|
Name |
Accession |
Description |
Interval |
E-value |
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
24-404 |
1.92e-106 |
|
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: 319.45 E-value: 1.92e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFESGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSFDK 103
Cdd:cd16027 2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRS--RGFPLPDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 104 VQSLPLLLSQAGVRTGIIGKKHVGPETVYPFDFafteENSSVLQVGRNITRIKQLVRKFLQTQD-DRPFFLYVALHDPHR 182
Cdd:cd16027 80 VKTLPELLREAGYYTGLIGKTHYNPDAVFPFDD----EMRGPDDGGRNAWDYASNAADFLNRAKkGQPFFLWFGFHDPHR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 183 CGHSQPQYGAfcekfgngesgmgripdwtpqIYDPQDVMVPYFVPDTPAARADLAAQYTTIGRMDQ-------------- 248
Cdd:cd16027 156 PYPPGDGEEP---------------------GYDPEKVKVPPYLPDTPEVREDLADYYDEIERLDQqvgeildeleedgl 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 249 -----------------------------------------------------DLTPTILDWFSIPYPSYaifgsktiqL 275
Cdd:cd16027 215 ldntiviftsdhgmpfprakgtlydsglrvplivrwpgkikpgsvsdalvsfiDLAPTLLDLAGIEPPEY---------L 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 276 TGRSLLPALEAE--PPWATVFSSQSHHEVTmSYPMRSVYHQNFRLIHNLsfkMPfpidqdfyvsptfqdllnrtaagqpt 353
Cdd:cd16027 286 QGRSFLPLLKGEkdPGRDYVFAERDRHDET-YDPIRSVRTGRYKYIRNY---MP-------------------------- 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958663166 354 gwyknlqhyyyrerWELYDISRDPRETRNLAAEPDFAQVLEVLKAQLVKWQ 404
Cdd:cd16027 336 --------------EELYDLKNDPDELNNLADDPEYAEVLEELRAALDAWM 372
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
24-410 |
6.80e-52 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 178.92 E-value: 6.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADD-GGFESGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFD 102
Cdd:COG3119 25 NILFILADDlGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGGLPPD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 103 kVQSLPLLLSQAGVRTGIIGKKHvgpetVYpFDFAFTEEnssvlqvgrnitrikqlVRKFLQTQ--DDRPFFLYVALHDP 180
Cdd:COG3119 105 -EPTLAELLKEAGYRTALFGKWH-----LY-LTDLLTDK-----------------AIDFLERQadKDKPFFLYLAFNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 181 HRCGHSQPQYGAfcekfgngesgmgripdwtpqIYDPQDVMVP-YFVPD---TPAARADLAAQYTTIGRMDQ-------- 248
Cdd:COG3119 161 HAPYQAPEEYLD---------------------KYDGKDIPLPpNLAPRdltEEELRRARAAYAAMIEEVDDqvgrllda 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 249 ----------------------------------------------------------------DLTPTILDWFSIPYPS 264
Cdd:COG3119 220 leelgladntivvftsdngpslgehglrggkgtlyeggirvplivrwpgkikagsvsdalvsliDLLPTLLDLAGVPIPE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 265 YaifgsktiqLTGRSLLPALE-AEPPWATVFssqsHHEVTMSYPMRSVYHQNFRLIHNlsfkmpfpidqdfyvsptfqdl 343
Cdd:COG3119 300 D---------LDGRSLLPLLTgEKAEWRDYL----YWEYPRGGGNRAIRTGRWKLIRY---------------------- 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958663166 344 lnrtaagqptgwyknlqhYYYRERWELYDISRDPRETRNLAAepDFAQVLEVLKAQLVKWQWETHDP 410
Cdd:COG3119 345 ------------------YDDDGPWELYDLKNDPGETNNLAA--DYPEVVAELRALLEAWLKELGDP 391
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
23-400 |
4.55e-38 |
|
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: 143.05 E-value: 4.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 23 RNVLLIVADDGGFES-GVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvhhfNSF 101
Cdd:cd16031 3 PNIIFILTDDHRYDAlGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNG-----PLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 102 DKVQ-SLPLLLSQAGVRTGIIGKKHVGPETVYP---FDF-------------AFTEENSSVLQVGRNITRIKQLVRKFLQ 164
Cdd:cd16031 78 DASQpTYPKLLRKAGYQTAFIGKWHLGSGGDLPppgFDYwvsfpgqgsyydpEFIENGKRVGQKGYVTDIITDKALDFLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 165 TQD-DRPFFLYVALHDPHRCGHSQPQYGafcEKFGNGEsgMGRIPDWTPQIYDPQ----------DVMVPYFVPDTPAAR 233
Cdd:cd16031 158 ERDkDKPFCLSLSFKAPHRPFTPAPRHR---GLYEDVT--IPEPETFDDDDYAGRpewareqrnrIRGVLDGRFDTPEKY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 234 ADLAAQY--------TTIGRM-------------------DQ-------------------------------------- 248
Cdd:cd16031 233 QRYMKDYlrtvtgvdDNVGRIldyleeqgladntiiiytsDNgfflgehglfdkrlmyeesirvpliirdprlikagtvv 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 249 -------DLTPTILDWFSIPYPSYaifgsktIQltGRSLLPALEAEPP--WATVFssqshhevtmsypmrsvYHQNFrli 319
Cdd:cd16031 313 dalvlniDFAPTILDLAGVPIPED-------MQ--GRSLLPLLEGEKPvdWRKEF-----------------YYEYY--- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 320 hnlsFKMPFPidqdfYVSPTFqdllnrtaaGQPTGWYKNLQHYYYRERWELYDISRDPRETRNLAAEPDFAQVLEVLKAQ 399
Cdd:cd16031 364 ----EEPNFH-----NVPTHE---------GVRTERYKYIYYYGVWDEEELYDLKKDPLELNNLANDPEYAEVLKELRKR 425
|
.
