|
Name |
Accession |
Description |
Interval |
E-value |
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
2-465 |
1.85e-97 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 299.10 E-value: 1.85e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRYDVL---GKGF--TPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLINPWEPADAVy 76
Cdd:COG3119 23 RPNILFILADDLGYGDLgcyGNPLikTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGGL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 77 gdvRPEFGSLYTMM-ERDWDSIHSGKQHLfttggkledrvdsdtrwfsteksykeflkehrvampgggkfrtkvpemvdg 155
Cdd:COG3119 102 ---PPDEPTLAELLkEAGYRTALFGKWHL--------------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 156 katrvssysnaetgryepgeqyYFDSYFTEMALEGLRRR-DTTKPLLLNAMFLAPHPPLQIPDPWYRAVGAEDFALPENi 234
Cdd:COG3119 128 ----------------------YLTDLLTDKAIDFLERQaDKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPLPPN- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 235 gvYYPRqsplqmynltgivgtRYGREHWKEAWRVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGEMLGSHGL- 313
Cdd:COG3119 185 --LAPR---------------DLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLr 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 314 FQKMCMYEESARVPLFMKFPKGFTPsDKSYGQVVSHIDVLPTLCDYLQMDSGNEMDGTSLMPLLRGESrAEDRNSAYIQY 393
Cdd:COG3119 248 GGKGTLYEGGIRVPLIVRWPGKIKA-GSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTGEK-AEWRDYLYWEY 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2629630740 394 DGNGSrsnfQRCMIWGRWKLIVDlFKDETFYELYDLEEDVQETSNLMfdGKHDEIAEEMANRLAAHSRETGD 465
Cdd:COG3119 326 PRGGG----NRAIRTGRWKLIRY-YDDDGPWELYDLKNDPGETNNLA--ADYPEVVAELRALLEAWLKELGD 390
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-465 |
8.14e-88 |
|
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: 274.87 E-value: 8.14e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLGKG-----FTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLINPwepADAVYG 77
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYgnpivKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNV---ENAGAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 78 DVRPEFGS-LYT--MMERDWDSIHSGKQHLfttggkledrvdsdtrwfSTEKSYKEFlkehrvampgggkfrtkvpeMVD 154
Cdd:cd16033 78 SRGLPPGVeTFSedLREAGYRNGYVGKWHV------------------GPEETPLDY--------------------GFD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 155 GkatrvssYSNAETgryepgeqyyFDSYFT-EMALEGLRR-RDTTKPLLLNAMFLAPHPPLQIPDPWYRAVGAEDFALPE 232
Cdd:cd16033 120 E-------YLPVET----------TIEYFLaDRAIEMLEElAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPE 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 233 NIGVYYPRQSPLQ-MYNLTGIVGTrYGREHWKEAWRVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGEMLGSH 311
Cdd:cd16033 183 SFADDFEDKPYIYrRERKRWGVDT-EDEEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAH 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 312 GLFQK-MCMYEESARVPLFMKFPkGFTPSDKSYGQVVSHIDVLPTLCDYLQMDSGNEMDGTSLMPLLRGESRAEDRNSAY 390
Cdd:cd16033 262 RLWDKgPFMYEETYRIPLIIKWP-GVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPEDWRDEVV 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2629630740 391 IQYDGNGSRSnFQRcMIW-GRWKLIvdlFKDETFYELYDLEEDVQETSNLMFDGKHDEIAEEMANRLAAHSRETGD 465
Cdd:cd16033 341 TEYNGHEFYL-PQR-MVRtDRYKYV---FNGFDIDELYDLESDPYELNNLIDDPEYEEILREMRTRLYEWMEETGD 411
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
2-439 |
1.10e-76 |
|
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: 245.56 E-value: 1.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRYDVLG-KG----FTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLIN--PWEPADA 74
Cdd:cd16034 1 KPNILFIFADQHRAQALGcAGddpvKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNdvPLPPDAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 75 VYGDVrpefgslytMMERDWDSIHSGKQHLfTTGGKLEDRVDSDT----RW--FSTEKSY---KEFLKEHrvampgggkF 145
Cdd:cd16034 81 TIADV---------LKDAGYRTGYIGKWHL-DGPERNDGRADDYTpppeRRhgFDYWKGYecnHDHNNPH---------Y 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 146 RTKVPEMVDGKatrvssysnaetgRYEPGEQyyfdsyfTEMALEGLRRR-DTTKPLllnAMFLA---PHPPLQI-PDPWY 220
Cdd:cd16034 142 YDDDGKRIYIK-------------GYSPDAE-------TDLAIEYLENQaDKDKPF---ALVLSwnpPHDPYTTaPEEYL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 221 RAVGAEDFALPENIgvyyprqsPLQMYnltgivgtryGREHWKEAWRVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILF 300
Cdd:cd16034 199 DMYDPKKLLLRPNV--------PEDKK----------EEAGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVF 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 301 TSDHGEMLGSHGLFQKMCMYEESARVPLFMKFPKGFtPSDKSYGQVVSHIDVLPTLCDYLQMDSGNEMDGTSLMPLLRGE 380
Cdd:cd16034 261 TSDHGDMLGSHGLMNKQVPYEESIRVPFIIRYPGKI-KAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGG 339
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2629630740 381 SRAEDRNSA--YIQYDGNGSRSNFQ--RCMIWGRWKLIVDLfKDETFyeLYDLEEDVQETSNL 439
Cdd:cd16034 340 KDDEPDSVLlqCFVPFGGGSARDGGewRGVRTDRYTYVRDK-NGPWL--LFDNEKDPYQLNNL 399
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
2-458 |
2.83e-76 |
|
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: 245.52 E-value: 2.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRYDVLG---KGF--TPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLIN--PWEPADA 74
Cdd:cd16031 2 RPNIIFILTDDHRYDALGcygNPIvkTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNngPLFDASQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 75 VYgdvrpefgslYTMMERDwdsihSGkqhlFTTG--GKLEDRVDSDTRwfstEKSYKEFlkehrVAMPGGGKFRTKVpem 152
Cdd:cd16031 82 PT----------YPKLLRK-----AG----YQTAfiGKWHLGSGGDLP----PPGFDYW-----VSFPGQGSYYDPE--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 153 vdgkatrvssysNAETGRYEPGEQYYFDSYfTEMALEGLRRRDTTKPLLLNAMFLAPHPPLqIPDPWYRAVGA-EDFALP 231
Cdd:cd16031 131 ------------FIENGKRVGQKGYVTDII-TDKALDFLKERDKDKPFCLSLSFKAPHRPF-TPAPRHRGLYEdVTIPEP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 232 ENIGV-YYPRQSPLQMYNLTGIVGTRYGREHWKEAW----RVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGE 306
Cdd:cd16031 197 ETFDDdDYAGRPEWAREQRNRIRGVLDGRFDTPEKYqrymKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGF 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 307 MLGSHGLFQKMCMYEESARVPLFMKFPKGFTPsdksyGQVVSH----IDVLPTLCDYLQMDSGNEMDGTSLMPLLRGESR 382
Cdd:cd16031 277 FLGEHGLFDKRLMYEESIRVPLIIRDPRLIKA-----GTVVDAlvlnIDFAPTILDLAGVPIPEDMQGRSLLPLLEGEKP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 383 AEDRNSAYIQYDGNGSRSNFQRCMiwG----RWKLIVdLFKDETFYELYDLEEDVQETSNLMFDGKHDEIAEEMANRLAA 458
Cdd:cd16031 352 VDWRKEFYYEYYEEPNFHNVPTHE--GvrteRYKYIY-YYGVWDEEELYDLKKDPLELNNLANDPEYAEVLKELRKRLEE 428
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
3-372 |
1.65e-72 |
|
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: 229.25 E-value: 1.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLGK-GF----TPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLINPWEPadavYG 77
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCyGNpdikTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNG----GG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 78 DVRPEFGSLYTMMERDWDSIHSGKQHlfttggkledrvdsdtrwfsteksykeflkehrvampgggkfrtkvpemvdgka 157
Cdd:cd16022 77 LPPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 158 trvssysnaetgryepgeqyyfdsyftEMALEGLRRRDTTKPLLLNAMFLAPHPPLqipdpwyravgaedfalpenigvy 237
Cdd:cd16022 103 ---------------------------DEAIDFIERRDKDKPFFLYVSFNAPHPPF------------------------ 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 238 yprqsplqmynltgivgtrygrehwkeawrVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGEMLGSHGL-FQK 316
Cdd:cd16022 132 ------------------------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKK 181
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2629630740 317 MCMYEESARVPLFMKFPKGFtPSDKSYGQVVSHIDVLPTLCDYLQMDSGNEMDGTS 372
Cdd:cd16022 182 GSLYEGGIRVPFIVRWPGKI-PAGQVSDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-432 |
1.51e-71 |
|
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: 229.74 E-value: 1.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLGKG-----FTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSlinpWEPADAVYG 77
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYghpvvRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGV----WDNADPYDG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 78 DVrPEFGSLytMMERDWDSIHSGKQHLfttggkledrVDSDTRWFsteksykeflkehrvampgggkfrtkvpemvdgka 157
Cdd:cd16037 77 DV-PSWGHA--LRAAGYETVLIGKLHF----------RGEDQRHG----------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 158 trvssysnaetgryepgeqYYFDSYFTEMALEGLRRRDT-TKPLLLNAMFLAPHPPLQIPDPWYravgaedfalpenigv 236
Cdd:cd16037 109 -------------------FRYDRDVTEAAVDWLREEAAdDKPWFLFVGFVAPHFPLIAPQEFY---------------- 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 237 yyprqsplQMYNltgivgtrygrehwKEAWRVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGEMLGSHGLFQK 316
Cdd:cd16037 154 --------DLYV--------------RRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGK 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 317 MCMYEESARVPLFMKFPKGFTPsdKSYGQVVSHIDVLPTLCDYLQMDSGNEMDGTSLMPLLRGESRAEDrnSAYIQYDGN 396
Cdd:cd16037 212 STMYEESVRVPMIISGPGIPAG--KRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEGPDDPDR--VVFSEYHAH 287
|
410 420 430
....*....|....*....|....*....|....*..
