|
Name |
Accession |
Description |
Interval |
E-value |
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
1-458 |
0e+00 |
|
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: 703.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 1 MAAYSRVGVFLFSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHHPLSHGFDYFYGLTMTNLRDCKL 80
Cdd:cd16159 68 MASSHGMRVILFTASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHGFDYFYGLPLTNLKDCGD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 81 GQGSVFLKGTEKSIVTSIQIFGITLLSLATVHFIGFlkVPFQALGYCLLITAILLVVLLFFFYNFRYLNCFLMRNHQIIQ 160
Cdd:cd16159 148 GSNGEYDLSFDPLFPLLTAFVLITALTIFLLLYLGA--VSKRFFVFLLILSLLFISLFFLLLITNRYFNCILMRNHEVVE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 161 QPLSYENLTQRLTKEAVQFIGRNTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLN 240
Cdd:cd16159 226 QPMSLENLTQRLTKEAISFLERNKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 241 NKTLVYFTSDQGAHVEEISSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAG 320
Cdd:cd16159 306 DNTFVYFTSDNGGHLEEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAG 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 321 AQLPCDRIIDGHDLMPLLQGKIIQSKHEFLFHYCNAYLNAVRWHPRNSESIWKVFFFTPNFNPEdSNGCHDSHVCFCYGS 400
Cdd:cd16159 386 APLPSDRIIDGRDLMPLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPG-TEGCCGTLLCRCFGD 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1444497662 401 FITRHDPPLLFDLSRDPEEKVPLTPETEsRFYEVLHVILRAVDNHTKSLHAVPDQLSW 458
Cdd:cd16159 465 SVTHHDPPLLFDLSADPSESNPLDPTDE-PYQEIIKKILEAVAEHQSSIEPVESQLSF 521
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
6-424 |
8.01e-136 |
|
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: 397.70 E-value: 8.01e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 6 RVGVF---LFSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndFCHHPLSHGFDYFYGLTMTNLRDCKLGQ 82
Cdd:cd16026 65 RVGLPgvvGPPGSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQ------PEFLPTRHGFDEYFGIPYSNDMWPFPLY 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 83 GsvflkgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffYNFRYLNCFLMRNHQIIQQP 162
Cdd:cd16026 139 R-----------------------------------------------------------NDPPGPLPPLMENEEVIEQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 163 LSYENLTQRLTKEAVQFIGRNTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNK 242
Cdd:cd16026 160 ADQSSLTQRYTDEAVDFIERNKDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEEN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 243 TLVYFTSDQGAHVEEISssgevHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQ 322
Cdd:cd16026 240 TLVIFTSDNGPWLEYGG-----HGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 323 LPCDRIIDGHDLMPLLQGKIIQSKHEFLFHYCNAYLNAVRWHPrnsesiWKVFFFTPNFNPEDSngchdshvcfcYGSFI 402
Cdd:cd16026 315 LPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGTDP-----------GGLDP 377
|
410 420
....*....|....*....|..
gi 1444497662 403 TRHDPPLLFDLSRDPEEKVPLT 424
Cdd:cd16026 378 TKLEPPLLYDLEEDPGETYNVA 399
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
4-438 |
4.03e-110 |
|
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: 333.63 E-value: 4.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 4 YSRVGVFLFSaSSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHHPLSHGFDyFYGltmTNLRdcklgqg 83
Cdd:cd16160 69 YGGTRVFLPW-DIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHSDGAHLPSHHGFD-FVG---TNLP------- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 84 svflkgteksivtsiqiFGITLLSLATVHFIGFlkvPFQALgycllitaillvvllfffynfrylnCFLMRNHQIIQQPL 163
Cdd:cd16160 137 -----------------FTNSWACDDTGRHVDF---PDRSA-------------------------CFLYYNDTIVEQPI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 164 SYENLTQRLTKEAVQFIGRNTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKT 243
Cdd:cd16160 172 QHEHLTETLVGDAKSFIEDNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 244 LVYFTSDQGAHVEEISssgevHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYiDEPTSNMDIFPTVIKLAGAQL 323
Cdd:cd16160 252 LVFFLSDHGPHVEYCL-----EGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIKPRVS-HEVVSTMDIFPTFVDLAGGTL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 324 PCDRIIDGHDLMPLLQGKiIQSKHEFLFHYCNAYLNAVRWHPrnsesiWKVFFFTPNFNPEDSN------GCHDSH--VC 395
Cdd:cd16160 326 PTDRIYDGLSITDLLLGE-ADSPHDDILYYCCSRLMAVRYGS------YKIHFKTQPLPSQESLdpncdgGGPLSDyiVC 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1444497662 396 -FCYGSFITRHDPPLLFDLSRDPEEKVPLTPET-ESRFYEVLHVI 438
Cdd:cd16160 399 yDCEDECVTKHNPPLIFDVEKDPGEQYPLQPSVyEHMLEAVEKLI 443
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
17-458 |
1.63e-73 |
|
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: 239.68 E-value: 1.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 17 GGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCEssndfcHHPLSHGFDYFYGLTmtnlrDCKLGQgsvflkgteksivt 96
Cdd:cd16157 86 GGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ------YHPLKHGFDEWFGAP-----NCHFGP-------------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 97 siqifgitllslatvhfigflkvpfqalgycllitaillvvllffFYNFRYLNCFLMRNHQIIQQplSYE---------- 166
Cdd:cd16157 141 ---------------------------------------------YDNKAYPNIPVYRDWEMIGR--YYEefkidkktge 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 167 -NLTQRLTKEAVQFIGR--NTDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKT 243
Cdd:cd16157 174 sNLTQIYLQEALEFIEKqhDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 244 LVYFTSDQGAHVeeisSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQL 323
Cdd:cd16157 254 FVFFSSDNGAAL----ISAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 324 PCDRIIDGHDLMP-LLQGKIIQSKHeflFHYCNAYLNAVRwhprnsESIWKVFFFT-PNFNPEDSNGCHdshvcFCYGSF 401
Cdd:cd16157 330 PSDRAIDGIDLLPvLLNGKEKDRPI---FYYRGDELMAVR------LGQYKAHFWTwSNSWEEFRKGIN-----FCPGQN 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444497662 402 I---TRH------DPPLLFDLSRDPEEKVPLTPETeSRFYEVLHVILRAVDNHTKSLHAVPDQLSW 458
Cdd:cd16157 396 VpgvTTHnqtdhtKLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLNV 460
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
4-424 |
9.71e-73 |
|
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: 235.06 E-value: 9.71e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 4 YSRVGV---FLfSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNcESsndfcHHPLSHGFDYFYGLtmtnlrdckl 80
Cdd:cd16161 64 GLRNGVghnFL-PTSVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQR-EA-----YLPNSRGFDYYFGI---------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 81 gqgsvflkgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiq 160
Cdd:cd16161 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 161 qPLSYE-NLTQRLTKEAVQFIGRNTDA--PFLLILSYLHVHTAL-YASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEK 236
Cdd:cd16161 127 -PFSHDsSLADRYAQFATDFIQRASAKdrPFFLYAALAHVHVPLaNLPRFQSPTSGRGPYGDALQEMDDLVGQIMDAVKH 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 237 SNLNNKTLVYFTSDQGAHVEEISSSGEVHGGY---NGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFP 313
Cdd:cd16161 206 AGLKDNTLTWFTSDNGPWEVKCELAVGPGTGDwqgNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 314 TVIKLAGAQLPCDRIIDGHDLMPLLQGKiIQSKHEFLFHYCNAY-----LNAVRWHPrnsesiWKVFFFTPNFNPEDSNG 388
Cdd:cd16161 286 TVVALAGASLPPGRIYDGKDLSPVLFGG-SKTGHRCLFHPNSGAagagaLSAVRCGD------YKAHYATGGALACCGST 358
|
410 420 430
....*....|....*....|....*....|....*.
