|
Name |
Accession |
Description |
Interval |
E-value |
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
35-469 |
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: 615.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDMGWGDLGANWAETKDTT-NLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGG 113
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAILTpNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNDmgctdnpgynyppcpacpqsdgrwrnpdr 193
Cdd:cd16161 81 LPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGIPFSHD----------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 194 dcytdvalplyenlniveqpvnlSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQSQR-LYRAS 272
Cdd:cd16161 132 -----------------------SSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRgPYGDA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 273 LQEMDSLVGQIKDKVDHV-AKENTLLWFAGDNGPWAQKCELAGsmGPFSGLWQTHQGGSPAKQTTWEGGHRVPALAYWPG 351
Cdd:cd16161 189 LQEMDDLVGQIMDAVKHAgLKDNTLTWFTSDNGPWEVKCELAV--GPGTGDWQGNLGGSVAKASTWEGGHREPAIVYWPG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 352 RVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHRVLFHPNSGAAGeYGALQTVRLDRYKAF 431
Cdd:cd16161 267 RIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAG-AGALSAVRCGDYKAH 345
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958659099 432 YITGGAKACDGGVGPEQHHVSPLIFNLEDDAAESSPLQ 469
Cdd:cd16161 346 YATGGALACCGSTGPKLYHDPPLLFDLEVDPAESFPLT 383
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-468 |
5.16e-178 |
|
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: 506.33 E-value: 5.16e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGG 113
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVvGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNDMGCTDNPGYNYPPCPAcpqsdgrwrnpdr 193
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYSNDMWPFPLYRNDPPGPLP------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 194 dcytdvalPLYENLNIVEQPVNLSGLAQKYAERAVEFIEQAstSGRPFLLYVGLAHMHVPLSVTPPLANPqSQR-LYRAS 272
Cdd:cd16026 148 --------PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGR-SGAgLYGDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 273 LQEMDSLVGQIKDKVD--HVAkENTLLWFAGDNGPWAQKCELAGSMGPFSGlwqthqggspAKQTTWEGGHRVPALAYWP 350
Cdd:cd16026 217 VEELDWSVGRILDALKelGLE-ENTLVIFTSDNGPWLEYGGHGGSAGPLRG----------GKGTTWEGGVRVPFIAWWP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 351 GRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHRVLFHPNSGaageyGALQTVRLDRYKA 430
Cdd:cd16026 286 GVIPAGTVSDELASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDG-----GDLQAVRSGRWKL 360
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958659099 431 FYITGGAKACDGGVGPEQHHVSPLIFNLEDDAAESSPL 468
Cdd:cd16026 361 HLPTTYRTGTDPGGLDPTKLEPPLLYDLEEDPGETYNV 398
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
36-522 |
1.70e-118 |
|
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: 357.53 E-value: 1.70e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN-FAVTSVGGL 114
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGvFYPGSRGGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 115 PLNETTLAEVLQQAGYVTAMIGKWHL--GHHGSYHPSFRGFDYYFGIPYSNDMGctdnPGYNYPPCPacpqsdgrwrnPD 192
Cdd:cd16158 82 PLNETTIAEVLKTVGYQTAMVGKWHLgvGLNGTYLPTHQGFDHYLGIPYSHDQG----PCQNLTCFP-----------PN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 193 RDCY-----TDVALPLYENLNIVEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQSQR 267
Cdd:cd16158 147 IPCFggcdqGEVPCPLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 268 LYRASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGPWAQKCELAGSmgpfSGLWQTHQGgspakqTTWEGGHRVPAL 346
Cdd:cd16158 227 PFGDALAELDGSVGELLQTLKENGiDNNTLVFFTSDNGPSTMRKSRGGN----AGLLKCGKG------TTYEGGVREPAI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 347 AYWPGRVPVNVTStALLSLLDIFPTVIALAGASLpPNRKFDGVDVSEVLFGKSQTGHRVLFHPNSGAAGEYGALqTVRLD 426
Cdd:cd16158 297 AYWPGRIKPGVTH-ELASTLDILPTIAKLAGAPL-PNVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVF-AVRWG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 427 RYKAFYITGGA--------KACDgGVGPEQHHVSPLIFNLEDDAAESSPLQKGsPEYQELLPKVTRVLADVLQDIAdDNS 498
Cdd:cd16158 374 KYKAHFYTQGAahsgttpdKDCH-PSAELTSHDPPLLFDLSQDPSENYNLLGL-PEYNQVLKQIQQVKERFEASMK-FGE 450
|
490 500
....*....|....*....|....*...
gi 1958659099 499 SQADYTQDPSVTPCCN----PYQITCRC 522
Cdd:cd16158 451 SEINKGEDPALEPCCKpgctPKPSCCQC 478
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
35-487 |
8.85e-114 |
|
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: 344.41 E-value: 8.85e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV---THNFAVTSV 111
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMyggTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 112 GGLPLNETTLAEVLQQAGYVTAMIGKWHLG-----HHGSYH-PSFRGFDYY-FGIPYSNDMGCtDNPGYNYPpcpacpqs 184
Cdd:cd16160 81 GGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennHSDGAHlPSHHGFDFVgTNLPFTNSWAC-DDTGRHVD-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 185 dgrwrNPDRD-CYtdvalpLYENLNIVEQPVNLSGLAQKYAERAVEFIEqaSTSGRPFLLYVGLAHMHVPLSVTPPLANp 263
Cdd:cd16160 152 -----FPDRSaCF------LYYNDTIVEQPIQHEHLTETLVGDAKSFIE--DNQENPFFLYFSFPQTHTPLFASKRFKG- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 264 QSQR-LYRASLQEMDSLVGQIKDK-VDHVAKENTLLWFAGDNGPWAQKCELAGSMGPFSGlwqthqggspAKQTTWEGGH 341
Cdd:cd16160 218 KSKRgRYGDNINEMSWAVGEVLDTlVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKG----------GKGNSWEGGI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 342 RVPALAYWPGRVPVNVtSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHR-VLFHPNSgaageygAL 420
Cdd:cd16160 288 RVPFIAYWPGTIKPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDdILYYCCS-------RL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 421 QTVRLDRYKAFYITG--------GAKACDGGVGPE------------QHHVSPLIFNLEDDAAESSPLQkgSPEYQELLP 480
Cdd:cd16160 360 MAVRYGSYKIHFKTQplpsqeslDPNCDGGGPLSDyivcydcedecvTKHNPPLIFDVEKDPGEQYPLQ--PSVYEHMLE 437
|
....*..
gi 1958659099 481 KVTRVLA 487
Cdd:cd16160 438 AVEKLIA 444
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
35-488 |
1.62e-106 |
|
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: 326.35 E-value: 1.62e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG--VTHNFAVTS-- 110
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfyTTNAHARNAyt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 111 ----VGGLPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNdMGCTDNPgyNYPPCPACPQSD- 185
Cdd:cd16157 81 pqniVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGAPNCH-FGPYDNK--AYPNIPVYRDWEm 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 186 -GRWrnpdrdcytdvalplYENLNIvEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQ 264
Cdd:cd16157 158 iGRY---------------YEEFKI-DKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 265 SQRLYRASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNG-PWAQKCELAGSMGPFSGlwqthqggspAKQTTWEGGHR 342
Cdd:cd16157 222 QRGLYGDAVMELDSSVGKILESLKSLGiENNTFVFFSSDNGaALISAPEQGGSNGPFLC----------GKQTTFEGGMR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 343 VPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHRVLFHPNSgaageygALQT 422
Cdd:cd16157 292 EPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVLLNGKEKDRPIFYYRGD-------ELMA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 423 VRLDRYKAFYIT---------GGAKACDG----GVGP---EQHHVSPLIFNLEDDAAESSPLQKGSPEYQELLPKVTRVL 486
Cdd:cd16157 365 VRLGQYKAHFWTwsnsweefrKGINFCPGqnvpGVTThnqTDHTKLPLLFHLGRDPGEKYPISFKSAEYKQAMPRISKVV 444
|
..
