|
Name |
Accession |
Description |
Interval |
E-value |
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
14-466 |
0e+00 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 550.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIRGNDEApergrvw 93
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 94 dflaaerdstlEGQRGLPSGTKTFVSILKEGGYRTGIVGKWGLGAPGTESLPLNHGFDFFYGYNCQRQAHTYFPLHLYRN 173
Cdd:cd16145 74 -----------GGQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHPTKQGFDYFYGYLDQVHAHNYYPEYLWRN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 174 EQREYLANdTVIPHTKLDPGADPLslssydkliSHVYSPDKIQEEALRFMEENKKQPFFLYYATPLPHVPIQAPQRLIDH 253
Cdd:cd16145 143 GEKVPLPN-NVIPPLDEGNNAGGG---------GGTYSHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDDGPYK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 254 YVRKFGDESPYLGQADyfparyPHAGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFNGG--VDSPWFRSG 331
Cdd:cd16145 213 YKPKDPGIYAYLPWPQ------PEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSEGGseHDPDFFDSN 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 332 GPFRSeygwGKCFLREGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNPATETDGISFYPTLMESGDQMKH 411
Cdd:cd16145 287 GPLRG----YKRSLYEGGIRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTLLGKPQQQQH 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1650049783 412 SYLYWEFMDIEGQQAVRMGKWKGLRNGLKRGnmKIELYDLETDSCEQRDVAPKHP 466
Cdd:cd16145 363 DYLYWEFYEGGGAQAVRMGGWKAVRHGKKDG--PFELYDLSTDPGETNNLAAQHP 415
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
13-486 |
4.64e-132 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 388.08 E-value: 4.64e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIRGNDEapergrv 92
Cdd:COG3119 23 RPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGE------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 wdflaaerdstlEGQRGLPSGTKTFVSILKEGGYRTGIVGKWglgapgteslplnhgfdffygyncqrqahtyfplhlyr 172
Cdd:COG3119 96 ------------GYNGGLPPDEPTLAELLKEAGYRTALFGKW-------------------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 173 neqreylandtviphtkldpgadplslssydklisHVYSPDKIQEEALRFMEEN--KKQPFFLYYATPLPHVPIQAPQRL 250
Cdd:COG3119 126 -----------------------------------HLYLTDLLTDKAIDFLERQadKDKPFFLYLAFNAPHAPYQAPEEY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 251 IDHYVRKFGDESPYLGQADYFPARYPH--AGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFNggvdSPWF 328
Cdd:COG3119 171 LDKYDGKDIPLPPNLAPRDLTEEELRRarAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLG----EHGL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 329 RsggpfrseygWGKCFLREGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNPATETDGISFYPTLmESGDQ 408
Cdd:COG3119 247 R----------GGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLL-TGEKA 315
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1650049783 409 MKHSYLYWEFMDIEGQQAVRMGKWKGLRNGLKRGnmKIELYDLETDSCEQRDVAPKHPEIVKKIGEIMKKEH-TVPVYP 486
Cdd:COG3119 316 EWRDYLYWEYPRGGGNRAIRTGRWKLIRYYDDDG--PWELYDLKNDPGETNNLAADYPEVVAELRALLEAWLkELGDPP 392
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
14-479 |
8.31e-121 |
|
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: 360.32 E-value: 8.31e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIrGNDEAPERGRVW 93
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGI-TDVIPGRRGPPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 94 DFLAAERDSTlegqRGLPSGTKTFVSILKEGGYRTGIVGKWGLGAPGtESLPLNHGFDFFYGYNCQRQAHTYFPLhlyrn 173
Cdd:cd16144 80 NTKLIPPPST----TRLPLEEVTIAEALKDAGYATAHFGKWHLGGEG-GYGPEDQGFDVNIGGTGNGGPPSYYFP----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 174 eqreylanDTVIPHTKLDPGADPlslssydklishvYSPDKIQEEALRFMEENKKQPFFLYYATPLPHVPIQAPQRLIDH 253
Cdd:cd16144 150 --------PGKPNPDLEDGPEGE-------------YLTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELIEK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 254 YVRKfgdespylgqADYFPARYPHAGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFNGGVDspwFRSGGP 333
Cdd:cd16144 209 YEKK----------KKGLRKGQKNPVYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGP---PTSNAP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 334 FRSeygwGKCFLREGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNPATE--TDGISFYPTLMESGDQMKH 411
Cdd:cd16144 276 LRG----GKGSLYEGGIRVPLIVRWPGVIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPqhLDGVSLVPLLKGGEADLPR 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1650049783 412 SYLYWEF--MDIEGQQ---AVRMGKWKGLRNgLKRGnmKIELYDLETDSCEQRDVAPKHPEIVKKigeiMKKE 479
Cdd:cd16144 352 RALFWHFphYHGQGGRpasAIRKGDWKLIEF-YEDG--RVELYNLKNDIGETNNLAAEMPEKAAE----LKKK 417
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
13-462 |
4.15e-108 |
|
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: 327.21 E-value: 4.15e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIRGNDEAPergrv 92
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 wdflaaerdstlEGQRGLPSGTKTFVSILKEGGYRTGIVGKWGLGAPGtESLPLNHGFDFFYG--YNcqrqaHTYFPLHL 170
Cdd:cd16026 76 ------------GSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQP-EFLPTRHGFDEYFGipYS-----NDMWPFPL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 171 YRNE----QREYLANDTVIphtkldpgADPLSLSSYDKLishvyspdkIQEEALRFMEENKKQPFFLYYATPLPHVPIQA 246
Cdd:cd16026 138 YRNDppgpLPPLMENEEVI--------EQPADQSSLTQR---------YTDEAVDFIERNKDQPFFLYLAHTMPHVPLFA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 247 PQRlidhyvrkfgdespylgqadyFPARYPHAGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFNGGVDSp 326
Cdd:cd16026 201 SEK---------------------FKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHG- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 327 wfRSGGPFRSEYG--WgkcflrEGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNPATE--TDGISFYPTL 402
Cdd:cd16026 259 --GSAGPLRGGKGttW------EGGVRVPFIAWWPGVIPAGTVSDELASTMDLLPTLAALAGAPLPEDrvIDGKDISPLL 330
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1650049783 403 MESGDQMKHSYLYweFMDIEGQQAVRMGKWK----------GLRNGLKRGNMK-IELYDLETDSCEQRDVA 462
Cdd:cd16026 331 LGGSKSPPHPFFY--YYDGGDLQAVRSGRWKlhlpttyrtgTDPGGLDPTKLEpPLLYDLEEDPGETYNVA 399
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
14-480 |
1.16e-103 |
|
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: 316.03 E-value: 1.16e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTgSPVSAAARCVLLTGKHsghcgirgndeaPERGRVW 93
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHV-SPVCAPTRAALLTGRY------------PFRTGVW 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 94 DflaaerdsTLEGQRGLPSGTKTFVSILKEGGYRTGIVGKWGLGAPgTESLPLNHGFDFFYGYNCQRQAHTYFPLHlyrN 173
Cdd:cd16146 68 H--------TILGRERMRLDETTLAEVFKDAGYRTGIFGKWHLGDN-YPYRPQDRGFDEVLGHGGGGIGQYPDYWG---N 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 174 EQRE--YLANDTVIPHTKldpgadplslssydklishvYSPDKIQEEALRFMEENKKQPFFLYYATPLPHVPIQAPQRLI 251
Cdd:cd16146 136 DYFDdtYYHNGKFVKTEG--------------------YCTDVFFDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 252 DHYvRKFGDESpylgqadyfparyPHAGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPtfNGGVDSPWFrsg 331
Cdd:cd16146 196 DPY-KDMGLDD-------------KLAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGP--AGGVPKRFN--- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 332 GPFRseyGWgKCFLREGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNPATET--DGISFYPTLMESGDQM 409
Cdd:cd16146 257 AGMR---GK-KGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIklDGRSLLPLLKGESDPW 332
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1650049783 410 KHSYLYWEFMDIEGQQ------AVRMGKWKGLRNGLKrgnmKIELYDLETDSCEQRDVAPKHPEIVKKigeiMKKEH 480
Cdd:cd16146 333 PERTLFTHSGRWPPPPkkkrnaAVRTGRWRLVSPKGF----QPELYDIENDPGEENDVADEHPEVVKR----LKAAY 401
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
13-461 |
9.66e-88 |
|
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: 274.71 E-value: 9.66e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLGCFGQRrIETPHIDRLAAEGMVFSNYYTgSPVSAAARCVLLTGKHSGHCGIRGNDEApergrv 92
Cdd:cd16025 2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNFHT-TALCSPTRAALLTGRNHHQVGMGTMAEL------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 wdflaaerDSTLEGQRG-LPSGTKTFVSILKEGGYRTGIVGKWGLGAPgteslplnhgfDFfygyncqrqahtyfplhly 171
Cdd:cd16025 74 --------ATGKPGYEGyLPDSAATIAEVLKDAGYHTYMSGKWHLGPD-----------DY------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 172 rneqreylandtviphtkldpgadplslssydklishvYSPDKIQEEALRFMEENKK--QPFFLYYATPLPHVPIQAPQR 249
Cdd:cd16025 116 --------------------------------------YSTDDLTDKAIEYIDEQKApdKPFFLYLAFGAPHAPLQAPKE 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 250 LIDHYVRKFGD------ESPY-----LG--QADYFPARYPH--------------------AGYAAMVTYIDEKVGEIVD 296
Cdd:cd16025 158 WIDKYKGKYDAgwdalrEERLerqkeLGliPADTKLTPRPPgvpawdslspeekklearrmEVYAAMVEHMDQQIGRLID 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 297 FLKKKGLYENTVIIISSDNGPTfnggVDSPWFR-SGGPFRseygWGKCFLREGGIRVPLIVTWKGHIRA-GAHTTLPCTS 374
Cdd:cd16025 238 YLKELGELDNTLIIFLSDNGAS----AEPGWANaSNTPFR----LYKQASHEGGIRTPLIVSWPKGIKAkGGIRHQFAHV 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 375 YDFYSTICELAGVN-PATET-------DGISFYPTLMESGDQMKHSYLYWEFMdieGQQAVRMGKWKGLRNGLKRGN-MK 445
Cdd:cd16025 310 IDIAPTILELAGVEyPKTVNgvpqlplDGVSLLPTLDGAAAPSRRRTQYFELF---GNRAIRKGGWKAVALHPPPGWgDQ 386
|
490
....*....|....*.
