|
Name |
Accession |
Description |
Interval |
E-value |
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
35-420 |
0e+00 |
|
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: 554.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 35 KPNFVIILADDMGWGDLGANWAET-KDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGG 113
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNaILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 114 LPLNETTLAEVLQQAGYVTGIIG----------------FDYYFGIPYSHDmgctdtpgynhppcpacpqgdgpsrnlqr 177
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGkwhlgqreaylpnsrgFDYYFGIPFSHD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 178 dcytdvalplyenlniveqpvnlSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQLPAAP-RGRSLYGAG 256
Cdd:cd16161 132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPtSGRGPYGDA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 257 LWEMDSLVGQIKDKVDH-TVKENTFLWFTGDNGPWAQKCELAgsVGPFTGFWQTRQGGSPAKQTTWEGGHRVPALAYWPG 335
Cdd:cd16161 189 LQEMDDLVGQIMDAVKHaGLKDNTLTWFTSDNGPWEVKCELA--VGPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 336 RVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGeFGALQTVRLERYKAF 415
Cdd:cd16161 267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAH 345
|
....*
gi 1209856998 416 YITAG 420
Cdd:cd16161 346 YATGG 350
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-421 |
5.15e-159 |
|
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: 454.71 E-value: 5.15e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRN-FAVTSVGG 113
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 114 LPLNETTLAEVLQQAGYVTGII----------------GFDYYFGIPYSHDMGCTDTPGYNHPPCPAcpqgdgpsrnlqr 177
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVgkwhlghqpeflptrhGFDEYFGIPYSNDMWPFPLYRNDPPGPLP------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 178 dcytdvalPLYENLNIVEQPVNLSSLAQKYAEKATQFIQRAstSGRPFLLYVALAHMHVPLPVTQLPAAPRGRSLYGAGL 257
Cdd:cd16026 148 --------PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 258 WEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRVPALAYWPGR 336
Cdd:cd16026 218 EELDWSVGRILDALKELgLEENTLVIFTSDNGPWLEYGGHGGSAGPLRG----------GKGTTWEGGVRVPFIAWWPGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 337 VPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQ-PGHRVLFHPNSgaagefGALQTVRLERYKAF 415
Cdd:cd16026 288 IPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKsPPHPFFYYYDG------GDLQAVRSGRWKLH 361
|
....*.
gi 1209856998 416 YITAGK 421
Cdd:cd16026 362 LPTTYR 367
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
35-420 |
8.80e-101 |
|
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: 308.99 E-value: 8.80e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRN-FAVTSVGG 113
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGvFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 114 LPLNETTLAEVLQQAGYVTGII------------------GFDYYFGIPYSHDMG-CTD-TPGYNHPPC-PACPQGDGPs 172
Cdd:cd16158 81 LPLNETTIAEVLKTVGYQTAMVgkwhlgvglngtylpthqGFDHYLGIPYSHDQGpCQNlTCFPPNIPCfGGCDQGEVP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 173 rnlqrdcytdvaLPLYENLNIVEQPVNLSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQLPAAPRGRSL 252
Cdd:cd16158 160 ------------CPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 253 YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFtgfwqtRQGgspaKQTTWEGGHRVPALA 331
Cdd:cd16158 228 FGDALAELDGSVGELLQTLKENgIDNNTLVFFTSDNGPSTMRKSRGGNAGLL------KCG----KGTTYEGGVREPAIA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 332 YWPGRVPVNVTStALLSVLDIFPTVVALAQASLPQgRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGEFGALqTVRLER 411
Cdd:cd16158 298 YWPGRIKPGVTH-ELASTLDILPTIAKLAGAPLPN-VTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVF-AVRWGK 374
|
....*....
gi 1209856998 412 YKAFYITAG 420
Cdd:cd16158 375 YKAHFYTQG 383
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
35-418 |
1.44e-97 |
|
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: 299.73 E-value: 1.44e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV---TRNFAVTSV 111
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 112 GGLPLNETTLAEVLQQAGYVTGIIGfDYYFGI-PYSHDMGC------------TDTPGYNHPPC-PACPQGDGPSRNLqr 177
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVG-KWHLGInENNHSDGAhlpshhgfdfvgTNLPFTNSWACdDTGRHVDFPDRSA-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 178 dCYtdvalpLYENLNIVEQPVNLSSLAQKYAEKATQFIQraSTSGRPFLLYVALAHMHVPLPVTQLPAAPRGRSLYGAGL 257
Cdd:cd16160 158 -CF------LYYNDTIVEQPIQHEHLTETLVGDAKSFIE--DNQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 258 WEMDSLVGQIKDK-VDHTVKENTFLWFTGDNGPWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRVPALAYWPGR 336
Cdd:cd16160 229 NEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKG----------GKGNSWEGGIRVPFIAYWPGT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 337 VPVNVtSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQ-PGHRVLFHPNSgaagefgALQTVRLERYKAF 415
Cdd:cd16160 299 IKPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADsPHDDILYYCCS-------RLMAVRYGSYKIH 370
|
...
gi 1209856998 416 YIT 418
Cdd:cd16160 371 FKT 373
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
34-426 |
1.13e-84 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 264.82 E-value: 1.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvTSVGG 113
Cdd:COG3119 22 KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE-GYNGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 114 LPLNETTLAEVLQQAGYVTGIIgfdyyfgipyshdmgctdtpGYNHppcpacpqgdgpsrnlqrdcytdvalpLYenlni 193
Cdd:COG3119 101 LPPDEPTLAELLKEAGYRTALF--------------------GKWH---------------------------LY----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 194 veqpvnlssLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVP-----------------LPVTQLPAA------PRGR 250
Cdd:COG3119 129 ---------LTDLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPyqapeeyldkydgkdipLPPNLAPRDlteeelRRAR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 251 SLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAqkcelagsvgpftGFWQTRQGgspaKQTTWEGGHRVPA 329
Cdd:COG3119 200 AAYAAMIEEVDDQVGRLLDALEELgLADNTIVVFTSDNGPSL-------------GEHGLRGG----KGTLYEGGIRVPL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 330 LAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHRVLFHpnsgAAGEFGALQTVRL 409
Cdd:COG3119 263 IVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED--LDGRSLLPLLTGEKAEWRDYLYW----EYPRGGGNRAIRT 336
|
410
....*....|....*..