gi 1958659099 487 AD 488
Cdd:cd16157 445 QQ 446
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
35-494 |
3.45e-106 |
|
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: 327.32 E-value: 3.45e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHN------FAV 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASShgmrviLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 109 TSVGGLPLNETTLAEVLQQAGYVTAMIGKWHLGHH------GSYHPSFRGFDYYFGIPYSN--DMGCTDNPGYNYPPCPA 180
Cdd:cd16159 81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHcesrndFCHHPLNHGFDYFYGLPLTNlkDCGDGSNGEYDLSFDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 181 CPQSDG------------------RWR----------------------NPDRDCYtdvalpLYENLNIVEQPVNLSGLA 220
Cdd:cd16159 161 FPLLTAfvlitaltiflllylgavSKRffvfllilsllfislfflllitNRYFNCI------LMRNHEVVEQPMSLENLT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 221 QKYAERAVEFIEQasTSGRPFLLYVGLAHMHVPLSVTPPLANPQSQRLYRASLQEMDSLVGQIKDKVDHVA-KENTLLWF 299
Cdd:cd16159 235 QRLTKEAISFLER--NKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGlKDNTFVYF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 300 AGDNGPWAQKCELAGSMGpfsGLWQTHQGGSpaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGAS 379
Cdd:cd16159 313 TSDNGGHLEEISVGGEYG---GGNGGIYGGK--KMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 380 LPPNRKFDGVDVSEVLFGKSQ-TGHRVLFH------------PNSGAAgeygalqtvrldRYKAFYIT-----GGAKACD 441
Cdd:cd16159 388 LPSDRIIDGRDLMPLLTGQEKrSPHEFLFHycgaelhavryrPRDGGA------------VWKAHYFTpnfypGTEGCCG 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659099 442 GGVGP-----EQHHVSPLIFNLEDDAAESSPLQKGSPEYQELLPKVTRVLADVLQDIA 494
Cdd:cd16159 456 TLLCRcfgdsVTHHDPPLLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIE 513
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-468 |
8.89e-95 |
|
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: 292.90 E-value: 8.89e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGAN---WAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHNFAVTSVG 112
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYgggIGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTTVGLPGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 113 GLPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNDmgctdnpgynyppcpacpqsDGRWrnpd 192
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYHTI--------------------DEEI---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 193 rdcytdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANPQS-QRLYRA 271
Cdd:cd16142 136 -------------------------------VDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSSgKGKYAD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 272 SLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGPWaQKCELAGSMGPFSGlwqthqggspAKQTTWEGGHRVPALAYWP 350
Cdd:cd16142 185 SMVELDDHVGQILDALDELGiADNTIVIFTTDNGPE-QDVWPDGGYTPFRG----------EKGTTWEGGVRVPAIVRWP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 351 GRVPVNVTSTALLSLLDIFPTVIALAGASLPP------NRKFDGVDVSEVLFGKS-QTGHRVLFHpnsGAAGEYGAlqtV 423
Cdd:cd16142 254 GKIKPGRVSNEIVSHLDWFPTLAALAGAPDPKdkllgkDRHIDGVDQSPFLLGKSeKSRRSEFFY---FGEGELGA---V 327
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958659099 424 RLDRYKAFYITGGAKACDGGVGPEQHHVsPLIFNLEDDAAESSPL 468
Cdd:cd16142 328 RWKNWKVHFKAQEDTGGPTGEPFYVLTF-PLIFNLRRDPKERYDV 371
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
25-474 |
5.49e-94 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 291.40 E-value: 5.49e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 25 FSISGETRAPRPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTH 104
Cdd:COG3119 13 AAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 105 NFAvTSVGGLPLNETTLAEVLQQAGYVTAMIGKWHLghhgsyhpsfrgfdyyfgipYSNDmgctdnpgynyppcpacpqs 184
Cdd:COG3119 93 NGE-GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL--------------------YLTD-------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 185 dgrwrnpdrdcytdvalplyenlniveqpvnlsglaqKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLANP- 263
Cdd:COG3119 132 -------------------------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKy 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 264 ----------------------QSQRLYRASLQEMDSLVGQIkdkVDHVAK----ENTLLWFAGDNGPWaqkcelAGSMG 317
Cdd:COG3119 175 dgkdiplppnlaprdlteeelrRARAAYAAMIEEVDDQVGRL---LDALEElglaDNTIVVFTSDNGPS------LGEHG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 318 pFSGlwqthqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPnrKFDGVDVSEVLFG 397
Cdd:COG3119 246 -LRG----------GKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPE--DLDGRSLLPLLTG 312
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659099 398 KSQTGHRVLFHpnsgAAGEYGALQTVRLDRYKAFYitggakaCDGGVGPEQhhvsplIFNLEDDAAESSPLQKGSPE 474
Cdd:COG3119 313 EKAEWRDYLYW----EYPRGGGNRAIRTGRWKLIR-------YYDDDGPWE------LYDLKNDPGETNNLAADYPE 372
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-474 |
8.24e-92 |
|
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: 286.75 E-value: 8.24e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--------- 106
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIpgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 107 ----AVTSVGGLPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGipysndMGCTDNPGYNYPPCPACP 182
Cdd:cd16144 81 tkliPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIG------GTGNGGPPSYYFPPGKPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 183 qsdGRWRNPDRDCYtdvalplyenlniveqpvnlsgLAQKYAERAVEFIEQAstSGRPFLLYvgLAH--MHVPLSVTP-- 258
Cdd:cd16144 155 ---PDLEDGPEGEY----------------------LTDRLTDEAIDFIEQN--KDKPFFLY--LSHyaVHTPIQARPel 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 259 ---------PLANPQSQRLYRASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGPWAQKCELAGSMGPFSGlwqthqg 328
Cdd:cd16144 206 iekyekkkkGLRKGQKNPVYAAMIESLDESVGRILDALEELGlADNTLVIFTSDNGGLSTRGGPPTSNAPLRG------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 329 gspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHR--VL 406
Cdd:cd16144 279 ---GKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRraLF 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659099 407 FH-PN-SGAAGEYGAlqTVRLDRYK--AFYITGgakacdggvgpeqhhvSPLIFNLEDDAAESSPLQKGSPE 474
Cdd:cd16144 356 WHfPHyHGQGGRPAS--AIRKGDWKliEFYEDG----------------RVELYNLKNDIGETNNLAAEMPE 409
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-465 |
1.34e-86 |
|
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: 272.54 E-value: 1.34e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETK-DTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGL 114
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSKiPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGG--VLGGFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 115 PL---NETTLAEVLQQAGYVTAMIGKWHLG-----------HHGSYH-----------PSFRGFDYYFGIPYSNdmgctd 169
Cdd:cd16143 79 PLiepDRVTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkaATGTGKdvdyskpikggPLDHGFDYYFGIPASE------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 170 npgynyppcpacpqsdgrwrnpdrdcytdvALPLyenlniveqpvnlsgLAQKyaerAVEFIEQASTSGRPFLLYVGLAH 249
Cdd:cd16143 153 ------------------------------VLPT---------------LTDK----AVEFIDQHAKKDKPFFLYFALPA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 250 MHVPLSVTPPLANPQSQRLYRASLQEMDSLVGQIKDKVD--HVAkENTLLWFAGDNGP----WAQKCELAG--SMGPFSG 321
Cdd:cd16143 184 PHTPIVPSPEFQGKSGAGPYGDFVYELDWVVGRILDALKelGLA-ENTLVIFTSDNGPspyaDYKELEKFGhdPSGPLRG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 322 LwqthqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQT 401
Cdd:cd16143 263 M----------KADIYEGGHRVPFIVRWPGKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQ 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659099 402 GHRVLFHPNSGAAGeygalQTVRLDRYKAFYITGGAKACDGGVGPEQHHVSPLIFNLEDDAAES 465
Cdd:cd16143 333 EVRESLVHHSGNGS-----FAIRKGDWKLIDGTGSGGFSYPRGKEKLGLPPGQLYNLSTDPGES 391
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
36-465 |
7.10e-83 |
|
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: 263.69 E-value: 7.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGLP 115
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 116 LNETTLAEVLQQAGYVTAMIGKWHLGHHGSY-HPSFRGFDYYFGipYSNDMGCTdnpGYnYPPCpacpqsdgRWRNPDRd 194
