|
Name |
Accession |
Description |
Interval |
E-value |
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
24-472 |
2.49e-152 |
|
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: 439.25 E-value: 2.49e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFESGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSFDK 103
Cdd:cd16027 2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRS--RGFPLPDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 104 VQSLPLLLNQAGVRTGIIGKKHVGPETVYPFDFafteENSSVMQVGRNITRIKQLVQKFLQTQD-DRPFFLYVAFHDPHR 182
Cdd:cd16027 80 VKTLPELLREAGYYTGLIGKTHYNPDAVFPFDD----EMRGPDDGGRNAWDYASNAADFLNRAKkGQPFFLWFGFHDPHR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 183 CGHSQPQYGTfcekfgngesgmgyipdwtpqIYDPQDVMVPYFVPDTPAARADLAAQYTTIGRMDQGVGLVLQELRGAGV 262
Cdd:cd16027 156 PYPPGDGEEP---------------------GYDPEKVKVPPYLPDTPEVREDLADYYDEIERLDQQVGEILDELEEDGL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 263 LNDTLIIFTSDNGIPFPSGRTNLYWPGTAEPLLVSSPEHPQRwGQVSDAYVSLLDLTPTILDWFSIPYPSYaifgsktiq 342
Cdd:cd16027 215 LDNTIVIFTSDHGMPFPRAKGTLYDSGLRVPLIVRWPGKIKP-GSVSDALVSFIDLAPTLLDLAGIEPPEY--------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 343 LTGRSLLPALEAE--PLWATVFSSQSHHEVTmSYPMRSVYHQNFRLIHNLsfkMPfpidqdfyvsptfqdllnrtttgrp 420
Cdd:cd16027 285 LQGRSFLPLLKGEkdPGRDYVFAERDRHDET-YDPIRSVRTGRYKYIRNY---MP------------------------- 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 31543697 421 tgwykdlhryyyrerWELYDISRDPRETRNLAADPDLAQVLEMLKAQLVKWQ 472
Cdd:cd16027 336 ---------------EELYDLKNDPDELNNLADDPEYAEVLEELRAALDAWM 372
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
10-478 |
1.61e-85 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 269.06 E-value: 1.61e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 10 TILLVLGLCGAHSR-------NVLLIVADD-GGFESGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGL 81
Cdd:COG3119 4 LLLLLLALLAAAAAaaaakrpNILFILADDlGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 82 PQHQNGMYGLHQDVHHFNSFDkVQSLPLLLNQAGVRTGIIGKKHvgpetVYpFDFAFTEEnssvmqvgrnitrikqlVQK 161
Cdd:COG3119 84 YPHRTGVTDNGEGYNGGLPPD-EPTLAELLKEAGYRTALFGKWH-----LY-LTDLLTDK-----------------AID 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 162 FLQTQ--DDRPFFLYVAFHDPHRCGHSQPQYgtfcekfgngesgmgyipdwtPQIYDPQDVMVP-YFVPD---TPAARAD 235
Cdd:COG3119 140 FLERQadKDKPFFLYLAFNAPHAPYQAPEEY---------------------LDKYDGKDIPLPpNLAPRdltEEELRRA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 236 LAAQYTTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGIPFPS-----GRTNLYWPGTAEPLLVSSPEHPQRwGQVSD 310
Cdd:COG3119 199 RAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEhglrgGKGTLYEGGIRVPLIVRWPGKIKA-GSVSD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 311 AYVSLLDLTPTILDWFSIPYPSYaifgsktiqLTGRSLLPALE-AEPLWATVFssqsHHEVTMSYPMRSVYHQNFRLIHN 389
Cdd:COG3119 278 ALVSLIDLLPTLLDLAGVPIPED---------LDGRSLLPLLTgEKAEWRDYL----YWEYPRGGGNRAIRTGRWKLIRY 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 390 lsfkmpfpidqdfyvsptfqdllnrtttgrptgwykdlhrYYYRERWELYDISRDPRETRNLAAdpDLAQVLEMLKAQLV 469
Cdd:COG3119 345 ----------------------------------------YDDDGPWELYDLKNDPGETNNLAA--DYPEVVAELRALLE 382
|
....*....
gi 31543697 470 KWQWETHDP 478
Cdd:COG3119 383 AWLKELGDP 391
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
23-468 |
4.37e-64 |
|
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: 214.32 E-value: 4.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 23 RNVLLIVADDGGFES-GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvhhfNSF 101
Cdd:cd16031 3 PNIIFILTDDHRYDAlGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG-----PLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 102 DKVQ-SLPLLLNQAGVRTGIIGKKHVGPETVYP---FDF-------------AFTEENSSVMQVGRNITRIKQLVQKFLQ 164
Cdd:cd16031 78 DASQpTYPKLLRKAGYQTAFIGKWHLGSGGDLPppgFDYwvsfpgqgsyydpEFIENGKRVGQKGYVTDIITDKALDFLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 165 TQD-DRPFFLYVAFHDPHRCGHSQPQYGtfcEKFGNGEsgMGYIPDWTPQIYDPQ----------DVMVPYFVPDTPAAR 233
Cdd:cd16031 158 ERDkDKPFCLSLSFKAPHRPFTPAPRHR---GLYEDVT--IPEPETFDDDDYAGRpewareqrnrIRGVLDGRFDTPEKY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 234 ADLA-AQYTTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGipFPSG-------RTnLYWPGTAEPLLVSSPEHPQRw 305
Cdd:cd16031 233 QRYMkDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNG--FFLGehglfdkRL-MYEESIRVPLIIRDPRLIKA- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 306 GQVSDAYVSLLDLTPTILDWFSIPYPSYaifgsktIQltGRSLLPALEAEPL--WATVFssqshhevtmsypmrsvYHQN 383
Cdd:cd16031 309 GTVVDALVLNIDFAPTILDLAGVPIPED-------MQ--GRSLLPLLEGEKPvdWRKEF-----------------YYEY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 384 FrlihnlsfkmpfpIDQDFYVSPTFQDLlnRTTTgrptgwYKDLHRYYYRERWELYDISRDPRETRNLAADPDLAQVLEM 463
Cdd:cd16031 363 Y-------------EEPNFHNVPTHEGV--RTER------YKYIYYYGVWDEEELYDLKKDPLELNNLANDPEYAEVLKE 421
|
....*
gi 31543697 464 LKAQL 468
Cdd:cd16031 422 LRKRL 426
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
24-451 |
3.50e-62 |
|
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: 208.45 E-value: 3.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGF-ESGVYNNtAIATPHLDALSRHSLIFRNaFTSVSSCSPSRASLLTGLPQHQNG---MYGLHQDVHHFN 99
Cdd:cd16025 4 NILLILADDLGFsDLGCFGG-EIPTPNLDALAAEGLRFTN-FHTTALCSPTRAALLTGRNHHQVGmgtMAELATGKPGYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 100 SF--DKVQSLPLLLNQAGVRTGIIGKKHVGPETVYpFDFAFTEenssvmqvgRNITRIKQlvqkflQTQDDRPFFLYVAF 177
Cdd:cd16025 82 GYlpDSAATIAEVLKDAGYHTYMSGKWHLGPDDYY-STDDLTD---------KAIEYIDE------QKAPDKPFFLYLAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 178 ---HDPHrcgHSQPQY-----GTFcekfgngESG--------------MGYIP-DWTPQIYDPQdvmvpyfVPD----TP 230
Cdd:cd16025 146 gapHAPL---QAPKEWidkykGKY-------DAGwdalreerlerqkeLGLIPaDTKLTPRPPG-------VPAwdslSP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 231 AARADL-------AAQyttIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNG------------IPFPSGRTNLYWPGTA 291
Cdd:cd16025 209 EEKKLEarrmevyAAM---VEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGasaepgwanasnTPFRLYKQASHEGGIR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 292 EPLLVSSPEHPQRWGQVSDAYVSLLDLTPTILDWFSIPYPSyAIFGSKTIQLTGRSLLPALEAEplwatvfsSQSHHEVT 371
Cdd:cd16025 286 TPLIVSWPKGIKAKGGIRHQFAHVIDIAPTILELAGVEYPK-TVNGVPQLPLDGVSLLPTLDGA--------AAPSRRRT 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 372 MSYPM---RSVYHQNFRLIhnlsfkmpfpidqdfyvsptfqdllnrtTTGRPTGWYkdlhryyyrERWELYDISRDPRET 448
Cdd:cd16025 357 QYFELfgnRAIRKGGWKAV----------------------------ALHPPPGWG---------DQWELYDLAKDPSET 399
|
...
