|
Name |
Accession |
Description |
Interval |
E-value |
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
20-503 |
0e+00 |
|
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: 850.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 20 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGG 99
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 100 LPLEEVTLAEVLAARGYLTGMAGKWHLGVGSEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVAI 179
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGTYLPTHQGFDHYLGIPYSHDQGPCQNLTCFPPNIPCFGGCDQGEVPC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 180 PLLANLSVEAQPPWLPRLEARYVAFARDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVG 259
Cdd:cd16158 161 PLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 260 TLMTAIRDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPT 339
Cdd:cd16158 241 ELLQTLKENGIDNNTLVFFTSDNGPSTMRKSRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTHELASTLDILPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 340 LAALAGAPLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSDPDEVRGVFAVRSGKYKAHFFTQGSAHSDTTADPACHASSS 419
Cdd:cd16158 321 IAKLAGAPLPNVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVFAVRWGKYKAHFYTQGAAHSGTTPDKDCHPSAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 420 LTAHEPPLLYDLSEDPGENYNLLGgvagaTPEVLQALKQLQLLKAQLDVAVTFGPSQMARGEDPALQICCRPGCTPHPAC 499
Cdd:cd16158 401 LTSHDPPLLFDLSQDPSENYNLLG-----LPEYNQVLKQIQQVKERFEASMKFGESEINKGEDPALEPCCKPGCTPKPSC 475
|
....
gi 1622837332 500 CHCP 503
Cdd:cd16158 476 CQCH 479
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
20-441 |
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: 567.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 20 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGG 99
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 100 LPLEEVTLAEVLAARGYLTGMAGKWHLgvGSEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCdggcdqglvai 179
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHL--GHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 180 PLLANLSVEAQPPWLPRLEARYVAFARDLMADAqrQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVG 259
Cdd:cd16026 148 PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 260 TLMTAIRDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLP 338
Cdd:cd16026 226 RILDALKELGLEENTLVIFTSDNGPWLEYGGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGtVSDELASTMDLLP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 339 TLAALAGAPLPN-VTLDGFDLSPLLLGTGKSPRQSLFFYPSDPDevrgVFAVRSGKYKAHFFTQGSAHSDTtadpachAS 417
Cdd:cd16026 306 TLAALAGAPLPEdRVIDGKDISPLLLGGSKSPPHPFFYYYDGGD----LQAVRSGRWKLHLPTTYRTGTDP-------GG 374
|
410 420
....*....|....*....|....
gi 1622837332 418 SSLTAHEPPLLYDLSEDPGENYNL 441
Cdd:cd16026 375 LDPTKLEPPLLYDLEEDPGETYNV 398
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
21-441 |
5.23e-137 |
|
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: 402.96 E-value: 5.23e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYPG--VLVPSSRG 98
Cdd:cd16160 2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGtrVFLPWDIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 99 GLPLEEVTLAEVLAARGYLTGMAGKWHLGVG----SEGAFLPPHQGFHrFLG--IPYSHdqgpcqNLTCFPPATPCDGGc 172
Cdd:cd16160 82 GLPKTEVTMAEALKEAGYTTGMVGKWHLGINennhSDGAHLPSHHGFD-FVGtnLPFTN------SWACDDTGRHVDFP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 173 DQGLVAipLLANLSVEAQPPWLPRLEARYVAFARDLMADaqRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLM 252
Cdd:cd16160 154 DRSACF--LYYNDTIVEQPIQHEHLTETLVGDAKSFIED--NQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNIN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 253 ELDAAVGTLMTAIRDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELAS 332
Cdd:cd16160 230 EMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 333 SLDLLPTLAALAGAPLPNVT-LDGFDLSPLLLGTGKSPRQSLFFYPSDPdevrgVFAVRSGKYKAHFFTQgSAHSDTTAD 411
Cdd:cd16160 310 TMDIFPTFVDLAGGTLPTDRiYDGLSITDLLLGEADSPHDDILYYCCSR-----LMAVRYGSYKIHFKTQ-PLPSQESLD 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1622837332 412 PACHA--------------SSSLTAHEPPLLYDLSEDPGENYNL 441
Cdd:cd16160 384 PNCDGggplsdyivcydceDECVTKHNPPLIFDVEKDPGEQYPL 427
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
21-441 |
2.14e-124 |
|
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: 368.01 E-value: 2.14e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSST---TPNLDQLAAGGLRLTDFYVpAPLCTPSRAALLTGRLPVRMGMYPgVLVPSSR 97
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYV-EPSCTPGRAAFITGRHPIRTGLTT-VGLPGSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 98 GGLPLEEVTLAEVLAARGYLTGMAGKWHLGvgSEGAFLPPHQGFHRFLGIPYSHdqgpcqnltcfppatpcdggcdqglv 177
Cdd:cd16142 79 GGLPPWEPTLAELLKDAGYATAQFGKWHLG--DEDGRLPTDHGFDEFYGNLYHT-------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 178 aipllanlsveaqppwlprLEARYVAFARDLMADAQRQDRPFFLYYASHHTHY-----PQFSGQSfaerSGRGPFGDSLM 252
Cdd:cd16142 131 -------------------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFptlpsPEFEGKS----SGKGKYADSMV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 253 ELDAAVGTLMTAIRDLGLLEETLVIFTADNGPETMRMSRGGcSGLLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELA 331
Cdd:cd16142 188 ELDDHVGQILDALDELGIADNTIVIFTTDNGPEQDVWPDGG-YTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGrVSNEIV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 332 SSLDLLPTLAALAGAPLPN-------VTLDGFDLSPLLLGTGKSPRQSLFFYPSDPDevrgVFAVRSGKYKAHFFTQgsa 404
Cdd:cd16142 267 SHLDWFPTLAALAGAPDPKdkllgkdRHIDGVDQSPFLLGKSEKSRRSEFFYFGEGE----LGAVRWKNWKVHFKAQ--- 339
|
410 420 430
....*....|....*....|....*....|....*..
gi 1622837332 405 hsDTTADPACHASSSLTAhepPLLYDLSEDPGENYNL 441
Cdd:cd16142 340 --EDTGGPTGEPFYVLTF---PLIFNLRRDPKERYDV 371
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
20-441 |
9.98e-122 |
|
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: 361.79 E-value: 9.98e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 20 PPNIVLIFADDLGYGDLGCYGHPSST-TPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMyPGVLVPSSRG 98
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 99 GLPLEEVTLAEVLAARGYLTGMAGKWHLGvgSEGAFLPPHQGFHRFLGIPYSHDQgpcqnltcfppatpcdggcdqglva 178
Cdd:cd16161 80 GLPLNETTLAEVLRQAGYATGMIGKWHLG--QREAYLPNSRGFDYYFGIPFSHDS------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 179 ipllanlsveaqppwlpRLEARYVAFARDLMADAQRQDRPFFLYYASHHTHYPQFSGQSF-AERSGRGPFGDSLMELDAA 257
Cdd:cd16161 133 -----------------SLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFqSPTSGRGPYGDALQEMDDL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 258 VGTLMTAIRDLGLLEETLVIFTADNGPETMRMSRGGCSGL--------LRCGKGTTYEGGVREPALAFWPGHIAPGVTHE 329
Cdd:cd16161 196 VGQIMDAVKHAGLKDNTLTWFTSDNGPWEVKCELAVGPGTgdwqgnlgGSVAKASTWEGGHREPAIVYWPGRIPANSTSA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 330 -LASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLGTGKSPRQSLFFYPSDPDEVRGVFAVRSGKYKAHFFTQGsahsd 407
Cdd:cd16161 276 aLVSTLDIFPTVVALAGASLPpGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAGAGALSAVRCGDYKAHYATGG----- 350
|
410 420 430
....*....|....*....|....*....|....
