|
Name |
Accession |
Description |
Interval |
E-value |
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-467 |
0e+00 |
|
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: 555.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYNQGML-GYQTPNIDSIAAEGAKFTSYYAEQSSTAGRSSFITGQMPFRTGMSKVGMPGAPQG 122
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGrGAPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGLTTVGLPGSPGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 123 LQKEDPTIANILKQLGYATGQFGKNHLGDRNEFLPTAHGFDEFMGNLYHlnaeeepenpdypqdpeykkqfgprgvikst 202
Cdd:cd16142 81 LPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFYGNLYH------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 203 adgkiedtgplnikrmeTVDEETLAANNDFMERQVKANKPFFTWYNTTRMHNKTHIKPADKG-VTGLGDYADGMVEHDKI 281
Cdd:cd16142 130 -----------------TIDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGkSSGKGKYADSMVELDDH 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 282 IGEVLKKIKDLGIEDNTIVVYTTDNGPMTATWPDAGITPFRGEKNTGWEGGFRVPAMIKWPGHIKPGTLVNDIVGSNDWF 361
Cdd:cd16142 193 VGQILDALDELGIADNTIVIFTTDNGPEQDVWPDGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHLDWF 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 362 PTLVAAAGVPDIKQQLLKgyktsamnYKVHLDGYNQLDYITGKTQEDPRKEFFYWsDDGDLLAMRYGRWKAHFMIQEHTG 441
Cdd:cd16142 273 PTLAALAGAPDPKDKLLG--------KDRHIDGVDQSPFLLGKSEKSRRSEFFYF-GEGELGAVRWKNWKVHFKAQEDTG 343
|
410 420
....*....|....*....|....*.
gi 1222961955 442 MDVWkYPFVKLRVPLIFDLKIDPLEK 467
Cdd:cd16142 344 GPTG-EPFYVLTFPLIFNLRRDPKER 368
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
43-467 |
5.99e-116 |
|
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: 348.40 E-value: 5.99e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 43 KPNIVVIFGDDIGYWNLSTYnqGMLGYQTPNIDSIAAEGAKFTSYYAEQS-STAGRSSFITGQMPFRTGM-SKVGMPGAP 120
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCY--GSPLIKTPNIDRLAAEGVRFTDFYAAAPvCSPSRAALLTGRYPVRVGLpGVVGPPGSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 121 QGLQKEDPTIANILKQLGYATGQFGKNHLGDRNEFLPTAHGFDEFMGNLY-HLNAEEEPENPDYPQDPEYKKQfgPRGVI 199
Cdd:cd16026 79 GGLPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIPYsNDMWPFPLYRNDPPGPLPPLME--NEEVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 200 KSTADgkiedtgplnikrMETVDEE-TLAANnDFMERQvkANKPFFTWYNTTRMHNKTHIKPADKGVTGLGDYADGMVEH 278
Cdd:cd16026 157 EQPAD-------------QSSLTQRyTDEAV-DFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEEL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 279 DKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMTATWPDAGIT-PFRGEKNTGWEGGFRVPAMIKWPGHIKPGTLVNDIVGS 357
Cdd:cd16026 221 DWSVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHGGSAgPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELAST 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 358 NDWFPTLVAAAGVPdikqqllkgyktsaMNYKVHLDGYNQLDYITGKTQEdPRKEFFYWSDDGDLLAMRYGRWKAHFMIQ 437
Cdd:cd16026 301 MDLLPTLAALAGAP--------------LPEDRVIDGKDISPLLLGGSKS-PPHPFFYYYDGGDLQAVRSGRWKLHLPTT 365
|
410 420 430
....*....|....*....|....*....|
gi 1222961955 438 EHTGMDVWKYPFVKLRVPLIFDLKIDPLEK 467
Cdd:cd16026 366 YRTGTDPGGLDPTKLEPPLLYDLEEDPGET 395
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
34-467 |
1.19e-100 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 308.73 E-value: 1.19e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 34 STAPEQNKGKPNIVVIFGDDIGYWNLSTYNQGMlgYQTPNIDSIAAEGAKFTSYYAEQSS-TAGRSSFITGQMPFRTGMS 112
Cdd:COG3119 14 AAAAAAAAKRPNILFILADDLGYGDLGCYGNPL--IKTPNIDRLAAEGVRFTNAYVTSPVcSPSRASLLTGRYPHRTGVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 113 KVGmPGAPQGLQKEDPTIANILKQLGYATGQFGKNHLgdrneflptahgfdefmgnlyhlnaeeepenpdypqdpeykkq 192
Cdd:COG3119 92 DNG-EGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 193 fgprgvikstadgkiedtgplnikrmeTVDEETLAANNDFMERQVKANKPFFTWYNTTRMHNKTHIKP------------ 260
Cdd:COG3119 128 ---------------------------YLTDLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEeyldkydgkdip 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 261 -----------ADKGVTGLGDYADGMVEHDKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMtatWPDAGitpFRGEKNTGW 329
Cdd:COG3119 181 lppnlaprdltEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS---LGEHG---LRGGKGTLY 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 330 EGGFRVPAMIKWPGHIKPGTLVNDIVGSNDWFPTLVAAAGVPdikqqllkgyktsamnYKVHLDGYNQLDYITGKTQEDP 409
Cdd:COG3119 255 EGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVP----------------IPEDLDGRSLLPLLTGEKAEWR 318
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1222961955 410 RKEFFYWSDDGDLLAMRYGRWKAHfmiqehtgmdvwkYPFVKLRVPLIFDLKIDPLEK 467
Cdd:COG3119 319 DYLYWEYPRGGGNRAIRTGRWKLI-------------RYYDDDGPWELYDLKNDPGET 363
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-467 |
4.71e-82 |
|
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: 260.60 E-value: 4.71e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYNQGMLgYQTPNIDSIAAEGAKFTSYYAEQS-STAGRSSFITGQMPFRTGMSKVGMPG-APQ 121
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDSK-IPTPNIDRLAAEGMRFTDAHSPSSvCTPSRYGLLTGRYPWRSRLKGGVLGGfSPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 122 GLQKEDPTIANILKQLGYATGQFGKNHLGdrneflptahgFDefmgnlyhlnaeeepenpDYPQDPEYKKQFGPRGVIKS 201
Cdd:cd16143 80 LIEPDRVTLAKMLKQAGYRTAMVGKWHLG-----------LD------------------WKKKDGKKAATGTGKDVDYS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 202 tadGKIEDtGPL-----------NIKRMETVDEETLaannDFMERQVKANKPFFTWYNTTRMHnkTHIKPAD--KGVTGL 268
Cdd:cd16143 131 ---KPIKG-GPLdhgfdyyfgipASEVLPTLTDKAV----EFIDQHAKKDKPFFLYFALPAPH--TPIVPSPefQGKSGA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 269 GDYADGMVEHDKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMTATWPDAGIT-------PFRGEKNTGWEGGFRVPAMIKW 341
Cdd:cd16143 201 GPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPYADYKELEKfghdpsgPLRGMKADIYEGGHRVPFIVRW 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 342 PGHIKPGTLVNDIVGSNDWFPTLVAAAGVPdikqqllkgYKTSAMnykvhLDGYNQLDYITGKTQEDPRKEFFYWSDDGD 421
Cdd:cd16143 281 PGKIPAGSVSDQLVSLTDLFATLAAIVGQK---------LPDNAA-----EDSFSFLPALLGPKKQEVRESLVHHSGNGS 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1222961955 422 lLAMRYGRWKahfMIqEHTGMDVWKYPFVKLRVPL----IFDLKIDPLEK 467
Cdd:cd16143 347 -FAIRKGDWK---LI-DGTGSGGFSYPRGKEKLGLppgqLYNLSTDPGES 391
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-431 |
8.11e-76 |
|
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: 245.53 E-value: 8.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYnqGMLGYQTPNIDSIAAEGAKFTSYYAEQS-STAGRSSFITGQMPFRTGMSKVGMPGAP-- 120
Cdd:cd16144 1 PNIVLILVDDLGWADLGCY--GSKFYETPNIDRLAKEGMRFTQAYAAAPvCSPSRASILTGQYPARLGITDVIPGRRGpp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 121 -----------QGLQKEDPTIANILKQLGYATGQFGKNHLGDRNEFLPTAHGFDE-FMGNLYHlnaeeepeNPDYPQDPE 188
Cdd:cd16144 79 dntklipppstTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVnIGGTGNG--------GPPSYYFPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 189 YKKQFGPrgvikstadgKIEDTGPlniKRMETVDEETLaannDFMERQvkANKPFFT--WYNTtrMHNKTHIKPAD---- 262
Cdd:cd16144 151 GKPNPDL----------EDGPEGE---YLTDRLTDEAI----DFIEQN--KDKPFFLylSHYA--VHTPIQARPELieky 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 263 -KGVTGLGD------YAdGMVEH-DKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMTATWPDAGIT-PFRGEKNTGWEGGF 333
Cdd:cd16144 210 eKKKKGLRKgqknpvYA-AMIESlDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTSNaPLRGGKGSLYEGGI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 334 RVPAMIKWPGHIKPGTLVNDIVGSNDWFPTLVAAAGVPDIKQQllkgyktsamnykvHLDGYNQLDYITGKTQEDPRKEF 413
Cdd:cd16144 289 RVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPQ--------------HLDGVSLVPLLKGGEADLPRRAL 354
|
410 420
....*....|....*....|....
