|
Name |
Accession |
Description |
Interval |
E-value |
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-489 |
2.55e-167 |
|
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: 479.35 E-value: 2.55e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYTVPVLEKGN--- 106
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAaAPVCSPSRASILTGQYPARLGITDVIPGRRGPpdn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 107 -DQVSIFSRWTVGEEHIMYSQPLADAGYKSIHLGKWHLVGPYPkkemeaswplkkklgqpkpsdfswvpyhkehckaYYP 185
Cdd:cd16144 81 tKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGG----------------------------------YGP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 186 EGRGYLKNIGGTYRGDPAlevggyksktGGYFAPFSNPFMDQKNPKDKWLTDHLTTEAINFMDEHKEGPFFINLHYYTVH 265
Cdd:cd16144 127 EDQGFDVNIGGTGNGGPP----------SYYFPPGKPNPDLEDGPEGEYLTDRLTDEAIDFIEQNKDKPFFLYLSHYAVH 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 266 RPVVARsEELTEKYMNKLGDPKTGQgmetgkkklTTAQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNG----- 340
Cdd:cd16144 197 TPIQAR-PELIEKYEKKKKGLRKGQ---------KNPVYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNGglstr 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 341 -QNIGSNLQLRGKKGYIYEAGIRVPAFVNWPGKVDA-RRTETPVMVTDYFPTFMELAGIDYR--GQLDGQSFAPLFKGED 416
Cdd:cd16144 267 gGPPTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPgSVSDVPVIGTDLYPTFLELAGGPLPppQHLDGVSLVPLLKGGE 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395161703 417 KALQARPIFWHLASEYRNGT--CSIIRKNDMKLIQFLATGELELYDLKKDPKEENNLALKNPETAQLLLKELTGW 489
Cdd:cd16144 347 ADLPRRALFWHFPHYHGQGGrpASAIRKGDWKLIEFYEDGRVELYNLKNDIGETNNLAAEMPEKAAELKKKLDAW 421
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
11-496 |
2.37e-119 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 355.73 E-value: 2.37e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 11 LAFAVLTGGTYAGASTPKVKPNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAY-MYPTCSPSRTALATGK 89
Cdd:COG3119 4 LLLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYvTSPVCSPSRASLLTGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 90 QSFRTGVYTVPVLekgndqvsifSRWTVGEEHIMYSQPLADAGYKSIHLGKWHLvgpypkkemeaswplkkklgqpkpsd 169
Cdd:COG3119 84 YPHRTGVTDNGEG----------YNGGLPPDEPTLAELLKEAGYRTALFGKWHL-------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 170 fswvpyhkehckayypegrgylkniggtyrgdpalevggyksktggyfapfsnpfmdqknpkdkWLTDHLTTEAINFMDE 249
Cdd:COG3119 128 ----------------------------------------------------------------YLTDLLTDKAIDFLER 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 250 H--KEGPFFINLHYYTVHRPVVARsEELTEKYMNK-LGDPKTGQGMETGKKKLTT--AQYATMIESLDDNVGRIAEFLDQ 324
Cdd:COG3119 144 QadKDKPFFLYLAFNAPHAPYQAP-EEYLDKYDGKdIPLPPNLAPRDLTEEELRRarAAYAAMIEEVDDQVGRLLDALEE 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 325 KGLRENTLIIFTSDNGQNIGSNlQLRGKKGYIYEAGIRVPAFVNWPGKVDA-RRTETPVMVTDYFPTFMELAGIDYRGQL 403
Cdd:COG3119 223 LGLADNTIVVFTSDNGPSLGEH-GLRGGKGTLYEGGIRVPLIVRWPGKIKAgSVSDALVSLIDLLPTLLDLAGVPIPEDL 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 404 DGQSFAPLFKGEDKALQaRPIFWHLASEYRNGTcsiIRKNDMKLIQFLA-TGELELYDLKKDPKEENNLALKNPETAQLL 482
Cdd:COG3119 302 DGRSLLPLLTGEKAEWR-DYLYWEYPRGGGNRA---IRTGRWKLIRYYDdDGPWELYDLKNDPGETNNLAADYPEVVAEL 377
|
490
....*....|....
gi 1395161703 483 LKELTGWRKANNVP 496
Cdd:COG3119 378 RALLEAWLKELGDP 391
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
31-489 |
4.92e-111 |
|
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: 335.29 E-value: 4.92e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYMYPTCSPSRTALATGKQSFRTGVYTvpvlekgndqvs 110
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTGVWH------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 111 ifsrwTVGEEHIMYS------QPLADAGYKSIHLGKWHLVGPYPkkemeaswplkkklgqpkpsdfswvpyhkehckaYY 184
Cdd:cd16146 69 -----TILGRERMRLdettlaEVFKDAGYRTGIFGKWHLGDNYP----------------------------------YR 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 185 PEGRG-----YLKN--IGGTY------RGDPALEVGGYKSKTGGYfapfsnpfmdqknpkdkwLTDHLTTEAINFMDEHK 251
Cdd:cd16146 110 PQDRGfdevlGHGGggIGQYPdywgndYFDDTYYHNGKFVKTEGY------------------CTDVFFDEAIDFIEENK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 252 EGPFFINLHYYTVHRPVVARsEELTEKYMNKLGDPKTgqgmetgkkklttAQYATMIESLDDNVGRIAEFLDQKGLRENT 331
Cdd:cd16146 172 DKPFFAYLATNAPHGPLQVP-DKYLDPYKDMGLDDKL-------------AAFYGMIENIDDNVGRLLAKLKELGLEENT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 332 LIIFTSDNGQNIGS----NLQLRGKKGYIYEAGIRVPAFVNWPGKVDA-RRTETPVMVTDYFPTFMELAGIDYR--GQLD 404
Cdd:cd16146 238 IVIFMSDNGPAGGVpkrfNAGMRGKKGSVYEGGHRVPFFIRWPGKILAgKDVDTLTAHIDLLPTLLDLCGVKLPegIKLD 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 405 GQSFAPLFKGEDKALQARPIFWH----LASEYRNGTCSiIRKNDMKLIQFLATGeLELYDLKKDPKEENNLALKNPETAQ 480
Cdd:cd16146 318 GRSLLPLLKGESDPWPERTLFTHsgrwPPPPKKKRNAA-VRTGRWRLVSPKGFQ-PELYDIENDPGEENDVADEHPEVVK 395
|
....*....
gi 1395161703 481 LLLKELTGW 489
Cdd:cd16146 396 RLKAAYEAW 404
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-476 |
1.22e-95 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 295.66 E-value: 1.22e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAY-MYPTCSPSRTALATGKQSFRTGVYtvpvlekGNDQV 109
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYaGAPVCAPSRASLLTGLHTGHTRVR-------GNSEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 110 SIFSRWTvgEEHIMYSQPLADAGYKSIHLGKWHLvGPYPkkemeasWPlkkklGQPKPSDFSwvpYHK-----EHCKAYY 184
Cdd:cd16145 74 GGQDPLP--PDDVTLAEVLKKAGYATAAFGKWGL-GGPG-------TP-----GHPTKQGFD---YFYgyldqVHAHNYY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 185 PEgrgYLkniggtYRGDpalEVGGYKSKTGGYFAPFSNPfmdqKNPKDKWLTDHLTTEAINFMDEHKEGPFFINLHYYTV 264
Cdd:cd16145 136 PE---YL------WRNG---EKVPLPNNVIPPLDEGNNA----GGGGGTYSHDLFTDEALDFIRENKDKPFFLYLAYTLP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 265 HRPVVARSEELtEKYMNKLGDPKTGQGMETGKKKlttaqYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNG---- 340
Cdd:cd16145 200 HAPLQVPDDGP-YKYKPKDPGIYAYLPWPQPEKA-----YAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGphse 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 341 -------QNIGSNLQLRGKKGYIYEAGIRVPAFVNWPGKVDA-RRTETPVMVTDYFPTFMELAGIDYRGQLDGQSFAPLF 412
Cdd:cd16145 274 ggsehdpDFFDSNGPLRGYKRSLYEGGIRVPFIARWPGKIPAgSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTL 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395161703 413 KGEDKALQARPIFWHlasEYRNGTCSIIRKNDMKLIQF-LATGELELYDLKKDPKEENNLALKNP 476
Cdd:cd16145 354 LGKPQQQQHDYLYWE---FYEGGGAQAVRMGGWKAVRHgKKDGPFELYDLSTDPGETNNLAAQHP 415
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
31-472 |
4.34e-82 |
|
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: 260.18 E-value: 4.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYMYPTCSPSRTALATGKQSFRTGVYtvpvlekgNDQVS 110
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQ--------HGVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 111 IFSRWTVGEEHIMYSQPLADAGYKSIHLGKWHLvgpypkkemeaswplkkklGQpkpsdfswvpYHKEHCkayyPEGRG- 189
Cdd:cd16029 73 AGEPYGLPLNETLLPQYLKELGYATHLVGKWHL-------------------GF----------YTWEYT----PTNRGf 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 190 ---YlknigGTYRGDpalevGGYKSKTGGYFAPFSNPFMDQKNP-----KDKWLTDHLTTEAINFMDEH-KEGPFFINLH 260
Cdd:cd16029 120 dsfY-----GYYGGA-----EDYYTHTSGGANDYGNDDLRDNEEpawdyNGTYSTDLFTDRAVDIIENHdPSKPLFLYLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 261 YYTVHRPVVArSEELTEKYMNKLGDPKTGQgmetgkkkltTAQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNG 340
Cdd:cd16029 190 FQAVHAPLQV-PPEYADPYEDKFAHIKDED----------RRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 341 -----QNIGSNLQLRGKKGYIYEAGIRVPAFVNWPGKVDARRTETPVM--VTDYFPTFMELAGIDY--RGQLDGQSFAPL 411
Cdd:cd16029 259 gptggGDGGSNYPLRGGKNTLWEGGVRVPAFVWSPLLPPKRGTVSDGLmhVTDWLPTLLSLAGGDPddLPPLDGVDQWDA 338
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395161703 412 FKGEDKAlQARPIFWHLASEYRNGTCSIIRKNDMKLIqflaTGElELYDLKKDPKEENNLA 472
Cdd:cd16029 339 LSGGAPS-PRTEILLNIDDITRTTGGAAIRVGDWKLI----VGK-PLFNIENDPCERNDLA 393
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
30-472 |
1.65e-81 |
|
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: 258.65 E-value: 1.65e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYMY-PTCSPSRTALATGKQSFRTGVYTVPvlekgndq 108
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAaPVCSPSRAALLTGRYPVRVGLPGVV-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 109 vsIFSRWTVG--EEHIMYSQPLADAGYKSIHLGKWHLvGPYPkkemeASWPLKkkLGqpkpsdFSW---VPYHKEHCKAY 183
Cdd:cd16026 73 --GPPGSKGGlpPDEITIAEVLKKAGYRTALVGKWHL-GHQP-----EFLPTR--HG------FDEyfgIPYSNDMWPFP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 184 YPEGRGYLKNIGGtYRGDPALEvggyksktggyfapfsnPFMDQKNpkdkwLTDHLTTEAINFMDEHKEGPFFINLHYYT 263
