|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
42-492 |
0e+00 |
|
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: 622.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTDDLDVSIGGMMPLVKTKKLIGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSSTAWQK 121
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPPGGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 122 TQEPETFSAFLQKHGtYQTFFAGKYLNEYGSKkaGGVEHVPLGWDHWFALESNSKYYNYTLSvNGRAQRHGQNYSEDYLT 201
Cdd:cd16147 81 GLERSTLPVWLQEAG-YRTAYAGKYLNGYGVP--GGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 202 DVLANISIDFLEN-KSNRRPFFMMVSTPAPHSPWTAAPQYESSFPNVKAPRDPNFN--IHGKDKHWLIRQAKTPMTnsSV 278
Cdd:cd16147 157 DVIANKALDFLRRaAADDKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPPRPPPNnpDVSDKPHWLRRLPPLNPT--QI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 279 EFLDNAYRKRWRTLLSVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLPMDKRQLYEFDIRVPLLVRGPYIKPN 358
Cdd:cd16147 235 AYIDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 359 QTSPLLIANVDLGPTILDIAGYNVNeTQMDGMSflpimtgkgnsstwrsdvlveyegegsnisdpacpllgpgvsecfpd 438
Cdd:cd16147 315 VTVDQLVSNIDLAPTILDLAGAPPP-SDMDGRS----------------------------------------------- 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2073632152 439 cvCEDSYNNTYACVRTVSQAANLQYCEFDDNevFVEVYNLTADPFQLSNIAKSI 492
Cdd:cd16147 347 --CGDSNNNTYKCVRTVDDTYNLLYFEWCTG--FRELYDLTTDPYQLTNLAGDL 396
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
42-507 |
1.67e-99 |
|
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: 307.53 E-value: 1.67e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTDDL--DvSIGGM-MPLVKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNtlEGNcSS 116
Cdd:cd16031 2 RPNIIFILTDDHryD-ALGCYgNPIVKTPNIdrLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDN--NGP-LF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 117 TAWQktqepETFSAFLQKHGtYQTFFAGKY-LNEYGskkaggvEHVPLGWDHWFALESNSKYYNYTLSVNG-RAQRHGqn 194
Cdd:cd16031 78 DASQ-----PTYPKLLRKAG-YQTAFIGKWhLGSGG-------DLPPPGFDYWVSFPGQGSYYDPEFIENGkRVGQKG-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 195 ysedYLTDVLANISIDFLENKSNRRPFFMMVSTPAPHSPWTAAPQYESSFPNVKAPRDPNFNI---HGKDKhWLiRQAKt 271
Cdd:cd16031 143 ----YVTDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPETFDDddyAGRPE-WA-REQR- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 272 pmtNSSVEFLDNAYRKRW----------RTLLSVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLpMDKRQLYE 341
Cdd:cd16031 216 ---NRIRGVLDGRFDTPEkyqrymkdylRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGL-FDKRLMYE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 342 FDIRVPLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNVNEtQMDGMSFLPIMTGKgNSSTWRSDVLVEYEGEGsni 420
Cdd:cd16031 292 ESIRVPLIIRDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPE-DMQGRSLLPLLEGE-KPVDWRKEFYYEYYEEP--- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 421 sdpacpllgpgvsecfpdcvcedSYNNTYAC--VRTvSQAANLQYCEFDDNEvfvEVYNLTADPFQLSNIAKSID-QEVL 497
Cdd:cd16031 367 -----------------------NFHNVPTHegVRT-ERYKYIYYYGVWDEE---ELYDLKKDPLELNNLANDPEyAEVL 419
|
490
....*....|
gi 2073632152 498 EKMNHRLMML 507
Cdd:cd16031 420 KELRKRLEEL 429
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
22-504 |
9.77e-92 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 286.39 E-value: 9.77e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 22 FILICVTLHCNSlAEAKANPRPNIVLILTDDL---DVSIGGMmPLVKTKKL--IGDAGITFTNAFVASPLCCPSRASILT 96
Cdd:COG3119 4 LLLLLLALLAAA-AAAAAAKRPNILFILADDLgygDLGCYGN-PLIKTPNIdrLAAEGVRFTNAYVTSPVCSPSRASLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 97 GKYPHNHHVVNNTLEGNCSSTAWQKTqepetFSAFLQKHGtYQTFFAGKYlneygskkaggveHVplgwdhwfalesnsk 176
Cdd:COG3119 82 GRYPHRTGVTDNGEGYNGGLPPDEPT-----LAELLKEAG-YRTALFGKW-------------HL--------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 177 yynytlsvngraqrhgqnysedYLTDVLANISIDFLENKSNR-RPFFMMVSTPAPHSPWTAAPQYESSFPNVKAPRDPNF 255
Cdd:COG3119 128 ----------------------YLTDLLTDKAIDFLERQADKdKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPLPPNL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 256 NIHGKDKhwlirqaktpmtnssvEFLDNAYRKRWRTLLSVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLPMD 335
Cdd:COG3119 186 APRDLTE----------------EELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 336 KRQLYEFDIRVPLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNVNETqMDGMSFLPIMTGKgnSSTWRSDVLVEYE 414
Cdd:COG3119 250 KGTLYEGGIRVPLIVRWPgKIKAGSVSDALVSLIDLLPTLLDLAGVPIPED-LDGRSLLPLLTGE--KAEWRDYLYWEYP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 415 GEGSNisdpacpllgpgvsecfpdcvcedsynntyACVRTvsqaANLQYCEFDDNEVFVEVYNLTADPFQLSNIAKSiDQ 494
Cdd:COG3119 327 RGGGN------------------------------RAIRT----GRWKLIRYYDDDGPWELYDLKNDPGETNNLAAD-YP 371
|
490
....*....|
gi 2073632152 495 EVLEKMNHRL 504
Cdd:COG3119 372 EVVAELRALL 381
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-401 |
1.33e-63 |
|
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: 213.94 E-value: 1.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDL---DVSIGGMmPLVKTKKLigDA----GITFTNAFVASPLCCPSRASILTGKYPHNHHvVNNTLEGNCS 115
Cdd:cd16144 1 PNIVLILVDDLgwaDLGCYGS-KFYETPNI--DRlakeGMRFTQAYAAAPVCSPSRASILTGQYPARLG-ITDVIPGRRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 116 STAWQKTQEPE----------TFSAFLQKHGtYQTFFAGKY-LneygskkAGGVEHVPL--GWDHWFALESNSKYYNYTL 182
Cdd:cd16144 77 PPDNTKLIPPPsttrlpleevTIAEALKDAG-YATAHFGKWhL-------GGEGGYGPEdqGFDVNIGGTGNGGPPSYYF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 183 SVNGRAQRHGQNYSEDYLTDVLANISIDFLEnKSNRRPFFMMVSTPAPHSPWTAAPQYESSFPNVKAPrdpnfnihGKDK 262
Cdd:cd16144 149 PPGKPNPDLEDGPEGEYLTDRLTDEAIDFIE-QNKDKPFFLYLSHYAVHTPIQARPELIEKYEKKKKG--------LRKG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 263 HWLIRQAktpmtnSSVEfldnayrkrwrtllSVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLPMD------- 335
Cdd:cd16144 220 QKNPVYA------AMIE--------------SLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTSnaplrgg 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073632152 336 KRQLYEFDIRVPLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNVNETQ-MDGMSFLPIMTGKGN 401
Cdd:cd16144 280 KGSLYEGGIRVPLIVRWPgVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQhLDGVSLVPLLKGGEA 347
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
43-504 |
2.34e-62 |
|
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: 209.29 E-value: 2.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDLDVSIGG-MMPLVKTKKLigDA----GITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTlegncsST 117
Cdd:cd16027 1 PNILWIIADDLSPDLGGyGGNVVKTPNL--DRlaaeGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLR------SR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 118 AWQKTQEPETFSAFLQKHGtYQTFFAGkylneygsKKAGGVEHVPLGWDHWFALESNSKyynytlsvngraqrhgqnyse 197
Cdd:cd16027 73 GFPLPDGVKTLPELLREAG-YYTGLIG--------KTHYNPDAVFPFDDEMRGPDDGGR--------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 198 dYLTDVLANISiDFLENKSNRRPFFMMVSTPAPHSPWTAAPQYESSFPNVKAPRDPNFnihgkdkhwlirqAKTPMTNSS 277
Cdd:cd16027 123 -NAWDYASNAA-DFLNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPYL-------------PDTPEVRED 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 278 V-EFLDNAYRkrwrtllsVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYhtgqfSLPMDKRQLYEFDIRVPLLVRGPY-I 355
Cdd:cd16027 188 LaDYYDEIER--------LDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkI 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 356 KPNQTSPLLIANVDLGPTILDIAGYNVNEtQMDGMSFLPIMtgKGNSSTWRSDVLVEYEGEGsnisdpacpllgpgvsec 435
Cdd:cd16027 255 KPGSVSDALVSFIDLAPTLLDLAGIEPPE-YLQGRSFLPLL--KGEKDPGRDYVFAERDRHD------------------ 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073632152 436 fpdcvcedsynNTYACVRTVSqaanlqycefDD------NEVFVEVYNLTADPFQLSNIAKSID-QEVLEKMNHRL 504