gi 1622837332 408 ttADPACHASSSLTAHEPPLLYDLSEDPGENYNL 441
Cdd:cd16161 351 --ALACCGSTGPKLYHDPPLLFDLEVDPAESFPL 382
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
19-452 |
5.51e-114 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 342.24 E-value: 5.51e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 19 RPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYPgvLVPSSRG 98
Cdd:COG3119 22 KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD--NGEGYNG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 99 GLPLEEVTLAEVLAARGYLTGMAGKWHLgvgsegaflpphqgfhrflgipYSHDqgpcqnltcfppatpcdggcdqglva 178
Cdd:COG3119 100 GLPPDEPTLAELLKEAGYRTALFGKWHL----------------------YLTD-------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 179 ipllanlsveaqppwlprleaRYVAFARDLMADAQRQDRPFFLYYASHHTHYP---------QFSGQSFAE--------- 240
Cdd:COG3119 132 ---------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPyqapeeyldKYDGKDIPLppnlaprdl 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 241 -----RSGRGPFGDSLMELDAAVGTLMTAIRDLGLLEETLVIFTADNGPEtmrmsrGGCSGlLRCGKGTTYEGGVREPAL 315
Cdd:COG3119 191 teeelRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS------LGEHG-LRGGKGTLYEGGIRVPLI 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 316 AFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFF-YPsdpdEVRGVFAVRSGK 393
Cdd:COG3119 264 VRWPGKIKAGsVSDALVSLIDLLPTLLDLAGVPIPE-DLDGRSLLPLLTGEKAEWRDYLYWeYP----RGGGNRAIRTGR 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622837332 394 YKAHFFTQGSahsdttadpachasssltahEPPLLYDLSEDPGENYNLlggvAGATPEV 452
Cdd:COG3119 339 WKLIRYYDDD--------------------GPWELYDLKNDPGETNNL----AADYPEV 373
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
21-451 |
3.62e-110 |
|
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: 333.36 E-value: 3.62e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMY------------ 88
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITdvipgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 89 PGVLVPSSRGGLPLEEVTLAEVLAARGYLTGMAGKWHLGvgSEGAFLPPHQGFHRflGIPYSHDQGPcqnltcfppatpc 168
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLG--GEGGYGPEDQGFDV--NIGGTGNGGP------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 169 DGGCDQGLVAIPLLANLSveaQPPWLP-RLEARYVAFARdlmadaQRQDRPFFLYYASHHTHYPQFSGQSFAE--RSGRG 245
Cdd:cd16144 144 PSYYFPPGKPNPDLEDGP---EGEYLTdRLTDEAIDFIE------QNKDKPFFLYLSHYAVHTPIQARPELIEkyEKKKK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 246 PFGD--------SLME-LDAAVGTLMTAIRDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALA 316
Cdd:cd16144 215 GLRKgqknpvyaAMIEsLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTSNAPLRGGKGSLYEGGIRVPLIV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 317 FWPGHIAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLGTG-KSPRQSLFF-YPS-DPDEVRGVFAVRS 391
Cdd:cd16144 295 RWPGVIKPGsVSDVPVIGTDLYPTFLELAGGPLPpPQHLDGVSLVPLLKGGEaDLPRRALFWhFPHyHGQGGRPASAIRK 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622837332 392 GKYK-AHFFTQGSAHsdttadpachasssltahepplLYDLSEDPGENYNLlggvAGATPE 451
Cdd:cd16144 375 GDWKlIEFYEDGRVE----------------------LYNLKNDIGETNNL----AAEMPE 409
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
21-441 |
6.89e-109 |
|
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: 329.16 E-value: 6.89e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGhPSST--TPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYPGVLVPSSRG 98
Cdd:cd16143 1 PNIVIILADDLGYGDISCYN-PDSKipTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 99 GLPLEEVTLAEVLAARGYLTGMAGKWHLGvGSEGAFLPPHQGFHRFLGIPYShdqGPcqnltcfPPATPCDGGCDQGLVa 178
Cdd:cd16143 80 LIEPDRVTLAKMLKQAGYRTAMVGKWHLG-LDWKKKDGKKAATGTGKDVDYS---KP-------IKGGPLDHGFDYYFG- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 179 iplLANLSVeaqppwLPRLEARyvafARDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAV 258
Cdd:cd16143 148 ---IPASEV------LPTLTDK----AVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQGKSGAGPYGDFVYELDWVV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 259 GTLMTAIRDLGLLEETLVIFTADNGPETMR----MSRGG--CSGLLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELA 331
Cdd:cd16143 215 GRILDALKELGLAENTLVIFTSDNGPSPYAdykeLEKFGhdPSGPLRGMKADIYEGGHRVPFIVRWPGKIPAGsVSDQLV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 332 SSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLGTGKSPRQSLFFYPSdpdeVRGVFAVRSGKYKAhFFTQGSAHSDTta 410
Cdd:cd16143 295 SLTDLFATLAAIVGQKLPdNAAEDSFSFLPALLGPKKQEVRESLVHHS----GNGSFAIRKGDWKL-IDGTGSGGFSY-- 367
|
410 420 430
....*....|....*....|....*....|.
gi 1622837332 411 dPACHASSSLTAHEpplLYDLSEDPGENYNL 441
Cdd:cd16143 368 -PRGKEKLGLPPGQ---LYNLSTDPGESNNL 394
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
20-437 |
1.40e-105 |
|
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: 325.01 E-value: 1.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 20 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGM-----YPGVLVP 94
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMasshgMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 95 SSRGGLPLEEVTLAEVLAARGYLTGMAGKWHLGVGSE----GAFLPPHQGFHRFLGIPYSH------DQGPCQNLTCFPP 164
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCEsrndFCHHPLNHGFDYFYGLPLTNlkdcgdGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 165 ATPCDGGCDQGLVAIPLL----------------------------------------ANLSVEAQPPWLPRLEARYVAF 204
Cdd:cd16159 161 FPLLTAFVLITALTIFLLlylgavskrffvfllilsllfislfflllitnryfncilmRNHEVVEQPMSLENLTQRLTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 205 ARDLMADaqRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIRDLGLLEETLVIFTADNGP 284
Cdd:cd16159 241 AISFLER--NKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 285 ETMRMSR-----GGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPN-VTLDGFD 357
Cdd:cd16159 319 HLEEISVggeygGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGsVIDEPTSLMDIFPTVAALAGAPLPSdRIIDGRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 358 LSPLLLGTGK-SPRQSLFFYPSdpDEVRGV-FAVRSGK--YKAHFFTQGSaHSDTTADPA---CHAS-SSLTAHEPPLLY 429
Cdd:cd16159 399 LMPLLTGQEKrSPHEFLFHYCG--AELHAVrYRPRDGGavWKAHYFTPNF-YPGTEGCCGtllCRCFgDSVTHHDPPLLF 475
|
....*...
gi 1622837332 430 DLSEDPGE 437
Cdd:cd16159 476 DLSADPSE 483
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
20-441 |
2.64e-105 |
|
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: 322.49 E-value: 2.64e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 20 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMY----------- 88
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYttnaharnayt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 89 PGVLVpssrGGLPLEEVTLAEVLAARGYLTGMAGKWHLGvgSEGAFLPPHQGFHRFLGIPYSHdqgpcqnltcFPPATpc 168
Cdd:cd16157 81 PQNIV----GGIPDSEILLPELLKKAGYRNKIVGKWHLG--HRPQYHPLKHGFDEWFGAPNCH----------FGPYD-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 169 dggcDQGLVAIPLLANLSVEAQ---------PPWLPRLEARYVAFARDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFA 239
Cdd:cd16157 143 ----NKAYPNIPVYRDWEMIGRyyeefkidkKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 240 ERSGRGPFGDSLMELDAAVGTLMTAIRDLGLLEETLVIFTADNGPETM-RMSRGGCSGLLRCGKGTTYEGGVREPALAFW 318
Cdd:cd16157 219 GTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALIsAPEQGGSNGPFLCGKQTTFEGGMREPAIAWW 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 319 PGHIAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLgTGKSPRQSLFFYPSDPdevrgVFAVRSGKYKA 396