Cdd:cd16026 137 LYRNDPPGPLPPL-MENEEVIE-----------------QPADQSS-----LTQRYTDEAVDFIERNKDQPFFLYLAHTM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 264 VHRPVVArSEELTEKymnklgdpkTGQGMetgkkklttaqYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNG--- 340
Cdd:cd16026 194 PHVPLFA-SEKFKGR---------SGAGL-----------YGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwl 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 341 ---QNIGSNLQLRGKKGYIYEAGIRVPAFVNWPGKVDA-RRTETPVMVTDYFPTFMELAGI---DYRgQLDGQSFAPLFK 413
Cdd:cd16026 253 eygGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAgTVSDELASTMDLLPTLAALAGAplpEDR-VIDGKDISPLLL 331
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395161703 414 GEDKALQaRPIFWHLASEYRNGtcsiIRKNDMKLI--------------QFLATGELELYDLKKDPKEENNLA 472
Cdd:cd16026 332 GGSKSPP-HPFFYYYDGGDLQA----VRSGRWKLHlpttyrtgtdpgglDPTKLEPPLLYDLEEDPGETYNVA 399
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-471 |
2.67e-81 |
|
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: 257.53 E-value: 2.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYMYPTCSPSRTALATGKQSFRTGVYtvpvlekgndqvs 110
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVV------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 111 ifsRWTVGEEHIMYSQPLADAGYKSIHLGKWHLVGPYPKKEMeaswplkkklgqpkPSDFSWvpyhKEHCkAYYPEGRGY 190
Cdd:cd16151 68 ---FGYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDGDY--------------PHEFGF----DEYC-LWQLTETGE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 191 LKNIGGTyrGDPALEVGGYKSKTGGYFAPfsnpfmDQknpkdkwLTDHLtteaINFMDEHKEGPFFInlhYYT---VHRP 267
Cdd:cd16151 126 KYSRPAT--PTFNIRNGKLLETTEGDYGP------DL-------FADFL----IDFIERNKDQPFFA---YYPmvlVHDP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 268 VVArseelTEkymnklgDPKTGQGMETGKKKLtTAQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQNIGSNL 347
Cdd:cd16151 184 FVP-----TP-------DSPDWDPDDKRKKDD-PEYFPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITS 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 348 QL-----RGKKGYIYEAGIRVPAFVNWPGKVDARR-TETPVMVTDYFPTFMELAGI--DYRGQLDGQSFAPLFKGEDKAL 419
Cdd:cd16151 251 RTngrevRGGKGKTTDAGTHVPLIVNWPGLIPAGGvSDDLVDFSDFLPTLAELAGAplPEDYPLDGRSFAPQLLGKTGSP 330
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1395161703 420 QARPIFWHLASEYRNGTCSIIRKNDMKLIqflATGelELYDLKKDPKEENNL 471
Cdd:cd16151 331 RREWIYWYYRNPHKKFGSRFVRTKRYKLY---ADG--RFFDLREDPLEKNPL 377
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-472 |
1.27e-73 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 238.25 E-value: 1.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVG-FNGSTYYETPHIDQLANDGLVIKNAYMY-PTCSPSRTALATGKQSFRT-------GVYTVPV 101
Cdd:cd16143 1 PNIVIILADDLGYGDIScYNPDSKIPTPNIDRLAAEGMRFTDAHSPsSVCTPSRYGLLTGRYPWRSrlkggvlGGFSPPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 102 LEKGndqvsifsRWTVGEehiMysqpLADAGYKSIHLGKWHLVGPYPKKemeasWPLKKKLGQPKPSDFSwVPYhkehck 181
Cdd:cd16143 81 IEPD--------RVTLAK---M----LKQAGYRTAMVGKWHLGLDWKKK-----DGKKAATGTGKDVDYS-KPI------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 182 AYYPEGRG--YlkniggtYRGDPALEVGgyksktggyfapfsnpfmdqknpkdkwltDHLTTEAINFMDEHKEG--PFFI 257
Cdd:cd16143 134 KGGPLDHGfdY-------YFGIPASEVL-----------------------------PTLTDKAVEFIDQHAKKdkPFFL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 258 nlhYY---TVHRPVVArSEELTekymnklgdpktgqgmetGKKKLTTaqYATMIESLDDNVGRIAEFLDQKGLRENTLII 334
Cdd:cd16143 178 ---YFalpAPHTPIVP-SPEFQ------------------GKSGAGP--YGDFVYELDWVVGRILDALKELGLAENTLVI 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 335 FTSDNG----------QNIG--SNLQLRGKKGYIYEAGIRVPAFVNWPGKVDA-RRTETPVMVTDYFPTFMELAGIDYRG 401
Cdd:cd16143 234 FTSDNGpspyadykelEKFGhdPSGPLRGMKADIYEGGHRVPFIVRWPGKIPAgSVSDQLVSLTDLFATLAAIVGQKLPD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 402 Q--LDGQSFAPLFKGEDKALQARPIFWHLAseyrNGTcSIIRKNDMKLIqfLATG----------------ELELYDLKK 463
Cdd:cd16143 314 NaaEDSFSFLPALLGPKKQEVRESLVHHSG----NGS-FAIRKGDWKLI--DGTGsggfsyprgkeklglpPGQLYNLST 386
|
....*....
gi 1395161703 464 DPKEENNLA 472
Cdd:cd16143 387 DPGESNNLY 395
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
31-491 |
6.02e-73 |
|
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: 235.87 E-value: 6.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYyETPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYtvpvlekGNDQv 109
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVV-KTPNLDRLAAEGVRFTNAFTtAPVCSPSRSALLTGLYPHQNGAH-------GLRS- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 110 sifSRWTVGEEHIMYSQPLADAGYKSIHLGKWHLVGPYPkkemeaswplkkklgqpkpsdfswvpyhkehckayypegrg 189
Cdd:cd16027 72 ---RGFPLPDGVKTLPELLREAGYYTGLIGKTHYNPDAV----------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 190 ylkniggtYRGDPALEVGGYKSKTGGYFAPFSNPFMDQKnPKDKwltdhltteainfmdehkegPFFINLHYYTVHRPVV 269
Cdd:cd16027 108 --------FPFDDEMRGPDDGGRNAWDYASNAADFLNRA-KKGQ--------------------PFFLWFGFHDPHRPYP 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 270 ARSEELTEKYMNKLGDPKTGQgmETGKKKLTTAQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGqnigsnLQL 349
Cdd:cd16027 159 PGDGEEPGYDPEKVKVPPYLP--DTPEVREDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG------MPF 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 350 RGKKGYIYEAGIRVPAFVNWPGKVDA-RRTETPVMVTDYFPTFMELAGIDYRGQLDGQSFAPLFKGEDKAlqARP-IF-- 425
Cdd:cd16027 231 PRAKGTLYDSGLRVPLIVRWPGKIKPgSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDP--GRDyVFae 308
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395161703 426 --WHLASEYRngtCSIIRKNDMKLIQFLATgeLELYDLKKDPKEENNLAlKNPE---TAQLLLKELTGWRK 491
Cdd:cd16027 309 rdRHDETYDP---IRSVRTGRYKYIRNYMP--EELYDLKNDPDELNNLA-DDPEyaeVLEELRAALDAWMK 373
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
31-407 |
6.93e-73 |
|
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293746 [Multi-domain] Cd Length: 236 Bit Score: 230.79 E-value: 6.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAY-MYPTCSPSRTALATGKQSFRTGVYTVPvlekGNDQV 109
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYvASPVCSPSRASLLTGRYPHRHGVRGNV----GNGGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 110 SIFSRWTVGEEhimysqpLADAGYKSIHLGKWHlvgpypkkemeaswplkkklgqpkpsdfswvpyhkehckayypegrg 189
Cdd:cd16022 77 LPPDEPTLAEL-------LKEAGYRTALIGKWH----------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 190 ylkniggtyrgdpalevggyksktggyfapfsnpfmdqknpkdkwltdhltTEAINFMDEH-KEGPFFINLHYYTVHRPV 268
Cdd:cd16022 103 ---------------------------------------------------DEAIDFIERRdKDKPFFLYVSFNAPHPPF 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 269 VarseeltekymnklgdpktgqgmetgkkklttaqYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQNIGSNlQ 348
Cdd:cd16022 132 A----------------------------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDH-G 176
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 349 LRGKKGYIYEAGIRVPAFVNWPGKVDA-RRTETPVMVTDYFPTFMELAGIDYRGQLDGQS 407
Cdd:cd16022 177 LRGKKGSLYEGGIRVPFIVRWPGKIPAgQVSDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
30-487 |
3.95e-71 |
|
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: 232.80 E-value: 3.95e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYMY-PTCSPSRTALATGKQSFRTGVYTvpvlekgnDQ 108
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTtSICAPSRASILTGQYSHRHGVTD--------NN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 109 VSIFSRWTVgeehiMYSQPLADAGYKSIHLGKWHLvgPYPKKEMEASWplkkklgqpkpsDFsWVPYHkehckayypeGR 188
Cdd:cd16031 74 GPLFDASQP-----TYPKLLRKAGYQTAFIGKWHL--GSGGDLPPPGF------------DY-WVSFP----------GQ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 189 GylkniggTYRGDPALEVGGYKSKTGgyfapfsnpfmdqknpkdkWLTDHLTTEAINFMDEHKEG-PFFINLHYYTVHRP 267
Cdd:cd16031 124 G-------SYYDPEFIENGKRVGQKG-------------------YVTDIITDKALDFLKERDKDkPFCLSLSFKAPHRP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 268 --------------------------VVARSEELTEkYMNKLGDPKTGQGMETGKKKLTTAQYATMIESLDDNVGRIAEF 321
Cdd:cd16031 178 ftpaprhrglyedvtipepetfddddYAGRPEWARE-QRNRIRGVLDGRFDTPEKYQRYMKDYLRTVTGVDDNVGRILDY 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 322 LDQKGLRENTLIIFTSDNGQNIGSNlQLRGKKgYIYEAGIRVPAFVNWPGKVDA-RRTETPVMVTDYFPTFMELAGIDYR 400
Cdd:cd16031 257 LEEQGLADNTIIIYTSDNGFFLGEH-GLFDKR-LMYEESIRVPLIIRDPRLIKAgTVVDALVLNIDFAPTILDLAGVPIP 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 401 GQLDGQSFAPLFKGEDKAlQARPIF----WHLASEYRNGTCSIIRKNDMKLIQFLA-TGELELYDLKKDPKEENNLAlKN 475
Cdd:cd16031 335 EDMQGRSLLPLLEGEKPV-DWRKEFyyeyYEEPNFHNVPTHEGVRTERYKYIYYYGvWDEEELYDLKKDPLELNNLA-ND 412
|
490
....*....|..