gi 1222961955 414 F----YWSDDGDLL--AMRYGRWK 431
Cdd:cd16144 355 FwhfpHYHGQGGRPasAIRKGDWK 378
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-467 |
5.91e-75 |
|
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: 242.89 E-value: 5.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYNQGMLgyQTPNIDSIAAEGAKFTSYYAEQSSTA-GRSSFITGQMPFRTGMSKVGMPGAPQG 122
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKI--KTPNLDRLAAEGMRFTQHYAGAPVCApSRASLLTGLHTGHTRVRGNSEPGGQDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 123 LQKEDPTIANILKQLGYATGQFGKNHLGDR-NEFLPTAHGFDEFMGNLYHLNAEEEpenpdYPqdpEYKKQFGPRGVIKS 201
Cdd:cd16145 79 LPPDDVTLAEVLKKAGYATAAFGKWGLGGPgTPGHPTKQGFDYFYGYLDQVHAHNY-----YP---EYLWRNGEKVPLPN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 202 TADGKIEDTGPLNIKRMETVDEETLAANNDFMERQvkANKPFFTWYNTTRMHNKTHI--------KPADKGVTGLGD--- 270
Cdd:cd16145 151 NVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIREN--KDKPFFLYLAYTLPHAPLQVpddgpykyKPKDPGIYAYLPwpq 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 271 ----YAdGMVEH-DKIIGEVLKKIKDLGIEDNTIVVYTTDNGPM-------TATWPDAGiTPFRGEKNTGWEGGFRVPAM 338
Cdd:cd16145 229 pekaYA-AMVTRlDRDVGRILALLKELGIDENTLVVFTSDNGPHseggsehDPDFFDSN-GPLRGYKRSLYEGGIRVPFI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 339 IKWPGHIKPGTLVNDIVGSNDWFPTLVAAAGVPDikqqllkgyktsamnyKVHLDGYNQLDYITGKTQEDPRkEFFYW-- 416
Cdd:cd16145 307 ARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEP----------------PEDIDGISLLPTLLGKPQQQQH-DYLYWef 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1222961955 417 SDDGDLLAMRYGRWKAhfmIQehtgMDVWKYPFvklrvpLIFDLKIDPLEK 467
Cdd:cd16145 370 YEGGGAQAVRMGGWKA---VR----HGKKDGPF------ELYDLSTDPGET 407
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
44-467 |
2.38e-73 |
|
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: 238.60 E-value: 2.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYNQGMLgyQTPNIDSIAAEGAKFTSYYAEQSSTAGRSSFITGQMPFRTGMSKVGMPGAPqgL 123
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPIL--KTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTGVWHTILGRER--M 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 124 QKEDPTIANILKQLGYATGQFGKNHLGDRNEFLPTAHGFDEFMGN-LYHLNaeeepENPDYPQDPEYKKQFGPRGVIKST 202
Cdd:cd16146 77 RLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHgGGGIG-----QYPDYWGNDYFDDTYYHNGKFVKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 203 aDGKIEDTgplnikrmetVDEETLaannDFMERQvkANKPFFTWYNTTRMHNKTHIKPADkgvtgLGDYAD--------- 273
Cdd:cd16146 152 -EGYCTDV----------FFDEAI----DFIEEN--KDKPFFAYLATNAPHGPLQVPDKY-----LDPYKDmglddklaa 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 274 --GMVEH-DKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMTATW--PDAGitpFRGEKNTGWEGGFRVPAMIKWPGHIKPG 348
Cdd:cd16146 210 fyGMIENiDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPkrFNAG---MRGKKGSVYEGGHRVPFFIRWPGKILAG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 349 TLVNDIVGSNDWFPTLVAAAGVPDIKqqllkgyktsamnyKVHLDGYNQLDYITGKTQEDPRKEFFYWSDDGDLL----- 423
Cdd:cd16146 287 KDVDTLTAHIDLLPTLLDLCGVKLPE--------------GIKLDGRSLLPLLKGESDPWPERTLFTHSGRWPPPpkkkr 352
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1222961955 424 --AMRYGRWKahfMIQEHTGMdvwkypfvklrvPLIFDLKIDPLEK 467
Cdd:cd16146 353 naAVRTGRWR---LVSPKGFQ------------PELYDIENDPGEE 383
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
43-467 |
2.84e-69 |
|
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: 229.24 E-value: 2.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 43 KPNIVVIFGDDIGYWNLSTYnqgmlGYQTPN---IDSIAAEGAKFTSYYAEQS-STAGRSSFITGQMPFRTGM---SKVG 115
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASY-----GHPTQErgpIDDMAAEGIRFTQAYSADSvCTPSRAALLTGRLPIRSGMyggTRVF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 116 MPGAPQGLQKEDPTIANILKQLGYATGQFGKNHLG------DRNEFLPTAHGFDeFMG-NLYHLNAEEEPENPDYPQDPE 188
Cdd:cd16160 76 LPWDIGGLPKTEVTMAEALKEAGYTTGMVGKWHLGinennhSDGAHLPSHHGFD-FVGtNLPFTNSWACDDTGRHVDFPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 189 YKKQFgprgviKSTADGKIEDtgPLNIKRM-ETVDEETLAanndFMERQVkaNKPFFTWYNTTRMHNKTHIKPADKGVTG 267
Cdd:cd16160 155 RSACF------LYYNDTIVEQ--PIQHEHLtETLVGDAKS----FIEDNQ--ENPFFLYFSFPQTHTPLFASKRFKGKSK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 268 LGDYADGMVEHDKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMTATWPDAGIT-PFRGEKNTGWEGGFRVPAMIKWPGHIK 346
Cdd:cd16160 221 RGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTgGLKGGKGNSWEGGIRVPFIAYWPGTIK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 347 PGtLVNDIVGSNDWFPTLVAAAGvpdikqqllkgyktSAMNYKVHLDGYNQLDYITGKTQEDPRKEFFYWSDdgDLLAMR 426
Cdd:cd16160 301 PR-VSHEVVSTMDIFPTFVDLAG--------------GTLPTDRIYDGLSITDLLLGEADSPHDDILYYCCS--RLMAVR 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222961955 427 YGRWKAHFMIQE-HTGM--------DVWKYPF-----------VKLRVPLIFDLKIDPLEK 467
Cdd:cd16160 364 YGSYKIHFKTQPlPSQEsldpncdgGGPLSDYivcydcedecvTKHNPPLIFDVEKDPGEQ 424
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
43-466 |
1.54e-68 |
|
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: 225.43 E-value: 1.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 43 KPNIVVIFGDDIGyWNLSTYNQGMLGYQTPNIDSIAAEGAKFTSYYAEQSS-TAGRSSFITGQMPFRTGMSKVGMPGAPQ 121
Cdd:cd16161 1 KPNFLLLFADDLG-WGDLGANWAPNAILTPNLDKLAAEGTRFVDWYSAASVcSPSRASLMTGRLGLRNGVGHNFLPTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 122 GLQKEDPTIANILKQLGYATGQFGKNHLGDRNEFLPTAHGFDEFMGnlyhlnaeeepenpdypqdpeykkqfgprgvIKS 201
Cdd:cd16161 80 GLPLNETTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFG-------------------------------IPF 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 202 TADGKIEDtgplnikrmETVDEETlaannDFMERQVKANKPFFTWYNTTRMH-NKTHIKPADKGVTGLGDYADGMVEHDK 280
Cdd:cd16161 129 SHDSSLAD---------RYAQFAT-----DFIQRASAKDRPFFLYAALAHVHvPLANLPRFQSPTSGRGPYGDALQEMDD 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 281 IIGEVLKKIKDLGIEDNTIVVYTTDNGPMTA---------TWPDAGITPFRGEKNTGWEGGFRVPAMIKWPGHIKPGTLV 351
Cdd:cd16161 195 LVGQIMDAVKHAGLKDNTLTWFTSDNGPWEVkcelavgpgTGDWQGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTS 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 352 NDIVGSNDWFPTLVAAAGVPdikqqlLKGYKTsamnykvhLDGYNQLDYITGKTQeDPRKEFFYWSDD----GDLLAMRY 427
Cdd:cd16161 275 AALVSTLDIFPTVVALAGAS------LPPGRI--------YDGKDLSPVLFGGSK-TGHRCLFHPNSGaagaGALSAVRC 339
|
410 420 430
....*....|....*....|....*....|....*....
gi 1222961955 428 GRWKAHFMIQEHTGMDVWKYPFVKLRVPLIFDLKIDPLE 466
Cdd:cd16161 340 GDYKAHYATGGALACCGSTGPKLYHDPPLLFDLEVDPAE 378
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-467 |
1.18e-66 |
|
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: 220.16 E-value: 1.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYnqGMLGYQTPNIDSIAAEGAKFTSYYAEQSSTAGRSSFITGQMPFRTGMskvgmpgAPQGL 123
Cdd:cd16151 1 PNIILIMADDLGYECIGCY--GGESYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYV-------VFGYL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 124 QKEDPTIANILKQLGYATGQFGKNHLG--DRNEFLPTAHGFDEFMgnLYHLNAEEEPENPdypqdPEYKKQFGPRGVIKS 201
Cdd:cd16151 72 DPKQKTFGHLLKDAGYATAIAGKWQLGggRGDGDYPHEFGFDEYC--LWQLTETGEKYSR-----PATPTFNIRNGKLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 202 TADGKIedtGPlnikrmetvDeetLAAN--NDFMERQvkANKPFFTWYNTTRMHNKT-------HIKPADKGVTGLGDYA 272
Cdd:cd16151 145 TTEGDY---GP---------D---LFADflIDFIERN--KDQPFFAYYPMVLVHDPFvptpdspDWDPDDKRKKDDPEYF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 273 DGMVEH-DKIIGEVLKKIKDLGIEDNTIVVYTTDNG--PMTATWPDAGITpfRGEKNTGWEGGFRVPAMIKWPGHIKPGT 349
Cdd:cd16151 208 PDMVAYmDKLVGKLVDKLEELGLRENTIIIFTGDNGthRPITSRTNGREV--RGGKGKTTDAGTHVPLIVNWPGLIPAGG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 350 LVNDIVGSNDWFPTLVAAAGVPdikqqllkgyktsaMNYKVHLDGYNQLDYITGKTqEDPRKEFFYWSDDgdllamRYGR 429
Cdd:cd16151 286 VSDDLVDFSDFLPTLAELAGAP--------------LPEDYPLDGRSFAPQLLGKT-GSPRREWIYWYYR------NPHK 344
|
410 420 430
....*....|....*....|....*....|....*...