Cdd:cd16027 314 -----------ETYDPIRSVR----------TGrykyirNYMPEELYDLKNDPDELNNLADDPEyAEVLEELRAAL 368
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-488 |
2.39e-62 |
|
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: 210.12 E-value: 2.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTDDL---DVSIGGMMPlVKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVnntleGNCSS 116
Cdd:cd16034 1 KPNILFIFADQHraqALGCAGDDP-VKTPNLdrLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF-----GNDVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 117 TAwqktQEPETFSAFLQKHGtYQTFFAGKY-LNEYGSKKAGGVEHVP-----LGWDHWFALESNSKYYNYTLSVNGRAQR 190
Cdd:cd16034 75 LP----PDAPTIADVLKDAG-YRTGYIGKWhLDGPERNDGRADDYTPpperrHGFDYWKGYECNHDHNNPHYYDDDGKRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 191 HGQNYSEDYLTDVLanisIDFLEN-KSNRRPFFMMVSTPAPHSPWTAAPQ-YESSFPNVKAPRDPNFNIHGKDKHWLIRQ 268
Cdd:cd16034 150 YIKGYSPDAETDLA----IEYLENqADKDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLLLRPNVPEDKKEEAGLRED 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 269 AKTPMtnSSVEfldnayrkrwrtllSVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLpMDKRQLYEFDIRVPL 348
Cdd:cd16034 226 LRGYY--AMIT--------------ALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGL-MNKQVPYEESIRVPF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 349 LVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNVNETqMDGMSFLPIMTGKGNSST-WRSDVLVEYEGEGSNISDPacp 426
Cdd:cd16034 289 IIRYPgKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT-VEGRDLSPLLLGGKDDEPdSVLLQCFVPFGGGSARDGG--- 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2073632152 427 llgpgvsecfpdcvcedsynnTYACVRTVsqaanlQY---CEFDDNEVFvevYNLTADPFQLSNI 488
Cdd:cd16034 365 ---------------------EWRGVRTD------RYtyvRDKNGPWLL---FDNEKDPYQLNNL 399
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
43-391 |
1.24e-60 |
|
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: 199.97 E-value: 1.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDL---DVSIGGMmPLVKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSST 117
Cdd:cd16022 1 PNILLIMTDDLgydDLGCYGN-PDIKTPNLdrLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 118 awqktqEPETFSAFLQKHGtYQTFFAGKylneygskkaggvehvplgwdhWfalesnskyynytlsvngraqrHGQnyse 197
Cdd:cd16022 80 ------DEPTLAELLKEAG-YRTALIGK----------------------W----------------------HDE---- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 198 dyltdvlaniSIDFLENKSNRRPFFMMVSTPAPHSPWtaapqyessfpnvkaprdpnfnihgkdkhwlirqaktpmtnss 277
Cdd:cd16022 105 ----------AIDFIERRDKDKPFFLYVSFNAPHPPF------------------------------------------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 278 vefldnAYrkrWRTLLSVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLPMDKRQLYEFDIRVPLLVRGP-YIK 356
Cdd:cd16022 132 ------AY---YAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPgKIP 202
|
330 340 350
....*....|....*....|....*....|....*
gi 2073632152 357 PNQTSPLLIANVDLGPTILDIAGYNVNETqMDGMS 391
Cdd:cd16022 203 AGQVSDALVSLLDLLPTLLDLAGIEPPEG-LDGRS 236
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
43-380 |
2.19e-59 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 198.80 E-value: 2.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDL---DVSIGG----MMPLVKTKKligDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTLegncs 115
Cdd:pfam00884 1 PNVVLVLGESLrapDLGLYGyprpTTPFLDRLA---EEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 116 staWQKTQEPETFSAFLQKHGtYQTFFAGKYLNEYGSKKAGGVehvpLGWDHWFALESNSKYYNYtlsvngRAQRHGQNY 195
Cdd:pfam00884 73 ---VGLPRTEPSLPDLLKRAG-YNTGAIGKWHLGWYNNQSPCN----LGFDKFFGRNTGSDLYAD------PPDVPYNCS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 196 SEDYLTDVLANISIDFLENKSnrRPFFMMVSTPAPHSPWTAAPQYESSFPNVKAPRDpnfnihgkdkhwlirqaktpmtn 275
Cdd:pfam00884 139 GGGVSDEALLDEALEFLDNND--KPFFLVLHTLGSHGPPYYPDRYPEKYATFKPSSC----------------------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 276 ssveFLDNAYRKRWRTLLSVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQF---SLPMDKRQLYEFDIRVPLLVRG 352
Cdd:pfam00884 194 ----SEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGggyLHGGKYDNAPEGGYRVPLLIWS 269
|
330 340
....*....|....*....|....*....
gi 2073632152 353 PY-IKPNQTSPLLIANVDLGPTILDIAGY 380
Cdd:pfam00884 270 PGgKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-504 |
1.48e-55 |
|
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: 192.44 E-value: 1.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDL--DVSIGGMMPLVKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSSTA 118
Cdd:cd16033 1 PNILFIMTDQQryDTLGCYGNPIVKTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 119 WQKTQepETFSAFLQKHGtYQTFFAGKYlneygskkAGGVEHVPL--GWDHWFALESNSKYYnytlsvngraqrhgqnys 196
Cdd:cd16033 81 LPPGV--ETFSEDLREAG-YRNGYVGKW--------HVGPEETPLdyGFDEYLPVETTIEYF------------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 197 edyltdvLANISIDFLEN-KSNRRPFFMMVSTPAPHSPWTAAPQYESSFPNVKAPRDPNFNIHGKDKHWLIRQAKTPMTn 275
Cdd:cd16033 132 -------LADRAIEMLEElAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYRRERKRWG- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 276 ssvefLDNAYRKRWRTLLS--------VDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLpMDKRQ-LYEFDIRV 346
Cdd:cd16033 204 -----VDTEDEEDWKEIIAhywgyitlIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRL-WDKGPfMYEETYRI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 347 PLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNVNETqMDGMSFLPIMTGKGNSStWRSDVLVEYEGEGSnisdpac 425
Cdd:cd16033 278 PLIIKWPgVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPK-VDGRSLLPLLRGEQPED-WRDEVVTEYNGHEF------- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 426 pllgpgvsecfpdcvcedsynntYACVRTVsqaanlqyceFDDNEVFV-------EVYNLTADPFQLSN-IAKSIDQEVL 497
Cdd:cd16033 349 -----------------------YLPQRMV----------RTDRYKYVfngfdidELYDLESDPYELNNlIDDPEYEEIL 395
|
....*..
gi 2073632152 498 EKMNHRL 504
Cdd:cd16033 396 REMRTRL 402
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
43-500 |
4.93e-49 |
|
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: 174.66 E-value: 4.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDL---DVSIGGMmPLVKTKKL--IGDAGITFTNaFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNcsst 117
Cdd:cd16146 1 PNVILILTDDQgygDLGFHGN-PILKTPNLdrLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRTGVWHTILGRE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 118 awqkTQEPE--TFSAFLQKHGtYQTFFAGKY--------------LNEYGSKKAGGVEHVPlgwDHWfalesNSKYYNYT 181
Cdd:cd16146 75 ----RMRLDetTLAEVFKDAG-YRTGIFGKWhlgdnypyrpqdrgFDEVLGHGGGGIGQYP---DYW-----GNDYFDDT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 182 LSVNGRAQRHgqnysEDYLTDVLANISIDFLENKSNRrPFFMMVSTPAPHSPWTAAPQYESSFPNvKAPRDPNFNIHGKd 261
Cdd:cd16146 142 YYHNGKFVKT-----EGYCTDVFFDEAIDFIEENKDK-PFFAYLATNAPHGPLQVPDKYLDPYKD-MGLDDKLAAFYGM- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 262 khwlirqaktpMTNssvefldnayrkrwrtllsVDDLVEKVVRKLEVSGELSSTYIIFTSDNG---YHTGQFSLPM--DK 336
Cdd:cd16146 214 -----------IEN-------------------IDDNVGRLLAKLKELGLEENTIVIFMSDNGpagGVPKRFNAGMrgKK 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 337 RQLYEFDIRVPLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNVNET-QMDGMSFLPIMTGKgnSSTWRSDVLVEYE 414
Cdd:cd16146 264 GSVYEGGHRVPFFIRWPgKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGiKLDGRSLLPLLKGE--SDPWPERTLFTHS 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 415 GEGSNisdpacpllgpgvsecfpdcvcEDSYNNTYAcVRtvsqaaNLQYCEFDDNEVFVEVYNLTADPFQLSNIAKSIdQ 494
Cdd:cd16146 342 GRWPP----------------------PPKKKRNAA-VR------TGRWRLVSPKGFQPELYDIENDPGEENDVADEH-P 391
|
....*.