gi 1395161703 476 PETAQlLLKELT 487
Cdd:cd16031 413 PEYAE-VLKELR 423
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-471 |
1.00e-69 |
|
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: 228.22 E-value: 1.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYtvpvlekGNDq 108
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSnYPVCSPYRASLLTGQYPLTNGVF-------GND- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 109 vsifsrWTVGEEHIMYSQPLADAGYKSIHLGKWHLVGPYPKKEmeaswplkkklgqpkPSDFSWVPyhkehckayyPEGR 188
Cdd:cd16034 73 ------VPLPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDG---------------RADDYTPP----------PERR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 189 G---YLKniggtyrgdpALEvggyksKTGGYFapfsNPFMDQKNPK----DKWLTDHLTTEAINFMDEH--KEGPFFINL 259
Cdd:cd16034 122 HgfdYWK----------GYE------CNHDHN----NPHYYDDDGKriyiKGYSPDAETDLAIEYLENQadKDKPFALVL 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 260 HYYTVHRPVVARSEELTEKYMNKLGD-----PKTGQGMETGKKKLttAQYATMIESLDDNVGRIAEFLDQKGLRENTLII 334
Cdd:cd16034 182 SWNPPHDPYTTAPEEYLDMYDPKKLLlrpnvPEDKKEEAGLREDL--RGYYAMITALDDNIGRLLDALKELGLLENTIVV 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 335 FTSDNGQNIGSNLQLRgkKGYIYEAGIRVPAFVNWPGKVDARRTE-TPVMVTDYFPTFMELAGIDYRGQLDGQSFAPLFK 413
Cdd:cd16034 260 FTSDHGDMLGSHGLMN--KQVPYEESIRVPFIIRYPGKIKAGRVVdLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLL 337
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395161703 414 GEDKALQARPIF-----WHLASEYRNGTCSIIRKNDMKLIQFLATGELeLYDLKKDPKEENNL 471
Cdd:cd16034 338 GGKDDEPDSVLLqcfvpFGGGSARDGGEWRGVRTDRYTYVRDKNGPWL-LFDNEKDPYQLNNL 399
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
30-471 |
3.21e-69 |
|
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: 226.94 E-value: 3.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLGHGDVGFNGStyyE--TPHIDQLANDGLVIKNAYMYPTCSPSRTALATGKQSFRTGVYTVPVLEKG-- 105
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGG---EipTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTMAELATGkp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 106 ------NDQVSifsrwTVGEEhimysqpLADAGYKSIHLGKWHLVGPypkkemeaswplkkklgqpkpsdfswvpyhkeh 179
Cdd:cd16025 79 gyegylPDSAA-----TIAEV-------LKDAGYHTYMSGKWHLGPD--------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 180 ckayypegrgylkniggtyrgdpalevggyksktgGYFapfsnpfmdqknpkdkwLTDHLTTEAINFMDEHKEG--PFFI 257
Cdd:cd16025 114 -----------------------------------DYY-----------------STDDLTDKAIEYIDEQKAPdkPFFL 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 258 NLHYYTVHRPVVARsEELTEKY------------------MNKLG----DPKTGQGMETGKK--KLTTAQ---------- 303
Cdd:cd16025 142 YLAFGAPHAPLQAP-KEWIDKYkgkydagwdalreerlerQKELGlipaDTKLTPRPPGVPAwdSLSPEEkklearrmev 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 304 YATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNG--QNIG----SNLQLRGKKGYIYEAGIRVPAFVNWPGKVDARR 377
Cdd:cd16025 221 YAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGasAEPGwanaSNTPFRLYKQASHEGGIRTPLIVSWPKGIKAKG 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 378 T--ETPVMVTDYFPTFMELAGIDY----RGQ----LDGQSFAPLFKGEDKALQARPIFWHLAseyrnGTCSiIRKNDMKL 447
Cdd:cd16025 301 GirHQFAHVIDIAPTILELAGVEYpktvNGVpqlpLDGVSLLPTLDGAAAPSRRRTQYFELF-----GNRA-IRKGGWKA 374
|
490 500
....*....|....*....|....*...
gi 1395161703 448 IQFLATG----ELELYDLKKDPKEENNL 471
Cdd:cd16025 375 VALHPPPgwgdQWELYDLAKDPSETHDL 402
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-489 |
5.11e-60 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 202.02 E-value: 5.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYM-----YPTCSPSRTALATGKQSFRtgvytvpvLEK 104
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNmggwsGAVCVPSRAMLMTGRTLFH--------APE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 105 GNDQVSifsrwtvGEEHIMYSQPLADAGYKSIHLGKWHLvgPYPKKEMEAswpLKKKLGQPKPSdFSWVPYHKEHckayy 184
Cdd:cd16155 74 GGKAAI-------PSDDKTWPETFKKAGYRTFATGKWHN--GFADAAIEF---LEEYKDGDKPF-FMYVAFTAPH----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 185 pegrgylkniggtyrgDPalevggyksktggyfapfsnpfmdqKNPKDKWLtDHLTTEAI----NFMDEHkegPFFINLH 260
Cdd:cd16155 136 ----------------DP-------------------------RQAPPEYL-DMYPPETIplpeNFLPQH---PFDNGEG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 261 yytvhrpvVARSEELtekymnkLGDPKTGQGMetgKKKLttAQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNG 340
Cdd:cd16155 171 --------TVRDEQL-------APFPRTPEAV---RQHL--AEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHG 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 341 QNIGSNlQLRGKKGYiYEAGIRVPAFVNWPGKVDARRTETPVMVTDYFPTFMELAGIDYRGQLDGQSFAPLFKGEDKAlq 420
Cdd:cd16155 231 LAVGSH-GLMGKQNL-YEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKA-- 306
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 421 ARPifwHLASEYRNGTCSIIRKnDMKLIQFL-ATGELELYDLKKDPKEENNLAlKNPETAQlLLKELTGW 489
Cdd:cd16155 307 VRD---TLYGAYRDGQRAIRDD-RWKLIIYVpGVKRTQLFDLKKDPDELNNLA-DEPEYQE-RLKKLLAE 370
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
31-472 |
2.16e-57 |
|
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: 195.06 E-value: 2.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTY---YETPHIDQLANDGLVIKNAYMYPTCSPSRTALATGKQSFRTGVYTVPV------ 101
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIgrgAPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGLTTVGLpgspgg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 102 LEKGNdqvsifsrWTVGEEhimysqpLADAGYKSIHLGKWHLvgpypkkemeaswplkkklGQpkpsdfswvpyHKEHck 181
Cdd:cd16142 81 LPPWE--------PTLAEL-------LKDAGYATAQFGKWHL-------------------GD-----------EDGR-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 182 ayYPEGRGYlkniggtyrgDpalEVGGYKSKTggyfapfsnpfMDqknpkdkwltDHLTTEAINFMDEHKEG--PFFINL 259
Cdd:cd16142 114 --LPTDHGF----------D---EFYGNLYHT-----------ID----------EEIVDKAIDFIKRNAKAdkPFFLYV 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 260 HYYTVHRPVVARseeltEKYMNKLgdpkTGQGmetgkkklttaQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDN 339
Cdd:cd16142 158 NFTKMHFPTLPS-----PEFEGKS----SGKG-----------KYADSMVELDDHVGQILDALDELGIADNTIVIFTTDN 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 340 GQNI-----GSNLQLRGKKGYIYEAGIRVPAFVNWPGKVDARRTETPVM-VTDYFPTFMELAGID--------YRGQLDG 405
Cdd:cd16142 218 GPEQdvwpdGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVsHLDWFPTLAALAGAPdpkdkllgKDRHIDG 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 406 QSFAPLFKGEDKALQARPIFWhlaseYRNGTCSIIRKNDMKLI--QFLATGEL-----------ELYDLKKDPKEENNLA 472
Cdd:cd16142 298 VDQSPFLLGKSEKSRRSEFFY-----FGEGELGAVRWKNWKVHfkAQEDTGGPtgepfyvltfpLIFNLRRDPKERYDVT 372
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-494 |
2.18e-53 |
|
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: 185.50 E-value: 2.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYTVPVLEKGNDQV 109
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTpSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 110 SIFSRWTvgeehimYSQPLADAGYKSIHLGKWHlVGPypkkemeaswplkkklgQPKPSDFSWVPYH-KEHCKAYYpegr 188
Cdd:cd16033 81 LPPGVET-------FSEDLREAGYRNGYVGKWH-VGP-----------------EETPLDYGFDEYLpVETTIEYF---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 189 gylkniggtyrgdpalevggyksktggyfapfsnpfmdqknpkdkwltdhLTTEAINFMDEHKEG--PFFINLHYYTVHR 266
Cdd:cd16033 132 --------------------------------------------------LADRAIEMLEELAADdkPFFLRVNFWGPHD 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 267 PVVARSE----------ELTEKYMNKLGDPKTGQGMETGKKKLTTAQ----------YATMIESLDDNVGRIAEFLDQKG 326
Cdd:cd16033 162 PYIPPEPyldmydpediPLPESFADDFEDKPYIYRRERKRWGVDTEDeedwkeiiahYWGYITLIDDAIGRILDALEELG 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 327 LRENTLIIFTSDNGQNIGSNLQLRgkKGYI-YEAGIRVPAFVNWPGKVDA-RRTETPVMVTDYFPTFMELAGIDYRGQLD 404
Cdd:cd16033 242 LADDTLVIFTSDHGDALGAHRLWD--KGPFmYEETYRIPLIIKWPGVIAAgQVVDEFVSLLDLAPTILDLAGVDVPPKVD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 405 GQSFAPLFKGEDKALQARPIFwhlaSEYrNG-----TCSIIRKNDMKLIqFLATGELELYDLKKDPKEENNLALKNP--E 477
Cdd:cd16033 320 GRSLLPLLRGEQPEDWRDEVV----TEY-NGhefylPQRMVRTDRYKYV-FNGFDIDELYDLESDPYELNNLIDDPEyeE 393
|
490
....*....|....*..