gi 31543697 449 RNL 451
Cdd:cd16025 400 HDL 402
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
24-331 |
1.70e-60 |
|
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293746 [Multi-domain] Cd Length: 236 Bit Score: 198.43 E-value: 1.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFES-GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNsfD 102
Cdd:cd16022 2 NILLIMTDDLGYDDlGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLP--P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 103 KVQSLPLLLNQAGVRTGIIGKKHvgpetvypfdfafteenssvmqvgrnitrikQLVQKFLQTQD-DRPFFLYVAFHDPH 181
Cdd:cd16022 80 DEPTLAELLKEAGYRTALIGKWH-------------------------------DEAIDFIERRDkDKPFFLYVSFNAPH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 182 rcghsqpqygtfcekfgngesgmgyipdwTPQIYdpqdvmvpyfvpdtpaaradlaaqYTTIGRMDQGVGLVLQELRGAG 261
Cdd:cd16022 129 -----------------------------PPFAY------------------------YAMVSAIDDQIGRILDALEELG 155
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543697 262 VLNDTLIIFTSDNGIPFPSGR-----TNLYWPGTAEPLLVSSPEHPQRwGQVSDAYVSLLDLTPTILDWFSIPYP 331
Cdd:cd16022 156 LLDNTLIVFTSDHGDMLGDHGlrgkkGSLYEGGIRVPFIVRWPGKIPA-GQVSDALVSLLDLLPTLLDLAGIEPP 229
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-471 |
2.82e-56 |
|
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: 193.14 E-value: 2.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADD-GGFESGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGL--PQHQNGMYGLHQDVHHFNS 100
Cdd:cd16144 2 NIVLILVDDlGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQypARLGITDVIPGRRGPPDNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 101 F-----------DKVQSLPLLLNQAGVRTGIIGKKHVGPE-TVYP----FD---------------FAFTEENSSVMQVG 149
Cdd:cd16144 82 KlipppsttrlpLEEVTIAEALKDAGYATAHFGKWHLGGEgGYGPedqgFDvniggtgnggppsyyFPPGKPNPDLEDGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 150 RNITRIKQLVQ---KFLQTQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgyipdwTPQIYDP------QDV 220
Cdd:cd16144 162 EGEYLTDRLTDeaiDFIEQNKDKPFFLYLSHYAVH-----------------------------TPIQARPeliekyEKK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 221 MVPYFVPDTPAARAdlaaqyTTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNG------------IPFPSGRTNLYWP 288
Cdd:cd16144 213 KKGLRKGQKNPVYA------AMIESLDESVGRILDALEELGLADNTLVIFTSDNGglstrggpptsnAPLRGGKGSLYEG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 289 GTAEPLLVSSPEHPQRwGQVSDAYVSLLDLTPTILDWFSIPYPSYAIfgsktiqLTGRSLLPALEAEplwatvfssqshh 368
Cdd:cd16144 287 GIRVPLIVRWPGVIKP-GSVSDVPVIGTDLYPTFLELAGGPLPPPQH-------LDGVSLVPLLKGG------------- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 369 evTMSYPMRSVYHqnfrliHnlsfkmpFPIdqdfyvsptfqdllNRTTTGRPTGW-----YKdLHRYYYRERWELYDISR 443
Cdd:cd16144 346 --EADLPRRALFW------H-------FPH--------------YHGQGGRPASAirkgdWK-LIEFYEDGRVELYNLKN 395
|
490 500
....*....|....*....|....*....
gi 31543697 444 DPRETRNLAAD-PDLAQvleMLKAQLVKW 471
Cdd:cd16144 396 DIGETNNLAAEmPEKAA---ELKKKLDAW 421
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-477 |
1.08e-55 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 191.67 E-value: 1.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFES-GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYglhQDVHHFNSF- 101
Cdd:cd16033 2 NILFIMTDQQRYDTlGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVL---NNVENAGAYs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 102 ----DKVQSLPLLLNQAGVRTGIIGKKHVGPETVyPFDFAFtEENSSVMQ------VGRNITRIKQLvqkflqTQDDRPF 171
Cdd:cd16033 79 rglpPGVETFSEDLREAGYRNGYVGKWHVGPEET-PLDYGF-DEYLPVETtieyflADRAIEMLEEL------AADDKPF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 172 FLYVAFHDPHrcghsQPqygtfcekfgngesgmgYIPdwtPQ----IYDPQDVMVP--YFVP--DTPAA----------- 232
Cdd:cd16033 151 FLRVNFWGPH-----DP-----------------YIP---PEpyldMYDPEDIPLPesFADDfeDKPYIyrrerkrwgvd 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 233 -------RADLAAQYTTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNG---------------------IPFPSGrtn 284
Cdd:cd16033 206 tedeedwKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGdalgahrlwdkgpfmyeetyrIPLIIK--- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 285 lyWPGTAEPllvsspehpqrwGQVSDAYVSLLDLTPTILDWFSIPYPSyaifgsktiQLTGRSLLPAL--EAEPLWATVF 362
Cdd:cd16033 283 --WPGVIAA------------GQVVDEFVSLLDLAPTILDLAGVDVPP---------KVDGRSLLPLLrgEQPEDWRDEV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 363 SSQSH-HEVTmsYPMRSVYHQNFRLIHNlsfkmPFPIDqdfyvsptfqdllnrtttgrptgwykdlhryyyrerwELYDI 441
Cdd:cd16033 340 VTEYNgHEFY--LPQRMVRTDRYKYVFN-----GFDID-------------------------------------ELYDL 375
|
490 500 510
....*....|....*....|....*....|....*.
gi 31543697 442 SRDPRETRNLAADPDLAQVLEMLKAQLVKWQWETHD 477
Cdd:cd16033 376 ESDPYELNNLIDDPEYEEILREMRTRLYEWMEETGD 411
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-468 |
9.78e-55 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 187.77 E-value: 9.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFES-GVYNNTAIATPHLDALSRHSLIFRNAF----TSVSSCSPSRASLLTGlpqhqngMYGLH-QDVHH 97
Cdd:cd16155 4 NILFILADDQRADTiGALGNPEIQTPNLDRLARRGTSFTNAYnmggWSGAVCVPSRAMLMTG-------RTLFHaPEGGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 98 FNSFDKVQSLPLLLNQAGVRTGIIGKKHVgpetvypfDFAfteeNSSVmqvgrnitrikqlvqKFL--QTQDDRPFFLYV 175
Cdd:cd16155 77 AAIPSDDKTWPETFKKAGYRTFATGKWHN--------GFA----DAAI---------------EFLeeYKDGDKPFFMYV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 176 AFHDPHrcghsQPQYGT--FCEKFGNGEsgmgyIPDwtPQIYDPQ------------DVMVPYfvPDTPAA-RADLAAQY 240
Cdd:cd16155 130 AFTAPH-----DPRQAPpeYLDMYPPET-----IPL--PENFLPQhpfdngegtvrdEQLAPF--PRTPEAvRQHLAEYY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 241 TTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGIPFPS----GRTNLYWPGTAEPLLVSSPEHPQrwGQVSDAYVSLL 316
Cdd:cd16155 196 AMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGShglmGKQNLYEHSMRVPLIISGPGIPK--GKRRDALVYLQ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 317 DLTPTILDWFSIPYPsyaifgsKTIQltGRSLLPALEAEplwatvfssqshhevtmsypmrsvyhqnfrlihnlsfkmpf 396
Cdd:cd16155 274 DVFPTLCELAGIEIP-------ESVE--GKSLLPVIRGE----------------------------------------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 397 pidqdfyvsptfqdllnrTTTGRPT--GWYKDLHRYYYRERW------------ELYDISRDPRETRNLAADPDLAQVLE 462
Cdd:cd16155 304 ------------------KKAVRDTlyGAYRDGQRAIRDDRWkliiyvpgvkrtQLFDLKKDPDELNNLADEPEYQERLK 365
|
....*.
gi 31543697 463 MLKAQL 468
Cdd:cd16155 366 KLLAEL 371
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
23-328 |
9.02e-54 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 183.01 E-value: 9.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 23 RNVLLIVADDGGFES-GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDvhhfNSF 101
Cdd:pfam00884 1 PNVVLVLGESLRAPDlGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPV----GLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 102 DKVQSLPLLLNQAGVRTGIIGKKHVGP-----ETVYPFDFAFTEENSSVMQVGRNITRI---------KQLVQKFLQ--T 165
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWynnqsPCNLGFDKFFGRNTGSDLYADPPDVPYncsgggvsdEALLDEALEflD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 166 QDDRPFFLYVAFHDPHRCGHSQPQYgtfcekfgngesgmgyipdwtpqiydpqDVMVPYFVPDTPAARADLAAQYTTIGR 245
Cdd:pfam00884 157 NNDKPFFLVLHTLGSHGPPYYPDRY----------------------------PEKYATFKPSSCSEEQLLNSYDNTLLY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 246 MDQGVGLVLQELRGAGVLNDTLIIFTSDNGIPF--------PSGRTNLYWPGTAEPLLVSSPEHPQRwGQVSDAYVSLLD 317
Cdd:pfam00884 209 TDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLgegggylhGGKYDNAPEGGYRVPLLIWSPGGKAK-GQKSEALVSHVD 287
|
330
....*....|.
gi 31543697 318 LTPTILDWFSI 328
Cdd:pfam00884 288 LFPTILDLAGI 298
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
24-471 |
6.47e-49 |
|
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293765 [Multi-domain] Cd Length: 409 Bit Score: 173.50 E-value: 6.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGF-ESGVYNNTAIATPHLDALSRHSLIFRNAFTSvSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSfd 102
Cdd:cd16146 2 NVILILTDDQGYgDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWHTILGRERMRL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 103 KVQSLPLLLNQAGVRTGIIGKKHVGpeTVYP-------FDFAFTEENSSVMQVG-------------RNITRIKQ----- 157
Cdd:cd16146 79 DETTLAEVFKDAGYRTGIFGKWHLG--DNYPyrpqdrgFDEVLGHGGGGIGQYPdywgndyfddtyyHNGKFVKTegyct 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 158 --LVQ---KFLQTQDDRPFFLYVAFHDPHRcghsqpqygtfcekfgngesgmgyipdwtpqiydpqdvmvPYFVPDTPAA 232
Cdd:cd16146 157 dvFFDeaiDFIEENKDKPFFAYLATNAPHG----------------------------------------PLQVPDKYLD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 233 R-------ADLAAQYTTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGipfPSGRTNLYWP-------------GTAE 292
Cdd:cd16146 197 PykdmgldDKLAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNG---PAGGVPKRFNagmrgkkgsvyegGHRV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 293 PLLVSSPEHPQRwGQVSDAYVSLLDLTPTILDWFSIPYPsyaifgsKTIQLTGRSLLPALEAE--PLWATVFSSQSHHEV 370
Cdd:cd16146 274 PFFIRWPGKILA-GKDVDTLTAHIDLLPTLLDLCGVKLP-------EGIKLDGRSLLPLLKGEsdPWPERTLFTHSGRWP 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 371 TMSYPMR--SVYHQNFRLIHNlsfkmpfpidqdfyvsptfqdllnrtttgrptgwykdlhryyYRERWELYDISRDPRET 448
Cdd:cd16146 346 PPPKKKRnaAVRTGRWRLVSP------------------------------------------KGFQPELYDIENDPGEE 383
|
490 500
....*....|....*....|....
