336 SHQLGSIMDLFTTSLALAGLTPPsDRAIDGLNLLPTLL-QGRLMDRPIFYYRGDT-----LMAATLGQHKAHFWTwtnsw 409
Cdd:cd16158 308 THELASTLDILPTIAKLAGAPLP-NVTLDGVDMSPILFeQGKSPRQTFFYYPTSPdpdkgVFAVRWGKYKAHFYT----- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 410 enfrqgidfcPGQNVSGVTTHN-------LEDHTKlPLIFHLGRDPGERFPLSfASAEYQEALSRITSVVQQHQEALVPA 482
Cdd:cd16158 382 ----------QGAAHSGTTPDKdchpsaeLTSHDP-PLLFDLSQDPSENYNLL-GLPEYNQVLKQIQQVKERFEASMKFG 449
|
....*
gi 530424707 483 QPQLN 487
Cdd:cd16158 450 ESEIN 454
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
30-454 |
1.54e-107 |
|
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: 327.89 E-value: 1.54e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 30 PPNILLLLMDDMGWGDLGVYGEPSR-ETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFyTTNAHARNay 108
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAiLTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 109 tpqeiVGGIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHfgpydnkarpnipvyrdwemvg 188
Cdd:cd16161 78 -----VGGLPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSH---------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 189 ryyeefpinlktgEANLTQIYLQEALDFIKR-QARHHPFFLYWAVDATHAPV-YASKPFLGTSQRGRYGDAVREIDDSIG 266
Cdd:cd16161 131 -------------DSSLADRYAQFATDFIQRaSAKDRPFFLYAALAHVHVPLaNLPRFQSPTSGRGPYGDALQEMDDLVG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 267 KILELLQDLHVADNTFVFFTSDNGAALISAPEQGG-------SNGPFLCGKQTTFEGGMREPALAWWPGHVTAGQVSHQL 339
Cdd:cd16161 198 QIMDAVKHAGLKDNTLTWFTSDNGPWEVKCELAVGpgtgdwqGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAAL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 340 GSIMDLFTTSLALAGLTPPSDRAIDGLNLLPTLLQGRLMDRPIFYY------RGDTLMAATLGQHKAHFWTwtnswenfr 413
Cdd:cd16161 278 VSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHpnsgaaGAGALSAVRCGDYKAHYAT--------- 348
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 530424707 414 QGI-----DFCPGQnvsgvtthnledHTKLPLIFHLGRDPGERFPL 454
Cdd:cd16161 349 GGAlaccgSTGPKL------------YHDPPLLFDLEVDPAESFPL 382
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-410 |
5.12e-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: 293763 [Multi-domain] Cd Length: 421 Bit Score: 325.27 E-value: 5.12e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAY-- 108
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 109 ---TPQEIVGGIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSpnCHFGPYDNKARPNIPVYRDWE 185
Cdd:cd16144 81 tklIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIGG--TGNGGPPSYYFPPGKPNPDLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 186 mvgryyeefpiNLKTGEaNLTQIYLQEALDFIKRQARhHPFFLYWAVDATHAPV----------YASKPFLGTSQRG-RY 254
Cdd:cd16144 159 -----------DGPEGE-YLTDRLTDEAIDFIEQNKD-KPFFLYLSHYAVHTPIqarpeliekyEKKKKGLRKGQKNpVY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 255 GDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGaALISAPEQGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTAGQ 334
Cdd:cd16144 226 AAMIESLDESVGRILDALEELGLADNTLVIFTSDNG-GLSTRGGPPTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 335 VSHQLGSIMDLFTTSLALAGLTPPSDRAIDGLNLLPTLLQG--RLMDRPIF-----YYRGDTLMAATL--GQHKAHFWTW 405
Cdd:cd16144 305 VSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGeaDLPRRALFwhfphYHGQGGRPASAIrkGDWKLIEFYE 384
|
....*
gi 530424707 406 TNSWE 410
Cdd:cd16144 385 DGRVE 389
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
13-479 |
1.44e-102 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 315.28 E-value: 1.44e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 13 LLLVLSAAGMGASGAPQPPNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLP 92
Cdd:COG3119 6 LLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 93 IRNGFYTTNAHARnaytpqeivGGIPDSEQLLPELLKKAGYVSKIVGKWHLghrpqfhplkhgfdewfgspnchfgpydn 172
Cdd:COG3119 86 HRTGVTDNGEGYN---------GGLPPDEPTLAELLKEAGYRTALFGKWHL----------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 173 karpnipvyrdwemvgryyeefpinlktgeaNLTQIYLQEALDFIKRQARH-HPFFLYWAVDATHAPVYASKPFLG---- 247
Cdd:COG3119 128 -------------------------------YLTDLLTDKAIDFLERQADKdKPFFLYLAFNAPHAPYQAPEEYLDkydg 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 248 -------------------TSQRGRYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALisaPEQGgsngpFLC 308
Cdd:COG3119 177 kdiplppnlaprdlteeelRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSL---GEHG-----LRG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 309 GKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDraIDGLNLLPTLLQGRLMDRPIFYY--- 385
Cdd:COG3119 249 GKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWeyp 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 386 RGDTLMAATLGQHKAHFWtwtnswenfrqgidfcpgqnvsgvttHNLEDHTKLpliFHLGRDPGERFPLsfaSAEYQEAL 465
Cdd:COG3119 327 RGGGNRAIRTGRWKLIRY--------------------------YDDDGPWEL---YDLKNDPGETNNL---AADYPEVV 374
|
490
....*....|....
gi 530424707 466 SRITSVVQQHQEAL 479
Cdd:COG3119 375 AELRALLEAWLKEL 388
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-410 |
4.30e-98 |
|
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: 304.52 E-value: 4.30e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTG----RLPIRngfyttnaharn 106
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGlhtgHTRVR------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 107 AYTPQEIVGGIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQF-HPLKHGFDEWFGSPN---CHFG--PY--DNKARPNI 178
Cdd:cd16145 69 GNSEPGGQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYGYLDqvhAHNYypEYlwRNGEKVPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 179 PvyrdwEMVGRYYEEFPINLKTGEANLTQIYLQEALDFIKRQaRHHPFFLYWAVDATHAPV------YASKPFLGTSQRG 252
Cdd:cd16145 149 P-----NNVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIREN-KDKPFFLYLAYTLPHAPLqvpddgPYKYKPKDPGIYA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 253 ---------RYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALISAPEQGG----SNGPFLCGKQTTFEGGMR 319
Cdd:cd16145 223 ylpwpqpekAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSEGGSEHDPdffdSNGPLRGYKRSLYEGGIR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 320 EPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDraIDGLNLLPTLLQGRL--MDRPIFY--YRGDTLMAATL 395
Cdd:cd16145 303 VPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQqqQHDYLYWefYEGGGAQAVRM 380
|
410
....*....|....*.