gi 1650049783 446 IELYDLETDSCEQRDV 461
Cdd:cd16025 387 WELYDLAKDPSETHDL 402
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
14-462 |
2.17e-87 |
|
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: 273.69 E-value: 2.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFG-QRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHsghcgirgndeaPERGRV 92
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRY------------PWRSRL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 WDFLAAERDSTLegqrgLPSGTKTFVSILKEGGYRTGIVGKWGLG----APGTESL-----------------PLNHGFD 151
Cdd:cd16143 69 KGGVLGGFSPPL-----IEPDRVTLAKMLKQAGYRTAMVGKWHLGldwkKKDGKKAatgtgkdvdyskpikggPLDHGFD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 152 FFYGyncqrqahtyfplhlyrneqreylandtvIPHTKLDPgadplslssydklishvyspdKIQEEALRFMEENKK--Q 229
Cdd:cd16143 144 YYFG-----------------------------IPASEVLP---------------------TLTDKAVEFIDQHAKkdK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 230 PFFLYYATPLPHVPIQAPQRlidhyvrkfgdespYLGQADyfparyphAG-YAAMVTYIDEKVGEIVDFLKKKGLYENTV 308
Cdd:cd16143 174 PFFLYFALPAPHTPIVPSPE--------------FQGKSG--------AGpYGDFVYELDWVVGRILDALKELGLAENTL 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 309 IIISSDNGPTFNGGVDSPW---FRSGGPFRSeygwGKCFLREGGIRVPLIVTWKGHIRAGAHT-TLPCTSyDFYSTICEL 384
Cdd:cd16143 232 VIFTSDNGPSPYADYKELEkfgHDPSGPLRG----MKADIYEGGHRVPFIVRWPGKIPAGSVSdQLVSLT-DLFATLAAI 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 385 AGVN-PATET-DGISFYPTLMESGDQMKHSYLYWEfmDIEGQQAVRMGKWK-----------GLRNGLKRGNMKIELYDL 451
Cdd:cd16143 307 VGQKlPDNAAeDSFSFLPALLGPKKQEVRESLVHH--SGNGSFAIRKGDWKlidgtgsggfsYPRGKEKLGLPPGQLYNL 384
|
490
....*....|.
gi 1650049783 452 ETDSCEQRDVA 462
Cdd:cd16143 385 STDPGESNNLY 395
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
14-479 |
2.22e-79 |
|
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: 252.04 E-value: 2.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYgDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIRGNdeapeRGRVW 93
Cdd:cd16027 1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGL-----RSRGF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 94 DflaaerdstlegqrgLPSGTKTFVSILKEGGYRTGIVGKWGLGAPgteslplnHGFDFFYGYNCQRQAHtyfplhlyrn 173
Cdd:cd16027 75 P---------------LPDGVKTLPELLREAGYYTGLIGKTHYNPD--------AVFPFDDEMRGPDDGG---------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 174 eqreylandtviphtkldpgadplslssydklishvYSPDKIQEEALRFMEENKK-QPFFLYYATPLPHVPiqapqrlid 252
Cdd:cd16027 122 ------------------------------------RNAWDYASNAADFLNRAKKgQPFFLWFGFHDPHRP--------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 253 hYVRKFGDESPYLGQADYFPARYP--------HAGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFnggvd 324
Cdd:cd16027 157 -YPPGDGEEPGYDPEKVKVPPYLPdtpevredLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPF----- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 325 spwfrsggPFrseygwGKCFLREGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNPATETDGISFYPTLmE 404
Cdd:cd16027 231 --------PR------AKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLL-K 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 405 SGDQMKHSYLYWE--FMDI--EGQQAVRMGKWKGLRNGlkrgnMKIELYDLETDSCEQRDVA--PKHPEIVKKigeiMKK 478
Cdd:cd16027 296 GEKDPGRDYVFAErdRHDEtyDPIRSVRTGRYKYIRNY-----MPEELYDLKNDPDELNNLAddPEYAEVLEE----LRA 366
|
.
gi 1650049783 479 E 479
Cdd:cd16027 367 A 367
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
14-397 |
3.30e-79 |
|
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: 246.96 E-value: 3.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIRGNdeapergrvw 93
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 94 dflaaerdstLEGQRGLPSGTKTFVSILKEGGYRTGIVGKWglgapgteslplnHgfdffygyncqrqahtyfplhlyrn 173
Cdd:cd16022 71 ----------VGNGGGLPPDEPTLAELLKEAGYRTALIGKW-------------H------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 174 eqreylandtviphtkldpgadplslssydklishvyspdkiqEEALRFMEENKK-QPFFLYYATPLPHvpiqapqrlid 252
Cdd:cd16022 103 -------------------------------------------DEAIDFIERRDKdKPFFLYVSFNAPH----------- 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 253 hyvrkfgdeSPYlgqadyfparyphaGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFNggvdspwfrsgg 332
Cdd:cd16022 129 ---------PPF--------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLG------------ 173
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1650049783 333 pfrsEYG--WGKCFLREGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNPATETDGIS 397
Cdd:cd16022 174 ----DHGlrGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
14-462 |
5.39e-79 |
|
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: 251.70 E-value: 5.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTgSPVSAAARCVLLTGKHSGHCGIRGNDEAPERGRvw 93
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYV-QPICTPSRAALMTGRYPIHTGMQHGVILAGEPY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 94 dflaaerdstlegqrGLPSGTKTFVSILKEGGYRTGIVGKWGLGAPGTESLPLNHGFDFFYGY---------NCQRQAHT 164
Cdd:cd16029 78 ---------------GLPLNETLLPQYLKELGYATHLVGKWHLGFYTWEYTPTNRGFDSFYGYyggaedyytHTSGGAND 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 165 YFPLHLYRNEQREYLANDTviphtkldpgadplslssydklishvYSPDKIQEEALRFMEE-NKKQPFFLYYATPLPHVP 243
Cdd:cd16029 143 YGNDDLRDNEEPAWDYNGT--------------------------YSTDLFTDRAVDIIENhDPSKPLFLYLAFQAVHAP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 244 IQAPQRLIDHYVRKFGDESPYlgqadyfparyPHAGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNG-PTFNGG 322
Cdd:cd16029 197 LQVPPEYADPYEDKFAHIKDE-----------DRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGgPTGGGD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 323 VDSPWfrsggPFRSeygwGKCFLREGGIRV------PLIVTWKGHIRAG-AHTTlpctsyDFYSTICELAGVNPATET-- 393
Cdd:cd16029 266 GGSNY-----PLRG----GKNTLWEGGVRVpafvwsPLLPPKRGTVSDGlMHVT------DWLPTLLSLAGGDPDDLPpl 330
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1650049783 394 DGISFYPTLMESGD----QMKHSYLYWEFMDIEGqqAVRMGKWKglrngLKRGNMkieLYDLETDSCEQRDVA 462
Cdd:cd16029 331 DGVDQWDALSGGAPsprtEILLNIDDITRTTGGA--AIRVGDWK-----LIVGKP---LFNIENDPCERNDLA 393
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
13-479 |
4.97e-78 |
|
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: 250.52 E-value: 4.97e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIRGNDEapergrv 92
Cdd:cd16031 2 RPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 wdflaaerdstlegqRGLPSGTKTFVSILKEGGYRTGIVGKWGLGapgTESLPLNHGFDFFYGYNCQrqaHTYFPLHLYR 172
Cdd:cd16031 75 ---------------PLFDASQPTYPKLLRKAGYQTAFIGKWHLG---SGGDLPPPGFDYWVSFPGQ---GSYYDPEFIE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 173 NEQREYlandtviphtkldpgadplslssydkliSHVYSPDKIQEEALRFMEENKK-QPFFLYYATPLPHVPIQAPQRLI 251
Cdd:cd16031 134 NGKRVG----------------------------QKGYVTDIITDKALDFLKERDKdKPFCLSLSFKAPHRPFTPAPRHR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 252 DHY------VRKFGDESPYLGQADYF-----------------PARYPHA--GYAAMVTYIDEKVGEIVDFLKKKGLYEN 306
Cdd:cd16031 186 GLYedvtipEPETFDDDDYAGRPEWAreqrnrirgvldgrfdtPEKYQRYmkDYLRTVTGVDDNVGRILDYLEEQGLADN 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 307 TVIIISSDNGpTFNGgvdspwfrsggpfrsEYGW-GKCFLREGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELA 385
Cdd:cd16031 266 TIIIYTSDNG-FFLG---------------EHGLfDKRLMYEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 386 GVNPATETDGISFYPtLMESGDQMKHS----YLYWEFMD---IEGQQAVRMGKWKglrngLKR--GNMKI-ELYDLETDS 455
Cdd:cd16031 330 GVPIPEDMQGRSLLP-LLEGEKPVDWRkefyYEYYEEPNfhnVPTHEGVRTERYK-----YIYyyGVWDEeELYDLKKDP 403
|
490 500
....*....|....*....|....*.
