|
Name |
Accession |
Description |
Interval |
E-value |
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
35-331 |
2.77e-134 |
|
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: 386.82 E-value: 2.77e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDMGWGDLGANWAETKDTT-NLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGG 113
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAILTpNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNDmgctdnpgynyppcpacpqsdgrwrnpdr 193
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 194 dcytdvalplyenlniveqpvnlSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQSQR-LYRAS 272
Cdd:cd16161 132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRgPYGDA 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 273 LQEMDSLVGQIKDKVDHV-AKENTLLWFAGDNGPWAQKCELAGsmGPFSGLWQTHQGGGG 331
Cdd:cd16161 189 LQEMDDLVGQIMDAVKHAgLKDNTLTWFTSDNGPWEVKCELAV--GPGTGDWQGNLGGSV 246
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-321 |
5.41e-125 |
|
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: 363.81 E-value: 5.41e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGG 113
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNDMGCTDNPGYNYPPCPAcpqsdgrwrnpdr 193
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 194 dcytdvalPLYENLNIVEQPVNLSGLAQKYAERAVEFIEQAstSGRPFLLYVGLAHMHVPLSVTPPLANPqSQR-LYRAS 272
Cdd:cd16026 148 --------PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGR-SGAgLYGDV 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958659108 273 LQEMDSLVGQIKDKVD--HVAkENTLLWFAGDNGPWAQKCELAGSMGPFSG 321
Cdd:cd16026 217 VEELDWSVGRILDALKelGLE-ENTLVIFTSDNGPWLEYGGHGGSAGPLRG 266
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
36-329 |
1.16e-78 |
|
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: 248.13 E-value: 1.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGGL 114
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGvFYPGSRGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 115 PLNETTLAEVLQQAGYVTAMIGKWHL--GHHGSYHPSFRGFDYYFGIPYSNDMGctdnPGYNYPPCPacpqsdgrwrnPD 192
Cdd:cd16158 82 PLNETTIAEVLKTVGYQTAMVGKWHLgvGLNGTYLPTHQGFDHYLGIPYSHDQG----PCQNLTCFP-----------PN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 193 RDCY-----TDVALPLYENLNIVEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQSQR 267
Cdd:cd16158 147 IPCFggcdqGEVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRG 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659108 268 LYRASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGPWAQKCELAGSMGPFS-GLWQTHQGG 329
Cdd:cd16158 227 PFGDALAELDGSVGELLQTLKENGiDNNTLVFFTSDNGPSTMRKSRGGNAGLLKcGKGTTYEGG 290
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
35-321 |
2.73e-75 |
|
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: 238.10 E-value: 2.73e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV---THNFAVTSV 111
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 112 GGLPLNETTLAEVLQQAGYVTAMIGKWHLG-----HHGSYH-PSFRGFDYY-FGIPYSNDMGCtDNPGYNYPpcpacpqs 184
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDFVgTNLPFTNSWAC-DDTGRHVD-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 185 dgrwrNPDRD-CYtdvalpLYENLNIVEQPVNLSGLAQKYAERAVEFIEqaSTSGRPFLLYVGLAHMHVPLSVTPPLANp 263
Cdd:cd16160 152 -----FPDRSaCF------LYYNDTIVEQPIQHEHLTETLVGDAKSFIE--DNQENPFFLYFSFPQTHTPLFASKRFKG- 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 264 QSQR-LYRASLQEMDSLVGQIKDK-VDHVAKENTLLWFAGDNGPWAQKCELAGSMGPFSG 321
Cdd:cd16160 218 KSKRgRYGDNINEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKG 277
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-329 |
1.38e-72 |
|
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: 231.97 E-value: 1.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG--VTHNFAVTS-- 110
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 111 ----VGGLPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNdMGCTDNPgyNYPPCPACPQSD- 185
Cdd:cd16157 81 pqniVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCH-FGPYDNK--AYPNIPVYRDWEm 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 186 -GRWrnpdrdcytdvalplYENLNIvEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQ 264
Cdd:cd16157 158 iGRY---------------YEEFKI-DKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTS 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659108 265 SQRLYRASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNG-PWAQKCELAGSMGPF-SGLWQTHQGG 329
Cdd:cd16157 222 QRGLYGDAVMELDSSVGKILESLKSLGiENNTFVFFSSDNGaALISAPEQGGSNGPFlCGKQTTFEGG 289
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
35-331 |
4.96e-71 |
|
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: 229.48 E-value: 4.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN------FAV 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASShgmrviLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 109 TSVGGLPLNETTLAEVLQQAGYVTAMIGKWHLGHH------GSYHPSFRGFDYYFGIPYSN--DMGCTDNPGYNYPPCPA 180
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHcesrndFCHHPLNHGFDYFYGLPLTNlkDCGDGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 181 CPQSDG------------------RWR----------------------NPDRDCYtdvalpLYENLNIVEQPVNLSGLA 220
Cdd:cd16159 161 FPLLTAfvlitaltiflllylgavSKRffvfllilsllfislfflllitNRYFNCI------LMRNHEVVEQPMSLENLT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 221 QKYAERAVEFIEQasTSGRPFLLYVGLAHMHVPLSVTPPLANPQSQRLYRASLQEMDSLVGQIKDKVDHVA-KENTLLWF 299
Cdd:cd16159 235 QRLTKEAISFLER--NKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGlKDNTFVYF 312
|
330 340 350
....*....|....*....|....*....|..