gi 530424707 396 GQHKA-HFWTWTNSWE 410
Cdd:cd16145 381 GGWKAvRHGKKDGPFE 396
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
31-470 |
1.02e-89 |
|
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: 282.52 E-value: 1.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYsANPLCSPSRAALLTGRLPIRNGFYTTnaharnaytp 110
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFH-VSPVCAPTRAALLTGRYPFRTGVWHT---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 qeIVGG--IPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFG---PYDNKARPNIPVYRDWE 185
Cdd:cd16146 70 --ILGRerMRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGGGIGqypDYWGNDYFDDTYYHNGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 186 MVGryYEEFpinlktgeanLTQIYLQEALDFIKRQaRHHPFFLYWAVDATHAPVYA----SKPF----LGTSQRGRYGdA 257
Cdd:cd16146 148 FVK--TEGY----------CTDVFFDEAIDFIEEN-KDKPFFAYLATNAPHGPLQVpdkyLDPYkdmgLDDKLAAFYG-M 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 258 VREIDDSIGKILELLQDLHVADNTFVFFTSDNGAAlisapeqGGSNGPFLCG----KQTTFEGGMREPALAWWPGHVTAG 333
Cdd:cd16146 214 IENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPA-------GGVPKRFNAGmrgkKGSVYEGGHRVPFFIRWPGKILAG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 334 QVSHQLGSIMDLFTTSLALAGLTPPSDRAIDGLNLLPTLLQGRLM--DRPIFYYRGDTLMAAtlgQHKAHFWTWTNSWen 411
Cdd:cd16146 287 KDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPwpERTLFTHSGRWPPPP---KKKRNAAVRTGRW-- 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 530424707 412 frqgidfcpgqnvsgvttHNLEDHTKLPLIFHLGRDPGERFPLsfaSAEYQEALSRITS 470
Cdd:cd16146 362 ------------------RLVSPKGFQPELYDIENDPGEENDV---ADEHPEVVKRLKA 399
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-451 |
1.60e-89 |
|
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: 281.40 E-value: 1.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSR-ETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIR--NGFYTTNAHARNA 107
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRsrLKGGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 108 ytpqeivggIPDSEQLLPELLKKAGYVSKIVGKWHLG---------HRPQFH-------------PLKHGFDEWFGSPNC 165
Cdd:cd16143 81 ---------IEPDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkKAATGTgkdvdyskpikggPLDHGFDYYFGIPAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 166 HFGPYdnkarpnipvyrdwemvgryyeefpinlktgeanLTQiylqEALDFIKRQARH-HPFFLYWAVDATHAPVYASKP 244
Cdd:cd16143 152 EVLPT----------------------------------LTD----KAVEFIDQHAKKdKPFFLYFALPAPHTPIVPSPE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 245 FLGTSQRGRYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGA---ALISAPEQGG--SNGPFLCGKQTTFEGGMR 319
Cdd:cd16143 194 FQGKSGAGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPspyADYKELEKFGhdPSGPLRGMKADIYEGGHR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 320 EPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDRAIDGLNLLPTLL-QGRLMDRP-IFYYRGDTLMAATLGQ 397
Cdd:cd16143 274 VPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLgPKKQEVREsLVHHSGNGSFAIRKGD 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 530424707 398 HKahfwtwtnswenfrqgidFCPGQNVSGVTTHNLEDHTKLPLI--FHLGRDPGER 451
Cdd:cd16143 354 WK------------------LIDGTGSGGFSYPRGKEKLGLPPGqlYNLSTDPGES 391
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
31-367 |
1.48e-86 |
|
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: 268.15 E-value: 1.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHArnaytp 110
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 qeivGGIPDSEQLLPELLKKAGYVSKIVGKWHlghrpqfhplkhgfdewfgspnchfgpydnkarpnipvyrdwemvgry 190
Cdd:cd16022 75 ----GGLPPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 191 yeefpinlktgeanltqiylQEALDFIKRQARHHPFFLYWAVDATHAPVYaskpflgtsqrgrYGDAVREIDDSIGKILE 270
Cdd:cd16022 103 --------------------DEAIDFIERRDKDKPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILD 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 271 LLQDLHVADNTFVFFTSDNGAALisapEQGGSNGpflcGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSL 350
Cdd:cd16022 150 ALEELGLLDNTLIVFTSDHGDML----GDHGLRG----KKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLL 221
|
330
....*....|....*..
gi 530424707 351 ALAGLTPPsdRAIDGLN 367
Cdd:cd16022 222 DLAGIEPP--EGLDGRS 236
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
31-355 |
2.94e-86 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 269.68 E-value: 2.94e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTnaharnaytp 110
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 qeIVGGIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKARPNIPVyrdwemVGRY 190
Cdd:pfam00884 71 --TPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNCS------GGGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 191 YeefpinlktgeanlTQIYLQEALDFIKRQARhhPFFLYWAVDATHAPVYASKPFLGT------------SQRGRYGDAV 258
Cdd:pfam00884 143 S--------------DEALLDEALEFLDNNDK--PFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscseeQLLNSYDNTL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 259 REIDDSIGKILELLQDLHVADNTFVFFTSDNGAALisapeqGGSNGPFLCGKQ-TTFEGGMREPALAWWPGHVTAGQVSH 337
Cdd:pfam00884 207 LYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESL------GEGGGYLHGGKYdNAPEGGYRVPLLIWSPGGKAKGQKSE 280
|
330
....*....|....*...
gi 530424707 338 QLGSIMDLFTTSLALAGL 355
Cdd:pfam00884 281 ALVSHVDLFPTILDLAGI 298
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
31-376 |
3.29e-86 |
|
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: 272.89 E-value: 3.29e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSaNPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYtp 110
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYV-QPICTPSRAALMTGRYPIHTGMQHGVILAGEPY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 qeivgGIPDSEQLLPELLKKAGYVSKIVGKWHLGH-RPQFHPLKHGFDEWFGSPNCHFGPYDNKARPnipvYRDWEMVGR 189
Cdd:cd16029 78 -----GLPLNETLLPQYLKELGYATHLVGKWHLGFyTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGG----ANDYGNDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 190 YYEEFPINLKTGEaNLTQIYLQEALDFIKRQARHHPFFLYWAVDATHAPVYASKPFLG----------TSQRGRYGDAVR 259
Cdd:cd16029 149 RDNEEPAWDYNGT-YSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADpyedkfahikDEDRRTYAAMVS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 260 EIDDSIGKILELLQDLHVADNTFVFFTSDNGAALISAPeqGGSNGPFLCGKQTTFEGGMREPALAWWPG-HVTAGQVSHQ 338
Cdd:cd16029 228 ALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGD--GGSNYPLRGGKNTLWEGGVRVPAFVWSPLlPPKRGTVSDG 305
|
330 340 350
....*....|....*....|....*....|....*...