gi 1444497662 389 CHDSHvcfcygsfitrHDPPLLFDLSRDPEEKVPLT 424
Cdd:cd16161 359 GPKLY-----------HDPPLLFDLEVDPAESFPLT 383
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
5-471 |
2.78e-72 |
|
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: 236.96 E-value: 2.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 5 SRVGVF---LFSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSndfcHHPLSHGFDYFYGltmtnlrdcklg 81
Cdd:cd16158 64 VRSGVYpgvFYPGSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGT----YLPTHQGFDHYLG------------ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 82 qgsvflkgteksivtsiqifgitllslatvhfigflkVPF-QALGYCLLITAILLVVLLFFFYNFRYLNCFLMRNHQIIQ 160
Cdd:cd16158 128 -------------------------------------IPYsHDQGPCQNLTCFPPNIPCFGGCDQGEVPCPLFYNESIVQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 161 QPLSYENLTQRLTKEAVQFIGRNT--DAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDWSVGRILDVLEKSN 238
Cdd:cd16158 171 QPVDLLTLEERYAKFAKDFIADNAkeGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVGELLQTLKENG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 239 LNNKTLVYFTSDQGAhveeiSSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIdEPTSNMDIFPTVIKL 318
Cdd:cd16158 251 IDNNTLVFFTSDNGP-----STMRKSRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTH-ELASTLDILPTIAKL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 319 AGAQLPcDRIIDGHDLMPLL--QGKiiqSKHEFLFHY-----CNAYLNAVRWHPrnsesiWKVFFFT---PNFNPEDSNG 388
Cdd:cd16158 325 AGAPLP-NVTLDGVDMSPILfeQGK---SPRQTFFYYptspdPDKGVFAVRWGK------YKAHFYTqgaAHSGTTPDKD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 389 CHDShvcfcygSFITRHDPPLLFDLSRDPEEKVPL--TPEtesrFYEVLHVILRAVDNHTKSLHAVPDQLSWDNllwKPW 466
Cdd:cd16158 395 CHPS-------AELTSHDPPLLFDLSQDPSENYNLlgLPE----YNQVLKQIQQVKERFEASMKFGESEINKGE---DPA 460
|
....*
gi 1444497662 467 LQPCC 471
Cdd:cd16158 461 LEPCC 465
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
15-420 |
3.94e-66 |
|
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: 218.95 E-value: 3.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 15 SSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndFCHHPLSHGFDYFYGltmtnlrDCKLGQGSVFlkgteksi 94
Cdd:cd16144 88 STTRLPLEEVTIAEALKDAGYATAHFGKWHLGGE------GGYGPEDQGFDVNIG-------GTGNGGPPSY-------- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 95 vtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllFFFYNFRYLNcflmrnhqiIQQPLSYENLTQRLTK 174
Cdd:cd16144 147 ---------------------------------------------YFPPGKPNPD---------LEDGPEGEYLTDRLTD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 175 EAVQFIGRNTDAPFLLILSYLHVHTALYASKNFI-----------GKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKT 243
Cdd:cd16144 173 EAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELIekyekkkkglrKGQKNPVYAAMIESLDESVGRILDALEELGLADNT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 244 LVYFTSDQGAHveeisSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQL 323
Cdd:cd16144 253 LVIFTSDNGGL-----STRGGPPTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 324 PCDRIIDGHDLMPLLQGKIIQSKHEFLFHYCNAYLNavrwHPRNSESI-----WK-VFFFtpnfnpedsngcHDSHVcfc 397
Cdd:cd16144 328 PPPQHLDGVSLVPLLKGGEADLPRRALFWHFPHYHG----QGGRPASAirkgdWKlIEFY------------EDGRV--- 388
|
410 420
....*....|....*....|...
gi 1444497662 398 ygsfitrhdppLLFDLSRDPEEK 420
Cdd:cd16144 389 -----------ELYNLKNDIGET 400
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
17-424 |
1.35e-58 |
|
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: 197.76 E-value: 1.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 17 GGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCEssndfcHHPLSHGFDYFYGltmtnlrdcklgqgsvflkgteksivt 96
Cdd:cd16142 79 GGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDG------RLPTDHGFDEFYG--------------------------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 97 siqifgitllslatvhfigflkvpfqalgycllitaillvvllfFFYNFrylncflmrnhqiiqqplsyenLTQRLTKEA 176
Cdd:cd16142 126 --------------------------------------------NLYHT----------------------IDEEIVDKA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 177 VQFIGRN--TDAPFLLILSYLHVHTALYASKNFIGKSK-HGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGA 253
Cdd:cd16142 140 IDFIKRNakADKPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 254 HVEEISSSGevhggyNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLP------CDR 327
Cdd:cd16142 220 EQDVWPDGG------YTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 328 IIDGHDLMPLLQGKIIQSKHEFLFHYCNAYLNAVRWHPrnsesiWKVFFFTpnfnpEDSNGCHDSHVcFCYGSFitrhdp 407
Cdd:cd16142 294 HIDGVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFKA-----QEDTGGPTGEP-FYVLTF------ 355
|
410
....*....|....*..