gi 31543697 449 RNLAAD-PDLAQVlemLKAQLVKW 471
Cdd:cd16146 384 NDVADEhPEVVKR---LKAAYEAW 404
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
24-452 |
1.79e-45 |
|
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: 163.89 E-value: 1.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFES-GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTG-LPQ---------HQNGMYGLH 92
Cdd:cd16026 3 NIVVILADDLGYGDlGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGrYPVrvglpgvvgPPGSKGGLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 93 QDvhhfnsfdkVQSLPLLLNQAGVRTGIIGKKHVG--PETvYP----FD-----------FAFTEENSSVMQVGRNITRI 155
Cdd:cd16026 83 PD---------EITIAEVLKKAGYRTALVGKWHLGhqPEF-LPtrhgFDeyfgipysndmWPFPLYRNDPPGPLPPLMEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 156 KQLVQ-----------------KFLQTQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgyipdwtpqiydpq 218
Cdd:cd16026 153 EEVIEqpadqssltqrytdeavDFIERNKDQPFFLYLAHTMPH------------------------------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 219 dvmVPYFVPDTPAARADLAAQYTTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGiPFPSGRTN-------------- 284
Cdd:cd16026 196 ---VPLFASEKFKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNG-PWLEYGGHggsagplrggkgtt 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 285 ----------LYWPGTAEPllvsspehpqrwGQVSDAYVSLLDLTPTILDWFSIPYPSYAIfgsktiqLTGRSLLPALEA 354
Cdd:cd16026 272 weggvrvpfiAWWPGVIPA------------GTVSDELASTMDLLPTLAALAGAPLPEDRV-------IDGKDISPLLLG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 355 EplwatvfsSQSHHEvTMSYpmrsvYHQNFRL--IHNLSFKMPFPidqDFYVSPTFQDLLNRTTTGRPtgwykdlhryyy 432
Cdd:cd16026 333 G--------SKSPPH-PFFY-----YYDGGDLqaVRSGRWKLHLP---TTYRTGTDPGGLDPTKLEPP------------ 383
|
490 500
....*....|....*....|
gi 31543697 433 rerwELYDISRDPRETRNLA 452
Cdd:cd16026 384 ----LLYDLEEDPGETYNVA 399
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-477 |
8.87e-45 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 162.40 E-value: 8.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 23 RNVLLIVADDGGFES-GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGmyglHQDVHHFNSF 101
Cdd:cd16150 1 PNIVIFVADQLRADSlGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG----HRTLHHLLRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 102 DKvqslPLL---LNQAGVRTGIIGKKHVGPETVYPFDFAFTEENssvmqvgrnitRIKQLVQKFLQTQDDRPFFLYVAFH 178
Cdd:cd16150 77 DE----PNLlktLKDAGYHVAWAGKNDDLPGEFAAEAYCDSDEA-----------CVRTAIDWLRNRRPDKPFCLYLPLI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 179 DPHrcghsqPQYGtfCEK--------------FGNGESGMGYiPDWTPQIYDPQDVMVpyfvpdTPAARADLAAQY-TTI 243
Cdd:cd16150 142 FPH------PPYG--VEEpwfsmidreklpprRPPGLRAKGK-PSMLEGIEKQGLDRW------SEERWRELRATYlGMV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 244 GRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGipfpsGRTNLY-----WPGTAE------PLLVSSPEHPQrwGQVSDAY 312
Cdd:cd16150 207 SRLDHQFGRLLEALKETGLYDDTAVFFFSDHG-----DYTGDYglvekWPNTFEdcltrvPLIIKPPGGPA--GGVSDAL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 313 VSLLDLTPTILDWFSIPyPSYAIFgsktiqltGRSLLPALEAEP--LWATVFSS--QSHHEvtmsYPMRSVYHQNFrlih 388
Cdd:cd16150 280 VELVDIPPTLLDLAGIP-LSHTHF--------GRSLLPVLAGETeeHRDAVFSEggRLHGE----EQAMEGGHGPY---- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 389 nlSFKMPFPIDQdfyvspTFQDLLNRTTTGRpTGWYKdlhrYYYR--ERWELYDISRDPRETRNLAADPDLAQVLEMLKA 466
Cdd:cd16150 343 --DLKWPRLLQQ------EEPPEHTKAVMIR-TRRYK----YVYRlyEPDELYDLEADPLELHNLIGDPAYAEIIAEMKQ 409
|
490
....*....|.
gi 31543697 467 QLVKWQWETHD 477
Cdd:cd16150 410 RLLRWMVETSD 420
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-392 |
6.48e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 157.32 E-value: 6.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 23 RNVLLIVADD-GGFESGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlhqdvhhfNS- 100
Cdd:cd16037 1 PNILIIMSDEhNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWD--------NAd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 101 --FDKVQSLPLLLNQAGVRTGIIGKKHVGPETVYPFdFAFTeenssvmqvgRNITrikQLVQKFLQTQ--DDRPFFLYVA 176
Cdd:cd16037 73 pyDGDVPSWGHALRAAGYETVLIGKLHFRGEDQRHG-FRYD----------RDVT---EAAVDWLREEaaDDKPWFLFVG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 177 FHDPHrcghsQPqygtfcekfgngesgmgYIPDwtPQIYDpqdvmvpYFVpdtpaaRADLAAQYTTIGRMDQGVGLVLQE 256
Cdd:cd16037 139 FVAPH-----FP-----------------LIAP--QEFYD-------LYV------RRARAAYYGLVEFLDENIGRVLDA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 257 LRGAGVLNDTLIIFTSDNGIPFPS----GRTNLYWPGTAEPLLVSSPEHPQrwGQVSDAYVSLLDLTPTILDWFSIPYPS 332
Cdd:cd16037 182 LEELGLLDNTLIIYTSDHGDMLGErglwGKSTMYEESVRVPMIISGPGIPA--GKRVKTPVSLVDLAPTILEAAGAPPPP 259
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543697 333 YaifgsktiqLTGRSLLPALEAEPLWA-TVFSSQSHHEVTMsyPMRSVYHQNFRLIHNLSF 392
Cdd:cd16037 260 D---------LDGRSLLPLAEGPDDPDrVVFSEYHAHGSPS--GAFMLRKGRWKYIYYVGY 309
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-454 |
8.16e-42 |
|
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: 154.29 E-value: 8.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADD-GGFESGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFD 102
Cdd:cd16145 2 NIIFILADDlGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 103 KVQSLPLLLNQAGVRTGIIGKKHVGPETV--YP----FDFAFT------------------------EENSSVMQVGRNI 152
Cdd:cd16145 82 DDVTLAEVLKKAGYATAAFGKWGLGGPGTpgHPtkqgFDYFYGyldqvhahnyypeylwrngekvplPNNVIPPLDEGNN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 153 TRIKQ------LVQ----KFLQTQDDRPFFLYVAFHDPHrcGHSQpqygtfcekfGNGESGMGYIPDWTPqiydpqdvmv 222
Cdd:cd16145 162 AGGGGgtyshdLFTdealDFIRENKDKPFFLYLAYTLPH--APLQ----------VPDDGPYKYKPKDPG---------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 223 PYFVPDTPAARADLAAQyttIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGI-----------------PFPSGRTNL 285
Cdd:cd16145 220 IYAYLPWPQPEKAYAAM---VTRLDRDVGRILALLKELGIDENTLVVFTSDNGPhseggsehdpdffdsngPLRGYKRSL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 286 YWPGTAEPLLVSSPEH-PQrwGQVSDAYVSLLDLTPTILDWFSIPYPSyaifgsktiQLTGRSLLPALEAEPLwatvfsS 364
Cdd:cd16145 297 YEGGIRVPFIARWPGKiPA--GSVSDHPSAFWDFMPTLADLAGAEPPE---------DIDGISLLPTLLGKPQ------Q 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 365 QSHhevtmsypmRSVYHQNFRLIHNLSFKMpfpidqdfyvsptfqdllnrtttgrptGWYKDLHRYYYRERWELYDISRD 444
Cdd:cd16145 360 QQH---------DYLYWEFYEGGGAQAVRM---------------------------GGWKAVRHGKKDGPFELYDLSTD 403
|
490
....*....|
gi 31543697 445 PRETRNLAAD 454
Cdd:cd16145 404 PGETNNLAAQ 413
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
24-456 |
1.73e-41 |
|
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: 153.88 E-value: 1.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFESGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSFDK 103
Cdd:cd16030 4 NVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNS--YFRKVAPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 104 VQSLPLLLNQAGVRTGIIGK---KHVGPE-------TVYPFDFAFTEENSSVMQVGRNITR------------------- 154
Cdd:cd16030 82 AVTLPQYFKENGYTTAGVGKifhPGIPDGdddpaswDEPPNPPGPEKYPPGKLCPGKKGGKgggggpaweaadvpdeayp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 155 --------IKQLVQKFlqtQDDRPFFLYVAFHDPHRcghsqPQYgtFCEKF------GNGESGMGYIP---------DWT 211
Cdd:cd16030 162 dgkvadeaIEQLRKLK---DSDKPFFLAVGFYKPHL-----PFV--APKKYfdlyplESIPLPNPFDPidlpevawnDLD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 212 --PQIYDPQDVMVPYFVPDTPAARADLAAQ--YTTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGipFPSG------ 281
Cdd:cd16030 232 dlPKYGDIPALNPGDPKGPLPDEQARELRQayYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHG--WHLGehghwg 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 282 -RTNlyWPGTAE-PLLVSSPEHPQRwGQVSDAYVSLLDLTPTILDWFSIPYPSYaifgsktiqLTGRSLLPALE-AEPLW 358
Cdd:cd16030 310 kHTL--FEEATRvPLIIRAPGVTKP-GKVTDALVELVDIYPTLAELAGLPAPPC---------LEGKSLVPLLKnPSAKW 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 359 ATVFSSQSHHEVTMSYPMRSvyhQNFRLIHnlsfkmpfpidqdfyvsptfqdllnrtttgrptgwYKDLHRYYYRerwEL 438
Cdd:cd16030 378 KDAAFSQYPRPSIMGYSIRT---ERYRYTE-----------------------------------WVDFDKVGAE---EL 416
|
490
....*....|....*...