gi 2629630740 397 GSRSnfQRCMI-WGRWKLIvdLFKDETfYELYDLEED 432
Cdd:cd16037 288 GSPS--GAFMLrKGRWKYI--YYVGYP-PQLFDLEND 319
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
5-465 |
2.56e-71 |
|
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: 233.31 E-value: 2.56e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 5 VIIIMADQLRYDVLGKGF-----TPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLINPwEPADA----- 74
Cdd:cd16028 3 VLFITADQWRADCLSCLGhplvkTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNG-TPLDArhltl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 75 -----VYGdVRPE-FGslYTMMERDWDSIHSgkqhlfttggkledrvdSDTRWFSTEksykeflkehrVAMPGggkFRTk 148
Cdd:cd16028 82 alelrKAG-YDPAlFG--YTDTSPDPRGLAP-----------------LDPRLLSYE-----------LAMPG---FDP- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 149 vPEMVDGKATRVSsysnaETgryepgeqyyfdSYFTEMALEGLRRRDTtKPLLLNAMFLAPHPPLQIPDPWYRAVGAEDF 228
Cdd:cd16028 127 -VDRLDEYPAEDS-----DT------------AFLTDRAIEYLDERQD-EPWFLHLSYIRPHPPFVAPAPYHALYDPADV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 229 ALP---ENIGVYYpRQSPL------QMYNLTGIVGTRYGREHWKEAWR----VYLGLVRMLDHCVGRVLEELKRQGIYDD 295
Cdd:cd16028 188 PPPiraESLAAEA-AQHPLlaafleRIESLSFSPGAANAADLDDEEVAqmraTYLGLIAEVDDHLGRLFDYLKETGQWDD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 296 SLILFTSDHGEMLGSHGLFQKMCMYEESARVPLFMKFPKGftPSDKSYGQVVS----HIDVLPTLCDYLQMDSGNEMDGT 371
Cdd:cd16028 267 TLIVFTSDHGEQLGDHWLWGKDGFFDQAYRVPLIVRDPRR--EADATRGQVVDafteSVDVMPTILDWLGGEIPHQCDGR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 372 SLMPLLRGESRAEDRNSAYIQYD-GNGSRSNFQR--------CMIW----GRWKLIvdlfkdeTFYE----LYDLEEDVQ 434
Cdd:cd16028 345 SLLPLLAGAQPSDWRDAVHYEYDfRDVSTRRPQEalglspdeCSLAvirdERWKYV-------HFAAlpplLFDLKNDPG 417
|
490 500 510
....*....|....*....|....*....|.
gi 2629630740 435 ETSNLMFDGKHDEIAEEMANRLAAHSRETGD 465
Cdd:cd16028 418 ELRDLAADPAYAAVVLRYAQKLLSWRMRHAD 448
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
1-465 |
2.24e-70 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 231.87 E-value: 2.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 1 MKPHVIIIMADQLRYDVLGKG-----FTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLinpwepadaV 75
Cdd:PRK13759 5 KKPNIILIMVDQMRGDCLGCNgnkavETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRV---------G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 76 YGDVRPeFGSLYTM--MERDWDsIHS---GKQHLFTTGGK-------LEDRVDSDTRwfSTEKSYKEFLKEHRVAmpggg 143
Cdd:PRK13759 76 YGDVVP-WNYKNTLpqEFRDAG-YYTqciGKMHVFPQRNLlgfhnvlLHDGYLHSGR--NEDKSQFDFVSDYLAW----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 144 kFRTKVPEMvDGKATRVSSYSNAETGR-YEPGEQYYFDSYFTEMALEGLRRRDTTKPLLLNAMFLAPHPPLQIPDPWYRA 222
Cdd:PRK13759 147 -LREKAPGK-DPDLTDIGWDCNSWVARpWDLEERLHPTNWVGSESIEFLRRRDPTKPFFLKMSFARPHSPYDPPKRYFDM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 223 VGAEDFALPENIGVYYPRQSPLQMYNLTGIVGtRYGREHWKEAWRVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTS 302
Cdd:PRK13759 225 YKDADIPDPHIGDWEYAEDQDPEGGSIDALRG-NLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 303 DHGEMLGSHGLFQKMCMYEESARVPLFMKFPKGFT--PSDKSYGQVVSHIDVLPTLCDYLQMDSGNEMDGTSLMPLLRGe 380
Cdd:PRK13759 304 DHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLagNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFG- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 381 SRAEDRNSAYIQYDGNGSRSNFqrcMIWGRWKLIvdLFKDETFYELYDLEEDVQETSNLMFDGKHDEIAEEMANRLAAHS 460
Cdd:PRK13759 383 QYEGWRPYLHGEHALGYSSDNY---LTDGKWKYI--WFSQTGEEQLFDLKKDPHELHNLSPSEKYQPRLREMRKKLVDHL 457
|
....*
gi 2629630740 461 RETGD 465
Cdd:PRK13759 458 RGREE 462
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-467 |
1.67e-67 |
|
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: 222.50 E-value: 1.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLG-----KGFTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNG-----SLINPWEPa 72
Cdd:cd16150 1 PNIVIFVADQLRADSLGhlgnpAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGhrtlhHLLRPDEP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 73 davygdvrpefGSLYTMMERDWDSIHSGKQHLFTTGGKLEDRVDSDTrwfsteksykeflkehrvampgggkfrtkvpEM 152
Cdd:cd16150 80 -----------NLLKTLKDAGYHVAWAGKNDDLPGEFAAEAYCDSDE-------------------------------AC 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 153 VDGkatrvssysnaetgryepgeqyyfdsyftemALEGLRRRDTTKPLLLnamFLA---PHPPLQIPDPWYRAVGAEDfa 229
Cdd:cd16150 118 VRT-------------------------------AIDWLRNRRPDKPFCL---YLPlifPHPPYGVEEPWFSMIDREK-- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 230 LPENIgvyypRQSPLQMYNLTGIVGTRY-GREHWKEA-WR----VYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSD 303
Cdd:cd16150 162 LPPRR-----PPGLRAKGKPSMLEGIEKqGLDRWSEErWRelraTYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSD 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 304 HGEMLGSHGLFQKM--CMYEESARVPLFMKFPKGftPSDKSYGQVVSHIDVLPTLCDYLQMDSGNEMDGTSLMPLLRGES 381
Cdd:cd16150 237 HGDYTGDYGLVEKWpnTFEDCLTRVPLIIKPPGG--PAGGVSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLPVLAGET 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 382 RAEDRnsaYIQYDGnGSRSNFQRCMIWG-----------------------------RWKLIVDLF-KDetfyELYDLEE 431
Cdd:cd16150 315 EEHRD---AVFSEG-GRLHGEEQAMEGGhgpydlkwprllqqeeppehtkavmirtrRYKYVYRLYePD----ELYDLEA 386
|
490 500 510
....*....|....*....|....*....|....*.
gi 2629630740 432 DVQETSNLMFDGKHDEIAEEMANRLAAHSRETGDLL 467
Cdd:cd16150 387 DPLELHNLIGDPAYAEIIAEMKQRLLRWMVETSDVV 422
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
3-467 |
1.13e-61 |
|
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: 208.39 E-value: 1.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLG-----KGFTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLINPWEPADAVYg 77
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGcygnkAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 78 dvrpefgslyTMMERDWDS-IHS---GKQHL-----FTTGgKLEDRVDSDTrWFSTeKSYKEFLKEHRvampgggkfrtk 148
Cdd:cd16156 80 ----------TIGQRLSDNgIHTayiGKWHLdggdyFGNG-ICPQGWDPDY-WYDM-RNYLDELTEEE------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 149 vpemvdgkaTRVSSYSNAETGRYEPGEQYYFDSYFTEMALEGLRRRdTTKPLLLNAMFLAPHPPLQIPDPWyrAVGAEDF 228
Cdd:cd16156 135 ---------RRKSRRGLTSLEAEGIKEEFTYGHRCTNRALDFIEKH-KDEDFFLVVSYDEPHHPFLCPKPY--ASMYKDF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 229 ALPENIGVYYPRQS-PL--QMYNltgivGTRYGREHWKEAWR--VYLGLVRMLDHCVGRVLEELKRqgIYDDSLILFTSD 303
Cdd:cd16156 203 EFPKGENAYDDLENkPLhqRLWA-----GAKPHEDGDKGTIKhpLYFGCNSFVDYEIGRVLDAADE--IAEDAWVIYTSD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 304 HGEMLGSHGLFQK-MCMYEESARVPLFMKFPKGftpsDKSYGQV---VSHIDVLPTLCDYLQMDSGNEMDGTSLMPLLRG 379
Cdd:cd16156 276 HGDMLGAHKLWAKgPAVYDEITNIPLIIRGKGG----EKAGTVTdtpVSHIDLAPTILDYAGIPQPKVLEGESILATIED 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 380 ESRAEDR------NSAYIQYDGNGSrsnFQ--RCMIWGRWKLIVDLFKDEtfyELYDLEEDVQETSNLMFDGKHDEIAEE 451
Cdd:cd16156 352 PEIPENRgvfvefGRYEVDHDGFGG---FQpvRCVVDGRYKLVINLLSTD---ELYDLEKDPYEMHNLIDDPDYADVRDQ 425
|
490
....*....|....*.