gi 1444497662 408 PLLFDLSRDPEEKVPLT 424
Cdd:cd16142 356 PLIFNLRRDPKERYDVT 372
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
4-420 |
3.97e-58 |
|
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: 197.42 E-value: 3.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 4 YSRVGVFLFSASSGgLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHH----------------PLSHGFDYF 67
Cdd:cd16143 67 RLKGGVLGGFSPPL-IEPDRVTLAKMLKQAGYRTAMVGKWHLGLDWKKKDGKKAAtgtgkdvdyskpikggPLDHGFDYY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 68 YGLTMTNLRDcklgqgsvflkgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfry 147
Cdd:cd16143 146 FGIPASEVLP---------------------------------------------------------------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 148 lncflmrnhqiiqqplsyenltqRLTKEAVQFIGRN--TDAPFLLILSYLHVHTALYASKNFIGKSKHGLYGDAVEEMDW 225
Cdd:cd16143 156 -----------------------TLTDKAVEFIDQHakKDKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDW 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 226 SVGRILDVLEKSNLNNKTLVYFTSDQGAHVEEISSSGEVHGGY-NGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDE 304
Cdd:cd16143 213 VVGRILDALKELGLAENTLVIFTSDNGPSPYADYKELEKFGHDpSGPLRGMKADIYEGGHRVPFIVRWPGKIPAGSVSDQ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 305 PTSNMDIFPTVIKLAGAQLPCDRIIDGHDLMPLLQGKIIQSKHEFLFHYCNAYLNAVRwhprnsESIWKVFFftpnfnpe 384
Cdd:cd16143 293 LVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSGNGSFAIR------KGDWKLID-------- 358
|
410 420 430
....*....|....*....|....*....|....*..
gi 1444497662 385 dsngCHDSHVCFCYGSFITRHDPP-LLFDLSRDPEEK 420
Cdd:cd16143 359 ----GTGSGGFSYPRGKEKLGLPPgQLYNLSTDPGES 391
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
5-443 |
1.30e-57 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 195.87 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 5 SRVGVF-LFSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLgmncessndfchhplshgfdyfygltmtnlrdcklgqg 83
Cdd:COG3119 86 HRTGVTdNGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL-------------------------------------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 84 svflkgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrylncflmrnhqiiqqpl 163
Cdd:COG3119 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 164 syeNLTQRLTKEAVQFIGRNT--DAPFLLILSYLHVHTALYASKNFIGK-----------------------SKHGLYGD 218
Cdd:COG3119 128 ---YLTDLLTDKAIDFLERQAdkDKPFFLYLAFNAPHAPYQAPEEYLDKydgkdiplppnlaprdlteeelrRARAAYAA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 219 AVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAHVEEisssgevHGgyngiYKGGKSMNWEGGIRVPGLLLWPGVIQA 298
Cdd:COG3119 205 MIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGE-------HG-----LRGGKGTLYEGGIRVPLIVRWPGKIKA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 299 GTYIDEPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKIIQSKHEFLFHYCNAYLN-AVRWHPrnsesiWK-VFF 376
Cdd:COG3119 273 GSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNrAIRTGR------WKlIRY 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 377 FTPNfnpedsngchdshvcfcygsfitrhDPPLLFDLSRDPEEKVPL---TPETESRFYEVLHVILRAVD 443
Cdd:COG3119 345 YDDD-------------------------GPWELYDLKNDPGETNNLaadYPEVVAELRALLEAWLKELG 389
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
345-480 |
1.57e-52 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 173.65 E-value: 1.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 345 SKHEFLFHYCNAYLNAVRWHPrnsesiWKVFFFTPNFNPEDSNGCHDSHVCfcygsfITRHDPPLLFDLSRDPEEKVPLT 424
Cdd:pfam14707 1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1444497662 425 PETEsRFYEVLHVILRAVDNHTKSLHAVPDQLSWDNLLWKPWLQPCCSSlFQSCYC 480
Cdd:pfam14707 69 PDSP-EYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPT-FPACTC 122
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
6-420 |
6.27e-51 |
|
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: 178.51 E-value: 6.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 6 RVGVFlfSASSGG--LPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndFCHHPLSHGFDYFYGLtmtnlrdcklGQG 83
Cdd:cd16146 63 RTGVW--HTILGRerMRLDETTLAEVFKDAGYRTGIFGKWHLGDN------YPYRPQDRGFDEVLGH----------GGG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 84 SVflkgteksivtsIQIFGitllslatvhfigflkvpfqalgycllitaillvvllffFYNFRYLNCFLMRNHQIIQqpl 163
Cdd:cd16146 125 GI------------GQYPD---------------------------------------YWGNDYFDDTYYHNGKFVK--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 164 sYEN-LTQRLTKEAVQFIGRNTDAPFLLILSYLHVHTALYA----SKNFIGKSKH----GLYGdAVEEMDWSVGRILDVL 234
Cdd:cd16146 151 -TEGyCTDVFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVpdkyLDPYKDMGLDdklaAFYG-MIENIDDNVGRLLAKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 235 EKSNLNNKTLVYFTSDQGahveeisSSGEVHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPT 314
Cdd:cd16146 229 KELGLEENTIVIFMSDNG-------PAGGVPKRFNAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 315 VIKLAGAQLPCDRIIDGHDLMPLLQGKIIQSKHEFLF-HYCNAYLNAVRWHP---RNSEsiWKVffftpnFNPEDsngch 390
Cdd:cd16146 302 LLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLFtHSGRWPPPPKKKRNaavRTGR--WRL------VSPKG----- 368
|
410 420 430
....*....|....*....|....*....|
gi 1444497662 391 dshvcfcygsfitrhDPPLLFDLSRDPEEK 420
Cdd:cd16146 369 ---------------FQPELYDIENDPGEE 383
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
19-420 |
4.40e-46 |
|
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: 165.85 E-value: 4.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 19 LPSEEITFSKLLKQRGYSTALIGKWHLGmnCESSNDfchHPLSHGFDYFYGltmtnlrdcklgqgsvFLKgteksivtsi 98
Cdd:cd16145 79 LPPDDVTLAEVLKKAGYATAAFGKWGLG--GPGTPG---HPTKQGFDYFYG----------------YLD---------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 99 QIFGitllslatvHFigflkvpfqalgycllitaillvvllFFFYnfrylncFLMRNHQIIQQPLSYENL---------- 168
Cdd:cd16145 128 QVHA---------HN--------------------------YYPE-------YLWRNGEKVPLPNNVIPPldegnnaggg 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 169 -----TQRLTKEAVQFIGRNTDAPFLLILSYLHVHTALYA---SKNFIGKSKHGLYGDA------------VEEMDWSVG 228
Cdd:cd16145 166 ggtysHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVpddGPYKYKPKDPGIYAYLpwpqpekayaamVTRLDRDVG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 229 RILDVLEKSNLNNKTLVYFTSDQGAHVE-EISSSGEVHGGyNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTS 307
Cdd:cd16145 246 RILALLKELGIDENTLVVFTSDNGPHSEgGSEHDPDFFDS-NGPLRGYKRSLYEGGIRVPFIARWPGKIPAGSVSDHPSA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 308 NMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKIIQSKHEFLF--HYCNAYLNAVRWHPrnsesiWKVFfftpNFNPED 385