gi 1650049783 456 CEQRDVA--PKHPEIVKKigeiMKKE 479
Cdd:cd16031 404 LELNNLAndPEYAEVLKE----LRKR 425
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
14-460 |
6.06e-78 |
|
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: 248.67 E-value: 6.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTgSPVSAAARCVLLTGKHSGHCGIR-GNDEAPErgrv 92
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRNYVVfGYLDPKQ---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 wdflaaerdstlegqrglpsgtKTFVSILKEGGYRTGIVGKWGLGA-PGTESLPLNHGFDFFYGYNCQRQAHTYFPlhly 171
Cdd:cd16151 76 ----------------------KTFGHLLKDAGYATAIAGKWQLGGgRGDGDYPHEFGFDEYCLWQLTETGEKYSR---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 172 RNEQREYLANDTVIPHTKLDpgadplslssydklishvYSPDKIQEEALRFMEENKKQPFFLYYATPLPHVPIQA-Pqrl 250
Cdd:cd16151 130 PATPTFNIRNGKLLETTEGD------------------YGPDLFADFLIDFIERNKDQPFFAYYPMVLVHDPFVPtP--- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 251 idhyvrkfgDESPYLGQADYFPARYPHagYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGptfNGGVDSpwFRS 330
Cdd:cd16151 189 ---------DSPDWDPDDKRKKDDPEY--FPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNG---THRPIT--SRT 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 331 GGpfrSEYGWGKCFLREGGIRVPLIVTWKGHIRAG------AHTTlpctsyDFYSTICELAGVNPATE--TDGISFYPTL 402
Cdd:cd16151 253 NG---REVRGGKGKTTDAGTHVPLIVNWPGLIPAGgvsddlVDFS------DFLPTLAELAGAPLPEDypLDGRSFAPQL 323
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1650049783 403 MESGDQMKHSYLYW---EFMDIEGQQAVRMGKWKGLRNGlkrgnmkiELYDLETDSCEQRD 460
Cdd:cd16151 324 LGKTGSPRREWIYWyyrNPHKKFGSRFVRTKRYKLYADG--------RFFDLREDPLEKNP 376
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
13-454 |
3.74e-71 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 231.69 E-value: 3.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIRGNDeapergrv 92
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGND-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 wdflaaerdstlegqRGLPSGTKTFVSILKEGGYRTGIVGKWGLGAPGTESLPLN---------HGFDFFYGYNCQrqaH 163
Cdd:cd16034 73 ---------------VPLPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRADdytppperrHGFDYWKGYECN---H 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 164 TYFPLHLYRNEQREYLANDtviphtkldpgadplslssydklishvYSPDKIQEEALRFMEENKK--QPFFLYYATPLPH 241
Cdd:cd16034 135 DHNNPHYYDDDGKRIYIKG---------------------------YSPDAETDLAIEYLENQADkdKPFALVLSWNPPH 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 242 VP-IQAPQRLIDHY---VRKFGDESPYLGQADYFPARYpHAGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGP 317
Cdd:cd16034 188 DPyTTAPEEYLDMYdpkKLLLRPNVPEDKKEEAGLRED-LRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 318 TFnggvdspwfrsggpfrSEYG-WGKCFLREGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNPATETDGI 396
Cdd:cd16034 267 ML----------------GSHGlMNKQVPYEESIRVPFIIRYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGR 330
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1650049783 397 SFYPTLMESGDQMKHSYLYWEFMDIEGQQAVRMGKWKGLRNG----LKRGNMKIELYDLETD 454
Cdd:cd16034 331 DLSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVRTDrytyVRDKNGPWLLFDNEKD 392
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
14-433 |
1.73e-65 |
|
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: 215.86 E-value: 1.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFG---QRRIETPHIDRLAAEGMVFSNYYtGSPVSAAARCVLLTGKHSghcgIR-GNDEAPER 89
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFY-VEPSCTPGRAAFITGRHP----IRtGLTTVGLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 90 GrvwdflaaerdstleGQRGLPSGTKTFVSILKEGGYRTGIVGKWGLGAPgTESLPLNHGFDFFYGYncqrqahtyfplh 169
Cdd:cd16142 76 G---------------SPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDE-DGRLPTDHGFDEFYGN------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 170 lyrneqreylandtvIPHTkLDpgadplslssydklishvyspDKIQEEALRFMEENKK--QPFFLYYATPLPHVP-IQA 246
Cdd:cd16142 127 ---------------LYHT-ID---------------------EEIVDKAIDFIKRNAKadKPFFLYVNFTKMHFPtLPS 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 247 PQrlidhyvrkfgdespylgqadyFPARYPHAG-YAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFNGGVDS 325
Cdd:cd16142 170 PE----------------------FEGKSSGKGkYADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGPEQDVWPDG 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 326 pwfrSGGPFRSEYG--WgkcflrEGGIRVPLIVTWKGHIRAG-------AHTtlpctsyDFYSTICELAGVNPATET--- 393
Cdd:cd16142 228 ----GYTPFRGEKGttW------EGGVRVPAIVRWPGKIKPGrvsneivSHL-------DWFPTLAALAGAPDPKDKllg 290
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1650049783 394 -----DGISFYPTLMESGDQMKHSYLYWefmDIEGQQ-AVRMGKWK 433
Cdd:cd16142 291 kdrhiDGVDQSPFLLGKSEKSRRSEFFY---FGEGELgAVRWKNWK 333
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
13-477 |
1.73e-61 |
|
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: 205.49 E-value: 1.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYT-GS---PVSAAARCVLLTGKHsghcgirgndeape 88
Cdd:cd16155 2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNmGGwsgAVCVPSRAMLMTGRT-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 89 rgrVWdflaaerDSTLEGQRGLPSGTKTFVSILKEGGYRTGIVGKWGLGapgteslplnhgfdffygyncqrqahtyfpl 168
Cdd:cd16155 68 ---LF-------HAPEGGKAAIPSDDKTWPETFKKAGYRTFATGKWHNG------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 169 hlyrneqreyLANDtviphtkldpgadplslssydklishvyspdkiqeeALRFMEENK--KQPFFLYYATPLPHVPIQA 246
Cdd:cd16155 107 ----------FADA------------------------------------AIEFLEEYKdgDKPFFMYVAFTAPHDPRQA 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 247 PQRLIDHYVRK-------FGDESPY----LGQADYFPARYP--------H-AGYAAMVTYIDEKVGEIVDFLKKKGLYEN 306
Cdd:cd16155 141 PPEYLDMYPPEtiplpenFLPQHPFdngeGTVRDEQLAPFPrtpeavrqHlAEYYAMITHLDAQIGRILDALEASGELDN 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 307 TVIIISSDNGPTF--NGGVdspwfrsggpfrseygwGKCFLREGGIRVPLIVTWKGhIRAGAHTTLPCTSYDFYSTICEL 384
Cdd:cd16155 221 TIIVFTSDHGLAVgsHGLM-----------------GKQNLYEHSMRVPLIISGPG-IPKGKRRDALVYLQDVFPTLCEL 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 385 AGVNPATETDGISFYPTLMESGDQMkHSYLYWEFMDieGQQAVRMGKWKGLR--NGLKRgnmkIELYDLETDSCEQRDVA 462
Cdd:cd16155 283 AGIEIPESVEGKSLLPVIRGEKKAV-RDTLYGAYRD--GQRAIRDDRWKLIIyvPGVKR----TQLFDLKKDPDELNNLA 355
|
490
....*....|....*..
gi 1650049783 463 --PKHPEIVKKIGEIMK 477
Cdd:cd16155 356 dePEYQERLKKLLAELK 372
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
14-478 |
2.87e-61 |
|
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: 205.92 E-value: 2.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKhsghcgirgndeAPERGRVW 93
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGL------------YPHEHGVL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 94 dflaAERDSTLEGQRGLPSGTKTFVSILKEGGYRTGIVGKWGLGapgTESLPLNHGFDffyGYNCQRQAHTYFplhlyrn 173
Cdd:cd16033 69 ----NNVENAGAYSRGLPPGVETFSEDLREAGYRNGYVGKWHVG---PEETPLDYGFD---EYLPVETTIEYF------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 174 eqreylandtviphtkldpgadplslssydklishvyspdkIQEEALRFMEENKK--QPFFLYYATPLPHVPIQAPQRLI 251
Cdd:cd16033 132 -----------------------------------------LADRAIEMLEELAAddKPFFLRVNFWGPHDPYIPPEPYL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 252 DHY----------VRKFGDESPYL--------GQADYFPARYPH--AGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIII 311
Cdd:cd16033 171 DMYdpediplpesFADDFEDKPYIyrrerkrwGVDTEDEEDWKEiiAHYWGYITLIDDAIGRILDALEELGLADDTLVIF 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 312 SSDNGPTF--NGGVDSPWFrsggPFRSEYgwgkcflreggiRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNP 389
Cdd:cd16033 251 TSDHGDALgaHRLWDKGPF----MYEETY------------RIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 390 ATETDGISFYPtLMESGDQMKH-SYLYWEFMDIE---GQQAVRMGKWKGLRNGLKRGnmkiELYDLETDSCEQRDVApKH 465
Cdd:cd16033 315 PPKVDGRSLLP-LLRGEQPEDWrDEVVTEYNGHEfylPQRMVRTDRYKYVFNGFDID----ELYDLESDPYELNNLI-DD 388
|
490
....*....|...