gi 2073632152 495 EVLEKM 500
Cdd:cd16146 392 EVVKRL 397
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-400 |
7.21e-49 |
|
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: 174.32 E-value: 7.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDL---DVSIGGMmPLVKTKKLigDA----GITFTNAFVASPLCCPSRASILTGKyphnhHVVNNTLEGNCS 115
Cdd:cd16145 1 PNIIFILADDLgygDLGCYGQ-KKIKTPNL--DRlaaeGMRFTQHYAGAPVCAPSRASLLTGL-----HTGHTRVRGNSE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 116 S-TAWQKTQEPETFSAFLQKHGtYQTFFAGKY-LNEYGSkkAGGVEhvPLGWDHWFA--------------LESNSKY-- 177
Cdd:cd16145 73 PgGQDPLPPDDVTLAEVLKKAG-YATAAFGKWgLGGPGT--PGHPT--KQGFDYFYGyldqvhahnyypeyLWRNGEKvp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 178 YNYTLSVNGRAQRHGQNYSEDYLTDVLANISIDFL-ENKSnrRPFFMMVSTPAPHSPWtAAPQyessfpnvkapRDPNFN 256
Cdd:cd16145 148 LPNNVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIrENKD--KPFFLYLAYTLPHAPL-QVPD-----------DGPYKY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 257 ihgKDKHWLIRqAKTPMTNSsvefldnayRKRWRTLLS-VDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHT-GQFSLPM 334
Cdd:cd16145 214 ---KPKDPGIY-AYLPWPQP---------EKAYAAMVTrLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeGGSEHDP 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073632152 335 D-----------KRQLYEFDIRVPLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNVnETQMDGMSFLPIMTGKG 400
Cdd:cd16145 281 DffdsngplrgyKRSLYEGGIRVPFIARWPgKIPAGSVSDHPSAFWDFMPTLADLAGAEP-PEDIDGISLLPTLLGKP 357
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
42-490 |
1.96e-48 |
|
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: 173.53 E-value: 1.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTDDLDVSIGGMM-PLVKTKKLigDA----GITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNtlegncsS 116
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYGgHPAKTPNI--DRlaarGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDN-------N 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 117 TAWQKTQEP-ETFSAFLQKHGtYQTFFAGKYLNEYGSKKaggvEHVPLGWDHWFALESNSKYYNYTLSVNGRAQRHGQNY 195
Cdd:cd16030 73 SYFRKVAPDaVTLPQYFKENG-YTTAGVGKIFHPGIPDG----DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 196 S---------EDYLTDVLANISIDFLENKSNR-RPFFMMVSTPAPHSPWTaAPQ-----YESSFPNVKAPRDPNF--NIH 258
Cdd:cd16030 148 PaweaadvpdEAYPDGKVADEAIEQLRKLKDSdKPFFLAVGFYKPHLPFV-APKkyfdlYPLESIPLPNPFDPIDlpEVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 259 GKDKHWLIRQAKTPMTNSSVEF--LDNAYrkrWRTLLS--------VDDLVEKVVRKLEVSGELSSTYIIFTSDNGYH-- 326
Cdd:cd16030 227 WNDLDDLPKYGDIPALNPGDPKgpLPDEQ---ARELRQayyasvsyVDAQVGRVLDALEELGLADNTIVVLWSDHGWHlg 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 327 -TGQFSlpmdKRQLYEFDIRVPLLVRGPYIK-PNQTSPLLIANVDLGPTILDIAGYNVNEtQMDGMSFLPIMtgKGNSST 404
Cdd:cd16030 304 eHGHWG----KHTLFEEATRVPLIIRAPGVTkPGKVTDALVELVDIYPTLAELAGLPAPP-CLEGKSLVPLL--KNPSAK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 405 WRSDVLVEYegegsnisdPACPLLGpgvsecfpdcvcedsynntYAcVRTvsqaANLQYCEF--DDNEVFVEVYNLTADP 482
Cdd:cd16030 377 WKDAAFSQY---------PRPSIMG-------------------YS-IRT----ERYRYTEWvdFDKVGAEELYDHKNDP 423
|
....*...
gi 2073632152 483 FQLSNIAK 490
Cdd:cd16030 424 NEWKNLAN 431
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-407 |
7.53e-47 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 167.78 E-value: 7.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDLDV-SIGGMMPLV-KTKKL--IGDAGITFTNAFvASPLCCPSRASILTGKYPHNHHVVNNTLegncssta 118
Cdd:cd16151 1 PNIILIMADDLGYeCIGCYGGESyKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYVVFGYL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 119 WQKTQepeTFSAFLQKHGtYQTFFAGKY-LNEYGSKKaggvEHVP-LGWDHWFALESN---SKYYNYTLSVNGRAQRHGQ 193
Cdd:cd16151 72 DPKQK---TFGHLLKDAG-YATAIAGKWqLGGGRGDG----DYPHeFGFDEYCLWQLTetgEKYSRPATPTFNIRNGKLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 194 NYSE-DYLTDVLANISIDFLENKSNrRPFFMMVSTPAPHSPWTAAPQYEssfpnvkaPRDPNFNIHGKDKHwlirqaktp 272
Cdd:cd16151 144 ETTEgDYGPDLFADFLIDFIERNKD-QPFFAYYPMVLVHDPFVPTPDSP--------DWDPDDKRKKDDPE--------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 273 mtnssvEFLD-NAYrkrwrtllsVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLPMD------KRQLYEFDIR 345
Cdd:cd16151 206 ------YFPDmVAY---------MDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTNGrevrggKGKTTDAGTH 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2073632152 346 VPLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNV-NETQMDGMSFLPIMTGKGNSSTWRS 407
Cdd:cd16151 271 VPLIVNWPgLIPAGGVSDDLVDFSDFLPTLAELAGAPLpEDYPLDGRSFAPQLLGKTGSPRREW 334
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-403 |
5.36e-45 |
|
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: 163.53 E-value: 5.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDL---DVSIGGMMPLVKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSSt 117
Cdd:cd16143 1 PNIVIILADDLgygDISCYNPDSKIPTPNIdrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 118 AWQKTQepETFSAFLQKHGtYQTFFAGK-------YLNEYGSKKAGGVEHV---------PL--GWDHWFALeSNSKyyn 179
Cdd:cd16143 80 LIEPDR--VTLAKMLKQAG-YRTAMVGKwhlgldwKKKDGKKAATGTGKDVdyskpikggPLdhGFDYYFGI-PASE--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 180 ytlsvngraqrhgqnysedyLTDVLANISIDFL-ENKSNRRPFFMMVSTPAPHSPWTAAPQYessfpNVKAprdpNFNIH 258
Cdd:cd16143 153 --------------------VLPTLTDKAVEFIdQHAKKDKPFFLYFALPAPHTPIVPSPEF-----QGKS----GAGPY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 259 GkDkhwLIRQaktpmtnssvefldnayrkrwrtllsVDDLVEKVVRKLEVSGELSSTYIIFTSDNG---YHTGQFSLPMD 335
Cdd:cd16143 204 G-D---FVYE--------------------------LDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 336 ----------KRQLYEFDIRVPLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNVNETQ-MDGMSFLPIMTGKGNSS 403
Cdd:cd16143 254 hdpsgplrgmKADIYEGGHRVPFIVRWPgKIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNAaEDSFSFLPALLGPKKQE 333
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-415 |
1.96e-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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 161.19 E-value: 1.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTDDL---DVSIGGMMPlVKTKKLigDA----GITFTNAFVA---SP-LCCPSRASILTGKYphnhhvVNNTL 110
Cdd:cd16155 2 KPNILFILADDQradTIGALGNPE-IQTPNL--DRlarrGTSFTNAYNMggwSGaVCVPSRAMLMTGRT------LFHAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 111 EGNcsstAWQKTQEPETFSAFLQKHGtYQTFFAGKYLNEYgskkaggvehvplgwdhwfalesnskyynytlsvngraqr 190
Cdd:cd16155 73 EGG----KAAIPSDDKTWPETFKKAG-YRTFATGKWHNGF---------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 191 hgqnysedyltdvlANISIDFLENKSNR-RPFFMMVSTPAPHSPWTAAPQYESSFPNVKAPRDPNF-NIHGKDKHWL-IR 267