gi 1958659108 300 AGDNGPWAQKCELAGSMGpfsGLWQTHQGGGG 331
Cdd:cd16159 313 TSDNGGHLEEISVGGEYG---GGNGGIYGGKK 341
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-329 |
2.17e-65 |
|
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: 212.02 E-value: 2.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--------- 106
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIpgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 107 ----AVTSVGGLPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGipysndMGCTDNPGYNYPPCPACP 182
Cdd:cd16144 81 tkliPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIG------GTGNGGPPSYYFPPGKPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 183 qsdGRWRNPDRDCYtdvalplyenlniveqpvnlsgLAQKYAERAVEFIEQAstSGRPFLLYvgLAH--MHVPLSVTP-- 258
Cdd:cd16144 155 ---PDLEDGPEGEY----------------------LTDRLTDEAIDFIEQN--KDKPFFLY--LSHyaVHTPIQARPel 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 259 ---------PLANPQSQRLYRASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGPWAQKCELAGSMGPF-SGLWQTHQ 327
Cdd:cd16144 206 iekyekkkkGLRKGQKNPVYAAMIESLDESVGRILDALEELGlADNTLVIFTSDNGGLSTRGGPPTSNAPLrGGKGSLYE 285
|
..
gi 1958659108 328 GG 329
Cdd:cd16144 286 GG 287
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
25-306 |
1.02e-61 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 201.65 E-value: 1.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 25 FSISGETRAPRPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTH 104
Cdd:COG3119 13 AAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 105 NFAvTSVGGLPLNETTLAEVLQQAGYVTAMIGKWHLghhgsyhpsfrgfdyyfgipYSNDmgctdnpgynyppcpacpqs 184
Cdd:COG3119 93 NGE-GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------YLTD-------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 185 dgrwrnpdrdcytdvalplyenlniveqpvnlsglaqKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANP- 263
Cdd:COG3119 132 -------------------------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKy 174
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659108 264 ----------------------QSQRLYRASLQEMDSLVGQIkdkVDHVAK----ENTLLWFAGDNGPW 306
Cdd:COG3119 175 dgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVGRL---LDALEElglaDNTIVVFTSDNGPS 240
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-321 |
3.84e-61 |
|
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: 199.30 E-value: 3.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGAN---WAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHNFAVTSVG 112
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYgggIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 113 GLPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNDmgctdnpgynyppcpacpqsDGRWrnpd 192
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYHTI--------------------DEEI---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 193 rdcytdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQS-QRLYRA 271
Cdd:cd16142 136 -------------------------------VDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYAD 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958659108 272 SLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGPWaQKCELAGSMGPFSG 321
Cdd:cd16142 185 SMVELDDHVGQILDALDELGiADNTIVIFTTDNGPE-QDVWPDGGYTPFRG 234
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-329 |
1.29e-59 |
|
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: 196.66 E-value: 1.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGLP 115
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 116 LNETTLAEVLQQAGYVTAMIGKWHLGHHGSY-HPSFRGFDYYFGipYSNDMGCTdnpGYnYPPCpacpqsdgRWRNPDRd 194
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYG--YLDQVHAH---NY-YPEY--------LWRNGEK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 195 cytdvaLPLYENLNIVEQPVNLSGLAQK-YAE-----RAVEFIEQAstSGRPFLLYVGL----AHMHVP----------- 253
Cdd:cd16145 146 ------VPLPNNVIPPLDEGNNAGGGGGtYSHdlftdEALDFIREN--KDKPFFLYLAYtlphAPLQVPddgpykykpkd 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 254 LSVTPPLANPQSQRLYRASLQEMDSLVGQIKDKV-DHVAKENTLLWFAGDNGP-----WAQKCELAGSMGPFSGL-WQTH 326
Cdd:cd16145 218 PGIYAYLPWPQPEKAYAAMVTRLDRDVGRILALLkELGIDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGYkRSLY 297
|
...