gi 31543697 439 YDISRDPRETRNLAADPD 456
Cdd:cd16030 417 YDHKNDPNEWKNLANDPE 434
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
23-478 |
1.70e-39 |
|
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: 148.56 E-value: 1.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 23 RNVLLIVADDGGFE-SGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMY--GLHQDVHHFN 99
Cdd:cd16028 1 RNVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVwnGTPLDARHLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 100 sfdkvqsLPLLLNQAGVRTGIIGKKHVG--PETVYPFDFAFTeENSSVMQ---VGRNITRIKQ-------LVQK---FLQ 164
Cdd:cd16028 81 -------LALELRKAGYDPALFGYTDTSpdPRGLAPLDPRLL-SYELAMPgfdPVDRLDEYPAedsdtafLTDRaieYLD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 165 TQDDRPFFLYVAFHDPH----------------------RCGHSQ------PQYGTFCEKFGNGESGMGYIPDWTpqiyd 216
Cdd:cd16028 153 ERQDEPWFLHLSYIRPHppfvapapyhalydpadvpppiRAESLAaeaaqhPLLAAFLERIESLSFSPGAANAAD----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 217 pqdvmvpyfvpDTPAARADLAAQYT-TIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGIPFP---SGRTNLYWPGTAE 292
Cdd:cd16028 228 -----------LDDEEVAQMRATYLgLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGdhwLWGKDGFFDQAYR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 293 -PLLVSSPEHPQR--WGQVSDAYVSLLDLTPTILDWFSIPYPSyaifgsktiQLTGRSLLPALEAE--PLWATvfssqsh 367
Cdd:cd16028 297 vPLIVRDPRREADatRGQVVDAFTESVDVMPTILDWLGGEIPH---------QCDGRSLLPLLAGAqpSDWRD------- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 368 hEVTMSYPMRSVYHQNFRL-----IHNLSFKMPFpiDQDF-YVspTFQDLlnrtttgRPTgwykdlhryyyrerweLYDI 441
Cdd:cd16028 361 -AVHYEYDFRDVSTRRPQEalglsPDECSLAVIR--DERWkYV--HFAAL-------PPL----------------LFDL 412
|
490 500 510
....*....|....*....|....*....|....*..
gi 31543697 442 SRDPRETRNLAADPDLAQVLEMLKAQLVKWQWETHDP 478
Cdd:cd16028 413 KNDPGELRDLAADPAYAAVVLRYAQKLLSWRMRHADR 449
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-474 |
2.78e-38 |
|
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: 143.52 E-value: 2.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFES-GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMY----GLHQDVHHf 98
Cdd:cd16152 3 NVIVFFTDQQRWDTlGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFrngiPLPADEKT- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 99 nsfdkvqsLPLLLNQAGVRTGIIGKKHVGpetVYPFDfAFTeenssvmqvgrnitrikQLVQKFLQT-QDDRPFFLYVAF 177
Cdd:cd16152 82 --------LAHYFRDAGYETGYVGKWHLA---GYRVD-ALT-----------------DFAIDYLDNrQKDKPFFLFLSY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 178 HDPHrcgHsQPQYGTF------CEKFGNgesgmgyipdwtpqiydpqdvmvpYFVPDTPAAR-----ADLAAQYTTIGRM 246
Cdd:cd16152 133 LEPH---H-QNDRDRYvapegsAERFAN------------------------FWVPPDLAALpgdwaEELPDYLGCCERL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 247 DQGVGLVLQELRGAGVLNDTLIIFTSDNGIPFPSgRTNLYWPGTAE-----PLLVSSPehPQRWGQVSDAYVSLLDLTPT 321
Cdd:cd16152 185 DENVGRIRDALKELGLYDNTIIVFTSDHGCHFRT-RNAEYKRSCHEssirvPLVIYGP--GFNGGGRVEELVSLIDLPPT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 322 ILDWFSIPYPSYAIfgsktiqltGRSLLPALEAEPL-WAT-VFSSQSHHEVTmsypmrsvyhqnfRLIHNLSFKmpfpid 399
Cdd:cd16152 262 LLDAAGIDVPEEMQ---------GRSLLPLVDGKVEdWRNeVFIQISESQVG-------------RAIRTDRWK------ 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543697 400 qdfYV--SPTfqdllnrtttgrpTGWYKDLHRYYYRERWeLYDISRDPRETRNLAADPDLAQVLEMLKAQLVKWQWE 474
Cdd:cd16152 314 ---YSvaAPD-------------KDGWKDSGSDVYVEDY-LYDLEADPYELVNLIGRPEYREVAAELRERLLARMAE 373
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-393 |
1.75e-36 |
|
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: 138.89 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFES-GVYNNTAIATPHLDALSRHSLIFRNAFTSvSSCSPSRASLLTGLPQHQNGmyglhqdVHHFNSFD 102
Cdd:cd16151 2 NIILIMADDLGYECiGCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNY-------VVFGYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 103 KVQSLPLLLNQAGVRTGIIGKKHVGPETV---YPFDFAFTEenSSVMQV-------GRNITRIkQLVQK----------- 161
Cdd:cd16151 74 KQKTFGHLLKDAGYATAIAGKWQLGGGRGdgdYPHEFGFDE--YCLWQLtetgekySRPATPT-FNIRNgkllettegdy 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 162 -----------FLQTQDDRPFFLY---VAFHDPHRCG-HSQPQYGTFCEKFGNgesgMGYIPDwtpqiydpqdvMVPYfv 226
Cdd:cd16151 151 gpdlfadflidFIERNKDQPFFAYypmVLVHDPFVPTpDSPDWDPDDKRKKDD----PEYFPD-----------MVAY-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 227 pdtpaaradlaaqyttigrMDQGVGLVLQELRGAGVLNDTLIIFTSDNGIPFP-SGRTN----------LYWPGTAEPLL 295
Cdd:cd16151 214 -------------------MDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPiTSRTNgrevrggkgkTTDAGTHVPLI 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 296 VSSPEHPQRwGQVSDAYVSLLDLTPTILDWFSIPYPsyaifgsKTIQLTGRSLLPALEAEPlwatvfsSQSHHEVTMSYP 375
Cdd:cd16151 275 VNWPGLIPA-GGVSDDLVDFSDFLPTLAELAGAPLP-------EDYPLDGRSFAPQLLGKT-------GSPRREWIYWYY 339
|
410
....*....|....*...
gi 31543697 376 MRSVYHQNFRLIHNLSFK 393
Cdd:cd16151 340 RNPHKKFGSRFVRTKRYK 357
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-451 |
2.44e-36 |
|
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: 138.86 E-value: 2.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFES-GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYG----LHQDVHhf 98
Cdd:cd16034 3 NILFIFADQHRAQAlGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGndvpLPPDAP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 99 nSFDKVqslpllLNQAGVRTGIIGKKHV-GPETVYP--------------FDF------------AFTEENSSVMQVGRN 151
Cdd:cd16034 81 -TIADV------LKDAGYRTGYIGKWHLdGPERNDGraddytppperrhgFDYwkgyecnhdhnnPHYYDDDGKRIYIKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 152 ITRIKQ--LVQKFL--QTQDDRPFFLYVAFHDPHrcghsqPQYGTFCEKFGNgesgmgyipdwtpqIYDPQDVMVPYFVP 227
Cdd:cd16034 154 YSPDAEtdLAIEYLenQADKDKPFALVLSWNPPH------DPYTTAPEEYLD--------------MYDPKKLLLRPNVP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 228 DTPAARADLAAQ----YTTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGIPFPS-GRT--NLYWPGTAE-PLLVSSP 299
Cdd:cd16034 214 EDKKEEAGLREDlrgyYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGShGLMnkQVPYEESIRvPFIIRYP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 300 EHpQRWGQVSDAYVSLLDLTPTILDWFSIPYPSyaifgskTIQltGRSLLPALEAEplwatvfSSQSHHEVTMSYpmrsv 379
Cdd:cd16034 294 GK-IKAGRVVDLLINTVDIMPTLLGLCGLPIPD-------TVE--GRDLSPLLLGG-------KDDEPDSVLLQC----- 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543697 380 yhqnfrlihnlsfkmPFPIDQDFYvsptfqdllnrtttgRPTGWYKDL--HRYYY----RERWELYDISRDPRETRNL 451
Cdd:cd16034 352 ---------------FVPFGGGSA---------------RDGGEWRGVrtDRYTYvrdkNGPWLLFDNEKDPYQLNNL 399
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-350 |
1.79e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 133.06 E-value: 1.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADdggfeS------GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLpqhqngmYGLHQDVHH 97
Cdd:cd16148 2 NVILIVID-----SlradhlGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGL-------YPFYHGVWG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 98 FNSFDKVQSLPLLLNQAGVRTGIIGkKHVGPETVYPFDFAFTEENSSVMQVGRNIT-------RIKQLVQKFLQTQ-DDR 169
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAVS-SNPHLFGGPGFDRGFDTFEDFRGQEGDPGEegderaeRVTDRALEWLDRNaDDD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 170 PFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgyipdwTPQIYDpqdvmvpyfvpdtpaaradlaaqyTTIGRMDQG 249
Cdd:cd16148 149 PFFLFLHYFDPH-----------------------------EPYLYD------------------------AEVRYVDEQ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 250 VGLVLQELRGAGVLNDTLIIFTSDNGIPF------PSGRTNLYWPGTAEPLLVSSPEHPQrwGQVSDAYVSLLDLTPTIL 323
Cdd:cd16148 176 IGRLLDKLKELGLLEDTLVIVTSDHGEEFgehglyWGHGSNLYDEQLHVPLIIRWPGKEP--GKRVDALVSHIDIAPTLL 253
|
330 340
....*....|....*....|....*..