gi 1222961955 430 WKAHFMIQEHTgmdvWKYpFVKLRVpliFDLKIDPLEK 467
Cdd:cd16151 345 KFGSRFVRTKR----YKL-YADGRF---FDLREDPLEK 374
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
43-466 |
1.67e-66 |
|
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: 222.71 E-value: 1.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 43 KPNIVVIFGDDIGYWNLSTYnqGMLGYQTPNIDSIAAEGAKFTSYYAEQS-STAGRSSFITGQMPFRTGM-SKVGMPGAP 120
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCY--GHPSSSTPNLDRLAANGLRFTDFYSSSPvCSPSRAALLTGRYQVRSGVyPGVFYPGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 121 QGLQKEDPTIANILKQLGYATGQFGKNHLG--DRNEFLPTAHGFDEFMGNLY-HLNAEEEPENPDYPQDPEY---KKQFG 194
Cdd:cd16158 79 GGLPLNETTIAEVLKTVGYQTAMVGKWHLGvgLNGTYLPTHQGFDHYLGIPYsHDQGPCQNLTCFPPNIPCFggcDQGEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 195 PrgvIKSTADGKIEDTgPLNIKRMEtvdEETLAANNDFMERQVKANKPFFTWYNTTRMHNKTHIKPADKGVTGLGDYADG 274
Cdd:cd16158 159 P---CPLFYNESIVQQ-PVDLLTLE---ERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 275 MVEHDKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMTATWPDAGITPF-RGEKNTGWEGGFRVPAMIKWPGHIKPGtLVND 353
Cdd:cd16158 232 LAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRKSRGGNAGLlKCGKGTTYEGGVREPAIAYWPGRIKPG-VTHE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 354 IVGSNDWFPTLVAAAGVPdikqqlLKgyktsamnyKVHLDGYNqLDYITGKTQEDPRKEFFYWSDDGD----LLAMRYGR 429
Cdd:cd16158 311 LASTLDILPTIAKLAGAP------LP---------NVTLDGVD-MSPILFEQGKSPRQTFFYYPTSPDpdkgVFAVRWGK 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1222961955 430 WKAHFMIQ--EHTGM--DVWKYPFVKLRV---PLIFDLKIDPLE 466
Cdd:cd16158 375 YKAHFYTQgaAHSGTtpDKDCHPSAELTShdpPLLFDLSQDPSE 418
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
44-431 |
7.98e-64 |
|
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: 213.18 E-value: 7.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYNQGMLgyQTPNIDSIAAEGAKFTSYYAEQSSTAGRSSFITGQMPFRTGM-SKVGMPGAPQG 122
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQI--KTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMqHGVILAGEPYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 123 LQKEDPTIANILKQLGYATGQFGKNHLG-DRNEFLPTAHGFDEFMGnlYHLNAEeepenpDYpqdpeYKKqfgprgviks 201
Cdd:cd16029 79 LPLNETLLPQYLKELGYATHLVGKWHLGfYTWEYTPTNRGFDSFYG--YYGGAE------DY-----YTH---------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 202 tadgkIEDTGPLNIKRMETVDEETLAANND------FMERQVK------ANKPFFTW---------------YNTTRMHN 254
Cdd:cd16029 136 -----TSGGANDYGNDDLRDNEEPAWDYNGtystdlFTDRAVDiienhdPSKPLFLYlafqavhaplqvppeYADPYEDK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 255 KTHIKPADKGVtglgdYAdGMVEH-DKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMTATWPDAGITPFRGEKNTGWEGGF 333
Cdd:cd16029 211 FAHIKDEDRRT-----YA-AMVSAlDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGGSNYPLRGGKNTLWEGGV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 334 RVPAMIkWPGHIKP--GTLVNDIVGSNDWFPTLVAAAGVPDIKqqllkgyktsamnyKVHLDGYNQLDYITGKTQEdPRK 411
Cdd:cd16029 285 RVPAFV-WSPLLPPkrGTVSDGLMHVTDWLPTLLSLAGGDPDD--------------LPPLDGVDQWDALSGGAPS-PRT 348
|
410 420
....*....|....*....|....
gi 1222961955 412 EFFY----WSDDGDLLAMRYGRWK 431
Cdd:cd16029 349 EILLniddITRTTGGAAIRVGDWK 372
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
44-371 |
1.04e-63 |
|
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: 207.67 E-value: 1.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYNQGMLgyQTPNIDSIAAEGAKFTSYYAEQSS-TAGRSSFITGQMPFRTGMskVGMPGAPQG 122
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDI--KTPNLDRLAAEGVRFTNAYVASPVcSPSRASLLTGRYPHRHGV--RGNVGNGGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 123 LQKEDPTIANILKQLGYATGQFGKNHlgdrneflptahgfdefmgnlyhlnaeeepenpdypqdpeykkqfgprgvikst 202
Cdd:cd16022 77 LPPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 203 adgkiedtgplnikrmetvdEETLaannDFMERQVKaNKPFFTWYNTTRMHNKTHikpadkgvtglgdYAdGMVEH-DKI 281
Cdd:cd16022 103 --------------------DEAI----DFIERRDK-DKPFFLYVSFNAPHPPFA-------------YY-AMVSAiDDQ 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 282 IGEVLKKIKDLGIEDNTIVVYTTDNGPMTAtwpDAGItpfRGEKNTGWEGGFRVPAMIKWPGHIKPGTLVNDIVGSNDWF 361
Cdd:cd16022 144 IGRILDALEELGLLDNTLIVFTSDHGDMLG---DHGL---RGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLL 217
|
330
....*....|
gi 1222961955 362 PTLVAAAGVP 371
Cdd:cd16022 218 PTLLDLAGIE 227
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
43-434 |
1.15e-60 |
|
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: 206.93 E-value: 1.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 43 KPNIVVIFGDDIGYWNLSTYnqGMLGYQTPNIDSIAAEGAKFTSYY-AEQSSTAGRSSFITGQMPFRTGM----SKVGMP 117
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVF--GEPSRETPNLDRMAAEGMLFTDFYsANPLCSPSRAALLTGRLPIRNGFyttnAHARNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 118 GAPQ----GLQKEDPTIANILKQLGYATGQFGKNHLGDRNEFLPTAHGFDEFMG--NLYHlnaeEEPENPDYPQDPEYKK 191
Cdd:cd16157 79 YTPQnivgGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFGapNCHF----GPYDNKAYPNIPVYRD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 192 QfgpRGVIKSTADGKIE-DTGPLNIKRMETvdEETLaannDFMERQVKANKPFFTWYNTTRMHNKTHIKPADKGVTGLGD 270
Cdd:cd16157 155 W---EMIGRYYEEFKIDkKTGESNLTQIYL--QEAL----EFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTSQRGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 271 YADGMVEHDKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMTATWPDAGIT--PFRGEKNTGWEGGFRVPAMIKWPGHIKPG 348
Cdd:cd16157 226 YGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALISAPEQGGSngPFLCGKQTTFEGGMREPAIAWWPGHIKPG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 349 TLVNDIVGSNDWFPTLVAAAGVPDIKQQLlkgyktsamnykvhLDGYNQLDYITGKTQEDpRKEFFYWSDdgDLLAMRYG 428
Cdd:cd16157 306 QVSHQLGSLMDLFTTSLALAGLPIPSDRA--------------IDGIDLLPVLLNGKEKD-RPIFYYRGD--ELMAVRLG 368
|
....*.
gi 1222961955 429 RWKAHF 434
Cdd:cd16157 369 QYKAHF 374
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
43-468 |
5.96e-58 |
|
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: 200.98 E-value: 5.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 43 KPNIVVIFGDDIGYWNLSTYNQGMLgyQTPNIDSIAAEGAKFTSYYAEQS-STAGRSSFITGQMPFRTGMSKVGMP---- 117
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTI--RTPNIDRLAKEGVKLTHHLAAAPlCTPSRAAFLTGRYPIRSGMASSHGMrvil 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 118 --GAPQGLQKEDPTIANILKQLGYATGQFGKNHLG----DRNEFL--PTAHGFDEFMG-NLYHLNAEEEPENP--DYPQD 186
Cdd:cd16159 79 ftASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGlhceSRNDFChhPLNHGFDYFYGlPLTNLKDCGDGSNGeyDLSFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 187 PEYKKQFG--------PRGVIKSTADGK--------------------IEDTGPLNIKRMET-------VDEETLAAN-- 229
Cdd:cd16159 159 PLFPLLTAfvlitaltIFLLLYLGAVSKrffvfllilsllfislffllLITNRYFNCILMRNhevveqpMSLENLTQRlt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 230 ---NDFMERQVkaNKPFFTWYNTTRMHNKTHIKPADKGVTGLGDYADGMVEHDKIIGEVLKKIKDLGIEDNTIVVYTTDN 306
Cdd:cd16159 239 keaISFLERNK--ERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 307 GP---------MTATWpDAGItpFRGEKNTGWEGGFRVPAMIKWPGHIKPGTLVNDIVGSNDWFPTLVAAAGVPdikqql 377
Cdd:cd16159 317 GGhleeisvggEYGGG-NGGI--YGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAP------ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 378 lkgyktsaMNYKVHLDGYNQLDYITGKTqEDPRKEFFYWSDDGDLLAMRY------GRWKAHFMIQE-HTGMDVWKYPFV 450
Cdd:cd16159 388 --------LPSDRIIDGRDLMPLLTGQE-KRSPHEFLFHYCGAELHAVRYrprdggAVWKAHYFTPNfYPGTEGCCGTLL 458
|
490 500
....*....|....*....|....*..