Cdd:cd16155 108 --------------ADAAIEFLEEYKDGdKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPLPENFlPQHPFDNGEGtVR 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 268 Q---AKTPMTNSSV-EFLDNAYRkrwrtLLS-VDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLpMDKRQLYEF 342
Cdd:cd16155 174 DeqlAPFPRTPEAVrQHLAEYYA-----MIThLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGL-MGKQNLYEH 247
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2073632152 343 DIRVPLLVRGPYIKPNQTSPLLIANVDLGPTILDIAGYNVNETqMDGMSFLPIMTGKGNssTWRSDVLVEYEG 415
Cdd:cd16155 248 SMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPES-VEGKSLLPVIRGEKK--AVRDTLYGAYRD 317
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-419 |
8.71e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 158.09 E-value: 8.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDLDVSIGGMM--PLVKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNtlegncsSTA 118
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYghPVVRTPNLdrLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDN-------ADP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 119 WQKTqePETFSAFLQKHGtYQTFFAGKylneygskkaggvehvplgwdhwfalesnskyynytLSVNGRAQRHGQNYSED 198
Cdd:cd16037 74 YDGD--VPSWGHALRAAG-YETVLIGK------------------------------------LHFRGEDQRHGFRYDRD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 199 yltdvLANISIDFL-ENKSNRRPFFMMVSTPAPHSPWTaAPQyessfpnvkaprdpnfnihgkdkhwlirqaktpmtnss 277
Cdd:cd16037 115 -----VTEAAVDWLrEEAADDKPWFLFVGFVAPHFPLI-APQ-------------------------------------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 278 vEFLDnAYRKRWRT----LLS-VDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLpMDKRQLYEFDIRVPLLVRG 352
Cdd:cd16037 151 -EFYD-LYVRRARAayygLVEfLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGL-WGKSTMYEESVRVPMIISG 227
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2073632152 353 PYIKPNQTSPLLIANVDLGPTILDIAGYNVNETQmDGMSFLPIMTGKGNsstWRSDVLVEYEGEGSN 419
Cdd:cd16037 228 PGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDL-DGRSLLPLAEGPDD---PDRVVFSEYHAHGSP 290
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-510 |
4.53e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 153.16 E-value: 4.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDLDV-SIGGM-MPLVKTKKLigDA----GITFTNAFVASPLCCPSRASILTGKYPHnhhvVNntleGNCSS 116
Cdd:cd16150 1 PNIVIFVADQLRAdSLGHLgNPAAVTPNL--DAlaaeGVRFSNAYCQNPVCSPSRCSFLTGWYPH----VN----GHRTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 117 TAWQKTQEPETFSAfLQKHGtYQTFFAGKylNEYgskkaggvehvplgWDHWFALESnskyynYTLSvngraqrhgqnys 196
Cdd:cd16150 71 HHLLRPDEPNLLKT-LKDAG-YHVAWAGK--NDD--------------LPGEFAAEA------YCDS------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 197 eDYLTdvlANISIDFLENKSNRRPFFMMVSTPAPHSPWTAAPQYESSFPNVKAP-RDPNFNIHGKDKHWLIRqaktpMTN 275
Cdd:cd16150 114 -DEAC---VRTAIDWLRNRRPDKPFCLYLPLIFPHPPYGVEEPWFSMIDREKLPpRRPPGLRAKGKPSMLEG-----IEK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 276 SSVEFLDNAyrkRWRTLLSV--------DDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLpMDKRQ--LYEFDIR 345
Cdd:cd16150 185 QGLDRWSEE---RWRELRATylgmvsrlDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGL-VEKWPntFEDCLTR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 346 VPLLVRGPYIKPNQTSPLLIANVDLGPTILDIAGYNVNETQMdGMSFLPIMtgKGNSSTWRSDVLVE---YEGEGSNISD 422
Cdd:cd16150 261 VPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHF-GRSLLPVL--AGETEEHRDAVFSEggrLHGEEQAMEG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 423 PACP--LLGPGVSECF-PDCVCedsynntyACVRTVSQAANLQYCEFDDNevfvEVYNLTADPFQLSNIAKSID-QEVLE 498
Cdd:cd16150 338 GHGPydLKWPRLLQQEePPEHT--------KAVMIRTRRYKYVYRLYEPD----ELYDLEADPLELHNLIGDPAyAEIIA 405
|
490
....*....|....
gi 2073632152 499 KMNHRLM--MLQSC 510
Cdd:cd16150 406 EMKQRLLrwMVETS 419
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
42-403 |
8.10e-39 |
|
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: 146.55 E-value: 8.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTDDL---DVSIGGMmPLVKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYPH---NHHVVnntlegn 113
Cdd:cd16026 1 KPNIVVILADDLgygDLGCYGS-PLIKTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVrvgLPGVV------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 114 csSTAWQKTQEPE---TFSAFLQKHGtYQTFFAGKY-LneyGSKKaggvEHVPL--GWDHWF-ALESN----SKYYNYTL 182
Cdd:cd16026 73 --GPPGSKGGLPPdeiTIAEVLKKAG-YRTALVGKWhL---GHQP----EFLPTrhGFDEYFgIPYSNdmwpFPLYRNDP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 183 SVNGR-----AQRHGQNYSEDYLTDVLANISIDFLENKSNrRPFFMMVSTPAPHSPWTAAPQYEssfpnvkaprdpnfni 257
Cdd:cd16026 143 PGPLPplmenEEVIEQPADQSSLTQRYTDEAVDFIERNKD-QPFFLYLAHTMPHVPLFASEKFK---------------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 258 hGKDKHWLIRQAktpmtnssVEfldnayrkrwrtllSVDDLVEKVVRKLEVSGELSSTYIIFTSDNG-----YHTGQFSL 332
Cdd:cd16026 206 -GRSGAGLYGDV--------VE--------------ELDWSVGRILDALKELGLEENTLVIFTSDNGpwleyGGHGGSAG 262
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2073632152 333 PMD--KRQLYEFDIRVPLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNVNETQM-DGMSFLPIMTGKGNSS 403
Cdd:cd16026 263 PLRggKGTTWEGGVRVPFIAWWPgVIPAGTVSDELASTMDLLPTLAALAGAPLPEDRViDGKDISPLLLGGSKSP 337
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-505 |
1.45e-35 |
|
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: 136.97 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTD----DldvSIGGM-MPLVKTKKLIGDA--GITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTLEgnc 114
Cdd:cd16152 1 KPNVIVFFTDqqrwD---TLGCYgQPLDLTPNLDALAeeGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNGIP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 115 sstawqktqEPE---TFSAFLQKHGtYQTFFAGKylneygskkaggvehvplgwdhWfalesnskyynytlsvngraqrH 191
Cdd:cd16152 75 ---------LPAdekTLAHYFRDAG-YETGYVGK----------------------W----------------------H 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 192 GQNYSEDYLTDvlanISIDFLENKSNRRPFFMMVSTPAPH----SPWTAAPQ-YESSFPNVKAPRDpnfnihgkdkhwLI 266
Cdd:cd16152 101 LAGYRVDALTD----FAIDYLDNRQKDKPFFLFLSYLEPHhqndRDRYVAPEgSAERFANFWVPPD------------LA 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 267 RQAKTpmtnssvefldnayrkrWRTLL--------SVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYH----TGQFslpm 334
Cdd:cd16152 165 ALPGD-----------------WAEELpdylgcceRLDENVGRIRDALKELGLYDNTIIVFTSDHGCHfrtrNAEY---- 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 335 dKRQLYEFDIRVPLLVRGPYIKPNQTSPLLIANVDLGPTILDIAGYNVNETqMDGMSFLPIMTGKGNssTWRSDVLVEye 414
Cdd:cd16152 224 -KRSCHESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEE-MQGRSLLPLVDGKVE--DWRNEVFIQ-- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 415 gegsnisdpacpllgpgVSECFpdcvcedsynnTYACVRT-----VSQAANLQYCEFDDNEVFVE--VYNLTADPFQLSN 487
Cdd:cd16152 298 -----------------ISESQ-----------VGRAIRTdrwkySVAAPDKDGWKDSGSDVYVEdyLYDLEADPYELVN 349
|
490
....*....|....*....
