|
Name |
Accession |
Description |
Interval |
E-value |
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
1-419 |
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: 731.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 1 MGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPP 80
Cdd:cd16158 66 SGVYPGVFYPGSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGTYLPTHQGFDHYLGIPYSHDQGPCQNLTCFPP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 81 ATPCDGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGR 160
Cdd:cd16158 146 NIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSR 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 161 GPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAP 240
Cdd:cd16158 226 GPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRKSRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 241 GVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSA 320
Cdd:cd16158 306 GVTHELASTLDILPTIAKLAGAPLPNVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVFAVRWGKYKAHFYTQGAA 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 321 HSDTTADPACHASSSLTAHEPPLLYDLSKDPGENYNLLGgvagaTPEVLQALKQLQLLKAQLDAAVTFGPSQVARGEDPA 400
Cdd:cd16158 386 HSGTTPDKDCHPSAELTSHDPPLLFDLSQDPSENYNLLG-----LPEYNQVLKQIQQVKERFEASMKFGESEINKGEDPA 460
|
410
....*....|....*....
gi 146229327 401 LQICCHPGCTPRPACCHCP 419
Cdd:cd16158 461 LEPCCKPGCTPKPSCCQCH 479
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
1-357 |
1.96e-147 |
|
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: 424.67 E-value: 1.96e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 1 MGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgaFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPP 80
Cdd:cd16026 66 VGLPGVVGPPGSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQPE--FLPTRHGFDEYFGIPYSNDMWPFPLYRNDPP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 81 atpcdggcdqgLVPIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQrqDRPFFLYYASHHTHYPQFSGQSFAERSGR 160
Cdd:cd16026 144 -----------GPLPPLMENEEVIEQPADQSSLTQRYTDEAVDFIERNK--DQPFFLYLAHTMPHVPLFASEKFKGRSGA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 161 GPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAP 240
Cdd:cd16026 211 GLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 241 G-VTHELASSLDLLPTLAALAGAPLPN-VTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDevrgVFAVRTGKYKAHFFTQG 318
Cdd:cd16026 291 GtVSDELASTMDLLPTLAALAGAPLPEdRVIDGKDISPLLLGGSKSPPHPFFYYYDGGD----LQAVRSGRWKLHLPTTY 366
|
330 340 350
....*....|....*....|....*....|....*....
gi 146229327 319 SAHSDTtadpachASSSLTAHEPPLLYDLSKDPGENYNL 357
Cdd:cd16026 367 RTGTDP-------GGLDPTKLEPPLLYDLEEDPGETYNV 398
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
2-357 |
1.54e-93 |
|
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: 288.56 E-value: 1.54e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 2 GMYPG--VLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPE----GAFLPPHQGFHrFLG--IPYSHdqgpcq 73
Cdd:cd16160 67 GMYGGtrVFLPWDIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGINENnhsdGAHLPSHHGFD-FVGtnLPFTN------ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 74 NLTCFPPATPCDGGcDQGLVPipLLANLSVEAQPPWLPGLEARYMAFAHDLMADaqRQDRPFFLYYASHHTHYPQFSGQS 153
Cdd:cd16160 140 SWACDDTGRHVDFP-DRSACF--LYYNDTIVEQPIQHEHLTETLVGDAKSFIED--NQENPFFLYFSFPQTHTPLFASKR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 154 FAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAF 233
Cdd:cd16160 215 FKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKGGKGNSWEGGIRVPFIAY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 234 WPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVT-LDGFDLSPLLLGTGKSPRQSLFFYpsYPDEvrgVFAVRTGKYKA 312
Cdd:cd16160 295 WPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDRiYDGLSITDLLLGEADSPHDDILYY--CCSR---LMAVRYGSYKI 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 146229327 313 HFFTQgSAHSDTTADPACHA--------------SSSLTAHEPPLLYDLSKDPGENYNL 357
Cdd:cd16160 370 HFKTQ-PLPSQESLDPNCDGggplsdyivcydceDECVTKHNPPLIFDVEKDPGEQYPL 427
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
5-357 |
5.35e-85 |
|
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: 264.72 E-value: 5.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 5 PGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVgpEGAFLPPHQGFHRFLGIPYSHDQGpcqnltcfppatpc 84
Cdd:cd16161 70 GHNFLPTSVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQ--REAYLPNSRGFDYYFGIPFSHDSS-------------- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 85 dggcdqglvpipllanlsveaqppwlpgLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSF-AERSGRGPF 163
Cdd:cd16161 134 ----------------------------LADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFqSPTSGRGPY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 164 GDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGL--------LRCGKGTTYEGGVREPALAFWP 235
Cdd:cd16161 186 GDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGPWEVKCELAVGPGTgdwqgnlgGSVAKASTWEGGHREPAIVYWP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 236 GHIAPGVTHE-LASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAH 313
Cdd:cd16161 266 GRIPANSTSAaLVSTLDIFPTVVALAGASLPpGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAGAGALSAVRCGDYKAH 345
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 146229327 314 FFTQGsahsdttADPACHASSSLTAHEPPLLYDLSKDPGENYNL 357
Cdd:cd16161 346 YATGG-------ALACCGSTGPKLYHDPPLLFDLEVDPAESFPL 382
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
2-357 |
1.82e-82 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 257.85 E-value: 1.82e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 2 GMYPgVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgaFLPPHQGFHRFLGIPYSHdqgpcqnltcfppa 81
Cdd:cd16142 68 GLTT-VGLPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDG--RLPTDHGFDEFYGNLYHT-------------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 82 tpcdggcdqglvpipllanlsveaqppwlpgLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHY-----PQFSGQSfae 156
Cdd:cd16142 131 -------------------------------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFptlpsPEFEGKS--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 157 rSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGcSGLLRCGKGTTYEGGVREPALAFWPG 236
Cdd:cd16142 177 -SGKGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGPEQDVWPDGG-YTPFRGEKGTTWEGGVRVPAIVRWPG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 237 HIAPG-VTHELASSLDLLPTLAALAGAPLPN-------VTLDGFDLSPLLLGTGKSPRQSLFFYpsYPDEVRGvfAVRTG 308
Cdd:cd16142 255 KIKPGrVSNEIVSHLDWFPTLAALAGAPDPKdkllgkdRHIDGVDQSPFLLGKSEKSRRSEFFY--FGEGELG--AVRWK 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 146229327 309 KYKAHFFTQgsahsDTTADPACHASSSLTAhepPLLYDLSKDPGENYNL 357
Cdd:cd16142 331 NWKVHFKAQ-----EDTGGPTGEPFYVLTF---PLIFNLRRDPKERYDV 371