gi 1222961955 451 ---------KLRVPLIFDLKIDPLEKG 468
Cdd:cd16159 459 crcfgdsvtHHDPPLLFDLSADPSESN 485
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
42-466 |
1.58e-53 |
|
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: 186.11 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 42 GKPNIVVIFGDDIGYWNLSTYnqgmlG--YQTPNIDSIAAEGAKFTSYYAEQSSTAGRSSFITGQMPFRTGMSkvGMPGA 119
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCF-----GgeIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMG--TMAEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 120 PQG-------LQKEDPTIANILKQLGYATGQFGKNHLGDRNeflptahgfdefmgnlYHLNAeeepenpDYpqdpeykkq 192
Cdd:cd16025 74 ATGkpgyegyLPDSAATIAEVLKDAGYHTYMSGKWHLGPDD----------------YYSTD-------DL--------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 193 fgprgvikstADGKIEdtgplnikrmetvdeetlaanndFMERQVKANKPFFTWYNTTRMHNKTHIKPAD----KGV--- 265
Cdd:cd16025 122 ----------TDKAIE-----------------------YIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkyKGKyda 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 266 ----------------------TGLGD-------------------------YAdGMVEH-DKIIGEVLKKIKDLGIEDN 297
Cdd:cd16025 169 gwdalreerlerqkelglipadTKLTPrppgvpawdslspeekklearrmevYA-AMVEHmDQQIGRLIDYLKELGELDN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 298 TIVVYTTDNGP-MTATWPDAGITPFRGEKNTGWEGGFRVPAMIKWPGHIK-PGTLVNDIVGSNDWFPTLVAAAGVPdikq 375
Cdd:cd16025 248 TLIIFLSDNGAsAEPGWANASNTPFRLYKQASHEGGIRTPLIVSWPKGIKaKGGIRHQFAHVIDIAPTILELAGVE---- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 376 qllkgYKTSAMNYKVH-LDGYNQLDYITGKTQEDPRKEFFYwsddgDLL---AMRYGRWKAHFMIQEHTGMDVWKypfvk 451
Cdd:cd16025 324 -----YPKTVNGVPQLpLDGVSLLPTLDGAAAPSRRRTQYF-----ELFgnrAIRKGGWKAVALHPPPGWGDQWE----- 388
|
490
....*....|....*
gi 1222961955 452 lrvplIFDLKIDPLE 466
Cdd:cd16025 389 -----LYDLAKDPSE 398
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
44-431 |
2.46e-52 |
|
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: 181.94 E-value: 2.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYNQGMlgyQTPNIDSIAAEGAKFTSYYAEQSS-TAGRSSFITGQMPFRTGMSkvGMPGAPQG 122
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVV---KTPNLDRLAAEGVRFTNAFTTAPVcSPSRSALLTGLYPHQNGAH--GLRSRGFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 123 LQKEDPTIANILKQLGYATGQFGKNHlgdrneflptahgfdefmgnlyhlnaeeepENPDYPQDPEYKKQFGPRGVIKst 202
Cdd:cd16027 76 LPDGVKTLPELLREAGYYTGLIGKTH------------------------------YNPDAVFPFDDEMRGPDDGGRN-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 203 adgkiedtgplnikrmetvDEETLAANNDFMERQvKANKPFFTWYNTTRMH--------NKTHIKPADKGV--------- 265
Cdd:cd16027 124 -------------------AWDYASNAADFLNRA-KKGQPFFLWFGFHDPHrpyppgdgEEPGYDPEKVKVppylpdtpe 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 266 --TGLGDYADGMVEHDKIIGEVLKKIKDLGIEDNTIVVYTTDNGPmtatwpdagitPFRGEKNTGWEGGFRVPAMIKWPG 343
Cdd:cd16027 184 vrEDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----------PFPRAKGTLYDSGLRVPLIVRWPG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 344 HIKPGTLVNDIVGSNDWFPTLVAAAGVPdikqqllkgyktsamnYKVHLDGYNQLDYITGKTQEdPRKEFF---YWSDDG 420
Cdd:cd16027 253 KIKPGSVSDALVSFIDLAPTLLDLAGIE----------------PPEYLQGRSFLPLLKGEKDP-GRDYVFaerDRHDET 315
|
410
....*....|...
gi 1222961955 421 DLL--AMRYGRWK 431
Cdd:cd16027 316 YDPirSVRTGRYK 328
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
44-370 |
2.53e-50 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 174.53 E-value: 2.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYnqGMLGYQTPNIDSIAAEGAKFTSYYAEQSSTA-GRSSFITGQMPFRTGMSKVGMPGAPQG 122
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLY--GYPRPTTPFLDRLAEEGLLFSNFYSGGTLTApSRFALLTGLPPHNFGSYVSTPVGLPRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 123 LqkedPTIANILKQLGYATGQFGKNHLGDRNEFLPTAHGFDEFMGNlyhlnaeeePENPDYPQDPEYkkqfgprgvikst 202
Cdd:pfam00884 79 E----PSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGR---------NTGSDLYADPPD------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 203 adgkiedtGPLNIKRMETVDEETLaannDFMERQVKAN-KPFFTWYNTTRMHNKTHIKP----ADKGVTGLGD------- 270
Cdd:pfam00884 133 --------VPYNCSGGGVSDEALL----DEALEFLDNNdKPFFLVLHTLGSHGPPYYPDrypeKYATFKPSSCseeqlln 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 271 -YADGMVEHDKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMTatwpDAGITPFRGEK-NTGWEGGFRVPAMIKWPGHIKPG 348
Cdd:pfam00884 201 sYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESL----GEGGGYLHGGKyDNAPEGGYRVPLLIWSPGGKAKG 276
|
330 340
....*....|....*....|..
gi 1222961955 349 TLVNDIVGSNDWFPTLVAAAGV 370
Cdd:pfam00884 277 QKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-466 |
1.60e-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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 172.75 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 43 KPNIVVIFGDDigywnlstYNQGMLGY------QTPNIDSIAAEGAKFTSYYAEQS-STAGRSSFITGQMPFRTGMSKVG 115
Cdd:cd16034 1 KPNILFIFADQ--------HRAQALGCagddpvKTPNLDRLAKEGVVFTNAVSNYPvCSPYRASLLTGQYPLTNGVFGND 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 116 MPgapqgLQKEDPTIANILKQLGYATGQFGKNHLGDRNEFLPTA----------HGFDEFMGNlyhlnaeeepENPDYPQ 185
Cdd:cd16034 73 VP-----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRAddytppperrHGFDYWKGY----------ECNHDHN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 186 DPEYKKQFGPRGVIKSTAdgkiedtgplnikrmetVDEETLAANnDFMERQVKANKPFF---------TWYNTTRMHNKT 256
Cdd:cd16034 138 NPHYYDDDGKRIYIKGYS-----------------PDAETDLAI-EYLENQADKDKPFAlvlswnpphDPYTTAPEEYLD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 257 HIKPAD------------KGVTGLGDYAD--GMVEH-DKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMtatwpdagitpf 321
Cdd:cd16034 200 MYDPKKlllrpnvpedkkEEAGLREDLRGyyAMITAlDDNIGRLLDALKELGLLENTIVVFTSDHGDM------------ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 322 RGE-----KNTGWEGGFRVPAMIKWPGHIKPGTLVNDIVGSNDWFPTLVAAAGVPDikqqllkgyktsamnyKVHLDGYN 396
Cdd:cd16034 268 LGShglmnKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPI----------------PDTVEGRD 331
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 397 QLDYITGKTQEDPRKEFFYWSDDGDLLAMRYGRWKAHFMiqehtgMDVWKYPFVKLRVPLIFDLKIDPLE 466
Cdd:cd16034 332 LSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVR------TDRYTYVRDKNGPWLLFDNEKDPYQ 395
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
42-466 |
1.50e-47 |
|
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: 170.79 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 42 GKPNIVVIFGDDIGYWNLSTYNQGMLgyQTPNIDSIAAEGAKFTSYYAEQS-STAGRSSFITGQMPFRTGMSKvgmpGAP 120
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIV--KTPNIDRLAKEGVRFDNAFVTTSiCAPSRASILTGQYSHRHGVTD----NNG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 121 QGLQKEDPTIANILKQLGYATGQFGKNHLGDRNEFLPTahGFDEFMGnlyhLNAEEEPENPDYPQDPEYKKQFGP----- 195
Cdd:cd16031 75 PLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPP--GFDYWVS----FPGQGSYYDPEFIENGKRVGQKGYvtdii 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 196 --RGV--IKSTADGK------------IEDTGP---------LNIKRMETVDEETLAANNDFMERQVKANKPFFTWYNTT 250
Cdd:cd16031 149 tdKALdfLKERDKDKpfclslsfkaphRPFTPAprhrglyedVTIPEPETFDDDDYAGRPEWAREQRNRIRGVLDGRFDT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 251 RMHNKTHIKpadkgvtglgDYADGMVEHDKIIGEVLKKIKDLGIEDNTIVVYTTDNGPmtatwpdagitpFRGE-----K 325
Cdd:cd16031 229 PEKYQRYMK----------DYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGF------------FLGEhglfdK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 326 NTGWEGGFRVPAMIKWPGHIKPGTLVNDIVGSNDWFPTLVAAAGVPdikqqllkgyKTSAMnykvhlDGYNQLDYITGKT 405
Cdd:cd16031 287 RLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVP----------IPEDM------QGRSLLPLLEGEK 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222961955 406 QEDPRKEFFY---WSDDGDL----LAMRYGRWKahfMIQEHTGMDVWKypfvklrvplIFDLKIDPLE 466
Cdd:cd16031 351 PVDWRKEFYYeyyEEPNFHNvpthEGVRTERYK---YIYYYGVWDEEE----------LYDLKKDPLE 405
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-380 |
5.86e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 137.37 E-value: 5.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYNQGMLgyQTPNIDSIAAEGAKFTSYYAEQS--STAgRSSFITGQMPFRTGM------SKVG 115
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEA--VTPNLDRLAAEGVRFENFFCTSPvcSPA-RASLLTGRMPSQHGIhdwiveGSHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 116 MPGAPQGLQKEDPTIANILKQLGYATGQFGKNHLGDRneflptahgfdefmgnlyhlnaeeepenpdypqdpeykkqfgp 195
Cdd:cd16149 78 KTKKPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLGDD------------------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 196 rgvikstadgkiedtgplnikrmetvdeetlAAnnDFMERQVKANKPFFTWYNTTRMHNKthikpadkgvtgLGDYA--D 273
Cdd:cd16149 115 -------------------------------AA--DFLRRRAEAEKPFFLSVNYTAPHSP------------WGYFAavT 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 274 GMvehDKIIGEVLKKIKDLGIEDNTIVVYTTDNGpMT-----------ATWPdagitpfrgeKNTgWEGGFRVPAMIKWP 342
Cdd:cd16149 150 GV---DRNVGRLLDELEELGLTENTLVIFTSDNG-FNmghhgiwgkgnGTFP----------LNM-YDNSVKVPFIIRWP 214
|
330 340 350
....*....|....*....|....*....|....*...