gi 2073632152 488 IAKSID-QEVLEKMNHRLM 505
Cdd:cd16152 350 LIGRPEyREVAAELRERLL 368
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
43-413 |
1.36e-34 |
|
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: 135.85 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDL--DVSIGGMMPLVKTKKLigDA----GITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSS 116
Cdd:cd16028 1 RNVLFITADQWraDCLSCLGHPLVKTPNL--DRlaaeGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGTPLDARH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 117 TawqktqepeTFSAFLQKHGtYQTFFAGKylNEYGSKKAGGVEHVPLGWDHWFALESnskyYNYTLSVNGRAQRHgqnyS 196
Cdd:cd16028 79 L---------TLALELRKAG-YDPALFGY--TDTSPDPRGLAPLDPRLLSYELAMPG----FDPVDRLDEYPAED----S 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 197 ED-YLTDVLanisIDFLENKSNRrPFFMMVSTPAPHSPWTAAPQYESSF--PNVKAP-RDPNFNIHGKD----KHWLIRQ 268
Cdd:cd16028 139 DTaFLTDRA----IEYLDERQDE-PWFLHLSYIRPHPPFVAPAPYHALYdpADVPPPiRAESLAAEAAQhpllAAFLERI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 269 AKTP--MTNSSVEFLDNAYRKRWRT----LLS-VDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLpMDKRQLYE 341
Cdd:cd16028 214 ESLSfsPGAANAADLDDEEVAQMRAtylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWL-WGKDGFFD 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073632152 342 FDIRVPLLVRGPYIKPNQTSPLLIAN----VDLGPTILDIAGYNVNEtQMDGMSFLPIMTGkGNSSTWRSDVLVEY 413
Cdd:cd16028 293 QAYRVPLIVRDPRREADATRGQVVDAftesVDVMPTILDWLGGEIPH-QCDGRSLLPLLAG-AQPSDWRDAVHYEY 366
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-418 |
2.87e-34 |
|
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: 133.24 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDLDV------SIGGMMPLVKTKKLIGDAGITFTNAFVAsPLCCPSRASILTGKYPHNHHVvnNTLEGNCSS 116
Cdd:cd16154 1 PNILLIIADDQGLdssaqySLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGV--LAVPDELLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 117 TawqktqePETFSAFLQKHGT---YQTFFAGKYL---NEYGSKKAGgvehvplGWDHWFAL--ESNSKYYNYTLSVNGra 188
Cdd:cd16154 78 S-------EETLLQLLIKDATtagYSSAVIGKWHlggNDNSPNNPG-------GIPYYAGIlgGGVQDYYNWNLTNNG-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 189 qrhGQNYSEDYLTDVLANISIDFLENKSNrrPFFMMVSTPAPHSPWTAAPQYESSFPNVKAPRDpnfnihgkdkhwlIRQ 268
Cdd:cd16154 142 ---QTTNSTEYATTKLTNLAIDWIDQQTK--PWFLWLAYNAPHTPFHLPPAELHSRSLLGDSAD-------------IEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 269 AKTPMTNSSVEFLDNAYRkrwRTLLSVDDlvekvvrklevsGELSSTYIIFTSDNGyhT-GQ-----FSLPMDKRQLYEF 342
Cdd:cd16154 204 NPRPYYLAAIEAMDTEIG---RLLASIDE------------EERENTIIIFIGDNG--TpGQvvdlpYTRNHAKGSLYEG 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2073632152 343 DIRVPLLVRGPYI-KPNQTSPLLIANVDLGPTILDIAGYNVNEtQMDGMSFLPIMTGkGNSSTwRSDVLVEYEGEGS 418
Cdd:cd16154 267 GINVPLIVSGAGVeRANERESALVNATDLYATIAELAGVDAAE-IHDSVSFKPLLSD-VNAST-RQYNYTEYESPTT 340
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
43-418 |
3.71e-34 |
|
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: 131.93 E-value: 3.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDLDVSIGGMM--PLVKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSsta 118
Cdd:cd16032 1 PNILLIMADQLTAAALPAYgnTVVKTPNLdrLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEFPAD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 119 wqktqEPeTFSAFLQKHGtYQTFFAGKYlneygskkaggvehvplgwdHWFalesnskyynytlsvnGRAQRHGQNYSED 198
Cdd:cd16032 78 -----IP-TFAHYLRAAG-YRTALSGKM--------------------HFV----------------GPDQLHGFDYDEE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 199 -------YLTDvlanisidfLENKSNRRPFFMMVSTPAPHSPWTAAPQYEssfpnvkaprdpnfnihgkdkHWLIRQAkt 271
Cdd:cd16032 115 vafkavqKLYD---------LARGEDGRPFFLTVSFTHPHDPYVIPQEYW---------------------DLYVRRA-- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 272 pmtnssvefldnayRKRWRTLLS-VDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLPMdKRQLYEFDIRVPLLV 350
Cdd:cd16032 163 --------------RRAYYGMVSyVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWY-KMSFFEGSARVPLII 227
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 351 RGPYIKPNQTSPLLIANVDLGPTILDIAGYNVNE--TQMDGMSFLPIMTGKGnsSTWRSDVLVEYEGEGS 418
Cdd:cd16032 228 SAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPhvPPLDGRSLLPLLEGGD--SGGEDEVISEYLAEGA 295
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
42-399 |
6.76e-33 |
|
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: 129.87 E-value: 6.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTDDL---DVSI-GGmmpLVKTKKL--IGDAGITFTNaFVASPLCCPSRASILTGkypHNHHVVNNtleGNCS 115
Cdd:cd16025 2 RPNILLILADDLgfsDLGCfGG---EIPTPNLdaLAAEGLRFTN-FHTTALCSPTRAALLTG---RNHHQVGM---GTMA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 116 STAWQK-------TQEPETFSAFLQKHGtYQTFFAGKylneygskkaggvehvplgWdHwfalesnskyynytlsvNGra 188
Cdd:cd16025 72 ELATGKpgyegylPDSAATIAEVLKDAG-YHTYMSGK-------------------W-H-----------------LG-- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 189 qrhGQNYsedYLTDVLANISIDFL-ENKSNRRPFFMMVSTPAPHSPWTAAPQY----------------ESSF------- 244
Cdd:cd16025 112 ---PDDY---YSTDDLTDKAIEYIdEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkykgkydagwdalrEERLerqkelg 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 245 ---PNVK-APRDPNfnihgkDKHWlirqaktpmtNSsvefLDNAYRKRWRTLLSV--------DDLVEKVVRKLEVSGEL 312
Cdd:cd16025 186 lipADTKlTPRPPG------VPAW----------DS----LSPEEKKLEARRMEVyaamvehmDQQIGRLIDYLKELGEL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 313 SSTYIIFTSDNG--YHTG--QFS---LPMDKRQLYEFDIRVPLLVRGP-YIKPN---QTSPLLIanVDLGPTILDIAG-- 379
Cdd:cd16025 246 DNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPkGIKAKggiRHQFAHV--IDIAPTILELAGve 323
|
410 420
....*....|....*....|....*
gi 2073632152 380 -----YNVNETQMDGMSFLPIMTGK 399
Cdd:cd16025 324 ypktvNGVPQLPLDGVSLLPTLDGA 348
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-394 |
7.79e-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: 126.51 E-value: 7.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDL--D-VSIGGMmPLVKTKKLigDA----GITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTLEgncs 115
Cdd:cd16148 1 MNVILIVIDSLraDhLGCYGY-DRVTTPNL--DRlaaeGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGPLE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 116 stawqktQEPETFSAFLQKHGtYQTffagkylneygskkAGGVEHVPLGWDHWFAlesnsKYYNYTlsVNGRAQRHGQNY 195
Cdd:cd16148 74 -------PDDPTLAEILRKAG-YYT--------------AAVSSNPHLFGGPGFD-----RGFDTF--EDFRGQEGDPGE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 196 SEDYLTDVLANISIDFLENKSNRRPFFMMVSTPAPHSPWtaapQYESSfpnvkaprdpnfnihgkdkhwlIRQaktpmtn 275
Cdd:cd16148 125 EGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPHEPY----LYDAE----------------------VRY------- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 276 ssvefldnayrkrwrtllsVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLpMDKRQ--LYEFDIRVPLLVRGP 353
Cdd:cd16148 172 -------------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGL-YWGHGsnLYDEQLHVPLIIRWP 231
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2073632152 354 YIKPNQTSPLLIANVDLGPTILDIAGYNVNETqMDGMSFLP 394
Cdd:cd16148 232 GKEPGKRVDALVSHIDIAPTLLDLLGVEPPDY-SDGRSLLP 271
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-394 |
5.44e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 123.89 E-value: 5.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDLDV-SIGGMMPL-VKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSST- 117
Cdd:cd16149 1 PNILFILTDDQGPwALGCYGNSeAVTPNLdrLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 118 ---AWQKTQepETFSAFLQKHGtYQTFFAGKYlneygskkaggveHvpLGWDHwfalesnskyynytlsvngraqrhgqn 194
Cdd:cd16149 81 kpeGYLEGQ--TTLPEVLQDAG-YRCGLSGKW-------------H--LGDDA--------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 195 ysedyltdvlanisIDFLE-NKSNRRPFFMMVSTPAPHSPWtaapQYESSfpnvkaprdpnfnihgkdkhwlirqaktpm 273
Cdd:cd16149 116 --------------ADFLRrRAEAEKPFFLSVNYTAPHSPW----GYFAA------------------------------ 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 274 tnssvefldnayrkrwrtLLSVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSL--------PMDkrqLYEFDIR 345
Cdd:cd16149 148 ------------------VTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIwgkgngtfPLN---MYDNSVK 206
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2073632152 346 VPLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNVNETQ-MDGMSFLP 394
Cdd:cd16149 207 VPFIIRWPgVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPrLPGRSFAD 257
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
43-413 |
3.34e-31 |
|
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: 124.97 E-value: 3.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDL---DVSIGGMmPLVKT---KKLIGDaGITFTNAFVAsPLCCPSRASILTGKYPHNH---HVVNNTLEGN 113
Cdd:cd16029 1 PHIVFILADDLgwnDVGFHGS-DQIKTpnlDALAAD-GVILNNYYVQ-PICTPSRAALMTGRYPIHTgmqHGVILAGEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 114 CSSTawqktqEPETFSAFLQKHGtYQTFFAGKYLNEYGSKkaggvEHVPL--GWDHWFALESNSK-YYNYTLS---VNGR 187
Cdd:cd16029 78 GLPL------NETLLPQYLKELG-YATHLVGKWHLGFYTW-----EYTPTnrGFDSFYGYYGGAEdYYTHTSGganDYGN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 188 AQRHGQN-----YSEDYLTDVLANISIDFLENKSNRRPFFMMVSTPAPHSPWTAAPQYessfpnvkAPRDPNFNIHGKDK 262
Cdd:cd16029 146 DDLRDNEepawdYNGTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEY--------ADPYEDKFAHIKDE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 263 HwliRQAKTPMtnssvefldnayrkrwrtLLSVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSL----PM--DK 336
Cdd:cd16029 218 D---RRTYAAM------------------VSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGgsnyPLrgGK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 337 RQLYEFDIRVPLLVRGPYIKPN--QTSPLLIANVDLGPTILDIAGYNVNET-QMDGMSFLPIMTGkGNSSTwRSDVLVEY 413
Cdd:cd16029 277 NTLWEGGVRVPAFVWSPLLPPKrgTVSDGLMHVTDWLPTLLSLAGGDPDDLpPLDGVDQWDALSG-GAPSP-RTEILLNI 354
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
42-406 |
1.70e-29 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 121.70 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTDDLDVSIGGMM--PLVKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVnntleGNCSST 117
Cdd:PRK13759 6 KPNIILIMVDQMRGDCLGCNgnKAVETPNLdmLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV-----GYGDVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 118 AWQKTQE-PETFSaflqKHGtYQTFFAGKyLNEYGSKKAGGVEHVPL--GWDH------------------WFALESNSK 176
Cdd:PRK13759 81 PWNYKNTlPQEFR----DAG-YYTQCIGK-MHVFPQRNLLGFHNVLLhdGYLHsgrnedksqfdfvsdylaWLREKAPGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 177 YYNYT------LSVNGRAQRHGQNYSEDYLTdvlANISIDFLENKSNRRPFFMMVSTPAPHSPWTAAPQYESSFPNVKAP 250
Cdd:PRK13759 155 DPDLTdigwdcNSWVARPWDLEERLHPTNWV---GSESIEFLRRRDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADIP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 251 RDPNFNIHGKDKHWLIRQAKT-PMTNSSVEFLDNAYRKRWRTLLSVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQ 329
Cdd:PRK13759 232 DPHIGDWEYAEDQDPEGGSIDaLRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 330 FSLpMDKRQLYEFDIRVPLLVRGP--YIKPNQTSplLIANV----DLGPTILDIAGYNVNETqMDGMSFLPIMtgKGNSS 403
Cdd:PRK13759 312 HYL-FRKGYPYEGSAHIPFIIYDPggLLAGNRGT--VIDQVvelrDIMPTLLDLAGGTIPDD-VDGRSLKNLI--FGQYE 385
|
...