gi 1650049783 466 PEIVKKIGEIMKK 478
Cdd:cd16033 389 PEYEEILREMRTR 401
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
13-433 |
6.53e-60 |
|
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: 203.43 E-value: 6.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIRGndeaPERGrv 92
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG----GTRV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 wdFLAAERDstlegqrGLPSGTKTFVSILKEGGYRTGIVGKWGLGAPGTES-----LPLNHGFDFF-----YGYNCQRQA 162
Cdd:cd16160 75 --FLPWDIG-------GLPKTEVTMAEALKEAGYTTGMVGKWHLGINENNHsdgahLPSHHGFDFVgtnlpFTNSWACDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 163 HTYFPLHLYRNEQREYlANDTVIphtkldpgADPlslssydklISHVYSPDKIQEEALRFMEENKKQPFFLYYATPLPHV 242
Cdd:cd16160 146 TGRHVDFPDRSACFLY-YNDTIV--------EQP---------IQHEHLTETLVGDAKSFIEDNQENPFFLYFSFPQTHT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 243 PIQAPQRLIDHYVR-KFGDESPYLGQAdyfparyphagyaamvtyidekVGEIVDFLKKKGLYENTVIIISSDNGP---- 317
Cdd:cd16160 208 PLFASKRFKGKSKRgRYGDNINEMSWA----------------------VGEVLDTLVDTGLDQNTLVFFLSDHGPhvey 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 318 TFNGGvdspwfrSGGPFRSeygwGKCFLREGGIRVPLIVTWKGHIRAGAHTTLpCTSYDFYSTICELAG--VNPATETDG 395
Cdd:cd16160 266 CLEGG-------STGGLKG----GKGNSWEGGIRVPFIAYWPGTIKPRVSHEV-VSTMDIFPTFVDLAGgtLPTDRIYDG 333
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1650049783 396 ISFYPTLMESGDQMKHSYLYW---EFMdiegqqAVRMGKWK 433
Cdd:cd16160 334 LSITDLLLGEADSPHDDILYYccsRLM------AVRYGSYK 368
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
14-454 |
1.40e-57 |
|
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: 193.53 E-value: 1.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHsghcgirgndeaPERGRVW 93
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRY------------VHETGVW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 94 DFLAAerdstlegqrgLPSGTKTFVSILKEGGYRTGIVGKwglgapgteslplnhgfdffygyncqrqahtyfpLHLYRN 173
Cdd:cd16037 69 DNADP-----------YDGDVPSWGHALRAAGYETVLIGK----------------------------------LHFRGE 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 174 EQREylandtviphtkldpGADplslssYDKLIShvyspdkiqEEALRFMEEN--KKQPFFLYYATPLPHVPIQAPQRLI 251
Cdd:cd16037 104 DQRH---------------GFR------YDRDVT---------EAAVDWLREEaaDDKPWFLFVGFVAPHFPLIAPQEFY 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 252 DHYVRKfgdespylgqadyfpARyphAGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPtfNGGvdspwfrsg 331
Cdd:cd16037 154 DLYVRR---------------AR---AAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGD--MLG--------- 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 332 gpfrsEYG-WGKCFLREGGIRVPLIVTWKGhIRAGAHTTLPCTSYDFYSTICELAGVNPATETDGISFYPtLMESGDQMK 410
Cdd:cd16037 205 -----ERGlWGKSTMYEESVRVPMIISGPG-IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLP-LAEGPDDPD 277
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1650049783 411 HSYL--YWEFMDIEGQQAVRMGKWKGLRNglkrGNMKIELYDLETD 454
Cdd:cd16037 278 RVVFseYHAHGSPSGAFMLRKGRWKYIYY----VGYPPQLFDLEND 319
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
14-400 |
6.62e-56 |
|
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: 187.06 E-value: 6.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKH-SGHcGIRgndeapergrv 92
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMpSQH-GIH----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 wDFLAAERDSTLEGQRGLPSGTKTFVSILKEGGYRTGIVGKWGLGapgteslplnhgfdffygyncqrqahtyfplhlyr 172
Cdd:cd16149 69 -DWIVEGSHGKTKKPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLG----------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 173 neqreylandtviphtkldpgadplslssydklishvyspdkiqEEALRFMEEN--KKQPFFLYYATPLPHvpiqapqrl 250
Cdd:cd16149 113 --------------------------------------------DDAADFLRRRaeAEKPFFLSVNYTAPH--------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 251 idhyvrkfgdeSPYlgqadyfparyphaGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGptFNGGVDSPWFRS 330
Cdd:cd16149 140 -----------SPW--------------GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNG--FNMGHHGIWGKG 192
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1650049783 331 GGPFRSEygwgkcfLREGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNPATETD--GISFYP 400
Cdd:cd16149 193 NGTFPLN-------MYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFAD 257
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
14-433 |
8.78e-56 |
|
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: 193.43 E-value: 8.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIR-GNDEAPERGrv 92
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYpGVFYPGSRG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 wdflaaerdstlegqrGLPSGTKTFVSILKEGGYRTGIVGKW--GLGAPGTeSLPLNHGFDFFYGY-----NCQRQAHTY 165
Cdd:cd16158 80 ----------------GLPLNETTIAEVLKTVGYQTAMVGKWhlGVGLNGT-YLPTHQGFDHYLGIpyshdQGPCQNLTC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 166 FPlhlyrneqreylandtviPHTKL----DPGADPLSLSSYDKLISHVYSPDKIQEE----ALRFMEENKK--QPFFLYY 235
Cdd:cd16158 143 FP------------------PNIPCfggcDQGEVPCPLFYNESIVQQPVDLLTLEERyakfAKDFIADNAKegKPFFLYY 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 236 ATPLPHVPIQAPQRLIDHYVR-KFGDEspylgqadyfparyphagyaamVTYIDEKVGEIVDFLKKKGLYENTVIIISSD 314
Cdd:cd16158 205 ASHHTHYPQFAGQKFAGRSSRgPFGDA----------------------LAELDGSVGELLQTLKENGIDNNTLVFFTSD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 315 NGPTF----NGGVdspwfrsGGPFRSeygwGKCFLREGGIRVPLIVTWKGHIRAGAHTTLpCTSYDFYSTICELAG-VNP 389
Cdd:cd16158 263 NGPSTmrksRGGN-------AGLLKC----GKGTTYEGGVREPAIAYWPGRIKPGVTHEL-ASTLDILPTIAKLAGaPLP 330
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1650049783 390 ATETDGISFYPTLMESGDQMKHSYLYW--EFMDIEGQQAVRMGKWK 433
Cdd:cd16158 331 NVTLDGVDMSPILFEQGKSPRQTFFYYptSPDPDKGVFAVRWGKYK 376
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
13-433 |
6.82e-55 |
|
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: 190.76 E-value: 6.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKhsghcgirgndeAPERGRV 92
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGR------------LPIRNGF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 WDFLAAERDSTL--EGQRGLPSGTKTFVSILKEGGYRTGIVGKWGLGAPgTESLPLNHGFDFFYGY-NCQ-----RQAHT 164
Cdd:cd16157 69 YTTNAHARNAYTpqNIVGGIPDSEILLPELLKKAGYRNKIVGKWHLGHR-PQYHPLKHGFDEWFGApNCHfgpydNKAYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 165 YFPLhlYRNEQ---REYlandtviPHTKLDpgadplsLSSYDKLISHVYspdkiQEEALRFMEE--NKKQPFFLYYATPL 239
Cdd:cd16157 148 NIPV--YRDWEmigRYY-------EEFKID-------KKTGESNLTQIY-----LQEALEFIEKqhDAQKPFFLYWAPDA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 240 PHVPIQAPQrlidhyvrkfgdesPYLGQADyfparypHAGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTF 319
Cdd:cd16157 207 THAPVYASK--------------PFLGTSQ-------RGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAAL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 320 NGGVDSPwfRSGGPFRSeygwGKCFLREGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNPATE--TDGIS 397
Cdd:cd16157 266 ISAPEQG--GSNGPFLC----GKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDraIDGID 339
|
410 420 430
....*....|....*....|....*....|....*...