gi 1222961955 343 GHIKPGTLVNDIVGSNDWFPTLVAAAGVPDIKQQLLKG 380
Cdd:cd16149 215 GVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRLPG 252
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-466 |
4.80e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 127.34 E-value: 4.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYnqGMLGYQTPNIDSIAAEGAKFTSYYAEQS-STAGRSSFITGQMPFRTGM-SKVGMPGAPQ 121
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCY--GNPIVKTPNIDRLAAEGVRFTNAYTPSPvCCPARASLLTGLYPHEHGVlNNVENAGAYS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 122 GLQKED-PTIANILKQLGYATGQFGKNHLGDRNefLPTAHGFDEFMgnlyhlnaeeePENPdypqdpeykkqFGPRgvik 200
Cdd:cd16033 79 RGLPPGvETFSEDLREAGYRNGYVGKWHVGPEE--TPLDYGFDEYL-----------PVET-----------TIEY---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 201 STADGKIEdtgplnikrmetvdeetlaanndFMERQVKANKPFFTWYNTT-----------------------------R 251
Cdd:cd16033 131 FLADRAIE-----------------------MLEELAADDKPFFLRVNFWgphdpyippepyldmydpediplpesfadD 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 252 MHNKTHIKPADKGVTGLGDYADGMVEH------------DKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMTAT---WpDA 316
Cdd:cd16033 188 FEDKPYIYRRERKRWGVDTEDEEDWKEiiahywgyitliDDAIGRILDALEELGLADDTLVIFTSDHGDALGAhrlW-DK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 317 GITPFrgekntgwEGGFRVPAMIKWPGHIKPGTLVNDIVGSNDWFPTLVAAAGVPdikqqllkgyktsamnYKVHLDGYN 396
Cdd:cd16033 267 GPFMY--------EETYRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVD----------------VPPKVDGRS 322
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222961955 397 QLDYITGKTQEDPRKEFFY-WSDDGDLLAMRYGRwkahfmiqehtgMDVWKYPFVKLRVPLIFDLKIDPLE 466
Cdd:cd16033 323 LLPLLRGEQPEDWRDEVVTeYNGHEFYLPQRMVR------------TDRYKYVFNGFDIDELYDLESDPYE 381
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-371 |
1.14e-30 |
|
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: 120.35 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGD----DigywNLSTYNQGMLgyQTPNIDSIAAEGAKFTSYYAEQSST-AGRSSFITGQMPFRTGMSKvgmpg 118
Cdd:cd16148 1 MNVILIVIDslraD----HLGCYGYDRV--TTPNLDRLAAEGVVFDNHYSGSNPTlPSRFSLFTGLYPFYHGVWG----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 119 apQGLQKEDPTIANILKQLGYATGQFGKN-HLGDRNEFlptAHGFDEFMGNLYHLnaEEEPENPDYPqdpeykkqfgprg 197
Cdd:cd16148 70 --GPLEPDDPTLAEILRKAGYYTAAVSSNpHLFGGPGF---DRGFDTFEDFRGQE--GDPGEEGDER------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 198 vikstadgkiedtgplnikrmetvDEETLAANNDFMERQvKANKPFFTWYNttrmHNKTHikpadkgvtglGDYA-DGMV 276
Cdd:cd16148 130 ------------------------AERVTDRALEWLDRN-ADDDPFFLFLH----YFDPH-----------EPYLyDAEV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 277 EH-DKIIGEVLKKIKDLGIEDNTIVVYTTDNGpmtatwpdagiTPFrGEKNTGWEGGF-------RVPAMIKWPGhIKPG 348
Cdd:cd16148 170 RYvDEQIGRLLDKLKELGLLEDTLVIVTSDHG-----------EEF-GEHGLYWGHGSnlydeqlHVPLIIRWPG-KEPG 236
|
330 340
....*....|....*....|...
gi 1222961955 349 TLVNDIVGSNDWFPTLVAAAGVP 371
Cdd:cd16148 237 KRVDALVSHIDIAPTLLDLLGVE 259
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-464 |
7.20e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 110.71 E-value: 7.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDigywnlstYNQGMLGY------QTPNIDSIAAEGAKFTSYYAeqSS---TAGRSSFITGQMPFRTGMSKV 114
Cdd:cd16037 1 PNILIIMSDE--------HNPDAMGCyghpvvRTPNLDRLAARGTRFENAYT--PSpicVPSRASFLTGRYVHETGVWDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 115 GMPgapqgLQKEDPTIANILKQLGYATGQFGKNHLGDRNEFlptaHGFDefmgnlyhlnaeeepenpdypQDpeykkqfg 194
Cdd:cd16037 71 ADP-----YDGDVPSWGHALRAAGYETVLIGKLHFRGEDQR----HGFR---------------------YD-------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 195 pRGVIKSTADgKIEDTGPlnikrmetvDEETLAANNDFMerqvkanKPFFTWYNTTRMHNKtHIKPADKGVTGLGDYADG 274
Cdd:cd16037 113 -RDVTEAAVD-WLREEAA---------DDKPWFLFVGFV-------APHFPLIAPQEFYDL-YVRRARAAYYGLVEFLDE 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 275 MvehdkiIGEVLKKIKDLGIEDNTIVVYTTDNGPMTATwpdagitpfRG--EKNTGWEGGFRVPAMIKWPGhIKPGTLVN 352
Cdd:cd16037 174 N------IGRVLDALEELGLLDNTLIIYTSDHGDMLGE---------RGlwGKSTMYEESVRVPMIISGPG-IPAGKRVK 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 353 DIVGSNDWFPTLVAAAGVPDIKqqllkgyktsamnykvHLDGYNQLDYITGKtqEDPRKEFF--YWSDDGD--LLAMRYG 428
Cdd:cd16037 238 TPVSLVDLAPTILEAAGAPPPP----------------DLDGRSLLPLAEGP--DDPDRVVFseYHAHGSPsgAFMLRKG 299
|
410 420 430
....*....|....*....|....*....|....*.