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
7-367 |
7.95e-69 |
|
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: 223.96 E-value: 7.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 7 VLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGvgPEGAFLPPHQGFHRflGIPYSHDQGPcqnltcfppatpcDG 86
Cdd:cd16144 83 LIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLG--GEGGYGPEDQGFDV--NIGGTGNGGP-------------PS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 87 GCDQGLVPIPLLANLSveaQPPWLPglearymafahDLMADA------QRQDRPFFLYYASHHTHYPQFSGQSFAE--RS 158
Cdd:cd16144 146 YYFPPGKPNPDLEDGP---EGEYLT-----------DRLTDEaidfieQNKDKPFFLYLSHYAVHTPIQARPELIEkyEK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 159 GRGPFGD--------SLME-LDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREP 229
Cdd:cd16144 212 KKKGLRKgqknpvyaAMIEsLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTSNAPLRGGKGSLYEGGIRVP 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 230 ALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLGTG-KSPRQSLFF-YPSY-PDEVRGVFA 304
Cdd:cd16144 292 LIVRWPGVIKPGsVSDVPVIGTDLYPTFLELAGGPLPpPQHLDGVSLVPLLKGGEaDLPRRALFWhFPHYhGQGGRPASA 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 146229327 305 VRTGKYK-AHFFTQGSAHsdttadpachasssltahepplLYDLSKDPGENYNLlggvAGATPE 367
Cdd:cd16144 372 IRKGDWKlIEFYEDGRVE----------------------LYNLKNDIGETNNL----AAEMPE 409
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
2-368 |
2.80e-68 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 221.68 E-value: 2.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 2 GMYP---GVL--VPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLgvgpegaflpphqgfhrflgipYSHDqgpcqnlt 76
Cdd:COG3119 82 GRYPhrtGVTdnGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL----------------------YLTD-------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 77 cfppatpcdggcdqglvpipllanlsveaqppwlpgleaRYMAFAHDLMADAQRQDRPFFLYYASHHTHYP--------- 147
Cdd:COG3119 132 ---------------------------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPyqapeeyld 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 148 QFSGQSFAE--------------RSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPEtmrmsrGGCSGl 213
Cdd:COG3119 173 KYDGKDIPLppnlaprdlteeelRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS------LGEHG- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 214 LRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFY 292
Cdd:COG3119 246 LRGGKGTLYEGGIRVPLIVRWPGKIKAGsVSDALVSLIDLLPTLLDLAGVPIPE-DLDGRSLLPLLTGEKAEWRDYLYWE 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 146229327 293 psYPDEvRGVFAVRTGKYKAHFFTQGSahsdttadpachasssltahEPPLLYDLSKDPGENYNLlggvAGATPEV 368
Cdd:COG3119 325 --YPRG-GGNRAIRTGRWKLIRYYDDD--------------------GPWELYDLKNDPGETNNL----AADYPEV 373
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
6-357 |
2.19e-67 |
|
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: 219.38 E-value: 2.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 6 GVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLG-----VGPEGAFL---------------PPHQGFHRFLGIPY 65
Cdd:cd16143 71 GVLGGFSPPLIEPDRVTLAKMLKQAGYRTAMVGKWHLGldwkkKDGKKAATgtgkdvdyskpikggPLDHGFDYYFGIPA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 66 ShdqgpcQNLtcfppatpcdggcdqglvpiPLLANLSVEaqppwlpglearymafahdLMADAQRQDRPFFLYYASHHTH 145
Cdd:cd16143 151 S------EVL--------------------PTLTDKAVE-------------------FIDQHAKKDKPFFLYFALPAPH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 146 YPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMR----MSRGG--CSGLLRCGKG 219
Cdd:cd16143 186 TPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPYAdykeLEKFGhdPSGPLRGMKA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 220 TTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLGTGKSPRQSLFFYPSypd 297
Cdd:cd16143 266 DIYEGGHRVPFIVRWPGKIPAGsVSDQLVSLTDLFATLAAIVGQKLPdNAAEDSFSFLPALLGPKKQEVRESLVHHS--- 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 298 eVRGVFAVRTGKYKAhFFTQGSAHSDTtadPACHASSSLTAHEpplLYDLSKDPGENYNL 357
Cdd:cd16143 343 -GNGSFAIRKGDWKL-IDGTGSGGFSY---PRGKEKLGLPPGQ---LYNLSTDPGESNNL 394
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
14-357 |
2.62e-65 |
|
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: 216.18 E-value: 2.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 14 GGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgaFLPPHQGFHRFLGIPYSHdqgpcqnltcFPPATpcdggcDQGLV 93
Cdd:cd16157 86 GGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ--YHPLKHGFDEWFGAPNCH----------FGPYD------NKAYP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 94 PIPLLANLSVEAQ---------PPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFG 164
Cdd:cd16157 148 NIPVYRDWEMIGRyyeefkidkKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGLYG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 165 DSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETM-RMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPG-V 242
Cdd:cd16157 228 DAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALIsAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGqV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 243 THELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLgTGKSPRQSLFFYpsypdevRG--VFAVRTGKYKAHFFT-QG 318
Cdd:cd16157 308 SHQLGSLMDLFTTSLALAGLPIPsDRAIDGIDLLPVLL-NGKEKDRPIFYY-------RGdeLMAVRLGQYKAHFWTwSN 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 146229327 319 SAHSDTTADPACHAS--SSLTAH------EPPLLYDLSKDPGENYNL 357
Cdd:cd16157 380 SWEEFRKGINFCPGQnvPGVTTHnqtdhtKLPLLFHLGRDPGEKYPI 426
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
11-353 |
1.86e-63 |
|
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: 212.53 E-value: 1.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 11 SSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPE----GAFLPPHQGFHRFLGIPYSH------DQGPCQNLTCFPP 80
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCEsrndFCHHPLNHGFDYFYGLPLTNlkdcgdGSNGEYDLSFDPL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 81 ATPCDGGCD--------------------------QGLVPIP--------------LLANLSVEAQPPWLPGLEARYMAF 120
Cdd:cd16159 161 FPLLTAFVLitaltiflllylgavskrffvfllilSLLFISLfflllitnryfnciLMRNHEVVEQPMSLENLTQRLTKE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 121 AHDLMADaqRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGP 200
Cdd:cd16159 241 AISFLER--NKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 201 ETMRMSR-----GGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPN-VTLDGFD 273
Cdd:cd16159 319 HLEEISVggeygGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGsVIDEPTSLMDIFPTVAALAGAPLPSdRIIDGRD 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 274 LSPLLLGTGK-SPRQSLFFYPSypDEVRGV-FAVRTGK--YKAHFFTQGSaHSDTTADPA---CHAS-SSLTAHEPPLLY 345
Cdd:cd16159 399 LMPLLTGQEKrSPHEFLFHYCG--AELHAVrYRPRDGGavWKAHYFTPNF-YPGTEGCCGtllCRCFgDSVTHHDPPLLF 475
|
....*...