gi 1395161703 478 TAQLLLKELTGWRKANN 494
Cdd:cd16033 394 ILREMRTRLYEWMEETG 410
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
30-477 |
8.80e-53 |
|
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: 184.31 E-value: 8.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLGHgDVGFNGSTYYETPHIDQLANDGLVIKNAY-MYPTCSPSRTALATGKQSFRTGVYtvpvlekGNDQ 108
Cdd:cd16030 2 KPNVLFIAVDDLRP-WLGCYGGHPAKTPNIDRLAARGVLFTNAYcQQPVCGPSRASLLTGRRPDTTGVY-------DNNS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 109 vsifSRWTVGEEHIMYSQPLADAGYKSIHLGK-WHlVGPYPKKEMEASWPlkkklgqpkpsdfswVPYHKEHCKAYYPEG 187
Cdd:cd16030 74 ----YFRKVAPDAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWD---------------EPPNPPGPEKYPPGK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 188 RGYLKNIGGTYRGDPALEVggyksktggyfapfsnpfmdqKNPKDKWLTDHLTTE-AINFMDEHKEG--PFFINLHYYTV 264
Cdd:cd16030 134 LCPGKKGGKGGGGGPAWEA---------------------ADVPDEAYPDGKVADeAIEQLRKLKDSdkPFFLAVGFYKP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 265 HRPVVA-------------------RSEELTEKYMNKLGD-PKTGQGMETGK------------KKLTTAQYATmIESLD 312
Cdd:cd16030 193 HLPFVApkkyfdlyplesiplpnpfDPIDLPEVAWNDLDDlPKYGDIPALNPgdpkgplpdeqaRELRQAYYAS-VSYVD 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 313 DNVGRIAEFLDQKGLRENTLIIFTSDNGQNIGSNLQLRgkKGYIYEAGIRVPAFVNWPG-KVDARRTETPVMVTDYFPTF 391
Cdd:cd16030 272 AQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWG--KHTLFEEATRVPLIIRAPGvTKPGKVTDALVELVDIYPTL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 392 MELAGIDYRGQLDGQSFAPLFKGEDKAlQARPIFwhlaSEYRNGT---CSiIRKNDMKLIQ---FLATGELELYDLKKDP 465
Cdd:cd16030 350 AELAGLPAPPCLEGKSLVPLLKNPSAK-WKDAAF----SQYPRPSimgYS-IRTERYRYTEwvdFDKVGAEELYDHKNDP 423
|
490
....*....|..
gi 1395161703 466 KEENNLAlKNPE 477
Cdd:cd16030 424 NEWKNLA-NDPE 434
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-465 |
1.07e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 170.42 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYTvpvlekgNDQV 109
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTpSPICVPSRASFLTGRYVHETGVWD-------NADP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 110 sifsrwtVGEEHIMYSQPLADAGYKSIHLGKWHLVGPypkkemeaswplkkklGQPkpsdfswvpyhkehckayypegrg 189
Cdd:cd16037 74 -------YDGDVPSWGHALRAAGYETVLIGKLHFRGE----------------DQR------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 190 ylkniggtyrgdpalevggyksktGGYFapfsnpfmdqknpKDkwltDHLTTEAINFMDEH--KEGPFFINLHYYTVHRP 267
Cdd:cd16037 107 ------------------------HGFR-------------YD----RDVTEAAVDWLREEaaDDKPWFLFVGFVAPHFP 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 268 VVARsEELTEKYMnklgdpktgqgmetgkKKLTTAQYAtMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQNIGSnl 347
Cdd:cd16037 146 LIAP-QEFYDLYV----------------RRARAAYYG-LVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGE-- 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 348 qlRG--KKGYIYEAGIRVPAFVNWPGKVDARRTETPVMVTDYFPTFMELAGIDYRGQLDGQSFAPLFKGEDKAlqARPIF 425
Cdd:cd16037 206 --RGlwGKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEGPDDP--DRVVF 281
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1395161703 426 whlaSEY--RNGTCSI--IRKNDMKLIQFLATGElELYDLKKDP 465
Cdd:cd16037 282 ----SEYhaHGSPSGAfmLRKGRWKYIYYVGYPP-QLFDLENDP 320
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-468 |
1.54e-45 |
|
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: 163.29 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHgDV--GFN-GSTYYETPHIDQLANDGLVIKNAYMYPTCSPSRTALATGKQSFRTGVYTVPVLEKGND 107
Cdd:cd16154 1 PNILLIIADDQGL-DSsaQYSlSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 108 QVSIFSRwtVGEEhimysqplADAGYKSIHLGKWHLVGpypkkemeaswplkkklGQPKPSDFSWVPYhkehckayypeg 187
Cdd:cd16154 80 ETLLQLL--IKDA--------TTAGYSSAVIGKWHLGG-----------------NDNSPNNPGGIPY------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 188 rgYLKNIGGTyrgdpaleVGGYksktggYFAPFSNPfmDQKNPKDKWLTDHLTTEAINFMDEHKEgPFFINLHYYTVHRP 267
Cdd:cd16154 121 --YAGILGGG--------VQDY------YNWNLTNN--GQTTNSTEYATTKLTNLAIDWIDQQTK-PWFLWLAYNAPHTP 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 268 VVARSEELTEKYMnklgdpkTGQGMETGKKKLTTaqYATMIESLDDNVGRIAEFLDQKgLRENTLIIFTSDNG---QNIG 344
Cdd:cd16154 182 FHLPPAELHSRSL-------LGDSADIEANPRPY--YLAAIEAMDTEIGRLLASIDEE-ERENTIIIFIGDNGtpgQVVD 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 345 SNLQLRGKKGYIYEAGIRVPAFVNWPGKVDARRTETP-VMVTDYFPTFMELAGIDYRGQLDGQSFAPLFKGEDKALQArp 423
Cdd:cd16154 252 LPYTRNHAKGSLYEGGINVPLIVSGAGVERANERESAlVNATDLYATIAELAGVDAAEIHDSVSFKPLLSDVNASTRQ-- 329
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1395161703 424 ifwHLASEYRNGTCS--IIRKNDMKLIQFlATGELELYDLKKDPKEE 468
Cdd:cd16154 330 ---YNYTEYESPTTTgwATRNQYYKLIES-ENGQEELYDLINDPSEQ 372
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
30-491 |
1.79e-45 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 166.00 E-value: 1.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLgHGD-VGFNGSTYYETPHIDQLANDGLVIKNAY-MYPTCSPSRTALATGKQSFRTGV--Ytvpvlekg 105
Cdd:PRK13759 6 KPNIILIMVDQM-RGDcLGCNGNKAVETPNLDMLASEGYNFENAYsAVPSCTPARAALLTGLSQWHHGRvgY-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 106 NDQVSIFSRWTVGEEhimysqpLADAGYKSIHLGKWHLvgpypkkemeasWPLKKKLGqpkpsdFSWVPYHKehckayyp 185
Cdd:PRK13759 77 GDVVPWNYKNTLPQE-------FRDAGYYTQCIGKMHV------------FPQRNLLG------FHNVLLHD-------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 186 egrGYLKNiGGTYRGDPALEVGGY----KSKTGGYFAPFSNPFMDQKN------PKDKWL--TDHLTTEAINFM---DEH 250
Cdd:PRK13759 124 ---GYLHS-GRNEDKSQFDFVSDYlawlREKAPGKDPDLTDIGWDCNSwvarpwDLEERLhpTNWVGSESIEFLrrrDPT 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 251 KegPFFINLHYYTVHRP-------------------VVARSEELTEKYMNKlGDPKTGQGmETGKKKLTTAQ--YATMIE 309
Cdd:PRK13759 200 K--PFFLKMSFARPHSPydppkryfdmykdadipdpHIGDWEYAEDQDPEG-GSIDALRG-NLGEEYARRARaaYYGLIT 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 310 SLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQNIGSNLQLRgkKGYIYEAGIRVPAFVNWPGKV----DARRTETPVMVT 385
Cdd:PRK13759 276 HIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFR--KGYPYEGSAHIPFIIYDPGGLlagnRGTVIDQVVELR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 386 DYFPTFMELAGIDYRGQLDGQSFAPLFKGEDKALqaRPifwHLASEYRNGTCSI--IRKNDMKLIQFLATGELELYDLKK 463
Cdd:PRK13759 354 DIMPTLLDLAGGTIPDDVDGRSLKNLIFGQYEGW--RP---YLHGEHALGYSSDnyLTDGKWKYIWFSQTGEEQLFDLKK 428
|
490 500
....*....|....*....|....*...