gi 1222961955 429 RWKAHFmiqeHTGMDvwkypfvklrvPLIFDLKIDP 464
Cdd:cd16037 300 RWKYIY----YVGYP-----------PQLFDLENDP 320
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-467 |
1.12e-26 |
|
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: 111.55 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 43 KPNIVVIFGDDIGYWNLSTYNQGM-LgyqTPNIDSIAAEGAKFTSYYAEQSSTA-GRSSFITGQMPFRTGMSKVGMPgap 120
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLdL---TPNLDALAEEGVLFENAFTPQPVCGpARACLQTGLYPTETGCFRNGIP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 121 qgLQKEDPTIANILKQLGYATGQFGKNHL-GDRNEFLpTAHGFDeFMGNL---------------YHLNAEEEPENPDYp 184
Cdd:cd16152 75 --LPADEKTLAHYFRDAGYETGYVGKWHLaGYRVDAL-TDFAID-YLDNRqkdkpfflflsylepHHQNDRDRYVAPEG- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 185 qdpeYKKQFGPRGVIKSTADGKiedtGplnikrmetvdeetlaanndfmerqvkankpffTWYNttrmhnkthikpadkg 264
Cdd:cd16152 150 ----SAERFANFWVPPDLAALP----G---------------------------------DWAE---------------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 265 vtGLGDYAdGMVEH-DKIIGEVLKKIKDLGIEDNTIVVYTTDNGpmtatwpdagiTPFR---GE-KNTGWEGGFRVPAMI 339
Cdd:cd16152 173 --ELPDYL-GCCERlDENVGRIRDALKELGLYDNTIIVFTSDHG-----------CHFRtrnAEyKRSCHESSIRVPLVI 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 340 KWPGhIKPGTLVNDIVGSNDWFPTLVAAAG--VPDikqqllkgyktsAMnykvhlDGYNQLDYITGKTQEDPRKEFFYWS 417
Cdd:cd16152 239 YGPG-FNGGGRVEELVSLIDLPPTLLDAAGidVPE------------EM------QGRSLLPLVDGKVEDWRNEVFIQIS 299
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1222961955 418 DDGDLLAMRYGRWKahfMIQEHTGMDVWKYPFVKLRVP-LIFDLKIDPLEK 467
Cdd:cd16152 300 ESQVGRAIRTDRWK---YSVAAPDKDGWKDSGSDVYVEdYLYDLEADPYEL 347
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-466 |
8.11e-26 |
|
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: 108.81 E-value: 8.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 43 KPNIVVIFGDDIGYWNLSTYNQGMLgyQTPNIDSIAAEGAKFTSYYAeQSSTAG------RSSFITGQMPFRTgmskvgM 116
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEI--QTPNLDRLARRGTSFTNAYN-MGGWSGavcvpsRAMLMTGRTLFHA------P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 117 PGAPQGLQKEDPTIANILKQLGYATGQFGKNHlgdrNEFLPTAHGFdefmgnlyhLNAEEEPENP-------DYPQDP-- 187
Cdd:cd16155 73 EGGKAAIPSDDKTWPETFKKAGYRTFATGKWH----NGFADAAIEF---------LEEYKDGDKPffmyvafTAPHDPrq 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 188 ---EYKKQFGPRGVikstadgkiedTGPLNIKRMETVDeetlaaNNDFMERqvkanKPFFTWYNTTRMHNKTHikpadkg 264
Cdd:cd16155 140 appEYLDMYPPETI-----------PLPENFLPQHPFD------NGEGTVR-----DEQLAPFPRTPEAVRQH------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 265 vtgLGDYAdGMVEH-DKIIGEVLKKIKDLGIEDNTIVVYTTDNG-------PMtatwpdagitpfrGEKNTgWEGGFRVP 336
Cdd:cd16155 191 ---LAEYY-AMITHlDAQIGRILDALEASGELDNTIIVFTSDHGlavgshgLM-------------GKQNL-YEHSMRVP 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 337 AMIKWPGhIKPGTLVNDIVGSNDWFPTLVAAAGVPDIKqqllkgyktsamnykvHLDGYNQLDYITGKTQEdPRKEFFYW 416
Cdd:cd16155 253 LIISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPE----------------SVEGKSLLPVIRGEKKA-VRDTLYGA 314
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1222961955 417 SDDGDLlAMRYGRWKAHfmiqehtgmdvWKYPfvKLRVPLIFDLKIDPLE 466
Cdd:cd16155 315 YRDGQR-AIRDDRWKLI-----------IYVP--GVKRTQLFDLKKDPDE 350
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
28-404 |
8.30e-26 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 111.28 E-value: 8.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 28 PDSNQPSTAPEQNKGKPNIVVI----FGDDigYWNLSTYNQGMlgyqTPNIDSIAAEGAKFTSYYAeqssTAGRSS---- 99
Cdd:COG1368 219 LKSNRPTPNPFGPAKKPNVVVIllesFSDF--FIGALGNGKDV----TPFLDSLAKESLYFGNFYS----QGGRTSrgef 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 100 -FITGqMPFRTGMSKVGMPGapqglQKEDPTIANILKQLGYATgQF---GKNHLGDRNEFLPtAHGFDEFMGnlyhlnae 175
Cdd:COG1368 289 aVLTG-LPPLPGGSPYKRPG-----QNNFPSLPSILKKQGYET-SFfhgGDGSFWNRDSFYK-NLGFDEFYD-------- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 176 eepenpdypqdpeyKKQFgprgvikstadgKIEDTGPLNIKrmetvDEETLaanNDFMERQVKANKPFFTWYNTTRMH-- 253
Cdd:COG1368 353 --------------REDF------------DDPFDGGWGVS-----DEDLF---DKALEELEKLKKPFFAFLITLSNHgp 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 254 ---NKTHIKPADKGVTGLGDYADGMVEHDKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMTATWPDAGITPFRgekntgwe 330
Cdd:COG1368 399 ytlPEEDKKIPDYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENPLER-------- 470
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1222961955 331 ggFRVPAMIKWPGHIKPGTlVNDIVGSNDWFPTLVAAAGVPDIKQQllkGYKTSAMNYKVHLDGYNQLDYITGK 404
Cdd:COG1368 471 --YRVPLLIYSPGLKKPKV-IDTVGSQIDIAPTLLDLLGIDYPSYY---AFGRDLLSPDTDPFAFRNGGFITDD 538
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-396 |
1.11e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 106.69 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 43 KPNIVVIFGDDIGYWNLSTYNQGM-------LGY-QTPNIDSIAAEGAKFTSYYAEQSSTA-GRSSFITGQMPFRTGMsk 113
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNAHtgksesrLGYvESPNIDALAAEGVLFTNAYCNSPVCVpSRTSMLTGRYPHRTGV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 114 VGMPGAPQGLQKEDPTIANILKQLGYATGQFGKNHLGDRNEFLPTAhgfdefmgnlyhlnaeeepenpdypqDPEYKkqf 193
Cdd:cd16153 79 YGFEAAHPALDHGLPTFPEVLKKAGYQTASFGKSHLEAFQRYLKNA--------------------------NQSYK--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 194 gprgviksTADGKIedtgplnikrmetvdeetlaanndfmERQVKANKPFFTWYNTTRMHnkTHIKPADKGVTGLGDYAd 273
Cdd:cd16153 130 --------SFWGKI--------------------------AKGADSDKPFFVRLSFLQPH--TPVLPPKEFRDRFDYYA- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 274 gMVEH-DKIIGEVLKKIKDLGI---EDNTIVVYTTDNGpmtATWPDAGITpfrgEKNTGWEGGFRVPAMIKWPGHIK--P 347
Cdd:cd16153 173 -FCAYgDAQVGRAVEAFKAYSLkqdRDYTIVYVTGDHG---WHLGEQGIL----AKFTFWPQSHRVPLIVVSSDKLKapA 244
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1222961955 348 GTLVNDIVGSNDWFPTLVAAAGVPdikqqllkgyktsAMNYKvHLDGYN 396
Cdd:cd16153 245 GKVRHDFVEFVDLAPTLLAAAGVD-------------VDAPD-YLDGRD 279
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
70-466 |
1.13e-24 |
|
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: 106.57 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 70 QTPNIDSIAAEGAKFTSYYAeQSSTAG--RSSFITGQMPFRTGMSKVGMPgapqgLQKEDPTIANILKQLGYATGQFGKN 147
Cdd:cd16028 25 KTPNLDRLAAEGVRFRNHYT-QAAPCGpsRASLYTGRYLMNHRSVWNGTP-----LDARHLTLALELRKAGYDPALFGYT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 148 HL--------------------------GDRNEFLP-----TAHGFDEFMGNLyhlnaEEEPENP-------DYPQDP-- 187
Cdd:cd16028 99 DTspdprglapldprllsyelampgfdpVDRLDEYPaedsdTAFLTDRAIEYL-----DERQDEPwflhlsyIRPHPPfv 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 188 ---EYKKQFGPrgvikstadgkiEDTGPLNikRMETVDEEtlAANNDFME--RQVKANKPFFTWYNTTRMHNKTHI---K 259
Cdd:cd16028 174 apaPYHALYDP------------ADVPPPI--RAESLAAE--AAQHPLLAafLERIESLSFSPGAANAADLDDEEVaqmR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 260 PAdkgvtglgdYAdGMV-EHDKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMtatWPDAGItpfrGEKNTGWEGGFRVPAM 338
Cdd:cd16028 238 AT---------YL-GLIaEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQ---LGDHWL----WGKDGFFDQAYRVPLI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 339 IKWPG---HIKPGTLVNDIVGSNDWFPTLVAAAGVPdIKQQllkgyktsamnykvhLDGYNQLDYITGKTQEDPRKEFFY 415
Cdd:cd16028 301 VRDPRreaDATRGQVVDAFTESVDVMPTILDWLGGE-IPHQ---------------CDGRSLLPLLAGAQPSDWRDAVHY 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222961955 416 WSDDGDLLamrYGRWKAHF----------MIQEHTgmdvWKY-PFVKLRvPLIFDLKIDPLE 466
Cdd:cd16028 365 EYDFRDVS---TRRPQEALglspdecslaVIRDER----WKYvHFAALP-PLLFDLKNDPGE 418
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-415 |
4.67e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 100.89 E-value: 4.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYNQGMLGYQTPNIDSIAAEGAKFTSYYAEQSSTAGRSSFITGQMPFRTGMSKVGMPGA---- 119
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGVLAVPDELLlsee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 120 --PQGLQKEDPTIanilkqlGYATGQFGKNHLGDRNEFLPTAHGFDEFMGNLyhlnaeeePEN-PDYPQDPeykkqfgpr 196
Cdd:cd16154 81 tlLQLLIKDATTA-------GYSSAVIGKWHLGGNDNSPNNPGGIPYYAGIL--------GGGvQDYYNWN--------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 197 gvikstadgKIEDTGPLNIKRMETVDEETLAAnnDFMERQvkaNKPFFTWYNTTRMHNKTHIKPADKGVTG-LGDYAD-- 273
Cdd:cd16154 137 ---------LTNNGQTTNSTEYATTKLTNLAI--DWIDQQ---TKPWFLWLAYNAPHTPFHLPPAELHSRSlLGDSADie 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 274 --------GMVEH-DKIIGEVLKKIkDLGIEDNTIVVYTTDNG-PMTATwpDAGITPfRGEKNTGWEGGFRVPAMIKWPG 343