gi 1958659108 327 QGG 329
Cdd:cd16145 298 EGG 300
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-305 |
2.02e-59 |
|
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: 195.50 E-value: 2.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETK-DTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGL 114
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGG--VLGGFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 115 PL---NETTLAEVLQQAGYVTAMIGKWHLG-----------HHGSYH-----------PSFRGFDYYFGIPYSNdmgctd 169
Cdd:cd16143 79 PLiepDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkaATGTGKdvdyskpikggPLDHGFDYYFGIPASE------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 170 npgynyppcpacpqsdgrwrnpdrdcytdvALPLyenlniveqpvnlsgLAQKyaerAVEFIEQASTSGRPFLLYVGLAH 249
Cdd:cd16143 153 ------------------------------VLPT---------------LTDK----AVEFIDQHAKKDKPFFLYFALPA 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659108 250 MHVPLSVTPPLANPQSQRLYRASLQEMDSLVGQIKDKVD--HVAkENTLLWFAGDNGP 305
Cdd:cd16143 184 PHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALKelGLA-ENTLVIFTSDNGP 240
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
36-306 |
5.82e-57 |
|
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: 189.68 E-value: 5.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTHnfavTSVGG-- 113
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWH----TILGRer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPysndmgctdnpgynyppcpacpqsDGRWRNPDR 193
Cdd:cd16146 76 MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHG------------------------GGGIGQYPD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 194 DCYTDVALPLYENLNIVEQpvnlsglAQKYA-----ERAVEFIEQASTsgRPFLLYVGLAHMHVPLSVTPPLANP----- 263
Cdd:cd16146 132 YWGNDYFDDTYYHNGKFVK-------TEGYCtdvffDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPykdmg 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958659108 264 --QSQRLYRASLQEMDSLVGQIKDKVD--HVAkENTLLWFAGDNGPW 306
Cdd:cd16146 203 ldDKLAAFYGMIENIDDNVGRLLAKLKelGLE-ENTIVIFMSDNGPA 248
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
36-329 |
6.73e-55 |
|
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: 183.91 E-value: 6.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFvDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSV-GGL 114
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVIL-NNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEpYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 115 PLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYH-PSFRGFDYYFGiPYSndmGCTDNpgYNYPPCPACPQSDGRWR---- 189
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYTWEYtPTNRGFDSFYG-YYG---GAEDY--YTHTSGGANDYGNDDLRdnee 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 190 --NPDRDCY-TDValplyenlniveqpvnlsglaqkYAERAVEFIEQASTSgRPFLLYVGLAHMHVPLSVTPPLANPQSQ 266
Cdd:cd16029 154 paWDYNGTYsTDL-----------------------FTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYED 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659108 267 ----------RLYRASLQEMDSLVGQIKDKVDHV-AKENTLLWFAGDNGPWAQKCElAGSMGPFSG----LWqthQGG 329
Cdd:cd16029 210 kfahikdedrRTYAAMVSALDESVGNVVDALKAKgMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRGgkntLW---EGG 283
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
36-306 |
1.47e-50 |
|
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: 168.00 E-value: 1.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGLP 115
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 116 LNETTLAEVLQQAGYVTAMIGKWHlghhgsyhpsfrgfdyyfgipysndmgctdnpgynyppcpacpqsdgrwrnpdrdc 195
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 196 ytdvalplyenlniveqpvnlsglaqkyaERAVEFIEQASTSgRPFLLYVGLAHMHvplsvtPPLAnpqsqrlYRASLQE 275
Cdd:cd16022 103 -----------------------------DEAIDFIERRDKD-KPFFLYVSFNAPH------PPFA-------YYAMVSA 139
|
250 260 270
....*....|....*....|....*....|....*
gi 1958659108 276 MDSLVGQIkdkVDHVAK----ENTLLWFAGDNGPW 306
Cdd:cd16022 140 IDDQIGRI---LDALEElgllDNTLIVFTSDHGDM 171
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
36-305 |