gi 1209856998 410 ERYKAFYITAGKEVPAL 426
Cdd:COG3119 337 GRWKLIRYYDDDGPWEL 353
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-418 |
2.54e-84 |
|
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: 266.26 E-value: 2.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG--VTRNFAVTS-- 110
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 111 ----VGGLPLNETTLAEVLQQAGYVTGII----------------GFDYYFGIPYSHdMGCTDTPGYNHPPcpacpqgdg 170
Cdd:cd16157 81 pqniVGGIPDSEILLPELLKKAGYRNKIVgkwhlghrpqyhplkhGFDEWFGAPNCH-FGPYDNKAYPNIP--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 171 psrnLQRDcyTDVALPLYENLNIvEQPVNLSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQLPAAPRGR 250
Cdd:cd16157 151 ----VYRD--WEMIGRYYEEFKI-DKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 251 SLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNG-PWAQKCELAGSVGPFTGfwqtrqggspAKQTTWEGGHRVP 328
Cdd:cd16157 224 GLYGDAVMELDSSVGKILESLKSLgIENNTFVFFSSDNGaALISAPEQGGSNGPFLC----------GKQTTFEGGMREP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 329 ALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSgaagefgALQTVR 408
Cdd:cd16157 294 AIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGD-------ELMAVR 366
|
410
....*....|
gi 1209856998 409 LERYKAFYIT 418
Cdd:cd16157 367 LGQYKAHFWT 376
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
35-418 |
2.01e-82 |
|
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: 262.99 E-value: 2.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGR------LGLRNGVTRNFAV 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRypirsgMASSHGMRVILFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 109 TSVGGLPLNETTLAEVLQQAGYVTGIIG----------------------FDYYFGIPYSHDMGCTDTPG--YNHPPCPA 164
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGkwhlglhcesrndfchhplnhgFDYFYGLPLTNLKDCGDGSNgeYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 165 CPQgdgpSRNLQRDCYTDVALPLY--------------------------------------ENLNIVEQPVNLSSLAQK 206
Cdd:cd16159 161 FPL----LTAFVLITALTIFLLLYlgavskrffvfllilsllfislfflllitnryfncilmRNHEVVEQPMSLENLTQR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 207 YAEKATQFIQRasTSGRPFLLYVALAHMHvplpvTQLPAAP--RGRS---LYGAGLWEMDSLVGQIKDKVDHT-VKENTF 280
Cdd:cd16159 237 LTKEAISFLER--NKERPFLLVMSFLHVH-----TALFTSKkfKGRSkhgRYGDNVEEMDWSVGQILDALDELgLKDNTF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 281 LWFTGDNGPWAqkcELAGSVGPFTGFWQTRQGGSpaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALA 360
Cdd:cd16159 310 VYFTSDNGGHL---EEISVGGEYGGGNGGIYGGK--KMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALA 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1209856998 361 QASLPQGRRFDGVDVSEVLFGRSQ-PGHRVLFH------------PNSGAAgefgalqtvrleRYKAFYIT 418
Cdd:cd16159 385 GAPLPSDRIIDGRDLMPLLTGQEKrSPHEFLFHycgaelhavryrPRDGGA------------VWKAHYFT 443
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-416 |
6.16e-80 |
|
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: 252.07 E-value: 6.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGAN---WAETKDTANLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTRNFAVTSVG 112
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYgggIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 113 GLPLNETTLAEVLQQAGYVTGIIG----------------FDYYFGIPYSHdmgctdtpgynhppcpacpqgdgpsrnlq 176
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGkwhlgdedgrlptdhgFDEFYGNLYHT----------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 177 rdcytdvalplyenlniveqpvnlssLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVP-LPVTQLPAAPRGRSLYGA 255
Cdd:cd16142 131 --------------------------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPtLPSPEFEGKSSGKGKYAD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 256 GLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSvGPFTGfwqtrqggspAKQTTWEGGHRVPALAYWP 334
Cdd:cd16142 185 SMVELDDHVGQILDALDELgIADNTIVIFTTDNGPEQDVWPDGGY-TPFRG----------EKGTTWEGGVRVPAIVRWP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 335 GRVPVNVTSTALLSVLDIFPTVVALAQASLP------QGRRFDGVDVSEVLFGRS-QPGHRVLFHpnsGAAGEFGAlqtV 407
Cdd:cd16142 254 GKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRHIDGVDQSPFLLGKSeKSRRSEFFY---FGEGELGA---V 327
|
....*....
gi 1209856998 408 RLERYKAFY 416
Cdd:cd16142 328 RWKNWKVHF 336
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-396 |
1.92e-73 |
|
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: 235.94 E-value: 1.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETK-DTANLDKMASEGMRFVDFHAAASTCSPSRASLLTG----RLGLRNGVTRNFavts 110
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGrypwRSRLKGGVLGGF---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 111 vgGLPL---NETTLAEVLQQAGYVTGIIG-----FDYYFGIPYSHDMGCTDTPGYNHPPcpacpqGDGPsrnLQR--D-C 179
Cdd:cd16143 77 --SPPLiepDRVTLAKMLKQAGYRTAMVGkwhlgLDWKKKDGKKAATGTGKDVDYSKPI------KGGP---LDHgfDyY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 180 YTDVAlplyenlniveqpvnlSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLpvtqLPAAP-RGRS---LYGA 255
Cdd:cd16143 146 FGIPA----------------SEVLPTLTDKAVEFIDQHAKKDKPFFLYFALPAPHTPI----VPSPEfQGKSgagPYGD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 256 GLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGPwaqkcelagsvGPFTGFWQT-RQGGSPA------KQTTWEGGHRV 327
Cdd:cd16143 206 FVYELDWVVGRILDALKeLGLAENTLVIFTSDNGP-----------SPYADYKELeKFGHDPSgplrgmKADIYEGGHRV 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1209856998 328 PALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSG 396
Cdd:cd16143 275 PFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVHHSG 343
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-413 |
2.85e-70 |
|
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: 228.58 E-value: 2.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTG----RLGL---------RNGV 102
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGqypaRLGItdvipgrrgPPDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 103 TRNFAVTSVGGLPLNETTLAEVLQQAGYVTGIIG----------------FDYYFGI-PYSHDMGCTDTPGYNHPPCPAC 165
Cdd:cd16144 81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGkwhlggeggygpedqgFDVNIGGtGNGGPPSYYFPPGKPNPDLEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 166 PQGDgpsrnlqrdcytdvalplyenlniveqpvnlsSLAQKYAEKATQFIQRAstSGRPFLLYvaLAH--MHVPLPVTQ- 242
Cdd:cd16144 161 PEGE--------------------------------YLTDRLTDEAIDFIEQN--KDKPFFLY--LSHyaVHTPIQARPe 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 243 -------LPAAPRGR---SLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCELAGSVGPFtgfwqtRQ 311
Cdd:cd16144 205 liekyekKKKGLRKGqknPVYAAMIESLDESVGRILDALEELgLADNTLVIFTSDNGGLSTRGGPPTSNAPL------RG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 312 GgspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHR--V 389
Cdd:cd16144 279 G----KGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRraL 354
|
410 420
....*....|....*....|....*.
gi 1209856998 390 LFH-PN-SGAAGEFGAlqTVRLERYK 413
Cdd:cd16144 355 FWHfPHyHGQGGRPAS--AIRKGDWK 378
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-414 |
1.72e-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: 293764 [Multi-domain] Cd Length: 415 Bit Score: 226.32 E-value: 1.72e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGGLP 115
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 116 LNETTLAEVLQQAGYVTGII-----------------GFDYYFGIpYSHdmgctdTPGYNHPPcpacPQGDgpsRNLQRd 178
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFgkwglggpgtpghptkqGFDYFYGY-LDQ------VHAHNYYP----EYLW---RNGEK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 179 cytdvaLPLYENLNIVEQPVNLSSLAQK-YAE-----KATQFIQRAstSGRPFLLYVALAHMHVPLPVTQLPAA---PRG 249
Cdd:cd16145 146 ------VPLPNNVIPPLDEGNNAGGGGGtYSHdlftdEALDFIREN--KDKPFFLYLAYTLPHAPLQVPDDGPYkykPKD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 250 RSLYGAGLWE------------MDSLVGQIKDKV-DHTVKENTFLWFTGDNGP-----WAQKCELAGSVGPFTGFwqtrq 311
Cdd:cd16145 218 PGIYAYLPWPqpekayaamvtrLDRDVGRILALLkELGIDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 312 ggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPG-HRVL 390
Cdd:cd16145 293 -----KRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPE--DIDGISLLPTLLGKPQQQqHDYL 365
|
410 420
....*....|....*....|....