Cdd:cd16154 203 anprpyylAAIEAmDTEIGRLLASI-DEEERENTIIIFIGDNGtPGQVV--DLPYTR-NHAKGSLYEGGINVPLIVSGAG 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222961955 344 HIKPGTLVNDIVGSNDWFPTLVAAAGVPDIKQQLLKGYKTSAMNYKVHLDGYNQLDYITGKTQEDPRKEFFY 415
Cdd:cd16154 279 VERANERESALVNATDLYATIAELAGVDAAEIHDSVSFKPLLSDVNASTRQYNYTEYESPTTTGWATRNQYY 350
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
43-371 |
7.40e-23 |
|
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: 100.70 E-value: 7.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 43 KPNIVVIFGDDigywnlSTYNQGMLGYQTPNIDSIAAEGAKFTSYYAeqsSTA----GRSSFITGQMPFRTGMSKVGMPG 118
Cdd:cd16147 1 RPNIVLILTDD------QDVELGSMDPMPKTKKLLADQGTTFTNAFV---TTPlccpSRASILTGQYAHNHGVTNNSPPG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 119 ---APQGLQKEDP-TIANILKQLGYATGQFGK--NHLGDRNEFLPTAHGFDEFMG------NLYHLNAEEEPENP--DYP 184
Cdd:cd16147 72 ggyPKFWQNGLERsTLPVWLQEAGYRTAYAGKylNGYGVPGGVSYVPPGWDEWDGlvgnstYYNYTLSNGGNGKHgvSYP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 185 QDpeYkkqfgprgvikSTadgkiedtgplnikrmetvdeeTLAAN--NDFMERQVKANKPFFTWYNTTRMHN-------- 254
Cdd:cd16147 152 GD--Y-----------LT----------------------DVIANkaLDFLRRAAADDKPFFLVVAPPAPHGpftpapry 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 255 --------KTHIKPAD-----KGVTGLGDYADGMVEH------------------DKIIGEVLKKIKDLGIEDNTIVVYT 303
Cdd:cd16147 197 anlfpnvtAPPRPPPNnpdvsDKPHWLRRLPPLNPTQiayidelyrkrlrtlqsvDDLVERLVNTLEATGQLDNTYIIYT 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 304 TDNGPMTATwpdagitpFR--GEKNTGWEGGFRVPAMIKWPGhIKPGTLVNDIVGSNDWFPTLVAAAGVP 371
Cdd:cd16147 277 SDNGYHLGQ--------HRlpPGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAP 337
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
44-465 |
7.53e-23 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 99.19 E-value: 7.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYNQGMLgyQTPNIDSIAAEGAKFTSYYAeqSS---TAGRSSFITGQMPFRTGMskvgMPGAP 120
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVV--KTPNLDRLAARGVVFDNAYC--NSplcAPSRASMMTGRLPSRIGA----YDNAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 121 QgLQKEDPTIANILKQLGYATGQFGKNHL--GDRneflptAHGFDefmgnlyhlnaeeepenpdYPQDPEYKkqfgprgv 198
Cdd:cd16032 73 E-FPADIPTFAHYLRAAGYRTALSGKMHFvgPDQ------LHGFD-------------------YDEEVAFK-------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 199 ikstADGKIEDtgplnikrmetvdeetLAANNDfmerqvkaNKPFFTW---------YNTTRMHNKTHIKPADKGVTGLG 269
Cdd:cd16032 119 ----AVQKLYD----------------LARGED--------GRPFFLTvsfthphdpYVIPQEYWDLYVRRARRAYYGMV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 270 DYADGMVehdkiiGEVLKKIKDLGIEDNTIVVYTTDNGPMTatwpdagitpfrGE-----KNTGWEGGFRVPAMIKWPGH 344
Cdd:cd16032 171 SYVDDKV------GQLLDTLERTGLADDTIVIFTSDHGDML------------GErglwyKMSFFEGSARVPLIISAPGR 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 345 IKPGTlVNDIVGSNDWFPTLVAAAGVPDIKqqllkgyktsamnYKVHLDGYNQLDYITGKTQEDPRKEFFYWSDDG---D 421
Cdd:cd16032 233 FAPRR-VAEPVSLVDLLPTLVDLAGGGTAP-------------HVPPLDGRSLLPLLEGGDSGGEDEVISEYLAEGavaP 298
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1222961955 422 LLAMRYGRWKahFMiqeHTGMDvwkyPfvklrvPLIFDLKIDPL 465
Cdd:cd16032 299 CVMIRRGRWK--FI---YCPGD----P------DQLFDLEADPL 327
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
43-371 |
1.34e-22 |
|
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.
Pssm-ID: 293754 [Multi-domain] Cd Length: 435 Bit Score: 100.34 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 43 KPNIVVIFGDDIGYWnLSTY-NQGMlgyQTPNIDSIAAEGAKFTSYYAEQS-STAGRSSFITGQMPFRTGMskVGMPGAP 120
Cdd:cd16030 2 KPNVLFIAVDDLRPW-LGCYgGHPA---KTPNIDRLAARGVLFTNAYCQQPvCGPSRASLLTGRRPDTTGV--YDNNSYF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 121 QGLQKEDPTIANILKQLGYATGQFGKNHLGDRNEFLPTAHGFDEFmgnlyhlnaeeePENPDYPQDPEYKKQFGPRGVIK 200
Cdd:cd16030 76 RKVAPDAVTLPQYFKENGYTTAGVGKIFHPGIPDGDDDPASWDEP------------PNPPGPEKYPPGKLCPGKKGGKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 201 StadGKIEDTGPLNIKRMETVDEETLAANNDFMERQVKANKPFF---------------------------TWYNTT--- 250
Cdd:cd16030 144 G---GGGPAWEAADVPDEAYPDGKVADEAIEQLRKLKDSDKPFFlavgfykphlpfvapkkyfdlyplesiPLPNPFdpi 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 251 -----RMHNKTHIKPADKGVTGLGDYADGMVEHDKI-----------------IGEVLKKIKDLGIEDNTIVVYTTDNGP 308
Cdd:cd16030 221 dlpevAWNDLDDLPKYGDIPALNPGDPKGPLPDEQArelrqayyasvsyvdaqVGRVLDALEELGLADNTIVVLWSDHGW 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222961955 309 M---TATWpdagitpfrgEKNTGWEGGFRVPAMIKWPGHIKPGTLVNDIVGSNDWFPTLVAAAGVP 371
Cdd:cd16030 301 HlgeHGHW----------GKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLP 356
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
44-369 |
7.53e-22 |
|
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: 95.44 E-value: 7.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVI----FGDDigYWNLSTYNQGMlgyqTPNIDSIAAEGAKFTSYYAeqSSTAGRSS-----FITGQMPFRTGmskv 114
Cdd:cd16015 1 PNVIVIllesFSDP--YIDKDVGGEDL----TPNLNKLAKEGLYFGNFYS--PGFGGGTAngefeVLTGLPPLPLG---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 115 gmPGAPQGLQKED-PTIANILKQLGYATgQF---GKNHLGDRNEFLPtAHGFDEFmgnlYHLNaeeepenpDYPQDPEYK 190
Cdd:cd16015 69 --SGSYTLYKLNPlPSLPSILKEQGYET-IFihgGDASFYNRDSVYP-NLGFDEF----YDLE--------DFPDDEKET 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 191 KQFGPRgvikstadgkiedtgplnikrmetvDEETLaannDFMERQVKAN--KPFFTWYNTTRMH--------NKTHIKP 260
Cdd:cd16015 133 NGWGVS-------------------------DESLF----DQALEELEELkkKPFFIFLVTMSNHgpydlpeeKKDEPLK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 261 ADKGVTGLGDYADGMVEHDKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMtatwpdagITPFRGEKNTGWEGGFRVPAMIK 340
Cdd:cd16015 184 VEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPS--------LGSDYDETDEDPLDLYRTPLLIY 255
|
330 340
....*....|....*....|....*....
gi 1222961955 341 WPGHIKPGTlVNDIVGSNDWFPTLVAAAG 369
Cdd:cd16015 256 SPGLKKPKK-IDRVGSQIDIAPTLLDLLG 283
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
42-420 |
1.55e-21 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 97.43 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 42 GKPNIVVIF-----GDDIGywnlstyNQGMLGYQTPNIDSIAAEGAKFTS-YYAEQSSTAGRSSFITGQMPFRTGMSkvg 115
Cdd:PRK13759 5 KKPNIILIMvdqmrGDCLG-------CNGNKAVETPNLDMLASEGYNFENaYSAVPSCTPARAALLTGLSQWHHGRV--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 116 mpgapqGLQKEDP-----TIANILKQLGYATGQFGKNHL-GDRNEflptaHGFDEFM---GNLYHlNAEEEPENPDYPQD 186
Cdd:PRK13759 75 ------GYGDVVPwnyknTLPQEFRDAGYYTQCIGKMHVfPQRNL-----LGFHNVLlhdGYLHS-GRNEDKSQFDFVSD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 187 peYKKQFgprgviKSTADGKIEDTGPLNIKRMETVD-----EETLAANN-------DFMERQVKAnKPFF---------- 244
Cdd:PRK13759 143 --YLAWL------REKAPGKDPDLTDIGWDCNSWVArpwdlEERLHPTNwvgsesiEFLRRRDPT-KPFFlkmsfarphs 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 245 -----------------------TWYNTTRMHNKTHIKPADKGVTGlGDYADGMVEH--------DKIIGEVLKKIKDLG 293
Cdd:PRK13759 214 pydppkryfdmykdadipdphigDWEYAEDQDPEGGSIDALRGNLG-EEYARRARAAyyglithiDHQIGRFLQALKEFG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 294 IEDNTIVVYTTDNGPMTAtwpDAGItpFRgeKNTGWEGGFRVPAMIKWPGHIKP---GTLVNDIVGSNDWFPTLVAAAG- 369
Cdd:PRK13759 293 LLDNTIILFVSDHGDMLG---DHYL--FR--KGYPYEGSAHIPFIIYDPGGLLAgnrGTVIDQVVELRDIMPTLLDLAGg 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1222961955 370 -VPDI--KQQLLKGYKTSAMNYKVHLDG-----YNQLDYITgktqeDPRKEFFYWSDDG 420
Cdd:PRK13759 366 tIPDDvdGRSLKNLIFGQYEGWRPYLHGehalgYSSDNYLT-----DGKWKYIWFSQTG 419
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
44-364 |
6.71e-16 |
|
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: 77.08 E-value: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYNQGMLgyQTPNIDSIAAEGA--KFTSYYAEQSSTAGRSSFITGQMPFRTG-----MSKVGM 116
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAP--TTPNLKRLASEGAtfNFRSVSPPTSSAPNHAALLTGAYPTLHGytgngSADPEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 117 PGAPQGLQKEDPTIANILKQLGYATGqfgknhlgdrneflptahgfdeFMGNLYHLNaeeepenpdypqdpeykkqfgpr 196
Cdd:cd00016 79 PSRAAGKDEDGPTIPELLKQAGYRTG----------------------VIGLLKAID----------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 197 gvikstadgkiedtgplnikrmetvdeetlaanndfmerQVKANKPFFTWYNTTRMHNKTHIKPADKGVtglgdYADGMV 276
Cdd:cd00016 114 ---------------------------------------ETSKEKPFVLFLHFDGPDGPGHAYGPNTPE-----YYDAVE 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 277 EHDKIIGEVLKKIKDLGIEDNTIVVYTTDNGpmTATWPDAGiTPFRGEKNTGWEGGFRVPAMIKWPGHIKPGTLVNDIvG 356
Cdd:cd00016 150 EIDERIGKVLDALKKAGDADDTVIIVTADHG--GIDKGHGG-DPKADGKADKSHTGMRVPFIAYGPGVKKGGVKHELI-S 225
|
....*...