Cdd:cd16145 325 FWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLYweFYEGGGAQAVRMGG------WKAV----RHGKKD 392
|
410 420 430
....*....|....*....|....*....|....*
gi 1444497662 386 sngchdshvcfcygsfitrhDPPLLFDLSRDPEEK 420
Cdd:cd16145 393 --------------------GPFELYDLSTDPGET 407
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
11-423 |
3.62e-39 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 146.54 E-value: 3.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 11 LFSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGMnceSSNDFChhPLSHGFDYFYGltmtnlrdcklgqgsvFLKGT 90
Cdd:cd16029 71 ILAGEPYGLPLNETLLPQYLKELGYATHLVGKWHLGF---YTWEYT--PTNRGFDSFYG----------------YYGGA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 91 EksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfFFYNFR------YLNCFLMRNHQIiqqPLS 164
Cdd:cd16029 130 E-------------------------------------------------DYYTHTsggandYGNDDLRDNEEP---AWD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 165 YEN--LTQRLTKEAVQFIGR-NTDAPFLLILSYLHVHTALYASKNFI----GKSKHGLYGD------AVEEMDWSVGRIL 231
Cdd:cd16029 158 YNGtySTDLFTDRAVDIIENhDPSKPLFLYLAFQAVHAPLQVPPEYAdpyeDKFAHIKDEDrrtyaaMVSALDESVGNVV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 232 DVLEKSNLNNKTLVYFTSDQGAHVeeisssGEVHGGYNGIYKGGKSMNWEGGIRVPGlLLWPGVI--QAGTYIDEPTSNM 309
Cdd:cd16029 238 DALKAKGMLDNTLIVFTSDNGGPT------GGGDGGSNYPLRGGKNTLWEGGVRVPA-FVWSPLLppKRGTVSDGLMHVT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 310 DIFPTVIKLAGAQLPCDRIIDGHDLMPLLQGKIIQSKHEFL----FHYCNAYLNAVRWHPrnsesiWKVFFFTPnfnped 385
Cdd:cd16029 311 DWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEILlnidDITRTTGGAAIRVGD------WKLIVGKP------ 378
|
410 420 430
....*....|....*....|....*....|....*...
gi 1444497662 386 sngchdshvcfcygsfitrhdpplLFDLSRDPEEKVPL 423
Cdd:cd16029 379 ------------------------LFNIENDPCERNDL 392
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
17-321 |
2.53e-37 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 139.09 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 17 GGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSndfchhPLSHGFDYFYGL--TMTNLRDCKlgqgsvflkgteksi 94
Cdd:pfam00884 73 VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS------PCNLGFDKFFGRntGSDLYADPP--------------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 95 vtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllFFFYNFRYLNCflmrnhqiiqqplsyenLTQRLTK 174
Cdd:pfam00884 132 ---------------------------------------------DVPYNCSGGGV-----------------SDEALLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 175 EAVQFIGRNTDaPFLLILSYLHVHTALYASKNFIGKSK------------HGLYGDAVEEMDWSVGRILDVLEKSNLNNK 242
Cdd:pfam00884 150 EALEFLDNNDK-PFFLVLHTLGSHGPPYYPDRYPEKYAtfkpsscseeqlLNSYDNTLLYTDDAIGRVLDKLEENGLLDN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 243 TLVYFTSDQGAHVEEisssgevhggYNGIYKGGKSMN-WEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGA 321
Cdd:pfam00884 229 TLVVYTSDHGESLGE----------GGGYLHGGKYDNaPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
17-423 |
4.07e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 140.43 E-value: 4.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 17 GGLPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNdfchHPLSHGFDYFYGLTMTNLRDCKLGQGSV-FLKGTEKSIV 95
Cdd:cd16151 69 GYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGD----YPHEFGFDEYCLWQLTETGEKYSRPATPtFNIRNGKLLE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 96 TSIQIFGITLLSlatvhfigflkvpfqalgycllitaillvvllfffynfRYLNcflmrnhqiiqqplsyenltqrltke 175
Cdd:cd16151 145 TTEGDYGPDLFA--------------------------------------DFLI-------------------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 176 avQFIGRNTDAPFLLILSYLHVHT----------ALYASKNFIGKSKHglYGDAVEEMDWSVGRILDVLEKSNLNNKTLV 245
Cdd:cd16151 161 --DFIERNKDQPFFAYYPMVLVHDpfvptpdspdWDPDDKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTII 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 246 YFTSDQGAHveeisssGEVHGGYNG-IYKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLP 324
Cdd:cd16151 237 IFTGDNGTH-------RPITSRTNGrEVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 325 CDRIIDGHDLMPLLQGKIIQSKHEFLFhycnaylnavrWHPRNSESIW-KVFFFTPNFNpedsngchdshvcfcygsfit 403
Cdd:cd16151 310 EDYPLDGRSFAPQLLGKTGSPRREWIY-----------WYYRNPHKKFgSRFVRTKRYK--------------------- 357
|
410 420
....*....|....*....|
gi 1444497662 404 RHDPPLLFDLSRDPEEKVPL 423
Cdd:cd16151 358 LYADGRFFDLREDPLEKNPL 377
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
175-333 |
1.01e-36 |
|
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: 135.26 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 175 EAVQFIGRN-TDAPFLLILSYLHVHTALYasknfigkskhglYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGA 253
Cdd:cd16022 104 EAIDFIERRdKDKPFFLYVSFNAPHPPFA-------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 254 HVEEisssgevHGGyngiyKGGKSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPcdRIIDGHD 333
Cdd:cd16022 171 MLGD-------HGL-----RGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPP--EGLDGRS 236
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
19-423 |
2.72e-35 |
|
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: 135.77 E-value: 2.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 19 LPSEEITFSKLLKQRGYSTALIGKWHLGMNCESSNDFCHH----PLSHGFDYFYGltmtnlrdcklgqgsvflkgteksi 94
Cdd:cd16034 75 LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADDYtpppERRHGFDYWKG------------------------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 95 vtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllFFFYNfRYLNCFLMRNHQIIQQPLSYEnlTQRLTK 174
Cdd:cd16034 130 ---------------------------------------------YECNH-DHNNPHYYDDDGKRIYIKGYS--PDAETD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 175 EAVQFIGR--NTDAPFLLILSYLHVHT----------ALYASKN---------------FIGKSKHGLYGdAVEEMDWSV 227
Cdd:cd16034 162 LAIEYLENqaDKDKPFALVLSWNPPHDpyttapeeylDMYDPKKlllrpnvpedkkeeaGLREDLRGYYA-MITALDDNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 228 GRILDVLEKSNLNNKTLVYFTSDqgaHveeisssGEVHGGYNGIYKGgksmNW-EGGIRVPGLLLWPGVIQAGTYIDEPT 306
Cdd:cd16034 241 GRLLDALKELGLLENTIVVFTSD---H-------GDMLGSHGLMNKQ----VPyEESIRVPFIIRYPGKIKAGRVVDLLI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 307 SNMDIFPTVIKLAGaqLPCDRIIDGHDLMPLLQGKIIQSKHEFLFhYCNAYLNavrWHPRNSESIWKvffftpnfnpeds 386
Cdd:cd16034 307 NTVDIMPTLLGLCG--LPIPDTVEGRDLSPLLLGGKDDEPDSVLL-QCFVPFG---GGSARDGGEWR------------- 367
|
410 420 430
....*....|....*....|....*....|....*..