Cdd:cd16145 81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTPgHPTKQGFDYFYG--YLDQVHAH---NY-YPEY--------LWRNGEK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 195 cytdvaLPLYENLNIVEQPVNLSGLAQK-YAE-----RAVEFIEQAstSGRPFLLYVGL----AHMHVP----------- 253
Cdd:cd16145 146 ------VPLPNNVIPPLDEGNNAGGGGGtYSHdlftdEALDFIREN--KDKPFFLYLAYtlphAPLQVPddgpykykpkd 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 254 LSVTPPLANPQSQRLYRASLQEMDSLVGQIKDKV-DHVAKENTLLWFAGDNGP-----WAQKCELAGSMGPFSGLwqthq 327
Cdd:cd16145 218 PGIYAYLPWPQPEKAYAAMVTRLDRDVGRILALLkELGIDENTLVVFTSDNGPhseggSEHDPDFFDSNGPLRGY----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 328 ggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASlPPNRKfDGVDVSEVLFGKS-QTGHRVL 406
Cdd:cd16145 293 -----KRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAE-PPEDI-DGISLLPTLLGKPqQQQHDYL 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659099 407 FHpnsgAAGEYGALQTVRLDRYKAFYITGGAKacdggvgpeqhhvSPLIFNLEDDAAES 465
Cdd:cd16145 366 YW----EFYEGGGAQAVRMGGWKAVRHGKKDG-------------PFELYDLSTDPGET 407
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
36-478 |
7.57e-82 |
|
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: 260.56 E-value: 7.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVTHnfavTSVGG-- 113
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWH----TILGRer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPysndmgctdnpgynyppcpacpqsDGRWRNPDR 193
Cdd:cd16146 76 MRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHG------------------------GGGIGQYPD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 194 DCYTDVALPLYENLNIVEQpvnlsglAQKYA-----ERAVEFIEQASTsgRPFLLYVGLAHMHVPLSVTPPLANP----- 263
Cdd:cd16146 132 YWGNDYFDDTYYHNGKFVK-------TEGYCtdvffDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPykdmg 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 264 --QSQRLYRASLQEMDSLVGQIKDKVD--HVAkENTLLWFAGDNGPWaqkcelagsmGPFSGLWQTHQGGSpaKQTTWEG 339
Cdd:cd16146 203 ldDKLAAFYGMIENIDDNVGRLLAKLKelGLE-ENTIVIFMSDNGPA----------GGVPKRFNAGMRGK--KGSVYEG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 340 GHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQ-TGHRVLF--HPNSGAAGE 416
Cdd:cd16146 270 GHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDpWPERTLFthSGRWPPPPK 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659099 417 YGALQTVRLDRYKAfyitggakacdggVGPeqHHVSPLIFNLEDDAAESSPLQKGSPE-YQEL 478
Cdd:cd16146 350 KKRNAAVRTGRWRL-------------VSP--KGFQPELYDIENDPGEENDVADEHPEvVKRL 397
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
36-390 |
1.25e-73 |
|
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: 233.48 E-value: 1.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfaVTSVGGLP 115
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN--VGNGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 116 LNETTLAEVLQQAGYVTAMIGKWHlghhgsyhpsfrgfdyyfgipysndmgctdnpgynyppcpacpqsdgrwrnpdrdc 195
Cdd:cd16022 79 PDEPTLAELLKEAGYRTALIGKWH-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 196 ytdvalplyenlniveqpvnlsglaqkyaERAVEFIEQASTSgRPFLLYVGLAHMHvplsvtPPLAnpqsqrlYRASLQE 275
Cdd:cd16022 103 -----------------------------DEAIDFIERRDKD-KPFFLYVSFNAPH------PPFA-------YYAMVSA 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 276 MDSLVGQIkdkVDHVAK----ENTLLWFAGDNGpwaqkcelaGSMGPFSGLWQthqggspaKQTTWEGGHRVPALAYWPG 351
Cdd:cd16022 140 IDDQIGRI---LDALEElgllDNTLIVFTSDHG---------DMLGDHGLRGK--------KGSLYEGGIRVPFIVRWPG 199
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958659099 352 RVPVNVTSTALLSLLDIFPTVIALAGASLPpnRKFDGVD 390
Cdd:cd16022 200 KIPAGQVSDALVSLLDLLPTLLDLAGIEPP--EGLDGRS 236
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
36-468 |
2.52e-71 |
|
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: 232.83 E-value: 2.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFvDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSV-GGL 114
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVIL-NNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEpYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 115 PLNETTLAEVLQQAGYVTAMIGKWHLGHHGSYH-PSFRGFDYYFGiPYSndmGCTDNpgYNYPPCPACPQSDGRWR---- 189
Cdd:cd16029 80 PLNETLLPQYLKELGYATHLVGKWHLGFYTWEYtPTNRGFDSFYG-YYG---GAEDY--YTHTSGGANDYGNDDLRdnee 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 190 --NPDRDCY-TDValplyenlniveqpvnlsglaqkYAERAVEFIEQASTSgRPFLLYVGLAHMHVPLSVTPPLANPQSQ 266
Cdd:cd16029 154 paWDYNGTYsTDL-----------------------FTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYED 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 267 ----------RLYRASLQEMDSLVGQIKDKVDHV-AKENTLLWFAGDNGPWAQKCElAGSMGPFSGlwqthqggspAKQT 335
Cdd:cd16029 210 kfahikdedrRTYAAMVSALDESVGNVVDALKAKgMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRG----------GKNT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 336 TWEGGHRVPALAYWPGRVPV-NVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHR-VLFHPNSGA 413
Cdd:cd16029 279 LWEGGVRVPAFVWSPLLPPKrGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTeILLNIDDIT 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1958659099 414 AGEYGAlqTVRLDRYKafYITGGakacdggvgpeqhhvsPLiFNLEDDAAESSPL 468
Cdd:cd16029 359 RTTGGA--AIRVGDWK--LIVGK----------------PL-FNIENDPCERNDL 392
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-468 |
1.60e-68 |
|
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: 224.79 E-value: 1.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAStCSPSRASLLTGRLGLRNGVTHnfavtsvGGLP 115
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPL-CTPSRVQLMTGKYNFRNYVVF-------GYLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 116 LNETTLAEVLQQAGYVTAMIGKWHLG--HHGSYHPSFRGFDYY--FGIPYsndmgcTDNPGynyppcpacpqsdGRWRNP 191
Cdd:cd16151 73 PKQKTFGHLLKDAGYATAIAGKWQLGggRGDGDYPHEFGFDEYclWQLTE------TGEKY-------------SRPATP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 192 DRDCYTDVALPLYENlniveqpvnlsglaqKY-----AERAVEFIEQAStsGRPFLLYVGLAHMHVPLSVTP--PLANPQ 264
Cdd:cd16151 134 TFNIRNGKLLETTEG---------------DYgpdlfADFLIDFIERNK--DQPFFAYYPMVLVHDPFVPTPdsPDWDPD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 265 SQRL------YRASLQEMDSLVGQIKDKVD--HVAkENTLLWFAGDNGpwaqkcelagSMGPFSGLW--QTHQGGspaKQ 334
Cdd:cd16151 197 DKRKkddpeyFPDMVAYMDKLVGKLVDKLEelGLR-ENTIIIFTGDNG----------THRPITSRTngREVRGG---KG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 335 TTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSEVLFGKSQTGHRVLFHPNSGAA 414
Cdd:cd16151 263 KTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPLDGRSFAPQLLGKTGSPRREWIYWYYRNP 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958659099 415 GEYGALQTVRLDRYKaFYITGGakacdggvgpeqhhvsplIFNLEDDAAESSPL 468
Cdd:cd16151 343 HKKFGSRFVRTKRYK-LYADGR------------------FFDLREDPLEKNPL 377
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
35-465 |
4.04e-57 |
|
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: 195.74 E-value: 4.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDMGWGDLGANWAETkDTTNLDKMASEGMRFVDFHAAAsTCSPSRASLLTGRLGLRNGV-THNFAVTSVGG 113
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGEI-PTPNLDALAAEGLRFTNFHTTA-LCSPTRAALLTGRNHHQVGMgTMAELATGKPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 114 ----LPLNETTLAEVLQQAGYVTAMIGKWHLGHHgsyhpsfrgfDYYFgipySNDmgctdnpgynyppcpacpqsdgrwr 189
Cdd:cd16025 80 yegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD----------DYYS----TDD------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 190 npdrdcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYV--GLAH--MHVP------------ 253
Cdd:cd16025 121 ---------------------------------LTDKAIEYIDEQKAPDKPFFLYLafGAPHapLQAPkewidkykgkyd 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 254 -------------------------LSVTPPLA------NPQSQRLYrASLQE--------MDSLVGQIkdkVDHVAK-- 292
Cdd:cd16025 168 agwdalreerlerqkelglipadtkLTPRPPGVpawdslSPEEKKLE-ARRMEvyaamvehMDQQIGRL---IDYLKElg 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 293 --ENTLLWFAGDNGP-----WAQkcelAGSmGPFSGlwqthqggspAKQTTWEGGHRVPALAYWPGRV-PVNVTSTALLS 364
Cdd:cd16025 244 elDNTLIIFLSDNGAsaepgWAN----ASN-TPFRL----------YKQASHEGGIRTPLIVSWPKGIkAKGGIRHQFAH 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 365 LLDIFPTVIALAGASLP------PNRKFDGVDVSEVLFGKSQ-TGHRVLFHPNSGAAGeygalqtVRLDRYKAFYITGGa 437
Cdd:cd16025 309 VIDIAPTILELAGVEYPktvngvPQLPLDGVSLLPTLDGAAApSRRRTQYFELFGNRA-------IRKGGWKAVALHPP- 380
|
490 500
....*....|....*....|....*...