gi 31543697 324 DWFSIPYPSYaifgsktiqLTGRSLLP 350
Cdd:cd16148 254 DLLGVEPPDY---------SDGRSLLP 271
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
23-483 |
2.24e-35 |
|
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: 137.51 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 23 RNVLLIVADDGGFES-GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlhqdvhhfNSF 101
Cdd:cd16156 1 KQFIFIMTDTQRWDMvGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWT--------NCM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 102 ---DKVQSLPLLLNQAGVRTGIIGKKHV-------------GPETVYPFDFA-----FTEENSSVMQVGRNIT------- 153
Cdd:cd16156 73 algDNVKTIGQRLSDNGIHTAYIGKWHLdggdyfgngicpqGWDPDYWYDMRnyldeLTEEERRKSRRGLTSLeaegike 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 154 ------RIKQLVQKFLQTQDDRPFFLYVAFHDPHRCGHSQPQYGTFCEKF---------GNGESGMGYIPDWTPQIY--- 215
Cdd:cd16156 153 eftyghRCTNRALDFIEKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFefpkgenayDDLENKPLHQRLWAGAKPhed 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 216 -DPQDVMVPYFVpdtpaARADLAaqyttigrmDQGVGLVLQELRgaGVLNDTLIIFTSDNGIPFpsGRTNLYWPGTAE-- 292
Cdd:cd16156 233 gDKGTIKHPLYF-----GCNSFV---------DYEIGRVLDAAD--EIAEDAWVIYTSDHGDML--GAHKLWAKGPAVyd 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 293 -----PLLVSSPEHPQRWGQVsDAYVSLLDLTPTILDWFSIPYPSyaifgsktiQLTGRSLLPALEAE--PLWATVFSSQ 365
Cdd:cd16156 295 eitniPLIIRGKGGEKAGTVT-DTPVSHIDLAPTILDYAGIPQPK---------VLEGESILATIEDPeiPENRGVFVEF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 366 SHHEVTMS-----YPMRSVYHQNFRLIHNLsfkmpfpIDQDfyvsptfqdllnrtttgrptgwykdlhryyyrerwELYD 440
Cdd:cd16156 365 GRYEVDHDgfggfQPVRCVVDGRYKLVINL-------LSTD-----------------------------------ELYD 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 31543697 441 ISRDPRETRNLAADPDLAQVLEMLKAQLVKWQWETHDP-----WVCAP 483
Cdd:cd16156 403 LEKDPYEMHNLIDDPDYADVRDQLHDELLDYMNETRDPfrgyyWECRP 450
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
24-470 |
2.35e-35 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 137.88 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFES-GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlHQDVhhfNSFD 102
Cdd:PRK13759 8 NIILIMVDQMRGDClGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVG-YGDV---VPWN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 103 KVQSLPLLLNQAGVRTGIIGKKHVGPETV--------------------YPFDFAFTEENSSVMQ---VGRNIT------ 153
Cdd:PRK13759 84 YKNTLPQEFRDAGYYTQCIGKMHVFPQRNllgfhnvllhdgylhsgrneDKSQFDFVSDYLAWLRekaPGKDPDltdigw 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 154 -------RIKQLVQK-------------FLQTQD-DRPFFLYVAFHDPHRcGHSQPQYgtFCEKFGNGESGMGYIPDWT- 211
Cdd:PRK13759 164 dcnswvaRPWDLEERlhptnwvgsesieFLRRRDpTKPFFLKMSFARPHS-PYDPPKR--YFDMYKDADIPDPHIGDWEy 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 212 -----PQIYDPQdvmVPY-FVPDTPAARAdLAAQYTTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNG---------- 275
Cdd:PRK13759 241 aedqdPEGGSID---ALRgNLGEEYARRA-RAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGdmlgdhylfr 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 276 ----------IPFPsgrtnLYWPGTAepllvsspEHPQRwGQVSDAYVSLLDLTPTILDWFSIPYPSyaifgsktiQLTG 345
Cdd:PRK13759 317 kgypyegsahIPFI-----IYDPGGL--------LAGNR-GTVIDQVVELRDIMPTLLDLAGGTIPD---------DVDG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 346 RSLLPALEA-EPLWATVFssqsHHEVTMSYpmrsvyhqnfrlihnlsfkmpfpiDQDFYVsptfqdllnrtTTGRptgwy 424
Cdd:PRK13759 374 RSLKNLIFGqYEGWRPYL----HGEHALGY------------------------SSDNYL-----------TDGK----- 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 31543697 425 kdlHRY---YYRERWELYDISRDPRETRNLAADPDLAQVLEMLKAQLVK 470
Cdd:PRK13759 410 ---WKYiwfSQTGEEQLFDLKKDPHELHNLSPSEKYQPRLREMRKKLVD 455
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
24-455 |
7.18e-35 |
|
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: 134.60 E-value: 7.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDggfESGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDvhhFNSFDK 103
Cdd:cd16147 3 NIVLILTDD---QDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPP---GGGYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 104 VQS-------LPLLLNQAGVRTGIIGK------KHVGPETVYP-FD-FAFTEENSS----VMQVGRNITR---------- 154
Cdd:cd16147 77 FWQnglerstLPVWLQEAGYRTAYAGKylngygVPGGVSYVPPgWDeWDGLVGNSTyynyTLSNGGNGKHgvsypgdylt 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 155 --IKQLVQKFLQT--QDDRPFFLYVAFHDPHRCGHSQPQYGtfcekfgNGESGMGYIPDWTPQIYDPQDVmvPYFVPDTP 230
Cdd:cd16147 157 dvIANKALDFLRRaaADDKPFFLVVAPPAPHGPFTPAPRYA-------NLFPNVTAPPRPPPNNPDVSDK--PHWLRRLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 231 AARADLAAQYTTIGR--------MDQGVGLVLQELRGAGVLNDTLIIFTSDNGipF-------PSGRTNLYWPGTAEPLL 295
Cdd:cd16147 228 PLNPTQIAYIDELYRkrlrtlqsVDDLVERLVNTLEATGQLDNTYIIYTSDNG--YhlgqhrlPPGKRTPYEEDIRVPLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 296 VSSPEHPQrwGQVSDAYVSLLDLTPTILDWFSIPYPSYaifgsktiqLTGRSLLPAleaeplwatvfssqshhevtmsyp 375
Cdd:cd16147 306 VRGPGIPA--GVTVDQLVSNIDLAPTILDLAGAPPPSD---------MDGRSCGDS------------------------ 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 376 mrsvyhqnfrlihnlsfkmpfpidqdfyVSPTFQDLlnRTTTGRPTGWYkdlHRYYYRERwELYDISRDPRETRNLAADP 455
Cdd:cd16147 351 ----------------------------NNNTYKCV--RTVDDTYNLLY---FEWCTGFR-ELYDLTTDPYQLTNLAGDL 396
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-452 |
1.02e-34 |
|
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: 134.25 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGF-ESGVYN-NTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTG-------LPQHQNGMYGLHQd 94
Cdd:cd16143 2 NIVIILADDLGYgDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGrypwrsrLKGGVLGGFSPPL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 95 vhhfnsFDKVQ-SLPLLLNQAGVRTGIIGKKHVG-------PETVYP--------------------FDFAFTEENSSVM 146
Cdd:cd16143 81 ------IEPDRvTLAKMLKQAGYRTAMVGKWHLGldwkkkdGKKAATgtgkdvdyskpikggpldhgFDYYFGIPASEVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 147 Q--VGRNITRIKQlvqkflQTQDDRPFFLYVAFHDPHrcGHSQPqygtfCEKFgNGESGMGyipdwtpqiydpqdvmvpy 224
Cdd:cd16143 155 PtlTDKAVEFIDQ------HAKKDKPFFLYFALPAPH--TPIVP-----SPEF-QGKSGAG------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 225 fvpdtpaARADLAAQyttigrMDQGVGLVLQELRGAGVLNDTLIIFTSDNG-IPFPSGRTNL---YWP------------ 288
Cdd:cd16143 202 -------PYGDFVYE------LDWVVGRILDALKELGLAENTLVIFTSDNGpSPYADYKELEkfgHDPsgplrgmkadiy 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 289 --GTAEPLLVSSPEH-PQrwGQVSDAYVSLLDLTPTILDWFSIPYPsyaifgsKTIQLTGRSLLPALEAEPLwATVFSSQ 365
Cdd:cd16143 269 egGHRVPFIVRWPGKiPA--GSVSDQLVSLTDLFATLAAIVGQKLP-------DNAAEDSFSFLPALLGPKK-QEVRESL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 366 SHHEVTMSYPMRsvyHQNFRLI-HNLSFKMPFPIDQDFYVSPTFQdllnrtttgrptgwykdlhryyyrerweLYDISRD 444
Cdd:cd16143 339 VHHSGNGSFAIR---KGDWKLIdGTGSGGFSYPRGKEKLGLPPGQ----------------------------LYNLSTD 387
|
....*...
gi 31543697 445 PRETRNLA 452
Cdd:cd16143 388 PGESNNLY 395
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-350 |
3.79e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 129.28 E-value: 3.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFES-GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGM-----YGLHQDVHH 97
Cdd:cd16149 2 NILFILTDDQGPWAlGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 98 FNSFDKVQ-SLPLLLNQAGVRTGIIGKKHVGPETVypfdfAFTEENSSvmqvgrnitrikqlvqkflqtqDDRPFFLYVA 176
Cdd:cd16149 82 PEGYLEGQtTLPEVLQDAGYRCGLSGKWHLGDDAA-----DFLRRRAE----------------------AEKPFFLSVN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 177 FHDPhrcgHSQPQYgtfcekfgngesgmgyipdwtpqiydpqdvmvpyfvpdtpaaradlaaqYTTIGRMDQGVGLVLQE 256
Cdd:cd16149 135 YTAP----HSPWGY-------------------------------------------------FAAVTGVDRNVGRLLDE 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 257 LRGAGVLNDTLIIFTSDNGipFPSG------------RTNLY-----------WPGTAEPllvsspehpqrwGQVSDAYV 313
Cdd:cd16149 162 LEELGLTENTLVIFTSDNG--FNMGhhgiwgkgngtfPLNMYdnsvkvpfiirWPGVVPA------------GRVVDSLV 227
|
330 340 350
....*....|....*....|....*....|....*..