gi 1444497662 387 nGCHDSHVCFCygsfITRHDPPLLFDLSRDPEEKVPL 423
Cdd:cd16034 368 -GVRTDRYTYV----RDKNGPWLLFDNEKDPYQLNNL 399
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
4-421 |
1.55e-32 |
|
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: 128.80 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 4 YSRV-GVFLFSASSggLPSEEITFSKLLKQRGYSTALIGKWHLGMNcessndfcHHPLSHGFDYFYGLTmtnlrdcklGQ 82
Cdd:cd16031 63 YSHRhGVTDNNGPL--FDASQPTYPKLLRKAGYQTAFIGKWHLGSG--------GDLPPPGFDYWVSFP---------GQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 83 GSvflkgteksivtsiqifgitllslatvhfigflkvpfqalgycllitaillvvllfffynfrYLNCFLMRNHQIIQQp 162
Cdd:cd16031 124 GS--------------------------------------------------------------YYDPEFIENGKRVGQ- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 163 lsYENLTQRLTKEAVQFIGRNTDA-PFLLILSYLHVHT--------------------ALYASKNFIGKSK--------- 212
Cdd:cd16031 141 --KGYVTDIITDKALDFLKERDKDkPFCLSLSFKAPHRpftpaprhrglyedvtipepETFDDDDYAGRPEwareqrnri 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 213 HGLYGD-----------------AVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGGYngiykgG 275
Cdd:cd16031 219 RGVLDGrfdtpekyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL------GE-HGLF------D 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 276 KSMNWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKIIQS-KHEFLFHYc 354
Cdd:cd16031 286 KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEY- 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444497662 355 naYLNAVRWHPRNSESI----WKVFFFtPNFNPEDSngchdshvcfcygsfitrhdpplLFDLSRDPEEKV 421
Cdd:cd16031 363 --YEEPNFHNVPTHEGVrterYKYIYY-YGVWDEEE-----------------------LYDLKKDPLELN 407
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
216-423 |
1.84e-25 |
|
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: 107.59 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 216 YGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGahveeisssgevhggynGIYKGGKSMNWEGGIRVPGLLLWPGV 295
Cdd:cd16027 191 YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG-----------------MPFPRAKGTLYDSGLRVPLIVRWPGK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 296 IQAGTYIDEPTSNMDIFPTVIKLAGAQLPcdRIIDGHDLMPLLQGKiIQSKHEFLFHYCNaylnavrWHPRNSE---SI- 371
Cdd:cd16027 254 IKPGSVSDALVSFIDLAPTLLDLAGIEPP--EYLQGRSFLPLLKGE-KDPGRDYVFAERD-------RHDETYDpirSVr 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1444497662 372 ---WK-VFfftpNFNPEDsngchdshvcfcygsfitrhdpplLFDLSRDPEEKVPL 423
Cdd:cd16027 324 tgrYKyIR----NYMPEE------------------------LYDLKNDPDELNNL 351
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
170-418 |
7.00e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 104.93 E-value: 7.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 170 QRLTKEAVQFIGRN--TDAPFLLILSYLHVHTALYASKNFIGKSKHGL---YGDAVEEMDWSVGRILDVLEKSNLNNKTL 244
Cdd:cd16037 113 RDVTEAAVDWLREEaaDDKPWFLFVGFVAPHFPLIAPQEFYDLYVRRAraaYYGLVEFLDENIGRVLDALEELGLLDNTL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 245 VYFTSDQGAHVeeisssgevhgGYNGIYkgGKSMNWEGGIRVPGLLLWPGvIQAGTYIDEPTSNMDIFPTVIKLAGAQLP 324
Cdd:cd16037 193 IIYTSDHGDML-----------GERGLW--GKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 325 CDRiiDGHDLMPLLQGK-----IIQSkhEFLFHYCNAYLNAVRWHPrnsesiWKVFFFTpnfnpedsngchdshvcfcyg 399
Cdd:cd16037 259 PDL--DGRSLLPLAEGPddpdrVVFS--EYHAHGSPSGAFMLRKGR------WKYIYYV--------------------- 307
|
250
....*....|....*....
gi 1444497662 400 sfitrHDPPLLFDLSRDPE 418
Cdd:cd16037 308 -----GYPPQLFDLENDPE 321
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
176-319 |
7.20e-25 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 102.88 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 176 AVQFIGRNTDA-PFLLILSYLHVHTALYASKnfigkSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAH 254
Cdd:cd00016 108 LLKAIDETSKEkPFVLFLHFDGPDGPGHAYG-----PNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGI 182
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444497662 255 VEEisssgevHGGYNGiyKGGKSMNWEGGIRVPGLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLA 319
Cdd:cd00016 183 DKG-------HGGDPK--ADGKADKSHTGMRVPFIAYGPGVKKGGV-KHELISQYDIAPTLADLL 237
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
176-418 |
1.44e-23 |
|
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: 101.12 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 176 AVQFI---GRNTDA-PFLLILSYLHVHTALYASKNF----IGKSKHGLYGdAVEEMDWSVGRILDVLEKSNLNNKTLVYF 247
Cdd:cd16032 119 AVQKLydlARGEDGrPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 248 TSDQGAHVeeisssGEvHGGYngiYKggksMNW-EGGIRVPGLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLAGAQL-PC 325
Cdd:cd16032 198 TSDHGDML------GE-RGLW---YK----MSFfEGSARVPLIISAPGRFAPRR-VAEPVSLVDLLPTLVDLAGGGTaPH 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 326 DRIIDGHDLMPLLQGKIIQSKHEFLFHYCN----AYLNAVRwhprnsESIWKvFFFTPNfnpedsngchdshvcfcygsf 401
Cdd:cd16032 263 VPPLDGRSLLPLLEGGDSGGEDEVISEYLAegavAPCVMIR------RGRWK-FIYCPG--------------------- 314
|
250
....*....|....*..