gi 1209856998 391 FHpnsgAAGEFGALQTVRLERYKA 414
Cdd:cd16145 366 YW----EFYEGGGAQAVRMGGWKA 385
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
36-374 |
3.38e-67 |
|
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: 214.22 E-value: 3.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNfaVTSVGGLP 115
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 116 LNETTLAEVLQQAGYVTGIIGfdyyfgipyshdmgctdtpgynhppcpacpqgdgpsrnlqrdcytdvalplyenlnive 195
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIG----------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 196 qpvnlsslaqKYAEKATQFIQRASTSgRPFLLYVALAHMHVPLpvtqlpaaprgrsLYGAGLWEMDSLVGQIKDKVDHT- 274
Cdd:cd16022 100 ----------KWHDEAIDFIERRDKD-KPFFLYVSFNAPHPPF-------------AYYAMVSAIDDQIGRILDALEELg 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 275 VKENTFLWFTGDNgpwaqkcelagsvGPFTGFWQTRQGgspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFP 354
Cdd:cd16022 156 LLDNTLIVFTSDH-------------GDMLGDHGLRGK----KGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLP 218
|
330 340
....*....|....*....|
gi 1209856998 355 TVVALAQASLPQGrrFDGVD 374
Cdd:cd16022 219 TLLDLAGIEPPEG--LDGRS 236
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
36-391 |
1.18e-63 |
|
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: 210.87 E-value: 1.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTRnfavTSVGG-- 113
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWH----TILGRer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 114 LPLNETTLAEVLQQAGYVTGII----------------GFDYYFGIPYSHDmgcTDTPGYnhppcpacpqgdgpsrnLQR 177
Cdd:cd16146 76 MRLDETTLAEVFKDAGYRTGIFgkwhlgdnypyrpqdrGFDEVLGHGGGGI---GQYPDY-----------------WGN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 178 DCYTDValpLYENlNIVEQpvnlsslAQKYA-----EKATQFIQRASTsgRPFLLYVALAHMHVPLPVTQLPAAP----- 247
Cdd:cd16146 136 DYFDDT---YYHN-GKFVK-------TEGYCtdvffDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPykdmg 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 248 --RGRSLYGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGPWaqkcelAGSVGPFTGFWQtrqgGSpaKQTTWEGG 324
Cdd:cd16146 203 ldDKLAAFYGMIENIDDNVGRLLAKLKeLGLEENTIVIFMSDNGPA------GGVPKRFNAGMR----GK--KGSVYEGG 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209856998 325 HRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQP-GHRVLF 391
Cdd:cd16146 271 HRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPwPERTLF 338
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-413 |
1.89e-57 |
|
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: 193.58 E-value: 1.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTRnfavtsvGGLP 115
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPL-CTPSRVQLMTGKYNFRNYVVF-------GYLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 116 LNETTLAEVLQQAGYVTGIIG----FDYYFGIPYSHDMG---------CTDTPGYNHPPCPACPQGDGPSRNLQRDCY-T 181
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGkwqlGGGRGDGDYPHEFGfdeyclwqlTETGEKYSRPATPTFNIRNGKLLETTEGDYgP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 182 DValplyenlniveqpvnlsslaqkYAEKATQFIQRAStsGRPFLLY--VALAH-MHVPLPVTQLPAAPRGRS-----LY 253
Cdd:cd16151 153 DL-----------------------FADFLIDFIERNK--DQPFFAYypMVLVHdPFVPTPDSPDWDPDDKRKkddpeYF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 254 GAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcelagSVGPFTGFW--QTRQGGspaKQTTWEGGHRVPAL 330
Cdd:cd16151 208 PDMVAYMDKLVGKLVDKLEELgLRENTIIIFTGDNG----------THRPITSRTngREVRGG---KGKTTDAGTHVPLI 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 331 AYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGEFGALQTVRLE 410
Cdd:cd16151 275 VNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWYYRNPHKKFGSRFVRTK 354
|
...
gi 1209856998 411 RYK 413
Cdd:cd16151 355 RYK 357
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
36-413 |
2.71e-53 |
|
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: 183.14 E-value: 2.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFvDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSV-GGL 114
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVIL-NNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEpYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 115 PLNETTLAEVLQQAGYVTGII-----------------GFDYYFGiPYShdmGCTDtpGYNHPPCPACP------QGDGP 171
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVgkwhlgfytweytptnrGFDSFYG-YYG---GAED--YYTHTSGGANDygnddlRDNEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 172 SRNLQRDCY-TDValplyenlniveqpvnlsslaqkYAEKATQFIQRASTSgRPFLLYVALAHMHVPLPVTQLPAAP--- 247
Cdd:cd16029 154 PAWDYNGTYsTDL-----------------------FTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPyed 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 248 -------RGRSLYGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAQKCElAGSVGPFTGfwqtrqggspAKQT 319
Cdd:cd16029 210 kfahikdEDRRTYAAMVSALDESVGNVVDALKAKgMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRG----------GKNT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 320 TWEGGHRVPALAYWPGRVPV-NVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHR-VLFHPNSGA 397
Cdd:cd16029 279 LWEGGVRVPAFVWSPLLPPKrGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTeILLNIDDIT 358
|
410
....*....|....*.
gi 1209856998 398 AGEFGAlqTVRLERYK 413
Cdd:cd16029 359 RTTGGA--AIRVGDWK 372
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
36-417 |
1.19e-50 |
|
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: 175.39 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGA--NWAETkdtANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFavTSVGG 113
Cdd:cd16027 1 PNILWIIADDLSPDLGGYggNVVKT---PNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR--SRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 114 LPLNETTLAEVLQQAGYVTGIIGF-DYYFGIPYSHDMGCTDTPGYNHPpcpacpqgdgpsrnlqrdcytdvalplyenln 192
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKtHYNPDAVFPFDDEMRGPDDGGRN-------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 193 iveqpvnlsslAQKYAEKATQFIQRAStSGRPFLLYVALAHMH-----------------VPLPvTQLPAAPRGR---SL 252
Cdd:cd16027 124 -----------AWDYASNAADFLNRAK-KGQPFFLWFGFHDPHrpyppgdgeepgydpekVKVP-PYLPDTPEVRedlAD 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 253 YGAGLWEMDSLVGQIKDKVD-HTVKENTFLWFTGDNGpwaqkcelagsvGPFTGfwqtrqggspAKQTTWEGGHRVPALA 331
Cdd:cd16027 191 YYDEIERLDQQVGEILDELEeDGLLDNTIVIFTSDHG------------MPFPR----------AKGTLYDSGLRVPLIV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 332 YWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGHRVLF-----HpnsgaaGEFGALQ- 405
Cdd:cd16027 249 RWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGRDYVFaerdrH------DETYDPIr 320
|
410
....*....|..