gi 146229327 346 DLSKDPGE 353
Cdd:cd16159 476 DLSADPSE 483
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
2-368 |
2.64e-55 |
|
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: 188.14 E-value: 2.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 2 GMYP---GVlVPSSRGG--LPLEEVTVAEVLAARGYLTGMAGKWHLGVGPegAFLPPHQGFHRFLGIpyshdqgpcqnlt 76
Cdd:cd16146 58 GRYPfrtGV-WHTILGRerMRLDETTLAEVFKDAGYRTGIFGKWHLGDNY--PYRPQDRGFDEVLGH------------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 77 cfppatpCDGGCDQglvpIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADA------QRQDRPFFLYYASHHTHYPQFS 150
Cdd:cd16146 122 -------GGGGIGQ----YPDYWGNDYFDDTYYHNGKFVKTEGYCTDVFFDEaidfieENKDKPFFAYLATNAPHGPLQV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 151 GQSFAERSGRGPFGDSL-----M--ELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSR--GGcsglLRCGKGTT 221
Cdd:cd16146 191 PDKYLDPYKDMGLDDKLaafygMieNIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRfnAG----MRGKKGSV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 222 YEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLG-TGKSPRQSLFFY---PSY 295
Cdd:cd16146 267 YEGGHRVPFFIRWPGKILAGkDVDTLTAHIDLLPTLLDLCGVKLPeGIKLDGRSLLPLLKGeSDPWPERTLFTHsgrWPP 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146229327 296 PDEVRGVFAVRTGKYKahfFTQGSAhsdttadpachasssltahEPPLLYDLSKDPGENYNllggVAGATPEV 368
Cdd:cd16146 347 PPKKKRNAAVRTGRWR---LVSPKG-------------------FQPELYDIENDPGEEND----VADEHPEV 393
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
10-357 |
4.62e-53 |
|
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: 182.41 E-value: 4.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 10 PSSRGGLPL--EEVTVAEVLAARGYLTGMAGKWHLG-VGPEGAflPPHQGFHRFLGIpysHDQGPCQNLtcFPPATPCDG 86
Cdd:cd16145 71 SEPGGQDPLppDDVTLAEVLKKAGYATAAFGKWGLGgPGTPGH--PTKQGFDYFYGY---LDQVHAHNY--YPEYLWRNG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 87 GcdqgLVPIPLlANLSVEAQPPWLPGLEARYmafAHDLMADA------QRQDRPFFLYYAS---H-HTHYPQFSG--QSF 154
Cdd:cd16145 144 E----KVPLPN-NVIPPLDEGNNAGGGGGTY---SHDLFTDEaldfirENKDKPFFLYLAYtlpHaPLQVPDDGPykYKP 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 155 AERSGRGPFGDSLME---------LDAAVGTLMTAIGDLGLLEETLVIFTADNGPEtmrmSRGGC---------SGLLRC 216
Cdd:cd16145 216 KDPGIYAYLPWPQPEkayaamvtrLDRDVGRILALLKELGIDENTLVVFTSDNGPH----SEGGSehdpdffdsNGPLRG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 217 GKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYPSY 295
Cdd:cd16145 292 YKRSLYEGGIRVPFIARWPGKIPAGsVSDHPSAFWDFMPTLADLAGAEPPE-DIDGISLLPTLLGKPQQQQHDYLYWEFY 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 146229327 296 pdEVRGVFAVRTGKYKAHFFTQGSahsdttadpachasssltahEPPLLYDLSKDPGENYNL 357
Cdd:cd16145 371 --EGGGAQAVRMGGWKAVRHGKKD--------------------GPFELYDLSTDPGETNNL 410
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
2-357 |
1.08e-48 |
|
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: 170.42 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 2 GMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgAFLPPHQGFHRFLGiPYSHDQGPCQNLTCFPPA 81
Cdd:cd16029 65 GMQHGVILAGEPYGLPLNETLLPQYLKELGYATHLVGKWHLGFYTW-EYTPTNRGFDSFYG-YYGGAEDYYTHTSGGAND 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 82 TPCDGGCDQGLVPipllanlsveaqppwlPGLEARYMAfahDLMAD-AQR------QDRPFFLYYASHHTHYP-QFSGQS 153
Cdd:cd16029 143 YGNDDLRDNEEPA----------------WDYNGTYST---DLFTDrAVDiienhdPSKPLFLYLAFQAVHAPlQVPPEY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 154 FAERSGRGPFGDS---------LMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSrGGCSGLLRCGKGTTYEG 224
Cdd:cd16029 204 ADPYEDKFAHIKDedrrtyaamVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRGGKNTLWEG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 225 GVREPALaFWPGHI---APGVTHELASSLDLLPTLAALAGA-PLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVR 300
Cdd:cd16029 283 GVRVPAF-VWSPLLppkRGTVSDGLMHVTDWLPTLLSLAGGdPDDLPPLDGVDQWDALSGGAPSPRTEILLNIDDITRTT 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 146229327 301 GVFAVRTGKYKAHFFTQgsahsdttadpachasssltahepplLYDLSKDPGENYNL 357
Cdd:cd16029 362 GGAAIRVGDWKLIVGKP--------------------------LFNIENDPCERNDL 392
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
2-329 |
9.65e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 156.61 E-value: 9.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 2 GMYP-------GVLVPSsrgglpleEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCqn 74
Cdd:cd16151 58 GKYNfrnyvvfGYLDPK--------QKTFGHLLKDAGYATAIAGKWQLGGGRGDGDYPHEFGFDEYCLWQLTETGEKY-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 75 ltcFPPATPcdggcdqglvpIPLLANLSVeaqppwlpgLEARYMAFAHDLMAD------AQRQDRPFFLYYASHHTHYP- 147
Cdd:cd16151 128 ---SRPATP-----------TFNIRNGKL---------LETTEGDYGPDLFADflidfiERNKDQPFFAYYPMVLVHDPf 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 148 ---------QFSGQSFAERSGRgpFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNG--PETMRMSRGgcsGLLRC 216
Cdd:cd16151 185 vptpdspdwDPDDKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGthRPITSRTNG---REVRG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 217 GKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLG-TGKSPRQSLFFYP 293
Cdd:cd16151 260 GKGKTTDAGTHVPLIVNWPGLIPAGgVSDDLVDFSDFLPTLAELAGAPLPeDYPLDGRSFAPQLLGkTGSPRREWIYWYY 339
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 146229327 294 SYPDEVRGVFAVRTGKYK----AHFFtqgsahsDTTADPA 329
Cdd:cd16151 340 RNPHKKFGSRFVRTKRYKlyadGRFF-------DLREDPL 372
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
2-357 |
8.20e-42 |
|
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: 151.51 E-value: 8.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 2 GMYP---GVLVPSSRGG-LPLEEVTVAEVLAARGYLTGMAGKWHlgVGPEGAFLPPHQGFHRFLGIPYSHDQgpcqnltc 77
Cdd:cd16027 58 GLYPhqnGAHGLRSRGFpLPDGVKTLPELLREAGYYTGLIGKTH--YNPDAVFPFDDEMRGPDDGGRNAWDY-------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 78 fppatpcdggcdqglvpipllanlsVEAQPPWLpglearymafahdlmaDAQRQDRPFFLYYASHHTHYPQFSGQSFAE- 156
Cdd:cd16027 128 -------------------------ASNAADFL----------------NRAKKGQPFFLWFGFHDPHRPYPPGDGEEPg 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 157 ------------------RSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGpetMRMSRggcsgllrcGK 218
Cdd:cd16027 167 ydpekvkvppylpdtpevREDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG---MPFPR---------AK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 219 GTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFY----P 293
Cdd:cd16027 235 GTLYDSGLRVPLIVRWPGKIKPGsVSDALVSFIDLAPTLLDLAGIEPPE-YLQGRSFLPLLKGEKDPGRDYVFAErdrhD 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 146229327 294 SYPDEVRgvfAVRTGKYK-AHFFtqgsahsdttadpachasssltahEPPLLYDLSKDPGENYNL 357
Cdd:cd16027 314 ETYDPIR---SVRTGRYKyIRNY------------------------MPEELYDLKNDPDELNNL 351
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
9-262 |
4.78e-38 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 139.48 E-value: 4.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 9 VPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAflPPHQGFHRFLGIPYSHDQgpcQNLTCFPPATPCDGGC 88
Cdd:pfam00884 68 YVSTPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS--PCNLGFDKFFGRNTGSDL---YADPPDVPYNCSGGGV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 89 dqglvpipllanlsveaqppwlpgLEARYMAFAHDLmadAQRQDRPFFLYYASHHTHYP------------QFSGQSFAE 156
Cdd:pfam00884 143 ------------------------SDEALLDEALEF---LDNNDKPFFLVLHTLGSHGPpyypdrypekyaTFKPSSCSE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 157 RSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPetmrmSRGGCSGLLRCGKG-TTYEGGVREPALAFWP 235
Cdd:pfam00884 196 EQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGE-----SLGEGGGYLHGGKYdNAPEGGYRVPLLIWSP 270
|
250 260
....*....|....*....|....*...