gi 1958663166 400 L 400
Cdd:cd16031 426 L 426
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
24-181 |
5.35e-36 |
|
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: 132.18 E-value: 5.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFES-GVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNsfD 102
Cdd:cd16022 2 NILLIMTDDLGYDDlGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLP--P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 103 KVQSLPLLLSQAGVRTGIIGKKHvgpetvypfdfafteenssvlqvgrnitrikQLVRKFLQTQD-DRPFFLYVALHDPH 181
Cdd:cd16022 80 DEPTLAELLKEAGYRTALIGKWH-------------------------------DEAIDFIERRDkDKPFFLYVSFNAPH 128
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
24-383 |
1.05e-33 |
|
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: 130.26 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGF-ESGVYNNtAINTPHLDALARHSLIFRNaFTSVSSCSPSRASLLTGLPQHQNG---MYGLHQDVHHFN 99
Cdd:cd16025 4 NILLILADDLGFsDLGCFGG-EIPTPNLDALAAEGLRFTN-FHTTALCSPTRAALLTGRNHHQVGmgtMAELATGKPGYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 100 SF--DKVQSLPLLLSQAGVRTGIIGKKHVGPETVYpFDFAFTEenssvlqvgRNITRIKQlvrkflQTQDDRPFFLYVAL 177
Cdd:cd16025 82 GYlpDSAATIAEVLKDAGYHTYMSGKWHLGPDDYY-STDDLTD---------KAIEYIDE------QKAPDKPFFLYLAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 178 ---HDPHrcgHSQPQYgafCEKF-GNGESG--------------MGRIPDWTPQIYDPQDV------------------- 220
Cdd:cd16025 146 gapHAPL---QAPKEW---IDKYkGKYDAGwdalreerlerqkeLGLIPADTKLTPRPPGVpawdslspeekklearrme 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 221 ----MVPY------------------------FVPD--------------TP-------------------------AAR 233
Cdd:cd16025 220 vyaaMVEHmdqqigrlidylkelgeldntliiFLSDngasaepgwanasnTPfrlykqasheggirtplivswpkgiKAK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 234 ADLAAQYTTIgrmdQDLTPTILDWFSIPYPSyAIFGSKTIQLTGRSLLPALEAEppwatvfsSQSHHEVTMSYPM---RS 310
Cdd:cd16025 300 GGIRHQFAHV----IDIAPTILELAGVEYPK-TVNGVPQLPLDGVSLLPTLDGA--------AAPSRRRTQYFELfgnRA 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958663166 311 VYHQNFRLIHNlsfkmpfpidqdfyvsptfqdllnrtaaGQPTGWYknlqhyyyrERWELYDISRDPRETRNL 383
Cdd:cd16025 367 IRKGGWKAVAL----------------------------HPPPGWG---------DQWELYDLAKDPSETHDL 402
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-403 |
1.80e-32 |
|
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: 127.27 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADD-GGFESGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGL--PQHQNGMYGLHQDVHHFNS 100
Cdd:cd16144 2 NIVLILVDDlGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQypARLGITDVIPGRRGPPDNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 101 F-----------DKVQSLPLLLSQAGVRTGIIGKKHVGPE-TVYP----FDFAFTE-----------------ENSSVLQ 147
Cdd:cd16144 82 KlipppsttrlpLEEVTIAEALKDAGYATAHFGKWHLGGEgGYGPedqgFDVNIGGtgnggppsyyfppgkpnPDLEDGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 148 VGRNIT-RIKQLVRKFLQTQDDRPFFLYV---ALHDPHRC-----------------GHSQPQYGAFCEKFGNgesGMGR 206
Cdd:cd16144 162 EGEYLTdRLTDEAIDFIEQNKDKPFFLYLshyAVHTPIQArpeliekyekkkkglrkGQKNPVYAAMIESLDE---SVGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 207 IPDW---------------------TPQIYDPQD---------------VMVPYFV--PDTPAARADLAAQYTTIgrmdq 248
Cdd:cd16144 239 ILDAleelgladntlviftsdngglSTRGGPPTSnaplrggkgslyeggIRVPLIVrwPGVIKPGSVSDVPVIGT----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 249 DLTPTILDWFSIPYPSYAIfgsktiqLTGRSLLPALEAEppwatvfssqshhevTMSYPMRSVYHqnfrliHnlsfkmpF 328
Cdd:cd16144 314 DLYPTFLELAGGPLPPPQH-------LDGVSLVPLLKGG---------------EADLPRRALFW------H-------F 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663166 329 PIDQDFYVSPTfqdllnrTAAGQptGWYKnLQHYYYRERWELYDISRDPRETRNLAAE-PDfaqVLEVLKAQLVKW 403
Cdd:cd16144 359 PHYHGQGGRPA-------SAIRK--GDWK-LIEFYEDGRVELYNLKNDIGETNNLAAEmPE---KAAELKKKLDAW 421