Cdd:cd16157 299 PGHIKPGqVSHQLGSLMDLFTTSLALAGLPIPsDRAIDGIDLLPVLL-NGKEKDRPIFYYRGDE-----LMAVRLGQYKA 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1622837332 397 HFFT-QGSAHSDTTADPACHAS--SSLTAH------EPPLLYDLSEDPGENYNL 441
Cdd:cd16157 373 HFWTwSNSWEEFRKGINFCPGQnvPGVTTHnqtdhtKLPLLFHLGRDPGEKYPI 426
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
21-452 |
3.18e-92 |
|
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: 286.75 E-value: 3.18e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVpAPLCTPSRAALLTGRLPVRMGmypgvlVPSSRGG- 99
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHV-SPVCAPTRAALLTGRYPFRTG------VWHTILGr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 100 --LPLEEVTLAEVLAARGYLTGMAGKWHLGVgsEGAFLPPHQGFHRFLGIpyshdqgpcqnltcfppatpCDGGCDQglv 177
Cdd:cd16146 74 erMRLDETTLAEVFKDAGYRTGIFGKWHLGD--NYPYRPQDRGFDEVLGH--------------------GGGGIGQ--- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 178 aIPLLANLSVEAQPPWLPRLEARYVAFARDLMADA------QRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSL 251
Cdd:cd16146 129 -YPDYWGNDYFDDTYYHNGKFVKTEGYCTDVFFDEaidfieENKDKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 252 -----M--ELDAAVGTLMTAIRDLGLLEETLVIFTADNGPETMRMSR--GGcsglLRCGKGTTYEGGVREPALAFWPGHI 322
Cdd:cd16146 208 aafygMieNIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRfnAG----MRGKKGSVYEGGHRVPFFIRWPGKI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 323 APG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLG-TGKSPRQSLFFY---PSDPDEVRGVFAVRSGKYKa 396
Cdd:cd16146 284 LAGkDVDTLTAHIDLLPTLLDLCGVKLPeGIKLDGRSLLPLLKGeSDPWPERTLFTHsgrWPPPPKKKRNAAVRTGRWR- 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622837332 397 hfFTQGSAhsdttadpachasssltahEPPLLYDLSEDPGENYNllggVAGATPEV 452
Cdd:cd16146 363 --LVSPKG-------------------FQPELYDIENDPGEEND----VADEHPEV 393
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
21-441 |
1.86e-90 |
|
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: 282.56 E-value: 1.86e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTG----RLPVRMGmypgvlvPSS 96
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGlhtgHTRVRGN-------SEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 97 RGGLPL--EEVTLAEVLAARGYLTGMAGKWHLG-VGSEGAflPPHQGFHRFLGIpysHDQGPCQNLtcFPPATPCDGgcd 173
Cdd:cd16145 74 GGQDPLppDDVTLAEVLKKAGYATAAFGKWGLGgPGTPGH--PTKQGFDYFYGY---LDQVHAHNY--YPEYLWRNG--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 174 qGLVAIPllanlsveaQPPWLPRLEARYVAFAR-----DLMADA------QRQDRPFFLYYAS---H-HTHYPQFSG--Q 236
Cdd:cd16145 144 -EKVPLP---------NNVIPPLDEGNNAGGGGgtyshDLFTDEaldfirENKDKPFFLYLAYtlpHaPLQVPDDGPykY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 237 SFAERSGRGPFGDSLME---------LDAAVGTLMTAIRDLGLLEETLVIFTADNGPEtmrmSRGGC---------SGLL 298
Cdd:cd16145 214 KPKDPGIYAYLPWPQPEkayaamvtrLDRDVGRILALLKELGIDENTLVVFTSDNGPH----SEGGSehdpdffdsNGPL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 299 RCGKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYP 377
Cdd:cd16145 290 RGYKRSLYEGGIRVPFIARWPGKIPAGsVSDHPSAFWDFMPTLADLAGAEPPE-DIDGISLLPTLLGKPQQQQHDYLYWE 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622837332 378 SdpDEVRGVFAVRSGKYKAHFFTQGSahsdttadpachasssltahEPPLLYDLSEDPGENYNL 441
Cdd:cd16145 369 F--YEGGGAQAVRMGGWKAVRHGKKD--------------------GPFELYDLSTDPGETNNL 410
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
21-441 |
2.04e-88 |
|
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: 276.35 E-value: 2.04e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVpAPLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGL 100
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYV-QPICTPSRAALMTGRYPIHTGMQHGVILAGEPYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 101 PLEEVTLAEVLAARGYLTGMAGKWHLGVGSEgAFLPPHQGFHRFLGiPYSHDQGPCQNLTCFPPATPCDGGCDQGLVAip 180
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYTW-EYTPTNRGFDSFYG-YYGGAEDYYTHTSGGANDYGNDDLRDNEEPA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 181 llanlsveaqppwlPRLEARYVA--FARDLMA--DAQRQDRPFFLYYASHHTHYP-QFSGQSFAERSGRGPFGDS----- 250
Cdd:cd16029 156 --------------WDYNGTYSTdlFTDRAVDiiENHDPSKPLFLYLAFQAVHAPlQVPPEYADPYEDKFAHIKDedrrt 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 251 ----LMELDAAVGTLMTAIRDLGLLEETLVIFTADNGPETMRMSrGGCSGLLRCGKGTTYEGGVREPALaFWPGHI---A 323
Cdd:cd16029 222 yaamVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRGGKNTLWEGGVRVPAF-VWSPLLppkR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 324 PGVTHELASSLDLLPTLAALAGA-PLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSDPDEVRGVFAVRSGKYKAHFFTQg 402
Cdd:cd16029 300 GTVSDGLMHVTDWLPTLLSLAGGdPDDLPPLDGVDQWDALSGGAPSPRTEILLNIDDITRTTGGAAIRVGDWKLIVGKP- 378
|
410 420 430
....*....|....*....|....*....|....*....
gi 1622837332 403 sahsdttadpachasssltahepplLYDLSEDPGENYNL 441
Cdd:cd16029 379 -------------------------LFNIENDPCERNDL 392
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
21-357 |
3.57e-80 |
|
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: 249.66 E-value: 3.57e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYpgvLVPSSRGGL 100
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVR---GNVGNGGGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 101 PLEEVTLAEVLAARGYLTGMAGKWHlgvgsegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdggcdqglvaip 180
Cdd:cd16022 78 PPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 181 llaNLSVEaqppWLprlearyvafardlmaDAQRQDRPFFLYYASHHTHYPqfsgqsFAersgrgpFGDSLMELDAAVGT 260
Cdd:cd16022 103 ---DEAID----FI----------------ERRDKDKPFFLYVSFNAPHPP------FA-------YYAMVSAIDDQIGR 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 261 LMTAIRDLGLLEETLVIFTADNGPetMRMSRGgcsglLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPT 339
Cdd:cd16022 147 ILDALEELGLLDNTLIVFTSDHGD--MLGDHG-----LRGKKGSLYEGGIRVPFIVRWPGKIPAGqVSDALVSLLDLLPT 219
|
330
....*....|....*...
gi 1622837332 340 LAALAGAPLPNvTLDGFD 357
Cdd:cd16022 220 LLDLAGIEPPE-GLDGRS 236
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-413 |
1.63e-76 |
|
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: 245.20 E-value: 1.63e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPaPLCTPSRAALLTGRLPVRMGMYPGVLVPSsrggl 100
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNYVVFGYLDPK----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 101 pleEVTLAEVLAARGYLTGMAGKWHLGVGSEGAFLPPHQGFHRFLgipyshdqgpcqnltCFPpatpcdggcdqglvaip 180
Cdd:cd16151 75 ---QKTFGHLLKDAGYATAIAGKWQLGGGRGDGDYPHEFGFDEYC---------------LWQ----------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 181 lLANLSVEAQPPWLPRLEAR----------------YVAFARDLMAdaQRQDRPFFLYYASHHTHYP----------QFS 234
Cdd:cd16151 120 -LTETGEKYSRPATPTFNIRngkllettegdygpdlFADFLIDFIE--RNKDQPFFAYYPMVLVHDPfvptpdspdwDPD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 235 GQSFAERSGRgpFGDSLMELDAAVGTLMTAIRDLGLLEETLVIFTADNG--PETMRMSRGgcsGLLRCGKGTTYEGGVRE 312
Cdd:cd16151 197 DKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGthRPITSRTNG---REVRGGKGKTTDAGTHV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 313 PALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLG-TGKSPRQSLFFYPSDPDEVRGVFAV 389
Cdd:cd16151 272 PLIVNWPGLIPAGgVSDDLVDFSDFLPTLAELAGAPLPeDYPLDGRSFAPQLLGkTGSPRREWIYWYYRNPHKKFGSRFV 351
|
410 420
....*....|....*....|....*...