gi 1650049783 398 FYPTLMESGDQMKHSYLYW--EFMdiegqqAVRMGKWK 433
Cdd:cd16157 340 LLPVLLNGKEKDRPIFYYRgdELM------AVRLGQYK 371
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
13-415 |
2.34e-54 |
|
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: 190.58 E-value: 2.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSghcgIRGNDEAPERGRV 92
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYP----IRSGMASSHGMRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 WDFLAAerdstlegQRGLPSGTKTFVSILKEGGYRTGIVGKWGLG-----APGTESLPLNHGFDFFYGY------NCQ-- 159
Cdd:cd16159 77 ILFTAS--------SGGLPPNETTFAEVLKQQGYSTALIGKWHLGlhcesRNDFCHHPLNHGFDYFYGLpltnlkDCGdg 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 160 ---RQAHTYFPLhLYRNEQREYLANDTVIPHTKLD-------------PGADPLSLSSYDKLI----SHVYSPDKIQE-- 217
Cdd:cd16159 149 sngEYDLSFDPL-FPLLTAFVLITALTIFLLLYLGavskrffvfllilSLLFISLFFLLLITNryfnCILMRNHEVVEqp 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 218 ------------EALRFMEENKKQPFFLYYATPLPHVPIQApqrlidhyvrkfgdespylgqADYFPARYPHAGYAAMVT 285
Cdd:cd16159 228 mslenltqrltkEAISFLERNKERPFLLVMSFLHVHTALFT---------------------SKKFKGRSKHGRYGDNVE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 286 YIDEKVGEIVDFLKKKGLYENTVIIISSDNGP----TFNGGvdspwfRSGGPFRSEYGWGKCFLREGGIRVPLIVTWKGH 361
Cdd:cd16159 287 EMDWSVGQILDALDELGLKDNTFVYFTSDNGGhleeISVGG------EYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGV 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1650049783 362 IRAGAHTTLPCTSYDFYSTICELAGVN-PATET-DGISFYPTLMESGDQMKHSYLY 415
Cdd:cd16159 361 IPPGSVIDEPTSLMDIFPTVAALAGAPlPSDRIiDGRDLMPLLTGQEKRSPHEFLF 416
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
13-458 |
1.33e-53 |
|
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: 184.98 E-value: 1.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLGCFGQ-RRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIRGNdeapergr 91
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHN-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 92 vwdFLAaerdstlEGQRGLPSGTKTFVSILKEGGYRTGIVGKWGLGAPGTeSLPLNHGFDFFYGyncqrqahtyfplhly 171
Cdd:cd16161 73 ---FLP-------TSVGGLPLNETTLAEVLRQAGYATGMIGKWHLGQREA-YLPNSRGFDYYFG---------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 172 rneqreylandtvIPHtkldpgadplslSSYDKLishvysPDKIQEEALRFMEE--NKKQPFFLYYATPLPHVPIQAPQR 249
Cdd:cd16161 126 -------------IPF------------SHDSSL------ADRYAQFATDFIQRasAKDRPFFLYAALAHVHVPLANLPR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 250 lidhyvrkfgdespylgqadyFPARYPHAG-YAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGP-----TFNGGV 323
Cdd:cd16161 175 ---------------------FQSPTSGRGpYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGPwevkcELAVGP 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 324 DSPWFRSGGPFRSeygwGKCFLREGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVN--PATETDGISFYPT 401
Cdd:cd16161 234 GTGDWQGNLGGSV----AKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASlpPGRIYDGKDLSPV 309
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1650049783 402 LMeSGDQMKHSYLY-WEFMDIEGQ--QAVRMGKWK------GLRNGLKRGNMKIE-----LYDLETDSCEQ 458
Cdd:cd16161 310 LF-GGSKTGHRCLFhPNSGAAGAGalSAVRCGDYKahyatgGALACCGSTGPKLYhdpplLFDLEVDPAES 379
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
14-387 |
3.87e-52 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 178.77 E-value: 3.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGkhsghcgirgndeapergrvw 93
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTG--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 94 dFLAAERDSTLEGQRGLPSGTKTFVSILKEGGYRTGIVGKWGLGaPGTESLPLNHGFDFFYGYNcqrqahtYFPLHLYRN 173
Cdd:pfam00884 60 -LPPHNFGSYVSTPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLG-WYNNQSPCNLGFDKFFGRN-------TGSDLYADP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 174 EQREYLandtviphtkldpgadplslssydkLISHVYSPDKIQEEALRFmEENKKQPFFLYYATPLPHVPIQAPQRLIDH 253
Cdd:pfam00884 131 PDVPYN-------------------------CSGGGVSDEALLDEALEF-LDNNDKPFFLVLHTLGSHGPPYYPDRYPEK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 254 YvRKFGDESPYLGQAdyfparypHAGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFNGGvdspwfrsGGP 333
Cdd:pfam00884 185 Y-ATFKPSSCSEEQL--------LNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEG--------GGY 247
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1650049783 334 FRSEYGWgkcFLREGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGV 387
Cdd:pfam00884 248 LHGGKYD---NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
13-462 |
5.76e-48 |
|
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.
Pssm-ID: 293754 [Multi-domain] Cd Length: 435 Bit Score: 171.22 E-value: 5.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYgDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHsghcgirgndeaPERGRV 92
Cdd:cd16030 2 KPNVLFIAVDDLRP-WLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRR------------PDTTGV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 WDFLAAERDSTlegqrglpsgtKTFVSI---LKEGGYRTGIVGK-----WGLGAPGTESlplnhgFDFFYGYNcqrqaht 164
Cdd:cd16030 69 YDNNSYFRKVA-----------PDAVTLpqyFKENGYTTAGVGKifhpgIPDGDDDPAS------WDEPPNPP------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 165 yfPLHLYRNEQREYLANDTVIPHTKLDPGADPLSLSSYdklishvysPD-KIQEEALRFMEE--NKKQPFFL---YYAtp 238
Cdd:cd16030 125 --GPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAY---------PDgKVADEAIEQLRKlkDSDKPFFLavgFYK-- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 239 lPHVPIQAPQRLIDHYVRKFG-------------------DESPYLGQADYFPARYPHA------------GYAAMVTYI 287
Cdd:cd16030 192 -PHLPFVAPKKYFDLYPLESIplpnpfdpidlpevawndlDDLPKYGDIPALNPGDPKGplpdeqarelrqAYYASVSYV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 288 DEKVGEIVDFLKKKGLYENTVIIISSDNGptFNGGvdspwfrsggpfrsEYG-WGKCFLREGGIRVPLIVTWKGHIRAGA 366
Cdd:cd16030 271 DAQVGRVLDALEELGLADNTIVVLWSDHG--WHLG--------------EHGhWGKHTLFEEATRVPLIIRAPGVTKPGK 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 367 HTTLPCTSYDFYSTICELAGVNPATETDGISFYPTLMESGDQMKH-SYLYWEFMDIEGqQAVRMGKWkglR-----NGLK 440
Cdd:cd16030 335 VTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLKNPSAKWKDaAFSQYPRPSIMG-YSIRTERY---RytewvDFDK 410
|
490 500
....*....|....*....|..
gi 1650049783 441 RGNMkiELYDLETDSCEQRDVA 462
Cdd:cd16030 411 VGAE--ELYDHKNDPNEWKNLA 430
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
14-454 |
2.13e-44 |
|
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: 158.90 E-value: 2.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHsghcgirgndeaPERGRVW 93
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRL------------PSRIGAY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 94 DFlAAErdstlegqrgLPSGTKTFVSILKEGGYRTGIVGKWGLGAPgtESLplnHGFDFfygyncqrqahtyfplhlyrN 173
Cdd:cd16032 69 DN-AAE----------FPADIPTFAHYLRAAGYRTALSGKMHFVGP--DQL---HGFDY--------------------D 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 174 EQREYLANDtviphtKLdpgadplslssYDKLISHvyspdkiqeealrfmeenKKQPFFLYYATPLPHVPIQAPQRLIDH 253
Cdd:cd16032 113 EEVAFKAVQ------KL-----------YDLARGE------------------DGRPFFLTVSFTHPHDPYVIPQEYWDL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 254 YVRKfgdespylgqadyfpARypHAgYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFngGVDSPWFRsggp 333
Cdd:cd16032 158 YVRR---------------AR--RA-YYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDML--GERGLWYK---- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 334 frseygwgKCFlREGGIRVPLIVTWKGhIRAGAHTTLPCTSYDFYSTICELAGVNPA---TETDGISFYPtLMESGDQMK 410
Cdd:cd16032 214 --------MSF-FEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTAphvPPLDGRSLLP-LLEGGDSGG 282
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1650049783 411 HSYLYWEFMDiEGQQA----VRMGKWKGLRNGLKRGnmkiELYDLETD 454