gi 146229327 236 GHIAPG-VTHELASSLDLLPTLAALAGA 262
Cdd:pfam00884 271 GGKAKGqKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
2-273 |
1.38e-36 |
|
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293746 [Multi-domain] Cd Length: 236 Bit Score: 133.72 E-value: 1.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 2 GMYP---GVLVPSSRG-GLPLEEVTVAEVLAARGYLTGMAGKWHlgvgpegaflpphqgfhrflgipyshdqgpcqnltc 77
Cdd:cd16022 59 GRYPhrhGVRGNVGNGgGLPPDEPTLAELLKEAGYRTALIGKWH------------------------------------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 78 fppatpcdggcdqglvpipllaNLSVEaqppWLpglearymafahdlmaDAQRQDRPFFLYYASHHTHYPqfsgqsFAer 157
Cdd:cd16022 103 ----------------------DEAID----FI----------------ERRDKDKPFFLYVSFNAPHPP------FA-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 158 sgrgpFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPetMRMSRGgcsglLRCGKGTTYEGGVREPALAFWPGH 237
Cdd:cd16022 133 -----YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGD--MLGDHG-----LRGKKGSLYEGGIRVPFIVRWPGK 200
|
250 260 270
....*....|....*....|....*....|....*..
gi 146229327 238 IAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFD 273
Cdd:cd16022 201 IPAGqVSDALVSLLDLLPTLLDLAGIEPPE-GLDGRS 236
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
10-357 |
1.68e-35 |
|
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: 134.88 E-value: 1.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 10 PSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGvgpegaflppHQGFHrflgipYSHDqgpcqnLTcfppatpcdggcD 89
Cdd:cd16025 78 PGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG----------PDDYY------STDD------LT------------D 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 90 QGLvpipllanlsveaqppwlpglearymafahDLMADAQRQDRPFFLYYASHHTHYP---------QFSGQ-------- 152
Cdd:cd16025 124 KAI------------------------------EYIDEQKAPDKPFFLYLAFGAPHAPlqapkewidKYKGKydagwdal 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 153 ------------------SFAERSGRGPFGDSL-----------ME--------LDAAVGTLMTAIGDLGLLEETLVIFT 195
Cdd:cd16025 174 reerlerqkelglipadtKLTPRPPGVPAWDSLspeekklearrMEvyaamvehMDQQIGRLIDYLKELGELDNTLIIFL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 196 ADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAP--GVTHELASSLDLLPTLAALAGAPLPNV------ 267
Cdd:cd16025 254 SDNGASAEPGWANASNTPFRLYKQASHEGGIRTPLIVSWPKGIKAkgGIRHQFAHVIDIAPTILELAGVEYPKTvngvpq 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 268 -TLDGFDLSPLLLG-TGKSPRQSLFFypsypdEVRGVFAVRTGKYKAhfftqgsahsdttadpachasssLTAHEPPL-- 343
Cdd:cd16025 334 lPLDGVSLLPTLDGaAAPSRRRTQYF------ELFGNRAIRKGGWKA-----------------------VALHPPPGwg 384
|
410
....*....|....*...
gi 146229327 344 ----LYDLSKDPGENYNL 357
Cdd:cd16025 385 dqweLYDLAKDPSETHDL 402
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
20-359 |
1.76e-35 |
|
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: 135.35 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 20 EVTVAEVLAARGYLTGMAGKWHLGVGPEgaflPPHQGFHRFLGIPYSHDQGPCQNLTcfppatpcdggcDQGLVPIP--- 96
Cdd:cd16031 81 QPTYPKLLRKAGYQTAFIGKWHLGSGGD----LPPPGFDYWVSFPGQGSYYDPEFIE------------NGKRVGQKgyv 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 97 --LLANLSVEaqppWLpglearymafahdlmaDAQRQDRPFFLYY---ASH--------HTH--------YPQ------F 149
Cdd:cd16031 145 tdIITDKALD----FL----------------KERDKDKPFCLSLsfkAPHrpftpaprHRGlyedvtipEPEtfddddY 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 150 SGQS-FAERSGRGPFGD--------------------SLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGpetmrmsrg 208
Cdd:cd16031 205 AGRPeWAREQRNRIRGVldgrfdtpekyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNG--------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 209 gcsglLRCG------KGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGT 281
Cdd:cd16031 276 -----FFLGehglfdKRLMYEESIRVPLIIRDPRLIKAGtVVDALVLNIDFAPTILDLAGVPIPE-DMQGRSLLPLLEGE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 282 GKSPRQSLFFY-----PSYPDeVRGVFAVRTGKYK-AHFFTQGsahsdttadpachassslTAHEpplLYDLSKDPGENY 355
Cdd:cd16031 350 KPVDWRKEFYYeyyeePNFHN-VPTHEGVRTERYKyIYYYGVW------------------DEEE---LYDLKKDPLELN 407
|
....