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
24-403 |
2.98e-32 |
|
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: 126.51 E-value: 2.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGF-ESGVYNNTAINTPHLDALARHSLIFRNAFTSvSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSfd 102
Cdd:cd16146 2 NVILILTDDQGYgDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWHTILGRERMRL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 103 KVQSLPLLLSQAGVRTGIIGKKHVG------PE-----TVY---------PFDFAFTEENSSVLQvgRNITRIK------ 156
Cdd:cd16146 79 DETTLAEVFKDAGYRTGIFGKWHLGdnypyrPQdrgfdEVLghggggigqYPDYWGNDYFDDTYY--HNGKFVKtegyct 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 157 ----QLVRKFLQTQDDRPFFLYVALHDPHRCGHSQPQYGAFCEKFGNGES-----GM--------GRIPDW--------- 210
Cdd:cd16146 157 dvffDEAIDFIEENKDKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKlaafyGMieniddnvGRLLAKlkelgleen 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 211 T---------PQIYDPQ----------------DVMVPYFV--PDTPAARAD---LAAQYttigrmdqDLTPTILDWFSI 260
Cdd:cd16146 237 TivifmsdngPAGGVPKrfnagmrgkkgsvyegGHRVPFFIrwPGKILAGKDvdtLTAHI--------DLLPTLLDLCGV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 261 PYPsyaifgsKTIQLTGRSLLPALEAE-PPWAT-VFSSQSHHEVTMSYPMR--SVYHQNFRLIHNlsfkmpfpidqdfyv 336
Cdd:cd16146 309 KLP-------EGIKLDGRSLLPLLKGEsDPWPErTLFTHSGRWPPPPKKKRnaAVRTGRWRLVSP--------------- 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958663166 337 sptfqdllnrtaagqptgwyknlqhyyYRERWELYDISRDPRETRNLAAE-PDfaqVLEVLKAQLVKW 403
Cdd:cd16146 367 ---------------------------KGFQPELYDIENDPGEENDVADEhPE---VVKRLKAAYEAW 404
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-409 |
2.61e-31 |
|
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: 123.87 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFES-GVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYglhQDVHHFNSF- 101
Cdd:cd16033 2 NILFIMTDQQRYDTlGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVL---NNVENAGAYs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 102 ----DKVQSLPLLLSQAGVRTGIIGKKHVGPETVyPFDFAFtEENSSVLQ------VGRNITRIKQLvrkflqTQDDRPF 171
Cdd:cd16033 79 rglpPGVETFSEDLREAGYRNGYVGKWHVGPEET-PLDYGF-DEYLPVETtieyflADRAIEMLEEL------AADDKPF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 172 FLYVALHDPHR-CGHSQP-----------QYGAFCEKFGN------------GESGMGrIPDWTPQI------------- 214
Cdd:cd16033 151 FLRVNFWGPHDpYIPPEPyldmydpedipLPESFADDFEDkpyiyrrerkrwGVDTED-EEDWKEIIahywgyitlidda 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 215 -------------YDpqDVMVPY------------------FVPDTpAARADLAAQYTTIGRMDQ---------DLTPTI 254
Cdd:cd16033 230 igrildaleelglAD--DTLVIFtsdhgdalgahrlwdkgpFMYEE-TYRIPLIIKWPGVIAAGQvvdefvsllDLAPTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 255 LDWFSIPYPSyaifgsktiQLTGRSLLPAL--EAEPPWATVFSSQSH-HEVTmsYPMRSVYHQNFRLIHNlsfkmPFPID 331
Cdd:cd16033 307 LDLAGVDVPP---------KVDGRSLLPLLrgEQPEDWRDEVVTEYNgHEFY--LPQRMVRTDRYKYVFN-----GFDID 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958663166 332 qdfyvsptfqdllnrtaagqptgwyknlqhyyyrerwELYDISRDPRETRNLAAEPDFAQVLEVLKAQLVKWQWETHD 409
Cdd:cd16033 371 -------------------------------------ELYDLESDPYELNNLIDDPEYEEILREMRTRLYEWMEETGD 411
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
23-203 |
3.71e-30 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 118.29 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 23 RNVLLIVADDGGFES-GVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDvhhfNSF 101
Cdd:pfam00884 1 PNVVLVLGESLRAPDlGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPV----GLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 102 DKVQSLPLLLSQAGVRTGIIGKKHVGP-----ETVYPFDFAFTEENSSVLQVGRNI------------TRIKQLVRKFLQ 164