Cdd:cd16032 283 EDEVISEYLA-EGAVApcvmIRRGRWKFIYCPGDPD----QLFDLEAD 325
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
14-458 |
2.07e-42 |
|
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: 154.82 E-value: 2.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLG------YGdlgcFGQRRIETPHIDRLAAEGMVFSNYYTgSPVSAAARCVLLTGKHsghcGIRGNDEAP 87
Cdd:cd16154 1 PNILLIIADDQGldssaqYS----LSSDLPVTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGKY----GFRTGVLAV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 88 ErgrvwDFLAAERDSTLEgQRGLPSGTKtfvsilkegGYRTGIVGKWGLGapGTESLPLNHG-FDFFYGYNcQRQAHTYF 166
Cdd:cd16154 72 P-----DELLLSEETLLQ-LLIKDATTA---------GYSSAVIGKWHLG--GNDNSPNNPGgIPYYAGIL-GGGVQDYY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 167 PLHLYRNEQREYlandtviphtkldpgadplslssydkliSHVYSPDKIQEEALRFMEeNKKQPFFLYYATPLPHVPIQA 246
Cdd:cd16154 134 NWNLTNNGQTTN----------------------------STEYATTKLTNLAIDWID-QQTKPWFLWLAYNAPHTPFHL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 247 PQRliDHYVRKFGDESPYLGQAdyfparyPHAGYAAMVTYIDEKVGEIVDFLKKKGLyENTVIIISSDNGpTFNGGVDSP 326
Cdd:cd16154 185 PPA--ELHSRSLLGDSADIEAN-------PRPYYLAAIEAMDTEIGRLLASIDEEER-ENTIIIFIGDNG-TPGQVVDLP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 327 WFRSGGpfrseygwgKCFLREGGIRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNPATETDGISFYPTLMEsG 406
Cdd:cd16154 254 YTRNHA---------KGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAEIHDSVSFKPLLSD-V 323
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1650049783 407 DQMKHSYLYWEFMDIEGQQAVRMGKWKGLR---NGLKrgnmkiELYDLETDSCEQ 458
Cdd:cd16154 324 NASTRQYNYTEYESPTTTGWATRNQYYKLIeseNGQE------ELYDLINDPSEQ 372
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
14-400 |
6.88e-42 |
|
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: 150.39 E-value: 6.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHsghcgirgndeaPERGRVW 93
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLY------------PFYHGVW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 94 DFLAAERDSTLegqrglpsgtktfVSILKEGGYRTGIVGKWGLGAPGTEslpLNHGFDFFygyncqrqahtyfplhlyrn 173
Cdd:cd16148 69 GGPLEPDDPTL-------------AEILRKAGYYTAAVSSNPHLFGGPG---FDRGFDTF-------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 174 eqreylandtviphtkldpgaDPLSLSSYDKLISHVYSPDKIQEEALRFMEENKK-QPFFL---YYAtplPHvpiqapqr 249
Cdd:cd16148 113 ---------------------EDFRGQEGDPGEEGDERAERVTDRALEWLDRNADdDPFFLflhYFD---PH-------- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 250 lidhyvrkfgdeSPYLgqadyfparyphagYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFNggvDSPWFR 329
Cdd:cd16148 161 ------------EPYL--------------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFG---EHGLYW 211
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1650049783 330 SGGPfrseygwgkcFLREGGIRVPLIVTWKGHIRAGAHTTLpCTSYDFYSTICELAGVNPATETDGISFYP 400
Cdd:cd16148 212 GHGS----------NLYDEQLHVPLIIRWPGKEPGKRVDAL-VSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
9-479 |
5.56e-41 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 153.29 E-value: 5.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 9 TDSVRPNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIRG-NDEAP 87
Cdd:PRK13759 2 VQTKKPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGyGDVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 88 ergrvWDFlaaerdstlegqrglpsgTKTFVSILKEGGYRTGIVGKWglgapgteslplnHGFDffygyncQRQAHTY-- 165
Cdd:PRK13759 82 -----WNY------------------KNTLPQEFRDAGYYTQCIGKM-------------HVFP-------QRNLLGFhn 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 166 -----FPLHLYRNEQREYLAN-DTVIPHTKL-DPGADP----LSLSSYD------KLISHVYSPDKIQEEALRFMEE-NK 227
Cdd:PRK13759 119 vllhdGYLHSGRNEDKSQFDFvSDYLAWLREkAPGKDPdltdIGWDCNSwvarpwDLEERLHPTNWVGSESIEFLRRrDP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 228 KQPFFLYYATPLPHVPIQAPQRLIDHYVRK------FGD----ESPYLGQADY------FPARYPH---AGYAAMVTYID 288
Cdd:PRK13759 199 TKPFFLKMSFARPHSPYDPPKRYFDMYKDAdipdphIGDweyaEDQDPEGGSIdalrgnLGEEYARrarAAYYGLITHID 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 289 EKVGEIVDFLKKKGLYENTVIIISSDNGPTFNggvDSPWFRSGGPFrseygwgkcflrEGGIRVPLIVTWKGHIRAGAHT 368
Cdd:PRK13759 279 HQIGRFLQALKEFGLLDNTIILFVSDHGDMLG---DHYLFRKGYPY------------EGSAHIPFIIYDPGGLLAGNRG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 369 TL---PCTSYDFYSTICELAGVNPATETDGISFYPTLMESGDQ------MKHSYLYWEFmdiegqQAVRMGKWK---GLR 436
Cdd:PRK13759 344 TVidqVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFGQYEGwrpylhGEHALGYSSD------NYLTDGKWKyiwFSQ 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1650049783 437 NGlkrgnmKIELYDLETDSCEQRDVA--PKHPEIVKKIGEIMKKE 479
Cdd:PRK13759 418 TG------EEQLFDLKKDPHELHNLSpsEKYQPRLREMRKKLVDH 456
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
13-397 |
3.57e-39 |
|
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: 146.54 E-value: 3.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLgygDLGCFGQRRIeTPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSgHC-GIRGNDEAPERGR 91
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPM-PKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYA-HNhGVTNNSPPGGGYP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 92 VWDflaaerdstlegQRGLPSgtKTFVSILKEGGYRTGIVGKW--GLGAPGTESL-PLnhGFDFFYGyncqrqahtyfPL 168
Cdd:cd16147 76 KFW------------QNGLER--STLPVWLQEAGYRTAYAGKYlnGYGVPGGVSYvPP--GWDEWDG-----------LV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 169 HLYRNEqreylaNDTVIPHTKLDPGADPlslssydkliSHVYSPDKIQEEALRFMEE--NKKQPFFLYYATPLPHVPIQ- 245
Cdd:cd16147 129 GNSTYY------NYTLSNGGNGKHGVSY----------PGDYLTDVIANKALDFLRRaaADDKPFFLVVAPPAPHGPFTp 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 246 APQrlidhYVRKF-GDESPYLGQAdYFPARYPHAGY--------AAMVTYI--------------DEKVGEIVDFLKKKG 302
Cdd:cd16147 193 APR-----YANLFpNVTAPPRPPP-NNPDVSDKPHWlrrlpplnPTQIAYIdelyrkrlrtlqsvDDLVERLVNTLEATG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 303 LYENTVIIISSDNGptFNggvdspWfrsgGPFRseYGWGKCFLREGGIRVPLIVTWKGhIRAGAHTTLPCTSYDFYSTIC 382
Cdd:cd16147 267 QLDNTYIIYTSDNG--YH------L----GQHR--LPPGKRTPYEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTIL 331
|
410
....*....|....*
gi 1650049783 383 ELAGVNPATETDGIS 397
Cdd:cd16147 332 DLAGAPPPSDMDGRS 346
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
13-479 |
1.83e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 133.12 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGirgndeapergrV 92
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETG------------C 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 WdflaaeRDStlegqRGLPSGTKTFVSILKEGGYRTGIVGKWglgapgteslplnhgfdffygyncqrqahtyfplHLYR 172
Cdd:cd16152 69 F------RNG-----IPLPADEKTLAHYFRDAGYETGYVGKW----------------------------------HLAG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 173 neqreylandtviphtkldpgadplslssydklishvYSPDKIQEEALRFMEE-NKKQPFFLYYATPLPH---------V 242
Cdd:cd16152 104 -------------------------------------YRVDALTDFAIDYLDNrQKDKPFFLFLSYLEPHhqndrdryvA 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 243 PIQAPQRLIDHYVRkfGDESPYLGQAdyfPARYPhaGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFNGg 322
Cdd:cd16152 147 PEGSAERFANFWVP--PDLAALPGDW---AEELP--DYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCHFRT- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 323 vdspwfRSGGPFRSeygwgkCFlrEGGIRVPLIVTWKGhIRAGAHTTLPCTSYDFYSTICELAGVNPATETDGISFYPTL 402
Cdd:cd16152 219 ------RNAEYKRS------CH--ESSIRVPLVIYGPG-FNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLV 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 403 MESGDQmkhsylyWE---FMDIEGQQ---AVRMGKWK------GLRNGLKRGNMKIE---LYDLETDSCEQRDVA--PKH 465
Cdd:cd16152 284 DGKVED-------WRnevFIQISESQvgrAIRTDRWKysvaapDKDGWKDSGSDVYVedyLYDLEADPYELVNLIgrPEY 356
|
490
....*....|....