gi 2073632152 404 TWR 406
Cdd:PRK13759 386 GWR 388
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
43-502 |
2.01e-29 |
|
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: 120.95 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTD----DLDVSIGGmmPLVKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYPHnhhvvNNTLEGNCSS 116
Cdd:cd16156 1 KQFIFIMTDtqrwDMVGCYGN--KAMKTPNLdrLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPH-----TNGSWTNCMA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 117 TAwqktQEPETFSAFLQKHGtYQTFFAGKYLNEYGSKKAGGVehVPLGWD--HWFALESnskYYNYTLSVNGRAQRHGQN 194
Cdd:cd16156 74 LG----DNVKTIGQRLSDNG-IHTAYIGKWHLDGGDYFGNGI--CPQGWDpdYWYDMRN---YLDELTEEERRKSRRGLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 195 --YSEDYLTDV-----LANISIDFLENKSNrRPFFMMVSTPAPHSPWTAAPQYESSFPNVKAPRDPNF--NIHGKDKH-- 263
Cdd:cd16156 144 slEAEGIKEEFtyghrCTNRALDFIEKHKD-EDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAydDLENKPLHqr 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 264 -W---LIRQAKTPMTNSSVEFLD-NAYrkrwrtllsVDDLVEKVVRKLEvsGELSSTYIIFTSDNGYHTGQFSLPMDKRQ 338
Cdd:cd16156 223 lWagaKPHEDGDKGTIKHPLYFGcNSF---------VDYEIGRVLDAAD--EIAEDAWVIYTSDHGDMLGAHKLWAKGPA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 339 LYEFDIRVPLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNVNEtQMDGMSFLPIMTGKGNSStwRSDVLVE---YE 414
Cdd:cd16156 292 VYDEITNIPLIIRGKgGEKAGTVTDTPVSHIDLAPTILDYAGIPQPK-VLEGESILATIEDPEIPE--NRGVFVEfgrYE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 415 gegsnisdpacpllgpgvsecfpdcVCEDSYNNtYACVRtvsqaanlqyCEFDDNEVFV-------EVYNLTADPFQLSN 487
Cdd:cd16156 369 -------------------------VDHDGFGG-FQPVR----------CVVDGRYKLVinllstdELYDLEKDPYEMHN 412
|
490 500
....*....|....*....|....
gi 2073632152 488 ---------IAKSIDQEVLEKMNH 502
Cdd:cd16156 413 liddpdyadVRDQLHDELLDYMNE 436
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-414 |
6.20e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 111.15 E-value: 6.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDD-------LDVSIGGMMPlvkTKKLIGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTlegncs 115
Cdd:cd16035 1 PNILLILTDQerypppwPAGWAALNLP---ARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 116 STAWQKTQEPE--TFSAFLQKHGtYQTFFAGKylneygskkaggvehvplgWdHwfalesnskyynytLSvngRAQRHGQ 193
Cdd:cd16035 72 GSPMQPLLSPDvpTLGHMLRAAG-YYTAYKGK-------------------W-H--------------LS---GAAGGGY 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 194 NYSEDYltdvlANISIDFLENK----SNRRPFFMMVSTPAPH---SPWTAAPQYEssfpnvkapRDPNFnihgkdKHWLI 266
Cdd:cd16035 114 KRDPGI-----AAQAVEWLRERgaknADGKPWFLVVSLVNPHdimFPPDDEERWR---------RFRNF------YYNLI 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 267 RQaktpmtnssvefldnayrkrwrtllsVDDLVEKVVRKLEVSGELSSTYIIFTSDNG----YHTGqfslpmdKRQ---L 339
Cdd:cd16035 174 RD--------------------------VDRQIGRVLDALDASGLADNTIVVFTSDHGemggAHGL-------RGKgfnA 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 340 YEFDIRVPLLVRGPYIKPN-QTSPLLIANVDLGPTILDIAGYNVNETQMD-----GMSFLPIMTGKGNSSTwRSDVLVEY 413
Cdd:cd16035 221 YEEALHVPLIISHPDLFGTgQTTDALTSHIDLLPTLLGLAGVDAEARATEapplpGRDLSPLLTDADADAV-RDGILFTY 299
|
.
gi 2073632152 414 E 414
Cdd:cd16035 300 D 300
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
43-418 |
8.86e-26 |
|
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: 108.77 E-value: 8.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDL---DVSI--GGMMPLVKTKKL--IGDAGITFTNaFVASPLCCPSRASILTGKYPhNHHvvnntlegNCS 115
Cdd:cd16142 1 PNILVILGDDIgwgDLGCygGGIGRGAPTPNIdrLAKEGLRFTS-FYVEPSCTPGRAAFITGRHP-IRT--------GLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 116 STAWQKTQ------EPeTFSAFLQKHGtYQTFFAGKylNEYGSKKaggvEHVPL--GWDHWFAlesnskYYNYTLsvngr 187
Cdd:cd16142 71 TVGLPGSPgglppwEP-TLAELLKDAG-YATAQFGK--WHLGDED----GRLPTdhGFDEFYG------NLYHTI----- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 188 aqrhgqnysEDYLTDVlaniSIDFL-ENKSNRRPFFMMVSTPAPHSPWTAAPQYEssfpnvkaprdpnfnihGKDKHWli 266
Cdd:cd16142 132 ---------DEEIVDK----AIDFIkRNAKADKPFFLYVNFTKMHFPTLPSPEFE-----------------GKSSGK-- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 267 rqaktpmtnssVEFLDnayrkrwrTLLSVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHtgQFSLPM--------DKRQ 338
Cdd:cd16142 180 -----------GKYAD--------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGPE--QDVWPDggytpfrgEKGT 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 339 LYEFDIRVPLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAG-------YNVNETQMDGMSFLPIMTGKGNSStwRSDVL 410
Cdd:cd16142 239 TWEGGVRVPAIVRWPgKIKPGRVSNEIVSHLDWFPTLAALAGapdpkdkLLGKDRHIDGVDQSPFLLGKSEKS--RRSEF 316
|
....*...
gi 2073632152 411 VeYEGEGS 418
Cdd:cd16142 317 F-YFGEGE 323
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
42-414 |
4.16e-24 |
|
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: 105.20 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTDDL---DVSIGGMmPlVKTKKLIGD---AGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNntleGNCS 115
Cdd:cd16160 1 KPNIVLFFADDMgygDLASYGH-P-TQERGPIDDmaaEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG----GTRV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 116 STAWQKTQEP--ETFSAFLQKHGTYQTFFAGKY---LNEYgsKKAGGVeHVPL--GWD----------HWFAleSNSK-- 176
Cdd:cd16160 75 FLPWDIGGLPktEVTMAEALKEAGYTTGMVGKWhlgINEN--NHSDGA-HLPShhGFDfvgtnlpftnSWAC--DDTGrh 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 177 -----------YYNYTLSvngraqrhGQNYSEDYLTDVLANISIDFLENKSNrRPFFMMVSTPAPHSPWTAAPQYessfp 245
Cdd:cd16160 150 vdfpdrsacflYYNDTIV--------EQPIQHEHLTETLVGDAKSFIEDNQE-NPFFLYFSFPQTHTPLFASKRF----- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 246 nvkaprdpnfnihgkdkhwlirqaktpmTNSSV--EFLDNAYRKRWRtllsvddlVEKVVRKLEVSGELSSTYIIFTSDN 323
Cdd:cd16160 216 ----------------------------KGKSKrgRYGDNINEMSWA--------VGEVLDTLVDTGLDQNTLVFFLSDH 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 324 GYH-----TGQFSLPMD--KRQLYEFDIRVPLLVRGPYIKPNQTSPLLIANVDLGPTILDIAGYNVNE-TQMDGMSFLPI 395
Cdd:cd16160 260 GPHveyclEGGSTGGLKggKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTdRIYDGLSITDL 339
|
410
....*....|....*....