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWynnqsPCNLGFDKFFGRNTGSDLYADPPDvpyncsgggvsdEALLDEALEFLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958663166 165 tQDDRPFFLYVALHDPHRCGHSQPQY-GAFCEKFGNGESG 203
Cdd:pfam00884 157 -NNDKPFFLVLHTLGSHGPPYYPDRYpEKYATFKPSSCSE 195
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
23-415 |
4.28e-27 |
|
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: 112.86 E-value: 4.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 23 RNVLLIVADDGGFES-GVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlhqdvhhfNSF 101
Cdd:cd16156 1 KQFIFIMTDTQRWDMvGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWT--------NCM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 102 ---DKVQSLPLLLSQAGVRTGIIGKKHV-------------GPETVYPFDFA-----FTEENSSVLQVGRNIT------- 153
Cdd:cd16156 73 algDNVKTIGQRLSDNGIHTAYIGKWHLdggdyfgngicpqGWDPDYWYDMRnyldeLTEEERRKSRRGLTSLeaegike 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 154 ------RIKQLVRKFLQTQDDRPFFLYVAL---HDPHRC----------------------------------------- 183
Cdd:cd16156 153 eftyghRCTNRALDFIEKHKDEDFFLVVSYdepHHPFLCpkpyasmykdfefpkgenayddlenkplhqrlwagakphed 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 184 ---GHSQPQYGAFCEKFGNGEsgMGRIPDWTPQIYdpQDVMVPY------------FVPDTPAARADLA--------AQY 240
Cdd:cd16156 233 gdkGTIKHPLYFGCNSFVDYE--IGRVLDAADEIA--EDAWVIYtsdhgdmlgahkLWAKGPAVYDEITnipliirgKGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 241 TTIGRMDQ------DLTPTILDWFSIPYPSyaifgsktiQLTGRSLLPALEAE--PPWATVFSSQSHHEVTMS-----YP 307
Cdd:cd16156 309 EKAGTVTDtpvshiDLAPTILDYAGIPQPK---------VLEGESILATIEDPeiPENRGVFVEFGRYEVDHDgfggfQP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 308 MRSVYHQNFRLIHNLsfkmpfpIDQDfyvsptfqdllnrtaagqptgwyknlqhyyyrerwELYDISRDPRETRNLAAEP 387
Cdd:cd16156 380 VRCVVDGRYKLVINL-------LSTD-----------------------------------ELYDLEKDPYEMHNLIDDP 417
|
490 500 510
....*....|....*....|....*....|...
gi 1958663166 388 DFAQVLEVLKAQLVKWQWETHDP-----WVCAP 415
Cdd:cd16156 418 DYADVRDQLHDELLDYMNETRDPfrgyyWECRP 450
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
24-181 |
5.61e-25 |
|
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: 105.72 E-value: 5.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFES-GVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTG-LPQ---------HQNGMYGLH 92
Cdd:cd16026 3 NIVVILADDLGYGDlGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGrYPVrvglpgvvgPPGSKGGLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 93 QDvhhfnsfdkVQSLPLLLSQAGVRTGIIGKKHVG--PETvYP----FDFAF---------------TEENSSVLQVGRN 151
Cdd:cd16026 83 PD---------EITIAEVLKKAGYRTALVGKWHLGhqPEF-LPtrhgFDEYFgipysndmwpfplyrNDPPGPLPPLMEN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958663166 152 ITRIKQ------LVR-------KFLQTQDDRPFFLYVALHDPH 181
Cdd:cd16026 153 EEVIEQpadqssLTQrytdeavDFIERNKDQPFFLYLAHTMPH 195
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-324 |
5.91e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 104.16 E-value: 5.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 23 RNVLLIVADD-GGFESGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlhqdvhhfNS- 100
Cdd:cd16037 1 PNILIIMSDEhNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWD--------NAd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 101 --FDKVQSLPLLLSQAGVRTGIIGKKHVGPETVYPFdFAFTeenssvlqvgRNITrikQLVRKFLQTQ--DDRPFFLYVA 176
Cdd:cd16037 73 pyDGDVPSWGHALRAAGYETVLIGKLHFRGEDQRHG-FRYD----------RDVT---EAAVDWLREEaaDDKPWFLFVG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 177 LHDPHrcghsQPQ-----------------YGAFCE----KFG--------------------------NGESGMgripd 209
Cdd:cd16037 139 FVAPH-----FPLiapqefydlyvrraraaYYGLVEfldeNIGrvldaleelglldntliiytsdhgdmLGERGL----- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 210 WTPQIYDPQDVMVPYFV--PDTPAARadlaaqyttigRMDQ-----DLTPTILDWFSIPYPSYaifgsktiqLTGRSLLP 282