gi 1650049783 466 PEIVKKIGEIMKKE 479
Cdd:cd16152 357 REVAAELRERLLAR 370
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
14-457 |
3.38e-33 |
|
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: 131.35 E-value: 3.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIRGNDEApergrvw 93
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 94 dflaaerdstlegqrgLPSGTKTFVSILKEGGYRTGIVGKWGLgapgteslplnHGFDFFYGYNCQRQAHtyfPLHLYrn 173
Cdd:cd16156 74 ----------------LGDNVKTIGQRLSDNGIHTAYIGKWHL-----------DGGDYFGNGICPQGWD---PDYWY-- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 174 EQREYLANDTVIPHTKLDPGADPLSLSSYDKLISHVYspdKIQEEALRFMEENKKQPFFLYYATPLPHVPIQAPQRlidh 253
Cdd:cd16156 122 DMRNYLDELTEEERRKSRRGLTSLEAEGIKEEFTYGH---RCTNRALDFIEKHKDEDFFLVVSYDEPHHPFLCPKP---- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 254 YVRKFGD-ESPYL-----------------GQADYFPAR----YPHAGYAAMVTYIDEKVGEIVDFLKKKglYENTVIII 311
Cdd:cd16156 195 YASMYKDfEFPKGenayddlenkplhqrlwAGAKPHEDGdkgtIKHPLYFGCNSFVDYEIGRVLDAADEI--AEDAWVIY 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 312 SSDNGpTFNGGvdspwfrsggpfRSEYGWGKCFLREggI-RVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNPA 390
Cdd:cd16156 273 TSDHG-DMLGA------------HKLWAKGPAVYDE--ItNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQP 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1650049783 391 TETDGISFYPTLmESGDQMKHSYLYWEFMDIE-------GQQAVRM---GKWKGLRNGLKRGnmkiELYDLETDSCE 457
Cdd:cd16156 338 KVLEGESILATI-EDPEIPENRGVFVEFGRYEvdhdgfgGFQPVRCvvdGRYKLVINLLSTD----ELYDLEKDPYE 409
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
13-397 |
6.81e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 118.25 E-value: 6.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLGCFGQ----------RRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIRG 82
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 83 NDEApergrvwdflaaerdstlegQRGLPSGTKTFVSILKEGGYRTGIVGKWGLGAPgteslplnhgfdffygyncQRqa 162
Cdd:cd16153 81 FEAA--------------------HPALDHGLPTFPEVLKKAGYQTASFGKSHLEAF-------------------QR-- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 163 htyfplhlyrneqreYLANDT---VIPHTKLDPGADPlslssydklishvyspdkiqeealrfmeenkKQPFFLYYATPL 239
Cdd:cd16153 120 ---------------YLKNANqsyKSFWGKIAKGADS-------------------------------DKPFFVRLSFLQ 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 240 PHVPIQAPQRLIDHYvrkfgdespylgqaDYFparyphagyaAMVTYIDEKVGEIVDFLKKKGLY---ENTVIIISSDNG 316
Cdd:cd16153 154 PHTPVLPPKEFRDRF--------------DYY----------AFCAYGDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHG 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 317 PTFN-GGVDS---PWFRSggpfrseygwgkcflreggIRVPLIVTWKGHIRAGAHT---TLpCTSYDFYSTICELAGVNP 389
Cdd:cd16153 210 WHLGeQGILAkftFWPQS-------------------HRVPLIVVSSDKLKAPAGKvrhDF-VEFVDLAPTLLAAAGVDV 269
|
410
....*....|
gi 1650049783 390 A--TETDGIS 397
Cdd:cd16153 270 DapDYLDGRD 279
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
14-476 |
5.79e-27 |
|
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: 113.12 E-value: 5.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKH-SGHcgirgndeaperGRV 92
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYlMNH------------RSV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 WDFLAaerdstlegqrgLPSGTKTFVSILKEGGYRTGIVGKwGLGAPGTESLPLNHGFDFFY-----GYNcqrqahTYFP 167
Cdd:cd16028 69 WNGTP------------LDARHLTLALELRKAGYDPALFGY-TDTSPDPRGLAPLDPRLLSYelampGFD------PVDR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 168 LHLYRNEQRE--YLAndtviphtkldpgadplslssydklishvyspdkiqEEALRFMEENKKQPFFLYYATPLPHVPIQ 245
Cdd:cd16028 130 LDEYPAEDSDtaFLT------------------------------------DRAIEYLDERQDEPWFLHLSYIRPHPPFV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 246 APQ---RLID------------------------HYVRKFGDESPYLGQADYFPARYPH-----AGYAAMVTYIDEKVGE 293
Cdd:cd16028 174 APApyhALYDpadvpppiraeslaaeaaqhpllaAFLERIESLSFSPGAANAADLDDEEvaqmrATYLGLIAEVDDHLGR 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 294 IVDFLKKKGLYENTVIIISSDNGptfnggvdspwfrsggpfrsEYG-----WGKCFLREGGIRVPLIVTWKGhiRAGAHT 368
Cdd:cd16028 254 LFDYLKETGQWDDTLIVFTSDHG--------------------EQLgdhwlWGKDGFFDQAYRVPLIVRDPR--READAT 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 369 TLPCT-----SYDFYSTICELAGVNPATETDGISFYPTLMESGDQMKHSYLYWEF---------------MDIEGQQ--A 426
Cdd:cd16028 312 RGQVVdafteSVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQPSDWRDAVHYEYdfrdvstrrpqealgLSPDECSlaV 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1650049783 427 VRMGKWK-----GLRNglkrgnmkiELYDLETDSCEQRDVA--PKHPEIVKKIGEIM 476
Cdd:cd16028 392 IRDERWKyvhfaALPP---------LLFDLKNDPGELRDLAadPAYAAVVLRYAQKL 439
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
14-471 |
1.64e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 108.48 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGK--H-SGHcgirgndeaperg 90
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWypHvNGH------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 91 RVWDFLaaerdstlegqrgLPSGTKTFVSILKEGGYRTGIVGKWGLgapgtesLPLNHGFDFF--YGYNCQRQAhtyfpl 168
Cdd:cd16150 68 RTLHHL-------------LRPDEPNLLKTLKDAGYHVAWAGKNDD-------LPGEFAAEAYcdSDEACVRTA------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 169 hlyrneqREYLANdtviphtkldpgadplslssydklishvYSPDKiqeealrfmeenkkqPFFLYYATPLPHVPIQAPQ 248
Cdd:cd16150 122 -------IDWLRN----------------------------RRPDK---------------PFCLYLPLIFPHPPYGVEE 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 249 RLIDHYVRK-----------FGDESPYLGQADYF------PARYP--HAGYAAMVTYIDEKVGEIVDFLKKKGLYENTVI 309
Cdd:cd16150 152 PWFSMIDREklpprrppglrAKGKPSMLEGIEKQgldrwsEERWRelRATYLGMVSRLDHQFGRLLEALKETGLYDDTAV 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 310 IISSDNgptfnggvdspwfrsgGPFRSEYG----WGKCFlREGGIRVPLIVTWKGHIrAGAHTTLPCTSYDFYSTICELA 385
Cdd:cd16150 232 FFFSDH----------------GDYTGDYGlvekWPNTF-EDCLTRVPLIIKPPGGP-AGGVSDALVELVDIPPTLLDLA 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 386 GVNPATETDGISFYPTLMESGDQMK-------------------HSYLYWEFMDIEGQQ----------AVRMGKWKGLR 436
Cdd:cd16150 294 GIPLSHTHFGRSLLPVLAGETEEHRdavfseggrlhgeeqamegGHGPYDLKWPRLLQQeeppehtkavMIRTRRYKYVY 373
|
490 500 510
....*....|....*....|....*....|....*..
gi 1650049783 437 nglkRGNMKIELYDLETDSCEQRDVA--PKHPEIVKK 471
Cdd:cd16150 374 ----RLYEPDELYDLEADPLELHNLIgdPAYAEIIAE 406
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
14-385 |
1.24e-20 |
|
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: 90.94 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVF----SNYYTGSPVSAAArcvLLTGKHSGHCGIRGNDEAPER 89
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnfrsVSPPTSSAPNHAA---LLTGAYPTLHGYTGNGSADPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 90 GRVWDFlaaerdstlegqrGLPSGTKTFVSILKEGGYRTGIVGKWglgapgteslplnhgfdffygyncqrqahtyfplh 169
Cdd:cd00016 78 LPSRAA-------------GKDEDGPTIPELLKQAGYRTGVIGLL----------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 170 lyrneqreylandtviphtkldpgadplslssydklishvyspDKIQEEAlrfmeenKKQPFFLYYATPLPHVPIQAPQR 249
Cdd:cd00016 110 -------------------------------------------KAIDETS-------KEKPFVLFLHFDGPDGPGHAYGP 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 250 LidhyvrkfgdespylgqadyfparypHAGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFnGGVDSPWFR 329
Cdd:cd00016 140 N--------------------------TPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGID-KGHGGDPKA 192
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1650049783 330 SGGPFRSeygwgkcflrEGGIRVPLIVTWKGHiRAGAHTTLPCTSYDFYSTICELA 385
Cdd:cd00016 193 DGKADKS----------HTGMRVPFIAYGPGV-KKGGVKHELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
14-418 |
1.52e-17 |
|
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: 83.41 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGKHSGHCGIRGNDEAPErgrvw 93
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPM----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 94 dflaaerdstlegQRGLPSGTKTFVSILKEGGYRTGIVGKWGLGAPGteslplNHGFDFfygyncqrqahtyfplhlyrn 173
Cdd:cd16035 76 -------------QPLLSPDVPTLGHMLRAAGYYTAYKGKWHLSGAA------GGGYKR--------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 174 eqreylandtviphtklDPGadplslssydklishvyspdkIQEEALRFMEENKK-----QPFFLyyATPL--PH---VP 243
Cdd:cd16035 116 -----------------DPG---------------------IAAQAVEWLRERGAknadgKPWFL--VVSLvnPHdimFP 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 244 IQAPQRLidHYVRKFgdespylgqadyfparyphagYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGptfnggv 323
Cdd:cd16035 156 PDDEERW--RRFRNF---------------------YYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG------- 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 324 dspwfrsggpfrsEYGWGKCFLREGG------IRVPLIVTWKGHIRAGAHTTLPCTSYDFYSTICELAGVNPATETD--- 394
Cdd:cd16035 206 -------------EMGGAHGLRGKGFnayeeaLHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATeap 272
|
410 420 430
....*....|....*....|....*....|..