gi 146229327 356 NLLG 359
Cdd:cd16031 408 NLAN 411
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
2-357 |
6.31e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 124.99 E-value: 6.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 2 GMYP---GVLVPSSRggLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEG-----AFLPPH---QGF---------HRFL 61
Cdd:cd16034 60 GQYPltnGVFGNDVP--LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNdgradDYTPPPerrHGFdywkgyecnHDHN 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 62 GIPYSHDQGPcqnltcfppaTPCDGGcdqglvpipllanlsveaqppWLPGLEARyMAFahDLMADAQRQDRPFFLY--Y 139
Cdd:cd16034 138 NPHYYDDDGK----------RIYIKG---------------------YSPDAETD-LAI--EYLENQADKDKPFALVlsW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 140 ASHHTHY---PQ-----FSGQSFAERsGRGPFGDSLME---------------LDAAVGTLMTAIGDLGLLEETLVIFTA 196
Cdd:cd16034 184 NPPHDPYttaPEeyldmYDPKKLLLR-PNVPEDKKEEAglredlrgyyamitaLDDNIGRLLDALKELGLLENTIVVFTS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 197 DNGpETMrmsrgGCSGLLRcgKGTTYEGGVREPALAFWPGHI-APGVTHELASSLDLLPTLAALAGAPLPNvTLDGFDLS 275
Cdd:cd16034 263 DHG-DML-----GSHGLMN--KQVPYEESIRVPFIIRYPGKIkAGRVVDLLINTVDIMPTLLGLCGLPIPD-TVEGRDLS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 276 PLLLGTGKSPRQSLFFYPSYP------DEVRGVFAVRTGKYKAhfftqgsahsdttadpachassSLTAHEPPLLYDLSK 349
Cdd:cd16034 334 PLLLGGKDDEPDSVLLQCFVPfgggsaRDGGEWRGVRTDRYTY----------------------VRDKNGPWLLFDNEK 391
|
....*...
gi 146229327 350 DPGENYNL 357
Cdd:cd16034 392 DPYQLNNL 399
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
121-357 |
6.46e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 104.95 E-value: 6.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 121 AHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRG------------PFGDSLM-------------------- 168
Cdd:cd16155 111 AIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPEtiplpenflpqhPFDNGEGtvrdeqlapfprtpeavrqh 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 169 ---------ELDAAVGTLMTAIGDLGLLEETLVIFTADNGpetmrMSRGGcSGLLrcGKGTTYEGGVREPALAFWPGhIA 239
Cdd:cd16155 191 laeyyamitHLDAQIGRILDALEASGELDNTIIVFTSDHG-----LAVGS-HGLM--GKQNLYEHSMRVPLIISGPG-IP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 240 PG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYpsYPDEVRgvfAVRTGKYKAHFFTQG 318
Cdd:cd16155 262 KGkRRDALVYLQDVFPTLCELAGIEIPE-SVEGKSLLPVIRGEKKAVRDTLYGA--YRDGQR---AIRDDRWKLIIYVPG 335
|
250 260 270
....*....|....*....|....*....|....*....
gi 146229327 319 SAHSdttadpachasssltaheppLLYDLSKDPGENYNL 357
Cdd:cd16155 336 VKRT--------------------QLFDLKKDPDELNNL 354
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
284-417 |
1.96e-24 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 97.38 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 284 SPRQSLFFYPSYPdevrgVFAVRTGKYKAHFFTqGSAHSDTtaDPACHASS-SLTAHEPPLLYDLSKDPGENYNLlggvA 362
Cdd:pfam14707 1 SPHEFLFHYCGAA-----LHAVRWGPYKAHFFT-PSFDPPG--AEGCYGSKvPVTHHDPPLLFDLERDPSEKYPL----S 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 146229327 363 GATPEVLQALKQLQLLKAQLDAAVTFGPSQVARGE---DPALQICChPGCtprPACCH 417
Cdd:pfam14707 69 PDSPEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNylwDPWLQPCC-PTF---PACTC 122
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
2-359 |
4.00e-24 |
|
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: 103.45 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 2 GMYP---GVL-----VPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGvgpegaflpphqgfhrflgipyshdqgpcq 73
Cdd:cd16033 59 GLYPhehGVLnnvenAGAYSRGLPPGVETFSEDLREAGYRNGYVGKWHVG------------------------------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 74 nltcfPPATPCDGGCDqGLVPipllanlsVEAQPpwlpglEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQ- 152
Cdd:cd16033 109 -----PEETPLDYGFD-EYLP--------VETTI------EYFLADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 153 --------------SFAE---------RSGRGPFGDSLME-----------------LDAAVGTLMTAIGDLGLLEETLV 192
Cdd:cd16033 169 yldmydpediplpeSFADdfedkpyiyRRERKRWGVDTEDeedwkeiiahywgyitlIDDAIGRILDALEELGLADDTLV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 193 IFTADNGpETMrmsrgGCSGLLRcgKGT-TYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNVTlD 270
Cdd:cd16033 249 IFTSDHG-DAL-----GAHRLWD--KGPfMYEETYRIPLIIKWPGVIAAGqVVDEFVSLLDLAPTILDLAGVDVPPKV-D 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 271 GFDLSPLLLG-TGKSPRQSLFF---YPSYPDEVRgvfAVRTGKYKAHFftqgsahSDTTADpachasssltahEpplLYD 346
Cdd:cd16033 320 GRSLLPLLRGeQPEDWRDEVVTeynGHEFYLPQR---MVRTDRYKYVF-------NGFDID------------E---LYD 374
|
410
....*....|...