gi 1958659099 438 kacdGGVGPEQHhvsplIFNLEDDAAES 465
Cdd:cd16025 381 ----PGWGDQWE-----LYDLAKDPSET 399
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
36-378 |
8.16e-57 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 191.48 E-value: 8.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtSVGGLP 115
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS----TPVGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 116 LNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPSFRGFDYYFG-IPYSNDMgctDNPGYNYPPCPACPQSDgrwrnpdrd 194
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGrNTGSDLY---ADPPDVPYNCSGGGVSD--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 195 cytdvalplyenlniveqpvnlsglaQKYAERAVEFIEQAStsgRPFLLYVGLAHMHVPLSVTPPLANP----------- 263
Cdd:pfam00884 145 --------------------------EALLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDRYPEKyatfkpsscse 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 264 -QSQRLYRASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGPwaqkcelagSMGPFSGLWQTHQGGspakqTTWEGGH 341
Cdd:pfam00884 196 eQLLNSYDNTLLYTDDAIGRVLDKLEENGLlDNTLVVYTSDHGE---------SLGEGGGYLHGGKYD-----NAPEGGY 261
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958659099 342 RVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGA 378
Cdd:pfam00884 262 RVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
36-433 |
1.61e-55 |
|
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: 190.41 E-value: 1.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGA--NWAETkdtTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFavTSVGG 113
Cdd:cd16027 1 PNILWIIADDLSPDLGGYggNVVKT---PNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR--SRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 114 LPLNETTLAEVLQQAGYVTAMIGKWHLghhgsyhpsfrgfdyyfgipysndmgctdNPGYNYPPCPACPQSDGRWRNPDR 193
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTHY-----------------------------NPDAVFPFDDEMRGPDDGGRNAWD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 194 dcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQAStSGRPFLLYVGLAHMHVP---LSVTPPLANPQSQRL-- 268
Cdd:cd16027 127 -----------------------------YASNAADFLNRAK-KGQPFFLWFGFHDPHRPyppGDGEEPGYDPEKVKVpp 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 269 --------------YRASLQEMDSLVGQIkdkVDHVAK----ENTLLWFAGDNGpwaqkcelagsmGPFSGlwqthqggs 330
Cdd:cd16027 177 ylpdtpevredladYYDEIERLDQQVGEI---LDELEEdgllDNTIVIFTSDHG------------MPFPR--------- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 331 pAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNrkFDGVDVSEVLFGKSQTGHRVLFHPN 410
Cdd:cd16027 233 -AKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLPLLKGEKDPGRDYVFAER 309
|
410 420
....*....|....*....|...
gi 1958659099 411 SGAAGEYGALQTVRLDRYKafYI 433
Cdd:cd16027 310 DRHDETYDPIRSVRTGRYK--YI 330
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-469 |
4.52e-54 |
|
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: 187.39 E-value: 4.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggL 114
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 115 PLNETTLAEVLQQAGYVTAMIGKWHL-GHHGSYHPSFR---------GFDYYFGipysndMGCTD---NPGYnyppcpac 181
Cdd:cd16034 76 PPDAPTIADVLKDAGYRTGYIGKWHLdGPERNDGRADDytppperrhGFDYWKG------YECNHdhnNPHY-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 182 pqsdgrWRNPDRDCYTDVALPLYEnlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYvglahmhvpLSVTPP-- 259
Cdd:cd16034 142 ------YDDDGKRIYIKGYSPDAE------------------TDLAIEYLENQADKDKPFALV---------LSWNPPhd 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 260 ---LANPQSQRLYRASLQEM----------------------------DSLVGQIkdkVDHVAK----ENTLLWFAGDNG 304
Cdd:cd16034 189 pytTAPEEYLDMYDPKKLLLrpnvpedkkeeaglredlrgyyamitalDDNIGRL---LDALKElgllENTIVVFTSDHG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 305 pwaqkcELAGSmgpfsglwqtHqgGSPAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGasLPPNR 384
Cdd:cd16034 266 ------DMLGS----------H--GLMNKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCG--LPIPD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 385 KFDGVDVSEVLFGKSQTGHR----VLFHPNSG-AAGEYGALQTVRLDRYKafYitggakACDGGVGpeqhhvsPLIFNLE 459
Cdd:cd16034 326 TVEGRDLSPLLLGGKDDEPDsvllQCFVPFGGgSARDGGEWRGVRTDRYT--Y------VRDKNGP-------WLLFDNE 390
|
490
....*....|
gi 1958659099 460 DDaaessPLQ 469
Cdd:cd16034 391 KD-----PYQ 395
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
35-479 |
2.32e-48 |
|
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: 172.71 E-value: 2.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvGGL 114
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG----PLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 115 PLNETTLAEVLQQAGYVTAMIGKWHLGHHGsyHPSFRGFDYYFGIPysndmgctdNPGYNYPPcpacpqsdgrwrnpdrd 194
Cdd:cd16031 78 DASQPTYPKLLRKAGYQTAFIGKWHLGSGG--DLPPPGFDYWVSFP---------GQGSYYDP----------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 195 cytdvalPLYENLNIVEQPVNLSGLaqkYAERAVEFIEQAStSGRPFLLYVGL-----------AHMHVPLSVT---PPL 260
Cdd:cd16031 130 -------EFIENGKRVGQKGYVTDI---ITDKALDFLKERD-KDKPFCLSLSFkaphrpftpapRHRGLYEDVTipePET 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 261 ANPQS-----------------------------QRLYR---ASLQEMDSLVGQIKDKVDH--VAkENTLLWFAGDNGpw 306
Cdd:cd16031 199 FDDDDyagrpewareqrnrirgvldgrfdtpekyQRYMKdylRTVTGVDDNVGRILDYLEEqgLA-DNTIIIYTSDNG-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 307 aqkcELAGSMGPFSglwqthqggspaKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNrkF 386
Cdd:cd16031 276 ----FFLGEHGLFD------------KRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--M 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 387 DGVDVSEVLFGKSQTGHR------VLFHPNS-GAAGEYGalqtVRLDRYKAFYITGGAKAcdggvgpEQhhvsplIFNLE 459
Cdd:cd16031 338 QGRSLLPLLEGEKPVDWRkefyyeYYEEPNFhNVPTHEG----VRTERYKYIYYYGVWDE-------EE------LYDLK 400
|
490 500
....*....|....*....|....