gi 1650049783 395 ---GISFYPTLM-ESGDQMKHSYLY----WEF 418
Cdd:cd16035 273 plpGRDLSPLLTdADADAVRDGILFtydrYKF 304
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
14-454 |
6.14e-17 |
|
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: 82.20 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGyGDLGCFGQRR-IETPHIDRLAAEGMVFSNYYTGSPVsaaarCvlltgkhsghCgirgndeaPERGRV 92
Cdd:cd16171 1 PNVVMVMSDSFD-GRLTFRPGNQvVDLPYINFMKQHGSVFLNAYTNSPI-----C----------C--------PSRAAM 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 WDFLAAERDSTLEGQRGLPSGTKTFVSILKEGGYRTGIVGKwglgapgteslplnhgFDFFYGYNCQR---QAHTYFPLH 169
Cdd:cd16171 57 WSGLFTHLTESWNNYKGLDPNYPTWMDRLEKHGYHTQKYGK----------------LDYTSGHHSVSnrvEAWTRDVPF 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 170 LYRNEQReylandtviphtkldPGADPLSLSSYDKLISHVYSPDKIQEEALRFMEENKKQPFFLYYATPLPHvpiqaPQR 249
Cdd:cd16171 121 LLRQEGR---------------PTVNLVGDRSTVRVMLKDWQNTDKAVHWIRKEAPNLTQPFALYLGLNLPH-----PYP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 250 lidhyvrkfgdeSPYLGQaDYFPARYPHAGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTfnggvdspwfr 329
Cdd:cd16171 181 ------------SPSMGE-NFGSIRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGEL----------- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 330 sGGPFRSEYgwgKCFLREGGIRVPLIVTWKGhIRAGAHTTLPCTSYDFYSTICELAGVNPATETDGISFYPTLMESGDQM 409
Cdd:cd16171 237 -AMEHRQFY---KMSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLLSESSIKE 311
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1650049783 410 KHS---YLYWEFMDIEGQQA------VRMGKWK--GLRNGLkrgNMKIELYDLETD 454
Cdd:cd16171 312 SPSrvpHPDWVLSEFHGCNVnastymLRTNSWKyiAYADGN---SVPPQLFDLSKD 364
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
13-316 |
9.44e-15 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 75.55 E-value: 9.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLgcfgqRRIETPHIDRLAAEGMVFSNYYTGSP-VSAAARCVLLTGKHSGHCGIRGND-EAPERG 90
Cdd:COG1524 23 AKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFPsTTAPAHTTLLTGLYPGEHGIVGNGwYDPELG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 91 RVWDFLAAERDSTLEGQRglpSGTKTFVSILKEGGYRTGIVGKWGLGAPGteslplnhgfdfFYGYNCQRQAHTYFPLHL 170
Cdd:COG1524 98 RVVNSLSWVEDGFGSNSL---LPVPTIFERARAAGLTTAAVFWPSFEGSG------------LIDAARPYPYDGRKPLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 171 YRnEQREYLANDTViphtkldpgadplslssydklishvyspdkiqeEALRfmeenKKQPFFLY-YatpLPHVpiqapqr 249
Cdd:COG1524 163 NP-AADRWIAAAAL---------------------------------ELLR-----EGRPDLLLvY---LPDL------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1650049783 250 liDHYVRKFGDESPylgqadyfparyphaGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNG 316
Cdd:COG1524 194 --DYAGHRYGPDSP---------------EYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
13-388 |
1.92e-14 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 75.85 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 13 RPNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYTGSPVSAAARCVLLTGkhsghcgirgndeapergrv 92
Cdd:COG1368 234 KPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTG-------------------- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 93 wdFLAAERDST--LEGQRGLPSgtktFVSILKEGGYRTgivgkwglgapgteslplnhgfDFFYGYNcqrqahTYFplhl 170
Cdd:COG1368 294 --LPPLPGGSPykRPGQNNFPS----LPSILKKQGYET----------------------SFFHGGD------GSF---- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 171 yRNEQREYLAN--DTVIphtkldpgadplSLSSYDKLISHVYS-PDKIQ-EEALRFMEEnKKQPFFLYYATPLPHVPIQA 246
Cdd:COG1368 336 -WNRDSFYKNLgfDEFY------------DREDFDDPFDGGWGvSDEDLfDKALEELEK-LKKPFFAFLITLSNHGPYTL 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 247 PqrliDHYVRKFGDESPYLGQadyfparyphagYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPtfnggvdsp 326
Cdd:COG1368 402 P----EEDKKIPDYGKTTLNN------------YLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGP--------- 456
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1650049783 327 wfRSGGPFRSEYGWGKcflreggIRVPLIVTWKGHIRAGAHTTLpCTSYDFYSTICELAGVN 388
Cdd:COG1368 457 --RSPGKTDYENPLER-------YRVPLLIYSPGLKKPKVIDTV-GSQIDIAPTLLDLLGID 508
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
14-386 |
2.81e-13 |
|
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: 70.02 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLGCFGQRRIETPHIDRLAAEGMVFSNYYtgSPV----SAAARCVLLTGkhsghcgirgndeaper 89
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFY--SPGfgggTANGEFEVLTG----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 90 grvwdfLAAERDSTLEGQRGLPSGTKTFVSILKEGGYRTGIVGkwglGAPGT----ESLPLNHGFDFFYGYNcqrqahtY 165
Cdd:cd16015 62 ------LPPLPLGSGSYTLYKLNPLPSLPSILKEQGYETIFIH----GGDASfynrDSVYPNLGFDEFYDLE-------D 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 166 FPlHLYRNEQREYLandtviphtkldpgadplslssYDKlisHVYspdkiqEEALRFMEENKKQPFFLYYATPLPHVPIQ 245
Cdd:cd16015 125 FP-DDEKETNGWGV----------------------SDE---SLF------DQALEELEELKKKPFFIFLVTMSNHGPYD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 246 APQRLIDHYVRKfGDESPYLGQadyfparyphagYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFNGGVDS 325
Cdd:cd16015 173 LPEEKKDEPLKV-EEDKTELEN------------YLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDE 239
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1650049783 326 PWFRSGGPFrseygwgkcflreggiRVPLIVtWKGHIRAGAHTTLPCTSYDFYSTICELAG 386
Cdd:cd16015 240 TDEDPLDLY----------------RTPLLI-YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
214-360 |
4.56e-12 |
|
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: 68.39 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 214 KIQEEALRFMEE-NKKQPFFLY--------YATPLPHVPIQAPQRLIDhYVRKFGDESPYLgqadyFPARYPHAgyaamV 284
Cdd:COG3083 365 QITAQWLQWLDQrDSDRPWFSYlfldaphaYSFPADYPKPFQPSEDCN-YLALDNESDPTP-----FKNRYRNA-----V 433
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1650049783 285 TYIDEKVGEIVDFLKKKGLYENTVIIISSDNGPTFNGGVDSPWfRSGGPFrSEYgwgkcflregGIRVPLIVTWKG 360
Cdd:COG3083 434 HYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQNYW-GHNSNF-SRY----------QLQVPLVIHWPG 497
|
|
| DUF4994 |
pfam16385 |
Domain of unknown function; This family around 100 residues locates in the C-terminal of some ... |
416-476 |
3.12e-07 |
|
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: 48.44 E-value: 3.12e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1650049783 416 WEFmdIEGQQAVRMGKWKGLrnglKRGNMKIE-LYDLETDSCEQRDVAPKHPEIVKKIGEIM 476
Cdd:pfam16385 43 WKY--IEPSDGPAYIKWTKI----ETGNSPEPqLYDLKADPGEQENVAKKHPEKVKELQTIL 98
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
39-316 |
4.43e-05 |
|
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: 45.49 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 39 TPHIDRLAAEGMVFSNYYTGSP-VSAAARCVLLTGKHSGHCGIRGND-EAPERGRVWDFlaaeRDSTLEGQRGLpSGTKT 116
Cdd:pfam01663 20 TPNLAALAKEGVSAPNLTPVFPtLTFPNHYTLVTGLYPGSHGIVGNTfYDPKTGEYLVF----VISDPEDPRWW-QGEPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 117 FVSILKEGgYRTGIVGkWglgaPGTEslplnhgfdffygyncqrqahtyFPLHLYRNEQREYLAndtviphtkldpgaDP 196
Cdd:pfam01663 95 WDTAAKAG-VRAAALF-W----PGSE-----------------------VDYSTYYGTPPRYLK--------------DD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 197 LSLS-SYDKLISHVYSPDKIQEEALRFMEEnkKQPFFLYYatpLPHvpiqapqrlIDHYVRKFGDESPylgqadyfpary 275
Cdd:pfam01663 132 YNNSvPFEDRVDTAVLQTWLDLPFADVAAE--RPDLLLVY---LEE---------PDYAGHRYGPDSP------------ 185
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1650049783 276 phaGYAAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNG 316
Cdd:pfam01663 186 ---EVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHG 223
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
14-316 |
5.98e-05 |
|
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: 44.88 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 14 PNIIFVLADDLGYGDLgcfgQRRIETPHIDRLAAEGMV------------FSNYYTgspvsaaarcvLLTGKHSGHCGIR 81
Cdd:cd16018 1 PPLIVISIDGFRWDYL----DRAGLTPNLKRLAEEGVRakyvkpvfptltFPNHYS-----------IVTGLYPESHGIV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 82 GN---DeaPERGRVWDFLAAERDSTLEGqrglpsgTKTFVSILKEGGYRTGIVGkWglgaPGTESLPLNHGFDFfygynC 158
Cdd:cd16018 66 GNyfyD--PKTNEEFSDSDWVWDPWWIG-------GEPIWVTAEKAGLKTASYF-W----PGSEVAIIGYNPTP-----I 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650049783 159 QRQAHTYFPLHLYRNEQREylanDTVIphtkldpgadplslssydklishvyspDKIQEEALRFMeenkkqpfFLYYATP 238
Cdd:cd16018 127 PLGGYWQPYNDSFPFEERV----DTIL---------------------------EWLDLERPDLI--------LLYFEEP 167
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1650049783 239 lphvpiqapqrliDHYVRKFGDESPylgQADyfparyphagyaAMVTYIDEKVGEIVDFLKKKGLYENTVIIISSDNG 316
Cdd:cd16018 168 -------------DSAGHKYGPDSP---EVN------------EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG 217
|
|
| |