gi 530424707 339 LGSIMDLFTTSLALAGLTPPSDRAIDGLNLLPTLLQGR 376
Cdd:cd16029 306 LMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGA 343
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-454 |
5.98e-77 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 248.28 E-value: 5.98e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYsANPLCSPSRAALLTGRLPIRNGfyttnaharnaytp 110
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNY-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 qeIVGGIPDSEQL-LPELLKKAGYVSKIVGKWHLGHRPQF--HPLKHGFDEWfgspnCHFGPYDNKARPNIPVYRDWEMv 187
Cdd:cd16151 66 --VVFGYLDPKQKtFGHLLKDAGYATAIAGKWQLGGGRGDgdYPHEFGFDEY-----CLWQLTETGEKYSRPATPTFNI- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 188 gryyeefpINLKTGEANLTQ----IYLQEALDFIKRQaRHHPFFLYWAVDATHAPVYA------SKPFLGTSQR--GRYG 255
Cdd:cd16151 138 --------RNGKLLETTEGDygpdLFADFLIDFIERN-KDQPFFAYYPMVLVHDPFVPtpdspdWDPDDKRKKDdpEYFP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 256 DAVREIDDSIGKILELLQDLHVADNTFVFFTSDNG-AALISAPEQGGS-NGpflcGKQTTFEGGMREPALAWWPGHVTAG 333
Cdd:cd16151 209 DMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGtHRPITSRTNGREvRG----GKGKTTDAGTHVPLIVNWPGLIPAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 334 QVSHQLGSIMDLFTTSLALAGLTPPSDRAIDGLNLLPTLL--QGRLMDRPIFYYrgdtlmAATLGQHKAHFWTWTNSWen 411
Cdd:cd16151 285 GVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLgkTGSPRREWIYWY------YRNPHKKFGSRFVRTKRY-- 356
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 530424707 412 frqgidfcpgqnvsgvtthNLEDHTKLpliFHLGRDPGERFPL 454
Cdd:cd16151 357 -------------------KLYADGRF---FDLREDPLEKNPL 377
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
29-410 |
1.32e-72 |
|
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293749 [Multi-domain] Cd Length: 402 Bit Score: 237.73 E-value: 1.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 29 QPPNILLLLMDDMGWGDLGVYGEPSReTPNLDRMAAEGLLFPNFYsANPLCSPSRAALLTGRLPIRNGF--YTTNAHARN 106
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEIP-TPNLDALAAEGLRFTNFH-TTALCSPTRAALLTGRNHHQVGMgtMAELATGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 107 AYTpqeivGGIPDSEQLLPELLKKAGYVSKIVGKWHLGHrPQFHplkhgfdewfgspnchfgpydnkarpnipvyrdwem 186
Cdd:cd16025 79 GYE-----GYLPDSAATIAEVLKDAGYHTYMSGKWHLGP-DDYY------------------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 187 vgryyeefpinlktgeanLTQIYLQEALDFIKRQARHH-PFFLYWAVDATHAPVYASKPFLgTSQRGRYG---DAVRE-- 260
Cdd:cd16025 117 ------------------STDDLTDKAIEYIDEQKAPDkPFFLYLAFGAPHAPLQAPKEWI-DKYKGKYDagwDALREer 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 261 --------------------------------------------------IDDSIGKILELLQDLHVADNTFVFFTSDNG 290
Cdd:cd16025 178 lerqkelglipadtkltprppgvpawdslspeekklearrmevyaamvehMDQQIGRLIDYLKELGELDNTLIIFLSDNG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 291 AalisAPEQG---GSNGPFLCGKQTTFEGGMREPALAWWPGHVTA-GQVSHQLGSIMDLFTTSLALAGLTPPSDR----- 361
Cdd:cd16025 258 A----SAEPGwanASNTPFRLYKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHVIDIAPTILELAGVEYPKTVngvpq 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 362 -AIDGLNLLPTLL--QGRLMDRPIFY--------YRGDtLMAATLgqHKAhfWTWTNSWE 410
Cdd:cd16025 334 lPLDGVSLLPTLDgaAAPSRRRTQYFelfgnraiRKGG-WKAVAL--HPP--PGWGDQWE 388
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
31-380 |
8.75e-72 |
|
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: 234.71 E-value: 8.75e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWgDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGfytTNAHARNAYTP 110
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNG---AHGLRSRGFPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 qeivggiPDSEQLLPELLKKAGYVSKIVGKWHlghrpqfhplkHGFDEwfgspncHFGPYDNKARPNIPVYRDWEmvgry 190
Cdd:cd16027 77 -------PDGVKTLPELLREAGYYTGLIGKTH-----------YNPDA-------VFPFDDEMRGPDDGGRNAWD----- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 191 yeefpinlktgeanltqiYLQEALDFIKRQARHHPFFLYWAVDATHAPVYASKPFLGT-------------------SQR 251
Cdd:cd16027 127 ------------------YASNAADFLNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGydpekvkvppylpdtpevrEDL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 252 GRYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALisapeqggsngPFlcGKQTTFEGGMREPALAWWPGHVT 331
Cdd:cd16027 189 ADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPF-----------PR--AKGTLYDSGLRVPLIVRWPGKIK 255
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 530424707 332 AGQVSHQLGSIMDLFTTSLALAGLTPPSDraIDGLNLLPTLLQGRLMDR 380
Cdd:cd16027 256 PGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGR 302
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
29-386 |
6.93e-68 |
|
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: 226.26 E-value: 6.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 29 QPPNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGfYTTNAHarnay 108
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHG-VTDNNG----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 109 tpqeivGGIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPlkHGFDEWFGSP-NCHFGPYDNKarpnipvyrdwEMV 187
Cdd:cd16031 75 ------PLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPP--PGFDYWVSFPgQGSYYDPEFI-----------ENG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 188 GRYYEEFPInlktgeanlTQIYLQEALDFIKRQARHHPFFLYWAVDATHAP-------------------------VYAS 242
Cdd:cd16031 136 KRVGQKGYV---------TDIITDKALDFLKERDKDKPFCLSLSFKAPHRPftpaprhrglyedvtipepetfdddDYAG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 243 KPFLGTSQRGR---------------------YGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALisapeqgG 301
Cdd:cd16031 207 RPEWAREQRNRirgvldgrfdtpekyqrymkdYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL-------G 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 302 SNGpfLCGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDraIDGLNLLPtLLQGRLMD-- 379
Cdd:cd16031 280 EHG--LFDKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLP-LLEGEKPVdw 354
|
....*..
gi 530424707 380 RPIFYYR 386
Cdd:cd16031 355 RKEFYYE 361
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-376 |
1.45e-59 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 203.18 E-value: 1.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHarnaytp 110
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 qeivggIPDSEQLLPELLKKAGYVSKIVGKWHL-GHRPQFH---------PLKHGFDEWFGSPNC--HFGPYDNKARPNI 178
Cdd:cd16034 75 ------LPPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGraddytpppERRHGFDYWKGYECNhdHNNPHYYDDDGKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 179 PVYRDWEmvgryyeefPInlktGEANLtqiylqeALDFIKRQA-RHHPFFLYWAVDATHAPvYASKP------------- 244
Cdd:cd16034 149 IYIKGYS---------PD----AETDL-------AIEYLENQAdKDKPFALVLSWNPPHDP-YTTAPeeyldmydpkkll 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 245 -------------FLGTSQRGRYGdAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGaalisapEQGGSNGpfLCGKQ 311
Cdd:cd16034 208 lrpnvpedkkeeaGLREDLRGYYA-MITALDDNIGRLLDALKELGLLENTIVVFTSDHG-------DMLGSHG--LMNKQ 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530424707 312 TTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDraIDGLNLLPTLLQGR 376
Cdd:cd16034 278 VPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGK 340
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
31-353 |
1.32e-57 |
|
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: 192.64 E-value: 1.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFpNFYSANPLCS--PSRAALLTGRLPIRNGFYTTNAHARnay 108
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATF-NFRSVSPPTSsaPNHAALLTGAYPTLHGYTGNGSADP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 109 TPQEIVGGIPDSEQLLPELLKKAGYVSKIVGkwhlghrpqfhplkhgfdewfgspnchfgpydnkarpnipvyrdwemvg 188
Cdd:cd00016 77 ELPSRAAGKDEDGPTIPELLKQAGYRTGVIG------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 189 ryyeefpinlktgeanltqiylqeALDFIKRQARHHPFFLYWAVDATHAPVYASKPflgtsQRGRYGDAVREIDDSIGKI 268
Cdd:cd00016 108 ------------------------LLKAIDETSKEKPFVLFLHFDGPDGPGHAYGP-----NTPEYYDAVEEIDERIGKV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 269 LELLQDLHVADNTFVFFTSDNGAALISAPEQggsngPFLCGKQTTFEGGMREPALAWWPGHVtAGQVSHQLGSIMDLFTT 348
Cdd:cd00016 159 LDALKKAGDADDTVIIVTADHGGIDKGHGGD-----PKADGKADKSHTGMRVPFIAYGPGVK-KGGVKHELISQYDIAPT 232
|
....*
gi 530424707 349 SLALA 353
Cdd:cd00016 233 LADLL 237
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-398 |
3.49e-54 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 189.35 E-value: 3.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTtnaharNAYTP 110
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLN------NVENA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 QEIVGGIPDSEQLLPELLKKAGYVSKIVGKWHLGhrPQFHPLKHGFDEWFgsPNCHFGPYDnkarpnipvyrdwemvgry 190
Cdd:cd16033 75 GAYSRGLPPGVETFSEDLREAGYRNGYVGKWHVG--PEETPLDYGFDEYL--PVETTIEYF------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 191 yeefpinlktgeanltqiYLQEALDFIKR-QARHHPFFLYWAVDATHAPVYASKPFL----------------------G 247
Cdd:cd16033 132 ------------------LADRAIEMLEElAADDKPFFLRVNFWGPHDPYIPPEPYLdmydpediplpesfaddfedkpY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 248 TSQRGR-------------------YGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALISapeQGGSN-GPFL 307
Cdd:cd16033 194 IYRRERkrwgvdtedeedwkeiiahYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGA---HRLWDkGPFM 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 308 cgkqttFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPsdRAIDGLNLLPTLLQGRLMDRPifyyrg 387
Cdd:cd16033 271 ------YEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVP--PKVDGRSLLPLLRGEQPEDWR------ 336
|
410
....*....|.