gi 1395161703 464 DPKEENNLAlkNPETAQlllKELTGWRK 491
Cdd:PRK13759 429 DPHELHNLS--PSEKYQ---PRLREMRK 451
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
31-494 |
1.51e-43 |
|
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: 159.73 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLgHGD-VGFNGSTYYETPHIDQLANDGLVIKNAY-MYPTCSPSRTALATGKQSFRTGVY--TVPvLEKGN 106
Cdd:cd16028 1 RNVLFITADQW-RADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYtQAAPCGPSRASLYTGRYLMNHRSVwnGTP-LDARH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 107 DqvsifsrwTVGEEhimysqpLADAGYKSIHLGKWHLVgpypkkemeaswplkkklgqPKPsdfswvpyhkehckayype 186
Cdd:cd16028 79 L--------TLALE-------LRKAGYDPALFGYTDTS--------------------PDP------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 187 grgylkniGGTYRGDPALevGGYKSKTGGYFAPFSNPFMdqknPKDKWLTDHLTTEAINFMDEHKEGPFFINLHYYTVHR 266
Cdd:cd16028 105 --------RGLAPLDPRL--LSYELAMPGFDPVDRLDEY----PAEDSDTAFLTDRAIEYLDERQDEPWFLHLSYIRPHP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 267 PVVA-----------------RSEELTEK---------YMNKLGDPKTGQGMETGKK--KLTTAQ----YATMIESLDDN 314
Cdd:cd16028 171 PFVApapyhalydpadvpppiRAESLAAEaaqhpllaaFLERIESLSFSPGAANAADldDEEVAQmratYLGLIAEVDDH 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 315 VGRIAEFLDQKGLRENTLIIFTSDNGQNIGSNlQLRGKKGYiYEAGIRVPAFVNWPG-KVDA---RRTETPVMVTDYFPT 390
Cdd:cd16028 251 LGRLFDYLKETGQWDDTLIVFTSDHGEQLGDH-WLWGKDGF-FDQAYRVPLIVRDPRrEADAtrgQVVDAFTESVDVMPT 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 391 FMELAGIDYRGQLDGQSFAPLFKGEDKALQARPIFWHLASEYRNGT------------CS--IIRKNDMKLIQFLATGEL 456
Cdd:cd16028 329 ILDWLGGEIPHQCDGRSLLPLLAGAQPSDWRDAVHYEYDFRDVSTRrpqealglspdeCSlaVIRDERWKYVHFAALPPL 408
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1395161703 457 eLYDLKKDPKEENNLAlKNPETAQLLLK---ELTGWRKANN 494
Cdd:cd16028 409 -LFDLKNDPGELRDLA-ADPAYAAVVLRyaqKLLSWRMRHA 447
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
31-397 |
4.57e-43 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 154.50 E-value: 4.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYTVPVLEKGNDQV 109
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSgGTLTAPSRFALLTGLPPHNFGSYVSTPVGLPRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 110 SIFsRWtvgeehimysqpLADAGYKSIHLGKWHLvGPYPKkemeaswplkkklGQPKPSDFSWVPYHkehckayypegrg 189
Cdd:pfam00884 81 SLP-DL------------LKRAGYNTGAIGKWHL-GWYNN-------------QSPCNLGFDKFFGR------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 190 ylkNIGGTYRGDPalevggyksktggyfaPFSNPFMDQKNPKDKWLTDhlttEAINFMDEHKEgPFFINLHYYTVHRPVV 269
Cdd:pfam00884 121 ---NTGSDLYADP----------------PDVPYNCSGGGVSDEALLD----EALEFLDNNDK-PFFLVLHTLGSHGPPY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 270 ArSEELTEKYMNKLGDPKTGQGMetgkkkltTAQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQNIG-SNLQ 348
Cdd:pfam00884 177 Y-PDRYPEKYATFKPSSCSEEQL--------LNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGeGGGY 247
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1395161703 349 LRGKKGYI-YEAGIRVPAFVNWPG-KVDARRTETPVMVTDYFPTFMELAGI 397
Cdd:pfam00884 248 LHGGKYDNaPEGGYRVPLLIWSPGgKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
30-472 |
9.18e-43 |
|
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: 156.56 E-value: 9.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLghgDVGFNGSTYYeTPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYTV--------P 100
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPM-PKTKKLLADQGTTFTNAFVtTPLCCPSRASILTGQYAHNHGVTNNsppgggypK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 101 VLEKGNDQvSIFSRWtvgeehimysqpLADAGYKSIHLGKwHLVGpYPKKEMeaswplkkklGQPKPSDFSWvpYHKEHC 180
Cdd:cd16147 77 FWQNGLER-STLPVW------------LQEAGYRTAYAGK-YLNG-YGVPGG----------VSYVPPGWDE--WDGLVG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 181 KAYYpegRGYLKNIGGtyrgdpalEVGGYKSKTGGYfapfsnpfmdqknpkdkwLTDHLTTEAINFMDEHKEG--PFFIN 258
Cdd:cd16147 130 NSTY---YNYTLSNGG--------NGKHGVSYPGDY------------------LTDVIANKALDFLRRAAADdkPFFLV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 259 LHYYTVHRPVV-----------ARSEELTEKYMNKLGDPKTGQGmetGKKKLTTAQYATM-------IESL---DDNVGR 317
Cdd:cd16147 181 VAPPAPHGPFTpapryanlfpnVTAPPRPPPNNPDVSDKPHWLR---RLPPLNPTQIAYIdelyrkrLRTLqsvDDLVER 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 318 IAEFLDQKGLRENTLIIFTSDNGQNIGsNLQLRGKKGYIYEAGIRVPAFVNWPGKVDARRTETPVMVTDYFPTFMELAGI 397
Cdd:cd16147 258 LVNTLEATGQLDNTYIIYTSDNGYHLG-QHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGA 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395161703 398 DYRGQLDGQSFAPlfkgedkalqarpifwhlaseYRNGTCSIIRKNDMKLIQFL---ATGELELYDLKKDPKEENNLA 472
Cdd:cd16147 337 PPPSDMDGRSCGD---------------------SNNNTYKCVRTVDDTYNLLYfewCTGFRELYDLTTDPYQLTNLA 393
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
30-446 |
9.80e-42 |
|
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: 155.32 E-value: 9.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAY-MYPTCSPSRTALATGKQSFRTGVYTvpvlEKGNDQ 108
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYsANPLCSPSRAALLTGRLPIRNGFYT----TNAHAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 109 VSIFSRWTVG---EEHIMYSQPLADAGYKSIHLGKWHLvgpypkkemeaswplkkklgqpkpsdfswvpyhkEHCKAYYP 185
Cdd:cd16157 77 NAYTPQNIVGgipDSEILLPELLKKAGYRNKIVGKWHL----------------------------------GHRPQYHP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 186 egrgyLKNIGGTYRGDPALEVGGYKSK-------------TGGYFAPFSnpfMDQKNPKDKwLTDHLTTEAINFMDEH-- 250
Cdd:cd16157 123 -----LKHGFDEWFGAPNCHFGPYDNKaypnipvyrdwemIGRYYEEFK---IDKKTGESN-LTQIYLQEALEFIEKQhd 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 251 KEGPFFInlhYYTV---HRPVVArseeltekymnklgdpktgqgmetGKKKLTTAQ---YATMIESLDDNVGRIAEFLDQ 324
Cdd:cd16157 194 AQKPFFL---YWAPdatHAPVYA------------------------SKPFLGTSQrglYGDAVMELDSSVGKILESLKS 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 325 KGLRENTLIIFTSDNG-------QNIGSNLQLRGKKGYIYEAGIRVPAFVNWPGKVDARRTETPV-MVTDYFPTFMELAG 396
Cdd:cd16157 247 LGIENNTFVFFSSDNGaalisapEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIKPGQVSHQLgSLMDLFTTSLALAG 326
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1395161703 397 IDYRG--QLDGQSFAPLFKgeDKALQARPIFWhlaseYRNGTCSIIRKNDMK 446
Cdd:cd16157 327 LPIPSdrAIDGIDLLPVLL--NGKEKDRPIFY-----YRGDELMAVRLGQYK 371
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
30-470 |
1.58e-41 |
|
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: 153.01 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLGHGDVGFNGS-TYYETPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYTVPVLEkgnd 107
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSaASVCSPSRASLMTGRLGLRNGVGHNFLPT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 108 qvsifsrwTVG----EEHIMYSQpLADAGYKSIHLGKWHLvgpypkkemeaswplkkklgqpkpsdfswvpyhkEHCKAY 183
Cdd:cd16161 77 --------SVGglplNETTLAEV-LRQAGYATGMIGKWHL----------------------------------GQREAY 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 184 YPEGRGYlkniggtyrgdpalevggyksktGGYFA-PFSNpfmdqknpkDKWLTDHLTTEAINFMDEHKEG--PFFINLH 260
Cdd:cd16161 114 LPNSRGF-----------------------DYYFGiPFSH---------DSSLADRYAQFATDFIQRASAKdrPFFLYAA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 261 YYTVHRPvvarseeltEKYMNKLGDPKTGQGMetgkkklttaqYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNG 340
Cdd:cd16161 162 LAHVHVP---------LANLPRFQSPTSGRGP-----------YGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNG 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 341 Q--------------NIGSNLQLRGKKGYIYEAGIRVPAFVNWPGKVDARRTETP-VMVTDYFPTFMELAGID---YRgQ 402
Cdd:cd16161 222 PwevkcelavgpgtgDWQGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAAlVSTLDIFPTVVALAGASlppGR-I 300
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395161703 403 LDGQSFAPLFKGEDKALQARPIFWHlASEYRNGTCSIIRKNDMKLiqFLATGELELYDLKKDPKEENN 470
Cdd:cd16161 301 YDGKDLSPVLFGGSKTGHRCLFHPN-SGAAGAGALSAVRCGDYKA--HYATGGALACCGSTGPKLYHD 365
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
30-427 |
1.67e-41 |
|
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: 154.12 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYMYPT-CSPSRTALATGKQSFRTGVYTvpvlekgndQ 108
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSvCTPSRAALLTGRLPIRSGMYG---------G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 109 VSIFSRWTVG---EEHIMYSQPLADAGYKSIHLGKWHLvgpypkkemeaswplkkKLGQPKPSDFSWVPYHKehckayyp 185
Cdd:cd16160 72 TRVFLPWDIGglpKTEVTMAEALKEAGYTTGMVGKWHL-----------------GINENNHSDGAHLPSHH-------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 186 eGRGYLKNI---GGTYRGDPAlevggyksktgGYFAPFSNP---FMDQKNP------KDKWLTDHLTTEAINFMDEHKEG 253
Cdd:cd16160 127 -GFDFVGTNlpfTNSWACDDT-----------GRHVDFPDRsacFLYYNDTiveqpiQHEHLTETLVGDAKSFIEDNQEN 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 254 PFFINLHYYTVHRPVVArSEELTEKYMNklgdpktgqgmetgkkklttAQYATMIESLDDNVGRIAEFLDQKGLRENTLI 333
Cdd:cd16160 195 PFFLYFSFPQTHTPLFA-SKRFKGKSKR--------------------GRYGDNINEMSWAVGEVLDTLVDTGLDQNTLV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 334 IFTSDNG------QNIGSNLQLRGKKGYIYEAGIRVPAFVNWPGKVDARRTETPVMVTDYFPTFMELAG--IDYRGQLDG 405
Cdd:cd16160 254 FFLSDHGphveycLEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGgtLPTDRIYDG 333
|
410 420
....*....|....*....|..