gi 2629630740 452 MANRLAAHSRETGDLL 467
Cdd:cd16156 426 LHDELLDYMNETRDPF 441
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
3-459 |
4.80e-61 |
|
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: 203.89 E-value: 4.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLGKGF----TPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSlinpwepadavygd 78
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGnvvkTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 79 vrpefgslytmmerdwdsihsgkQHLFTTGGKLEDRVdsdtrwfsteKSYKEFLKEH--RVAMpgGGKFRTKVPEMVDGK 156
Cdd:cd16027 67 -----------------------HGLRSRGFPLPDGV----------KTLPELLREAgyYTGL--IGKTHYNPDAVFPFD 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 157 ATRVSSYSNAETGRYEPGEQYYFdsyftemalegLRRRDTTKPLLLNAMFLAPHPPLQIPDPWYRAVGAEDFALPEnigv 236
Cdd:cd16027 112 DEMRGPDDGGRNAWDYASNAADF-----------LNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPP---- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 237 YYPrQSPlqmynltgivGTRygrehwkEAWRVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGemlGSHgLFQK 316
Cdd:cd16027 177 YLP-DTP----------EVR-------EDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG---MPF-PRAK 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 317 MCMYEESARVPLFMKFPKGFTPSDKSYgQVVSHIDVLPTLCDYLQMDSGNEMDGTSLMPLLRGESrAEDRNSAYIQYDGN 396
Cdd:cd16027 235 GTLYDSGLRVPLIVRWPGKIKPGSVSD-ALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEK-DPGRDYVFAERDRH 312
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2629630740 397 GSRSNFQRCMIWGRWKLIVDLFkdetFYELYDLEEDVQETSNLMFDGKHDEIAEEMANRLAAH 459
Cdd:cd16027 313 DETYDPIRSVRTGRYKYIRNYM----PEELYDLKNDPDELNNLADDPEYAEVLEELRAALDAW 371
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
3-432 |
2.09e-60 |
|
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: 200.88 E-value: 2.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVL---GKGF--TPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLINPWE-PADAvy 76
Cdd:cd16032 1 PNILLIMADQLTAAALpayGNTVvkTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEfPADI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 77 gdvrPEFGSLYTMMerDWDSIHSGKQHlFTTGGKLEDrVDSDtrwfsteksykeflkehrvampgggkfrtkvpEMVDGK 156
Cdd:cd16032 79 ----PTFAHYLRAA--GYRTALSGKMH-FVGPDQLHG-FDYD--------------------------------EEVAFK 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 157 ATrvssysnaetgryepgeQYYFDsyftemalegLRRRDTTKPLLLNAMFLAPHPPLQIPdpwyravgaedfalpenigv 236
Cdd:cd16032 119 AV-----------------QKLYD----------LARGEDGRPFFLTVSFTHPHDPYVIP-------------------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 237 yyprqsplqmynltgivgtrygREHW----KEAWRVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGEMLGSHG 312
Cdd:cd16032 152 ----------------------QEYWdlyvRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERG 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 313 LFQKMCMYEESARVPLFMKFPKGFTPSDKSygQVVSHIDVLPTLCDYL---QMDSGNEMDGTSLMPLLRGESRAEDRnSA 389
Cdd:cd16032 210 LWYKMSFFEGSARVPLIISAPGRFAPRRVA--EPVSLVDLLPTLVDLAgggTAPHVPPLDGRSLLPLLEGGDSGGED-EV 286
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2629630740 390 YIQYDGNGSRSnfQRCMI-WGRWKLIVdLFKDETFyeLYDLEED 432
Cdd:cd16032 287 ISEYLAEGAVA--PCVMIrRGRWKFIY-CPGDPDQ--LFDLEAD 325
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
2-456 |
4.49e-60 |
|
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: 201.64 E-value: 4.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRYD---VLGKGF--TPNIDSIAADGTAFGRAYCA---CP-LCVPARGSFFTGtypnrngslinpwepa 72
Cdd:cd16155 2 KPNILFILADDQRADtigALGNPEiqTPNLDRLARRGTSFTNAYNMggwSGaVCVPSRAMLMTG---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 73 davygdvrpefgslytmmerdwdsihsgkQHLFTTGGKLEDRVDSDTRWFSteksykEFLKEHrvampGGGKFRTkvpem 152
Cdd:cd16155 66 -----------------------------RTLFHAPEGGKAAIPSDDKTWP------ETFKKA-----GYRTFAT----- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 153 vdGKAtrvssysnaetgryepgeqyyfDSYFTEMALEGLRRR-DTTKPLLLNAMFLAPHPPLQIPDPWYRAVGAEDFALP 231
Cdd:cd16155 101 --GKW----------------------HNGFADAAIEFLEEYkDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPLP 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 232 ENIGVYYPRQSPLQM---YNLTGIVGTRYG-REHWKEawrvYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGEM 307
Cdd:cd16155 157 ENFLPQHPFDNGEGTvrdEQLAPFPRTPEAvRQHLAE----YYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLA 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 308 LGSHGLFQKMCMYEESARVPLFMKFPkGFtPSDKSYGQVVSHIDVLPTLCDYLQMDSGNEMDGTSLMPLLRGESRAEdRN 387
Cdd:cd16155 233 VGSHGLMGKQNLYEHSMRVPLIISGP-GI-PKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAV-RD 309
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2629630740 388 SAYIQYdgngsrSNFQRCMIWGRWKLIVdLFKDETFYELYDLEEDVQETSNLMFDGKHDEIAEEMANRL 456
Cdd:cd16155 310 TLYGAY------RDGQRAIRDDRWKLII-YVPGVKRTQLFDLKKDPDELNNLADEPEYQERLKKLLAEL 371
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
2-439 |
3.10e-57 |
|
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: 195.87 E-value: 3.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRyDVLG-----KGFTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGslinpwepadaVY 76
Cdd:cd16030 2 KPNVLFIAVDDLR-PWLGcygghPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTG-----------VY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 77 GdvrpeFGSLYTMMERDWDSIHsgkQHL-----FTTG-GKL--------EDRVDS-DTRWFSTEKSYKEFLKEHRVAMPG 141
Cdd:cd16030 70 D-----NNSYFRKVAPDAVTLP---QYFkengyTTAGvGKIfhpgipdgDDDPASwDEPPNPPGPEKYPPGKLCPGKKGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 142 GGKFRTKVPEMVDgkatrvssysnaetgryEPGEQYyFDSYFTEMALEGLRRR-DTTKPLLLNAMFLAPHPPLQIPDPWY 220
Cdd:cd16030 142 KGGGGGPAWEAAD-----------------VPDEAY-PDGKVADEAIEQLRKLkDSDKPFFLAVGFYKPHLPFVAPKKYF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 221 RAVGAEDFALPENigvYYPRQSPLQMYN-----------LTGIVGTRYGR---EHWKEAWRVYLGLVRMLDHCVGRVLEE 286
Cdd:cd16030 204 DLYPLESIPLPNP---FDPIDLPEVAWNdlddlpkygdiPALNPGDPKGPlpdEQARELRQAYYASVSYVDAQVGRVLDA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 287 LKRQGIYDDSLILFTSDHGEMLGSHGLFQKMCMYEESARVPLFMKFPkGFTPSDKSYGQVVSHIDVLPTLCDYLQMDSGN 366
Cdd:cd16030 281 LEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRVPLIIRAP-GVTKPGKVTDALVELVDIYPTLAELAGLPAPP 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2629630740 367 EMDGTSLMPLLRGESrAEDRNSAYIQY--DGNGSRSnfqrcMIWGRWKLI--VDlFKDETFYELYDLEEDVQETSNL 439
Cdd:cd16030 360 CLEGKSLVPLLKNPS-AKWKDAAFSQYprPSIMGYS-----IRTERYRYTewVD-FDKVGAEELYDHKNDPNEWKNL 429
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
2-462 |
6.52e-51 |
|
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: 177.42 E-value: 6.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRYDVLG-----KGFTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGslinpwepadaVY 76
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGcygqpLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETG-----------CF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 77 GDVRPEFGSLYT----MMERDWDSIHSGKQHLfttggkledrvdsdtrwfsteksykeflkehrvampggGKFRtkvpem 152
Cdd:cd16152 70 RNGIPLPADEKTlahyFRDAGYETGYVGKWHL--------------------------------------AGYR------ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 153 VDgkatrvssysnaetgryepgeqyyfdsYFTEMALEGLRRRDTTKPLLLNAMFLAPHppLQipDPWYRAVGAE------ 226
Cdd:cd16152 106 VD---------------------------ALTDFAIDYLDNRQKDKPFFLFLSYLEPH--HQ--NDRDRYVAPEgsaerf 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 227 -DFALPENigvyyprqsplqmynLTGIVGTrygrehWKEAWRVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHg 305
Cdd:cd16152 155 aNFWVPPD---------------LAALPGD------WAEELPDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 306 emlGSH-----GLFQKMCmYEESARVPLFMKFPkGFTPSdKSYGQVVSHIDVLPTLCDYLQMDSGNEMDGTSLMPLLRGE 380
Cdd:cd16152 213 ---GCHfrtrnAEYKRSC-HESSIRVPLVIYGP-GFNGG-GRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGK 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 381 sRAEDRNSAYIQYdgngSRSNFQRCMIWGRWKLIV-----DLFKD-------ETFyeLYDLEEDVQETSNLMFDGKHDEI 448
Cdd:cd16152 287 -VEDWRNEVFIQI----SESQVGRAIRTDRWKYSVaapdkDGWKDsgsdvyvEDY--LYDLEADPYELVNLIGRPEYREV 359
|
490
....*....|....
gi 2629630740 449 AEEMANRLAAHSRE 462
Cdd:cd16152 360 AAELRERLLARMAE 373
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
3-459 |
1.23e-48 |
|
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: 172.34 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYD---VLGKGF--TPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNG-------------- 63
Cdd:cd16144 1 PNIVLILVDDLGWAdlgCYGSKFyeTPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGitdvipgrrgppdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 64 -SLINPWepadavYGDVRPEfgSLYTMMER----DWDSIHSGKQHLfttGGKLE--------DRVDSDTRWfsteksyke 130
Cdd:cd16144 81 tKLIPPP------STTRLPL--EEVTIAEAlkdaGYATAHFGKWHL---GGEGGygpedqgfDVNIGGTGN--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 131 flkehRVAMPGGGKFRTKVPEMVDGKatrvssysnaetgryePGEqYYFDSYfTEMALEGLRRRDTtKPLLLNAMFLAPH 210
Cdd:cd16144 141 -----GGPPSYYFPPGKPNPDLEDGP----------------EGE-YLTDRL-TDEAIDFIEQNKD-KPFFLYLSHYAVH 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 211 PPLQipdpwyravgaedfALPENIGVYYPRQSPLqmynltgivgtrygREHWKEAwrVYLGLVRMLDHCVGRVLEELKRQ 290
Cdd:cd16144 197 TPIQ--------------ARPELIEKYEKKKKGL--------------RKGQKNP--VYAAMIESLDESVGRILDALEEL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 291 GIYDDSLILFTSDHGEMLGSHGLF--------QKMCMYEESARVPLFMKFPkGFTPSDKSYGQVVSHIDVLPTLCD--YL 360
Cdd:cd16144 247 GLADNTLVIFTSDNGGLSTRGGPPtsnaplrgGKGSLYEGGIRVPLIVRWP-GVIKPGSVSDVPVIGTDLYPTFLElaGG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 361 QMDSGNEMDGTSLMPLLRGESRAEDRNSAYI---QYDGNGSRSnfQRCMIWGRWKLIVDLFKDEtfYELYDLEEDVQETS 437
Cdd:cd16144 326 PLPPPQHLDGVSLVPLLKGGEADLPRRALFWhfpHYHGQGGRP--ASAIRKGDWKLIEFYEDGR--VELYNLKNDIGETN 401
|
490 500
....*....|....*....|..