gi 530424707 388 DTLMAATLGQH 398
Cdd:cd16033 337 DEVVTEYNGHE 347
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-370 |
2.55e-53 |
|
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: 182.05 E-value: 2.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTP 110
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 QEIvgGIPDSEQLLPELLKKAGYVSKIVGKWHLGhrpqfhplkhgfdewfgspnchfgpydnkarpnipvyrdwemvgry 190
Cdd:cd16149 81 KPE--GYLEGQTTLPEVLQDAGYRCGLSGKWHLG---------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 191 yeefpinlktgeanltqiylQEALDF-IKRQARHHPFFLYWAVDATHAPvyaskpflgtsqrGRYGDAVREIDDSIGKIL 269
Cdd:cd16149 113 --------------------DDAADFlRRRAEAEKPFFLSVNYTAPHSP-------------WGYFAAVTGVDRNVGRLL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 270 ELLQDLHVADNTFVFFTSDNGAALisapeqgGSNGPFlcGK------QTTFEGGMREPALAWWPGHVTAGQVSHQLGSIM 343
Cdd:cd16149 160 DELEELGLTENTLVIFTSDNGFNM-------GHHGIW--GKgngtfpLNMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAY 230
|
330 340
....*....|....*....|....*..
gi 530424707 344 DLFTTSLALAGLTPPSDRAIDGLNLLP 370
Cdd:cd16149 231 DFFPTLLELAGVDPPADPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-383 |
1.07e-48 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 171.96 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYtTNAHArnaytp 110
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVW-DNADP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 qeivggIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQFhplkHGFDewfgspnchfgpYDnkarpnipvyrdwEMVgry 190
Cdd:cd16037 74 ------YDGDVPSWGHALRAAGYETVLIGKLHFRGEDQR----HGFR------------YD-------------RDV--- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 191 yeefpinlktgeanltqiyLQEALDFIKRQARH-HPFFLYWAVDATHAPVYASKPFLG----TSQRGRYGdAVREIDDSI 265
Cdd:cd16037 116 -------------------TEAAVDWLREEAADdKPWFLFVGFVAPHFPLIAPQEFYDlyvrRARAAYYG-LVEFLDENI 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 266 GKILELLQDLHVADNTFVFFTSDNGaalisapEQGGSNGpfLCGKQTTFEGGMREPALAWWPGhVTAGQVSHQLGSIMDL 345
Cdd:cd16037 176 GRVLDALEELGLLDNTLIIYTSDHG-------DMLGERG--LWGKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDL 245
|
330 340 350
....*....|....*....|....*....|....*...
gi 530424707 346 FTTSLALAGLTPPSDRaiDGLNLLPTLLQGRLMDRPIF 383
Cdd:cd16037 246 APTILEAAGAPPPPDL--DGRSLLPLAEGPDDPDRVVF 281
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-470 |
1.35e-46 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 167.74 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANP----LCSPSRAALLTGrlpiRNGFYTTNAHARN 106
Cdd:cd16155 3 PNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGwsgaVCVPSRAMLMTG----RTLFHAPEGGKAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 107 aytpqeivggIPDSEQLLPELLKKAGYVSKIVGKWHLGHrpqfhplkhgfdewfgspnchfgpydnkarpnipvyrdwem 186
Cdd:cd16155 79 ----------IPSDDKTWPETFKKAGYRTFATGKWHNGF----------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 187 vgryyeefpinlktgeANltqiylqEALDFIKRQARH-HPFFLYWAVDATHAPVYASKPFL------------------- 246
Cdd:cd16155 108 ----------------AD-------AAIEFLEEYKDGdKPFFMYVAFTAPHDPRQAPPEYLdmyppetiplpenflpqhp 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 247 -----------------GTS-----QRGRYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALisapeqgGSNG 304
Cdd:cd16155 165 fdngegtvrdeqlapfpRTPeavrqHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAV-------GSHG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 305 pfLCGKQTTFEGGMREPALAWWPGhVTAGQVSHQLGSIMDLFTTSLALAGLTPPSdrAIDGLNLLPtLLQG---RLMDRP 381
Cdd:cd16155 238 --LMGKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPE--SVEGKSLLP-VIRGekkAVRDTL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 382 IFYYRGDTLMAATlGQHKahfwtwtnswenfrqGIDFCPGQnvsgvtthnleDHTKLpliFHLGRDPGERFPLSfASAEY 461
Cdd:cd16155 312 YGAYRDGQRAIRD-DRWK---------------LIIYVPGV-----------KRTQL---FDLKKDPDELNNLA-DEPEY 360
|
....*....
gi 530424707 462 QEALSRITS 470
Cdd:cd16155 361 QERLKKLLA 369
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-370 |
9.79e-45 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 159.64 E-value: 9.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMD----DMgwgdLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYttnaharn 106
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 107 aytpqeiVGGIPDSEQLLPELLKKAGYVSKIVGKW-HLGHRPQFHplkHGFDEWfgspncHFGPYDNKARPNIPVYRDWE 185
Cdd:cd16148 69 -------GGPLEPDDPTLAEILRKAGYYTAAVSSNpHLFGGPGFD---RGFDTF------EDFRGQEGDPGEEGDERAER 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 186 MVgryyeefpinlktgeanltqiylQEALDFIKRQARHHPFFLYWAVDATHAPvYaskpflgtsqrgRYGDAVREIDDSI 265
Cdd:cd16148 133 VT-----------------------DRALEWLDRNADDDPFFLFLHYFDPHEP-Y------------LYDAEVRYVDEQI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 266 GKILELLQDLHVADNTFVFFTSDNGAALisapeqgGSNGpFLCGKQTTF-EGGMREPALAWWPGhVTAGQVSHQLGSIMD 344
Cdd:cd16148 177 GRLLDKLKELGLLEDTLVIVTSDHGEEF-------GEHG-LYWGHGSNLyDEQLHVPLIIRWPG-KEPGKRVDALVSHID 247
|
330 340
....*....|....*....|....*.