gi 1622837332 390 RSGKYK----AHFFtqgsahsDTTADPA 413
Cdd:cd16151 352 RTKRYKlyadGRFF-------DLREDPL 372
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
21-441 |
1.54e-75 |
|
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: 242.41 E-value: 1.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYgDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYPgvlVPSSRGGL 100
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHG---LRSRGFPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 101 PLEEVTLAEVLAARGYLTGMAGKWHLGVGSEGAFLPPHQGFHRFLGIPYshdqgpcqnltcfppatpcdggcdqglvaip 180
Cdd:cd16027 77 PDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAW------------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 181 llanlsveaqppwlprleaRYVAFARDLMaDAQRQDRPFFLYYASHHTHYPQFSGQSFAE-------------------R 241
Cdd:cd16027 126 -------------------DYASNAADFL-NRAKKGQPFFLWFGFHDPHRPYPPGDGEEPgydpekvkvppylpdtpevR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 242 SGRGPFGDSLMELDAAVGTLMTAIRDLGLLEETLVIFTADNGpetMRMSRggcsgllrcGKGTTYEGGVREPALAFWPGH 321
Cdd:cd16027 186 EDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG---MPFPR---------AKGTLYDSGLRVPLIVRWPGK 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 322 IAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFY----PSDPDEVRgvfAVRSGKYK- 395
Cdd:cd16027 254 IKPGsVSDALVSFIDLAPTLLDLAGIEPPE-YLQGRSFLPLLKGEKDPGRDYVFAErdrhDETYDPIR---SVRTGRYKy 329
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1622837332 396 AHFFtqgsahsdttadpachasssltahEPPLLYDLSEDPGENYNL 441
Cdd:cd16027 330 IRNY------------------------MPEELYDLKNDPDELNNL 351
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
20-441 |
1.38e-73 |
|
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293749 [Multi-domain] Cd Length: 402 Bit Score: 238.50 E-value: 1.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 20 PPNIVLIFADDLGYGDLGCYGHPSSTtPNLDQLAAGGLRLTDFYVpAPLCTPSRAALLTGRLP--VRMGMYPGVL--VPS 95
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGEIPT-PNLDALAAEGLRFTNFHT-TALCSPTRAALLTGRNHhqVGMGTMAELAtgKPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 96 SRGGLPLEEVTLAEVLAARGYLTGMAGKWHLGvgsegaflppHQGFHrflgipYSHDqgpcqnltcfppatpcdggcdqg 175
Cdd:cd16025 80 YEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG----------PDDYY------STDD----------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 176 lvaipllanlsveaqppwlprlearYVAFARDLMADAQRQDRPFFLYYASHHTHYP---------QFSGQ---------- 236
Cdd:cd16025 121 -------------------------LTDKAIEYIDEQKAPDKPFFLYLAFGAPHAPlqapkewidKYKGKydagwdalre 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 237 ----------------SFAERSGRGPFGDSL-----------ME--------LDAAVGTLMTAIRDLGLLEETLVIFTAD 281
Cdd:cd16025 176 erlerqkelglipadtKLTPRPPGVPAWDSLspeekklearrMEvyaamvehMDQQIGRLIDYLKELGELDNTLIIFLSD 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 282 NGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAP--GVTHELASSLDLLPTLAALAGAPLPNV-------T 352
Cdd:cd16025 256 NGASAEPGWANASNTPFRLYKQASHEGGIRTPLIVSWPKGIKAkgGIRHQFAHVIDIAPTILELAGVEYPKTvngvpqlP 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 353 LDGFDLSPLLLG-TGKSPRQSLFFypsdpdEVRGVFAVRSGKYKAhfftqgsahsdttadpachasssLTAHEPPL---- 427
Cdd:cd16025 336 LDGVSLLPTLDGaAAPSRRRTQYF------ELFGNRAIRKGGWKA-----------------------VALHPPPGwgdq 386
|
490
....*....|....*.
gi 1622837332 428 --LYDLSEDPGENYNL 441
Cdd:cd16025 387 weLYDLAKDPSETHDL 402
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
21-346 |
1.29e-71 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 230.00 E-value: 1.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYpgvlvPSSRGGL 100
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSY-----VSTPVGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 101 PLEEVTLAEVLAARGYLTGMAGKWHLGVGSEGAflPPHQGFHRFLGIPYSHDQgpcQNLTCFPPATPCDGGCdqglvaip 180
Cdd:pfam00884 76 PRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS--PCNLGFDKFFGRNTGSDL---YADPPDVPYNCSGGGV-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 181 llanlsveaqppwlprLEARYVAFARDLmadAQRQDRPFFLYYASHHTHYP------------QFSGQSFAERSGRGPFG 248
Cdd:pfam00884 143 ----------------SDEALLDEALEF---LDNNDKPFFLVLHTLGSHGPpyypdrypekyaTFKPSSCSEEQLLNSYD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 249 DSLMELDAAVGTLMTAIRDLGLLEETLVIFTADNGPetmrmSRGGCSGLLRCGKG-TTYEGGVREPALAFWPGHIAPG-V 326
Cdd:pfam00884 204 NTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGE-----SLGEGGGYLHGGKYdNAPEGGYRVPLLIWSPGGKAKGqK 278
|
330 340
....*....|....*....|
gi 1622837332 327 THELASSLDLLPTLAALAGA 346
Cdd:pfam00884 279 SEALVSHVDLFPTILDLAGI 298
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
19-443 |
3.18e-64 |
|
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: 214.70 E-value: 3.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 19 RPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTgrlpvrmGMYP---GVlVPS 95
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILT-------GQYShrhGV-TDN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 96 SRGGLPLEEVTLAEVLAARGYLTGMAGKWHLGVGSEgaflPPHQGFHRFLGIPyshDQGpcqnlTCFPPATPCDGGCDQg 175
Cdd:cd16031 73 NGPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGD----LPPPGFDYWVSFP---GQG-----SYYDPEFIENGKRVG- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 176 lvaipllanlsveaQPPWLPRLearYVAFARDLMaDAQRQDRPFFLYY---ASH--------HTH--------YPQ---- 232
Cdd:cd16031 140 --------------QKGYVTDI---ITDKALDFL-KERDKDKPFCLSLsfkAPHrpftpaprHRGlyedvtipEPEtfdd 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 233 --FSGQS-FAERSGRGPFGD--------------------SLMELDAAVGTLMTAIRDLGLLEETLVIFTADNGpetmrm 289
Cdd:cd16031 202 ddYAGRPeWAREQRNRIRGVldgrfdtpekyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNG------ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 290 srggcsglLRCG------KGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLL 362
Cdd:cd16031 276 --------FFLGehglfdKRLMYEESIRVPLIIRDPRLIKAGtVVDALVLNIDFAPTILDLAGVPIPE-DMQGRSLLPLL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 363 LGTGKSPRQSLFFY----PSDPDEVRGVFAVRSGKYK-AHFFTQGsahsdttadpachassslTAHEpplLYDLSEDPGE 437
Cdd:cd16031 347 EGEKPVDWRKEFYYeyyeEPNFHNVPTHEGVRTERYKyIYYYGVW------------------DEEE---LYDLKKDPLE 405
|
....*.
gi 1622837332 438 NYNLLG 443
Cdd:cd16031 406 LNNLAN 411
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-441 |
3.42e-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: 200.49 E-value: 3.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYPGVLVpssrggL 100
Cdd:cd16034 2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 101 PLEEVTLAEVLAARGYLTGMAGKWHLG------VGSEGAFLPP--HQGF---------HRFLGIPYSHDQGPCQNLTCFp 163
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGKWHLDgperndGRADDYTPPPerRHGFdywkgyecnHDHNNPHYYDDDGKRIYIKGY- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 164 patpcdggcdqglvaipllanlSVEAQppwlprlearyVAFARDLMADAQRQDRPFFLY--YASHHTHY---PQ-----F 233
Cdd:cd16034 155 ----------------------SPDAE-----------TDLAIEYLENQADKDKPFALVlsWNPPHDPYttaPEeyldmY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 234 SGQSFAERsGRGPFGDSLME---------------LDAAVGTLMTAIRDLGLLEETLVIFTADNGpETMrmsrgGCSGLL 298
Cdd:cd16034 202 DPKKLLLR-PNVPEDKKEEAglredlrgyyamitaLDDNIGRLLDALKELGLLENTIVVFTSDHG-DML-----GSHGLM 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 299 RcgKGTTYEGGVREPALAFWPGHI-APGVTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYP 377
Cdd:cd16034 275 N--KQVPYEESIRVPFIIRYPGKIkAGRVVDLLINTVDIMPTLLGLCGLPIPD-TVEGRDLSPLLLGGKDDEPDSVLLQC 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 378 SDP------DEVRGVFAVRSGKYKAhfftqgsahsdttadpachassSLTAHEPPLLYDLSEDPGENYNL 441
Cdd:cd16034 352 FVPfgggsaRDGGEWRGVRTDRYTY----------------------VRDKNGPWLLFDNEKDPYQLNNL 399
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-436 |
2.69e-50 |
|
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: 174.65 E-value: 2.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYpgvlvpSSRGGL 100
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVW------DNADPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 101 PLEEVTLAEVLAARGYLTGMAGKWHLgVGSEgaflPPHqGFHrflgipysHDqgpcqnltcfppatpcdggcdqglvaip 180
Cdd:cd16037 75 DGDVPSWGHALRAAGYETVLIGKLHF-RGED----QRH-GFR--------YD---------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 181 llanlsveaqppwlprleaRYVA-FARDLMADAQRQDRPFFLYYASHHTHYPQFSGQSF----AERSGRGPFGdsLME-L 254
Cdd:cd16037 113 -------------------RDVTeAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFydlyVRRARAAYYG--LVEfL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 255 DAAVGTLMTAIRDLGLLEETLVIFTADNGpETMrmsrgGCSGLLrcGKGTTYEGGVREPALAFWPGHIAPGVTHELASSL 334
Cdd:cd16037 172 DENIGRVLDALEELGLLDNTLIIYTSDHG-DML-----GERGLW--GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLV 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 335 DLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYPSDPDEVrGVFAVRSGKYKAHFFtqgsahsdttadpac 414
Cdd:cd16037 244 DLAPTILEAAGAPPPP-DLDGRSLLPLAEGPDDPDRVVFSEYHAHGSPS-GAFMLRKGRWKYIYY--------------- 306
|
410 420
....*....|....*....|..