gi 2073632152 396 MtgKGNSSTWRSDVLVEYE 414
Cdd:cd16160 340 L--LGEADSPHDDILYYCC 356
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-391 |
8.98e-22 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 95.52 E-value: 8.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTDDLDV----SIGGMMPLVKTKKLIG------DA----GITFTNAFVASPLCCPSRASILTGKYPHNHHVVN 107
Cdd:cd16153 1 KPNILWIITDDQRVdslsCYNNAHTGKSESRLGYvespniDAlaaeGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 108 NtlEGncsstAWQKTQE-PETFSAFLQKHGtYQTFFAGKylneygskkaggvehvplgwdhwfalesnSKYYNYtlsvng 186
Cdd:cd16153 81 F--EA-----AHPALDHgLPTFPEVLKKAG-YQTASFGK-----------------------------SHLEAF------ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 187 raQRHGQNYSEDYLTDVLANIsidflENKSNRRPFFMMVSTPAPHSPWTAAPQYESSFpnvkaprdpnfnihgkDKHWLI 266
Cdd:cd16153 118 --QRYLKNANQSYKSFWGKIA-----KGADSDKPFFVRLSFLQPHTPVLPPKEFRDRF----------------DYYAFC 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 267 rqaktpmtnssvefldnAYrkrwrtllsVDDLVEKVVRKLEVSGELS---STYIIFTSDNGYHTGQFSLpMDKRQLYEFD 343
Cdd:cd16153 175 -----------------AY---------GDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQGI-LAKFTFWPQS 227
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2073632152 344 IRVPLLVRGPYIKP---NQTSPLLIANVDLGPTILDIAGYNVNE-TQMDGMS 391
Cdd:cd16153 228 HRVPLIVVSSDKLKapaGKVRHDFVEFVDLAPTLLAAAGVDVDApDYLDGRD 279
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
43-421 |
5.43e-21 |
|
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: 94.92 E-value: 5.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDLDVSIGGMmPLVKTKKL-----IGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSST 117
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFR-PGNQVVDLpyinfMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNYKGLDPNYP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 118 AWQKTqepetfsafLQKHGtYQTFFAGKYlnEYGSKkaggvehvplgwDHWFA--LESNSKYYNYTLSVNGR-------A 188
Cdd:cd16171 80 TWMDR---------LEKHG-YHTQKYGKL--DYTSG------------HHSVSnrVEAWTRDVPFLLRQEGRptvnlvgD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 189 QRHGQNYSEDYLTDVLANISIDFlENKSNRRPFFMMVSTPAPHsPWTAapqyESSFPNVKAPRDpnfnihgkdkhwlIRQ 268
Cdd:cd16171 136 RSTVRVMLKDWQNTDKAVHWIRK-EAPNLTQPFALYLGLNLPH-PYPS----PSMGENFGSIRN-------------IRA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 269 AKTPMTNSSvefldnayrkrwrtllsvDDLVEKVVRKLEVSGELSSTYIIFTSDNGyhtgqfSLPMDKRQ-----LYEFD 343
Cdd:cd16171 197 FYYAMCAET------------------DAMLGEIISALKDTGLLDKTYVFFTSDHG------ELAMEHRQfykmsMYEGS 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 344 IRVPLLVRGPYIKPNQTSPLLIANVDLGPTILDIAGynVNETQ-MDGMSFLPIMTGKGNSSTWRSD-----VLVEYEGEG 417
Cdd:cd16171 253 SHVPLLIMGPGIKAGQQVSDVVSLVDIYPTMLDIAG--VPQPQnLSGYSLLPLLSESSIKESPSRVphpdwVLSEFHGCN 330
|
....
gi 2073632152 418 SNIS 421
Cdd:cd16171 331 VNAS 334
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
42-398 |
2.93e-20 |
|
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: 92.92 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTDDL---DVSIGGMMPLVKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSS 116
Cdd:cd16161 1 KPNFLLLFADDLgwgDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 117 TAWQKTQEPETfsafLQKHGtYQTFFAGKYlnEYGSKKAggveHVPlgwdhwfalesNSKYYNYTLsvngraqrhGQNYS 196
Cdd:cd16161 81 LPLNETTLAEV----LRQAG-YATGMIGKW--HLGQREA----YLP-----------NSRGFDYYF---------GIPFS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 197 ED-YLTDVLANISIDFLENKSNR-RPFFMMVSTPAPHSPWTAAPQYESSfpnvkaprdpnfnihgkdkhwlirqaktpmT 274
Cdd:cd16161 130 HDsSLADRYAQFATDFIQRASAKdRPFFLYAALAHVHVPLANLPRFQSP------------------------------T 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 275 NSSVEFLDnayrkrwrTLLSVDDLVEKVVRKLEVSGELSSTYIIFTSDNG-------YHTGQFSLPMDKRQ--------L 339
Cdd:cd16161 180 SGRGPYGD--------ALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkceLAVGPGTGDWQGNLggsvakasT 251
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073632152 340 YEFDIRVPLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNVNETQM-DGMSFLPIMTG 398
Cdd:cd16161 252 WEGGHREPAIVYWPgRIPANSTSAALVSTLDIFPTVVALAGASLPPGRIyDGKDLSPVLFG 312
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
42-410 |
8.75e-20 |
|
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: 92.14 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTDDL---DVSIGGMmPLVKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYP-------HNHHVVNNT 109
Cdd:cd16157 1 KPNIILMLMDDMgwgDLGVFGE-PSRETPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPirngfytTNAHARNAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 110 LEGNCSSTAwqkTQEPETFSAFLQKHGtYQTFFAGKYlnEYGSKKaggvEHVPL--GWDHWFALES-------NSKYYNY 180
Cdd:cd16157 80 TPQNIVGGI---PDSEILLPELLKKAG-YRNKIVGKW--HLGHRP----QYHPLkhGFDEWFGAPNchfgpydNKAYPNI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 181 TLSVN----GRAQRH---GQNYSEDYLTDVLANISIDFLENKSNR-RPFFMMVSTPAPHSPWTAAPQYEssfpnvkaprd 252
Cdd:cd16157 150 PVYRDwemiGRYYEEfkiDKKTGESNLTQIYLQEALEFIEKQHDAqKPFFLYWAPDATHAPVYASKPFL----------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 253 pnfnihGKDKHWLIRQAktpmtnssvefldnayrkrwrtLLSVDDLVEKVVRKLEVSGELSSTYIIFTSDNGYHTgqFSL 332
Cdd:cd16157 219 ------GTSQRGLYGDA----------------------VMELDSSVGKILESLKSLGIENNTFVFFSSDNGAAL--ISA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 333 PMD----------KRQLYEFDIRVPLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNV-NETQMDGMSFLP-IMTGK 399
Cdd:cd16157 269 PEQggsngpflcgKQTTFEGGMREPAIAWWPgHIKPGQVSHQLGSLMDLFTTSLALAGLPIpSDRAIDGIDLLPvLLNGK 348
|
410
....*....|....
gi 2073632152 400 GNSST---WRSDVL 410
Cdd:cd16157 349 EKDRPifyYRGDEL 362
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
43-378 |
1.05e-18 |
|
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: 85.55 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDL-DVSIGGMMPLVKTK---KLIGDAGITFtNAFVASPLC--CPSRASILTGKYPHNHHVVnntleGNCSS 116
Cdd:cd00016 1 KHVVLIVLDGLgADDLGKAGNPAPTTpnlKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYT-----GNGSA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 117 TawqktqePETFSAFLQKHGTYQTFFagKYLNEYGskkaggvehvpLGWDhWFALEsnskyynytlsvngraqrhgqnys 196
Cdd:cd00016 75 D-------PELPSRAAGKDEDGPTIP--ELLKQAG-----------YRTG-VIGLL------------------------ 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 197 edyltdvlanisiDFLENKSNRRPFFMMVSTPAPHSPWTA-APQYESSFPNVKAprdpnfnihgkdkhwlirqaktpmtn 275
Cdd:cd00016 110 -------------KAIDETSKEKPFVLFLHFDGPDGPGHAyGPNTPEYYDAVEE-------------------------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 276 ssvefldnayrkrwrtllsVDDLVEKVVRKLEVSGELSSTYIIFTSDNG---YHTGQFSLPMDKRQLYEFDIRVPLLVRG 352
Cdd:cd00016 151 -------------------IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYG 211
|
330 340
....*....|....*....|....*.