gi 530424707 345 LFTTSLALAGLTPPSDraIDGLNLLP 370
Cdd:cd16148 248 IAPTLLDLLGVEPPDY--SDGRSLLP 271
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
29-372 |
3.40e-40 |
|
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: 151.57 E-value: 3.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 29 QPPNILLLLMDDMG-WgdLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNA 107
Cdd:cd16030 1 KKPNVLFIAVDDLRpW--LGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 108 ytpqeivggIPDSeQLLPELLKKAGYVSKIVGK-WHlGHRPQFHPLKHGFDEWFGSPncHFGPYDNKARPNIPVYRDWEM 186
Cdd:cd16030 79 ---------APDA-VTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPP--GPEKYPPGKLCPGKKGGKGGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 187 VGRYYEEFPInlkTGEANLTQIYLQEALDFIKRQARHH-PFFL----------------YW------------AVDATHA 237
Cdd:cd16030 146 GGPAWEAADV---PDEAYPDGKVADEAIEQLRKLKDSDkPFFLavgfykphlpfvapkkYFdlyplesiplpnPFDPIDL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 238 PVYASKPFLGTSQRGRYGD------------------------AVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAAL 293
Cdd:cd16030 223 PEVAWNDLDDLPKYGDIPAlnpgdpkgplpdeqarelrqayyaSVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHL 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530424707 294 isapeqgGSNGPFlcGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDraIDGLNLLPTL 372
Cdd:cd16030 303 -------GEHGHW--GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPPC--LEGKSLVPLL 370
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
31-381 |
5.07e-40 |
|
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: 148.50 E-value: 5.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYtTNAHARNAYTP 110
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAY-DNAAEFPADIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 QeivggipdseqlLPELLKKAGYVSKIVGKWHL-GhrPQFHplkHGFDewfgspnchfgpYDnkarpnipvyrdwEMVGR 189
Cdd:cd16032 80 T------------FAHYLRAAGYRTALSGKMHFvG--PDQL---HGFD------------YD-------------EEVAF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 190 yyeefpinlktgeanltqiylqEALDFIKRQARHH---PFFLywAVDAT--HAPVYASKPFLG----TSQRGRYGdAVRE 260
Cdd:cd16032 118 ----------------------KAVQKLYDLARGEdgrPFFL--TVSFThpHDPYVIPQEYWDlyvrRARRAYYG-MVSY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 261 IDDSIGKILELLQDLHVADNTFVFFTSDNGAALisapeqgGSNGpfLCGKQTTFEGGMREPALAWWPGHVTAGQVShQLG 340
Cdd:cd16032 173 VDDKVGQLLDTLERTGLADDTIVIFTSDHGDML-------GERG--LWYKMSFFEGSARVPLIISAPGRFAPRRVA-EPV 242
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 530424707 341 SIMDLFTTSLALAGL-TPPSDRAIDGLNLLPtLLQGRLMDRP 381
Cdd:cd16032 243 SLVDLLPTLVDLAGGgTAPHVPPLDGRSLLP-LLEGGDSGGE 283
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
27-475 |
5.91e-40 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 152.13 E-value: 5.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 27 APQPPNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARN 106
Cdd:PRK13759 3 QTKKPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVPW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 107 AYTPQeivggipdseqlLPELLKKAGYVSKIVGKWHlghrpqFHP--LKHGFDE-WFGSPNCHFGPYDNKARPN-IPVYR 182
Cdd:PRK13759 83 NYKNT------------LPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHNvLLHDGYLHSGRNEDKSQFDfVSDYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 183 DW---EMVGRYYEEFPINLK---------TGEANL--TQIYLQEALDFIKRQARHHPFFLYWAVDATHAP---------V 239
Cdd:PRK13759 145 AWlreKAPGKDPDLTDIGWDcnswvarpwDLEERLhpTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSPydppkryfdM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 240 Y----ASKPFLGT----------------------------SQRGRYGDaVREIDDSIGKILELLQDLHVADNTFVFFTS 287
Cdd:PRK13759 225 YkdadIPDPHIGDweyaedqdpeggsidalrgnlgeeyarrARAAYYGL-ITHIDHQIGRFLQALKEFGLLDNTIILFVS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 288 DNGaalisapEQGGSNGPFLcgKQTTFEGGMREPALAWWPGHVTA---GQVSHQLGSIMDLFTTSLALAGLTPPSDraID 364
Cdd:PRK13759 304 DHG-------DMLGDHYLFR--KGYPYEGSAHIPFIIYDPGGLLAgnrGTVIDQVVELRDIMPTLLDLAGGTIPDD--VD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 365 GLNLLPTLLQGRLMDRPIFY----YRGDTLMAATLGQHKAHFWTWTNSWEnfrqgidfcpgqnvsgvtthnledhtklpl 440
Cdd:PRK13759 373 GRSLKNLIFGQYEGWRPYLHgehaLGYSSDNYLTDGKWKYIWFSQTGEEQ------------------------------ 422
|
490 500 510
....*....|....*....|....*....|....*
gi 530424707 441 IFHLGRDPGERFPLSfASAEYQEALSRITSVVQQH 475
Cdd:PRK13759 423 LFDLKKDPHELHNLS-PSEKYQPRLREMRKKLVDH 456
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-359 |
1.09e-39 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 148.65 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSR--ETPNLDRMAAEGLLFPNFYsANPLCSPSRAALLTGRLPIRNGFyttnaharnay 108
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFDNLW-ATPACSPTRATILTGKYGFRTGV----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 109 tpQEIVGGIPDSEQLLPELLKK----AGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNchfgpydnkarPNIPVYRDW 184
Cdd:cd16154 69 --LAVPDELLLSEETLLQLLIKdattAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGILG-----------GGVQDYYNW 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 185 EMVgryyeefpINLKTGEAN--LTQIYLQEALDFIKRQarHHPFFLYWAVDATHAPVYA------SKPFLGTSQ------ 250
Cdd:cd16154 136 NLT--------NNGQTTNSTeyATTKLTNLAIDWIDQQ--TKPWFLWLAYNAPHTPFHLppaelhSRSLLGDSAdieanp 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 251 RGRYGDAVREIDDSIGKILELLqDLHVADNTFVFFTSDNGAALISAPEQGGSNGpflcGKQTTFEGGMREPALAWWPGHV 330
Cdd:cd16154 206 RPYYLAAIEAMDTEIGRLLASI-DEEERENTIIIFIGDNGTPGQVVDLPYTRNH----AKGSLYEGGINVPLIVSGAGVE 280
|
330 340
....*....|....*....|....*....