gi 31543697 314 SLLDLTPTILDWFSIPYPSyaifgskTIQLTGRSLLP 350
Cdd:cd16149 228 SAYDFFPTLLELAGVDPPA-------DPRLPGRSFAD 257
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
24-388 |
2.60e-33 |
|
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: 128.85 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADD-GGFESGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYG----LHQDV--- 95
Cdd:cd16032 2 NILLIMADQlTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDnaaeFPADIptf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 96 -HHfnsfdkvqslpllLNQAGVRTGIIGKKH-VGPETVYPFDfaFTEEnssVMQVGRNitRIKQLVQKflqtQDDRPFFL 173
Cdd:cd16032 82 aHY-------------LRAAGYRTALSGKMHfVGPDQLHGFD--YDEE---VAFKAVQ--KLYDLARG----EDGRPFFL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 174 YVAFHDPHrcghsqpqygtfcekfgngesgmgyipdwtpqiyDPQDVMVPYFVPDTPAARadlAAQYTTIGRMDQGVGLV 253
Cdd:cd16032 138 TVSFTHPH----------------------------------DPYVIPQEYWDLYVRRAR---RAYYGMVSYVDDKVGQL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 254 LQELRGAGVLNDTLIIFTSDN-------GIPFpsgRTNLYWPGTAEPLLVSSPEHPQRwGQVSDAyVSLLDLTPTILDWF 326
Cdd:cd16032 181 LDTLERTGLADDTIVIFTSDHgdmlgerGLWY---KMSFFEGSARVPLIISAPGRFAP-RRVAEP-VSLVDLLPTLVDLA 255
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31543697 327 SIPYPSYAifgsktIQLTGRSLLPALE-AEPLWATVFSSQSHHEVTMSyPMRSVYHQNFRLIH 388
Cdd:cd16032 256 GGGTAPHV------PPLDGRSLLPLLEgGDSGGEDEVISEYLAEGAVA-PCVMIRRGRWKFIY 311
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
24-352 |
4.06e-30 |
|
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: 122.58 E-value: 4.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGF-ESGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSF- 101
Cdd:cd16157 3 NIILMLMDDMGWgDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNA--HARNAYt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 102 ---------DKVQSLPLLLNQAGVRTGIIGKKHVGPETVY-P----FDFAFTEENSSV-----------------MQVGR 150
Cdd:cd16157 81 pqnivggipDSEILLPELLKKAGYRNKIVGKWHLGHRPQYhPlkhgFDEWFGAPNCHFgpydnkaypnipvyrdwEMIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 151 --------------NITRI-KQLVQKFLQTQ--DDRPFFLYVAFHDPHrcghsQPQYGTfcEKFGnGESGMGYIPDwtpq 213
Cdd:cd16157 161 yyeefkidkktgesNLTQIyLQEALEFIEKQhdAQKPFFLYWAPDATH-----APVYAS--KPFL-GTSQRGLYGD---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 214 iydpqdvmvpyfvpdtpaaradlaaqytTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGI-------------PFPS 280
Cdd:cd16157 229 ----------------------------AVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAalisapeqggsngPFLC 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543697 281 GRTNLYWPGTAEPLLVSSPEHpQRWGQVSDAYVSLLDLTPTILDWFSIPYPSyaifgskTIQLTGRSLLPAL 352
Cdd:cd16157 281 GKQTTFEGGMREPAIAWWPGH-IKPGQVSHQLGSLMDLFTTSLALAGLPIPS-------DRAIDGIDLLPVL 344
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
24-325 |
4.15e-29 |
|
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: 118.42 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGF-ESGVYNNTAIATPHLDALSRHSLIFRNAFTSvSSCSPSRASLLTGLPQHQNGMYG--LHQDVHHFNS 100
Cdd:cd16029 2 HIVFILADDLGWnDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHgvILAGEPYGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 101 FDKVQsLPLLLNQAGVRTGIIGKKHVG--------------------------------PETVYPFDFAFTEENSSVMQV 148
Cdd:cd16029 81 LNETL-LPQYLKELGYATHLVGKWHLGfytweytptnrgfdsfygyyggaedyythtsgGANDYGNDDLRDNEEPAWDYN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 149 GRNITRI-KQLVQKFLQTQD-DRPFFLYVAFHDPHrcghsqpqygtfcekfgngeSGMGYIPDWTPQIYDPqdvmvpyFV 226
Cdd:cd16029 160 GTYSTDLfTDRAVDIIENHDpSKPLFLYLAFQAVH--------------------APLQVPPEYADPYEDK-------FA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 227 PDTPAARADLAAqytTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGIPFPSGRT--N---------LYWPGTAEPLL 295
Cdd:cd16029 213 HIKDEDRRTYAA---MVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGgsNyplrggkntLWEGGVRVPAF 289
|
330 340 350
....*....|....*....|....*....|
gi 31543697 296 VSSPEHPQRWGQVSDAYVSLLDLTPTILDW 325
Cdd:cd16029 290 VWSPLLPPKRGTVSDGLMHVTDWLPTLLSL 319
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
24-347 |
2.62e-28 |
|
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: 116.03 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFESGVYNN--TAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTglpqhqnGMYGLHQDVHHFNSF 101
Cdd:cd16161 3 NFLLLFADDLGWGDLGANWapNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMT-------GRLGLRNGVGHNFLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 102 DKVQSLPL-------LLNQAGVRTGIIGKKHVGPETVY-P----FDFAFT---EENSSVMQvgrnitRIKQLVQKFLQ-- 164
Cdd:cd16161 76 TSVGGLPLnettlaeVLRQAGYATGMIGKWHLGQREAYlPnsrgFDYYFGipfSHDSSLAD------RYAQFATDFIQra 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 165 TQDDRPFFLYVAFHDPHRcghSQPQYGTFCekfgNGESGMGYIPDwtpqiydpqdvmvpyfvpdtpaaradlaaqytTIG 244
Cdd:cd16161 150 SAKDRPFFLYAALAHVHV---PLANLPRFQ----SPTSGRGPYGD--------------------------------ALQ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 245 RMDQGVGLVLQELRGAGVLNDTLIIFTSDNG--------IPFPSG---RTNLYWP---------GTAEPLLVSSPEHPQR 304
Cdd:cd16161 191 EMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcelAVGPGTgdwQGNLGGSvakastwegGHREPAIVYWPGRIPA 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 31543697 305 wGQVSDAYVSLLDLTPTILDWFSIPYPSYAIFGSKTIQ--LTGRS 347
Cdd:cd16161 271 -NSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSpvLFGGS 314
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-325 |
3.91e-26 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 109.55 E-value: 3.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGF-ESGVYNNTAI---ATPHLDALSRHSLIFRNaFTSVSSCSPSRASLLTG---------LPQHQNGMYG 90
Cdd:cd16142 2 NILVILGDDIGWgDLGCYGGGIGrgaPTPNIDRLAKEGLRFTS-FYVEPSCTPGRAAFITGrhpirtgltTVGLPGSPGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 91 LHQDVHhfnsfdkvqSLPLLLNQAGVRTGIIGKKHVG--PE---TVYPFD--FAFTEENSSVMQVGRNITRIKQlvqkfl 163
Cdd:cd16142 81 LPPWEP---------TLAELLKDAGYATAQFGKWHLGdeDGrlpTDHGFDefYGNLYHTIDEEIVDKAIDFIKR------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 164 QTQDDRPFFLYVAFHDPHRCGHSQPQYgtfcekfgngesgMGYIPDWTPQiydpQDVMVpyfvpdtpaaradlaaqytti 243
Cdd:cd16142 146 NAKADKPFFLYVNFTKMHFPTLPSPEF-------------EGKSSGKGKY----ADSMV--------------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 244 gRMDQGVGLVLQELRGAGVLNDTLIIFTSDNG---IPFP-SGRTNL------------------YWPGTAEPllvsspeh 301
Cdd:cd16142 188 -ELDDHVGQILDALDELGIADNTIVIFTTDNGpeqDVWPdGGYTPFrgekgttweggvrvpaivRWPGKIKP-------- 258
|
330 340
....*....|....*....|....
gi 31543697 302 pqrwGQVSDAYVSLLDLTPTILDW 325
Cdd:cd16142 259 ----GRVSNEIVSHLDWFPTLAAL 278
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-356 |
6.75e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 107.68 E-value: 6.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFESgVYNNTAIAT--PHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYglhqDVHHFNSF 101
Cdd:cd16035 2 NILLILTDQERYPP-PWPAGWAALnlPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT----DTLGSPMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 102 ----DKVQSLPLLLNQAGVRTGIIGKKHV--GPETVYPFDFAFTEEnssvmqvgrnitrikqlVQKFLQTQ-----DDRP 170
Cdd:cd16035 77 pllsPDVPTLGHMLRAAGYYTAYKGKWHLsgAAGGGYKRDPGIAAQ-----------------AVEWLRERgaknaDGKP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 171 FFLYVAFHDPHrcghsqpqygtfcekfgngesgmgyipdwtpqiydpqDVMvpYFVPDTPAARADLAAQYTTIGRMDQGV 250
Cdd:cd16035 140 WFLVVSLVNPH-------------------------------------DIM--FPPDDEERWRRFRNFYYNLIRDVDRQI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 251 GLVLQELRGAGVLNDTLIIFTSDNG----------IPFpsgrtNLYWPGTAEPLLVSspeHPQRW--GQVSDAYVSLLDL 318
Cdd:cd16035 181 GRVLDALDASGLADNTIVVFTSDHGemggahglrgKGF-----NAYEEALHVPLIIS---HPDLFgtGQTTDALTSHIDL 252
|
330 340 350
....*....|....*....|....*....|....*...