gi 146229327 347 LSKDPGENYNLLG 359
Cdd:cd16033 375 LESDPYELNNLID 387
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
121-352 |
6.21e-24 |
|
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: 101.47 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 121 AHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSF----AERSGRGPFGdsLME-LDAAVGTLMTAIGDLGLLEETLVIFT 195
Cdd:cd16037 119 AVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFydlyVRRARAAYYG--LVEfLDENIGRVLDALEELGLLDNTLIIYT 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 196 ADNGpETMrmsrgGCSGLLrcGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNvTLDGFDLS 275
Cdd:cd16037 197 SDHG-DML-----GERGLW--GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPP-DLDGRSLL 267
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 146229327 276 PLLLGTGKSPRQSLFFYPSYPDEVrGVFAVRTGKYKAHFFtqgsahsdttadpachasssltAHEPPLLYDLSKDPG 352
Cdd:cd16037 268 PLAEGPDDPDRVVFSEYHAHGSPS-GAFMLRKGRWKYIYY----------------------VGYPPQLFDLENDPE 321
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
112-260 |
4.61e-22 |
|
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: 94.02 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 112 GLEARYMAFAHDLmaDAQRQDRPFFLYYashhtHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETL 191
Cdd:cd00016 100 GYRTGVIGLLKAI--DETSKEKPFVLFL-----HFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTV 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 192 VIFTADNGpetmrMSRGGCSGLLR-CGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALA 260
Cdd:cd00016 173 IIVTADHG-----GIDKGHGGDPKaDGKADKSHTGMRVPFIAYGPGVKKGGVKHELISQYDIAPTLADLL 237
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
129-351 |
1.66e-21 |
|
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: 94.57 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 129 QRQDRPFFLYYASHHTHYPQFSGQSF----AERSGRGPFGdSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGpeTMR 204
Cdd:cd16032 129 GEDGRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHG--DML 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 205 MSRGgcsgllRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNV--TLDGFDLSPLLLGTG 282
Cdd:cd16032 206 GERG------LWYKMSFFEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHvpPLDGRSLLPLLEGGD 279
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146229327 283 KSPRQSlfFYPSYPDEvrGVFA----VRTGKYKahfFTqgsahsdttadpACHAsssltahEPPLLYDLSKDP 351
Cdd:cd16032 280 SGGEDE--VISEYLAE--GAVApcvmIRRGRWK---FI------------YCPG-------DPDQLFDLEADP 326
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
19-276 |
2.18e-20 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 89.99 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 19 EEVTVAEVLAARGYLTGMAGKWHLGvgpegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdggcDQGLvpipll 98
Cdd:cd16149 88 GQTTLPEVLQDAGYRCGLSGKWHLG---------------------------------------------DDAA------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 99 anlsveaqppwlpglearymafahDLMADAQRQDRPFFL---YYASHHTHypqfsgQSFAERSGrgpfgdslmeLDAAVG 175
Cdd:cd16149 117 ------------------------DFLRRRAEAEKPFFLsvnYTAPHSPW------GYFAAVTG----------VDRNVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 176 TLMTAIGDLGLLEETLVIFTADNGpetMRMsrgGCSGLLRCGKGTT----YEGGVREPALAFWPGHIAPG-VTHELASSL 250
Cdd:cd16149 157 RLLDELEELGLTENTLVIFTSDNG---FNM---GHHGIWGKGNGTFplnmYDNSVKVPFIIRWPGVVPAGrVVDSLVSAY 230
|
250 260
....*....|....*....|....*..
gi 146229327 251 DLLPTLAALAGAPLP-NVTLDGFDLSP 276
Cdd:cd16149 231 DFFPTLLELAGVDPPaDPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
2-359 |
2.90e-20 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 91.52 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 2 GMYP---GVLVpsSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLgvgpegaflpphqgfhrflgipyshdqgpcqnltcf 78
Cdd:cd16152 60 GLYPtetGCFR--NGIPLPADEKTLAHYFRDAGYETGYVGKWHL------------------------------------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 79 ppatpcdggcdqglvpipllanlsveaqppwlpgleARYMA-----FAHDLMADAQrQDRPFFL---YYASHHT----HY 146
Cdd:cd16152 102 ------------------------------------AGYRVdaltdFAIDYLDNRQ-KDKPFFLflsYLEPHHQndrdRY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 147 --PQFSGQSFAERS------GRGpfGDSLMEL----------DAAVGTLMTAIGDLGLLEETLVIFTADNGpetmrmsrg 208
Cdd:cd16152 145 vaPEGSAERFANFWvppdlaALP--GDWAEELpdylgccerlDENVGRIRDALKELGLYDNTIIVFTSDHG--------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 209 gCSGLLRCG--KGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPR 286
Cdd:cd16152 214 -CHFRTRNAeyKRSCHESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPE-EMQGRSLLPLVDGKVEDWR 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146229327 287 QSLFFYPSypdEVRGVFAVRTGKYKAhfftqgsAHSDTTADPACHASSSltAHEPPLLYDLSKDPGENYNLLG 359
Cdd:cd16152 292 NEVFIQIS---ESQVGRAIRTDRWKY-------SVAAPDKDGWKDSGSD--VYVEDYLYDLEADPYELVNLIG 352
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
18-359 |
2.08e-18 |
|
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: 86.45 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 18 LEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGI--PYSHDqgpcqNLTcfppatpcdggcdqglvpi 95
Cdd:cd16147 82 LERSTLPVWLQEAGYRTAYAGKYLNGYGVPGGVSYVPPGWDEWDGLvgNSTYY-----NYT------------------- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 96 plLANLSVEAQPPWLPGlearymAFAHDLMAD--------AQRQDRPFFLYYASH--HTHY---PQFSGQSF-AERSGRG 161
Cdd:cd16147 138 --LSNGGNGKHGVSYPG------DYLTDVIANkaldflrrAAADDKPFFLVVAPPapHGPFtpaPRYANLFPnVTAPPRP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 162 PFGD---------------------------------SLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETmrmsrg 208
Cdd:cd16147 210 PPNNpdvsdkphwlrrlpplnptqiayidelyrkrlrTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHL------ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 209 GCSGLLRcGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNvTLDgfdlsplllgtGKSPRQS 288
Cdd:cd16147 284 GQHRLPP-GKRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGAPPPS-DMD-----------GRSCGDS 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146229327 289 LffYPSYPdevrgvfAVRT--GKYKAHFFtqgsahSDTTADpachasssltaHEpplLYDLSKDPGENYNLLG 359
Cdd:cd16147 351 N--NNTYK-------CVRTvdDTYNLLYF------EWCTGF-----------RE---LYDLTTDPYQLTNLAG 394
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
16-292 |
5.97e-17 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 81.10 E-value: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 16 LPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAflpphqgfhrflgipYSHDQGPCQNLTCFppatpcdggcdqglvpi 95
Cdd:cd16035 79 LSPDVPTLGHMLRAAGYYTAYKGKWHLSGAAGGG---------------YKRDPGIAAQAVEW----------------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 96 plLANL--SVEAQPPWL-------PglearymafaHDLMADAQRQDRpfflyYASHHTHYpqfsgqsfaersgrgpfGDS 166
Cdd:cd16035 127 --LRERgaKNADGKPWFlvvslvnP----------HDIMFPPDDEER-----WRRFRNFY-----------------YNL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 167 LMELDAAVGTLMTAIGDLGLLEETLVIFTADNGpetmrmSRGGCSGLLRCGkGTTYEGGVREPAL----AFWPGhiaPGV 242
Cdd:cd16035 173 IRDVDRQIGRVLDALDASGLADNTIVVFTSDHG------EMGGAHGLRGKG-FNAYEEALHVPLIishpDLFGT---GQT 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 146229327 243 THELASSLDLLPTLAALAGAPLPNV-----TLDGFDLSPLLLGTGKSPRQ--SLFFY 292
Cdd:cd16035 243 TDALTSHIDLLPTLLGLAGVDAEARateapPLPGRDLSPLLTDADADAVRdgILFTY 299
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
13-276 |
2.88e-16 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 78.36 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 13 RGGLPLEEVTVAEVLAARGYLTGMAGkWHLGVGPEGAFlppHQGFHRFLGIPYSHDQGPcqnltcFPPATPCDGGCDQGL 92
Cdd:cd16148 69 GGPLEPDDPTLAEILRKAGYYTAAVS-SNPHLFGGPGF---DRGFDTFEDFRGQEGDPG------EEGDERAERVTDRAL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 93 vpipllanlsveaqpPWLpglearymafahdlmaDAQRQDRPFFL---YYASHHthypqfsgqsfaersgrgPFG--DSL 167
Cdd:cd16148 139 ---------------EWL----------------DRNADDDPFFLflhYFDPHE------------------PYLydAEV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 168 MELDAAVGTLMTAIGDLGLLEETLVIFTADNGpETMrmsrgGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELA 247
Cdd:cd16148 170 RYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG-EEF-----GEHGLYWGHGSNLYDEQLHVPLIIRWPGKEPGKRVDALV 243
|
250 260
....*....|....*....|....*....