gi 530424707 331 TAGQVSHQLGSIMDLFTTSLALAGLTPPS 359
Cdd:cd16154 281 RANERESALVNATDLYATIAELAGVDAAE 309
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
30-365 |
1.45e-39 |
|
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: 148.85 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 30 PPNILLLLMDDMGWGDLGVYGEPsretPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFyTTNAHARNAYT 109
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMP----KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGV-TNNSPPGGGYP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 110 PQEIVGGIPDSeqlLPELLKKAGYVSKIVGK----WHLGHRPQFHPLkhGFDEWFGSpnchFGPYdnkarpnipVYRDWE 185
Cdd:cd16147 76 KFWQNGLERST---LPVWLQEAGYRTAYAGKylngYGVPGGVSYVPP--GWDEWDGL----VGNS---------TYYNYT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 186 MVGRYYEEFPINLKtgEANLTQIYLQEALDFIKRQARHH-PFFLYWAVDATHAPV------------------------- 239
Cdd:cd16147 138 LSNGGNGKHGVSYP--GDYLTDVIANKALDFLRRAAADDkPFFLVVAPPAPHGPFtpapryanlfpnvtapprpppnnpd 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 240 YASKP---------------FLGTSQRGRYGdAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALisapeqgGSNG 304
Cdd:cd16147 216 VSDKPhwlrrlpplnptqiaYIDELYRKRLR-TLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHL-------GQHR 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530424707 305 -PFlcGKQTTFEGGMREPALAWWPGhVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDraIDG 365
Cdd:cd16147 288 lPP--GKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPSD--MDG 344
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-368 |
2.05e-38 |
|
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: 142.51 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEP------SR----ETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTt 100
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNAhtgkseSRlgyvESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 101 naharNAYTPQEivggIPDSEQLLPELLKKAGYVSKIVGKWHlghrpqfhplkhgfdewfgspnchfgpydnkarpnipv 180
Cdd:cd16153 81 -----FEAAHPA----LDHGLPTFPEVLKKAGYQTASFGKSH-------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 181 yrdwemvgryYEEFPINLKtgeaNLTQIYLQEALDFIKRQARHHPFFLYWAVDATHAPVYASKPFlgtSQRGRYGDAVRE 260
Cdd:cd16153 114 ----------LEAFQRYLK----NANQSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEF---RDRFDYYAFCAY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 261 IDDSIGKILELLQDLHVA---DNTFVFFTSDNGAALisapeqgGSNGpfLCGKQTTFEGGMREPALAWWPGH--VTAGQV 335
Cdd:cd16153 177 GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHL-------GEQG--ILAKFTFWPQSHRVPLIVVSSDKlkAPAGKV 247
|
330 340 350
....*....|....*....|....*....|...
gi 530424707 336 SHQLGSIMDLFTTSLALAGLTPPSDRAIDGLNL 368
Cdd:cd16153 248 RHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-381 |
7.00e-38 |
|
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: 143.52 E-value: 7.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 30 PPNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYttnahaRNAyt 109
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCF------RNG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 110 pqeivGGIPDSEQLLPELLKKAGYVSKIVGKWHL-GHRPQFhplkhgfdewfgspnchfgpydnkarpnipvyrdwemvg 188
Cdd:cd16152 73 -----IPLPADEKTLAHYFRDAGYETGYVGKWHLaGYRVDA--------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 189 ryyeefpinlktgeanLTQIylqeALDFIKRQARHHPFFLYWA---------VDATHAPV-YASK-----------PFLG 247
Cdd:cd16152 109 ----------------LTDF----AIDYLDNRQKDKPFFLFLSylephhqndRDRYVAPEgSAERfanfwvppdlaALPG 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 248 TSQRGrYGD---AVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALISapeqggSNGPFlcgKQTTFEGGMREPALA 324
Cdd:cd16152 169 DWAEE-LPDylgCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCHFRT------RNAEY---KRSCHESSIRVPLVI 238
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 530424707 325 WWPGhVTAGQVSHQLGSIMDLFTTSLALAGLTPPSdrAIDGLNLLPtLLQGRLMDRP 381
Cdd:cd16152 239 YGPG-FNGGGRVEELVSLIDLPPTLLDAAGIDVPE--EMQGRSLLP-LVDGKVEDWR 291
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
380-513 |
5.05e-34 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 125.12 E-value: 5.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 380 RPIFYYRGDTLMAATLGQHKAHFWTwtNSWenFRQGIDFCPGQNVsGVTTHNLedhtklPLIFHLGRDPGERFPLSFASA 459
Cdd:pfam14707 4 EFLFHYCGAALHAVRWGPYKAHFFT--PSF--DPPGAEGCYGSKV-PVTHHDP------PLLFDLERDPSEKYPLSPDSP 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 530424707 460 EYQEALSRITSVVQQHQEALVPAQPQLNVCNWAVMAPTQsstsvqpdktrPCSP 513
Cdd:pfam14707 73 EYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQ-----------PCCP 115
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
31-383 |
1.64e-28 |
|
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: 118.64 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharnaytp 110
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCM-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 qeivgGIPDSEQLLPELLKKAGYVSKIVGKWHL-GHrpqfhplkhgfdEWFGSPNCHFGpYDnkarpniPVYrdWEMVGR 189
Cdd:cd16156 73 -----ALGDNVKTIGQRLSDNGIHTAYIGKWHLdGG------------DYFGNGICPQG-WD-------PDY--WYDMRN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 190 YYEEFP---INLKTGEANLTQIY------------LQEALDFIkRQARHHPFFLYWAVDATHAPVYASKPF--------- 245
Cdd:cd16156 126 YLDELTeeeRRKSRRGLTSLEAEgikeeftyghrcTNRALDFI-EKHKDEDFFLVVSYDEPHHPFLCPKPYasmykdfef 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 246 -LGTS-----------QR---GRYGDAVRE---------------IDDSIGKILELLQDLhvADNTFVFFTSDNGAALis 295
Cdd:cd16156 205 pKGENayddlenkplhQRlwaGAKPHEDGDkgtikhplyfgcnsfVDYEIGRVLDAADEI--AEDAWVIYTSDHGDML-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 296 apeqgGSNGPFLCGKqTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPsdRAIDGLNLLPTLLQG 375
Cdd:cd16156 281 -----GAHKLWAKGP-AVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQP--KVLEGESILATIEDP 352
|
....*....