gi 1222961955 357 SNDWFPTL 364
Cdd:cd00016 226 QYDIAPTL 233
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-380 |
6.62e-15 |
|
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: 75.71 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWnlSTYNQGMLGYQTPNIDSIAAEGAKFTSYYAeqSSTA---GRSSFITGQMPFRTGMSK-VGMPGA 119
Cdd:cd16035 1 PNILLILTDQERYP--PPWPAGWAALNLPARERLAANGLSFENHYT--AACMcspSRSTLYTGLHPQQTGVTDtLGSPMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 120 PQgLQKEDPTIANILKQLGYATGQFGKNHLgdrneflpTAHGfdefmgnlyhlnaeeepeNPDYPQDPEYKKQFgprgvi 199
Cdd:cd16035 77 PL-LSPDVPTLGHMLRAAGYYTAYKGKWHL--------SGAA------------------GGGYKRDPGIAAQA------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 200 kstadgkiedtgplnikrmetvdEETLAAnndfMERQVKANKPFFTWYNTTRMHNKTHIKPADKGVTGLGD-YADGMVEH 278
Cdd:cd16035 124 -----------------------VEWLRE----RGAKNADGKPWFLVVSLVNPHDIMFPPDDEERWRRFRNfYYNLIRDV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 279 DKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMtatwpdAGITPFRGEKNTGWEGGFRVPAMIKWPGHIKPGTLVNDIVGSN 358
Cdd:cd16035 177 DRQIGRVLDALDASGLADNTIVVFTSDHGEM------GGAHGLRGKGFNAYEEALHVPLIISHPDLFGTGQTTDALTSHI 250
|
330 340
....*....|....*....|....*.
gi 1222961955 359 DWFPTLVAAAGVPD----IKQQLLKG 380
Cdd:cd16035 251 DLLPTLLGLAGVDAearaTEAPPLPG 276
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-371 |
7.21e-15 |
|
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: 76.50 E-value: 7.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTYnqGMLGYQTPNIDSIAAEGAKFTSYYAeQSS--TAGRSSFITGQMP----FRTgMSkvgmp 117
Cdd:cd16150 1 PNIVIFVADQLRADSLGHL--GNPAAVTPNLDALAAEGVRFSNAYC-QNPvcSPSRCSFLTGWYPhvngHRT-LH----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 118 gapQGLQKEDPTIANILKQLGYATGQFGKNHLgdrnefLPTAHGFDEFmgnlyhlnaeeepenpdypqdpeykkqfgprg 197
Cdd:cd16150 72 ---HLLRPDEPNLLKTLKDAGYHVAWAGKNDD------LPGEFAAEAY-------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 198 vikstadgkiedtgplnikrmETVDEETLAANNDFMERQvKANKPFF----------------TWYNttrMHNKTHIKPA 261
Cdd:cd16150 111 ---------------------CDSDEACVRTAIDWLRNR-RPDKPFClylplifphppygveePWFS---MIDREKLPPR 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 262 DKGVT---------------GLGDYAD-----------GMVEH-DKIIGEVLKKIKDLGIEDNTIVVYTTDNGPMTAtwp 314
Cdd:cd16150 166 RPPGLrakgkpsmlegiekqGLDRWSEerwrelratylGMVSRlDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTG--- 242
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222961955 315 DAGITpfrgEKntgWEGGF-----RVPAMIKWPGHIKPGTlVNDIVGSNDWFPTLVAAAGVP 371
Cdd:cd16150 243 DYGLV----EK---WPNTFedcltRVPLIIKPPGGPAGGV-SDALVELVDIPPTLLDLAGIP 296
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
44-371 |
1.25e-13 |
|
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: 73.19 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 44 PNIVVIFGDDIGYWNLSTY-NQGMlgyQTPNIDSIAAEGAKFTSYYAEQS-STAGRSSFITGQMPFRTGMSKVGMPgapq 121
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYgNKAM---KTPNLDRLAAEGVRFDSAYTTQPvCGPARSGLFTGLYPHTNGSWTNCMA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 122 gLQKEDPTIANILKQLGYATGQFGKNHLgDRNEFLPTA---HGFDEF----MGN-LYHLNAEE---------EPENPDYP 184
Cdd:cd16156 74 -LGDNVKTIGQRLSDNGIHTAYIGKWHL-DGGDYFGNGicpQGWDPDywydMRNyLDELTEEErrksrrgltSLEAEGIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 185 QDPEYKKQFGPRGV--IKSTADgkiED--------------TGPLNIKRM-ETVDEETLAANNDFMErqvkaNKPFF--T 245
Cdd:cd16156 152 EEFTYGHRCTNRALdfIEKHKD---EDfflvvsydephhpfLCPKPYASMyKDFEFPKGENAYDDLE-----NKPLHqrL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 246 WYNtTRMH---NKTHIKPadKGVTGLGDYADGMvehdkiIGEVLKKIKDLGieDNTIVVYTTDNGPMtatwpdAGITPFR 322
Cdd:cd16156 224 WAG-AKPHedgDKGTIKH--PLYFGCNSFVDYE------IGRVLDAADEIA--EDAWVIYTSDHGDM------LGAHKLW 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1222961955 323 GEKNTGWEGGFRVPAMIKWPGHIKPGTLVNDIVGSNDWFPTLVAAAGVP 371
Cdd:cd16156 287 AKGPAVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIP 335
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
277-381 |
3.16e-08 |
|
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: 55.63 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 277 EHDKIIGEVLKKIKDLGIEDNTIVVYTTDNGpmtatwpDAGITPFRGEKNTGWEGGFRVPAMIKWPGhIKPGTLVNDIVG 356
Cdd:cd16171 204 ETDAMLGEIISALKDTGLLDKTYVFFTSDHG-------ELAMEHRQFYKMSMYEGSSHVPLLIMGPG-IKAGQQVSDVVS 275
|
90 100
....*....|....*....|....*
gi 1222961955 357 SNDWFPTLVAAAGVPdiKQQLLKGY 381
Cdd:cd16171 276 LVDIYPTMLDIAGVP--QPQNLSGY 298
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
409-514 |
4.24e-08 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 51.54 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 409 PRKEFFYWSDDgDLLAMRYGRWKAHFMIQEH-----TGMDVWKYPFVKLRVPLIFDLKIDPLEK---GTDGMDYNHwfyd 480
Cdd:pfam14707 2 PHEFLFHYCGA-ALHAVRWGPYKAHFFTPSFdppgaEGCYGSKVPVTHHDPPLLFDLERDPSEKyplSPDSPEYPE---- 76
|
90 100 110
....*....|....*....|....*....|....
gi 1222961955 481 rlfLLGGAQKYAAEMLQSFKEFPPRQKPGSFTVS 514
Cdd:pfam14707 77 ---VLAEIKAAVEEHKATLVPVPNQLSKGNYLWD 107
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
222-388 |
9.41e-08 |
|
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: 54.91 E-value: 9.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 222 DEETLAANNDFMERQvKANKPFFTW--YNTTrmHN----KTHIKPADKGVTGLGDYADGMVEHDKI-------------- 281
Cdd:COG3083 363 DRQITAQWLQWLDQR-DSDRPWFSYlfLDAP--HAysfpADYPKPFQPSEDCNYLALDNESDPTPFknryrnavhyvdsq 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222961955 282 IGEVLKKIKDLGIEDNTIVVYTTDNGpmtatwpdagiTPFRGEKNTGWEGGF-------RVPAMIKWPGhiKPGTLVNDI 354
Cdd:COG3083 440 IGRVLDTLEQRGLLENTIVIITADHG-----------EEFNENGQNYWGHNSnfsryqlQVPLVIHWPG--TPPQVISKL 506
|
170 180 190
....*....|....*....|....*....|....
gi 1222961955 355 VGSNDWFPTLVaaagvpdikQQLLkGYKTSAMNY 388
Cdd:COG3083 507 TSHLDIVPTLM---------QRLL-GVQNPASDY 530
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
36-111 |
5.62e-03 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 38.96 E-value: 5.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222961955 36 APEQNKGKPNIVVIFGDDIGYWNLSTYNqgmlgyqTPNIDSIAAEGAKFTSYYAEQSST--AGRSSFITGQMPFRTGM 111
Cdd:COG1524 16 AAAAAPPAKKVVLILVDGLRADLLERAH-------APNLAALAARGVYARPLTSVFPSTtaPAHTTLLTGLYPGEHGI 86
|
|
| |