gi 1395161703 406 QSFAPLFKGEDKAlQARPIFWH 427
Cdd:cd16160 334 LSITDLLLGEADS-PHDDILYY 354
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
31-465 |
3.03e-41 |
|
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: 150.42 E-value: 3.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYtvpvlekgnDQV 109
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCnSPLCAPSRASMMTGRLPSRIGAY---------DNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 110 SIFSRwtvgeehimySQP-----LADAGYKSIHLGKWHLVGPypkkemeaswplkkklGQpkpsdfswvpYHkehckayy 184
Cdd:cd16032 72 AEFPA----------DIPtfahyLRAAGYRTALSGKMHFVGP----------------DQ----------LH-------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 185 pegrGYlkniggtyrgDPALEVGgYKSKtggyfapfsnpfmdqknpkdKWLTDHltteainfMDEHKEGPFFINLHYYTV 264
Cdd:cd16032 108 ----GF----------DYDEEVA-FKAV--------------------QKLYDL--------ARGEDGRPFFLTVSFTHP 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 265 HRPVVARsEELTEKYMnklgdpktgqgmetgkKKLTTAQYAtMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQNIG 344
Cdd:cd16032 145 HDPYVIP-QEYWDLYV----------------RRARRAYYG-MVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLG 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 345 SnlqlRG---KKGYiYEAGIRVPAFVNWPGKVDARRTETPVMVTDYFPTFMELAGI---DYRGQLDGQSFAPLFKGEDKA 418
Cdd:cd16032 207 E----RGlwyKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGgtaPHVPPLDGRSLLPLLEGGDSG 281
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1395161703 419 LqARPIFwhlaSEYR-NGTCS---IIRKNDMKLIQFLATGELeLYDLKKDP 465
Cdd:cd16032 282 G-EDEVI----SEYLaEGAVApcvMIRRGRWKFIYCPGDPDQ-LFDLEADP 326
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-410 |
7.74e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 147.69 E-value: 7.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYTVPVLEkgnDQV 109
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSgSNPTLPSRFSLFTGLYPFYHGVWGGPLEP---DDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 110 SIFSRwtvgeehimysqpLADAGYKSihlgkwHLVgpypkkemeaswplkkklgqpkpSDFSWvpyhkehckayYPEGRG 189
Cdd:cd16148 78 TLAEI-------------LRKAGYYT------AAV-----------------------SSNPH-----------LFGGPG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 190 YLKniggtyrgdpalevggyksktgGYFAPFSNPFMDQKNPKDKWLTDHLTTE-AINFMDEHK-EGPFFINLHYYTVHRP 267
Cdd:cd16148 105 FDR----------------------GFDTFEDFRGQEGDPGEEGDERAERVTDrALEWLDRNAdDDPFFLFLHYFDPHEP 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 268 vvarseeltekYmnklgdpktgqgmetgkkklttaQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQNIGSNL 347
Cdd:cd16148 163 -----------Y-----------------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHG 208
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395161703 348 QLRGKKGYIYEAGIRVPAFVNWPGKVDARRTETPVMVTDYFPTFMELAGIDYRGQLDGQSFAP 410
Cdd:cd16148 209 LYWGHGSNLYDEQLHVPLIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
30-417 |
9.17e-41 |
|
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: 153.60 E-value: 9.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIK-NAYMYPTCSPSRTALATGKQSFRTGVYTVpvlekGNDQ 108
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLThHLAAAPLCTPSRAAFLTGRYPIRSGMASS-----HGMR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 109 VSIFSRWTVG--EEHIMYSQPLADAGYKSIHLGKWHLVGPYPKKEMEASWPLKK-------------KLGQPKPSDFSWV 173
Cdd:cd16159 76 VILFTASSGGlpPNETTFAEVLKQQGYSTALIGKWHLGLHCESRNDFCHHPLNHgfdyfyglpltnlKDCGDGSNGEYDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 174 PYhkehcKAYYPEGRGYLKNIGGTYRG---DPALEVGGYKSKTGGYFAPFSNPF-----------------------MDQ 227
Cdd:cd16159 156 SF-----DPLFPLLTAFVLITALTIFLllyLGAVSKRFFVFLLILSLLFISLFFlllitnryfncilmrnhevveqpMSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 228 KNpkdkwLTDHLTTEAINFMDEHKEGPFFINLHYYTVHRPVVArseelTEKYmnklgdpktgqgmeTGKKKltTAQYATM 307
Cdd:cd16159 231 EN-----LTQRLTKEAISFLERNKERPFLLVMSFLHVHTALFT-----SKKF--------------KGRSK--HGRYGDN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 308 IESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQNI-----------GSNLQLRGKKGYIYEAGIRVPAFVNWPGKVDA- 375
Cdd:cd16159 285 VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPg 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1395161703 376 RRTETPVMVTDYFPTFMELAGI---DYRgQLDGQSFAPLFKGEDK 417
Cdd:cd16159 365 SVIDEPTSLMDIFPTVAALAGAplpSDR-IIDGRDLMPLLTGQEK 408
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
30-482 |
9.48e-41 |
|
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: 152.98 E-value: 9.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYtvP-VLEKGnd 107
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSsSPVCSPSRAALLTGRYQVRSGVY--PgVFYPG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 108 qvsifSRWTVGEEHIMYSQPLADAGYKSIHLGKWHL-VGPyPKKEMEASWPLKKKLGQPKPSDFSwvPYHKEHCkaYYPE 186
Cdd:cd16158 77 -----SRGGLPLNETTIAEVLKTVGYQTAMVGKWHLgVGL-NGTYLPTHQGFDHYLGIPYSHDQG--PCQNLTC--FPPN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 187 GRGYlkniGGTYRGDPALEVggyksktggyfapFSNPFMDQKNPKDKWLTDHLTTEAINFM-DEHKEG-PFFINLHYYTV 264
Cdd:cd16158 147 IPCF----GGCDQGEVPCPL-------------FYNESIVQQPVDLLTLEERYAKFAKDFIaDNAKEGkPFFLYYASHHT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 265 HRPVVArseelTEKYMNklgdpKTGQGmetgkkklttaQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQNI- 343
Cdd:cd16158 210 HYPQFA-----GQKFAG-----RSSRG-----------PFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTm 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 344 -----GSNLQLRGKKGYIYEAGIRVPAFVNWPGKVDARRTETPVMVTDYFPTFMELAG-IDYRGQLDGQSFAPLFKGEDK 417
Cdd:cd16158 269 rksrgGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTHELASTLDILPTIAKLAGaPLPNVTLDGVDMSPILFEQGK 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 418 AL---------QARPIF------WH--LASEYRNGT--CSIIRKNDMKLIQFLATGELE-LYDLKKDPKEENNLaLKNPE 477
Cdd:cd16158 349 SPrqtffyyptSPDPDKgvfavrWGkyKAHFYTQGAahSGTTPDKDCHPSAELTSHDPPlLFDLSQDPSENYNL-LGLPE 427
|
....*
gi 1395161703 478 TAQLL 482
Cdd:cd16158 428 YNQVL 432
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-410 |
3.94e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 145.46 E-value: 3.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAY-MYPTCSPSRTALATGKQSFRTGVYTVpVLEKGNDQV 109
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFcTSPVCSPARASLLTGRMPSQHGIHDW-IVEGSHGKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 110 SIFSRWTvgEEHIMYSQPLADAGYKSIHLGKWHLvgpypkkemeaswplkkklgqpkpsdfswvpyhkehckayypegrg 189
Cdd:cd16149 80 KKPEGYL--EGQTTLPEVLQDAGYRCGLSGKWHL---------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 190 ylkniggtyrGDPALEvggyksktggyfapfsnpFMDQKNPKDKwltdhltteainfmdehkegPFFINLHYYTVHRPvv 269
Cdd:cd16149 112 ----------GDDAAD------------------FLRRRAEAEK--------------------PFFLSVNYTAPHSP-- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 270 arseeltekymnklgdpktgqgmetgkkklttAQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQNIGSNlQL 349
Cdd:cd16149 142 --------------------------------WGYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHH-GI 188
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395161703 350 RGK-KGYI----YEAGIRVPAFVNWPGKVDA-RRTETPVMVTDYFPTFMELAGIDYRGQ--LDGQSFAP 410
Cdd:cd16149 189 WGKgNGTFplnmYDNSVKVPFIIRWPGVVPAgRVVDSLVSAYDFFPTLLELAGVDPPADprLPGRSFAD 257
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-480 |
5.85e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 134.66 E-value: 5.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYTvpvlekgNDQ 108
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTpQPVCGPARACLQTGLYPTETGCFR-------NGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 109 VSIFSRWTVGEEhimysqpLADAGYKSIHLGKWHLVGpypkkemeaswplkkklgqpkpsdfswvpyhkehckayypegr 188
Cdd:cd16152 74 PLPADEKTLAHY-------FRDAGYETGYVGKWHLAG------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 189 gylkniggtYRgdpalevggyksktggyfapfsnpfmdqknpkdkwlTDHLTTEAINFMDEH-KEGPFFINLHYYTVH-- 265
Cdd:cd16152 104 ---------YR------------------------------------VDALTDFAIDYLDNRqKDKPFFLFLSYLEPHhq 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 266 ---RPVVArSEELTEKYMNKL--GDPKTGQGmeTGKKKLttAQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNg 340
Cdd:cd16152 139 ndrDRYVA-PEGSAERFANFWvpPDLAALPG--DWAEEL--PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 341 qniGSNLQLRGK--KGYIYEAGIRVPAFVNWPGKVDARRTETPVMVTDYFPTFMELAGIDYRGQLDGQSFAPLFKGEDka 418
Cdd:cd16152 213 ---GCHFRTRNAeyKRSCHESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKV-- 287
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395161703 419 lQARP--IFWHLaSEYRNGTCsiIRKNDMKLIQFLATG------------ELELYDLKKDPKEENNLAlKNPETAQ 480
Cdd:cd16152 288 -EDWRneVFIQI-SESQVGRA--IRTDRWKYSVAAPDKdgwkdsgsdvyvEDYLYDLEADPYELVNLI-GRPEYRE 358
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
31-489 |
4.52e-31 |
|
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: 125.19 E-value: 4.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAY-MYPTCSPSRTALATGKQSFRTGVYT--VPVlekgND 107
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYtTQPVCGPARSGLFTGLYPHTNGSWTncMAL----GD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 108 QVSifsrwTVGeehimysQPLADAGYKSIHLGKWHLVGpypkkemeaswplkkklgqpkpSDF--------SWVPyhkeh 179
Cdd:cd16156 77 NVK-----TIG-------QRLSDNGIHTAYIGKWHLDG----------------------GDYfgngicpqGWDP----- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 180 ckAYYPEGRGYLKNIGGTYRgdpalevggYKSKTGgyfapfsNPFMDQKNPKDKWLTDHLTTE-AINFMDEHKEGPFFIN 258
Cdd:cd16156 118 --DYWYDMRNYLDELTEEER---------RKSRRG-------LTSLEAEGIKEEFTYGHRCTNrALDFIEKHKDEDFFLV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 259 LHYYTVHRPVVArSEELTEKY------------MNKLGDP-------KTGQGMETGKKKLTTAQYATMIESLDDNVGRIA 319
Cdd:cd16156 180 VSYDEPHHPFLC-PKPYASMYkdfefpkgenayDDLENKPlhqrlwaGAKPHEDGDKGTIKHPLYFGCNSFVDYEIGRVL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 320 EFLDQKglRENTLIIFTSDNGQNIGSNlQLRGKKGYIYEAGIRVPAFVNWPGKVDARRT-ETPVMVTDYFPTFMELAGID 398
Cdd:cd16156 259 DAADEI--AEDAWVIYTSDHGDMLGAH-KLWAKGPAVYDEITNIPLIIRGKGGEKAGTVtDTPVSHIDLAPTILDYAGIP 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 399 YRGQLDGQSFAPLFkgEDKALQA-RPIFwhlaSEYR--------NGTCSIIR---KNDMKLIQFLATGElELYDLKKDPK 466
Cdd:cd16156 336 QPKVLEGESILATI--EDPEIPEnRGVF----VEFGryevdhdgFGGFQPVRcvvDGRYKLVINLLSTD-ELYDLEKDPY 408
|
490 500
....*....|....*....|....*.