gi 1209856998 406 TVRLERYKafYI 417
Cdd:cd16027 321 SVRTGRYK--YI 330
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
36-362 |
9.73e-50 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 171.07 E-value: 9.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrnfaVTSVGGLP 115
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSY----VSTPVGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 116 LNETTLAEVLQQAGYVTGIIGfdYYFGIPYSHDMGCTDtpGYNHPPcpacpqGDGPSRNLQRDCYtdvalplyenlNIVE 195
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIG--KWHLGWYNNQSPCNL--GFDKFF------GRNTGSDLYADPP-----------DVPY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 196 QPVNLSSLAQKYAEKATQFIQRAStsgRPFLLYVALAHMHVPLPVTQLPAAP------------RGRSLYGAGLWEMDSL 263
Cdd:pfam00884 136 NCSGGGVSDEALLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscseeQLLNSYDNTLLYTDDA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 264 VGQIKDKV-DHTVKENTFLWFTGDNGPwaqkcelagSVGPFTGFWQTRQGGspakqTTWEGGHRVPALAYWPGRVPVNVT 342
Cdd:pfam00884 213 IGRVLDKLeENGLLDNTLVVYTSDHGE---------SLGEGGGYLHGGKYD-----NAPEGGYRVPLLIWSPGGKAKGQK 278
|
330 340
....*....|....*....|
gi 1209856998 343 STALLSVLDIFPTVVALAQA 362
Cdd:pfam00884 279 SEALVSHVDLFPTILDLAGI 298
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
34-414 |
6.92e-48 |
|
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: 169.16 E-value: 6.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 34 QKPNFVIILADDMGWGDLGANWAETkDTANLDKMASEGMRFVDFHAAAsTCSPSRASLLTGRLGLRNGVtRNFAVTSVGG 113
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEI-PTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 114 ------LPLNETTLAEVLQQAGYVTGIIG------FDYYFgipySHDmgctdtpgynhppcpacpqgdgpsrnlqrdcyt 181
Cdd:cd16025 78 pgyegyLPDSAATIAEVLKDAGYHTYMSGkwhlgpDDYYS----TDD--------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 182 dvalplyenlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYVALAHMHVPL----------------------- 238
Cdd:cd16025 121 -------------------------LTDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLqapkewidkykgkydagwdalre 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 239 -------------PVTQLPAAPRG-----------RSLYG------AGLWE-MDSLVGQIKDKVDHT-VKENTFLWFTGD 286
Cdd:cd16025 176 erlerqkelglipADTKLTPRPPGvpawdslspeeKKLEArrmevyAAMVEhMDQQIGRLIDYLKELgELDNTLIIFLSD 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 287 NGP-----WAQkcelAGSvGPFTGFwqtrqggspaKQTTWEGGHRVPALAYWPGRV-PVNVTSTALLSVLDIFPTVVALA 360
Cdd:cd16025 256 NGAsaepgWAN----ASN-TPFRLY----------KQASHEGGIRTPLIVSWPKGIkAKGGIRHQFAHVIDIAPTILELA 320
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1209856998 361 QASLPQGRR------FDGVDVSEVLFGRSQPG-HRVLFHPNSGAAGefgalqtVRLERYKA 414
Cdd:cd16025 321 GVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSrRRTQYFELFGNRA-------IRKGGWKA 374
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-413 |
3.84e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 148.10 E-value: 3.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVtsvggL 114
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 115 PLNETTLAEVLQQAGYVTGIIG--------------------------FDYYFGipyshdMGCTDtpGYNHPPCpacpQG 168
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGkwhldgperndgraddytppperrhgFDYWKG------YECNH--DHNNPHY----YD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 169 DGPSRNlQRDCYTdvalPLYEnlniveqpvnlsslaqkyAEKATQFIQRASTSGRPFLLYVALAHMHVP----------- 237
Cdd:cd16034 144 DDGKRI-YIKGYS----PDAE------------------TDLAIEYLENQADKDKPFALVLSWNPPHDPyttapeeyldm 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 238 -----------LPVTQLPAAPRGRSL---YGA--GLwemDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSV 300
Cdd:cd16034 201 ydpkklllrpnVPEDKKEEAGLREDLrgyYAMitAL---DDNIGRLLDALKELgLLENTIVVFTSDHG------DMLGSH 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 301 GPFtgfwqtrqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLF 380
Cdd:cd16034 272 GLM------------NKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLL 337
|
410 420 430
....*....|....*....|....*....|....*...
gi 1209856998 381 GRSQPGHR----VLFHPNSG-AAGEFGALQTVRLERYK 413
Cdd:cd16034 338 GGKDDEPDsvllQCFVPFGGgSARDGGEWRGVRTDRYT 375
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-372 |
2.04e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 136.98 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV-----TRNFAVTS 110
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 111 VG-GLPLNETTLAEVLQQAGYVTGIIGfDYYFGipyshdmgctdtpgynhppcpacpqgdgpsrnlqrdcytdvalplye 189
Cdd:cd16149 81 KPeGYLEGQTTLPEVLQDAGYRCGLSG-KWHLG----------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 190 nlniveqpvnlsslaqkyaEKATQFIQRASTSGRPFLLYVAlahmhvplpvTQLPAAPRGrslYGAGLWEMDSLVGQIKD 269
Cdd:cd16149 113 -------------------DDAADFLRRRAEAEKPFFLSVN----------YTAPHSPWG---YFAAVTGVDRNVGRLLD 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 270 KVDHT-VKENTFLWFTGDNGpwaqkcelagsvgpFT----GFWQTRQGGSPakQTTWEGGHRVPALAYWPGRVPVNVTST 344
Cdd:cd16149 161 ELEELgLTENTLVIFTSDNG--------------FNmghhGIWGKGNGTFP--LNMYDNSVKVPFIIRWPGVVPAGRVVD 224
|
330 340
....*....|....*....|....*...