gi 146229327 248 SSLDLLPTLAALAGAPlPNVTLDGFDLSP 276
Cdd:cd16148 244 SHIDIAPTLLDLLGVE-PPDYSDGRSLLP 271
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
171-357 |
3.92e-16 |
|
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: 79.92 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 171 DAAVGTLMTAIGDLGLLEETLVIFTADNGpetmrMSRG--GcsgllRCGKGTTYEGGVREPaLAFW-PGHIAPG-VTHEL 246
Cdd:cd16030 271 DAQVGRVLDALEELGLADNTIVVLWSDHG-----WHLGehG-----HWGKHTLFEEATRVP-LIIRaPGVTKPGkVTDAL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 247 ASSLDLLPTLAALAGAPLPNVtLDGFDLSPLLLGTGKSPRQslFFYPSYPDEVRGVFAVRTGKYKahfFTQgsaHSDtta 326
Cdd:cd16030 340 VELVDIYPTLAELAGLPAPPC-LEGKSLVPLLKNPSAKWKD--AAFSQYPRPSIMGYSIRTERYR---YTE---WVD--- 407
|
170 180 190
....*....|....*....|....*....|.
gi 146229327 327 dpachaSSSLTAHEpplLYDLSKDPGENYNL 357
Cdd:cd16030 408 ------FDKVGAEE---LYDHKNDPNEWKNL 429
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
169-367 |
5.43e-16 |
|
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: 79.61 E-value: 5.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 169 ELDAAVGTLMTAIGDLGLLEETLVIFTADNGpETMrmsrgGCSGLLrcGKGTTYEGGVREPALAFWPG----HIAPGVTH 244
Cdd:cd16028 246 EVDDHLGRLFDYLKETGQWDDTLIVFTSDHG-EQL-----GDHWLW--GKDGFFDQAYRVPLIVRDPRreadATRGQVVD 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 245 ELASSLDLLPTLAALAGAPLPNVtLDGFDLSPLLLG-TGKSPRQSLF----FYPSYPDEVR----------GVFAVRTGK 309
Cdd:cd16028 318 AFTESVDVMPTILDWLGGEIPHQ-CDGRSLLPLLAGaQPSDWRDAVHyeydFRDVSTRRPQealglspdecSLAVIRDER 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 146229327 310 YK-AHFftqgsahsdttadpachassslTAHePPLLYDLSKDPGENYNLlggvaGATPE 367
Cdd:cd16028 397 WKyVHF----------------------AAL-PPLLFDLKNDPGELRDL-----AADPA 427
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
124-351 |
7.74e-16 |
|
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: 78.35 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 124 LMADAQRQDRPFFLYYASHHTH-YP-QFSGQSFAE-RSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGP 200
Cdd:cd16171 156 IRKEAPNLTQPFALYLGLNLPHpYPsPSMGENFGSiRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 201 ETMRMSrggcsgllRCGKGTTYEGGVREPALAFWPGhIAPGVTHELASSL-DLLPTLAALAGAPLPNvTLDGFDLSPLLL 279
Cdd:cd16171 236 LAMEHR--------QFYKMSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLvDIYPTMLDIAGVPQPQ-NLSGYSLLPLLS 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 146229327 280 GTGKSPRQSLFFYPSYP-DEVRG------VFAVRTGKYKAHFFTQGsahsdttadpachasssltAHEPPLLYDLSKDP 351
Cdd:cd16171 306 ESSIKESPSRVPHPDWVlSEFHGcnvnasTYMLRTNSWKYIAYADG-------------------NSVPPQLFDLSKDP 365
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
151-359 |
2.71e-14 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 74.32 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 151 GQSFAERSGRGPFGdSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGpETMrmsrgGCSGLLRcgKGTTYEGGVREPA 230
Cdd:PRK13759 259 GEEYARRARAAYYG-LITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG-DML-----GDHYLFR--KGYPYEGSAHIPF 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 231 LAFWPGHIAPG----VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSL-----FFYPS--Ypdev 299
Cdd:PRK13759 330 IIYDPGGLLAGnrgtVIDQVVELRDIMPTLLDLAGGTIPD-DVDGRSLKNLIFGQYEGWRPYLhgehaLGYSSdnY---- 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 300 rgvfaVRTGKYKAHFFTQgsahsdttadpachassslTAHEPplLYDLSKDPGENYNLLG 359
Cdd:PRK13759 405 -----LTDGKWKYIWFSQ-------------------TGEEQ--LFDLKKDPHELHNLSP 438
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
2-354 |
1.05e-12 |
|
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: 68.92 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 2 GMY---PGVLVPSSRGGLPLEEVTVAEVLAAR--GYLTGMAGKWHLGVGPEGAFLPPhqGFHRFLGIPYSHDQGPCQ-NL 75
Cdd:cd16154 60 GKYgfrTGVLAVPDELLLSEETLLQLLIKDATtaGYSSAVIGKWHLGGNDNSPNNPG--GIPYYAGILGGGVQDYYNwNL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 76 TCFPPATPCDGGCDQGLVpipllaNLSVEaqppWLpglearymafahdlmadaQRQDRPFFLYYA-----------SHHT 144
Cdd:cd16154 138 TNNGQTTNSTEYATTKLT------NLAID----WI------------------DQQTKPWFLWLAynaphtpfhlpPAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 145 HYPQFSGQSFAERSGRGPFGDSLME-LDAAVGTLMTAIgDLGLLEETLVIFTADNG-PETMR---MSRGGcsgllrcGKG 219
Cdd:cd16154 190 HSRSLLGDSADIEANPRPYYLAAIEaMDTEIGRLLASI-DEEERENTIIIFIGDNGtPGQVVdlpYTRNH-------AKG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 220 TTYEGGVREPALAFWPGhIAPGVTHE--LASSLDLLPTLAALAGAPLPNVTlDGFDLSPLLLGTGKSPRQslFFYPSYPD 297
Cdd:cd16154 262 SLYEGGINVPLIVSGAG-VERANEREsaLVNATDLYATIAELAGVDAAEIH-DSVSFKPLLSDVNASTRQ--YNYTEYES 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 146229327 298 EVRGVFAVRTGKYKAHFFTQGSAHsdttadpachasssltahepplLYDLSKDPGEN 354
Cdd:cd16154 338 PTTTGWATRNQYYKLIESENGQEE----------------------LYDLINDPSEQ 372
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
168-359 |
2.09e-11 |
|
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: 65.33 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 168 MELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETmrmsrgGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELA 247
Cdd:cd16150 207 SRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYT------GDYGLVEKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALV 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 248 SSLDLLPTLAALAGAPLPNVTLdGFDLSPLLLGTGKSPRQSLF----FYPSYPDevrgvfAVRTGKYKAHFFT-QGSAHS 322