gi 1958659099 460 DDaaessPLQK----GSPEYQELL 479
Cdd:cd16031 401 KD-----PLELnnlaNDPEYAEVL 419
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-388 |
8.83e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 155.86 E-value: 8.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGV-----THNFAVTS 110
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 111 VG-GLPLNETTLAEVLQQAGYVTAMIGKWHLGhhgsyhpsfrgfdyyfgipysndmgctdnpgynyppcpacpqsdgrwr 189
Cdd:cd16149 81 KPeGYLEGQTTLPEVLQDAGYRCGLSGKWHLG------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 190 npdrdcytdvalplyenlniveqpvnlsglaqkyaERAVEFIEQASTSGRPFLLYVGLAHMHVPLSvtpplanpqsqrlY 269
Cdd:cd16149 113 -----------------------------------DDAADFLRRRAEAEKPFFLSVNYTAPHSPWG-------------Y 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 270 RASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGpwaqkcelaGSMGpFSGLWQTHQGGSPakQTTWEGGHRVPALAY 348
Cdd:cd16149 145 FAAVTGVDRNVGRLLDELEELGlTENTLVIFTSDNG---------FNMG-HHGIWGKGNGTFP--LNMYDNSVKVPFIIR 212
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958659099 349 WPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDG 388
Cdd:cd16149 213 WPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPG 252
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
35-388 |
9.35e-42 |
|
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: 154.25 E-value: 9.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDMGWgDLGANWAETKdTTNLdkMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtSVGGL 114
Cdd:cd16147 1 RPNIVLILTDDQDV-ELGSMDPMPK-TKKL--LADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSP--PGGGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 115 P------LNETTLAEVLQQAGYVTAMIGK----WHLGHHGSYHPsfRGFDYYFGI--PYSNDMGCTDNPGYNYPPcpacp 182
Cdd:cd16147 75 PkfwqngLERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYVP--PGWDEWDGLvgNSTYYNYTLSNGGNGKHG----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 183 qsdgrwRNPDRDCYTDValplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYVG-------------LAH 249
Cdd:cd16147 148 ------VSYPGDYLTDV-----------------------IANKALDFLRRAAADDKPFFLVVAppaphgpftpaprYAN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 250 MHVPLSVTPPLANP-----------------------QSQRLYRA---SLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGD 302
Cdd:cd16147 199 LFPNVTAPPRPPPNnpdvsdkphwlrrlpplnptqiaYIDELYRKrlrTLQSVDDLVERLVNTLEATGQlDNTYIIYTSD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 303 NGPWaqkcelagsMGPFsGLWqthqggsPAKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSLLDIFPTVIALAGASLPP 382
Cdd:cd16147 279 NGYH---------LGQH-RLP-------PGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPS 340
|
....*.
gi 1958659099 383 NrkFDG 388
Cdd:cd16147 341 D--MDG 344
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-479 |
4.20e-41 |
|
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: 151.56 E-value: 4.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAAST----CSPSRASLLTGRlglrngvtHNFAVTS 110
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGR--------TLFHAPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 111 VGG--LPLNETTLAEVLQQAGYVTAMIGKWHLGhhgsyhpsfrgfdyyfgipysndmgctdnpgynyppcpacpqsdgrw 188
Cdd:cd16155 74 GGKaaIPSDDKTWPETFKKAGYRTFATGKWHNG----------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 189 rnpdrdcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPL-------- 260
Cdd:cd16155 107 ----------------------------------FADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYldmyppet 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 261 ----ANPQSQ-----------------------------RLYRASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGpw 306
Cdd:cd16155 153 iplpENFLPQhpfdngegtvrdeqlapfprtpeavrqhlAEYYAMITHLDAQIGRILDALEASGElDNTIIVFTSDHG-- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 307 aqkceLA----GSMGpfsglwqthqggspaKQTTWEGGHRVPALAYWPGrVPVNVTSTALLSLLDIFPTVIALAGASLPP 382
Cdd:cd16155 231 -----LAvgshGLMG---------------KQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPE 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 383 nrKFDGVDVSEVLFGKSQTGHRVLFhpnsgaaGEYGALQ-TVRLDRYKAFYITGGAKAcdggvgpeqhhvsPLIFNLEDD 461
Cdd:cd16155 290 --SVEGKSLLPVIRGEKKAVRDTLY-------GAYRDGQrAIRDDRWKLIIYVPGVKR-------------TQLFDLKKD 347
|
490
....*....|....*...
gi 1958659099 462 AAESSPLQkGSPEYQELL 479
Cdd:cd16155 348 PDELNNLA-DEPEYQERL 364
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-436 |
5.31e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 148.65 E-value: 5.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWgDLGANWAETKD---TTNLDKMASEGMRFVDFHAAaSTCSPSRASLLTGRLGLRNGVThnfavtSVG 112
Cdd:cd16154 1 PNILLIIADDQGL-DSSAQYSLSSDlpvTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVL------AVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 113 G-LPLNETTL--AEVLQQ--AGYVTAMIGKWHLGHHGSYHPSFRGFDYYFGIPYSNdmgctdnpgynyppcpacPQSDGR 187
Cdd:cd16154 73 DeLLLSEETLlqLLIKDAttAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGILGGG------------------VQDYYN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 188 WrnpdrdcytdvalplyeNLNIVEQPVNLSGLA-QKYAERAVEFIEQASTsgrPFLLYVGLAHMHVPLSVtPP------- 259
Cdd:cd16154 135 W-----------------NLTNNGQTTNSTEYAtTKLTNLAIDWIDQQTK---PWFLWLAYNAPHTPFHL-PPaelhsrs 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 260 --------LANPQSqrLYRASLQEMDSLVGQIKDKVDHVAKENTLLWFAGDNG-PwaqkcelagsmGPFSGLWQTHQGgs 330
Cdd:cd16154 194 llgdsadiEANPRP--YYLAAIEAMDTEIGRLLASIDEEERENTIIIFIGDNGtP-----------GQVVDLPYTRNH-- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 331 pAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPpnRKFDGVDVSEVLFGKSQTGHRVLFHPN 410
Cdd:cd16154 259 -AKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAA--EIHDSVSFKPLLSDVNASTRQYNYTEY 335
|
410 420
....*....|....*....|....*.
gi 1958659099 411 SGAAgeyGALQTVRLDRYKAFYITGG 436
Cdd:cd16154 336 ESPT---TTGWATRNQYYKLIESENG 358
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-432 |
6.40e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 149.29 E-value: 6.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNF--AVTSVGG 113
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVenAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 114 LPLNETTLAEVLQQAGYVTAMIGKWHLGHHGSyhPSFRGFDYYFGIpysndmgctdnpgynyppcpacpqsdgrwrNPDR 193
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGKWHVGPEET--PLDYGFDEYLPV------------------------------ETTI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 194 DCYTdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYVGL-------------AHMHVPLSVTPP- 259
Cdd:cd16033 129 EYFL--------------------------ADRAIEMLEELAADDKPFFLRVNFwgphdpyippepyLDMYDPEDIPLPe 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 260 -----LAN-PQSQRLYRASLQ---------------------EMDSLVGQIKDKVDHV-AKENTLLWFAGDNGpwaqkcE 311
Cdd:cd16033 183 sfaddFEDkPYIYRRERKRWGvdtedeedwkeiiahywgyitLIDDAIGRILDALEELgLADDTLVIFTSDHG------D 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 312 LAGSmgpfSGLWQthQGGSPAKQTtweggHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGAslPPNRKFDGVDV 391
Cdd:cd16033 257 ALGA----HRLWD--KGPFMYEET-----YRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGV--DVPPKVDGRSL 323
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958659099 392 SEVLFGKSQTGHR--VL--FHPNsgaaGEYGALQTVRLDRYKAFY 432
Cdd:cd16033 324 LPLLRGEQPEDWRdeVVteYNGH----EFYLPQRMVRTDRYKYVF 364
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-461 |
2.75e-38 |
|