gi 2629630740 438 NLMfdGKHDEIAEEMANRLAAH 459
Cdd:cd16144 402 NLA--AEMPEKAAELKKKLDAW 421
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-375 |
3.47e-48 |
|
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: 166.95 E-value: 3.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLG-----KGFTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGslinPWEPADAVYG 77
Cdd:cd16148 1 MNVILIVIDSLRADHLGcygydRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHG----VWGGPLEPDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 78 DVRPEfgslyTMMERDWDSihsgkqHLFttggkledrvdSDTRWFStekSYKEFLKEHRVAMPGGGKFrtkvpemvdgka 157
Cdd:cd16148 77 PTLAE-----ILRKAGYYT------AAV-----------SSNPHLF---GGPGFDRGFDTFEDFRGQE------------ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 158 trvssySNAETGRYEPGEQYyfdsyfTEMALEGLRRRDTTKPLLLNAMFLAPHPPlqipdpwYRavgaedfalpenigvy 237
Cdd:cd16148 120 ------GDPGEEGDERAERV------TDRALEWLDRNADDDPFFLFLHYFDPHEP-------YL---------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 238 yprqsplqmynltgivgtrygrehwkeawrvYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGEMLGSHGLFQK- 316
Cdd:cd16148 165 -------------------------------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGh 213
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 317 -MCMYEESARVPLFMKFPkGFTPsDKSYGQVVSHIDVLPTLCDYLQMDSGNEMDGTSLMP 375
Cdd:cd16148 214 gSNLYDEQLHVPLIIRWP-GKEP-GKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
3-439 |
4.20e-47 |
|
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: 168.16 E-value: 4.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLG-----KGFTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTG-----TYPNRNGSLIN--PWE 70
Cdd:cd16145 1 PNIIFILADDLGYGDLGcygqkKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGlhtghTRVRGNSEPGGqdPLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 71 PADAVYGDVRPEFGslYT--MMerdwdsihsGKQHLF---TTGGKLEDRVD--------SDTRWFsteksYKEFLKEH-- 135
Cdd:cd16145 81 PDDVTLAEVLKKAG--YAtaAF---------GKWGLGgpgTPGHPTKQGFDyfygyldqVHAHNY-----YPEYLWRNge 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 136 RVAMPGGGKFRTKVPEMVDGKATRVSSYsnaetgryepgeqyyfdsYFTEMALEGLRR-RDttKPLLLNAMFLAPHPPLQ 214
Cdd:cd16145 145 KVPLPNNVIPPLDEGNNAGGGGGTYSHD------------------LFTDEALDFIREnKD--KPFFLYLAYTLPHAPLQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 215 IPDPWYravgAEDFALPENIGVYYPrqsplqmynltgivgtrygrehWKEAWRVYLGLVRMLDHCVGRVLEELKRQGIYD 294
Cdd:cd16145 205 VPDDGP----YKYKPKDPGIYAYLP----------------------WPQPEKAYAAMVTRLDRDVGRILALLKELGIDE 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 295 DSLILFTSDHG-----------EMLGSHGLFQ--KMCMYEESARVPLFMKFPKGFTPsdksyGQVVSHI----DVLPTLC 357
Cdd:cd16145 259 NTLVVFTSDNGphseggsehdpDFFDSNGPLRgyKRSLYEGGIRVPFIARWPGKIPA-----GSVSDHPsafwDFMPTLA 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 358 DYLQMDSGNEMDGTSLMPLLRGESRAEDRNSAYIQYDGNGsrsnFQRCMIWGRWKLIVDLFKDETFyELYDLEEDVQETS 437
Cdd:cd16145 334 DLAGAEPPEDIDGISLLPTLLGKPQQQQHDYLYWEFYEGG----GAQAVRMGGWKAVRHGKKDGPF-ELYDLSTDPGETN 408
|
..
gi 2629630740 438 NL 439
Cdd:cd16145 409 NL 410
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
3-452 |
7.37e-45 |
|
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: 161.95 E-value: 7.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLG-------KgfTPNIDSIAADGTAFGRAYcACPLCVPARGSFFTGTYPNRNG--------SLIN 67
Cdd:cd16146 1 PNVILILTDDQGYGDLGfhgnpilK--TPNLDRLAAESVRFTNFH-VSPVCAPTRAALLTGRYPFRTGvwhtilgrERMR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 68 PWEP------ADAVY----------GDVRPefgslYTMMER--DWDSIHSGKQHLFTTGGKLEDRVDSDTRWFSTEKSYK 129
Cdd:cd16146 78 LDETtlaevfKDAGYrtgifgkwhlGDNYP-----YRPQDRgfDEVLGHGGGGIGQYPDYWGNDYFDDTYYHNGKFVKTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 130 eflkehrvampgggKFRTKVpemvdgkatrvssysnaetgryepgeqyyfdsyFTEMALEGLRRrDTTKPLLLNAMFLAP 209
Cdd:cd16146 153 --------------GYCTDV---------------------------------FFDEAIDFIEE-NKDKPFFAYLATNAP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 210 HPPLQIPDPWYravgaedfalpenigvyyprqsplqmynltgivgTRYGREHWKEAWRVYLGLVRMLDHCVGRVLEELKR 289
Cdd:cd16146 185 HGPLQVPDKYL----------------------------------DPYKDMGLDDKLAAFYGMIENIDDNVGRLLAKLKE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 290 QGIYDDSLILFTSDHGEMLGSHGLF------QKMCMYEESARVPLFMKFPKGFTPSDKSYgQVVSHIDVLPTLCDY--LQ 361
Cdd:cd16146 231 LGLEENTIVIFMSDNGPAGGVPKRFnagmrgKKGSVYEGGHRVPFFIRWPGKILAGKDVD-TLTAHIDLLPTLLDLcgVK 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 362 MDSGNEMDGTSLMPLLRGESRAE-DRNSAYIQYDGNGSRSNFQRCMIW-GRWKLIVDlfkDETFYELYDLEEDVQETSNL 439
Cdd:cd16146 310 LPEGIKLDGRSLLPLLKGESDPWpERTLFTHSGRWPPPPKKKRNAAVRtGRWRLVSP---KGFQPELYDIENDPGEENDV 386
|
490
....*....|...
gi 2629630740 440 MfdGKHDEIAEEM 452
Cdd:cd16146 387 A--DEHPEVVKRL 397
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-394 |
1.38e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 158.52 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRY-DVLGKGFT----PNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLIN---PWEPada 74
Cdd:cd16035 1 PNILLILTDQERYpPPWPAGWAalnlPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTlgsPMQP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 75 vygDVRPEFGSLYTMM-ERDWDSIHSGKQHLfttggkledrvdsdtrwfsteksykeflkehrVAMPGGGkfrtkvpemv 153
Cdd:cd16035 78 ---LLSPDVPTLGHMLrAAGYYTAYKGKWHL--------------------------------SGAAGGG---------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 154 dgkatrvssysnaetgryepgeqYYFDSYFTEMALEGLRRRDT----TKPLLLNAMFLAPHPPLQIPDPWYRAVGAEDFa 229
Cdd:cd16035 113 -----------------------YKRDPGIAAQAVEWLRERGAknadGKPWFLVVSLVNPHDIMFPPDDEERWRRFRNF- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 230 lpenigvyyprqsplqmynltgivgtrygrehwkeawrvYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGEMLG 309
Cdd:cd16035 169 ---------------------------------------YYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGG 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 310 SHGLFQKM-CMYEESARVPLFMKFPKGFtPSDKSYGQVVSHIDVLPTLCDYLQMDS------GNEMDGTSLMPLLRGESR 382
Cdd:cd16035 210 AHGLRGKGfNAYEEALHVPLIISHPDLF-GTGQTTDALTSHIDLLPTLLGLAGVDAearateAPPLPGRDLSPLLTDADA 288
|
410
....*....|..
gi 2629630740 383 AEDRNSAYIQYD 394
Cdd:cd16035 289 DAVRDGILFTYD 300
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
2-439 |
7.50e-38 |
|
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: 142.97 E-value: 7.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLrydvlgkGF-----------TPNIDSIAADGTAFGRAYcACPLCVPARGSFFTGTYPNRNG-SLINPW 69
Cdd:cd16025 2 RPNILLILADDL-------GFsdlgcfggeipTPNLDALAAEGLRFTNFH-TTALCSPTRAALLTGRNHHQVGmGTMAEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 70 EPADAVY-GDVRPEFGSLYTMM-ERDWDSIHSGKQHLfttggkledrvdsdtrwfsteksykeflkehrvampgggkfrt 147
Cdd:cd16025 74 ATGKPGYeGYLPDSAATIAEVLkDAGYHTYMSGKWHL------------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 148 kvpemvdgkatrvssysnaetgryePGEQYYFDSYFTEMALEGLR-RRDTTKPLLLNAMFLAPHPPLQIPDPW---YRav 223
Cdd:cd16025 111 -------------------------GPDDYYSTDDLTDKAIEYIDeQKAPDKPFFLYLAFGAPHAPLQAPKEWidkYK-- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 224 gaedfalpeniGVY-----------YPRQspLQMynltGIV--GTRY-GREHWKEAW------------R---VYLGLVR 274
Cdd:cd16025 164 -----------GKYdagwdalreerLERQ--KEL----GLIpaDTKLtPRPPGVPAWdslspeekkleaRrmeVYAAMVE 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 275 MLDHCVGRVLEELKRQGIYDDSLILFTSDHG---E----MLGShGLFQ--KMCMYEESARVPLFMKFPKGFTPSDKSYGQ 345
Cdd:cd16025 227 HMDQQIGRLIDYLKELGELDNTLIIFLSDNGasaEpgwaNASN-TPFRlyKQASHEGGIRTPLIVSWPKGIKAKGGIRHQ 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 346 VVSHIDVLPTLCDYLQMD-----SGNE---MDGTSLMPLLRGESRAEDRNSAYIQYDGNgsrsnfqRCMIWGRWKLI--V 415
Cdd:cd16025 306 FAHVIDIAPTILELAGVEypktvNGVPqlpLDGVSLLPTLDGAAAPSRRRTQYFELFGN-------RAIRKGGWKAValH 378
|
490 500
....*....|....*....|....