gi 1209856998 345 ALLSVLDIFPTVVALAQASLPQGRRFDG 372
Cdd:cd16149 225 SLVSAYDFFPTLLELAGVDPPADPRLPG 252
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
34-417 |
2.89e-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: 2.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvGG 113
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG----PL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 114 LPLNETTLAEVLQQAGYVTGIIG--------------FDYYFGIPyshdmgctdtpgynhppcpacPQGDgpsrnlqrdc 179
Cdd:cd16031 77 FDASQPTYPKLLRKAGYQTAFIGkwhlgsggdlpppgFDYWVSFP---------------------GQGS---------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 180 YTDvaLPLYENLNIVEQPVNLSSLaqkYAEKATQFIQRAStSGRPFLLYV-----------ALAHMHV------PLPVTQ 242
Cdd:cd16031 126 YYD--PEFIENGKRVGQKGYVTDI---ITDKALDFLKERD-KDKPFCLSLsfkaphrpftpAPRHRGLyedvtiPEPETF 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 243 LPA--APRGRSL---------------------------YGAGLWEMDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaq 292
Cdd:cd16031 200 DDDdyAGRPEWAreqrnrirgvldgrfdtpekyqrymkdYLRTVTGVDDNVGRILDYLEEQgLADNTIIIYTSDNG---- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 293 kcELAGSVGpFTGfwqtrqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPqgRRFDG 372
Cdd:cd16031 276 --FFLGEHG-LFD-----------KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIP--EDMQG 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1209856998 373 VDVSEVLFGRSQPGHR------VLFHPNS-GAAGEFGalqtVRLERYKafYI 417
Cdd:cd16031 340 RSLLPLLEGEKPVDWRkefyyeYYEEPNFhNVPTHEG----VRTERYK--YI 385
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
35-372 |
5.93e-32 |
|
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: 125.74 E-value: 5.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 35 KPNFVIILADDMGWgDLGANWAETKdTANLdkMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtSVGGL 114
Cdd:cd16147 1 RPNIVLILTDDQDV-ELGSMDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSP--PGGGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 115 P------LNETTLAEVLQQAGYVTgiigfdYYFGiPYSHdmGCTDTPGYNHPPcpacPQGD------GPSRNLQrdcYTd 182
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRT------AYAG-KYLN--GYGVPGGVSYVP----PGWDewdglvGNSTYYN---YT- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 183 valplYENLNIVEQPVN-----LSSLaqkYAEKATQFIQRASTSGRPFLLYVA-------------LAHMHVPLPVT--- 241
Cdd:cd16147 138 -----LSNGGNGKHGVSypgdyLTDV---IANKALDFLRRAAADDKPFFLVVAppaphgpftpaprYANLFPNVTAPprp 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 242 ---------------QLPAAP-----------RGRslygaglWE----MDSLVGQIKDKVDHT-VKENTFLWFTGDNgpw 290
Cdd:cd16147 210 ppnnpdvsdkphwlrRLPPLNptqiayidelyRKR-------LRtlqsVDDLVERLVNTLEATgQLDNTYIIYTSDN--- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 291 aqkcelagsvgpftGFW--QTRQGgsPAKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDIFPTVVALAQASLPqgR 368
Cdd:cd16147 280 --------------GYHlgQHRLP--PGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPP--S 340
|
....
gi 1209856998 369 RFDG 372
Cdd:cd16147 341 DMDG 344
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-426 |
1.13e-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: 116.12 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 34 QKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAAST----CSPSRASLLTGRLGLRNGVTRNFAvt 109
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFHAPEGGKAA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 110 svggLPLNETTLAEVLQQAGYVTgiigfdyyFGIpyshdmgctdtpGYNHPPcpacpqgdgpsrnlqrdcytdvalplye 189
Cdd:cd16155 79 ----IPSDDKTWPETFKKAGYRT--------FAT------------GKWHNG---------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 190 nlniveqpvnlsslaqkYAEKATQFIQRASTSGRPFLLYVALAHMH-----------------VPLPVTQLPAAP----- 247
Cdd:cd16155 107 -----------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHdprqappeyldmyppetIPLPENFLPQHPfdnge 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 248 -------------------RGRSLYGAGLWEMDSLVGQIKDKVDHTVK-ENTFLWFTGDNGpwaqkceLAgsVGpftgfw 307
Cdd:cd16155 170 gtvrdeqlapfprtpeavrQHLAEYYAMITHLDAQIGRILDALEASGElDNTIIVFTSDHG-------LA--VG------ 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 308 qtrQGGSPAKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSVLDIFPTVVALAQASLPQGrrFDGVDVSEVLFGRSQPGH 387
Cdd:cd16155 235 ---SHGLMGKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES--VEGKSLLPVIRGEKKAVR 308
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1209856998 388 RVLFhpnsgaaGEFGALQ-TVRLERYKAFYITAGKEVPAL 426
Cdd:cd16155 309 DTLY-------GAYRDGQrAIRDDRWKLIIYVPGVKRTQL 341
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-423 |
2.33e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 115.14 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWgDLGANWAETKD---TANLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGvtrnfaVTSVG 112
Cdd:cd16154 1 PNILLIIADDQGL-DSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTG------VLAVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 113 G-LPLNETTL--AEVLQQ--AGYVTGIIGfDYYFGipyshdmGCTDTPgYNHPPCP---ACPQGDGPSrnlqrdcYTDVA 184
Cdd:cd16154 73 DeLLLSEETLlqLLIKDAttAGYSSAVIG-KWHLG-------GNDNSP-NNPGGIPyyaGILGGGVQD-------YYNWN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 185 LplyeNLNIVEQPVN------LSSLAQKYAEKATQfiqrastsgrPFLLYVALAHMHVPLpvtQLPAA---PRG------ 249
Cdd:cd16154 137 L----TNNGQTTNSTeyattkLTNLAIDWIDQQTK----------PWFLWLAYNAPHTPF---HLPPAelhSRSllgdsa 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 250 ------RSLYGAGLWEMDSLVGQIKDKVDHTVKENTFLWFTGDNG-PwaqkcelagsvGPFTGFWQTRQGgspAKQTTWE 322
Cdd:cd16154 200 dieanpRPYYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGtP-----------GQVVDLPYTRNH---AKGSLYE 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 323 GGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQgrRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGEFG 402
Cdd:cd16154 266 GGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAE--IHDSVSFKPLLSDVNASTRQYNYTEYESPTTTGW 343
|
410 420
....*....|....*....|.
gi 1209856998 403 AlqtVRLERYKAFYITAGKEV 423
Cdd:cd16154 344 A---TRNQYYKLIESENGQEE 361
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-374 |
1.15e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 111.10 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILAD----DMgwgdLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrnfavtsV 111
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW-------G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 112 GGLPLNETTLAEVLQQAGYVTGIIgfdyyfgipyshdmgcTDTPGYnhppcpacpqgdGPSRNLQRDCYTDVALPLYENL 191
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAV----------------SSNPHL------------FGGPGFDRGFDTFEDFRGQEGD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 192 NIVEQPVNlsslAQKYAEKATQFIQRASTSgRPFLLYValaHMHvplpvtqlpaAPRGRSLYGAGLWEMDSLVGQIKDKV 271
Cdd:cd16148 122 PGEEGDER----AERVTDRALEWLDRNADD-DPFFLFL---HYF----------DPHEPYLYDAEVRYVDEQIGRLLDKL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 272 D-HTVKENTFLWFTGDNGpwaqkcELAGSVGPFTGFWqtrqggspakQTTWEGGHRVPALAYWPGRVPVNVTStALLSVL 350
Cdd:cd16148 184 KeLGLLEDTLVIVTSDHG------EEFGEHGLYWGHG----------SNLYDEQLHVPLIIRWPGKEPGKRVD-ALVSHI 246
|
330 340
....*....|....*....|....