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: 142.68 E-value: 2.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVtsvggLP 115
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADP-----YD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 116 LNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHpsfrGFDYyfgipysndmgctdnpgynyppcpacpqsdgrwrnpDRDC 195
Cdd:cd16037 76 GDVPSWGHALRAAGYETVLIGKLHFRGEDQRH----GFRY------------------------------------DRDV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 196 ytdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAnpqsqRLYR----- 270
Cdd:cd16037 116 ----------------------------TEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFY-----DLYVrrara 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 271 ---ASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGpwaqkcELAGSmgpfSGLWQthqggspaKQTTWEGGHRVPAL 346
Cdd:cd16037 163 ayyGLVEFLDENIGRVLDALEELGLlDNTLIIYTSDHG------DMLGE----RGLWG--------KSTMYEESVRVPMI 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 347 AYWPGRVPVNVTSTALlSLLDIFPTVIALAGASLPPNRkfDGVDVSEVLFGKSQTGHRVL--FHpnsgAAGEYGALQTVR 424
Cdd:cd16037 225 ISGPGIPAGKRVKTPV-SLVDLAPTILEAAGAPPPPDL--DGRSLLPLAEGPDDPDRVVFseYH----AHGSPSGAFMLR 297
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958659099 425 LDRYKafYItggakacdggvgpeqHHVS--PLIFNLEDD 461
Cdd:cd16037 298 KGRWK--YI---------------YYVGypPQLFDLEND 319
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
35-492 |
1.27e-36 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 141.73 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDMGwGD-LGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLT-------GRLGLRNGVTHNF 106
Cdd:PRK13759 6 KPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTglsqwhhGRVGYGDVVPWNY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 107 avtsvgglplnETTLAEVLQQAGYVTAMIGKWHlghhgsYHP--SFRGFDYYF---GIPYSndmgctdnpGYNYPPCPAC 181
Cdd:PRK13759 85 -----------KNTLPQEFRDAGYYTQCIGKMH------VFPqrNLLGFHNVLlhdGYLHS---------GRNEDKSQFD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 182 PQSDGR-W-------RNPDR-----DCYTDVALP--LYENLNiveqPVNLSGlaqkyaERAVEFIEQAStSGRPFLLYVG 246
Cdd:PRK13759 139 FVSDYLaWlrekapgKDPDLtdigwDCNSWVARPwdLEERLH----PTNWVG------SESIEFLRRRD-PTKPFFLKMS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 247 LAHMHVPLSvtPP-----------------------------LANPQ-------------SQRLYRASLQEMDSLVGQI- 283
Cdd:PRK13759 208 FARPHSPYD--PPkryfdmykdadipdphigdweyaedqdpeGGSIDalrgnlgeeyarrARAAYYGLITHIDHQIGRFl 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 284 ---KDKVDHvakENTLLWFAGDNGpwaqkcELAGSmgpfSGLWQthqggspaKQTTWEGGHRVPALAYWPG---RVPVNV 357
Cdd:PRK13759 286 qalKEFGLL---DNTIILFVSDHG------DMLGD----HYLFR--------KGYPYEGSAHIPFIIYDPGgllAGNRGT 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 358 TSTALLSLLDIFPTVIALAGASLPPNrkFDGVDVSEVLFGKsQTGHRVLFHpnsgaaGE----YGALQTVRLDRYKafYI 433
Cdd:PRK13759 345 VIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLIFGQ-YEGWRPYLH------GEhalgYSSDNYLTDGKWK--YI 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659099 434 TGgakacdGGVGPEQhhvsplIFNLEDDAAESSPLQkGSPEYQELLPKVTRVLADVLQD 492
Cdd:PRK13759 414 WF------SQTGEEQ------LFDLKKDPHELHNLS-PSEKYQPRLREMRKKLVDHLRG 459
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
35-428 |
1.40e-33 |
|
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: 132.31 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDM----GWgdLGANWAETKdttNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVtHNFAVTS 110
Cdd:cd16030 2 KPNVLFIAVDDLrpwlGC--YGGHPAKTP---NIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGV-YDNNSYF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 111 VGGLPlNETTLAEVLQQAGYVTAMIGK-WHlGHHGSYHPSFRGFDYYFGIP--------YSNDMGCTDNPGYNYPPCPAC 181
Cdd:cd16030 76 RKVAP-DAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNPPgpekyppgKLCPGKKGGKGGGGGPAWEAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 182 PQSDGRwrnpdrdcYTDvalplyenlniveqpvnlsglaQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSV----- 256
Cdd:cd16030 154 DVPDEA--------YPD----------------------GKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVApkkyf 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 257 --------------------------------------------TPPLANPQSQRL---YRASLQEMDSLVGQIKDKVD- 288
Cdd:cd16030 204 dlyplesiplpnpfdpidlpevawndlddlpkygdipalnpgdpKGPLPDEQARELrqaYYASVSYVDAQVGRVLDALEe 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 289 HVAKENTLLWFAGDNGpwaqkcelagsmgpFS----GLWqthqggspAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLS 364
Cdd:cd16030 284 LGLADNTIVVLWSDHG--------------WHlgehGHW--------GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVE 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659099 365 LLDIFPTVIALAGasLPPNRKFDGVDVSEVLFGKSQTGHRVLF--HPNSGAAGEygalqTVRLDRY 428
Cdd:cd16030 342 LVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSAKWKDAAFsqYPRPSIMGY-----SIRTERY 400
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-390 |
1.57e-33 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 128.05 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILAD----DMgwgdLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHnfavtsv 111
Cdd:cd16148 1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWG------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 112 GGLPLNETTLAEVLQQAGYVTAMIGKWhlGHHGSYHPSFRGFDYYFGIPYsndmgctdnpgynyppcpacpQSDGRWRNP 191
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAVSSN--PHLFGGPGFDRGFDTFEDFRG---------------------QEGDPGEEG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 192 DRDcytdvalplyenlniveqpvnlsglAQKYAERAVEFIEQASTSgRPFLLYVglaHM---HVPLsvtpplanpqsqrL 268
Cdd:cd16148 127 DER-------------------------AERVTDRALEWLDRNADD-DPFFLFL---HYfdpHEPY-------------L 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 269 YRASLQEMDSLVGQIKDKVD-HVAKENTLLWFAGDNGpwaqkcELAGSmgpfSGLWQTHQggspakQTTWEGGHRVPALA 347
Cdd:cd16148 165 YDAEVRYVDEQIGRLLDKLKeLGLLEDTLVIVTSDHG------EEFGE----HGLYWGHG------SNLYDEQLHVPLII 228
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958659099 348 YWPGRVPVNVTStALLSLLDIFPTVIALAGasLPPNRKFDGVD 390
Cdd:cd16148 229 RWPGKEPGKRVD-ALVSHIDIAPTLLDLLG--VEPPDYSDGRS 268
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
402-522 |
4.34e-32 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 119.34 E-value: 4.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 402 GHRVLFHpNSGAAgeygaLQTVRLDRYKAFYITG-----GAKACDGGVGPEQHHVSPLIFNLEDDAAESSPLQKGSPEYQ 476
Cdd:pfam14707 2 PHEFLFH-YCGAA-----LHAVRWGPYKAHFFTPsfdppGAEGCYGSKVPVTHHDPPLLFDLERDPSEKYPLSPDSPEYP 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958659099 477 ELLPKVTRVLADVLQDI--ADDNSSQADYTQDPSVTPCCnPYQITCRC 522
Cdd:pfam14707 76 EVLAEIKAAVEEHKATLvpVPNQLSKGNYLWDPWLQPCC-PTFPACTC 122
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-408 |
1.63e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 118.08 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDM-GWGDLGANWAETKdTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGL 114
Cdd:cd16035 1 PNILLILTDQErYPPPWPAGWAALN-LPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 115 PLNETTLAEVLQQAGYVTAMIGKWHLGHHGsyhpsfrgfdyyfgipysndmgctdNPGYNYppcpacpqsDGRwrnpdrd 194
Cdd:cd16035 80 SPDVPTLGHMLRAAGYYTAYKGKWHLSGAA-------------------------GGGYKR---------DPG------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 195 cytdvalplyenlniveqpvnlsglaqkYAERAVEFIEQASTS---GRPFLLYVGLAHMH-VplsVTPPLANPQSQRL-- 268