gi 31543697 319 TPTILDWFSIPYPSYAifgSKTIQLTGRSLLPALEAEP 356
Cdd:cd16035 253 LPTLLGLAGVDAEARA---TEAPPLPGRDLSPLLTDAD 287
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
24-497 |
5.72e-25 |
|
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: 107.53 E-value: 5.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGF-ESGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMY-GLhqdvhhfnsF 101
Cdd:cd16158 3 NIVLLFADDLGYgDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYpGV---------F 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 102 DKVQS--LPL-------LLNQAGVRTGIIGKKH--VGPETVY-PFDFAFTE----------------------------- 140
Cdd:cd16158 74 YPGSRggLPLnettiaeVLKTVGYQTAMVGKWHlgVGLNGTYlPTHQGFDHylgipyshdqgpcqnltcfppnipcfggc 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 141 ----------ENSSVMQVGRNITRIKQLVQKFLQ------TQDDRPFFLYVAFHDPHrcghsQPQYGTfcEKFGnGESGM 204
Cdd:cd16158 154 dqgevpcplfYNESIVQQPVDLLTLEERYAKFAKdfiadnAKEGKPFFLYYASHHTH-----YPQFAG--QKFA-GRSSR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 205 GYIPDwtpqiydpqdvmvpyfvpdtpaaradlaaqytTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGipfPS---- 280
Cdd:cd16158 226 GPFGD--------------------------------ALAELDGSVGELLQTLKENGIDNNTLVFFTSDNG---PStmrk 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 281 -----------GRTNLYWPGTAEPLLVSSPEHPQrwGQVSDAYVSLLDLTPTILDWFSIPYPSyaifgsktIQLTGRSLL 349
Cdd:cd16158 271 srggnagllkcGKGTTYEGGVREPAIAYWPGRIK--PGVTHELASTLDILPTIAKLAGAPLPN--------VTLDGVDMS 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 350 PALeaeplwatVFSSQSHHEVTMSYPMRSVYHQNFRLIHNLSFKMPFpIDQDFYVSPTFQDLLNRTTTGRPtgwykdlhr 429
Cdd:cd16158 341 PIL--------FEQGKSPRQTFFYYPTSPDPDKGVFAVRWGKYKAHF-YTQGAAHSGTTPDKDCHPSAELT--------- 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543697 430 yyYRERWELYDISRDPRETRNLAADPDLAQVLEMLkaQLVKWQWETHDPWvcAP-------DGVLEEKLTPQCRP 497
Cdd:cd16158 403 --SHDPPLLFDLSQDPSENYNLLGLPEYNQVLKQI--QQVKERFEASMKF--GEseinkgeDPALEPCCKPGCTP 471
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-348 |
3.29e-23 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 99.37 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFES-GVYNN----------TAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGL- 91
Cdd:cd16153 3 NILWIITDDQRVDSlSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 92 --HQDVHHFNsfdkvQSLPLLLNQAGVRTGIIGKKHVGPETvypfDFAFTEENSSVMQVGRNITRIKQlvqkflqtqdDR 169
Cdd:cd16153 83 aaHPALDHGL-----PTFPEVLKKAGYQTASFGKSHLEAFQ----RYLKNANQSYKSFWGKIAKGADS----------DK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 170 PFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgyipdwTPqiydpqdvMVPyfvpdtPAARADLAAQYTTIGRMDQG 249
Cdd:cd16153 144 PFFVRLSFLQPH-----------------------------TP--------VLP------PKEFRDRFDYYAFCAYGDAQ 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 250 VGLVLQELRGAGVLND---TLIIFTSD-------NGIPFPSGrtnlYWPGTAE-PLLVSSPEH-PQRWGQVSDAYVSLLD 317
Cdd:cd16153 181 VGRAVEAFKAYSLKQDrdyTIVYVTGDhgwhlgeQGILAKFT----FWPQSHRvPLIVVSSDKlKAPAGKVRHDFVEFVD 256
|
330 340 350
....*....|....*....|....*....|.
gi 31543697 318 LTPTILDWFSIPYPSYAifgsktiQLTGRSL 348
Cdd:cd16153 257 LAPTLLAAAGVDVDAPD-------YLDGRDL 280
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
24-324 |
1.33e-22 |
|
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: 100.20 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGF-ESGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNS-- 100
Cdd:cd16160 3 NIVLFFADDMGYgDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRVFLPWDIgg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 101 --FDKVqSLPLLLNQAGVRTGIIGKKHVG------------PE--------TVYPF-------------DFA-----FTE 140
Cdd:cd16160 83 lpKTEV-TMAEALKEAGYTTGMVGKWHLGinennhsdgahlPShhgfdfvgTNLPFtnswacddtgrhvDFPdrsacFLY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 141 ENSSVMQVGRNITRIKQLV----QKFLQTQDDRPFFLYVAFHDPHrcghsQPQYGT--FCEKFGNGESGmgyipdwtpqi 214
Cdd:cd16160 162 YNDTIVEQPIQHEHLTETLvgdaKSFIEDNQENPFFLYFSFPQTH-----TPLFASkrFKGKSKRGRYG----------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 215 ydpqdvmvpyfvpdtpaaradlaaqyTTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGI------------PFPSGR 282
Cdd:cd16160 226 --------------------------DNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPhveycleggstgGLKGGK 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 31543697 283 TN-----------LYWPGTAEPllvsspehpqrwgQVSDAYVSLLDLTPTILD 324
Cdd:cd16160 280 GNsweggirvpfiAYWPGTIKP-------------RVSHEVVSTMDIFPTFVD 319
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
23-324 |
9.89e-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: 88.25 E-value: 9.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 23 RNVLLIVADDGGF-ESGVYNNTAIATPHLDALSRHSLIFR-NAFTSVSSCSPSRASLLTGLPQHQ-----NGMYGLHQDV 95
Cdd:cd00016 1 KHVVLIVLDGLGAdDLGKAGNPAPTTPNLKRLASEGATFNfRSVSPPTSSAPNHAALLTGAYPTLhgytgNGSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 96 HHFNSFDKVQSLPLLLNQAGVRTGIIGkkhvgpetvypfdfafteenssvmqvgrnitrikqLVQKFLQTQDDRPFFLYV 175
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIG-----------------------------------LLKAIDETSKEKPFVLFL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 176 AFHDPHRCGHSqpqygtfcekfgngesgmgyipdwtpqiydpqdvmvpyFVPDTPAaradlaaQYTTIGRMDQGVGLVLQ 255
Cdd:cd00016 126 HFDGPDGPGHA--------------------------------------YGPNTPE-------YYDAVEEIDERIGKVLD 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543697 256 ELRGAGVLNDTLIIFTSDNG-IPFPSGRT--NLYWPGTAE-----PLLVSSPEHPQrwGQVSDAYVSLLDLTPTILD 324
Cdd:cd00016 161 ALKKAGDADDTVIIVTADHGgIDKGHGGDpkADGKADKSHtgmrvPFIAYGPGVKK--GGVKHELISQYDIAPTLAD 235
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-324 |
2.59e-19 |
|
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: 89.33 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGFES-GVYN--NTAIATPHLDALSRHSLIFRNAFtSVSSCSPSRASLLTglpqhqnGMYGLHQDVHHF-- 98
Cdd:cd16154 2 NILLIIADDQGLDSsAQYSlsSDLPVTPTLDSLANSGIVFDNLW-ATPACSPTRATILT-------GKYGFRTGVLAVpd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 99 NSFDKVQSLPLLL----NQAGVRTGIIGKKHVG------PETVYPFDFA--------------FTEENSSVMQVGRNITR 154
Cdd:cd16154 74 ELLLSEETLLQLLikdaTTAGYSSAVIGKWHLGgndnspNNPGGIPYYAgilgggvqdyynwnLTNNGQTTNSTEYATTK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 155 IKQLVQKFLQTQdDRPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgyipdwTPQIYDPQDVMVPYFVPDTPAARA 234
Cdd:cd16154 154 LTNLAIDWIDQQ-TKPWFLWLAYNAPH-----------------------------TPFHLPPAELHSRSLLGDSADIEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 235 D-----LAAqyttIGRMDQGVGLVLQELRGAgVLNDTLIIFTSDNGIP-------FPSGRT--NLYWPGTAEPLLVSSPE 300
Cdd:cd16154 204 NprpyyLAA----IEAMDTEIGRLLASIDEE-ERENTIIIFIGDNGTPgqvvdlpYTRNHAkgSLYEGGINVPLIVSGAG 278
|
330 340
....*....|....*....|....
gi 31543697 301 HPQRwGQVSDAYVSLLDLTPTILD 324
Cdd:cd16154 279 VERA-NERESALVNATDLYATIAE 301
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
23-337 |
2.53e-16 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 81.62 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 23 RNVLLIVAddggfES------GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLP-QHQNGMYGLHQDV 95
Cdd:COG1368 235 PNVVVILL-----ESfsdffiGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKRPGQN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 96 HHFnsfdkvqSLPLLLNQAGVRTGIIgkkHVGPET------VYP---FDFAFTEENssvMQVGRNIT-RI--KQLVQKFL 163
Cdd:COG1368 310 NFP-------SLPSILKKQGYETSFF---HGGDGSfwnrdsFYKnlgFDEFYDRED---FDDPFDGGwGVsdEDLFDKAL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 164 QT--QDDRPFFLYV---AFHDPhrcghsqpqygtfcekfgngesgmgyipdWTpqiYDPQDVMVPYFVPDTPAARADlAA 238
Cdd:COG1368 377 EEleKLKKPFFAFLitlSNHGP-----------------------------YT---LPEEDKKIPDYGKTTLNNYLN-AV 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 239 QYTtigrmDQGVGLVLQELRGAGVLNDTLIIFTSDNGIPFPsGRTNLYWPGTAE--PLLVSSPEHPQrwGQVSDAYVSLL 316
Cdd:COG1368 424 RYA-----DQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSP-GKTDYENPLERYrvPLLIYSPGLKK--PKVIDTVGSQI 495
|
330 340
....*....|....*....|.
gi 31543697 317 DLTPTILDWFSIPYPSYAIFG 337
Cdd:COG1368 496 DIAPTLLDLLGIDYPSYYAFG 516
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
24-466 |
2.69e-15 |
|
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.