gi 2629630740 416 DLFKDETFYELYDLEEDVQETSNL 439
Cdd:cd16025 379 PPPGWGDQWELYDLAKDPSETHDL 402
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
3-439 |
2.17e-36 |
|
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: 138.49 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRY-DV-----LGKGFTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLINPWEPADAVY 76
Cdd:cd16143 1 PNIVIILADDLGYgDIscynpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 77 gdVRPEFGSLYTMMerdwdsihsgKQHLFTTG--GKledrvdsdtrWfsteksykeflkeHRvampgGGKFRTKVPEMVD 154
Cdd:cd16143 81 --IEPDRVTLAKML----------KQAGYRTAmvGK----------W-------------HL-----GLDWKKKDGKKAA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 155 GKATRVSSYSnaetGRYEPGEQYY-FDSYF-----------TEMALEGLRR-RDTTKPLLLNAMFLAPHPPLqipdpwyr 221
Cdd:cd16143 121 TGTGKDVDYS----KPIKGGPLDHgFDYYFgipasevlptlTDKAVEFIDQhAKKDKPFFLYFALPAPHTPI-------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 222 aVGAEDFALPENIGVYyprqsplqmynltgivgtrygrehwkeawrvyLGLVRMLDHCVGRVLEELKRQGIYDDSLILFT 301
Cdd:cd16143 189 -VPSPEFQGKSGAGPY--------------------------------GDFVYELDWVVGRILDALKELGLAENTLVIFT 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 302 SDHG-------EMLGSHGLF-------QKMCMYEESARVPLFMKFPKGfTPSDKSYGQVVSHIDVLPTLCDYL--QMDSG 365
Cdd:cd16143 236 SDNGpspyadyKELEKFGHDpsgplrgMKADIYEGGHRVPFIVRWPGK-IPAGSVSDQLVSLTDLFATLAAIVgqKLPDN 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 366 NEMDGTSLMPLLRGESRAEDRNSAYIQyDGNGSRSNFQrcmiwGRWKLIVDLFK------------DETFYELYDLEEDV 433
Cdd:cd16143 315 AAEDSFSFLPALLGPKKQEVRESLVHH-SGNGSFAIRK-----GDWKLIDGTGSggfsyprgkeklGLPPGQLYNLSTDP 388
|
....*.
gi 2629630740 434 QETSNL 439
Cdd:cd16143 389 GESNNL 394
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
3-360 |
2.36e-35 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 133.32 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLG-KGF----TPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLINPWEPadavyg 77
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGlYGYprptTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 78 dVRPEFGSLYTMM-ERDWDSIHSGKQHLFttggkledrvdsdtrWFSteksykeflkehRVAMPGGGKfrtkvpEMVDGK 156
Cdd:pfam00884 75 -LPRTEPSLPDLLkRAGYNTGAIGKWHLG---------------WYN------------NQSPCNLGF------DKFFGR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 157 ATRVSSYSNAETGRYEPGEQYYFDSYFTEMALEGLRRRDttKPLLLNAMFLAPHPPLQIPDPWYravgaedfalPENIGV 236
Cdd:pfam00884 121 NTGSDLYADPPDVPYNCSGGGVSDEALLDEALEFLDNND--KPFFLVLHTLGSHGPPYYPDRYP----------EKYATF 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 237 YYPRQSPLQMYNltgivgtrygrehwkeawrVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGEMLGSHGLF-- 314
Cdd:pfam00884 189 KPSSCSEEQLLN-------------------SYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYlh 249
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2629630740 315 --QKMCMYEESARVPLFMKFPKGFTPSDKSYgQVVSHIDVLPTLCDYL 360
Cdd:pfam00884 250 ggKYDNAPEGGYRVPLLIWSPGGKAKGQKSE-ALVSHVDLFPTILDLA 296
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
2-439 |
2.65e-35 |
|
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: 135.77 E-value: 2.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRYDVLG-------KgfTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLINPWEPADA 74
Cdd:cd16026 1 KPNIVVILADDLGYGDLGcygspliK--TPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 75 vYGdVRPEFgslYTMME----RDWDSIHSGKQHLFTTGGKLEDRVDSDtRWFSTEKS-----YKEFLKEHRVAMPGGGKF 145
Cdd:cd16026 79 -GG-LPPDE---ITIAEvlkkAGYRTALVGKWHLGHQPEFLPTRHGFD-EYFGIPYSndmwpFPLYRNDPPGPLPPLMEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 146 RTKVPEMVDgkatrvssysnaetgryepgeQYYFDSYFTEMALEGLRR-RDttKPLLLnamFLA---PHPPLQIPdpwyr 221
Cdd:cd16026 153 EEVIEQPAD---------------------QSSLTQRYTDEAVDFIERnKD--QPFFL---YLAhtmPHVPLFAS----- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 222 avgaEDFALPENIGVYyprqsplqmynltGIVgtrygrehwkeawrvylglVRMLDHCVGRVLEELKRQGIYDDSLILFT 301
Cdd:cd16026 202 ----EKFKGRSGAGLY-------------GDV-------------------VEELDWSVGRILDALKELGLEENTLVIFT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 302 SDHG------EMLGSHGLFQ--KMCMYEESARVPLFMKFPkGFTPSDKSYGQVVSHIDVLPTLCDY--LQMDSGNEMDGT 371
Cdd:cd16026 246 SDNGpwleygGHGGSAGPLRggKGTTWEGGVRVPFIAWWP-GVIPAGTVSDELASTMDLLPTLAALagAPLPEDRVIDGK 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 372 SLMPLLRGESRAEDRnsAYIQYDGNGsrsNFQrCMIWGRWKLIVD------------LFKDETFYELYDLEEDVQETSNL 439
Cdd:cd16026 325 DISPLLLGGSKSPPH--PFFYYYDGG---DLQ-AVRSGRWKLHLPttyrtgtdpgglDPTKLEPPLLYDLEEDPGETYNV 398
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
3-439 |
7.36e-35 |
|
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: 134.21 E-value: 7.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRY-DVlgkGF-------TPNIDSIAADGTAFGRAYcACPLCVPARGSFFTGTYPNRNGslinpwePADA 74
Cdd:cd16029 1 PHIVFILADDLGWnDV---GFhgsdqikTPNLDALAADGVILNNYY-VQPICTPSRAALMTGRYPIHTG-------MQHG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 75 VYGDVRPEFGSL-YTMM-----ERDWDSIHSGKQHLfttgGkledrvdsdtrwFSTEksykEFLKEHR-----VAMPGGg 143
Cdd:cd16029 70 VILAGEPYGLPLnETLLpqylkELGYATHLVGKWHL----G------------FYTW----EYTPTNRgfdsfYGYYGG- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 144 kfrtkvpeMVDG---KATRVSSYSNAETGRYEPGEQYYFDSY----FTEMALEGLRRRDTTKPLLLNAMFLAPHPPLQIP 216
Cdd:cd16029 129 --------AEDYythTSGGANDYGNDDLRDNEEPAWDYNGTYstdlFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 217 dpwyravgaedfalpenigvyyPRQSPLQMYNLTGIvgTRYGRehwkeawRVYLGLVRMLDHCVGRVLEELKRQGIYDDS 296
Cdd:cd16029 201 ----------------------PEYADPYEDKFAHI--KDEDR-------RTYAAMVSALDESVGNVVDALKAKGMLDNT 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 297 LILFTSDHG-----EMLGSHGLF--QKMCMYEESARVPLFMKFPKGFTPSDKSYGQVVSHIDVLPTLCDY--LQMDSGNE 367
Cdd:cd16029 250 LIVFTSDNGgptggGDGGSNYPLrgGKNTLWEGGVRVPAFVWSPLLPPKRGTVSDGLMHVTDWLPTLLSLagGDPDDLPP 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2629630740 368 MDGTSLMPLLRGESRAEdRNSAYIQYDGNGsRSNFQRCMIWGRWKLIvdlfkdeTFYELYDLEEDVQETSNL 439
Cdd:cd16029 330 LDGVDQWDALSGGAPSP-RTEILLNIDDIT-RTTGGAAIRVGDWKLI-------VGKPLFNIENDPCERNDL 392
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-375 |
9.59e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 130.44 E-value: 9.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLG-KG----FTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSL--INPWEPADAv 75
Cdd:cd16149 1 PNILFILTDDQGPWALGcYGnseaVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHdwIVEGSHGKT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 76 ygdvrpefgslytmmerdwdsihsgkqhlfttggkledrvDSDTRWFSTEKSYKEFLKEHrvampgggkfrtkvpemvdg 155
Cdd:cd16149 80 ----------------------------------------KKPEGYLEGQTTLPEVLQDA-------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 156 katrvsSYSNAETGRYEPGEQyyfdsyftemALEGLRRR-DTTKPLLLNAMFLAPHpplqipDPW--YRAVGAEDFAlpe 232
Cdd:cd16149 100 ------GYRCGLSGKWHLGDD----------AADFLRRRaEAEKPFFLSVNYTAPH------SPWgyFAAVTGVDRN--- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 233 nigvyyprqsplqmynltgivgtrygrehwkeawrvylglvrmldhcVGRVLEELKRQGIYDDSLILFTSDHGEMLGSHG 312
Cdd:cd16149 155 -----------------------------------------------VGRLLDELEELGLTENTLVIFTSDNGFNMGHHG 187
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2629630740 313 LFQK------MCMYEESARVPLFMKFPkGFTPSDKSYGQVVSHIDVLPTLCDYLQMDSGNEMD--GTSLMP 375
Cdd:cd16149 188 IWGKgngtfpLNMYDNSVKVPFIIRWP-GVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFAD 257
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-439 |
3.79e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 129.26 E-value: 3.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLG-------KgfTPNIDSIAADGTAFGRAYcACPLCVPARGSFFTGTYPNRNGSLINPWEPADAV 75
Cdd:cd16151 1 PNIILIMADDLGYECIGcyggesyK--TPNIDALAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 76 YGDVRPEFGslY-TMMerdwdsihSGKQHLfttgGKLEDRVDSDTR--------WFSTEKSYKeflkehrvampgGGKFR 146
Cdd:cd16151 78 FGHLLKDAG--YaTAI--------AGKWQL----GGGRGDGDYPHEfgfdeyclWQLTETGEK------------YSRPA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 147 TKVPEMVDGKatrVSSYSNaetGRYEPgeqyyfDsYFTEMALEGLRR-RDttKPLLL-NAMFLA--PHPPLQIPDPWYra 222
Cdd:cd16151 132 TPTFNIRNGK---LLETTE---GDYGP------D-LFADFLIDFIERnKD--QPFFAyYPMVLVhdPFVPTPDSPDWD-- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 223 vgaedfalpenigvyyprqsplqmynltgivgtrYGREHWKEAWRVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTS 302
Cdd:cd16151 195 ----------------------------------PDDKRKKDDPEYFPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 303 DHGEMLGSHGLFQ-------KMCMYEESARVPLFMKFPkGFTPSDKSYGQVVSHIDVLPTLCD--YLQMDSGNEMDGTSL 373
Cdd:cd16151 241 DNGTHRPITSRTNgrevrggKGKTTDAGTHVPLIVNWP-GLIPAGGVSDDLVDFSDFLPTLAElaGAPLPEDYPLDGRSF 319
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2629630740 374 MPLLRGESrAEDRNSAYIQYDGNGSRSNFQRCMIWGRWKLIVDlfkdetfYELYDLEEDVQETSNL 439
Cdd:cd16151 320 APQLLGKT-GSPRREWIYWYYRNPHKKFGSRFVRTKRYKLYAD-------GRFFDLREDPLEKNPL 377
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
2-373 |
7.11e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 126.34 E-value: 7.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRYD---------------VLGKGFTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLI 66
Cdd:cd16153 1 KPNILWIITDDQRVDslscynnahtgksesRLGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 67 NPW-EPADAVYGDVRPEfgslyTMMERDWDSIHSGKQHlfttggkledrvdsdtrwfsteksYKEFLKehrvampgggkf 145