3.58e-45 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 155.66 E-value: 3.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtSVGGLP 115
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS----TPVGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 116 LNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFG-IPYSNDMgctDNPGYNYPPCPACPQSDgrwrnpdrd 194
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLY---ADPPDVPYNCSGGGVSD--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 195 cytdvalplyenlniveqpvnlsglaQKYAERAVEFIEQAStsgRPFLLYVGLAHMHVPLSVTPPLANP----------- 263
Cdd:pfam00884 145 --------------------------EALLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscse 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958659108 264 -QSQRLYRASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGP 305
Cdd:pfam00884 196 eQLLNSYDNTLLYTDDAIGRVLDKLEENGLlDNTLVVYTSDHGE 239
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-304 |
6.71e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 151.98 E-value: 6.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHnfavtsvGGLP 115
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPL-CTPSRVQLMTGKYNFRNYVVF-------GYLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 116 LNETTLAEVLQQAGYVTAMIGKWHLG--HHGSYHPSFRGFDYY--FGIPYsndmgcTDNPGynyppcpacpqsdGRWRNP 191
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGKWQLGggRGDGDYPHEFGFDEYclWQLTE------TGEKY-------------SRPATP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 192 DRDCYTDVALPLYENlniveqpvnlsglaqKY-----AERAVEFIEQAstSGRPFLLYVGLAHMHVPLSVTP--PLANPQ 264
Cdd:cd16151 134 TFNIRNGKLLETTEG---------------DYgpdlfADFLIDFIERN--KDQPFFAYYPMVLVHDPFVPTPdsPDWDPD 196
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958659108 265 SQRL------YRASLQEMDSLVGQIKDKVD--HVAkENTLLWFAGDNG 304
Cdd:cd16151 197 DKRKkddpeyFPDMVAYMDKLVGKLVDKLEelGLR-ENTIIIFTGDNG 243
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
35-329 |
6.96e-43 |
|
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: 152.60 E-value: 6.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDMGWGDLGANWAETkDTTNLDKMASEGMRFVDFHAAAsTCSPSRASLLTGRLGLRNGV-THNFAVTSVGG 113
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGEI-PTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQVGMgTMAELATGKPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 114 ----LPLNETTLAEVLQQAGYVTAMIGKWHLGHHgsyhpsfrgfDYYFgipySNDmgctdnpgynyppcpacpqsdgrwr 189
Cdd:cd16025 80 yegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------DYYS----TDD------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 190 npdrdcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYV--GLAH--MHVP------------ 253
Cdd:cd16025 121 ---------------------------------LTDKAIEYIDEQKAPDKPFFLYLafGAPHapLQAPkewidkykgkyd 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 254 -------------------------LSVTPPLA------NPQSQRLYrASLQE--------MDSLVGQIkdkVDHVAK-- 292
Cdd:cd16025 168 agwdalreerlerqkelglipadtkLTPRPPGVpawdslSPEEKKLE-ARRMEvyaamvehMDQQIGRL---IDYLKElg 243
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958659108 293 --ENTLLWFAGDNGP-----WAQkcelAGSmGPFSgLW--QTHQGG 329
Cdd:cd16025 244 elDNTLIIFLSDNGAsaepgWAN----ASN-TPFR-LYkqASHEGG 283
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-259 |
2.01e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 135.00 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggL 114
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 115 PLNETTLAEVLQQAGYVTAMIGKWHL-GHHGSYHPSFR---------GFDYYFGipysndMGCTD---NPGYnyppcpac 181
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGRADDytppperrhGFDYWKG------YECNHdhnNPHY-------- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659108 182 pqsdgrWRNPDRDCYTDVALPLYEnlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYvglahmhvpLSVTPP 259
Cdd:cd16034 142 ------YDDDGKRIYIKGYSPDAE------------------TDLAIEYLENQADKDKPFALV---------LSWNPP 186
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
36-312 |
3.79e-36 |
|
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: 133.79 E-value: 3.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGA--NWAETkdtTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFavTSVGG 113