gi 1444497662 402 itrhDPPLLFDLSRDPE 418
Cdd:cd16032 315 ----DPDQLFDLEADPL 327
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
175-336 |
3.00e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 98.85 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 175 EAVQFIGRN--TDAPFLLILSYLHVHtalyasknfigkSKHGlYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQG 252
Cdd:cd16149 114 DAADFLRRRaeAEKPFFLSVNYTAPH------------SPWG-YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 253 AHVeeisssgevhgGYNGIY-KG-GKS-MN-WEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDRI 328
Cdd:cd16149 181 FNM-----------GHHGIWgKGnGTFpLNmYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPR 249
|
....*...
gi 1444497662 329 IDGHDLMP 336
Cdd:cd16149 250 LPGRSFAD 257
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
220-366 |
3.43e-21 |
|
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: 95.59 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 220 VEEMDWSVGRILDVLEKSN-LNNkTLVYFTSDQGAhveeissSGEVHGGY--NGIYKGGKSMNWEGGIRVPGLLLWPGVI 296
Cdd:cd16025 225 VEHMDQQIGRLIDYLKELGeLDN-TLIIFLSDNGA-------SAEPGWANasNTPFRLYKQASHEGGIRTPLIVSWPKGI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 297 QA-GTYIDEPTSNMDIFPTVIKLAGAQLPcDRI-------IDGHDLMPLLQGKIIQSKHEFLF--HYCNAYL-----NAV 361
Cdd:cd16025 297 KAkGGIRHQFAHVIDIAPTILELAGVEYP-KTVngvpqlpLDGVSLLPTLDGAAAPSRRRTQYfeLFGNRAIrkggwKAV 375
|
....*
gi 1444497662 362 RWHPR 366
Cdd:cd16025 376 ALHPP 380
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
220-430 |
1.35e-20 |
|
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: 93.40 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 220 VEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGGYngiykgGKSMNWEGGIRVPGLLLWPGvIQAG 299
Cdd:cd16155 198 ITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAV------GS-HGLM------GKQNLYEHSMRVPLIISGPG-IPKG 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 300 TYIDEPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKiIQSKHEFLFHycnAYLN---AVRwhprnsESIWKVFF 376
Cdd:cd16155 264 KRRDALVYLQDVFPTLCELAGIEIPES--VEGKSLLPVIRGE-KKAVRDTLYG---AYRDgqrAIR------DDRWKLII 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1444497662 377 FTPnfnpedsngchdshvcfcyGSFITRhdpplLFDLSRDPEEKVPL--TPETESR 430
Cdd:cd16155 332 YVP-------------------GVKRTQ-----LFDLKKDPDELNNLadEPEYQER 363
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
219-340 |
2.58e-20 |
|
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: 93.02 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 219 AVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGGYngiykgGKSMNWEGGIRVPglLLW--PGVI 296
Cdd:cd16030 266 SVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHL------GE-HGHW------GKHTLFEEATRVP--LIIraPGVT 330
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1444497662 297 QAGTYIDEPTSNMDIFPTVIKLAGaqLPCDRIIDGHDLMPLLQG 340
Cdd:cd16030 331 KPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKN 372
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
173-418 |
3.19e-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: 89.14 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 173 TKEAVQFIGR---NTDAPFLLIL--SYLHVHTALYASKNFIG-KSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVY 246
Cdd:cd16171 149 TDKAVHWIRKeapNLTQPFALYLglNLPHPYPSPSMGENFGSiRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVF 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 247 FTSDQGAHVEEisssgevhggYNGIYKggKSMnWEGGIRVPGLLLWPGvIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCD 326
Cdd:cd16171 229 FTSDHGELAME----------HRQFYK--MSM-YEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 327 riIDGHDLMPLLQGKIIQSKHEFL---------FHYCNAylNAVRWHPRNSEsiWKvffftpnfnpedsngchdsHVCFC 397
Cdd:cd16171 295 --LSGYSLLPLLSESSIKESPSRVphpdwvlseFHGCNV--NASTYMLRTNS--WK-------------------YIAYA 349
|
250 260
....*....|....*....|.
gi 1444497662 398 YGSFItrhdPPLLFDLSRDPE 418
Cdd:cd16171 350 DGNSV----PPQLFDLSKDPD 366
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
220-423 |
4.53e-19 |
|
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: 89.63 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 220 VEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGgyngiyKGGKSMNWEGGIRVPGLLLWPGV---I 296
Cdd:cd16028 244 IAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQL------GD-HW------LWGKDGFFDQAYRVPLIVRDPRReadA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 297 QAGTYIDEPTSNMDIFPTVIKLAGaqLPCDRIIDGHDLMPLLQGKIIQSKHEFLfHYCNAYLNAVRWHPRNSESIwkvff 376
Cdd:cd16028 311 TRGQVVDAFTESVDVMPTILDWLG--GEIPHQCDGRSLLPLLAGAQPSDWRDAV-HYEYDFRDVSTRRPQEALGL----- 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1444497662 377 ftpnfNPEDSNGC---HDSHVCFCYGSFitrhdPPLLFDLSRDPEEKVPL 423
Cdd:cd16028 383 -----SPDECSLAvirDERWKYVHFAAL-----PPLLFDLKNDPGELRDL 422
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
169-336 |
9.06e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 86.06 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 169 TQRLTKEAVQFIGRN-TDAPFLLILSYLHVHtALYasknfigkskhgLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYF 247
Cdd:cd16148 130 AERVTDRALEWLDRNaDDDPFFLFLHYFDPH-EPY------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 248 TSDQGahvEEIsssGEvhggyNGIYKGGKSMNWEGGIRVPGLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLAGAQLPcdR 327
Cdd:cd16148 197 TSDHG---EEF---GE-----HGLYWGHGSNLYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPP--D 262
|
....*....