Cdd:cd16153 81 FEAaHPALDHGLPTFPE-----VLKKAGYQTASFGKSH------------------------LEAFQR------------ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 146 rtkvpemvdgkatrvssYSNAETGRYEPgeqyyFDSYFTEMAleglrrrDTTKPLLLNAMFLAPHPPLQIPDPWyravga 225
Cdd:cd16153 120 -----------------YLKNANQSYKS-----FWGKIAKGA-------DSDKPFFVRLSFLQPHTPVLPPKEF------ 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 226 edfalpenigvyyprqsplqmynltgivgtrygREHWKeawrvYLGLVRMLDHCVGRVLEELKRQGIY---DDSLILFTS 302
Cdd:cd16153 165 ---------------------------------RDRFD-----YYAFCAYGDAQVGRAVEAFKAYSLKqdrDYTIVYVTG 206
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2629630740 303 DHGEMLGSHGLFQKMCMYEESARVPLFMKFP-KGFTPSDKSYGQVVSHIDVLPTLCDY--LQMDSGNEMDGTSL 373
Cdd:cd16153 207 DHGWHLGEQGILAKFTFWPQSHRVPLIVVSSdKLKAPAGKVRHDFVEFVDLAPTLLAAagVDVDAPDYLDGRDL 280
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
2-442 |
4.75e-29 |
|
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: 118.04 E-value: 4.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRYDVLGKGFTPNIDSIAAD-GTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLinpwepadavygDVR 80
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADqGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVT------------NNS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 81 PEFGSlytmmerdWDSIHSGKQhlfttggkledrvdsDTRWFST---EKSYK-----EFLKEHRVamPGGGKFrtkVPE- 151
Cdd:cd16147 69 PPGGG--------YPKFWQNGL---------------ERSTLPVwlqEAGYRtayagKYLNGYGV--PGGVSY---VPPg 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 152 ------MVDGkatRVSSYSNAETGRYEPGEQYYFDSYFT----EMALEGLRR-RDTTKPLLLNAMFLAPHPPLQiPDPWY 220
Cdd:cd16147 121 wdewdgLVGN---STYYNYTLSNGGNGKHGVSYPGDYLTdviaNKALDFLRRaAADDKPFFLVVAPPAPHGPFT-PAPRY 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 221 RAVGAEDFALP-----ENI---GVYYPRQSPLQMynLTGIvgtRYGREHWKEAWRVYLGLVRMldhcVGRVLEELKRQGI 292
Cdd:cd16147 197 ANLFPNVTAPPrpppnNPDvsdKPHWLRRLPPLN--PTQI---AYIDELYRKRLRTLQSVDDL----VERLVNTLEATGQ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 293 YDDSLILFTSDHGEMLGSHGL-FQKMCMYEESARVPLFMKFP---KGFTPSdksygQVVSHIDVLPTLCDYLQMDSGNEM 368
Cdd:cd16147 268 LDNTYIIYTSDNGYHLGQHRLpPGKRTPYEEDIRVPLLVRGPgipAGVTVD-----QLVSNIDLAPTILDLAGAPPPSDM 342
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2629630740 369 DGTslmpllrgeSRAEDRNSAYiqydgngsrsnfqRCMIWGRWKLIVDLFKDET-FYELYDLEEDVQETSNLMFD 442
Cdd:cd16147 343 DGR---------SCGDSNNNTY-------------KCVRTVDDTYNLLYFEWCTgFRELYDLTTDPYQLTNLAGD 395
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
3-432 |
1.67e-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: 95.69 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLGKGFT-----PNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLINpwepadavYG 77
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNqvvdlPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNN--------YK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 78 DVRPEFGSLYTMMERDWDSIHS-GKQHLFTTGGKLEDRVDSDTRWFsteksykEFLkehrVAMPGggkfRTKVPEMVDGK 156
Cdd:cd16171 73 GLDPNYPTWMDRLEKHGYHTQKyGKLDYTSGHHSVSNRVEAWTRDV-------PFL----LRQEG----RPTVNLVGDRS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 157 ATRVSSYsnaetgryepgeqyyfDSYFTEMALEGLRRR--DTTKPLLLNAMFLAPHPplqipdpwyravgaedfalpeni 234
Cdd:cd16171 138 TVRVMLK----------------DWQNTDKAVHWIRKEapNLTQPFALYLGLNLPHP----------------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 235 gvyYPrqSPLQMYNLTGIVGTRygrehwkeawRVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGEMLGSHGLF 314
Cdd:cd16171 179 ---YP--SPSMGENFGSIRNIR----------AFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQF 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 315 QKMCMYEESARVPLFMKFPKgfTPSDKSYGQVVSHIDVLPTLCDYLQMDSGNEMDGTSLMPLLRGESRAE--DRN--SAY 390
Cdd:cd16171 244 YKMSMYEGSSHVPLLIMGPG--IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLLSESSIKEspSRVphPDW 321
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2629630740 391 IQYDGNGSRSNFQRCMIW-GRWKLIVDLFKDETFYELYDLEED 432
Cdd:cd16171 322 VLSEFHGCNVNASTYMLRtNSWKYIAYADGNSVPPQLFDLSKD 364
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
2-394 |
1.35e-19 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 91.64 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIM-----ADQLRYDVLGKGFTPNIDSIAADGTAFGRAYcacplcVPARGS------FFTGTYPNRNGSlinpwe 70
Cdd:COG1368 234 KPNVVVILlesfsDFFIGALGNGKDVTPFLDSLAKESLYFGNFY------SQGGRTsrgefaVLTGLPPLPGGS------ 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 71 padAVYGDVRPEFGSLYTMMerdwdsihsgKQH----LFTTGGkledrvdsDTRWFSTEKSYKEFlkehrvampgggKFR 146
Cdd:COG1368 302 ---PYKRPGQNNFPSLPSIL----------KKQgyetSFFHGG--------DGSFWNRDSFYKNL------------GFD 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 147 tkvpEMVDGkatrvSSYSNAETGRYepGeqyYFDSYFTEMALEGLRRRDttKPLLLNAMFLAPHPPLQIPDPWYRAVGAE 226
Cdd:COG1368 349 ----EFYDR-----EDFDDPFDGGW--G---VSDEDLFDKALEELEKLK--KPFFAFLITLSNHGPYTLPEEDKKIPDYG 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 227 DfalpenigvyyprqsplqmynltgivgtrygrehwkEAWRVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGE 306
Cdd:COG1368 413 K------------------------------------TTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 307 MLGSHGLFQkmcMYEESARVPLFMKFPKGFTPsdKSYGQVVSHIDVLPTLCDYLQMDSGNE-MDGTSLMpllrgesRAED 385
Cdd:COG1368 457 RSPGKTDYE---NPLERYRVPLLIYSPGLKKP--KVIDTVGSQIDIAPTLLDLLGIDYPSYyAFGRDLL-------SPDT 524
|
....*....
gi 2629630740 386 RNSAYIQYD 394
Cdd:COG1368 525 DPFAFRNGG 533
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
3-360 |
2.68e-18 |
|
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: 85.04 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIM----ADQLR-YDVLGKGFTPNIDSIAADGTAFGRAYcacplcVPARG--------SFFTGTYPNRNGSLINpw 69
Cdd:cd16015 1 PNVIVILlesfSDPYIdKDVGGEDLTPNLNKLAKEGLYFGNFY------SPGFGggtangefEVLTGLPPLPLGSGSY-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 70 epadavYGDVRPEFGSL-YTMMERDWDSIhsgkqhlFTTGGkledrvdsDTRWFSTEKSYKEFlkehrvampGGGKFRTK 148
Cdd:cd16015 73 ------TLYKLNPLPSLpSILKEQGYETI-------FIHGG--------DASFYNRDSVYPNL---------GFDEFYDL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 149 vpemvdgkatrvSSYSNAETGRYEPGeqyYFDSYFTEMALEGLRRRDTtKPLLLNAMFLAPHPPlqipdpwyravgaedF 228
Cdd:cd16015 123 ------------EDFPDDEKETNGWG---VSDESLFDQALEELEELKK-KPFFIFLVTMSNHGP---------------Y 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 229 ALPENIGVYYPrqsplqmynltgivgtryGREHWKEAWRVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGEML 308
Cdd:cd16015 172 DLPEEKKDEPL------------------KVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSL 233
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2629630740 309 GSHGLFQKMcMYEESARVPLFMKFPKGFTPSDKSygQVVSHIDVLPTLCDYL 360
Cdd:cd16015 234 GSDYDETDE-DPLDLYRTPLLIYSPGLKKPKKID--RVGSQIDIAPTLLDLL 282
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
2-305 |
1.74e-15 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 77.87 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRYDVLGKGFTPNIDSIAADGTAFGRAYCACP-LCVPARGSFFTGTYPNRNGsLINpwepadavYGDVR 80
Cdd:COG1524 23 AKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPsTTAPAHTTLLTGLYPGEHG-IVG--------NGWYD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 81 PEFGSLYTMMERDWDsihsgkqhlfttGGKLEDRVDSDTRWfsteksykEFLKEH--RVA------MPGGGKFRTKVPEM 152
Cdd:COG1524 94 PELGRVVNSLSWVED------------GFGSNSLLPVPTIF--------ERARAAglTTAavfwpsFEGSGLIDAARPYP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 153 VDGKATRVSSYSNaetgryepgeqyyfDSYFTEMALEGLRRRDTtkplllnamflaphpplqipdpwyravgaeDFALpe 232
Cdd:COG1524 154 YDGRKPLLGNPAA--------------DRWIAAAALELLREGRP------------------------------DLLL-- 187
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2629630740 233 nigVYYPRqsplqmynlTGIVGTRYGREHWKeawrvYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHG 305
Cdd:COG1524 188 ---VYLPD---------LDYAGHRYGPDSPE-----YRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
2-396 |
1.84e-15 |
|
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: 78.66 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRYDVLG-----KGFTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGSLI------NPWE 70
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGvfgepSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTtnaharNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 71 PADAVYGDVRPEFGSLYTMMERDWDSIHSGKQHLFTTGGKLEDRVDSDtRWFSTEKSYKeflkehrvampgGGKFRTKVP 150
Cdd:cd16157 81 PQNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFD-EWFGAPNCHF------------GPYDNKAYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 151 emvdgkatRVSSYSNAE-TGRYEpgEQYYFD-----SYFTEM----ALEGL-RRRDTTKPLLLNAMFLAPHPPLQIPDPw 219
Cdd:cd16157 148 --------NIPVYRDWEmIGRYY--EEFKIDkktgeSNLTQIylqeALEFIeKQHDAQKPFFLYWAPDATHAPVYASKP- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 220 yravgaedFALPENIGvyyprqsplqmynltgivgtRYGrehwkeawrvylGLVRMLDHCVGRVLEELKRQGIYDDSLIL 299
Cdd:cd16157 217 --------FLGTSQRG--------------------LYG------------DAVMELDSSVGKILESLKSLGIENNTFVF 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 300 FTSDHGEML-------GSHGLF--QKMCMYEESARVPLFMKFPKGFTPSDKSYgQVVSHIDVLPTLCDY--LQMDSGNEM 368
Cdd:cd16157 257 FSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPGHIKPGQVSH-QLGSLMDLFTTSLALagLPIPSDRAI 335
|
410 420
....*....|....*....|....*...