gi 1395161703 467 EENNLaLKNPETAQL---LLKELTGW 489
Cdd:cd16156 409 EMHNL-IDDPDYADVrdqLHDELLDY 433
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-489 |
1.22e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 117.72 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAY-MYPTCSPSRTalatgkqSFRTGVYTvpvlekgndqv 109
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYcQNPVCSPSRC-------SFLTGWYP----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 110 sifsrwtvgeeHImysqpladAGYKSIHlgkwHLVGPYpkkemEASwpLKKKLgqpkpsdfswvpyhKEHckayypegrG 189
Cdd:cd16150 63 -----------HV--------NGHRTLH----HLLRPD-----EPN--LLKTL--------------KDA---------G 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 190 YLKNIGGTyRGDpalevggykskTGGYFAPFSNPFMDQKNPKDkwltdhltteAINFMDEHK-EGPFFINL-----H-YY 262
Cdd:cd16150 90 YHVAWAGK-NDD-----------LPGEFAAEAYCDSDEACVRT----------AIDWLRNRRpDKPFCLYLplifpHpPY 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 263 TV-----------HRPVVARSEELTEKYMNKLGDPKTgQGMEtgkkKLT-------TAQYATMIESLDDNVGRIAEFLDQ 324
Cdd:cd16150 148 GVeepwfsmidreKLPPRRPPGLRAKGKPSMLEGIEK-QGLD----RWSeerwrelRATYLGMVSRLDHQFGRLLEALKE 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 325 KGLRENTLIIFTSDNGQNIGSNLQLRGKKGYIYEAGIRVPAFVNWPGKVDARRTETPVMVTDYFPTFMELAGIDYRGQLD 404
Cdd:cd16150 223 TGLYDDTAVFFFSDHGDYTGDYGLVEKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHF 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 405 GQSFAPLFKGEDK------------------ALQARP----IFWHLASEYRNGTCS----IIRKNDMKLIQFLaTGELEL 458
Cdd:cd16150 303 GRSLLPVLAGETEehrdavfseggrlhgeeqAMEGGHgpydLKWPRLLQQEEPPEHtkavMIRTRRYKYVYRL-YEPDEL 381
|
490 500 510
....*....|....*....|....*....|....
gi 1395161703 459 YDLKKDPKEENNLAlKNPETAQL---LLKELTGW 489
Cdd:cd16150 382 YDLEADPLELHNLI-GDPAYAEIiaeMKQRLLRW 414
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
30-409 |
2.48e-24 |
|
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: 102.45 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 30 KPNIVFILVDDLGHGDVG-FNGST---------YYETPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYT 98
Cdd:cd16153 1 KPNILWIITDDQRVDSLScYNNAHtgksesrlgYVESPNIDALAAEGVLFTNAYCnSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 99 vpvLEKGNDQVSIFSrwtvgeehIMYSQPLADAGYKSIHLGkwhlvgpypkkemeaswplkkklgqpkpsdfswvpyhKE 178
Cdd:cd16153 81 ---FEAAHPALDHGL--------PTFPEVLKKAGYQTASFG-------------------------------------KS 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 179 HCKAYypegRGYLKNIGGTYRGDPALEVGGYKSKtggyfapfsnpfmdqknpkdkwltdhltteainfmdehkeGPFFIN 258
Cdd:cd16153 113 HLEAF----QRYLKNANQSYKSFWGKIAKGADSD----------------------------------------KPFFVR 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 259 LHYYTVHRPVVArSEELTEKYmnklgdpktgqgmetgkkklttaQYATMIESLDDNVGRIAEFLDQKGL---RENTLIIF 335
Cdd:cd16153 149 LSFLQPHTPVLP-PKEFRDRF-----------------------DYYAFCAYGDAQVGRAVEAFKAYSLkqdRDYTIVYV 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 336 TSDNGQNIGSNlQLRGKKGYiYEAGIRVPAFVNWPGKVDA---RRTETPVMVTDYFPTFMELAGID---YRGqLDGQSFA 409
Cdd:cd16153 205 TGDHGWHLGEQ-GILAKFTF-WPQSHRVPLIVVSSDKLKApagKVRHDFVEFVDLAPTLLAAAGVDvdaPDY-LDGRDLF 281
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-425 |
4.12e-16 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 79.17 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYMYPT-CSPSRTALATGKQSFRTGVY-TVPVLEKGNDQ 108
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACmCSPSRSTLYTGLHPQQTGVTdTLGSPMQPLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 109 VSIFsrwTVGeeHIMysqplADAGYKSIHLGKWHLvgpypkkemeaswplkkklgqpkpSDFSWvpyhkehckayypegr 188
Cdd:cd16035 81 PDVP---TLG--HML-----RAAGYYTAYKGKWHL------------------------SGAAG---------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 189 gylkniggtyrgdpalevGGYKsKTGGYfapfsnpfmdqknpkdkwltdhlTTEAINFMDEHKEG-----PF-----FIN 258
Cdd:cd16035 111 ------------------GGYK-RDPGI-----------------------AAQAVEWLRERGAKnadgkPWflvvsLVN 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 259 LHyytvhrPVVARSEELTE-KYMNKLgdpktgqgmetgkkklttaqYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTS 337
Cdd:cd16035 149 PH------DIMFPPDDEERwRRFRNF--------------------YYNLIRDVDRQIGRVLDALDASGLADNTIVVFTS 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 338 DNGQNIGSNlQLRGKKGYIYEAGIRVPAFVNWPG-KVDARRTETPVMVTDYFPTFMELAGID-------YRGqLDGQSFA 409
Cdd:cd16035 203 DHGEMGGAH-GLRGKGFNAYEEALHVPLIISHPDlFGTGQTTDALTSHIDLLPTLLGLAGVDaearateAPP-LPGRDLS 280
|
410
....*....|....*..