gi 1622837332 415 hasssltAHEPPLLYDLSEDPG 436
Cdd:cd16037 307 -------VGYPPQLFDLENDPE 321
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-443 |
4.56e-50 |
|
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: 176.64 E-value: 4.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYPGVLVPSS-RGG 99
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAySRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 100 LPLEEVTLAEVLAARGYLTGMAGKWHLGvgsegaflpphqgfhrflgipyshdqgpcqnltcfPPATPCDGGCDqglvai 179
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVG-----------------------------------PEETPLDYGFD------ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 180 pllANLSVEAQPpwlprlEARYVAFARDLMADAQRQDRPFFLYYASHHTHYPQFSGQ---------------SFAE---- 240
Cdd:cd16033 120 ---EYLPVETTI------EYFLADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEpyldmydpediplpeSFADdfed 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 241 -----RSGRGPFGDSLME-----------------LDAAVGTLMTAIRDLGLLEETLVIFTADNGpETMrmsrgGCSGLL 298
Cdd:cd16033 191 kpyiyRRERKRWGVDTEDeedwkeiiahywgyitlIDDAIGRILDALEELGLADDTLVIFTSDHG-DAL-----GAHRLW 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 299 RcgKGT-TYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNVTlDGFDLSPLLLG-TGKSPRQSLFF 375
Cdd:cd16033 265 D--KGPfMYEETYRIPLIIKWPGVIAAGqVVDEFVSLLDLAPTILDLAGVDVPPKV-DGRSLLPLLRGeQPEDWRDEVVT 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622837332 376 ypsdpdEVRGVF------AVRSGKYKAHFftqgsahSDTTADpachasssltahEpplLYDLSEDPGENYNLLG 443
Cdd:cd16033 342 ------EYNGHEfylpqrMVRTDRYKYVF-------NGFDID------------E---LYDLESDPYELNNLID 387
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-360 |
1.04e-49 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 171.27 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMY---PGVLVPSSR 97
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHdwiVEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 98 GGLPL--EEVTLAEVLAARGYLTGMAGKWHLGvgsegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdggcDQG 175
Cdd:cd16149 81 KPEGYleGQTTLPEVLQDAGYRCGLSGKWHLG---------------------------------------------DDA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 176 LVaipllanlsveaqppwlprlearyvaFARDLmadaQRQDRPFFL---YYASHHTHypqfsgQSFAERSGrgpfgdslm 252
Cdd:cd16149 116 AD--------------------------FLRRR----AEAEKPFFLsvnYTAPHSPW------GYFAAVTG--------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 253 eLDAAVGTLMTAIRDLGLLEETLVIFTADNGpetMRMsrgGCSGLLRCGKGTT----YEGGVREPALAFWPGHIAPG-VT 327
Cdd:cd16149 151 -VDRNVGRLLDELEELGLTENTLVIFTSDNG---FNM---GHHGIWGKGNGTFplnmYDNSVKVPFIIRWPGVVPAGrVV 223
|
330 340 350
....*....|....*....|....*....|....
gi 1622837332 328 HELASSLDLLPTLAALAGAPLP-NVTLDGFDLSP 360
Cdd:cd16149 224 DSLVSAYDFFPTLLELAGVDPPaDPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-441 |
3.61e-47 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 167.74 E-value: 3.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAP----LCTPSRAALLTGR----LPVRMGMypgvl 92
Cdd:cd16155 3 PNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGwsgaVCVPSRAMLMTGRtlfhAPEGGKA----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 93 vpssrgGLPLEEVTLAEVLAARGYLTGMAGKWHLGVGSE------------------GAFLPPH------QGFHrflgip 148
Cdd:cd16155 78 ------AIPSDDKTWPETFKKAGYRTFATGKWHNGFADAaiefleeykdgdkpffmyVAFTAPHdprqapPEYL------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 149 yshDQGPCQNLTC---FPPATPCDGGcdQGLVAIPLLAnlsveaqpPWlPRLEAryvafardlMADAQRQDrpfflYYA- 224
Cdd:cd16155 146 ---DMYPPETIPLpenFLPQHPFDNG--EGTVRDEQLA--------PF-PRTPE---------AVRQHLAE-----YYAm 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 225 -SHhthypqfsgqsfaersgrgpfgdslmeLDAAVGTLMTAIRDLGLLEETLVIFTADNGpetmrMSRGGcSGLLrcGKG 303
Cdd:cd16155 198 iTH---------------------------LDAQIGRILDALEASGELDNTIIVFTSDHG-----LAVGS-HGLM--GKQ 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 304 TTYEGGVREPALAFWPGhIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYPSDpde 382
Cdd:cd16155 243 NLYEHSMRVPLIISGPG-IPKGkRRDALVYLQDVFPTLCELAGIEIPE-SVEGKSLLPVIRGEKKAVRDTLYGAYRD--- 317
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622837332 383 vrGVFAVRSGKYKAHFFTQGSAHSdttadpachasssltaheppLLYDLSEDPGENYNL 441
Cdd:cd16155 318 --GQRAIRDDRWKLIIYVPGVKRT--------------------QLFDLKKDPDELNNL 354
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
20-443 |
6.74e-43 |
|
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: 156.23 E-value: 6.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 20 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYpgvlvpSSRGG 99
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCF------RNGIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 100 LPLEEVTLAEVLAARGYLTGMAGKWHLgvgsegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdggcdqglvai 179
Cdd:cd16152 75 LPADEKTLAHYFRDAGYETGYVGKWHL----------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 180 pllanlsveaqppwlprleARY-----VAFARDLMADAQrQDRPFFL---YYASHHT----HY--PQFSGQSFAERS--- 242
Cdd:cd16152 102 -------------------AGYrvdalTDFAIDYLDNRQ-KDKPFFLflsYLEPHHQndrdRYvaPEGSAERFANFWvpp 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 243 ---GRGpfGDSLMEL----------DAAVGTLMTAIRDLGLLEETLVIFTADNgpetmrmsrgGCSGLLRCG--KGTTYE 307
Cdd:cd16152 162 dlaALP--GDWAEELpdylgccerlDENVGRIRDALKELGLYDNTIIVFTSDH----------GCHFRTRNAeyKRSCHE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 308 GGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYPSDPDEVRgvf 387
Cdd:cd16152 230 SSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPE-EMQGRSLLPLVDGKVEDWRNEVFIQISESQVGR--- 305
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622837332 388 AVRSGKYKAhfftqgsAHSDTTADPACHASSSltAHEPPLLYDLSEDPGENYNLLG 443
Cdd:cd16152 306 AIRTDRWKY-------SVAAPDKDGWKDSGSD--VYVEDYLYDLEADPYELVNLIG 352
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
21-435 |
6.80e-43 |
|
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: 155.04 E-value: 6.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYPGVlvpssrGGL 100
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA------AEF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 101 PLEEVTLAEVLAARGYLTGMAGKWHlgvgsegaFLPPHQgFHRFlgipySHDQgpcqnltcfppatpcdggcdqglvaip 180
Cdd:cd16032 75 PADIPTFAHYLRAAGYRTALSGKMH--------FVGPDQ-LHGF-----DYDE--------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 181 llanlsveaqppwlpRLEARYVAFARDLmadAQRQD-RPFFLYYASHHTHYPQFSGQSF----AERSGRGPFGdSLMELD 255
Cdd:cd16032 114 ---------------EVAFKAVQKLYDL---ARGEDgRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 256 AAVGTLMTAIRDLGLLEETLVIFTADNGpeTMRMSRGgcsgllRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLD 335
Cdd:cd16032 175 DKVGQLLDTLERTGLADDTIVIFTSDHG--DMLGERG------LWYKMSFFEGSARVPLIISAPGRFAPRRVAEPVSLVD 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 336 LLPTLAALAGAPLPNV--TLDGFDLSPLLLGTGKSPRQSLFFYPSDPDEVRGVFAVRSGKYKahfFTqgsahsdttadpA 413
Cdd:cd16032 247 LLPTLVDLAGGGTAPHvpPLDGRSLLPLLEGGDSGGEDEVISEYLAEGAVAPCVMIRRGRWK---FI------------Y 311
|
410 420
....*....|....*....|..