gi 530424707 376 RL-MDRPIF 383
Cdd:cd16156 353 EIpENRGVF 361
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
31-375 |
1.11e-27 |
|
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: 115.82 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGfyttnaHARNAyTP 110
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHR------SVWNG-TP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 qeivggIPDSEQLLPELLKKAGYVSKIVGKWH----LGHRPQFHPLKH-------GFDewfgsPNCHFGPYdnKARPNIP 179
Cdd:cd16028 74 ------LDARHLTLALELRKAGYDPALFGYTDtspdPRGLAPLDPRLLsyelampGFD-----PVDRLDEY--PAEDSDT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 180 VY--------------RDWEMVGRYYEEFPINLKTGEANL----TQIYLQEALDFIKRQARHHPFFlywavdATHAPVYA 241
Cdd:cd16028 141 AFltdraieylderqdEPWFLHLSYIRPHPPFVAPAPYHAlydpADVPPPIRAESLAAEAAQHPLL------AAFLERIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 242 SKPFLGTSQRGRYGDA-------------VREIDDSIGKILELLQDLHVADNTFVFFTSDNGaalisapEQGGSNgpFLC 308
Cdd:cd16028 215 SLSFSPGAANAADLDDeevaqmratylglIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG-------EQLGDH--WLW 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 309 GKQTTFEGGMREPALAWWPG---HVTAGQVSHQLGSIMDLFTTSLALAGLTPPSdrAIDGLNLLPtLLQG 375
Cdd:cd16028 286 GKDGFFDQAYRVPLIVRDPRreaDATRGQVVDAFTESVDVMPTILDWLGGEIPH--QCDGRSLLP-LLAG 352
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-372 |
6.92e-25 |
|
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: 107.32 E-value: 6.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTtnaharnaytp 110
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRT----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 qeIVGGIPDSEQLLPELLKKAGYVSKIVGKWHLghrpqfhpLKHGFDewfgspnchFGPYdnkarpnipVYRDWEMVgry 190
Cdd:cd16150 70 --LHHLLRPDEPNLLKTLKDAGYHVAWAGKNDD--------LPGEFA---------AEAY---------CDSDEACV--- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 191 yeefpinlktgeanltqiylQEALDFIKRQARHHPFFLYWAVDATHAPVYASKPF------------------------- 245
Cdd:cd16150 119 --------------------RTAIDWLRNRRPDKPFCLYLPLIFPHPPYGVEEPWfsmidreklpprrppglrakgkpsm 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 246 ---LGTSQRGRYGDAV-REI-----------DDSIGKILELLQDLHVADNTFVFFTSDNGaalisapEQGGSNGpfLCGK 310
Cdd:cd16150 179 legIEKQGLDRWSEERwRELratylgmvsrlDHQFGRLLEALKETGLYDDTAVFFFSDHG-------DYTGDYG--LVEK 249
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530424707 311 -QTTFEGGM-REPALAWWPGhVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDRAidGLNLLPTL 372
Cdd:cd16150 250 wPNTFEDCLtRVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAGIPLSHTHF--GRSLLPVL 310
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-375 |
1.39e-19 |
|
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: 89.57 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTnaharnaytp 110
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDT---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 111 qeivGGIPDSEQLLPEL------LKKAGYVSKIVGKWHLGhrpqfhplkhgfdewfGSPNchfGPYDNKARpnipvyrdw 184
Cdd:cd16035 71 ----LGSPMQPLLSPDVptlghmLRAAGYYTAYKGKWHLS----------------GAAG---GGYKRDPG--------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 185 emvgryyeefpinlktgeanltqiYLQEALDFIKRQAR----HHPFFLywAV------DathapVYASKPFLGTSQRGR- 253
Cdd:cd16035 119 ------------------------IAAQAVEWLRERGAknadGKPWFL--VVslvnphD-----IMFPPDDEERWRRFRn 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 254 -YGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGaalisapEQGGSNGpflcGKQ---TTFEGGMREPALAWWPGH 329
Cdd:cd16035 168 fYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG-------EMGGAHG----LRGkgfNAYEEALHVPLIISHPDL 236
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 530424707 330 VTAGQVSHQLGSIMDLFTTSLALAGLTPPSDRAID----GLNLLPTLLQG 375
Cdd:cd16035 237 FGTGQTTDALTSHIDLLPTLLGLAGVDAEARATEApplpGRDLSPLLTDA 286
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
31-448 |
3.40e-19 |
|
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: 89.52 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGwGDLGVYGEPSR-ETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGrlpirngFYTTNAHARNAYT 109
Cdd:cd16171 1 PNVVMVMSDSFD-GRLTFRPGNQVvDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG-------LFTHLTESWNNYK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 110 pqeivgGIPDSEQLLPELLKKAGYVSKIVGKwhLGHRPQFHPLKHGFDEWfgspnchfgpydnkarpnipvYRDWEMVGR 189
Cdd:cd16171 73 ------GLDPNYPTWMDRLEKHGYHTQKYGK--LDYTSGHHSVSNRVEAW---------------------TRDVPFLLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 190 YyEEFPINLKTGEANLTQIYLQE------ALDFIKRQARHH--PFFLYWAVDATHA-PVYASKPFLGTSQRGR--YGDAV 258
Cdd:cd16171 124 Q-EGRPTVNLVGDRSTVRVMLKDwqntdkAVHWIRKEAPNLtqPFALYLGLNLPHPyPSPSMGENFGSIRNIRafYYAMC 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 259 REIDDSIGKILELLQDLHVADNTFVFFTSDNGaalisapEQGGSNGPFLcgKQTTFEGGMREPALAWWPGhVTAGQVSHQ 338
Cdd:cd16171 203 AETDAMLGEIISALKDTGLLDKTYVFFTSDHG-------ELAMEHRQFY--KMSMYEGSSHVPLLIMGPG-IKAGQQVSD 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 339 LGSIMDLFTTSLALAGLTPPSDraIDGLNLLPTLLQGRLMDRPIFYYRGDTLMAATLG--QHKAHFWTWTNSWENfrqgI 416
Cdd:cd16171 273 VVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLLSESSIKESPSRVPHPDWVLSEFHGcnVNASTYMLRTNSWKY----I 346
|
410 420 430
....*....|....*....|....*....|..
gi 530424707 417 DFCPGQNVSgvtthnledhtklPLIFHLGRDP 448
Cdd:cd16171 347 AYADGNSVP-------------PQLFDLSKDP 365
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
31-354 |
8.34e-16 |
|
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: 78.11 E-value: 8.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDdmGWGDLGVYGEPSRE--TPNLDRMAAEGLLFPNFYSANPLCSPSRA--ALLTGRLPIRNGFYTTNAHARN 106
Cdd:cd16015 1 PNVIVILLE--SFSDPYIDKDVGGEdlTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 107 AYTpqeivggipdSeqlLPELLKKAGYVSKIVgkwHLGH-----RPQFHPlKHGFDEWFGspnCHFGPYDNKARPNIPVY 181
Cdd:cd16015 79 PLP----------S---LPSILKEQGYETIFI---HGGDasfynRDSVYP-NLGFDEFYD---LEDFPDDEKETNGWGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 182 rDWEMvgryyeefpinlktgeanltqiyLQEALDFIKRQARhHPFFLY---------WAVDATHAPVYASKPFLGTSQrG 252
Cdd:cd16015 139 -DESL-----------------------FDQALEELEELKK-KPFFIFlvtmsnhgpYDLPEEKKDEPLKVEEDKTEL-E 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 253 RYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALISAPEQGGSNgpflcgkqttFEGGMREPALAWWPGhVTA 332
Cdd:cd16015 193 NYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDED----------PLDLYRTPLLIYSPG-LKK 261
|
330 340
....*....|....*....|..
gi 530424707 333 GQVSHQLGSIMDLFTTSLALAG 354
Cdd:cd16015 262 PKKIDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
24-369 |
2.10e-14 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 76.23 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 24 ASGAPQPPNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGrLPIRNGFYTTNAH 103
Cdd:COG1368 228 PFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTG-LPPLPGGSPYKRP 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 104 ARNAYtpqeivggipdseQLLPELLKKAGYVSKIV--GKWHLGHRPQFHPlKHGFDEWFGSPNchfgpYDNKARPNIPVY 181
Cdd:COG1368 307 GQNNF-------------PSLPSILKKQGYETSFFhgGDGSFWNRDSFYK-NLGFDEFYDRED-----FDDPFDGGWGVS 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 182 rDWEMvgryyeefpinlktgeanltqiyLQEALDFIKRQARhhPFFLYWAVDATHAP-----VYASKPFLGTSQRGRYGD 256
Cdd:COG1368 368 -DEDL-----------------------FDKALEELEKLKK--PFFAFLITLSNHGPytlpeEDKKIPDYGKTTLNNYLN 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 257 AVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALisapeQGGSNGPFLCGKQTTfeggmrePALAWWPGHvTAGQVS 336
Cdd:COG1368 422 AVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRS-----PGKTDYENPLERYRV-------PLLIYSPGL-KKPKVI 488
|
330 340 350
....*....|....*....|....*....|...