gi 1209856998 351 DIFPTVVALAQASLPqgRRFDGVD 374
Cdd:cd16148 247 DIAPTLLDLLGVEPP--DYSDGRS 268
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
31-392 |
1.53e-27 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 114.38 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 31 TRGQKPNFVIILADDMGwGD-LGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNGV 102
Cdd:PRK13759 2 VQTKKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 103 TRNFavtsvgglplnETTLAEVLQQAGYVTGIIGFDYYFgiPYSHDMGCTDT---PGY------NHPPCPACP------- 166
Cdd:PRK13759 81 PWNY-----------KNTLPQEFRDAGYYTQCIGKMHVF--PQRNLLGFHNVllhDGYlhsgrnEDKSQFDFVsdylawl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 167 QGDGPSRN-----LQRDCYTDVALP--LYENLNiveqPVNLSslaqkyAEKATQFIQRAStSGRPFLLYVALAHMHVPL- 238
Cdd:PRK13759 148 REKAPGKDpdltdIGWDCNSWVARPwdLEERLH----PTNWV------GSESIEFLRRRD-PTKPFFLKMSFARPHSPYd 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 239 -PV--------TQLPAAPRGRSLYGAGLW----EMDSLVGQIKDK---------------VDH-------TVKE-----N 278
Cdd:PRK13759 217 pPKryfdmykdADIPDPHIGDWEYAEDQDpeggSIDALRGNLGEEyarraraayyglithIDHqigrflqALKEfglldN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 279 TFLWFTGDNGpwaqkcELAGSVGPFTgfwqtrqggspaKQTTWEGGHRVPALAYWPG---RVPVNVTSTALLSVLDIFPT 355
Cdd:PRK13759 297 TIILFVSDHG------DMLGDHYLFR------------KGYPYEGSAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPT 358
|
410 420 430
....*....|....*....|....*....|....*..
gi 1209856998 356 VVALAQASLPqgRRFDGVDVSEVLFGrSQPGHRVLFH 392
Cdd:PRK13759 359 LLDLAGGTIP--DDVDGRSLKNLIFG-QYEGWRPYLH 392
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-416 |
6.26e-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: 111.54 E-value: 6.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNF--AVTSVGG 113
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 114 LPLNETTLAEVLQQAGYvtgiigfdyyfgipyshDMGCTdtpGYNHppcpaCPQGDGPSrnlqrDCYtdvalplYENLNI 193
Cdd:cd16033 81 LPPGVETFSEDLREAGY-----------------RNGYV---GKWH-----VGPEETPL-----DYG-------FDEYLP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 194 VEqpvnlSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMH-----------------VPLP------------VTQLP 244
Cdd:cd16033 124 VE-----TTIEYFLADRAIEMLEELAADDKPFFLRVNFWGPHdpyippepyldmydpedIPLPesfaddfedkpyIYRRE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 245 AAPRGRSLYGAGLWE------------MDSLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGPFTgfwqtrQ 311
Cdd:cd16033 199 RKRWGVDTEDEEDWKeiiahywgyitlIDDAIGRILDALEELgLADDTLVIFTSDHG------DALGAHRLWD------K 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 312 GGSPAKQTtweggHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPqgRRFDGVDVSEVLFGRSQPGHR--V 389
Cdd:cd16033 267 GPFMYEET-----YRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVP--PKVDGRSLLPLLRGEQPEDWRdeV 339
|
410 420 430
....*....|....*....|....*....|
gi 1209856998 390 L--FHPNsgaagEFGALQT-VRLERYKAFY 416
Cdd:cd16033 340 VteYNGH-----EFYLPQRmVRTDRYKYVF 364
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
36-360 |
1.57e-26 |
|
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: 106.74 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCS-PSRASLLTGRLGLRNGVTRNFAVT----- 109
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSaPNHAALLTGAYPTLHGYTGNGSADpelps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 110 SVGGLPLNETTLAEVLQQAGYVTGIIGFDyyfgipyshdmgctdtpgynhppcpacpqgdgpsrnlqrdcytdvalplye 189
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIGLL--------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 190 nlniveqpvnlsslaqkyaekatQFIQRaSTSGRPFLLYVALAHMHVPL--PVTQLPaaprgrsLYGAGLWEMDSLVGQI 267
Cdd:cd00016 110 -----------------------KAIDE-TSKEKPFVLFLHFDGPDGPGhaYGPNTP-------EYYDAVEEIDERIGKV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 268 KDKV-DHTVKENTFLWFTGDNGpwaqkcelAGSVGPftgfwqTRQGGSPAKQTTWEGGHRVPALAYWPGrVPVNVTSTAL 346
Cdd:cd00016 159 LDALkKAGDADDTVIIVTADHG--------GIDKGH------GGDPKADGKADKSHTGMRVPFIAYGPG-VKKGGVKHEL 223
|
330
....*....|....
gi 1209856998 347 LSVLDIFPTVVALA 360
Cdd:cd00016 224 ISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-377 |
2.29e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 104.76 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 35 KPNFVIILADDMGWGDLGA-NWAETKD---------TANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTR 104
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCyNNAHTGKsesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 105 NFAVTSVGGLPLneTTLAEVLQQAGYVTGIIGFDYYfgipyshdmgctdtpgynhppcpacpqgdgpsRNLQRdcYTDVA 184
Cdd:cd16153 81 FEAAHPALDHGL--PTFPEVLKKAGYQTASFGKSHL--------------------------------EAFQR--YLKNA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 185 LPLYENLNIVEqpvnlsslaqkyaekatqfIQRASTSGrPFLLYVALAHMHVP-LPvtqlPAAPRGRSLYGAGLWEMDSL 263
Cdd:cd16153 125 NQSYKSFWGKI-------------------AKGADSDK-PFFVRLSFLQPHTPvLP----PKEFRDRFDYYAFCAYGDAQ 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 264 VGQIKDKVD----HTVKENTFLWFTGDNGpwaqkcelagsvgpftgfWQTRQGGSPAKQTTWEGGHRVPALAYWPGR--V 337
Cdd:cd16153 181 VGRAVEAFKayslKQDRDYTIVYVTGDHG------------------WHLGEQGILAKFTFWPQSHRVPLIVVSSDKlkA 242
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1209856998 338 PVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSE 377
Cdd:cd16153 243 PAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
34-412 |
6.38e-24 |
|
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: 103.42 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 34 QKPNFVIILADDM----GWgdLGANWAETkdtANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTrNFAVT 109
Cdd:cd16030 1 KKPNVLFIAVDDLrpwlGC--YGGHPAKT---PNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVY-DNNSY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 110 SVGGLPlNETTLAEVLQQAGYVTGIIGFDYYFGIPYSHDMGCTDTPGYNHPPCPACPQGDGPSRNLQRDCytDVALPLYE 189
Cdd:cd16030 75 FRKVAP-DAVTLPQYFKENGYTTAGVGKIFHPGIPDGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKG--GGGGPAWE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 190 NLNIVEqpvnlSSLA-QKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQ-------------------------- 242
Cdd:cd16030 152 AADVPD-----EAYPdGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKkyfdlyplesiplpnpfdpidlpeva 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 243 ------LPAAPRGRSLYG--------AGLWE------------MDSLVGQIKDKVD-HTVKENTFLWFTGDNGpWaqkce 295
Cdd:cd16030 227 wndlddLPKYGDIPALNPgdpkgplpDEQARelrqayyasvsyVDAQVGRVLDALEeLGLADNTIVVLWSDHG-W----- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 296 lagSVGPfTGFWqtrqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQasLPQGRRFDGVDV 375
Cdd:cd16030 301 ---HLGE-HGHW--------GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSL 366
|
410 420 430
....*....|....*....|....*....|....*....