gi 1622837332 414 CHAsssltahEPPLLYDLSEDP 435
Cdd:cd16032 312 CPG-------DPDQLFDLEADP 326
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-360 |
3.17e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 146.15 E-value: 3.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYPGVLVPssrggl 100
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGPLEP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 101 plEEVTLAEVLAARGYLTGMAGkWHLGVGSEGAFlppHQGFHRFLGIPYSHDQGPcqnltcFPPATPCDGGCDQGLvaip 180
Cdd:cd16148 75 --DDPTLAEILRKAGYYTAAVS-SNPHLFGGPGF---DRGFDTFEDFRGQEGDPG------EEGDERAERVTDRAL---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 181 llanlsveaqpPWLprlearyvafardlmaDAQRQDRPFFL---YYASHHthypqfsgqsfaersgrgPFG--DSLMELD 255
Cdd:cd16148 139 -----------EWL----------------DRNADDDPFFLflhYFDPHE------------------PYLydAEVRYVD 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 256 AAVGTLMTAIRDLGLLEETLVIFTADNGpETMrmsrgGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLD 335
Cdd:cd16148 174 EQIGRLLDKLKELGLLEDTLVIVTSDHG-EEF-----GEHGLYWGHGSNLYDEQLHVPLIIRWPGKEPGKRVDALVSHID 247
|
330 340
....*....|....*....|....*
gi 1622837332 336 LLPTLAALAGAPlPNVTLDGFDLSP 360
Cdd:cd16148 248 IAPTLLDLLGVE-PPDYSDGRSLLP 271
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
20-441 |
2.16e-37 |
|
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: 142.71 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 20 PPNIVLIFADDLGYgDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYPgvLVPSSRGG 99
Cdd:cd16030 2 KPNVLFIAVDDLRP-WLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYD--NNSYFRKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 100 LPlEEVTLAEVLAARGYLTGMAGK-WHLGVGSEG------AFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGC 172
Cdd:cd16030 79 AP-DAVTLPQYFKENGYTTAGVGKiFHPGIPDGDddpaswDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 173 DQ---GLV---AIPLLANLSVEAQP---------PWLPrlearYVA-------FARDLMADAQRQDRPFFLYYASHHTHY 230
Cdd:cd16030 158 EAypdGKVadeAIEQLRKLKDSDKPfflavgfykPHLP-----FVApkkyfdlYPLESIPLPNPFDPIDLPEVAWNDLDD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 231 PQFSGQSFAERSGR--GPFGDSL-MEL-----------DAAVGTLMTAIRDLGLLEETLVIFTADNGpetmrMSRG--Gc 294
Cdd:cd16030 233 LPKYGDIPALNPGDpkGPLPDEQaRELrqayyasvsyvDAQVGRVLDALEELGLADNTIVVLWSDHG-----WHLGehG- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 295 sgllRCGKGTTYEGGVREPaLAFW-PGHIAPG-VTHELASSLDLLPTLAALAGAPLPNVtLDGFDLSPLLLGTGKSPRQS 372
Cdd:cd16030 307 ----HWGKHTLFEEATRVP-LIIRaPGVTKPGkVTDALVELVDIYPTLAELAGLPAPPC-LEGKSLVPLLKNPSAKWKDA 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 373 LF-FYPSDPdeVRGvFAVRSGKYKahfFTQgsaHSDttadpachaSSSLTAHEpplLYDLSEDPGENYNL 441
Cdd:cd16030 381 AFsQYPRPS--IMG-YSIRTERYR---YTE---WVD---------FDKVGAEE---LYDHKNDPNEWKNL 429
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
21-443 |
1.22e-34 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 135.95 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLgYGD-LGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMypgvlVPSSRGG 99
Cdd:PRK13759 7 PNIILIMVDQM-RGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGR-----VGYGDVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 100 LPLEEVTLAEVLAARGYLTGMAGKWHlgVGSEGAFLpphqGFHRFL---GIPYS-HDQGPCQN------LTCFPPATPcd 169
Cdd:PRK13759 81 PWNYKNTLPQEFRDAGYYTQCIGKMH--VFPQRNLL----GFHNVLlhdGYLHSgRNEDKSQFdfvsdyLAWLREKAP-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 170 gGCDQGLVAIPLLANlSVEAQPPWLP-RLEARY--VAFARDLMadaQRQDR--PFFLY--YASHHTHY--PQF------- 233
Cdd:PRK13759 153 -GKDPDLTDIGWDCN-SWVARPWDLEeRLHPTNwvGSESIEFL---RRRDPtkPFFLKmsFARPHSPYdpPKRyfdmykd 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 234 --------SGQSFAERSG---------RGPFGDSLME------------LDAAVGTLMTAIRDLGLLEETLVIFTADNGp 284
Cdd:PRK13759 228 adipdphiGDWEYAEDQDpeggsidalRGNLGEEYARraraayyglithIDHQIGRFLQALKEFGLLDNTIILFVSDHG- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 285 ETMrmsrgGCSGLLRcgKGTTYEGGVREPALAFWPGHIAPG----VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSP 360
Cdd:PRK13759 307 DML-----GDHYLFR--KGYPYEGSAHIPFIIYDPGGLLAGnrgtVIDQVVELRDIMPTLLDLAGGTIPD-DVDGRSLKN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 361 LLLGTGKSPRQSL---FFYPSDPDEVrgvfaVRSGKYKAHFFTQgsahsdttadpachassslTAHEPplLYDLSEDPGE 437
Cdd:PRK13759 379 LIFGQYEGWRPYLhgeHALGYSSDNY-----LTDGKWKYIWFSQ-------------------TGEEQ--LFDLKKDPHE 432
|
....*.
gi 1622837332 438 NYNLLG 443
Cdd:PRK13759 433 LHNLSP 438
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
21-344 |
2.96e-34 |
|
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: 129.08 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDF-YVPAPLCTPSRAALLTGRLPVRMGMY----PGVLVPS 95
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRsVSPPTSSAPNHAALLTGAYPTLHGYTgngsADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 96 SRGGLPLEEVTLAEVLAARGYLTGMAGkwhlgvgsegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdggcdqg 175
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 176 lvaipllanlsveaqppwlprlearyvafARDlMADAQRQDRPFFLYYashhtHYPQFSGQSFAERSGRGPFGDSLMELD 255
Cdd:cd00016 108 -----------------------------LLK-AIDETSKEKPFVLFL-----HFDGPDGPGHAYGPNTPEYYDAVEEID 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 256 AAVGTLMTAIRDLGLLEETLVIFTADNGpetmrMSRGGCSGLLR-CGKGTTYEGGVREPALAFWPGHIAPGVTHELASSL 334
Cdd:cd00016 153 ERIGKVLDALKKAGDADDTVIIVTADHG-----GIDKGHGGDPKaDGKADKSHTGMRVPFIAYGPGVKKGGVKHELISQY 227
|
330
....*....|
gi 1622837332 335 DLLPTLAALA 344
Cdd:cd00016 228 DIAPTLADLL 237
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-438 |
4.20e-33 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 129.39 E-value: 4.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSS--TTPNLDQLAAGGLRLTDFYVpAPLCTPSRAALLTGRLPVRMgmypGVLVPSSRG 98
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGKYGFRT----GVLAVPDEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 99 GLPLEEVTLAEVLAAR--GYLTGMAGKWHLGVGSEGAFLPPHQGfHRFLGIPyshdqGPCQNLTCFpPATPCDGGCDQGL 176
Cdd:cd16154 76 LLSEETLLQLLIKDATtaGYSSAVIGKWHLGGNDNSPNNPGGIP-YYAGILG-----GGVQDYYNW-NLTNNGQTTNSTE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 177 VAIPLLANLSVEaqppWLprlearyvafardlmadaQRQDRPFFLYYA-----------SHHTHYPQFSGQSFAERSGRG 245
Cdd:cd16154 149 YATTKLTNLAID----WI------------------DQQTKPWFLWLAynaphtpfhlpPAELHSRSLLGDSADIEANPR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 246 PFGDSLME-LDAAVGTLMTAIrDLGLLEETLVIFTADNG-PETMR---MSRGGcsgllrcGKGTTYEGGVREPALAFWPG 320
Cdd:cd16154 207 PYYLAAIEaMDTEIGRLLASI-DEEERENTIIIFIGDNGtPGQVVdlpYTRNH-------AKGSLYEGGINVPLIVSGAG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 321 hIAPGVTHE--LASSLDLLPTLAALAGAPLPNVTlDGFDLSPLLLGTGKSPRQslFFYPSDPDEVRGVFAVRSGKYKAHF 398
Cdd:cd16154 279 -VERANEREsaLVNATDLYATIAELAGVDAAEIH-DSVSFKPLLSDVNASTRQ--YNYTEYESPTTTGWATRNQYYKLIE 354
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1622837332 399 FTQGSAHsdttadpachasssltahepplLYDLSEDPGEN 438
Cdd:cd16154 355 SENGQEE----------------------LYDLINDPSEQ 372
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
20-355 |
6.51e-33 |
|
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: 129.21 E-value: 6.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 20 PPNIVLIFADDLGYGDLGcyghPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYpGVLVPSsrGG 99
Cdd:cd16147 1 RPNIVLILTDDQDVELGS----MDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVT-NNSPPG--GG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 100 LP------LEEVTLAEVLAARGYLTGMAGKWHLGVGSEGAFLPPHQGFHRFLGI--PYSHDQGpcqnltcfppaTPCDGG 171
Cdd:cd16147 74 YPkfwqngLERSTLPVWLQEAGYRTAYAGKYLNGYGVPGGVSYVPPGWDEWDGLvgNSTYYNY-----------TLSNGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 172 CDQGLVAIP------LLANLSVeaqppwlprlearyvafarDLMADAQRQDRPFFLYYASH--HTHY---PQFSGQSF-A 239
Cdd:cd16147 143 NGKHGVSYPgdyltdVIANKAL-------------------DFLRRAAADDKPFFLVVAPPapHGPFtpaPRYANLFPnV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 240 ERSGRGPFGD---------------------------------SLMELDAAVGTLMTAIRDLGLLEETLVIFTADNGPET 286
Cdd:cd16147 204 TAPPRPPPNNpdvsdkphwlrrlpplnptqiayidelyrkrlrTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHL 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622837332 287 mrmsrgGCSGLLRcGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNvTLDG 355
Cdd:cd16147 284 ------GQHRLPP-GKRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGAPPPS-DMDG 344
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
21-451 |
2.76e-32 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 128.53 E-value: 2.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYpgvlvpssRGGL 100
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV--------WNGT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 101 PL--EEVTLAEVLAARGYLTGMAGKWHLGVGSEG---------AFLPPHQGFH---RFLGIPYSHDqgPCQNLTcfppat 166
Cdd:cd16028 73 PLdaRHLTLALELRKAGYDPALFGYTDTSPDPRGlapldprllSYELAMPGFDpvdRLDEYPAEDS--DTAFLT------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 167 pcdggcDQGLVAI------PLLANLS-VEAQPPWLprLEARYVAF---------ARDLMADAQRQDRPFflyYASHHTHY 230
Cdd:cd16028 145 ------DRAIEYLderqdePWFLHLSyIRPHPPFV--APAPYHALydpadvpppIRAESLAAEAAQHPL---LAAFLERI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 231 PQ--FSGQSFAERSGRGPFGDSLM--------ELDAAVGTLMTAIRDLGLLEETLVIFTADNGpETMrmsrgGCSGLLrc 300
Cdd:cd16028 214 ESlsFSPGAANAADLDDEEVAQMRatylgliaEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG-EQL-----GDHWLW-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 301 GKGTTYEGGVREPALAFWPG----HIAPGVTHELASSLDLLPTLAALAGAPLPNVtLDGFDLSPLLLGTGKSPRQSLFFY 376
Cdd:cd16028 286 GKDGFFDQAYRVPLIVRDPRreadATRGQVVDAFTESVDVMPTILDWLGGEIPHQ-CDGRSLLPLLAGAQPSDWRDAVHY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 377 PSD----------------PDEVRgVFAVRSGKYK-AHFftqgsahsdttadpachassslTAHePPLLYDLSEDPGENY 439
Cdd:cd16028 365 EYDfrdvstrrpqealglsPDECS-LAVIRDERWKyVHF----------------------AAL-PPLLFDLKNDPGELR 420
|
490
....*....|..