Cdd:cd16037 209 WGKSTMYEESVRVPMIIsgPGIPAGK-----------RVKTpvslvDLAPTILEAAGAPPPPD---------LDGRSLLP 268
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958663166 283 ALEAEPPWA-TVFSSQSHHEVTMsyPMRSVYHQNFRLIHNLSF 324
Cdd:cd16037 269 LAEGPDDPDrVVFSEYHAHGSPS--GAFMLRKGRWKYIYYVGY 309
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-400 |
1.45e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 104.18 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFES-GVYNNTAINTPHLDALARHSLIFRNAF----TSVSSCSPSRASLLTGlpqhqngMYGLH-QDVHH 97
Cdd:cd16155 4 NILFILADDQRADTiGALGNPEIQTPNLDRLARRGTSFTNAYnmggWSGAVCVPSRAMLMTG-------RTLFHaPEGGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 98 FNSFDKVQSLPLLLSQAGVRTGIIGKKHVgpetvypfDFAfteeNSSVlqvgrnitrikqlvrKFLQ--TQDDRPFFLYV 175
Cdd:cd16155 77 AAIPSDDKTWPETFKKAGYRTFATGKWHN--------GFA----DAAI---------------EFLEeyKDGDKPFFMYV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 176 AL---HDPhrcgHSQPQygAFCEKFGNGEsgmgrIPDwtPQIYDPQ------------DVMVPYfvPDTPAA-RADLAAQ 239
Cdd:cd16155 130 AFtapHDP----RQAPP--EYLDMYPPET-----IPL--PENFLPQhpfdngegtvrdEQLAPF--PRTPEAvRQHLAEY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 240 YTTIGRMDqdltptildwfsipypsyaifgsktIQLtGRsLLPALEAEPPWA-T--VFSSQ------SHHevtmsypmrs 310
Cdd:cd16155 195 YAMITHLD-------------------------AQI-GR-ILDALEASGELDnTiiVFTSDhglavgSHG---------- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 311 vyhqnfrLI--HNL---SFKMPF-----------PIDQDFY---VSPTFQDLL------------------NRTAAGQPT 353
Cdd:cd16155 238 -------LMgkQNLyehSMRVPLiisgpgipkgkRRDALVYlqdVFPTLCELAgieipesvegksllpvirGEKKAVRDT 310
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958663166 354 --GWYKNLQHYYYRERW------------ELYDISRDPRETRNLAAEPDFAQVLEVLKAQL 400
Cdd:cd16155 311 lyGAYRDGQRAIRDDRWkliiyvpgvkrtQLFDLKKDPDELNNLADEPEYQERLKKLLAEL 371
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-282 |
2.09e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 101.86 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADdggfeS------GVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLpqhqngmYGLHQDVHH 97
Cdd:cd16148 2 NVILIVID-----SlradhlGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGL-------YPFYHGVWG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 98 FNSFDKVQSLPLLLSQAGVRTGIIGkKHVGPETVYPFDFAFTEENSSVLQVGRNIT-------RIKQLVRKFLQTQ-DDR 169
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAVS-SNPHLFGGPGFDRGFDTFEDFRGQEGDPGEegderaeRVTDRALEWLDRNaDDD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 170 PFFLYVALHDPHRcghsqP------------QYGAFCEK-------------------FGNGESGMGRIPDWTPqiYDPQ 218
Cdd:cd16148 149 PFFLFLHYFDPHE-----PylydaevryvdeQIGRLLDKlkelglledtlvivtsdhgEEFGEHGLYWGHGSNL--YDEQ 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663166 219 dVMVPYFV--PDTPAARADlAAQYTTIgrmdqDLTPTILDWFSIPYPSYaifgsktiqLTGRSLLP 282
Cdd:cd16148 222 -LHVPLIIrwPGKEPGKRV-DALVSHI-----DIAPTLLDLLGVEPPDY---------SDGRSLLP 271
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-409 |
4.75e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 103.47 E-value: 4.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 23 RNVLLIVADDGGFES-GVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGmyglHQDVHHFNSF 101
Cdd:cd16150 1 PNIVIFVADQLRADSlGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG----HRTLHHLLRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 102 DKvqslPLLLS---QAGVRTGIIGKKHVGPETVYPFDFAFTEEnssvLQVGRNITRIKqlvrkflQTQDDRPFFLYVALH 178
Cdd:cd16150 77 DE----PNLLKtlkDAGYHVAWAGKNDDLPGEFAAEAYCDSDE----ACVRTAIDWLR-------NRRPDKPFCLYLPLI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 179 DPHrcghsqPQYGafCEK--------------------FGNGESGMGRIP-----DWTPQIYDP-QDV---MVPYF---- 225