gi 1209856998 376 SEVLFGRSQPGHRVLF--HPNSGAAGEfgalqTVRLERY 412
Cdd:cd16030 367 VPLLKNPSAKWKDAAFsqYPRPSIMGY-----SIRTERY 400
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-426 |
1.06e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 101.08 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVtsvggLP 115
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP-----YD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 116 LNETTLAEVLQQAGYVTGIIGFDYYFGIPYSHdmgctdtpGYNHppcpacpqgdgpsrnlqrdcytdvalplyenlnivE 195
Cdd:cd16037 76 GDVPSWGHALRAAGYETVLIGKLHFRGEDQRH--------GFRY-----------------------------------D 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 196 QPVnlsslaqkyAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQ---LPAAPRGRSLYGAGLWEMDSLVGQIKDKVD 272
Cdd:cd16037 113 RDV---------TEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQefyDLYVRRARAAYYGLVEFLDENIGRVLDALE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 273 HT-VKENTFLWFTGDNGpwaqkcELAGSvgpfTGFWQtrqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTAlLSVLD 351
Cdd:cd16037 184 ELgLLDNTLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMIISGPGIPAGKRVKTP-VSLVD 244
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1209856998 352 IFPTVVALAQASLPqgRRFDGVDVSEVLFGRSQPGHRVL--FHPNSGAAGEFgalqTVRLERYKafYITAGKEVPAL 426
Cdd:cd16037 245 LAPTILEAAGAPPP--PDLDGRSLLPLAEGPDDPDRVVFseYHAHGSPSGAF----MLRKGRWK--YIYYVGYPPQL 313
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
36-417 |
2.42e-23 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 99.96 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvgGLP 115
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-----EFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 116 LNETTLAEVLQQAGYVTGI------IGFDYYFGipYSHDmgctdtpgynhppcpacpqgdgpsrnlqrdcyTDVALplye 189
Cdd:cd16032 76 ADIPTFAHYLRAAGYRTALsgkmhfVGPDQLHG--FDYD--------------------------------EEVAF---- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 190 nlniveqpvnlsslaqkyaeKATQFI-QRA-STSGRPFLLYVALAHMHVPLPVTQ------LPAApRgRSLYGAGLWeMD 261
Cdd:cd16032 118 --------------------KAVQKLyDLArGEDGRPFFLTVSFTHPHDPYVIPQeywdlyVRRA-R-RAYYGMVSY-VD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 262 SLVGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAGSvgpfTGFWQtrqggspaKQTTWEGGHRVPALAYWPGR-VPV 339
Cdd:cd16032 175 DKVGQLLDTLERTgLADDTIVIFTSDHG------DMLGE----RGLWY--------KMSFFEGSARVPLIISAPGRfAPR 236
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1209856998 340 NVTstALLSVLDIFPTVVALAQASLPQGR-RFDGVDVSEVLFGRSQPGHRVLFHPNSGaAGEFGALQTVRLERYKAFYI 417
Cdd:cd16032 237 RVA--EPVSLVDLLPTLVDLAGGGTAPHVpPLDGRSLLPLLEGGDSGGEDEVISEYLA-EGAVAPCVMIRRGRWKFIYC 312
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-392 |
2.14e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 96.89 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDM-GWGDLGANWAETKDTAnLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGGL 114
Cdd:cd16035 1 PNILLILTDQErYPPPWPAGWAALNLPA-RERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 115 PLNETTLAEVLQQAGYVTgiigfdYYFGipYSHdmgCTDTP--GYNHppcpacpqgDGpsrnlqrdcytdvalplyenln 192
Cdd:cd16035 80 SPDVPTLGHMLRAAGYYT------AYKG--KWH---LSGAAggGYKR---------DP---------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 193 iveqpvnlsslaqKYAEKATQFIQRASTS---GRPFLLYVALAHMH-VPLPVTQLPAAPRGRSLYGAGLWEMDSLVGQIK 268
Cdd:cd16035 118 -------------GIAAQAVEWLRERGAKnadGKPWFLVVSLVNPHdIMFPPDDEERWRRFRNFYYNLIRDVDRQIGRVL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 269 DKVDHT-VKENTFLWFTGDNGpwaqkcELAGSVGpftgfwQTRQGGSPAKQTTwegghRVPALAYWPGRVPVNVTSTALL 347
Cdd:cd16035 185 DALDASgLADNTIVVFTSDHG------EMGGAHG------LRGKGFNAYEEAL-----HVPLIISHPDLFGTGQTTDALT 247
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1209856998 348 SVLDIFPTVVALAQASLPQ----GRRFDGVDVSEVLfgRSQPGHRV----LFH 392
Cdd:cd16035 248 SHIDLLPTLLGLAGVDAEArateAPPLPGRDLSPLL--TDADADAVrdgiLFT 298
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-383 |
1.54e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 81.13 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGR----LGLRngvtrnfavTSV 111
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWyphvNGHR---------TLH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 112 GGLPLNETTLAEVLQQAGYvtgiigFDYYFGipyshdmgctdtpgynhppcpacpqgdgpsrnlQRDCYT-DVALPLYEN 190
Cdd:cd16150 72 HLLRPDEPNLLKTLKDAGY------HVAWAG---------------------------------KNDDLPgEFAAEAYCD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 191 LNiveqpvnlsslaQKYAEKATQFIQRASTsGRPFLLYVALAHMHVP---------------LPVT--------QLPAAP 247
Cdd:cd16150 113 SD------------EACVRTAIDWLRNRRP-DKPFCLYLPLIFPHPPygveepwfsmidrekLPPRrppglrakGKPSML 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 248 RGRSLYGAGLW-----------------EMDSLVGQIKDKVDHT-VKENTFLWFTGDNGPWAqkcelagsvGPFtGFWQT 309
Cdd:cd16150 180 EGIEKQGLDRWseerwrelratylgmvsRLDHQFGRLLEALKETgLYDDTAVFFFSDHGDYT---------GDY-GLVEK 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1209856998 310 RQGGSPAKQTtwegghRVPALAYWPGRVPVNVTStALLSVLDIFPTVVALAqaslpqgrrfdGVDVSEVLFGRS 383
Cdd:cd16150 250 WPNTFEDCLT------RVPLIIKPPGGPAGGVSD-ALVELVDIPPTLLDLA-----------GIPLSHTHFGRS 305
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-136 |
2.28e-16 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 80.35 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 35 KPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNfavtsVGGL 114
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPL 75
|
90 100
....*....|....*....|..