gi 1622837332 440 NLlggvaGATPE 451
Cdd:cd16028 421 DL-----AADPA 427
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-358 |
5.16e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 115.94 E-value: 5.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSST----------TPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYP- 89
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNAHTGksesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 90 GVLVPSSRGGLPleevTLAEVLAARGYLTGMAGKWHlgvgsegaflppHQGFHRFLGIPYSHDQGPcqnltcfppatpcD 169
Cdd:cd16153 82 EAAHPALDHGLP----TFPEVLKKAGYQTASFGKSH------------LEAFQRYLKNANQSYKSF-------------W 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 170 GGCDQGLvaipllanlsveaqppwlprlearyvafardlmadaqRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFgd 249
Cdd:cd16153 133 GKIAKGA-------------------------------------DSDKPFFVRLSFLQPHTPVLPPKEFRDRFDYYAF-- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 250 sLMELDAAVGTLMTAIRDLGLL---EETLVIFTADNGpetmrmSRGGCSGLLrcGKGTTYEGGVREPALAFWPGHI---A 323
Cdd:cd16153 174 -CAYGDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHG------WHLGEQGIL--AKFTFWPQSHRVPLIVVSSDKLkapA 244
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622837332 324 PGVTHELASSLDLLPTLAALAGAPLPNVT-LDGFDL 358
Cdd:cd16153 245 GKVRHDFVEFVDLAPTLLAAAGVDVDAPDyLDGRDL 280
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-376 |
8.29e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 115.77 E-value: 8.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMY--PGvlvPSSRG 98
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTdtLG---SPMQP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 99 GLPLEEVTLAEVLAARGYLTGMAGKWHLGVGSEGAflpphqgfhrflgipYSHDqgpcqnltcfppatpcdggcdqglva 178
Cdd:cd16035 78 LLSPDVPTLGHMLRAAGYYTAYKGKWHLSGAAGGG---------------YKRD-------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 179 ipllanlsveaqppwlPRLEARYVAFARDLMADAQrQDRPFFLYyAS----HHTHYPQfsgqSFAERSGRGP--FGDSLM 252
Cdd:cd16035 117 ----------------PGIAAQAVEWLRERGAKNA-DGKPWFLV-VSlvnpHDIMFPP----DDEERWRRFRnfYYNLIR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 253 ELDAAVGTLMTAIRDLGLLEETLVIFTADNGpetmrmSRGGCSGLLRCGkGTTYEGGVREPAL----AFWPGhiaPGVTH 328
Cdd:cd16035 175 DVDRQIGRVLDALDASGLADNTIVVFTSDHG------EMGGAHGLRGKG-FNAYEEALHVPLIishpDLFGT---GQTTD 244
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622837332 329 ELASSLDLLPTLAALAGAPLPNV-----TLDGFDLSPLLLGTGKSPRQ--SLFFY 376
Cdd:cd16035 245 ALTSHIDLLPTLLGLAGVDAEARateapPLPGRDLSPLLTDADADAVRdgILFTY 299
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-443 |
1.49e-26 |
|
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: 111.56 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRlpvrmgmYPGVlvpssRGG- 99
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGW-------YPHV-----NGHr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 100 -----LPLEEVTLAEVLAARGYLTGMAGKWHLgvgsegaflpphqgfhrflgIPYSHDQGpcqnltcfpPATPCDGGCDQ 174
Cdd:cd16150 69 tlhhlLRPDEPNLLKTLKDAGYHVAWAGKNDD--------------------LPGEFAAE---------AYCDSDEACVR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 175 GLVAipllanlsveaqppwlpRLEARyvafardlmadaqRQDRPFFLYYASH--HTHY----PQFS-------------- 234
Cdd:cd16150 120 TAID-----------------WLRNR-------------RPDKPFCLYLPLIfpHPPYgveePWFSmidreklpprrppg 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 235 ---GQSFAERSGRGPFG-DSLME----------------LDAAVGTLMTAIRDLGLLEETLVIFTADNGPETmrmsrgGC 294
Cdd:cd16150 170 lraKGKPSMLEGIEKQGlDRWSEerwrelratylgmvsrLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYT------GD 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 295 SGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLdGFDLSPLLLGTGKSPRQSLF 374
Cdd:cd16150 244 YGLVEKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHF-GRSLLPVLAGETEEHRDAVF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 375 ----FYPSDPDevrgvfAVRSGKYKAHFFT-QGSAHSDTTADPACHASSSLTA------HEPPLLYDLSEDPGENYNLLG 443
Cdd:cd16150 323 seggRLHGEEQ------AMEGGHGPYDLKWpRLLQQEEPPEHTKAVMIRTRRYkyvyrlYEPDELYDLEADPLELHNLIG 396
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
368-501 |
1.04e-24 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 98.92 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 368 SPRQSLFFYPSDPdevrgVFAVRSGKYKAHFFTqGSAHSDTtaDPACHASS-SLTAHEPPLLYDLSEDPGENYNLlggvA 446
Cdd:pfam14707 1 SPHEFLFHYCGAA-----LHAVRWGPYKAHFFT-PSFDPPG--AEGCYGSKvPVTHHDPPLLFDLERDPSEKYPL----S 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622837332 447 GATPEVLQALKQLQLLKAQLDVAVTFGPSQMARGE---DPALQICCRpgctPHPACCH 501
Cdd:pfam14707 69 PDSPEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNylwDPWLQPCCP----TFPACTC 122
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
21-443 |
6.01e-24 |
|
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: 104.39 E-value: 6.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYPGVLVPSSrggl 100
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 101 plEEVTLAEVLAARGYLTGMAGKWHLGVGSE-GAFLPPhQGFHRflgiPYSHDqgpcqnLTCFPPATPCDggcDQGLVAI 179
Cdd:cd16156 77 --NVKTIGQRLSDNGIHTAYIGKWHLDGGDYfGNGICP-QGWDP----DYWYD------MRNYLDELTEE---ERRKSRR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 180 PL--LANLSVEAQPPWLPRLEARYVAFARdlmadaQRQDRPFFLYYASHHTHYPQFSGQSFAE----------------- 240
Cdd:cd16156 141 GLtsLEAEGIKEEFTYGHRCTNRALDFIE------KHKDEDFFLVVSYDEPHHPFLCPKPYASmykdfefpkgenayddl 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 241 -----------RSGRGPFGDSL---MEL--------DAAVGTLMTAIRDlgLLEETLVIFTADNGpETMrmsrgGCSGLL 298
Cdd:cd16156 215 enkplhqrlwaGAKPHEDGDKGtikHPLyfgcnsfvDYEIGRVLDAADE--IAEDAWVIYTSDHG-DML-----GAHKLW 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 299 rcGKG-TTYEGGVREPALAFWPGHI-APGVTHELASSLDLLPTLAALAGAPLPNVtLDGFDLSPLLLGTGKSPRQSLFF- 375
Cdd:cd16156 287 --AKGpAVYDEITNIPLIIRGKGGEkAGTVTDTPVSHIDLAPTILDYAGIPQPKV-LEGESILATIEDPEIPENRGVFVe 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622837332 376 ---YPSDPDEVRGVFAVR---SGKYK--AHFFTQGSahsdttadpachasssltahepplLYDLSEDPGENYNLLG 443
Cdd:cd16156 364 fgrYEVDHDGFGGFQPVRcvvDGRYKlvINLLSTDE------------------------LYDLEKDPYEMHNLID 415
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
19-358 |
2.06e-19 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 91.25 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 19 RPPNIVLI----FADDLgygdLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLcTpSRA--ALLTGRLPVRMGmypGVL 92
Cdd:COG1368 233 KKPNVVVIllesFSDFF----IGALGNGKDVTPFLDSLAKESLYFGNFYSQGGR-T-SRGefAVLTGLPPLPGG---SPY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 93 VPSSRGGLPleevTLAEVLAARGYLTGMagkWHLGVGS---EGAFLpPHQGFHRFLGIPYshdqgpcqnltcFPPatPCD 169
Cdd:COG1368 304 KRPGQNNFP----SLPSILKKQGYETSF---FHGGDGSfwnRDSFY-KNLGFDEFYDRED------------FDD--PFD 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 170 GG---CDQglvaipllanlsveaqppwlprlearyvAFARDLMADAQRQDRPFFLYY--ASHHTHYPQFSGQSFAERSGR 244
Cdd:COG1368 362 GGwgvSDE----------------------------DLFDKALEELEKLKKPFFAFLitLSNHGPYTLPEEDKKIPDYGK 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 245 GPFGD---SLMELDAAVGTLMTAIRDLGLLEETLVIFTADNGPetmrMSRGGCSGLLRCGKGTTyeggvrePALaFW-PG 320
Cdd:COG1368 414 TTLNNylnAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGP----RSPGKTDYENPLERYRV-------PLL-IYsPG 481
|
330 340 350
....*....|....*....|....*....|....*...