gi 2629630740 369 DGTSLMPLLRgESRAEDRNSAYiqYDGN 396
Cdd:cd16157 336 DGIDLLPVLL-NGKEKDRPIFY--YRGD 360
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
3-440 |
2.69e-15 |
|
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: 77.19 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRY-DV------LGKGF-TPNIDSIAADGTAFGRAYcACPLCVPARGSFFTGTYPNRNGSL--------- 65
Cdd:cd16142 1 PNILVILGDDIGWgDLgcygggIGRGApTPNIDRLAKEGLRFTSFY-VEPSCTPGRAAFITGRHPIRTGLTtvglpgspg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 66 -INPWEPADAvygdvrpEFGSlytmmERDWDSIHSGKQHLfttgGkledrvDSDTRWfSTEKSYKEFlkehrvampgggk 144
Cdd:cd16142 80 gLPPWEPTLA-------ELLK-----DAGYATAQFGKWHL----G------DEDGRL-PTDHGFDEF------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 145 frtkvpemvdgkatrvssYSNAEtgryepgeqYYFDSYFTEMALEGLRRR-DTTKPLLLNAMFLAPHPPlqipdpwyrav 223
Cdd:cd16142 124 ------------------YGNLY---------HTIDEEIVDKAIDFIKRNaKADKPFFLYVNFTKMHFP----------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 224 gaeDFALPENIGvyyprQSPlqmynltgivgtrygrehwkeAWRVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSD 303
Cdd:cd16142 166 ---TLPSPEFEG-----KSS---------------------GKGKYADSMVELDDHVGQILDALDELGIADNTIVIFTTD 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 304 HGEML-----GSHGLF--QKMCMYEESARVPLFMKFPkGFTPSDKSYGQVVSHIDVLPTLcdyLQMdSGNEM-------- 368
Cdd:cd16142 217 NGPEQdvwpdGGYTPFrgEKGTTWEGGVRVPAIVRWP-GKIKPGRVSNEIVSHLDWFPTL---AAL-AGAPDpkdkllgk 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 369 ----DGTSLMPLLRGESRAEDRNSAYIQYDGNgsrsnfQRCMIWGRWKLIVDLFKDE-----------TFYELYDLEEDV 433
Cdd:cd16142 292 drhiDGVDQSPFLLGKSEKSRRSEFFYFGEGE------LGAVRWKNWKVHFKAQEDTggptgepfyvlTFPLIFNLRRDP 365
|
....*..
gi 2629630740 434 QETSNLM 440
Cdd:cd16142 366 KERYDVT 372
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
2-384 |
7.17e-15 |
|
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: 76.70 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRY-DVLGKG-----FTPnIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGslinpwepadaV 75
Cdd:cd16160 1 KPNIVLFFADDMGYgDLASYGhptqeRGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSG-----------M 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 76 YGDVRPEFGSLYTMMERDWDSIHSG-KQHLFTTG--GKLEDRVDSDTRwfstekSYKEFLKEHR------VAMPGGGKFR 146
Cdd:cd16160 69 YGGTRVFLPWDIGGLPKTEVTMAEAlKEAGYTTGmvGKWHLGINENNH------SDGAHLPSHHgfdfvgTNLPFTNSWA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 147 ---TKVPemVDGKATRVSSYSNAETGRYEPgeqYYFDsYFTEMALEGLRRRDTT---KPLLLNAMFLAPHPPLqipdpwy 220
Cdd:cd16160 143 cddTGRH--VDFPDRSACFLYYNDTIVEQP---IQHE-HLTETLVGDAKSFIEDnqeNPFFLYFSFPQTHTPL------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 221 raVGAEDFALPENIGvyyprqsplqmynltgivgtRYGREhwkeawrvylglVRMLDHCVGRVLEELKRQGIYDDSLILF 300
Cdd:cd16160 210 --FASKRFKGKSKRG--------------------RYGDN------------INEMSWAVGEVLDTLVDTGLDQNTLVFF 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 301 TSDHGEML------GSHGLFQ--KMCMYEESARVPLFMKFPKGFTPSDKSygQVVSHIDVLPTLCDYlqmdSGNEM---- 368
Cdd:cd16160 256 LSDHGPHVeyclegGSTGGLKggKGNSWEGGIRVPFIAYWPGTIKPRVSH--EVVSTMDIFPTFVDL----AGGTLptdr 329
|
410
....*....|....*...
gi 2629630740 369 --DGTSLMPLLRGESRAE 384
Cdd:cd16160 330 iyDGLSITDLLLGEADSP 347
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
3-358 |
2.58e-13 |
|
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: 69.37 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLGKG-----FTPNIDSIAADGTAFgRAYCACPLC--VPARGSFFTGTYPNRNGSLINPWEpadav 75
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAgnpapTTPNLKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 76 ygdvRPEFGSlytmmerdwdsihsgkqhlftTGGKLEDRVDSdtrwfsteksykeflkehrvampgggkfrtkVPEMVDG 155
Cdd:cd00016 75 ----DPELPS---------------------RAAGKDEDGPT-------------------------------IPELLKQ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 156 KATRVSSYsnaetgryepgeqyYFDSYFTEMALEglrrrdttKPLLLNAMFLAPHPPlqipdpwyravgaedfalpeniG 235
Cdd:cd00016 99 AGYRTGVI--------------GLLKAIDETSKE--------KPFVLFLHFDGPDGP----------------------G 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 236 VYYPRQSPlqmynltgivgtrygrehwkeawrVYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGEMLGSHGLFQ 315
Cdd:cd00016 135 HAYGPNTP------------------------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDP 190
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2629630740 316 KMCMYEESA----RVPLFMKFPKGFTPSDKSygQVVSHIDVLPTLCD 358
Cdd:cd00016 191 KADGKADKShtgmRVPFIAYGPGVKKGGVKH--ELISQYDIAPTLAD 235
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
2-381 |
2.95e-13 |
|
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: 71.94 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRYDVLGkGF------TPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNR------NGSLINPW 69
Cdd:cd16159 1 KPNIVLFMADDLGIGDVG-CFgndtirTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRsgmassHGMRVILF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 70 EpadAVYGDVRPEFGSLYTMMerdwdsihsgKQHLFTTG--GKLEDRVDSDTR--------------WFSTEKS-YKEFL 132
Cdd:cd16159 80 T---ASSGGLPPNETTFAEVL----------KQQGYSTAliGKWHLGLHCESRndfchhplnhgfdyFYGLPLTnLKDCG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 133 KEHRVAMPGGGK-FRTKVPEMV--DGKATRVSSYSNAETGR---------------------------------YEPGEQ 176
Cdd:cd16159 147 DGSNGEYDLSFDpLFPLLTAFVliTALTIFLLLYLGAVSKRffvfllilsllfislfflllitnryfncilmrnHEVVEQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 177 YY----FDSYFTEMALEGLRRRdTTKPLLLNAMFLAPHPPLqipdpwyravgaedFALPENIGVyyprqsplqmynltgi 252
Cdd:cd16159 227 PMslenLTQRLTKEAISFLERN-KERPFLLVMSFLHVHTAL--------------FTSKKFKGR---------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 253 vgTRYGRehwkeawrvYLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHG----------EMLGSHGLF---QKMCM 319
Cdd:cd16159 276 --SKHGR---------YGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGghleeisvggEYGGGNGGIyggKKMGG 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2629630740 320 YEESARVPLFMKFPKGFTPsdksyGQVV----SHIDVLPTLCDY--LQMDSGNEMDGTSLMPLLRGES 381
Cdd:cd16159 345 WEGGIRVPTIVRWPGVIPP-----GSVIdeptSLMDIFPTVAALagAPLPSDRIIDGRDLMPLLTGQE 407
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
2-395 |
5.75e-13 |
|
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: 70.19 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRYDVLG------KGFTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGslinpwepadaV 75
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGanwapnAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNG-----------V 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 76 YGDVRPEfgslytmmerdwdsihsgkqhlfTTGGkLEdrvdsdtrwfsteksykefLKEhrvampgggkfrTKVPEmvdg 155
Cdd:cd16161 70 GHNFLPT-----------------------SVGG-LP-------------------LNE------------TTLAE---- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 156 kATRVSSYSNAETGRYEPG--EQYY-----FDSYF--------------TEMALEGLRR-RDTTKPLLLNAMFLAPHPPL 213
Cdd:cd16161 91 -VLRQAGYATGMIGKWHLGqrEAYLpnsrgFDYYFgipfshdssladryAQFATDFIQRaSAKDRPFFLYAALAHVHVPL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 214 qipdpwyravgaedfalpeniGVYYPRQSPLQmynltgiVGTRYGREHWKeawrvylglvrmLDHCVGRVLEELKRQGIY 293
Cdd:cd16161 170 ---------------------ANLPRFQSPTS-------GRGPYGDALQE------------MDDLVGQIMDAVKHAGLK 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 294 DDSLILFTSD---------------HGEMLGSHGL-FQKMCMYEESARVPLFMKFPkGFTPSDKSYGQVVSHIDVLPTLC 357
Cdd:cd16161 210 DNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGsVAKASTWEGGHREPAIVYWP-GRIPANSTSAALVSTLDIFPTVV 288
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2629630740 358 DYLQ--MDSGNEMDGTSLMPLLRGESRAEDR-----NSAYIQYDG 395
Cdd:cd16161 289 ALAGasLPPGRIYDGKDLSPVLFGGSKTGHRclfhpNSGAAGAGA 333
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
366-465 |
6.41e-13 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 64.58 E-value: 6.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 366 NEMDGTSLMPLLRGESRAEDRNSAYIQYDGNGSRSNFQRCmiWG----RWKLIvDLFKDETFYELYDLEEDVQETSNLMF 441
Cdd:pfam16347 3 ADMQGKSFLPLLKGKKPKNWRDALYYHYYEYPAEHAVKRH--YGvrteRYKLI-HFYNDIDEWELYDLQKDPKEMNNVYG 79
|
90 100
....*....|....*....|....