gi 1444497662 328 IIDGHDLMP 336
Cdd:cd16148 263 YSDGRSLLP 271
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
25-324 |
2.50e-16 |
|
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: 80.67 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 25 TFSKLLKQRGYSTALIGKWhlgMN-CESSNDFCHHPLshGFDYFYGLTMtnlrdcklgqgsvflkgteksivtsiqifgi 103
Cdd:cd16147 86 TLPVWLQEAGYRTAYAGKY---LNgYGVPGGVSYVPP--GWDEWDGLVG------------------------------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 104 tllslatvhfigflkvpfqalgycllitaillvvllfffyNFRYLNCFLmRNHQIIQQPLSYEN--LTQRLTKEAVQFIG 181
Cdd:cd16147 130 ----------------------------------------NSTYYNYTL-SNGGNGKHGVSYPGdyLTDVIANKALDFLR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 182 R--NTDAPFLLILSYL--HV-------HTALYA--------SKNFIGKS--KHGL------------YGD---------- 218
Cdd:cd16147 169 RaaADDKPFFLVVAPPapHGpftpaprYANLFPnvtapprpPPNNPDVSdkPHWLrrlpplnptqiaYIDelyrkrlrtl 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 219 -AVEEMdwsVGRILDVLEKSNLNNKTLVYFTSDQGAHVeeisssGEvHGgyngiYKGGKSMNWEGGIRVPGLLLWPGvIQ 297
Cdd:cd16147 249 qSVDDL---VERLVNTLEATGQLDNTYIIYTSDNGYHL------GQ-HR-----LPPGKRTPYEEDIRVPLLVRGPG-IP 312
|
330 340
....*....|....*....|....*..
gi 1444497662 298 AGTYIDEPTSNMDIFPTVIKLAGAQLP 324
Cdd:cd16147 313 AGVTVDQLVSNIDLAPTILDLAGAPPP 339
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
172-430 |
4.00e-16 |
|
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: 79.96 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 172 LTKEAVQFI-GRNTDAPFLLILSYLHVH----------TALYASK---NFIGKSKHGLYGDA----------VEEMDWSV 227
Cdd:cd16152 109 LTDFAIDYLdNRQKDKPFFLFLSYLEPHhqndrdryvaPEGSAERfanFWVPPDLAALPGDWaeelpdylgcCERLDENV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 228 GRILDVLEKSNLNNKTLVYFTSDQGAHVEEisssgevhggYNGIYKggKSMNwEGGIRVPGLLLWPGvIQAGTYIDEPTS 307
Cdd:cd16152 189 GRIRDALKELGLYDNTIIVFTSDHGCHFRT----------RNAEYK--RSCH-ESSIRVPLVIYGPG-FNGGGRVEELVS 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 308 NMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKIIQSKHEFLFHYcnaylnavrwhprnSESI---------WKVFFFT 378
Cdd:cd16152 255 LIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNEVFIQI--------------SESQvgrairtdrWKYSVAA 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1444497662 379 PnfnpeDSNGCHDShvcfcyGS--FITRHdpplLFDLSRDPEEKVPLTPETESR 430
Cdd:cd16152 319 P-----DKDGWKDS------GSdvYVEDY----LYDLEADPYELVNLIGRPEYR 357
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-342 |
1.15e-15 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 78.80 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 12 FSASSGGLPSEEITFSKLLKQRGYSTALIGKWHLGmNCESSNDFC---HHPLSHGFDYFYG-LTMTNLRDCKLGQGSVFL 87
Cdd:cd16033 74 AGAYSRGLPPGVETFSEDLREAGYRNGYVGKWHVG-PEETPLDYGfdeYLPVETTIEYFLAdRAIEMLEELAADDKPFFL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 88 kgteksivtsiqifgitllslaTVHFIG-----FLKVPFqalgycllitaillvvllfffynfrylncFLMRNHQIIQQP 162
Cdd:cd16033 153 ----------------------RVNFWGphdpyIPPEPY-----------------------------LDMYDPEDIPLP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 163 LSYENltQRLTKEAVQfigRNTDAPFLLILSYLHVHtalyasKNFIGKskhglYGDAVEEMDWSVGRILDVLEKSNLNNK 242
Cdd:cd16033 182 ESFAD--DFEDKPYIY---RRERKRWGVDTEDEEDW------KEIIAH-----YWGYITLIDDAIGRILDALEELGLADD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 243 TLVYFTSDQGAHVeeisssGEvHGGYNgiyKGgKSMnWEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAq 322
Cdd:cd16033 246 TLVIFTSDHGDAL------GA-HRLWD---KG-PFM-YEETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGV- 312
|
330 340
....*....|....*....|
gi 1444497662 323 lPCDRIIDGHDLMPLLQGKI 342
Cdd:cd16033 313 -DVPPKVDGRSLLPLLRGEQ 331
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
179-334 |
1.50e-15 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 77.03 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 179 FIGRNTDAPFLLILSYLHVHTALYASKNFIGK-SKHGL--YGDAVeemdwsVGRILDVLEKSNLNNK---TLVYFTSDQG 252
Cdd:cd16153 136 AKGADSDKPFFVRLSFLQPHTPVLPPKEFRDRfDYYAFcaYGDAQ------VGRAVEAFKAYSLKQDrdyTIVYVTGDHG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 253 AHVeeisssgevhgGYNGIYkgGKSMNWEGGIRVPGLLLWPGVIQ--AGTYIDEPTSNMDIFPTVIKLAGAQLPCDRIID 330
Cdd:cd16153 210 WHL-----------GEQGIL--AKFTFWPQSHRVPLIVVSSDKLKapAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLD 276
|
....
gi 1444497662 331 GHDL 334
Cdd:cd16153 277 GRDL 280
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
199-419 |
8.05e-15 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 76.63 E-value: 8.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 199 TALYASKNFIGK-----SKHGLYGDaVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDqgaHveeisssGEVHGGYngiYK 273
Cdd:PRK13759 249 GSIDALRGNLGEeyarrARAAYYGL-ITHIDHQIGRFLQALKEFGLLDNTIILFVSD---H-------GDMLGDH---YL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 274 GGKSMNWEGGIRVPGLLLWPG---VIQAGTYIDEPTSNMDIFPTVIKLAGAQLPCDriIDGHDLMPLLQGKiiqskhefl 350
Cdd:PRK13759 315 FRKGYPYEGSAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQ--------- 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444497662 351 fhycnaylnavrwhprnsESIWKVFFFTPNFNPEDSNgcH---DSHVCFCYGSFITRHDpplLFDLSRDPEE 419
Cdd:PRK13759 384 ------------------YEGWRPYLHGEHALGYSSD--NyltDGKWKYIWFSQTGEEQ---LFDLKKDPHE 432
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
19-340 |
2.34e-14 |
|
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: 74.31 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 19 LPSEEITFSKLLKQR--GYSTALIGKWHLGmNCESSNDfcHHPlshGFDYFYGLTMTNLRDcklgqgsvflkgteksivt 96
Cdd:cd16154 77 LSEETLLQLLIKDATtaGYSSAVIGKWHLG-GNDNSPN--NPG---GIPYYAGILGGGVQD------------------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 97 siqifgitllslatvhfigflkvpfqalgycllitaillvvllffFYNFRYLNcflmrNHQiiqQPLSYENLTQRLTKEA 176
Cdd:cd16154 132 ---------------------------------------------YYNWNLTN-----NGQ---TTNSTEYATTKLTNLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 177 VQFIGRNTDaPFLLILSYLHVHT-------ALYASKNF-----IGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNkTL 244
Cdd:cd16154 159 IDWIDQQTK-PWFLWLAYNAPHTpfhlppaELHSRSLLgdsadIEANPRPYYLAAIEAMDTEIGRLLASIDEEEREN-TI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 245 VYFTSDQGAHVEEISSSGEVHGGYNGIYkggksmnwEGGIRVPGLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLP 324
Cdd:cd16154 237 IIFIGDNGTPGQVVDLPYTRNHAKGSLY--------EGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAA 308
|
330
....*....|....*.