Cdd:cd16035 119 ----------------------------IAAQAVEWLRERGAKnadGKPWFLVVSLVNPHdI---MFPPDDEERWRRFrn 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 269 -YRASLQEMDSLVGQIKDKVDHVA-KENTLLWFAGDNGpwaqkcELAGSMGpfsGLwqtHQGGSPAKQTTwegghRVPAL 346
Cdd:cd16035 168 fYYNLIRDVDRQIGRVLDALDASGlADNTIVVFTSDHG------EMGGAHG---LR---GKGFNAYEEAL-----HVPLI 230
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659099 347 AYWPGRVPVNVTSTALLSLLDIFPTVIALAGASLPPNRK----FDGVDVSEVLFGKSQTGHR--VLFH 408
Cdd:cd16035 231 ISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATeappLPGRDLSPLLTDADADAVRdgILFT 298
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
36-461 |
2.71e-29 |
|
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: 117.68 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAA-----EFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 116 LNETTLAEVLQQAGYVTAMIGKWHL-G---HHGsyhpsfrgFDYyfgipysndmgctDNpgynyppcpacpqsdgrwrnp 191
Cdd:cd16032 76 ADIPTFAHYLRAAGYRTALSGKMHFvGpdqLHG--------FDY-------------DE--------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 192 drdcytDVALplyenlniveqpvnlsglaqkyaeRAVEFIEQASTS--GRPFLLYVGLAHMHVPLSVTPPLAN---PQSQ 266
Cdd:cd16032 114 ------EVAF------------------------KAVQKLYDLARGedGRPFFLTVSFTHPHDPYVIPQEYWDlyvRRAR 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 267 RLYRASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGpwaqkcELAGSmgpfSGLWQthqggspaKQTTWEGGHRVPA 345
Cdd:cd16032 164 RAYYGMVSYVDDKVGQLLDTLERTGLaDDTIVIFTSDHG------DMLGE----RGLWY--------KMSFFEGSARVPL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 346 LAYWPGR-VPVNVTstALLSLLDIFPTVIALAGASLPPNR-KFDGVDVSEVLFGKSQTGHRVLFhpnsgaaGEYGA---- 419
Cdd:cd16032 226 IISAPGRfAPRRVA--EPVSLVDLLPTLVDLAGGGTAPHVpPLDGRSLLPLLEGGDSGGEDEVI-------SEYLAegav 296
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958659099 420 --LQTVRLDRYKAFYITGgakacDGgvgpeqhhvsPLIFNLEDD 461
Cdd:cd16032 297 apCVMIRRGRWKFIYCPG-----DP----------DQLFDLEAD 325
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-393 |
3.38e-29 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 116.32 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDMGWGDLGA-NWAETKD---------TTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTH 104
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCyNNAHTGKsesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 105 NFAVTSVGGLPLneTTLAEVLQQAGYVTAMIGKWHLGHHGSYhpsfrgfdyyfgipysndmgcTDNPGYNYppcpacpqs 184
Cdd:cd16153 81 FEAAHPALDHGL--PTFPEVLKKAGYQTASFGKSHLEAFQRY---------------------LKNANQSY--------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 185 dgrwrnpdrdcytdvalplyenlniveqpvnlsglaqkyaERAVEFIEQASTSGRPFLLYVGLAHMHVPlsVTPPlaNPQ 264
Cdd:cd16153 129 ----------------------------------------KSFWGKIAKGADSDKPFFVRLSFLQPHTP--VLPP--KEF 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 265 SQRL-YRASLQEMDSLVGQIKDKVD----HVAKENTLLWFAGDNGpwaqkcelagsmgpfsglWQTHQGGSPAKQTTWEG 339
Cdd:cd16153 165 RDRFdYYAFCAYGDAQVGRAVEAFKayslKQDRDYTIVYVTGDHG------------------WHLGEQGILAKFTFWPQ 226
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659099 340 GHRVPALAYWPGR--VPVNVTSTALLSLLDIFPTVIALAGASLPPNRKFDGVDVSE 393
Cdd:cd16153 227 SHRVPLIVVSSDKlkAPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDLFE 282
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
36-376 |
1.96e-25 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 104.81 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCS-PSRASLLTGRLGLRNGVTHNFAVT----- 109
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSaPNHAALLTGAYPTLHGYTGNGSADpelps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 110 SVGGLPLNETTLAEVLQQAGYVTAMIGkwhlghhgsyhpsfrgfdyyfgipysndmgctdnpgynyppcpacpqsdgrwr 189
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 190 npdrdcytdvalplyenlniveqpvnlsglaqkyaerAVEFIEQaSTSGRPFLLYVGLAHMHVPLsvTPPLANPQSqrlY 269
Cdd:cd00016 108 -------------------------------------LLKAIDE-TSKEKPFVLFLHFDGPDGPG--HAYGPNTPE---Y 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 270 RASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGpwaqkcelagsmGPFSGLwqTHQGGSPAKQTTWEGGHRVPALAY 348
Cdd:cd00016 145 YDAVEEIDERIGKVLDALKKAGDaDDTVIIVTADHG------------GIDKGH--GGDPKADGKADKSHTGMRVPFIAY 210
|
330 340 350
....*....|....*....|....*....|..
gi 1958659099 349 WPG----RVPVNVTSTAllsllDIFPTVIALA 376
Cdd:cd00016 211 GPGvkkgGVKHELISQY-----DIAPTLADLL 237
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
36-429 |
6.12e-24 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293775 [Multi-domain] Cd Length: 468 Bit Score: 104.77 E-value: 6.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNG-VTHNFAVTSvggl 114
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGsWTNCMALGD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 115 plNETTLAEVLQQAGYVTAMIGKWHLGhhgsyhpsfrGFDYY-FGIpysndmgCTD--NPGYNYppcpacpqsDGR---- 187
Cdd:cd16156 77 --NVKTIGQRLSDNGIHTAYIGKWHLD----------GGDYFgNGI-------CPQgwDPDYWY---------DMRnyld 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 188 ---------WRNPdrdcytdvaLPLYENLNIVEQPVnlsgLAQKYAERAVEFIEQASTsgRPFLLYVGLAHMHVPLSVTP 258
Cdd:cd16156 129 elteeerrkSRRG---------LTSLEAEGIKEEFT----YGHRCTNRALDFIEKHKD--EDFFLVVSYDEPHHPFLCPK 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 259 PLAN--------------------PQSQRL-------------------YRASLQEMDSLVGQIKDKVDHVAkENTLLWF 299
Cdd:cd16156 194 PYASmykdfefpkgenayddlenkPLHQRLwagakphedgdkgtikhplYFGCNSFVDYEIGRVLDAADEIA-EDAWVIY 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 300 AGDNGpwaqkcELAGSmgpfSGLWqthqGGSPAkqtTWEGGHRVPALAYWPGRVPVNVTSTALLSLLDIFPTVIALAGAS 379
Cdd:cd16156 273 TSDHG------DMLGA----HKLW----AKGPA---VYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIP 335
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659099 380 LPPnrKFDGVDVSEVLFGKSQTGHRVLF---------HPNsgaageYGALQTVRL---DRYK 429
Cdd:cd16156 336 QPK--VLEGESILATIEDPEIPENRGVFvefgryevdHDG------FGGFQPVRCvvdGRYK 389
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
35-140 |
2.46e-21 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 95.76 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 35 RPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNfavtsVGGL 114
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRN-----GIPL 75
|
90 100
....*....|....*....|....*.
gi 1958659099 115 PLNETTLAEVLQQAGYVTAMIGKWHL 140
Cdd:cd16152 76 PADEKTLAHYFRDAGYETGYVGKWHL 101
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-399 |
4.13e-20 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 92.68 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGR----LGLRNgvTHNFavtsv 111
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWyphvNGHRT--LHHL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 112 ggLPLNETTLAEVLQQAGYVTAMIGKWHLghhgsyhpsfrgfdyyFGIPYSNDMGCTdnpgynyppcpacpqsdgrwrnP 191
Cdd:cd16150 74 --LRPDEPNLLKTLKDAGYHVAWAGKNDD----------------LPGEFAAEAYCD----------------------S 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 192 DRDCytdvalplyenlniveqpvnlsglaqkyAERAVEFIEQASTsGRPFLLYVGLAHMHVPLSVTPP------------ 259
Cdd:cd16150 114 DEAC----------------------------VRTAIDWLRNRRP-DKPFCLYLPLIFPHPPYGVEEPwfsmidreklpp 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 260 --------------LANPQSQRLYRAS---LQEM-----------DSLVGQIKDKVDHVA-KENTLLWFAGDNGPWAqkc 310
Cdd:cd16150 165 rrppglrakgkpsmLEGIEKQGLDRWSeerWRELratylgmvsrlDHQFGRLLEALKETGlYDDTAVFFFSDHGDYT--- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 311 elagsmGPFsGLWQTHQGGSPAKQTtwegghRVPALAYWPGRVPVNVTStALLSLLDIFPTVIALAgaslppnrkfdGVD 390
Cdd:cd16150 242 ------GDY-GLVEKWPNTFEDCLT------RVPLIIKPPGGPAGGVSD-ALVELVDIPPTLLDLA-----------GIP 296
|
....*....