gi 1209856998 115 PLNETTLAEVLQQAGYVTGIIG 136
Cdd:cd16152 76 PADEKTLAHYFRDAGYETGYVG 97
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
36-413 |
4.93e-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: 76.65 E-value: 4.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGvtrnfAVTSVGGLP 115
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNG-----SWTNCMALG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 116 LNETTLAEVLQQAGYVTGII------GFDYY-FGIpyshdmgctdtpgynhppcpaCPQGDGPSRNLQRDCYTD------ 182
Cdd:cd16156 76 DNVKTIGQRLSDNGIHTAYIgkwhldGGDYFgNGI---------------------CPQGWDPDYWYDMRNYLDelteee 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 183 -----VALPLYENLNIVEQpvnlSSLAQKYAEKATQFIQraSTSGRPFLLYVALAHMHVPL------------------- 238
Cdd:cd16156 135 rrksrRGLTSLEAEGIKEE----FTYGHRCTNRALDFIE--KHKDEDFFLVVSYDEPHHPFlcpkpyasmykdfefpkge 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 239 ----------PVTQLPAAPRGRSLYGAGLWEM----------DSLVGQIKDKVDHTVkENTFLWFTGDNGpwaqkcELAG 298
Cdd:cd16156 209 nayddlenkpLHQRLWAGAKPHEDGDKGTIKHplyfgcnsfvDYEIGRVLDAADEIA-EDAWVIYTSDHG------DMLG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 299 SvgpftgfwQTRQGGSPAkqtTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQasLPQGRRFDGVDVSEV 378
Cdd:cd16156 282 A--------HKLWAKGPA---VYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAG--IPQPKVLEGESILAT 348
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1209856998 379 LFGRSQPGHRVLF---------HPNsgaageFGALQTVRL---ERYK 413
Cdd:cd16156 349 IEDPEIPENRGVFvefgryevdHDG------FGGFQPVRCvvdGRYK 389
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
36-372 |
3.32e-14 |
|
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: 74.22 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAvtsvgGLP 115
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT-----PLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 116 LNETTLAEVLQQAGYVTGIIGFdyyfgipyshdmgcTDTPgynhppcpacPQGDGPSRNLQRDCYTDVALPLY-ENLNIV 194
Cdd:cd16028 76 ARHLTLALELRKAGYDPALFGY--------------TDTS----------PDPRGLAPLDPRLLSYELAMPGFdPVDRLD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 195 EQPVNLSSLAqkY-AEKATQFIQraSTSGRPFLL----------YVALAHMH-------VPLPVTQLPAA---------- 246
Cdd:cd16028 132 EYPAEDSDTA--FlTDRAIEYLD--ERQDEPWFLhlsyirphppFVAPAPYHalydpadVPPPIRAESLAaeaaqhplla 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 247 -----PRGRSLYGAGL-------WEMDSLV----GQIKDkVDHTV-------KE-----NTFLWFTGDNGpwaqkcELAG 298
Cdd:cd16028 208 aflerIESLSFSPGAAnaadlddEEVAQMRatylGLIAE-VDDHLgrlfdylKEtgqwdDTLIVFTSDHG------EQLG 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209856998 299 SvgpftgFWqtrQGGspaKQTTWEGGHRVPALAYWPGRvPVNVTS----TALLSVLDIFPTVvaLAQASLPQGRRFDG 372
Cdd:cd16028 281 D------HW---LWG---KDGFFDQAYRVPLIVRDPRR-EADATRgqvvDAFTESVDVMPTI--LDWLGGEIPHQCDG 343
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
36-367 |
3.91e-14 |
|
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: 73.34 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 36 PNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGrlgLRNGVTRNFavTSVGGLP 115
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG---LFTHLTESW--NNYKGLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 116 LNETTLAEVLQQAGYVTgiigfdyyfgipysHDMGCTDTPGYNHppcpacpqgdgpSRNLQRDCYT-DVALPLYE----- 189
Cdd:cd16171 76 PNYPTWMDRLEKHGYHT--------------QKYGKLDYTSGHH------------SVSNRVEAWTrDVPFLLRQegrpt 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 190 -NLNIVEQPVNLSSLAQKYAEKATQFIQRASTS-GRPFLLYVALAHMHvPLPVTQLPAAPRG----RSLYGAGLWEMDSL 263
Cdd:cd16171 130 vNLVGDRSTVRVMLKDWQNTDKAVHWIRKEAPNlTQPFALYLGLNLPH-PYPSPSMGENFGSirniRAFYYAMCAETDAM 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 264 VGQIKDKVDHT-VKENTFLWFTGDNGpwaqkcELAgsvgpftgfWQTRQGgspAKQTTWEGGHRVPALAYWPGrVPVNVT 342
Cdd:cd16171 209 LGEIISALKDTgLLDKTYVFFTSDHG------ELA---------MEHRQF---YKMSMYEGSSHVPLLIMGPG-IKAGQQ 269
|
330 340
....*....|....*....|....*
gi 1209856998 343 STALLSVLDIFPTVVALAQASLPQG 367
Cdd:cd16171 270 VSDVVSLVDIYPTMLDIAGVPQPQN 294
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
20-355 |
6.17e-05 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 45.28 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 20 YPLVDfcISGKTRGQKPNFVIILADDMGWGDLGAnwaetKDTANLDKMASEGMRFVDfHAAASTCSPsrasllTGRLGLR 99
Cdd:COG3083 231 YPLHP--LQFSDPAKPPNILLIVVDSLRADMLDP-----EVMPNLYAFAQRSLRFTN-HYSSGNSTR------AGLFGLF 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 100 NGVTRNFAvTSVgglpLNETT---LAEVLQQAGYVTGIigfdyyfgipYSHDmgctdtpGYNHPPcpacpqgdgpsrnLQ 176
Cdd:COG3083 297 YGLPGNYW-DSI----LAERTppvLIDALQQQGYQFGL----------FSSA-------GFNSPL-------------FR 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 177 RDCYTDVALPLYENLNIVEQPvnlsslAQKYAEKATQFIQRAStSGRPFLLYVALAHMH------------------VPL 238
Cdd:COG3083 342 QTIFSDVSLPRLHTPGGPAQR------DRQITAQWLQWLDQRD-SDRPWFSYLFLDAPHaysfpadypkpfqpsedcNYL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 239 PVTQLPAAPRGRSLYGAGLWEMDSLVGQIKDKVDHTVK-ENTFLWFTGDNGPwaqkcelagsvgPF----TGFWQTRQGG 313
Cdd:COG3083 415 ALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLlENTIVIITADHGE------------EFnengQNYWGHNSNF 482
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1209856998 314 SPAkQTtwegghRVPALAYWPGRVPVNVTStaLLSVLDIFPT 355
Cdd:COG3083 483 SRY-QL------QVPLVIHWPGTPPQVISK--LTSHLDIVPT 515
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
28-145 |
3.46e-04 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 43.10 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209856998 28 SGKTRGQKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVtrnfA 107
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGS----P 302
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1209856998 108 VTSVGGLPLNetTLAEVLQQAGYVT-----------------GIIGFDYYFGIPY 145
Cdd:COG1368 303 YKRPGQNNFP--SLPSILKKQGYETsffhggdgsfwnrdsfyKNLGFDEFYDRED 355
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
386-418 |
1.26e-03 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 38.45 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|...
gi 1209856998 386 GHRVLFHpNSGAAgefgaLQTVRLERYKAFYIT 418
Cdd:pfam14707 2 PHEFLFH-YCGAA-----LHAVRWGPYKAHFFT 28
|
|
| |