Cdd:cd16027 1 PNILWIIADDLSPDLGGYggNVVKT---PNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR--SRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 114 LPLNETTLAEVLQQAGYVTAMIGKWHLghhgsyhpsfrgfdyyfgipysndmgctdNPGYNYPPCPACPQSDGRWRNPDR 193
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTHY-----------------------------NPDAVFPFDDEMRGPDDGGRNAWD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 194 dcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQAStSGRPFLLYVGLAHMHVP---LSVTPPLANPQSQRL-- 268
Cdd:cd16027 127 -----------------------------YASNAADFLNRAK-KGQPFFLWFGFHDPHRPyppGDGEEPGYDPEKVKVpp 176
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659108 269 --------------YRASLQEMDSLVGQIkdkVDHVAK----ENTLLWFAGDNG---PWAqKCEL 312
Cdd:cd16027 177 ylpdtpevredladYYDEIERLDQQVGEI---LDELEEdgllDNTIVIFTSDHGmpfPRA-KGTL 237
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
35-304 |
1.67e-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: 133.42 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvGGL 114
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG----PLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 115 PLNETTLAEVLQQAGYVTAMIGKWHLGHHGsyHPSFRGFDYYFGIPysndmgctdNPGYNYPPcpacpqsdgrwrnpdrd 194
Cdd:cd16031 78 DASQPTYPKLLRKAGYQTAFIGKWHLGSGG--DLPPPGFDYWVSFP---------GQGSYYDP----------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 195 cytdvalPLYENLNIVEQPVNLSGLaqkYAERAVEFIEQAStSGRPFLLYVGL-----------AHMHVPLSVT---PPL 260
Cdd:cd16031 130 -------EFIENGKRVGQKGYVTDI---ITDKALDFLKERD-KDKPFCLSLSFkaphrpftpapRHRGLYEDVTipePET 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659108 261 ANPQS-----------------------------QRLYR---ASLQEMDSLVGQIKDKVDH--VAkENTLLWFAGDNG 304
Cdd:cd16031 199 FDDDDyagrpewareqrnrirgvldgrfdtpekyQRYMKdylRTVTGVDDNVGRILDYLEEqgLA-DNTIIIYTSDNG 275
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-304 |
4.42e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 122.84 E-value: 4.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWgDLGANWAETKD---TTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVThnfavtSVG 112
Cdd:cd16154 1 PNILLIIADDQGL-DSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVL------AVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 113 G-LPLNETTL--AEVLQQ--AGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNdmgctdnpgynyppcpacPQSDGR 187
Cdd:cd16154 73 DeLLLSEETLlqLLIKDAttAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGILGGG------------------VQDYYN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 188 WrnpdrdcytdvalplyeNLNIVEQPVNLSGLA-QKYAERAVEFIEQASTsgrPFLLYVGLAHMHVPLSVtPP------- 259
Cdd:cd16154 135 W-----------------NLTNNGQTTNSTEYAtTKLTNLAIDWIDQQTK---PWFLWLAYNAPHTPFHL-PPaelhsrs 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958659108 260 --------LANPQSqrLYRASLQEMDSLVGQIKDKVDHVAKENTLLWFAGDNG 304
Cdd:cd16154 194 llgdsadiEANPRP--YYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNG 244
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
35-304 |
1.17e-31 |
|
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: 122.27 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDMGWgDLGANWAETKdTTNLdkMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtSVGGL 114
Cdd:cd16147 1 RPNIVLILTDDQDV-ELGSMDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSP--PGGGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 115 P------LNETTLAEVLQQAGYVTAMIGK----WHLGHHGSYHPsfRGFDYYFGI--PYSNDMGCTDNPGYNYPPcpacp 182
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYVP--PGWDEWDGLvgNSTYYNYTLSNGGNGKHG----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 183 qsdgrwRNPDRDCYTDValplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYVG-------------LAH 249
Cdd:cd16147 148 ------VSYPGDYLTDV-----------------------IANKALDFLRRAAADDKPFFLVVAppaphgpftpaprYAN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 250 MHVPLSVTPPLANP-----------------------QSQRLYRA---SLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGD 302
Cdd:cd16147 199 LFPNVTAPPRPPPNnpdvsdkphwlrrlpplnptqiaYIDELYRKrlrTLQSVDDLVERLVNTLEATGQlDNTYIIYTSD 278
|
..