gi 2073632152 353 PYIKPNQTSPLLIANVDLGPTILDIA 378
Cdd:cd00016 212 PGVKKGGVKHELISQYDIAPTLADLL 237
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
43-402 |
1.68e-16 |
|
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: 82.11 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLILTDDL---DVSIGGMmPLVKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYPHNHHVVNNTLEGNCSST 117
Cdd:cd16158 2 PNIVLLFADDLgygDLGCYGH-PSSSTPNLdrLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 118 AwqkTQEPETFSAFLQKHGtYQTFFAGKYlnEYGSKKAGGVEHVPLGWDHWFA--------------------------- 170
Cdd:cd16158 81 L---PLNETTIAEVLKTVG-YQTAMVGKW--HLGVGLNGTYLPTHQGFDHYLGipyshdqgpcqnltcfppnipcfggcd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 171 -------LESNSKYYNYTLSVNGRAQRHgQNYSEDYLTDvlanisidfleNKSNRRPFFMMVSTPAPHSPWTAAPQYESs 243
Cdd:cd16158 155 qgevpcpLFYNESIVQQPVDLLTLEERY-AKFAKDFIAD-----------NAKEGKPFFLYYASHHTHYPQFAGQKFAG- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 244 fpnvKAPRDPnfnihgkdkhwlirqaktpmtnssveFLDnayrkrwrTLLSVDDLVEKVVRKLEVSGELSSTYIIFTSDN 323
Cdd:cd16158 222 ----RSSRGP--------------------------FGD--------ALAELDGSVGELLQTLKENGIDNNTLVFFTSDN 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 324 GYHTGQFS-------LPMDKRQLYEFDIRVPLLVRGP-YIKPNQTSPlLIANVDLGPTILDIAGYNVNETQMDGMSFLPI 395
Cdd:cd16158 264 GPSTMRKSrggnaglLKCGKGTTYEGGVREPAIAYWPgRIKPGVTHE-LASTLDILPTIAKLAGAPLPNVTLDGVDMSPI 342
|
....*..
gi 2073632152 396 MTGKGNS 402
Cdd:cd16158 343 LFEQGKS 349
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
42-403 |
3.02e-15 |
|
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: 78.48 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 42 RPNIVLILTDDL---DVSIGGMMPLvKTKKL--IGDAGITFTNAFVASPLCCPSRASILTGKYP-------HNHHVVNNt 109
Cdd:cd16159 1 KPNIVLFMADDLgigDVGCFGNDTI-RTPNIdrLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPirsgmasSHGMRVIL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 110 legNCSSTAWQKTQEpETFSAFLQKHGtYQTFFAGKY-------------------------------LNEYGSKKAGGV 158
Cdd:cd16159 79 ---FTASSGGLPPNE-TTFAEVLKQQG-YSTALIGKWhlglhcesrndfchhplnhgfdyfyglpltnLKDCGDGSNGEY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 159 EHVPLGWDH----------------------------------------WFALESNSKYYNYTLSVNGRAQRhgQNYSED 198
Cdd:cd16159 154 DLSFDPLFPlltafvlitaltiflllylgavskrffvfllilsllfislFFLLLITNRYFNCILMRNHEVVE--QPMSLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 199 YLTDVLANISIDFLENKSnRRPFFMMVSTPAPHSPWTAAPQYEssfpnvkaprdpnfnihGKDKHWLIRQAktpmtnssV 278
Cdd:cd16159 232 NLTQRLTKEAISFLERNK-ERPFLLVMSFLHVHTALFTSKKFK-----------------GRSKHGRYGDN--------V 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 279 EFLDnayrkrWRtllsvddlVEKVVRKLEVSGELSSTYIIFTSDNGYHTGQFSLPMD------------KRQLYEFDIRV 346
Cdd:cd16159 286 EEMD------WS--------VGQILDALDELGLKDNTFVYFTSDNGGHLEEISVGGEygggnggiyggkKMGGWEGGIRV 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2073632152 347 PLLVRGP-YIKPNQTSPLLIANVDLGPTILDIAGYNV-NETQMDGMSFLPIMTGKGNSS 403
Cdd:cd16159 352 PTIVRWPgVIPPGSVIDEPTSLMDIFPTVAALAGAPLpSDRIIDGRDLMPLLTGQEKRS 410
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
88-379 |
5.06e-09 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 57.21 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 88 CPSRASILTGKYPHNHHVVNNTL--------EGNCSSTAWQKTQEPETFSAFLQKHGtyqtffagkylneygsKKAGgve 159
Cdd:cd16018 47 FPNHYSIVTGLYPESHGIVGNYFydpktneeFSDSDWVWDPWWIGGEPIWVTAEKAG----------------LKTA--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 160 hvplgwdHWFALESNSKYYNYTLSVNGRaQRHGQNYSEDYLTDVLANISIDFLENksnRRPFFMMVSTPAP----Hspwt 235
Cdd:cd16018 108 -------SYFWPGSEVAIIGYNPTPIPL-GGYWQPYNDSFPFEERVDTILEWLDL---ERPDLILLYFEEPdsagH---- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 236 aapQYessfpnvkAPRDPNFNihgkdkhwlirqaktpmtnssvefldNAYRKrwrtllsVDDLVEKVVRKLEVSGELSST 315
Cdd:cd16018 173 ---KY--------GPDSPEVN--------------------------EALKR-------VDRRLGYLIEALKERGLLDDT 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073632152 316 YIIFTSDNGYHT----GQFSlpmdkrqlYEFDIRVPLLVRGPYIKPNQTSPlLIANVDLGPTILDIAG 379
Cdd:cd16018 209 NIIVVSDHGMTDvgthGYDN--------ELPDMRAIFIARGPAFKKGKKLG-PFRNVDIYPLMCNLLG 267
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
43-379 |
3.79e-08 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 55.00 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 43 PNIVLIL-----TDDLDVSIGGMMPLVKTKKLIGDaGITFTNAFVASPLCCPSRA--SILTGKYPhnhhvvnntLEGNCS 115
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKE-GLYFGNFYSPGFGGGTANGefEVLTGLPP---------LPLGSG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 116 STAWQKTQEPETFSAFLQKHGtYQTFFA-GKYLNEYGSKKAggveHVPLGWDHWFALEsnskYYNYTlsvngraqrhGQN 194
Cdd:cd16015 71 SYTLYKLNPLPSLPSILKEQG-YETIFIhGGDASFYNRDSV----YPNLGFDEFYDLE----DFPDD----------EKE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 195 YSEDYLTD-VLANISIDFLENKSNRrPFFMMVSTPAPHSPWTaAPQYESSFPNVKAPRDPNFNihgkdkhwlirqaktpm 273
Cdd:cd16015 132 TNGWGVSDeSLFDQALEELEELKKK-PFFIFLVTMSNHGPYD-LPEEKKDEPLKVEEDKTELE----------------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 274 tnssvEFLdNAYRKrwrtllsVDDLVEKVVRKLEVSGELSSTYIIFTSDngyHTGQFSLPMDKRQLYEFDI-RVPLLVRG 352
Cdd:cd16015 193 -----NYL-NAIHY-------TDKALGEFIEKLKKSGLYENTIIVIYGD---HLPSLGSDYDETDEDPLDLyRTPLLIYS 256
|
330 340
....*....|....*....|....*..
gi 2073632152 353 PYIKPNQTSPLLIANVDLGPTILDIAG 379
Cdd:cd16015 257 PGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
41-393 |
1.55e-06 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 50.81 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 41 PRPNIVLIL-----TDDLDVSIGGMMPLVKTKKLIGDaGITFTNAFVASPLCCPSRASILTGKYPhnhhvvnnTLEGNCS 115
Cdd:COG1368 233 KKPNVVVILlesfsDFFIGALGNGKDVTPFLDSLAKE-SLYFGNFYSQGGRTSRGEFAVLTGLPP--------LPGGSPY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 116 STAWQKTQEpeTFSAFLQKHGtYQTFFagkylneygskkaggvehvplgwdhwfalesnskYYNYTLSVNGRAQRHGQN- 194
Cdd:COG1368 304 KRPGQNNFP--SLPSILKKQG-YETSF----------------------------------FHGGDGSFWNRDSFYKNLg 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 195 ----YSEDYLTDVLANI-----------SIDFLENKSnrRPFFMMVSTPAPHSPWTAaPQYESSFPnvkaprdpnfnihg 259
Cdd:COG1368 347 fdefYDREDFDDPFDGGwgvsdedlfdkALEELEKLK--KPFFAFLITLSNHGPYTL-PEEDKKIP-------------- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073632152 260 kdkhwlirqaktpmtnssvEFLDNAYRKRWRTLLSVDDLVEKVVRKLEVSGELSSTYIIFTSDngyHTGqfslPMDKRQL 339
Cdd:COG1368 410 -------------------DYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGD---HGP----RSPGKTD 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2073632152 340 YEFDI---RVPLLVRGPYIKPNQTSPLLIANVDLGPTILDIAGYNVNETQMDGMSFL 393
Cdd:COG1368 464 YENPLeryRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLL 520
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
88-109 |
3.74e-03 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 39.71 E-value: 3.74e-03
|
| |