gi 1622837332 321 HIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDL 358
Cdd:COG1368 482 LKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDL 519
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
21-435 |
1.74e-18 |
|
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: 86.83 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLIFADDLgygDLGCYGHPSSTT---PNLDQLAAGGLRLTDFYVPAPLCTPSRAALLTGRLPVRMGMYpgvlvpSSR 97
Cdd:cd16171 1 PNVVMVMSDSF---DGRLTFRPGNQVvdlPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW------NNY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 98 GGLPLEEVTLAEVLAARGYLTGMAGKWHLGVGSegaflppHQGFHRFLG----IPYSHDQG--PCQNLTCfppatpcdgg 171
Cdd:cd16171 72 KGLDPNYPTWMDRLEKHGYHTQKYGKLDYTSGH-------HSVSNRVEAwtrdVPFLLRQEgrPTVNLVG---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 172 cDQGLVAIPLLANLSVEAQPPWLPRlearyvafardlmaDAQRQDRPFFLYYASHHTH-YP-QFSGQSFAE-RSGRGPFG 248
Cdd:cd16171 135 -DRSTVRVMLKDWQNTDKAVHWIRK--------------EAPNLTQPFALYLGLNLPHpYPsPSMGENFGSiRNIRAFYY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 249 DSLMELDAAVGTLMTAIRDLGLLEETLVIFTADNGPETMRMSrggcsgllRCGKGTTYEGGVREPALAFWPGhIAPGVTH 328
Cdd:cd16171 200 AMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHR--------QFYKMSMYEGSSHVPLLIMGPG-IKAGQQV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 329 ELASSL-DLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYPS-DPDEVRG------VFAVRSGKYKAHFFT 400
Cdd:cd16171 271 SDVVSLvDIYPTMLDIAGVPQPQ-NLSGYSLLPLLSESSIKESPSRVPHPDwVLSEFHGcnvnasTYMLRTNSWKYIAYA 349
|
410 420 430
....*....|....*....|....*....|....*
gi 1622837332 401 QGsahsdttadpachasssltAHEPPLLYDLSEDP 435
Cdd:cd16171 350 DG-------------------NSVPPQLFDLSKDP 365
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
21-345 |
7.82e-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: 77.72 E-value: 7.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 21 PNIVLI----FADDLgygdLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPSRA--ALLTGRLPVRMGmyPGVLVP 94
Cdd:cd16015 1 PNVIVIllesFSDPY----IDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLG--SGSYTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 95 SSRGGLPleevTLAEVLAARGY----LTGMAGKWhlgvGSEGAFLpPHQGFHRFLGIPYshdqgpcqnltcFPPATPCDG 170
Cdd:cd16015 75 YKLNPLP----SLPSILKEQGYetifIHGGDASF----YNRDSVY-PNLGFDEFYDLED------------FPDDEKETN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 171 G---CDQGLvaipllanlsveaqppwlprlearyVAFARDLMADAQRQdrPFFLY---YASHH-----THYPQFSGQSFA 239
Cdd:cd16015 134 GwgvSDESL-------------------------FDQALEELEELKKK--PFFIFlvtMSNHGpydlpEEKKDEPLKVEE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 240 ERSGRGPFGDSLMELDAAVGTLMTAIRDLGLLEETLVIFTADNGPetmrmsrggcsGLLRCGKGTTYEGGVRE--PALAF 317
Cdd:cd16015 187 DKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLP-----------SLGSDYDETDEDPLDLYrtPLLIY 255
|
330 340
....*....|....*....|....*...
gi 1622837332 318 WPGHIAPGVTHELASSLDLLPTLAALAG 345
Cdd:cd16015 256 SPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
19-283 |
3.46e-08 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 55.52 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 19 RPPNIVLIFADDLGYGDLGcyghpSSTTPNLDQLAAGGLRLTDFYVPAPLCT-PSRAALLTGRLPVRMGM---------Y 88
Cdd:COG1524 22 PAKKVVLILVDGLRADLLE-----RAHAPNLAALAARGVYARPLTSVFPSTTaPAHTTLLTGLYPGEHGIvgngwydpeL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 89 PGVLVPSSRGGLP------LEEVTLAEVLAARGYLTGMAGKWhlgvGSEGAflpphqGFHRFlGIPYSHDQgpcqnltcf 162
Cdd:COG1524 97 GRVVNSLSWVEDGfgsnslLPVPTIFERARAAGLTTAAVFWP----SFEGS------GLIDA-ARPYPYDG--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 163 ppatpcdggcdqglvAIPLLANlsveaqppwlPRLEARYVAFARDLMadaqRQDRPFFLY-------YASHHThypqfsg 235
Cdd:COG1524 157 ---------------RKPLLGN----------PAADRWIAAAALELL----REGRPDLLLvylpdldYAGHRY------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622837332 236 qsfaersgrGPFG----DSLMELDAAVGTLMTAIRDLGLLEETLVIFTADNG 283
Cdd:COG1524 201 ---------GPDSpeyrAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
187-283 |
9.84e-06 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 47.19 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 187 VEAQPPWLPRLEARYVAFARDLMADAQRQDRPFFLYYashHTHYPQFSGQSFaersgrGPFG----DSLMELDAAVGTLM 262
Cdd:cd16018 126 IPLGGYWQPYNDSFPFEERVDTILEWLDLERPDLILL---YFEEPDSAGHKY------GPDSpevnEALKRVDRRLGYLI 196
|
90 100
....*....|....*....|.
gi 1622837332 263 TAIRDLGLLEETLVIFTADNG 283
Cdd:cd16018 197 EALKERGLLDDTNIIVVSDHG 217
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
207-291 |
1.19e-03 |
|
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: 41.25 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622837332 207 DLMADAQRQDRPFFLYYASHHTHYpqfSGQSFAERSGRgpFGDSLMELDAAVGTLMTAIRDLGLLEETLVIFTADNGPET 286
Cdd:pfam01663 152 DLPFADVAAERPDLLLVYLEEPDY---AGHRYGPDSPE--VEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTP 226
|
....*
gi 1622837332 287 MRMSR 291
Cdd:pfam01663 227 VSDDK 231
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
19-72 |
4.86e-03 |
|
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: 39.14 E-value: 4.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622837332 19 RPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRLTDFYVPAPLCTPS 72
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLKKNLIVFDNVISCGTSTAVS 54
|
|
| |