gi 1958659108 303 NG 304
Cdd:cd16147 279 NG 280
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-304 |
5.80e-31 |
|
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: 117.34 E-value: 5.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV-----THNFAVTS 110
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 111 VG-GLPLNETTLAEVLQQAGYVTAMIGKWHLGhhgsyhpsfrgfdyyfgipysndmgctdnpgynyppcpacpqsdgrwr 189
Cdd:cd16149 81 KPeGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 190 npdrdcytdvalplyenlniveqpvnlsglaqkyaERAVEFIEQASTSGRPFLLYVGLAHMHVPLSvtpplanpqsqrlY 269
Cdd:cd16149 113 -----------------------------------DDAADFLRRRAEAEKPFFLSVNYTAPHSPWG-------------Y 144
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958659108 270 RASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNG 304
Cdd:cd16149 145 FAAVTGVDRNVGRLLDELEELGlTENTLVIFTSDNG 180
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-304 |
1.84e-28 |
|
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: 113.04 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAST----CSPSRASLLTGRlglrngvtHNFAVTS 110
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGR--------TLFHAPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 111 VGG--LPLNETTLAEVLQQAGYVTAMIGKWHLGhhgsyhpsfrgfdyyfgipysndmgctdnpgynyppcpacpqsdgrw 188
Cdd:cd16155 74 GGKaaIPSDDKTWPETFKKAGYRTFATGKWHNG----------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 189 rnpdrdcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPL-------- 260
Cdd:cd16155 107 ----------------------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYldmyppet 152
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659108 261 ----ANPQSQ-----------------------------RLYRASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNG 304
Cdd:cd16155 153 iplpENFLPQhpfdngegtvrdeqlapfprtpeavrqhlAEYYAMITHLDAQIGRILDALEASGElDNTIIVFTSDHG 230
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-304 |
1.47e-27 |
|
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: 111.16 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--AVTSVGG 113
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSyhPSFRGFDYYFGIpysndmgctdnpgynyppcpacpqsdgrwrNPDR 193
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVGPEET--PLDYGFDEYLPV------------------------------ETTI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 194 DCYTdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYVGL-------------AHMHVPLSVTPP- 259
Cdd:cd16033 129 EYFL--------------------------ADRAIEMLEELAADDKPFFLRVNFwgphdpyippepyLDMYDPEDIPLPe 182
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659108 260 -----LAN-PQSQRLYRASLQ---------------------EMDSLVGQIKDKVDHV-AKENTLLWFAGDNG 304
Cdd:cd16033 183 sfaddFEDkPYIYRRERKRWGvdtedeedwkeiiahywgyitLIDDAIGRILDALEELgLADDTLVIFTSDHG 255
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-304 |
1.48e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 97.62 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILAD----DMgwgdLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHnfavtsv 111
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWG------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 112 GGLPLNETTLAEVLQQAGYVTAMIGKWhlGHHGSYHPSFRGFDYYFGIPYsndmgctdnpgynyppcpacpQSDGRWRNP 191
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAVSSN--PHLFGGPGFDRGFDTFEDFRG---------------------QEGDPGEEG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 192 DRDcytdvalplyenlniveqpvnlsglAQKYAERAVEFIEQASTSgRPFLLYVglaHM---HVPLsvtpplanpqsqrL 268
Cdd:cd16148 127 DER-------------------------AERVTDRALEWLDRNADD-DPFFLFL---HYfdpHEPY-------------L 164
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958659108 269 YRASLQEMDSLVGQIKDKVD-HVAKENTLLWFAGDNG 304
Cdd:cd16148 165 YDAEVRYVDEQIGRLLDKLKeLGLLEDTLVIVTSDHG 201
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
35-259 |
3.13e-23 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 99.74 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDMGwGD-LGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNGVTHNF 106
Cdd:PRK13759 6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDVVPWNY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 107 avtsvgglplnETTLAEVLQQAGYVTAMIGKWHlghhgsYHP--SFRGFDYYF---GIPYSndmgctdnpGYNYPPCPAC 181
Cdd:PRK13759 85 -----------KNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHNVLlhdGYLHS---------GRNEDKSQFD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 182 PQSDGR-W-------RNPDR-----DCYTDVALP--LYENLNiveqPVNLSGlaqkyaERAVEFIEQAStSGRPFLLYVG 246
Cdd:PRK13759 139 FVSDYLaWlrekapgKDPDLtdigwDCNSWVARPwdLEERLH----PTNWVG------SESIEFLRRRD-PTKPFFLKMS 207
|
250
....*....|...
gi 1958659108 247 LAHMHVPLSvtPP 259
Cdd:PRK13759 208 FARPHSPYD--PP 218
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-140 |
2.82e-22 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 95.76 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtsVGGL 114
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPL 75
|
90 100
....*....|....*....|....*.