Pssm-ID: 293778 [Multi-domain] Cd Length: 521 Bit Score: 78.10 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVADDGGF-ESGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMyGLHQDVHHFNSFD 102
Cdd:cd16159 3 NIVLFMADDLGIgDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGM-ASSHGMRVILFTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 103 KVQSLP-------LLLNQAGVRTGIIGKKHVG-------------------------------------PETVYPFDFAF 138
Cdd:cd16159 82 SSGGLPpnettfaEVLKQQGYSTALIGKWHLGlhcesrndfchhplnhgfdyfyglpltnlkdcgdgsnGEYDLSFDPLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 139 TEE-------------------------------------------------NSSVMQ---------VGRNIT-RIKQLV 159
Cdd:cd16159 162 PLLtafvlitaltiflllylgavskrffvfllilsllfislfflllitnryfNCILMRnhevveqpmSLENLTqRLTKEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 160 QKFLQTQDDRPFFLYVAFHDPHRcghsqpqyGTFCEKFGNGESGMGYIPDwtpqiydpqdvmvpyfvpdtpaaradlaaq 239
Cdd:cd16159 242 ISFLERNKERPFLLVMSFLHVHT--------ALFTSKKFKGRSKHGRYGD------------------------------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 240 ytTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNG-----------------IPFPSGRTNLYWPGTAEPLLVSSPEHP 302
Cdd:cd16159 284 --NVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGghleeisvggeygggngGIYGGKKMGGWEGGIRVPTIVRWPGVI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 303 QRwGQVSDAYVSLLDLTPTILDWFSIPYPSyaifgskTIQLTGRSLLPALEAeplwatvFSSQSHHEVTMSYP----MRS 378
Cdd:cd16159 362 PP-GSVIDEPTSLMDIFPTVAALAGAPLPS-------DRIIDGRDLMPLLTG-------QEKRSPHEFLFHYCgaelHAV 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 379 VYHQNFrliHNLSFKMpfpidqdFYVSPTFQDLLNRTTTGRPTGWYKDlhRYYYRERWELYDISRDPRETRNL-AADPDL 457
Cdd:cd16159 427 RYRPRD---GGAVWKA-------HYFTPNFYPGTEGCCGTLLCRCFGD--SVTHHDPPLLFDLSADPSESNPLdPTDEPY 494
|
570
....*....|
gi 31543697 458 AQVLE-MLKA 466
Cdd:cd16159 495 QEIIKkILEA 504
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
24-354 |
6.88e-13 |
|
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: 69.88 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 24 NVLLIVAD--DGGFeSGVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRASLLTGLPQHqngmygLHQDVHHFNSF 101
Cdd:cd16171 2 NVVMVMSDsfDGRL-TFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTH------LTESWNNYKGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 102 DK-VQSLPLLLNQAGVRTGIIGK------KHVGPETV--YPFDFAFT---EENSSVMQVG-RNITRIK-----------Q 157
Cdd:cd16171 75 DPnYPTWMDRLEKHGYHTQKYGKldytsgHHSVSNRVeaWTRDVPFLlrqEGRPTVNLVGdRSTVRVMlkdwqntdkavH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 158 LVQKFLQTQDdRPFFLYVAFHDPHRcgHSQPQYGtfcEKFGngesgmgyipdwtpqiydpqdvmvpyfvpdtpAARADLA 237
Cdd:cd16171 155 WIRKEAPNLT-QPFALYLGLNLPHP--YPSPSMG---ENFG--------------------------------SIRNIRA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 238 AQYTTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGIPFPSGR----TNLYWPGTAEPLLVSSPEHPQrwGQVSDAYV 313
Cdd:cd16171 197 FYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRqfykMSMYEGSSHVPLLIMGPGIKA--GQQVSDVV 274
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 31543697 314 SLLDLTPTILDWFSIPYPSyaifgsktiQLTGRSLLPALEA 354
Cdd:cd16171 275 SLVDIYPTMLDIAGVPQPQ---------NLSGYSLLPLLSE 306
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
23-326 |
5.94e-11 |
|
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: 63.09 E-value: 5.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 23 RNVLLIVAddggfES------GVYNNTAIATPHLDALSRHSLIFRNAFTSVSSCSPSRA--SLLTGLPQHQNGMYGLHQD 94
Cdd:cd16015 1 PNVIVILL-----ESfsdpyiDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 95 VHHfnsfdKVQSLPLLLNQAGVRTGIIgkkHVGP------ETVYP---FDFAFTEENSSVMQVGRNITRIK-----QLVQ 160
Cdd:cd16015 76 KLN-----PLPSLPSILKEQGYETIFI---HGGDasfynrDSVYPnlgFDEFYDLEDFPDDEKETNGWGVSdeslfDQAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 161 KFLQTQDDRPFFLYV---AFHDPhrcghsqpqYGTFCEKFgngesgmgyipdwtpqiydpqdvmvpYFVPDTPAARADLA 237
Cdd:cd16015 148 EELEELKKKPFFIFLvtmSNHGP---------YDLPEEKK--------------------------DEPLKVEEDKTELE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 238 AQYTTIGRMDQGVGLVLQELRGAGVLNDTLIIFTSD---NGIPFPSGRTNLYWPGTAEPLLVSSPEHPQrwGQVSDAYVS 314
Cdd:cd16015 193 NYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDhlpSLGSDYDETDEDPLDLYRTPLLIYSPGLKK--PKKIDRVGS 270
|
330
....*....|..
gi 31543697 315 LLDLTPTILDWF 326
Cdd:cd16015 271 QIDIAPTLLDLL 282
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
5-276 |
2.16e-10 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 62.46 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 5 GLACCTILLVLGLCGAHSRNVLLIVADdgGFESGVYnnTAIATPHLDALSRHSLIFRNAFTSVSSCS-PSRASLLTGLP- 82
Cdd:COG1524 6 SLLLASLLAAAAAAAPPAKKVVLILVD--GLRADLL--ERAHAPNLAALAARGVYARPLTSVFPSTTaPAHTTLLTGLYp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 83 -QHQ---NGMY-----------GLHQDVHHFNSFDKVQSLPLLLNQAGVRTGIIG-KKHVGPETV-YPFDFAFTEENSSV 145
Cdd:COG1524 82 gEHGivgNGWYdpelgrvvnslSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFwPSFEGSGLIdAARPYPYDGRKPLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 146 MQVGRNITRIKQLVQkflQTQDDRPFFLYVAFHDPHRCGHsqpQYGtfcekfgngesgmgyipdwtpqiydpqdvmvpyf 225
Cdd:COG1524 162 GNPAADRWIAAAALE---LLREGRPDLLLVYLPDLDYAGH---RYG---------------------------------- 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 31543697 226 vPDTPAARADLAaqyttigRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGI 276
Cdd:COG1524 202 -PDSPEYRAALR-------EVDAALGRLLDALKARGLYEGTLVIVTADHGM 244
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
424-477 |
2.49e-08 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 51.87 E-value: 2.49e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 31543697 424 YKDLHRYYYRERWELYDISRDPRETRNLAADPDLAQVLEMLKAQLVKWQWETHD 477
Cdd:pfam16347 50 YKLIHFYNDIDEWELYDLQKDPKEMNNVYGDPEYAEVQAELKEELEELRKQYKD 103
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
23-276 |
6.77e-08 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 53.74 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 23 RNVLLIVADdgGFESGvYNNTAIATPHLDALSRHSLIF---RNAFTSVSScsPSRASLLTGLP--QHQ---NGMY----- 89
Cdd:cd16018 1 PPLIVISID--GFRWD-YLDRAGLTPNLKRLAEEGVRAkyvKPVFPTLTF--PNHYSIVTGLYpeSHGivgNYFYdpktn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 90 --GLHQDVHHFNSFDKVQSLPLLLNQAGVRTGII-----GKKHVGPETVYPFDFAFTEENSSVMQVGRnitRIKQLVQKF 162
Cdd:cd16018 76 eeFSDSDWVWDPWWIGGEPIWVTAEKAGLKTASYfwpgsEVAIIGYNPTPIPLGGYWQPYNDSFPFEE---RVDTILEWL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 163 lqtQDDRPFFLYVAFHDPHRCGHsqpQYGtfcekfgngesgmgyipdwtpqiydpqdvmvpyfvPDTPAARADLAaqytt 242
Cdd:cd16018 153 ---DLERPDLILLYFEEPDSAGH---KYG-----------------------------------PDSPEVNEALK----- 186
|
250 260 270
....*....|....*....|....*....|....
gi 31543697 243 igRMDQGVGLVLQELRGAGVLNDTLIIFTSDNGI 276
Cdd:cd16018 187 --RVDRRLGYLIEALKERGLLDDTNIIVVSDHGM 218
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
47-276 |
8.02e-06 |
|
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: 47.80 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 47 TPHLDALSRHSLIFRNAFTSV-SSCSPSRASLLTGLPQHQNGMYG-----------LHQDVHHFNSFDKVQSLPLL--LN 112
Cdd:pfam01663 20 TPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVGntfydpktgeyLVFVISDPEDPRWWQGEPIWdtAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 113 QAGVRTGII----GKKHVGPETVYPFDFAFTEENSSVMQVGRNITRIKQ--LVQKFLQTQDDRPFFLYVAFHDPHRCGHs 186
Cdd:pfam01663 100 KAGVRAAALfwpgSEVDYSTYYGTPPRYLKDDYNNSVPFEDRVDTAVLQtwLDLPFADVAAERPDLLLVYLEEPDYAGH- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543697 187 qpQYGtfcekfgngesgmgyipdwtpqiydpqdvmvpyfvPDTPAARADLAaqyttigRMDQGVGLVLQELRGAGVLNDT 266
Cdd:pfam01663 179 --RYG-----------------------------------PDSPEVEDALR-------RVDRAIGDLLEALDERGLFEDT 214
|
250
....*....|
gi 31543697 267 LIIFTSDNGI 276
Cdd:pfam01663 215 NVIVVSDHGM 224
|
|
| |