gi 2629630740 442 DGKHDEIAEEMANRLAAHSRETGD 465
Cdd:pfam16347 80 DPEYAEVQAELKEELEELRKQYKD 103
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
3-436 |
8.90e-12 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 66.60 E-value: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVL-------GKGFTPNIDSIAADGTAFGRAYcACPLCVPARGSFFTGTYPNRNGSLINPWEPADAV 75
Cdd:cd16154 1 PNILLIIADDQGLDSSaqyslssDLPVTPTLDSLANSGIVFDNLW-ATPACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 76 YGDVRPEFGSLYTmmeRDWDSIHSGKQHLfttGGKLedrvdsdtrwfsteksykeflkEHRVAMPGGGKFrtkvpEMVDG 155
Cdd:cd16154 80 ETLLQLLIKDATT---AGYSSAVIGKWHL---GGND----------------------NSPNNPGGIPYY-----AGILG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 156 KAtrVSSYSN---AETGRYEPGEQYYfDSYFTEMALEGLrrRDTTKPLLLNAMFLAPHPPLQIPdpwyravgaedfalpe 232
Cdd:cd16154 127 GG--VQDYYNwnlTNNGQTTNSTEYA-TTKLTNLAIDWI--DQQTKPWFLWLAYNAPHTPFHLP---------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 233 nigvyyprqsPLQMYNlTGIVGTRYGREHWKEAWrvYLGLVRMLDHCVGRVLEELKrQGIYDDSLILFTSDHG------- 305
Cdd:cd16154 186 ----------PAELHS-RSLLGDSADIEANPRPY--YLAAIEAMDTEIGRLLASID-EEERENTIIIFIGDNGtpgqvvd 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 306 EMLGSHGlfQKMCMYEESARVPLfMKFPKGFTPSDKSYGQVVSHIDVLPTLCDYLQMDSGNEMDGTSLMPLLRGESRAEd 385
Cdd:cd16154 252 LPYTRNH--AKGSLYEGGINVPL-IVSGAGVERANERESALVNATDLYATIAELAGVDAAEIHDSVSFKPLLSDVNAST- 327
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2629630740 386 RNSAYIQYDGNGSRSNFQRCmiwGRWKLIVdlFKDETfYELYDLEEDVQET 436
Cdd:cd16154 328 RQYNYTEYESPTTTGWATRN---QYYKLIE--SENGQ-EELYDLINDPSEQ 372
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
2-377 |
9.92e-11 |
|
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: 63.62 E-value: 9.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 2 KPHVIIIMADQLRYDVLG-----KGFTPNIDSIAADGTAFGRAYCACPLCVPARGSFFTGTYPNRNGslinpwepadaVY 76
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGcyghpSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSG-----------VY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 77 GDVrpefgslytmmerdWDSIHSGkqhlfttGGKLEdrvdsdtrwfstEKSYKEFLKEHRVAMPGGGKFRTKVpemvdgk 156
Cdd:cd16158 70 PGV--------------FYPGSRG-------GLPLN------------ETTIAEVLKTVGYQTAMVGKWHLGV------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 157 atrvssysnAETGRYEPGEQyYFDSYF-------------------TEMALEGLRRRDTTKPLLLNAMFLAPHPPLQIPD 217
Cdd:cd16158 110 ---------GLNGTYLPTHQ-GFDHYLgipyshdqgpcqnltcfppNIPCFGGCDQGEVPCPLFYNESIVQQPVDLLTLE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 218 PWYRAVgAEDF---ALPENIG--VYYPRQSplqmynltgivgTRY----GREHWKEAWRVYLGLVRM-LDHCVGRVLEEL 287
Cdd:cd16158 180 ERYAKF-AKDFiadNAKEGKPffLYYASHH------------THYpqfaGQKFAGRSSRGPFGDALAeLDGSVGELLQTL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 288 KRQGIYDDSLILFTSDHGEML------GSHGLFQ--KMCMYEESARVPLFMKFPKGFTPSDKSygQVVSHIDVLPTLCDY 359
Cdd:cd16158 247 KENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcgKGTTYEGGVREPAIAYWPGRIKPGVTH--ELASTLDILPTIAKL 324
|
410
....*....|....*....
gi 2629630740 360 LQMDSGN-EMDGTSLMPLL 377
Cdd:cd16158 325 AGAPLPNvTLDGVDMSPIL 343
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
3-358 |
1.11e-08 |
|
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: 56.05 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 3 PHVIIIMADQLRYDVLGK-GFTPNIDSIAADGTAFGRAYCACP-LCVPARGSFFTGTYPNRNGslinpwepadaVYGDVR 80
Cdd:cd16018 1 PPLIVISIDGFRWDYLDRaGLTPNLKRLAEEGVRAKYVKPVFPtLTFPNHYSIVTGLYPESHG-----------IVGNYF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 81 --PEFGSLYTMMERDWDSihsgkqhlfttggkleDRVDSDTRWFSTEKSYKeflkehRVAM---PGGGKfrtkvpemvdg 155
Cdd:cd16018 70 ydPKTNEEFSDSDWVWDP----------------WWIGGEPIWVTAEKAGL------KTASyfwPGSEV----------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 156 katRVSSYSNAETGRYEPGEQYYFDSYFTEMALEGLRRRDTTKPlllnamflaphpplqipdpwyravgaeDFALpenig 235
Cdd:cd16018 117 ---AIIGYNPTPIPLGGYWQPYNDSFPFEERVDTILEWLDLERP---------------------------DLIL----- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 236 VYYPRqsplqmynlTGIVGTRYGREHwKEAWRVylglVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGeM--LGSHG- 312
Cdd:cd16018 162 LYFEE---------PDSAGHKYGPDS-PEVNEA----LKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG-MtdVGTHGy 226
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2629630740 313 LFQKMCMYeesarvPLFMkfpkGFTPSDKSYGQVVSH--IDVLPTLCD 358
Cdd:cd16018 227 DNELPDMR------AIFI----ARGPAFKKGKKLGPFrnVDIYPLMCN 264
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
5-305 |
2.53e-07 |
|
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: 52.42 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 5 VIIIMADQLRYDVLGK-GFTPNIDSIAADGTAFGRAYCACP-LCVPARGSFFTGTYPNRNGslinpwepadaVYGDvrpe 82
Cdd:pfam01663 1 LLVISLDGFRADYLDRfELTPNLAALAKEGVSAPNLTPVFPtLTFPNHYTLVTGLYPGSHG-----------IVGN---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 83 fgslyTMMERdwdsiHSGKQHLFTTGGKLedrvdsDTRWFSTEKSY-KEFLKEHRVAM---PGggkfrtkvpemvdgkat 158
Cdd:pfam01663 66 -----TFYDP-----KTGEYLVFVISDPE------DPRWWQGEPIWdTAAKAGVRAAAlfwPG----------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 159 rvSSYSNAETGRYEPGeqyYFDSYFTemALEGLRRRDTTkpLLLNAMFLAPHPPLQIPDPwyravgaeDFALpenigVYY 238
Cdd:pfam01663 113 --SEVDYSTYYGTPPR---YLKDDYN--NSVPFEDRVDT--AVLQTWLDLPFADVAAERP--------DLLL-----VYL 170
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2629630740 239 PRqsplqmynlTGIVGTRYGREHwkEAWRVYLglvRMLDHCVGRVLEELKRQGIYDDSLILFTSDHG 305
Cdd:pfam01663 171 EE---------PDYAGHRYGPDS--PEVEDAL---RRVDRAIGDLLEALDERGLFEDTNVIVVSDHG 223
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
273-360 |
5.97e-07 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 51.08 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 273 VRMLDHCVGRVLEELKRQGiyDDSLILFTSDHGEMLGSHGLF--QKMCMYEESARVPLFMKFPKGFTPSD------KSYG 344
Cdd:cd16017 192 ILYTDYVLSQIIERLKKKD--KDAALIYFSDHGESLGENGLYlhGAPYAPKEQYHVPFIIWSSDSYKQRYpverlrANKD 269
|
90
....*....|....*.
gi 2629630740 345 QVVSHIDVLPTLCDYL 360
Cdd:cd16017 270 RPFSHDNLFHTLLGLL 285
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
269-356 |
1.48e-06 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 50.67 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 269 YLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGE--------MLGSHGLFQkmcmyEESARVPLFMKFPkGFTPsd 340
Cdd:COG3083 429 YRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEefnengqnYWGHNSNFS-----RYQLQVPLVIHWP-GTPP-- 500
|
90
....*....|....*.
gi 2629630740 341 KSYGQVVSHIDVLPTL 356
Cdd:COG3083 501 QVISKLTSHLDIVPTL 516
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
277-357 |
2.15e-05 |
|
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 46.02 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 277 DHCVGRVLEELKRQGIYDDSLILFTSDHGeM--LGSHGlfqkMCMYEESaRVPLFMKFPK-----GFTPSDKSYGQVVSH 349
Cdd:cd16024 177 DDVIKRIYESLEEQSSNNPTLLVVCGDHG-MtdAGNHG----GSSPGET-SVPLLFISPKfsskpSNADGELSYYETVQQ 250
|
....*...
gi 2629630740 350 IDVLPTLC 357
Cdd:cd16024 251 VDLAPTLA 258
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
269-381 |
2.18e-04 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 43.49 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2629630740 269 YLGLVRMLDHCVGRVLEELKRQGIYDDSLILFTSDHGEMLGSH-GLFQKmcMYEEsaRVPL-FMKFPKGFTpsdKSYGQV 346
Cdd:pfam02995 306 DFNYASALDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKLrRTSQG--MLEE--RLPLmSIRYPPWFR---ETYPQA 378
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2629630740 347 V-----------SHIDVLPTLCDYLQMDSGNEMDGTSLMPLL---RGES 381
Cdd:pfam02995 379 VenlelnanrltTPFDLHATLKDILHLGELSDKELQDRMKALdcpRGIS 427
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
284-336 |
8.02e-03 |
|
uncharacterized Alkaline phosphatase subfamily; 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.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 38.27 E-value: 8.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2629630740 284 LEELKRQGIYDDSLILFTSDHGEMLGSHgLFQKMCMYEEsaRVPLF-MKFPKGF 336
Cdd:cd16021 193 LKRLKENGLLDNTFVIFMSDHGLRFGKI-RETLQGKLEE--RLPFLsISLPKWF 243
|
|
| |