Cdd:cd16150 281 ELVDIPPTLLDLAGIPLSHTHF-GRSLLPVLAGETEEHRDAVFseggRLHGEEQ------AMEGGHGPYDLKWpRLLQQE 353
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 146229327 323 DTTADPACHASSSLTA------HEPPLLYDLSKDPGENYNLLG 359
Cdd:cd16150 354 EPPEHTKAVMIRTRRYkyvyrlYEPDELYDLEADPLELHNLIG 396
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
130-274 |
7.08e-10 |
|
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: 59.70 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 130 RQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFgdsLMELDAAVGTLMTAIGDLGLL---EETLVIFTADNGpetmrmS 206
Cdd:cd16153 140 DSDKPFFVRLSFLQPHTPVLPPKEFRDRFDYYAF---CAYGDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHG------W 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 146229327 207 RGGCSGLLrcGKGTTYEGGVREPALAFWPGHI---APGVTHELASSLDLLPTLAALAGAPLPNVT-LDGFDL 274
Cdd:cd16153 211 HLGEQGIL--AKFTFWPQSHRVPLIVVSSDKLkapAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDyLDGRDL 280
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
119-274 |
9.93e-10 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 60.44 E-value: 9.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 119 AFAHDLMADAQRQDRPFFLYY--ASHHTHYPQFSGQSFAERSGRGPFGD---SLMELDAAVGTLMTAIGDLGLLEETLVI 193
Cdd:COG1368 370 DLFDKALEELEKLKKPFFAFLitLSNHGPYTLPEEDKKIPDYGKTTLNNylnAVRYADQALGEFIEKLKKSGWYDNTIFV 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 194 FTADNGPetmrMSRGGCSGLLRCGKGTTyeggvrePALaFW-PGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGF 272
Cdd:COG1368 450 IYGDHGP----RSPGKTDYENPLERYRV-------PLL-IYsPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGR 517
|
..
gi 146229327 273 DL 274
Cdd:COG1368 518 DL 519
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
118-261 |
1.56e-08 |
|
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: 55.38 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 118 MAFAHDLMADAQRQdrPFFLY---YASHH-----THYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEE 189
Cdd:cd16015 143 FDQALEELEELKKK--PFFIFlvtMSNHGpydlpEEKKDEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYEN 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 146229327 190 TLVIFTADNGPetmrmsrggcsGLLRCGKGTTYEGGVRE--PALAFWPGHIAPGVTHELASSLDLLPTLAALAG 261
Cdd:cd16015 221 TIIVIYGDHLP-----------SLGSDYDETDEDPLDLYrtPLLIYSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
2-359 |
5.98e-07 |
|
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: 51.61 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 2 GMYPgvlvpSSRGG----LPLEE--VTVAEVLAARGYLTGMAGKWHL--------GVGPEGaflpphqgfhrflgipysh 67
Cdd:cd16156 59 GLYP-----HTNGSwtncMALGDnvKTIGQRLSDNGIHTAYIGKWHLdggdyfgnGICPQG------------------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 68 dqgpcqnltcFPPATPCDGGCdqglvpipLLANLSVEAQPPW---LPGLEARYMA----FAHDLMADA-----QRQDRPF 135
Cdd:cd16156 115 ----------WDPDYWYDMRN--------YLDELTEEERRKSrrgLTSLEAEGIKeeftYGHRCTNRAldfieKHKDEDF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 136 FLYYASHHTHYPQFSGQSFAE----------------------------RSGRGPFGDSL---MEL--------DAAVGT 176
Cdd:cd16156 177 FLVVSYDEPHHPFLCPKPYASmykdfefpkgenayddlenkplhqrlwaGAKPHEDGDKGtikHPLyfgcnsfvDYEIGR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 177 LMTAIGDLglLEETLVIFTADNGpETMrmsrgGCSGLLrcGKG-TTYEGGVREPALAFWPGHI-APGVTHELASSLDLLP 254
Cdd:cd16156 257 VLDAADEI--AEDAWVIYTSDHG-DML-----GAHKLW--AKGpAVYDEITNIPLIIRGKGGEkAGTVTDTPVSHIDLAP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 255 TLAALAGAPLPNVtLDGFDLSPLLLGTGKSPRQSLF---------------FYPsypdeVRGVFavrTGKYK--AHFFTQ 317
Cdd:cd16156 327 TILDYAGIPQPKV-LEGESILATIEDPEIPENRGVFvefgryevdhdgfggFQP-----VRCVV---DGRYKlvINLLST 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 146229327 318 GSahsdttadpachasssltahepplLYDLSKDPGENYNLLG 359
Cdd:cd16156 398 DE------------------------LYDLEKDPYEMHNLID 415
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
103-199 |
2.52e-04 |
|
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: 42.57 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 103 VEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYashHTHYPQFSGQSFaersgrGPFG----DSLMELDAAVGTLM 178
Cdd:cd16018 126 IPLGGYWQPYNDSFPFEERVDTILEWLDLERPDLILL---YFEEPDSAGHKY------GPDSpevnEALKRVDRRLGYLI 196
|
90 100
....*....|....*....|.
gi 146229327 179 TAIGDLGLLEETLVIFTADNG 199
Cdd:cd16018 197 EALKERGLLDDTNIIVVSDHG 217
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
123-199 |
1.92e-03 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 40.12 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 123 DLMADAQRQDRPFFLY-------YASHHThypqfsgqsfaersgrGPFG----DSLMELDAAVGTLMTAIGDLGLLEETL 191
Cdd:COG1524 172 AAALELLREGRPDLLLvylpdldYAGHRY----------------GPDSpeyrAALREVDAALGRLLDALKARGLYEGTL 235
|
....*...
gi 146229327 192 VIFTADNG 199
Cdd:COG1524 236 VIVTADHG 243
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
123-207 |
2.12e-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: 40.10 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229327 123 DLMADAQRQDRPFFLYYASHHTHYpqfSGQSFAERSGRgpFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPET 202
Cdd:pfam01663 152 DLPFADVAAERPDLLLVYLEEPDY---AGHRYGPDSPE--VEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTP 226
|
....*
gi 146229327 203 MRMSR 207
Cdd:pfam01663 227 VSDDK 231
|
|
| |