gi 1395161703 410 PLFKGED-KALQARPIF 425
Cdd:cd16035 281 PLLTDADaDAVRDGILF 297
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
31-465 |
3.35e-14 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 74.11 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 31 PNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYM-YPTCSPSRTALATGKQSFRTGVYTVpvlEKGNDqv 109
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTnSPICCPSRAAMWSGLFTHLTESWNN---YKGLD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 110 SIFSRWTVG-EEHIMYSQPLADAGYKSIHlgkwHLVgpypKKEMEAswplkkklgqpkpsdfsW---VPYHKEHckayyp 185
Cdd:cd16171 76 PNYPTWMDRlEKHGYHTQKYGKLDYTSGH----HSV----SNRVEA-----------------WtrdVPFLLRQ------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 186 EGRgylkniggtyrgdPALEVGGYKSKtggyfapfsnpfmDQKNPKDKWLTDHLTT----EAINFMDehkegPFFInlhY 261
Cdd:cd16171 125 EGR-------------PTVNLVGDRST-------------VRVMLKDWQNTDKAVHwirkEAPNLTQ-----PFAL---Y 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 262 YTVHRPVVARSEELTEKYmnklgdpktgqgmetGKKKLTTAQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQ 341
Cdd:cd16171 171 LGLNLPHPYPSPSMGENF---------------GSIRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGE 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 342 nigsnLQLRGKKGY---IYEAGIRVPAFVNWPGKVDARRTETPVMVTDYFPTFMELAGIDYRGQLDGQSFAPL----FKG 414
Cdd:cd16171 236 -----LAMEHRQFYkmsMYEGSSHVPLLIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLlsesSIK 310
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1395161703 415 EDKALQARPIfWHLaSEYR----NGTCSIIRKNDMKLIQFlATGEL---ELYDLKKDP 465
Cdd:cd16171 311 ESPSRVPHPD-WVL-SEFHgcnvNASTYMLRTNSWKYIAY-ADGNSvppQLFDLSKDP 365
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
242-395 |
3.79e-12 |
|
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: 65.90 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 242 EAINFMDEHKegPFFINLHYYTVHRPVVARSEELTEkymnklgdpktgqgmetgkkklttaqYATMIESLDDNVGRIAEF 321
Cdd:cd00016 110 KAIDETSKEK--PFVLFLHFDGPDGPGHAYGPNTPE--------------------------YYDAVEEIDERIGKVLDA 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395161703 322 LDQKGLRENTLIIFTSDNGqNIGSNLQLRGKKGYI---YEAGIRVPAFVNWPGKVDARRTETPVMVTDYFPTFMELA 395
Cdd:cd00016 162 LKKAGDADDTVIIVTADHG-GIDKGHGGDPKADGKadkSHTGMRVPFIAYGPGVKKGGVKHELISQYDIAPTLADLL 237
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
218-473 |
2.49e-11 |
|
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: 66.08 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 218 APFSNPFMDQ-----------KNPKDKWLTDHLTT-EAINFMDEHKEG-PFFINLHYYTVHRPVVARSEELTEKYMNKLG 284
Cdd:COG3083 333 AGFNSPLFRQtifsdvslprlHTPGGPAQRDRQITaQWLQWLDQRDSDrPWFSYLFLDAPHAYSFPADYPKPFQPSEDCN 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 285 DPKTGQGMETgkkKLTTAQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQNIGSNLQLR-GKKGYIYEAGIRV 363
Cdd:COG3083 413 YLALDNESDP---TPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQNYwGHNSNFSRYQLQV 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 364 PAFVNWPGKvDARRTETPVMVTDYFPTFM-ELAGI-----DYRgqlDGQSfapLFKGEDKalqaRPifWHLASEYRNgtC 437
Cdd:COG3083 490 PLVIHWPGT-PPQVISKLTSHLDIVPTLMqRLLGVqnpasDYS---QGED---LFDPQRR----RD--WVLAGDYRN--L 554
|
250 260 270
....*....|....*....|....*....|....*...
gi 1395161703 438 SIIRKNDMKLIQflATGELELYDLKKDPKEEN--NLAL 473
Cdd:COG3083 555 AIITPDRITVLD--PSGNYQVYDRDYRPLKDAkpPLGL 590
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
22-400 |
1.61e-10 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 63.52 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 22 AGASTPKVKPNIVFILVDDLGHGDVGFNGSTYYETPHIDQLANDGLVIKNAYmyptcspsrtalATGKQSFR------TG 95
Cdd:COG1368 226 PNPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFY------------SQGGRTSRgefavlTG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 96 VYTVP-----VLEKGNDQVSIFSrwtvgeehimysqPLADAGYKS--IHlgkwhlvgpypkkemeaswplkkklgqpkPS 168
Cdd:COG1368 294 LPPLPggspyKRPGQNNFPSLPS-------------ILKKQGYETsfFH-----------------------------GG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 169 DFSWvpyhkEHCKAYYPeGRGYLKNIGGTYRGDPalEVGGYksktgGYfapfsnpfmdqknpKDKWLTDhlttEAINFMD 248
Cdd:COG1368 332 DGSF-----WNRDSFYK-NLGFDEFYDREDFDDP--FDGGW-----GV--------------SDEDLFD----KALEELE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 249 EHKEgPFFInlHYYTV--HRPVvarseELTEKYMNKLGDPKTGQGmetgkKKLTTAQYAtmieslDDNVGRIAEFLDQKG 326
Cdd:COG1368 381 KLKK-PFFA--FLITLsnHGPY-----TLPEEDKKIPDYGKTTLN-----NYLNAVRYA------DQALGEFIEKLKKSG 441
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395161703 327 LRENTLIIFTSD-NGQNIGSNLQLRGKKGYiyeagiRVPAFVNWPGKVDARRTETPVMVTDYFPTFMELAGIDYR 400
Cdd:COG1368 442 WYDNTIFVIYGDhGPRSPGKTDYENPLERY------RVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYP 510
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
224-396 |
5.33e-10 |
|
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: 60.39 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 224 FMDQKNPKDKW-LTDH-LTTEAINFMDEHKEGPFFInlHYYTV--HRPvvarseeltekYmnKLGDPKTGQGMETGKKKL 299
Cdd:cd16015 125 FPDDEKETNGWgVSDEsLFDQALEELEELKKKPFFI--FLVTMsnHGP-----------Y--DLPEEKKDEPLKVEEDKT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 300 TTAQYATMIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQNIGSNLQLRGKKGYIYEagiRVPAFVNWPGKVDARRTE 379
Cdd:cd16015 190 ELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY---RTPLLIYSPGLKKPKKID 266
|
170
....*....|....*..
gi 1395161703 380 TPVMVTDYFPTFMELAG 396
Cdd:cd16015 267 RVGSQIDIAPTLLDLLG 283
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
7-342 |
7.56e-10 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 60.53 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 7 MATGLAFaVLTGGTYAGASTPKVKPNIVFILVDDLGHGDVgfngsTYYETPHIDQLANDGLVIKNAY-MYPTCS-PSRTA 84
Cdd:COG1524 1 MKRGLSL-LLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTsVFPSTTaPAHTT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 85 LATGKQSFRTGVYtvpvlekGNDqvsIFSRWTVGEehimysqpladagyksIHLGKWHLVGPYPKKEMEAswplkkklgq 164
Cdd:COG1524 75 LLTGLYPGEHGIV-------GNG---WYDPELGRV----------------VNSLSWVEDGFGSNSLLPV---------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 165 pkPSDFSWVPYHKEHCKAYYPEGRgylkNIGGTYRGDPALEVGGYKSKTGGYFApfsnpfmdqknpkDKWLTDHLTtEAI 244
Cdd:COG1524 119 --PTIFERARAAGLTTAAVFWPSF----EGSGLIDAARPYPYDGRKPLLGNPAA-------------DRWIAAAAL-ELL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 245 nfmdeHKEGPFFINLHY----YTVHRpvvarseeltekymnklgdpktgQGMETgkkklttAQYATMIESLDDNVGRIAE 320
Cdd:COG1524 179 -----REGRPDLLLVYLpdldYAGHR-----------------------YGPDS-------PEYRAALREVDAALGRLLD 223
|
330 340
....*....|....*....|..
gi 1395161703 321 FLDQKGLRENTLIIFTSDNGQN 342
Cdd:COG1524 224 ALKARGLYEGTLVIVTADHGMV 245
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
405-491 |
1.37e-06 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 46.86 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 405 GQSFAPLFKGEDKALQARPIFWHLaSEYRNGTCSI----IRKNDMKLIQFLATG-ELELYDLKKDPKEENNLaLKNPETA 479
Cdd:pfam16347 7 GKSFLPLLKGKKPKNWRDALYYHY-YEYPAEHAVKrhygVRTERYKLIHFYNDIdEWELYDLQKDPKEMNNV-YGDPEYA 84
|
90
....*....|....*
gi 1395161703 480 QL---LLKELTGWRK 491
Cdd:pfam16347 85 EVqaeLKEELEELRK 99
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
242-398 |
1.47e-05 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 46.85 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 242 EAINFMDEHKegpfFINLHYYTVHRPVVARSEELTEKYMnklgdPKTGQGMETGKKKLTTAQYATMIESLDDNVGRIAEF 321
Cdd:cd16017 135 EALADSSKKK----LIVLHLMGSHGPYYDRYPEEFAKFT-----PDCDNELQSCSKEELINAYDNSILYTDYVLSQIIER 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 322 LDQKGlrENTLIIFTSDNGQNIGSNLQLRGKKGYIYEAGIRVPAFV--------NWPGKVDARRTETPVMVTDYFPTFME 393
Cdd:cd16017 206 LKKKD--KDAALIYFSDHGESLGENGLYLHGAPYAPKEQYHVPFIIwssdsykqRYPVERLRANKDRPFSHDNLFHTLLG 283
|
....*
gi 1395161703 394 LAGID 398
Cdd:cd16017 284 LLGIK 288
|
|
| DUF4994 |
pfam16385 |
Domain of unknown function; This family around 100 residues locates in the C-terminal of some ... |
404-477 |
1.05e-04 |
|
Domain of unknown function; This family around 100 residues locates in the C-terminal of some uncharacterized proteins in various Bacteroides and Prevotella species. The function of this family remains unknown.
Pssm-ID: 406720 [Multi-domain] Cd Length: 98 Bit Score: 41.12 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 404 DGQSFAPLFKGEDKalQARPifwHLASEYRNGTCSIiRKNDMKLI---------QF--LATG---ELELYDLKKDPKEEN 469
Cdd:pfam16385 8 DSQNYLPALLGKDK--KGRP---YVIEQALNGTLSV-RTGDWKYIepsdgpayiKWtkIETGnspEPQLYDLKADPGEQE 81
|
....*...
gi 1395161703 470 NLALKNPE 477
Cdd:pfam16385 82 NVAKKHPE 89
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
307-396 |
2.01e-03 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 39.88 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395161703 307 MIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQ-NIGSNlqlrgkkGYIYE-AGIRVPaFVNWPGKVDARRTETPVMV 384
Cdd:cd16018 184 ALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMtDVGTH-------GYDNElPDMRAI-FIARGPAFKKGKKLGPFRN 255
|
90
....*....|..
gi 1395161703 385 TDYFPTFMELAG 396
Cdd:cd16018 256 VDIYPLMCNLLG 267
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
307-341 |
5.99e-03 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 38.94 E-value: 5.99e-03
10 20 30
....*....|....*....|....*....|....*
gi 1395161703 307 MIESLDDNVGRIAEFLDQKGLRENTLIIFTSDNGQ 341
Cdd:pfam01663 190 ALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGM 224
|
|
| |