gi 1958659099 391 VSEVLFGKS 399
Cdd:cd16150 297 LSHTHFGRS 305
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
36-382 |
1.29e-16 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 82.31 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAvtsvgGLP 115
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT-----PLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 116 LNETTLAEVLQQAGYVTAMIGKWHL-----GHH------GSYHPSFRGFDYYFGIPYsndmgctdnpgynYPPcpacPQS 184
Cdd:cd16028 76 ARHLTLALELRKAGYDPALFGYTDTspdprGLApldprlLSYELAMPGFDPVDRLDE-------------YPA----EDS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 185 DGRWrnpdrdcytdvalplyenlniveqpvnlsglaqkYAERAVEFIEqaSTSGRPFLLYVGLAHMHVPL---------- 254
Cdd:cd16028 139 DTAF----------------------------------LTDRAIEYLD--ERQDEPWFLHLSYIRPHPPFvapapyhaly 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 255 ---SVTPPLANPQSQR------LYRASLQEMDS---------------------------LVGQIKDKVDHVAK------ 292
Cdd:cd16028 183 dpaDVPPPIRAESLAAeaaqhpLLAAFLERIESlsfspgaanaadlddeevaqmratylgLIAEVDDHLGRLFDylketg 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 293 --ENTLLWFAGDNGpwaqkcELAGsmgpfsglwQTHQGGspaKQTTWEGGHRVPALAYWPGRvPVNVTS----TALLSLL 366
Cdd:cd16028 263 qwDDTLIVFTSDHG------EQLG---------DHWLWG---KDGFFDQAYRVPLIVRDPRR-EADATRgqvvDAFTESV 323
|
410
....*....|....*.
gi 1958659099 367 DIFPTVIALAGASLPP 382
Cdd:cd16028 324 DVMPTILDWLGGEIPH 339
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
36-383 |
6.38e-12 |
|
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: 67.18 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 36 PNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGrlgLRNGVTHNFavTSVGGLP 115
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSG---LFTHLTESW--NNYKGLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 116 LNETTLAEVLQQAGYVTAMIGK--WHLGHHGSyhpSFRGFDYYFGIPYSndmgctdnpgynyppcpacpqsdgrWRNPDR 193
Cdd:cd16171 76 PNYPTWMDRLEKHGYHTQKYGKldYTSGHHSV---SNRVEAWTRDVPFL-------------------------LRQEGR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 194 DCytdvalplyENLNIVEQPVNLSGLAQKYAERAVEFIEQASTS-GRPFLLYVGL--AHMHVPLSVTPPLANPQSQR-LY 269
Cdd:cd16171 128 PT---------VNLVGDRSTVRVMLKDWQNTDKAVHWIRKEAPNlTQPFALYLGLnlPHPYPSPSMGENFGSIRNIRaFY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 270 RASLQEMDSLVGQIKDKV-DHVAKENTLLWFAGDNGpwaqkcELAGSMGPFSglwqthqggspaKQTTWEGGHRVPALAY 348
Cdd:cd16171 199 YAMCAETDAMLGEIISALkDTGLLDKTYVFFTSDHG------ELAMEHRQFY------------KMSMYEGSSHVPLLIM 260
|
330 340 350
....*....|....*....|....*....|....*
gi 1958659099 349 WPGrVPVNVTSTALLSLLDIFPTVIALAGASLPPN 383
Cdd:cd16171 261 GPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQN 294
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
28-391 |
6.47e-12 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 67.76 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 28 SGETRAPRPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVthnfA 107
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGS----P 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 108 VTSVGGLPLNetTLAEVLQQAGYVTAMIgkwHlGHHGS------YHPSFrGFDYYFGIpysNDMGctdnpgynyppcpac 181
Cdd:COG1368 303 YKRPGQNNFP--SLPSILKKQGYETSFF---H-GGDGSfwnrdsFYKNL-GFDEFYDR---EDFD--------------- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 182 PQSDGRWRNPDRDcytdvalpLYEnlniveqpvnlsglaqkyaeravEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLA 261
Cdd:COG1368 358 DPFDGGWGVSDED--------LFD-----------------------KALEELEKLKKPFFAFLITLSNHGPYTLPEEDK 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 262 -----NPQSQRLYRASLQEMDSLVGQIKDKvdhvAK-----ENTLLWFAGDngpwaqkcelagsmgpfsglwqtHQGGSP 331
Cdd:COG1368 407 kipdyGKTTLNNYLNAVRYADQALGEFIEK----LKksgwyDNTIFVIYGD-----------------------HGPRSP 459
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958659099 332 AKQTTWE--GGHRVPALAYWPGRVPVNVTSTaLLSLLDIFPTVIALAGASLPPNRKFdGVDV 391
Cdd:COG1368 460 GKTDYENplERYRVPLLIYSPGLKKPKVIDT-VGSQIDIAPTLLDLLGIDYPSYYAF-GRDL 519
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
13-304 |
2.62e-07 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 52.83 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 13 MVFSGLLYPFVDFSISGETRAPRPNIVIILADDMGWGDLGANwaetkDTTNLDKMASEGMRFVDFHAA--ASTCsPSRAS 90
Cdd:COG1524 1 MKRGLSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLLERA-----HAPNLAALAARGVYARPLTSVfpSTTA-PAHTT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 91 LLTGRLGLRNGVTHNF--------AVTSVGGLP--------LNETTLAEVLQQAGYVTAMIGKWHLGHHGSYHPS----F 150
Cdd:COG1524 75 LLTGLYPGEHGIVGNGwydpelgrVVNSLSWVEdgfgsnslLPVPTIFERARAAGLTTAAVFWPSFEGSGLIDAArpypY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 151 RGFDYYFGIPYSNdmgctdnpgynyppcpacpqsdgrwrnpdrdcytdvalplyenlniveqpvnlsglaqkyaERAVEF 230
Cdd:COG1524 155 DGRKPLLGNPAAD-------------------------------------------------------------RWIAAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 231 IEQASTSGRPFLLYVGL------AHMHVPLSvtpplanPQsqrlYRASLQEMDSLVGQIKDKVD-HVAKENTLLWFAGDN 303
Cdd:COG1524 174 ALELLREGRPDLLLVYLpdldyaGHRYGPDS-------PE----YRAALREVDAALGRLLDALKaRGLYEGTLVIVTADH 242
|
.
gi 1958659099 304 G 304
Cdd:COG1524 243 G 243
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
16-371 |
6.29e-04 |
|
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: 42.58 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 16 SGLLYPFVDFSISgeTRAPRPNIVIILADDMGWGDLGAnwaetKDTTNLDKMASEGMRFVDfHAAASTCSPsrasllTGR 95
Cdd:COG3083 227 SSLNYPLHPLQFS--DPAKPPNILLIVVDSLRADMLDP-----EVMPNLYAFAQRSLRFTN-HYSSGNSTR------AGL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 96 LGLRNGVTHNFAvTSVgglpLNETT---LAEVLQQAGYVtamigkwhlghhgsyhpsfrgfdyyFGIPYSNdmgctdnpG 172
Cdd:COG3083 293 FGLFYGLPGNYW-DSI----LAERTppvLIDALQQQGYQ-------------------------FGLFSSA--------G 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 173 YNYPPCpacpqsdgrwrnpDRDCYTDVALPLYENLNIVEQPvnlsglAQKYAERAVEFIEQAStSGRPFLLYVGLAHMH- 251
Cdd:COG3083 335 FNSPLF-------------RQTIFSDVSLPRLHTPGGPAQR------DRQITAQWLQWLDQRD-SDRPWFSYLFLDAPHa 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659099 252 -----------------VPLSVTPPLANPQSQRLYRASLQEMDSLVGQIKDKVDHVAK-ENTLLWFAGDNGP-------- 305
Cdd:COG3083 395 ysfpadypkpfqpsedcNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLlENTIVIITADHGEefnengqn 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659099 306 -WaqkcelaGSMGPFSgLWQTHqggspakqttwegghrVPALAYWPGRVPVNVTStaLLSLLDIFPT 371
Cdd:COG3083 475 yW-------GHNSNFS-RYQLQ----------------VPLVIHWPGTPPQVISK--LTSHLDIVPT 515
|
|
| |