Cdd:cd16150 142 FPH------PPYG--VEEpwfsmidreklpprrppglrAKGKPSMLEGIEkqgldRWSEERWRElRATylgMVSRLdhqf 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 226 ------VPDTPAAR----------ADLAAQY--------------------------TTIGRMDQ-----DLTPTILDWF 258
Cdd:cd16150 214 grlleaLKETGLYDdtavfffsdhGDYTGDYglvekwpntfedcltrvpliikppggPAGGVSDAlvelvDIPPTLLDLA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 259 SIPyPSYAIFgsktiqltGRSLLPALEAEP--PWATVFSS--QSHHEvtmsYPMRSVYHQNFrlihnlSFKMPFPIDQdf 334
Cdd:cd16150 294 GIP-LSHTHF--------GRSLLPVLAGETeeHRDAVFSEggRLHGE----EQAMEGGHGPY------DLKWPRLLQQ-- 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958663166 335 yvspTFQDLLNRtAAGQPTGWYKnlqhYYYR--ERWELYDISRDPRETRNLAAEPDFAQVLEVLKAQLVKWQWETHD 409
Cdd:cd16150 353 ----EEPPEHTK-AVMIRTRRYK----YVYRlyEPDELYDLEADPLELHNLIGDPAYAEIIAEMKQRLLRWMVETSD 420
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-222 |
7.16e-24 |
|
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: 102.66 E-value: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGF-ESGVYN-NTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTG-------LPQHQNGMYGLHQd 94
Cdd:cd16143 2 NIVIILADDLGYgDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGrypwrsrLKGGVLGGFSPPL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 95 vhhfnsFDKVQ-SLPLLLSQAGVRTGIIGKKHVG-------PETVYP--------------------FDFAFTEENSSVL 146
Cdd:cd16143 81 ------IEPDRvTLAKMLKQAGYRTAMVGKWHLGldwkkkdGKKAATgtgkdvdyskpikggpldhgFDYYFGIPASEVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958663166 147 qvgrniTRIKQLVRKFLQTQ--DDRPFFLYVALHDPHrcGHSQPqygafCEKFgNGESGMGRIPDWTPQIydpqDVMV 222
Cdd:cd16143 155 ------PTLTDKAVEFIDQHakKDKPFFLYFALPAPH--TPIVP-----SPEF-QGKSGAGPYGDFVYEL----DWVV 214
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
23-410 |
6.09e-23 |
|
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: 100.41 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 23 RNVLLIVADDGGFE-SGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMY--GLHQDVHHFN 99
Cdd:cd16028 1 RNVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVwnGTPLDARHLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 100 sfdkvqsLPLLLSQAGVRTGIIGKKHVGP----------------------ETVYPFDFaFTEENSSVlqvgrniTRIKQ 157
Cdd:cd16028 81 -------LALELRKAGYDPALFGYTDTSPdprglapldprllsyelampgfDPVDRLDE-YPAEDSDT-------AFLTD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 158 LVRKFLQTQDDRPFFL----------------YVALHD------PHRCGHSQ------PQYGAFCEK-----FGNGESGM 204
Cdd:cd16028 146 RAIEYLDERQDEPWFLhlsyirphppfvapapYHALYDpadvppPIRAESLAaeaaqhPLLAAFLERieslsFSPGAANA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 205 GRIPDWTPQ------------------------------------------------------IYDPQDVMVPYFVPDtP 230
Cdd:cd16028 226 ADLDDEEVAqmratylgliaevddhlgrlfdylketgqwddtlivftsdhgeqlgdhwlwgkdGFFDQAYRVPLIVRD-P 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 231 AARADlAAQYTTIGRMDQ--DLTPTILDWFSIPYPSyaifgsktiQLTGRSLLPALEAEPP--WATvfssqshhEVTMSY 306
Cdd:cd16028 305 RREAD-ATRGQVVDAFTEsvDVMPTILDWLGGEIPH---------QCDGRSLLPLLAGAQPsdWRD--------AVHYEY 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 307 PMRSVYHQNFRL-----IHNLSFKMPFpiDQDF-YVspTFQDLlnrtaagqptgwyknlqhyyyreRWELYDISRDPRET 380
Cdd:cd16028 367 DFRDVSTRRPQEalglsPDECSLAVIR--DERWkYV--HFAAL-----------------------PPLLFDLKNDPGEL 419
|
490 500 510
....*....|....*....|....*....|
gi 1958663166 381 RNLAAEPDFAQVLEVLKAQLVKWQWETHDP 410
Cdd:cd16028 420 RDLAADPAYAAVVLRYAQKLLSWRMRHADR 449
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-282 |
2.37e-22 |
|
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: 95.77 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFES-GVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGM-----YGLHQDVHH 97