gi 1444497662 325 cdRIIDGHDLMPLLQG 340
Cdd:cd16154 309 --EIHDSVSFKPLLSD 322
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
175-353 |
7.12e-14 |
|
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: 72.24 E-value: 7.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 175 EAVQFI---GRNTDA--PFLLILSYLHVHTALY---ASKNFIGKSKhgLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVY 246
Cdd:cd16035 122 QAVEWLrerGAKNADgkPWFLVVSLVNPHDIMFppdDEERWRRFRN--FYYNLIRDVDRQIGRVLDALDASGLADNTIVV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 247 FTSD----QGAHveeisssGEVHGGYNgIYkggksmnwEGGIRVPglLLW--PGVIQAGTYIDEPTSNMDIFPTVIKLAG 320
Cdd:cd16035 200 FTSDhgemGGAH-------GLRGKGFN-AY--------EEALHVP--LIIshPDLFGTGQTTDALTSHIDLLPTLLGLAG 261
|
170 180 190
....*....|....*....|....*....|....*...
gi 1444497662 321 AQLPCDRIID----GHDLMPLLQGKIIQS-KHEFLFHY 353
Cdd:cd16035 262 VDAEARATEApplpGRDLSPLLTDADADAvRDGILFTY 299
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
171-350 |
2.31e-12 |
|
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: 68.95 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 171 RLTKEAVQFIGRNTDAPFLLILSYLHVH-----TALYASK--------------NFIGKSKH------GLYGDAVEEM-- 223
Cdd:cd16156 159 RCTNRALDFIEKHKDEDFFLVVSYDEPHhpflcPKPYASMykdfefpkgenaydDLENKPLHqrlwagAKPHEDGDKGti 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 224 ------------DWSVGRILDVLEKSNLNnkTLVYFTSD----QGAHveeisssgevhggynGIYKGGKSMnWEGGIRVP 287
Cdd:cd16156 239 khplyfgcnsfvDYEIGRVLDAADEIAED--AWVIYTSDhgdmLGAH---------------KLWAKGPAV-YDEITNIP 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444497662 288 GLLLWPGVIQAGTYIDEPTSNMDIFPTVIKLAGAQLPcdRIIDGHDLMPLLQGKIIQSKHEFL 350
Cdd:cd16156 301 LIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQP--KVLEGESILATIEDPEIPENRGVF 361
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
155-317 |
6.33e-11 |
|
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: 64.54 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 155 NHQIIQQPLSYENLTQRLTKEAVQFIG-RNTDAPFLLILSYLHVHtALYASKNFIGKSKHGLYGD--------------- 218
Cdd:COG3083 349 SLPRLHTPGGPAQRDRQITAQWLQWLDqRDSDRPWFSYLFLDAPH-AYSFPADYPKPFQPSEDCNylaldnesdptpfkn 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 219 ----AVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGahvEEISSSGEVHGGYNGIYKggksmnwEGGIRVPGLLLWPG 294
Cdd:COG3083 428 ryrnAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHG---EEFNENGQNYWGHNSNFS-------RYQLQVPLVIHWPG 497
|
170 180
....*....|....*....|...
gi 1444497662 295 vIQAGTyIDEPTSNMDIFPTVIK 317
Cdd:COG3083 498 -TPPQV-ISKLTSHLDIVPTLMQ 518
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
220-340 |
2.49e-09 |
|
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: 59.17 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 220 VEEMDWSVGRILDVLEKSNLNNKTLVYFTSDqgahveeisssgevHGGYNGIYkgGKSMNWEGGI-----RVPGLLLWPG 294
Cdd:cd16150 206 VSRLDHQFGRLLEALKETGLYDDTAVFFFSD--------------HGDYTGDY--GLVEKWPNTFedcltRVPLIIKPPG 269
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1444497662 295 VIQAGTyIDEPTSNMDIFPTVIKLAGAQLPCDRIidGHDLMPLLQG 340
Cdd:cd16150 270 GPAGGV-SDALVELVDIPPTLLDLAGIPLSHTHF--GRSLLPVLAG 312
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
216-320 |
1.90e-06 |
|
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: 49.60 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 216 YGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDqgahveeisssgevHGGYNGIYKGGKSMNWEGGIRVPGLLLWPGV 295
Cdd:cd16015 194 YLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGD--------------HLPSLGSDYDETDEDPLDLYRTPLLIYSPGL 259
|
90 100
....*....|....*....|....*
gi 1444497662 296 IQAGTyIDEPTSNMDIFPTVIKLAG 320
Cdd:cd16015 260 KKPKK-IDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
208-335 |
3.55e-05 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 46.19 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 208 IGKSKHGLYGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDqgahveeisssgevHGGynGIYKGGKSMNWEGGIRVP 287
Cdd:COG1368 411 YGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGD--------------HGP--RSPGKTDYENPLERYRVP 474
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1444497662 288 GLLLWPGVIQAGTyIDEPTSNMDIFPTVIKLAGAQLPcDRIIDGHDLM 335
Cdd:COG1368 475 LLIYSPGLKKPKV-IDTVGSQIDIAPTLLDLLGIDYP-SYYAFGRDLL 520
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
212-252 |
7.55e-03 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 38.58 E-value: 7.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1444497662 212 KHGL----YGDAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQG 252
Cdd:COG1524 199 RYGPdspeYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
218-320 |
7.92e-03 |
|
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: 38.33 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444497662 218 DAVEEMDWSVGRILDVLEKSNLNNKTLVYFTSDQGahveeISSSGeVHGGYNGIykggKSMNweggirvPGLLLWPGVIQ 297
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG-----MTDVG-THGYDNEL----PDMR-------AIFIARGPAFK 245
|
90 100
....*....|....*....|...
gi 1444497662 298 AGTYIdEPTSNMDIFPTVIKLAG 320
Cdd:cd16018 246 KGKKL-GPFRNVDIYPLMCNLLG 267
|
|
| |