gi 1958659108 115 PLNETTLAEVLQQAGYVTAMIGKWHL 140
Cdd:cd16152 76 PADEKTLAHYFRDAGYETGYVGKWHL 101
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
35-304 |
5.71e-22 |
|
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: 95.72 E-value: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDM----GWgdLGANWAETKdttNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVtHNFAVTS 110
Cdd:cd16030 2 KPNVLFIAVDDLrpwlGC--YGGHPAKTP---NIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGV-YDNNSYF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 111 VGGLPlNETTLAEVLQQAGYVTAMIGK-WHlGHHGSYHPSFRGFDYYFGIP--------YSNDMGCTDNPGYNYPPCPAC 181
Cdd:cd16030 76 RKVAP-DAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPPgpekyppgKLCPGKKGGKGGGGGPAWEAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 182 PQSDGRwrnpdrdcYTDvalplyenlniveqpvnlsglaQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSV----- 256
Cdd:cd16030 154 DVPDEA--------YPD----------------------GKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVApkkyf 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 257 --------------------------------------------TPPLANPQSQRL---YRASLQEMDSLVGQIKDKVD- 288
Cdd:cd16030 204 dlyplesiplpnpfdpidlpevawndlddlpkygdipalnpgdpKGPLPDEQARELrqaYYASVSYVDAQVGRVLDALEe 283
|
330
....*....|....*.
gi 1958659108 289 HVAKENTLLWFAGDNG 304
Cdd:cd16030 284 LGLADNTIVVLWSDHG 299
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-323 |
3.20e-21 |
|
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: 92.22 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggLP 115
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP-----YD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 116 LNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHpsfrGFDYyfgipysndmgctdnpgynyppcpacpqsdgrwrnpDRDC 195
Cdd:cd16037 76 GDVPSWGHALRAAGYETVLIGKLHFRGEDQRH----GFRY------------------------------------DRDV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 196 ytdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAnpqsqRLYR----- 270
Cdd:cd16037 116 ----------------------------TEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFY-----DLYVrrara 162
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659108 271 ---ASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGpwaqkcELAGSmgpfSGLW 323
Cdd:cd16037 163 ayyGLVEFLDENIGRVLDALEELGLlDNTLIIYTSDHG------DMLGE----RGLW 209
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-317 |
8.35e-20 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 88.03 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDM-GWGDLGANWAETKdTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGL 114
Cdd:cd16035 1 PNILLILTDQErYPPPWPAGWAALN-LPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 115 PLNETTLAEVLQQAGYVTAMIGKWHLGHHGsyhpsfrgfdyyfgipysndmgctdNPGYNYppcpacpqsDGRwrnpdrd 194
Cdd:cd16035 80 SPDVPTLGHMLRAAGYYTAYKGKWHLSGAA-------------------------GGGYKR---------DPG------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 195 cytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTS---GRPFLLYVGLAHMH-VplsVTPPLANPQSQRL-- 268
Cdd:cd16035 119 ----------------------------IAAQAVEWLRERGAKnadGKPWFLVVSLVNPHdI---MFPPDDEERWRRFrn 167
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958659108 269 -YRASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGpwaqkcELAGSMG 317
Cdd:cd16035 168 fYYNLIRDVDRQIGRVLDALDASGlADNTIVVFTSDHG------EMGGAHG 212
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-141 |
6.49e-18 |
|
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: 82.42 E-value: 6.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 35 RPNIVIILADDMGWGDLGA-NWAETKD---------TTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTH 104
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCyNNAHTGKsesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958659108 105 NFAVTSVGGLPLneTTLAEVLQQAGYVTAMIGKWHLG 141
Cdd:cd16153 81 FEAAHPALDHGL--PTFPEVLKKAGYQTASFGKSHLE 115
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
36-136 |
1.64e-17 |
|
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: 80.16 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCS-PSRASLLTGRLGLRNGVTHNFAVT----- 109
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSaPNHAALLTGAYPTLHGYTGNGSADpelps 80
|
90 100
....*....|....*....|....*..