Cdd:cd16149 2 NILFILTDDQGPWAlGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 98 FNSFDKVQ-SLPLLLSQAGVRTGIIGKKHVGPETVYPFDFAFTEENSSVLQVG------------------RNITRI-KQ 157
Cdd:cd16149 82 PEGYLEGQtTLPEVLQDAGYRCGLSGKWHLGDDAADFLRRRAEAEKPFFLSVNytaphspwgyfaavtgvdRNVGRLlDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 158 LVRKFLqtqDDRPFFLYVALHDpHRCGHsqpqYGAFcEKfGNGEsgmgripdWTPQIYDpQDVMVPYFV---PDTPAARA 234
Cdd:cd16149 162 LEELGL---TENTLVIFTSDNG-FNMGH----HGIW-GK-GNGT--------FPLNMYD-NSVKVPFIIrwpGVVPAGRV 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958663166 235 --DLAAQYttigrmdqDLTPTILDWFSIPYPSyaifgskTIQLTGRSLLP 282
Cdd:cd16149 223 vdSLVSAY--------DFFPTLLELAGVDPPA-------DPRLPGRSFAD 257
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-189 |
2.99e-22 |
|
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: 98.02 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFES-GVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYG----LHQDVHhf 98
Cdd:cd16034 3 NILFIFADQHRAQAlGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGndvpLPPDAP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 99 nSFDKVqslpllLSQAGVRTGIIGKKHV-GPETVYP--------------FDF------------AFTEENSSVLQVGRN 151
Cdd:cd16034 81 -TIADV------LKDAGYRTGYIGKWHLdGPERNDGraddytppperrhgFDYwkgyecnhdhnnPHYYDDDGKRIYIKG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958663166 152 ITRIKQ--LVRKFL--QTQDDRPFFLYVALHDPHRCGHSQPQ 189
Cdd:cd16034 154 YSPDAEtdLAIEYLenQADKDKPFALVLSWNPPHDPYTTAPE 195
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-249 |
1.08e-21 |
|
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: 96.51 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADD-GGFESGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFD 102
Cdd:cd16145 2 NIIFILADDlGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 103 KVQSLPLLLSQAGVRTGIIGKKHVGPETV--YP----FDFAFT------------------------EENSSVLQVGRNI 152
Cdd:cd16145 82 DDVTLAEVLKKAGYATAAFGKWGLGGPGTpgHPtkqgFDYFYGyldqvhahnyypeylwrngekvplPNNVIPPLDEGNN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 153 TRIKQ------LVR----KFLQTQDDRPFFLYVALHDPHrcGHSQpqygafcekfgngesgmgrIPDWTPQIYDPqDVMV 222
Cdd:cd16145 162 AGGGGgtyshdLFTdealDFIRENKDKPFFLYLAYTLPH--APLQ-------------------VPDDGPYKYKP-KDPG 219
|
250 260
....*....|....*....|....*..
gi 1958663166 223 PYFVPDTPAARADLAAQyttIGRMDQD 249
Cdd:cd16145 220 IYAYLPWPQPEKAYAAM---VTRLDRD 243
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-181 |
1.29e-21 |
|
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: 95.74 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFES-GVYNNTAINTPHLDALARHSLIFRNAFTSvSSCSPSRASLLTGLPQHQNGmyglhqdVHHFNSFD 102
Cdd:cd16151 2 NIILIMADDLGYECiGCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNY-------VVFGYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 103 KVQSLPLLLSQAGVRTGIIGKKHVGPETV---YPFDFAFTEenSSVLQV-------GRNITRIKQLVRK----------- 161
Cdd:cd16151 74 KQKTFGHLLKDAGYATAIAGKWQLGGGRGdgdYPHEFGFDE--YCLWQLtetgekySRPATPTFNIRNGkllettegdyg 151
|
170 180 190
....*....|....*....|....*....|...
gi 1958663166 162 ----------FLQTQDDRPFFLY---VALHDPH 181
Cdd:cd16151 152 pdlfadflidFIERNKDQPFFAYypmVLVHDPF 184
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
24-181 |
1.71e-21 |
|
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: 96.10 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFESGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSFDK 103
Cdd:cd16030 4 NVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNS--YFRKVAPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 104 VQSLPLLLSQAGVRTGIIGK---KHVGPE-------TVYPFDFAFTEENSSVLQVGRNIT-------------------- 153
Cdd:cd16030 82 AVTLPQYFKENGYTTAGVGKifhPGIPDGdddpaswDEPPNPPGPEKYPPGKLCPGKKGGkgggggpaweaadvpdeayp 161
|
170 180 190
....*....|....*....|....*....|..