gi 530424707 337 HQLGSIMDLFTTSLALAGLTPPSDRAIdGLNLL 369
Cdd:COG1368 489 DTVGSQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
13-290 |
1.40e-12 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 69.39 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 13 LLLVLSAAGMGASGAPQPPNILLLLMDDMGWGDLGvygepSRETPNLDRMAAEGLLFPNFYSANP-LCSPSRAALLTGRL 91
Cdd:COG1524 6 SLLLASLLAAAAAAAPPAKKVVLILVDGLRADLLE-----RAHAPNLAALAARGVYARPLTSVFPsTTAPAHTTLLTGLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 92 PIR-----NGFYTTNAHARNAYTPQEIVGGIPDSEQLLP---ELLKKAGYVSKIVGKWHLGHRPQFhplkhgfdewfgsp 163
Cdd:COG1524 81 PGEhgivgNGWYDPELGRVVNSLSWVEDGFGSNSLLPVPtifERARAAGLTTAAVFWPSFEGSGLI-------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 164 nchfgpydnkaRPNIPVYRDwemvGRYYeefpinlKTGEANLTQIYLQEALDFIKRQARHhPFFLYW-AVDAT-Hapvya 241
Cdd:COG1524 147 -----------DAARPYPYD----GRKP-------LLGNPAADRWIAAAALELLREGRPD-LLLVYLpDLDYAgH----- 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 530424707 242 skpflgtsqrgRYG-------DAVREIDDSIGKILELLQDLHVADNTFVFFTSDNG 290
Cdd:COG1524 199 -----------RYGpdspeyrAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
34-295 |
6.22e-11 |
|
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: 63.98 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 34 LLLLMDDMGWGDLgvygEPSRETPNLDRMAAEGLLFPNFYSA-NPLCSPSRAALLTGRLPIRNGfyttnaharnaytpqe 112
Cdd:pfam01663 2 LVISLDGFRADYL----DRFELTPNLAALAKEGVSAPNLTPVfPTLTFPNHYTLVTGLYPGSHG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 113 IVG-GIPDseqllPELLKKAGYV--SKIVGKWHLGHRPQFHPLKHGFdewfgSPNCHFGPYDNKARPNIPVYRDWEMVGR 189
Cdd:pfam01663 62 IVGnTFYD-----PKTGEYLVFVisDPEDPRWWQGEPIWDTAAKAGV-----RAAALFWPGSEVDYSTYYGTPPRYLKDD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 190 YYEEFPINLKTGEANLTQ-IYLQEALDFIKRqarhhPFFLYWAVDAThapvyaskpflGTSQRgRYG-------DAVREI 261
Cdd:pfam01663 132 YNNSVPFEDRVDTAVLQTwLDLPFADVAAER-----PDLLLVYLEEP-----------DYAGH-RYGpdspeveDALRRV 194
|
250 260 270
....*....|....*....|....*....|....
gi 530424707 262 DDSIGKILELLQDLHVADNTFVFFTSDNGAALIS 295
Cdd:pfam01663 195 DRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVS 228
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
29-369 |
2.10e-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: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 29 QPPNILLLLMDDMGWGDLGvygepSRETPNLDRMAAEGLLFPNFYSAnplcSPSRAALLTGrLpirngFYTTNAHarnaY 108
Cdd:COG3083 243 KPPNILLIVVDSLRADMLD-----PEVMPNLYAFAQRSLRFTNHYSS----GNSTRAGLFG-L-----FYGLPGN----Y 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 109 TPQEIVGGIPdseQLLPELLKKAGYvskivgkwhlghrpQFHplkhgfdeWFGSPNCHFGPYDnKArpnipVYRDwemvg 188
Cdd:COG3083 304 WDSILAERTP---PVLIDALQQQGY--------------QFG--------LFSSAGFNSPLFR-QT-----IFSD----- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 189 ryYEEFPINLKTGEANLTQIYLQEALDFIKRQARHHPFFLYWAVDATHA---PVYASKPFLGTSQRG------------- 252
Cdd:COG3083 348 --VSLPRLHTPGGPAQRDRQITAQWLQWLDQRDSDRPWFSYLFLDAPHAysfPADYPKPFQPSEDCNylaldnesdptpf 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 253 --RYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALisaPEQG----GSNGPFlcGKQTTfeggmREPALAWW 326
Cdd:COG3083 426 knRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEF---NENGqnywGHNSNF--SRYQL-----QVPLVIHW 495
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 530424707 327 PGhVTAGQVSHqLGSIMDLFTTSL--ALAGLTPPSDRAIdGLNLL 369
Cdd:COG3083 496 PG-TPPQVISK-LTSHLDIVPTLMqrLLGVQNPASDYSQ-GEDLF 537
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
31-290 |
2.10e-08 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 55.67 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 31 PNILLLLMDDMGWGDLgvygEPSRETPNLDRMAAEGLLFPNFYSANP-LCSPSRAALLTGRLPIR-----NGFY--TTNA 102
Cdd:cd16018 1 PPLIVISIDGFRWDYL----DRAGLTPNLKRLAEEGVRAKYVKPVFPtLTFPNHYSIVTGLYPEShgivgNYFYdpKTNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 103 --HARNAYTPQEIVGGIPdseqlLPELLKKAGYVSKIVgkwhlghrpqfhplkhgFdeWFGSPNCHFGPYdnkarpNIPV 180
Cdd:cd16018 77 efSDSDWVWDPWWIGGEP-----IWVTAEKAGLKTASY-----------------F--WPGSEVAIIGYN------PTPI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 181 YRDWeMVGRYYEEFPInlktgeanltqiylQEALD-FIKRQARHHPFFLYW---AVDAT-HapvyaskpflgtsqrgRYG 255
Cdd:cd16018 127 PLGG-YWQPYNDSFPF--------------EERVDtILEWLDLERPDLILLyfeEPDSAgH----------------KYG 175
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 530424707 256 -------DAVREIDDSIGKILELLQDLHVADNTFVFFTSDNG 290
Cdd:cd16018 176 pdspevnEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG 217
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
119-291 |
1.96e-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: 46.74 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 119 DSEQLLPELLKKAGYVskivgkWHLG----HRPQFHPLKHGFDEwfgspnchfGPYDNKARP-NIPVYRDWEMVGRYYEE 193
Cdd:cd16021 76 DNCPFIWKDFKKAGYV------TAFAedwpKIGTFNYRKKGFKK---------PPTDHYLRPfWLAAEKTTSYSTKSYCT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 194 FPINLktgeanlTQIYLQEALDFIKRQaRHHPFF-LYWAVDATHapvyaskpflgtsqrgRYGDAVREIDDSIGKILELL 272
Cdd:cd16021 141 GCRPS-------HKALLDYLEDFIEAY-KDRPKFsFFWLSELTH----------------DYLNGLSLADEDLLEFLKRL 196
|
170
....*....|....*....
gi 530424707 273 QDLHVADNTFVFFTSDNGA 291
Cdd:cd16021 197 KENGLLDNTFVIFMSDHGL 215
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
46-133 |
8.74e-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: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530424707 46 LGVYGEPsRET-PNLDRMAAEGLLFPNFYSANPLCSPSRAALLTgrlpirngfyttnaharnAYTPQEivGGIPDSEQLL 124
Cdd:cd16017 18 MSLYGYP-RDTtPFLSKLKKNLIVFDNVISCGTSTAVSLPCMLS------------------FANREN--YDRAYYQENL 76
|
....*....
gi 530424707 125 PELLKKAGY 133
Cdd:cd16017 77 IDLAKKAGY 85
|
|
| |