gi 1958659108 110 SVGGLPLNETTLAEVLQQAGYVTAMIG 136
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIG 107
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
36-157 |
3.21e-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: 78.84 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT-----PLD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958659108 116 LNETTLAEVLQQAGYVTAMIGKWHL-----GHH------GSYHPSFRGFDYYF 157
Cdd:cd16028 76 ARHLTLALELRKAGYDPALFGYTDTspdprGLApldprlLSYELAMPGFDPVD 128
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
36-304 |
1.14e-15 |
|
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: 77.42 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG-VTHNFAVTSvggl 114
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGsWTNCMALGD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 115 plNETTLAEVLQQAGYVTAMIGKWHLGhhgsyhpsfrGFDYY-FGIpysndmgCTD--NPGYNYppcpacpqsDGR---- 187
Cdd:cd16156 77 --NVKTIGQRLSDNGIHTAYIGKWHLD----------GGDYFgNGI-------CPQgwDPDYWY---------DMRnyld 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 188 ---------WRNPdrdcytdvaLPLYENLNIVEQPVnlsgLAQKYAERAVEFIEQASTsgRPFLLYVGLAHMHVPLSVTP 258
Cdd:cd16156 129 elteeerrkSRRG---------LTSLEAEGIKEEFT----YGHRCTNRALDFIEKHKD--EDFFLVVSYDEPHHPFLCPK 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 259 PLAN--------------------PQSQRL-------------------YRASLQEMDSLVGQIKDKVDHVAkENTLLWF 299
Cdd:cd16156 194 PYASmykdfefpkgenayddlenkPLHQRLwagakphedgdkgtikhplYFGCNSFVDYEIGRVLDAADEIA-EDAWVIY 272
|
....*
gi 1958659108 300 AGDNG 304
Cdd:cd16156 273 TSDHG 277
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
36-155 |
1.37e-14 |
|
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: 73.38 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-----EFP 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1958659108 116 LNETTLAEVLQQAGYVTAMIGKWHL-G---HHgsyhpsfrGFDY 155
Cdd:cd16032 76 ADIPTFAHYLRAAGYRTALSGKMHFvGpdqLH--------GFDY 111
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-307 |
1.05e-13 |
|
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: 71.50 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGR----LGLRNgvTHNFavtsv 111
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWyphvNGHRT--LHHL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 112 ggLPLNETTLAEVLQQAGYVTAMIGKWHLghhgsyhpsfrgfdyyFGIPYSNDMGCTdnpgynyppcpacpqsdgrwrnP 191
Cdd:cd16150 74 --LRPDEPNLLKTLKDAGYHVAWAGKNDD----------------LPGEFAAEAYCD----------------------S 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 192 DRDCytdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTsGRPFLLYVGLAHMHVPLSVTPP------------ 259
Cdd:cd16150 114 DEAC----------------------------VRTAIDWLRNRRP-DKPFCLYLPLIFPHPPYGVEEPwfsmidreklpp 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659108 260 --------------LANPQSQRLYRAS---LQEM-----------DSLVGQIKDKVDHVA-KENTLLWFAGDNGPWA 307
Cdd:cd16150 165 rrppglrakgkpsmLEGIEKQGLDRWSeerWRELratylgmvsrlDHQFGRLLEALKETGlYDDTAVFFFSDHGDYT 241
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
13-304 |
1.95e-07 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 52.06 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 13 MVFSGLLYPFVDFSISGETRAPRPNIVIILADDMGWGDLGANwaetkDTTNLDKMASEGMRFVDFHAA--ASTCsPSRAS 90
Cdd:COG1524 1 MKRGLSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLLERA-----HAPNLAALAARGVYARPLTSVfpSTTA-PAHTT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 91 LLTGRLGLRNGVTHNF--------AVTSVGGLP--------LNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPS----F 150
Cdd:COG1524 75 LLTGLYPGEHGIVGNGwydpelgrVVNSLSWVEdgfgsnslLPVPTIFERARAAGLTTAAVFWPSFEGSGLIDAArpypY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 151 RGFDYYFGIPYSNdmgctdnpgynyppcpacpqsdgrwrnpdrdcytdvalplyenlniveqpvnlsglaqkyaERAVEF 230
Cdd:COG1524 155 DGRKPLLGNPAAD-------------------------------------------------------------RWIAAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 231 IEQASTSGRPFLLYVGL------AHMHVPLSvtpplanPQsqrlYRASLQEMDSLVGQIKDKVD-HVAKENTLLWFAGDN 303
Cdd:COG1524 174 ALELLREGRPDLLLVYLpdldyaGHRYGPDS-------PE----YRAALREVDAALGRLLDALKaRGLYEGTLVIVTADH 242
|
.
gi 1958659108 304 G 304
Cdd:COG1524 243 G 243
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
28-161 |
2.04e-07 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 52.35 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 28 SGETRAPRPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVthnfA 107
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGS----P 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 108 VTSVGGLPLNetTLAEVLQQAGYVTAMIgkwHlGHHGS------YHPSFrGFDYYFGIPY 161
Cdd:COG1368 303 YKRPGQNNFP--SLPSILKKQGYETSFF---H-GGDGSfwnrdsFYKNL-GFDEFYDRED 355
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
36-143 |
1.07e-05 |
|
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: 46.77 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659108 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGrlgLRNGVTHNFavTSVGGLP 115
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG---LFTHLTESW--NNYKGLD 75
|
90 100 110
....*....|....*....|....*....|
gi 1958659108 116 LNETTLAEVLQQAGYVTAMIGK--WHLGHH 143
Cdd:cd16171 76 PNYPTWMDRLEKHGYHTQKYGKldYTSGHH 105
|
|
| |