gi 1958663166 154 --RIKQLVRKFLQT--QDDRPFFLYVALHDPH 181
Cdd:cd16030 162 dgKVADEAIEQLRKlkDSDKPFFLAVGFYKPH 193
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
24-320 |
2.62e-21 |
|
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: 94.18 E-value: 2.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADD-GGFESGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYG----LHQDV--- 95
Cdd:cd16032 2 NILLIMADQlTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDnaaeFPADIptf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 96 -HHfnsfdkvqslpllLSQAGVRTGIIGKKH-VGPETVYPFDfaFTEEnssvlqVG-RNITRIKQLVRKflqtQDDRPFF 172
Cdd:cd16032 82 aHY-------------LRAAGYRTALSGKMHfVGPDQLHGFD--YDEE------VAfKAVQKLYDLARG----EDGRPFF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 173 LYVALHDPHRCGHSQPQ-------------YGA---------------------------FCEKFGN--GESGMgripdW 210
Cdd:cd16032 137 LTVSFTHPHDPYVIPQEywdlyvrrarrayYGMvsyvddkvgqlldtlertgladdtiviFTSDHGDmlGERGL-----W 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 211 TPQIYDPQDVMVPYFV--PDTPAARadlaaqyttigRMDQ-----DLTPTILDWFSIPYPSYAifgsktIQLTGRSLLPA 283
Cdd:cd16032 212 YKMSFFEGSARVPLIIsaPGRFAPR-----------RVAEpvslvDLLPTLVDLAGGGTAPHV------PPLDGRSLLPL 274
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958663166 284 LE-AEPPWATVFSSQSHHEVTMSyPMRSVYHQNFRLIH 320
Cdd:cd16032 275 LEgGDSGGEDEVISEYLAEGAVA-PCVMIRRGRWKFIY 311
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-181 |
7.65e-21 |
|
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: 92.05 E-value: 7.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFES-GVYNN----------TAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGL- 91
Cdd:cd16153 3 NILWIITDDQRVDSlSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 92 --HQDVHHFNsfdkvQSLPLLLSQAGVRTGIIGKKHVGPETvypfDFAFTEENSSVLQVGRNITRIKQlvrkflqtqdDR 169
Cdd:cd16153 83 aaHPALDHGL-----PTFPEVLKKAGYQTASFGKSHLEAFQ----RYLKNANQSYKSFWGKIAKGADS----------DK 143
|
170
....*....|..
gi 1958663166 170 PFFLYVALHDPH 181
Cdd:cd16153 144 PFFVRLSFLQPH 155
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-406 |
1.30e-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: 293771 [Multi-domain] Cd Length: 373 Bit Score: 89.98 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFES-GVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMY----GLHQDV--- 95
Cdd:cd16152 3 NVIVFFTDQQRWDTlGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFrngiPLPADEktl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 96 -HHFNsfdkvqslplllsQAGVRTGIIGKKHVGpetVYPFDfAFTeenssvlqvgrnitrikQLVRKFLQT-QDDRPFFL 173
Cdd:cd16152 83 aHYFR-------------DAGYETGYVGKWHLA---GYRVD-ALT-----------------DFAIDYLDNrQKDKPFFL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 174 YVALHDPH----RCGHSQPQYGAfcEKFGN-----------GES--------GM--------GRIPDWTPQ--IYDpqDV 220
Cdd:cd16152 129 FLSYLEPHhqndRDRYVAPEGSA--ERFANfwvppdlaalpGDWaeelpdylGCcerldenvGRIRDALKElgLYD--NT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 221 MVPYF----------------VPDTPAARADLAAQ---YTTIGRMDQ-----DLTPTILDWFSIPYPSYAIfgsktiqlt 276
Cdd:cd16152 205 IIVFTsdhgchfrtrnaeykrSCHESSIRVPLVIYgpgFNGGGRVEElvsliDLPPTLLDAAGIDVPEEMQ--------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 277 GRSLLPALEAEPP-WAT-VFSSQSHHEVTmsypmRSVyhqnfrlihnlsfkmpfpidqdfyvsptfqdllnRT-----AA 349
Cdd:cd16152 276 GRSLLPLVDGKVEdWRNeVFIQISESQVG-----RAI----------------------------------RTdrwkySV 316
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958663166 350 GQPT-GWYKNLQHYYYRERWeLYDISRDPRETRNLAAEPDFAQVLEVLKAQLVKWQWE 406
Cdd:cd16152 317 AAPDkDGWKDSGSDVYVEDY-LYDLEADPYELVNLIGRPEYREVAAELRERLLARMAE 373
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
24-181 |
1.31e-18 |
|
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: 87.52 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGF-ESGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSF- 101
Cdd:cd16157 3 NIILMLMDDMGWgDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNA--HARNAYt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 102 ---------DKVQSLPLLLSQAGVRTGIIGKKHVGPETVY-P----FDFAFTEENSSV-----------------LQVGR 150
Cdd:cd16157 81 pqnivggipDSEILLPELLKKAGYRNKIVGKWHLGHRPQYhPlkhgFDEWFGAPNCHFgpydnkaypnipvyrdwEMIGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958663166 151 --------------NITRI-KQLVRKFLQTQ--DDRPFFLYVAL---HDPH 181
Cdd:cd16157 161 yyeefkidkktgesNLTQIyLQEALEFIEKQhdAQKPFFLYWAPdatHAPV 211
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
24-181 |
2.60e-18 |
|
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: 85.98 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFESGVYNN--TAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTglpqhqnGMYGLHQDVHHFNSF 101
Cdd:cd16161 3 NFLLLFADDLGWGDLGANWapNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMT-------GRLGLRNGVGHNFLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 102 DKVQSLPL-------LLSQAGVRTGIIGKKHVGPETVY-P----FD--FAFTEENSSVLQvgrniTRIKQLVRKFLQ--T 165
Cdd:cd16161 76 TSVGGLPLnettlaeVLRQAGYATGMIGKWHLGQREAYlPnsrgFDyyFGIPFSHDSSLA-----DRYAQFATDFIQraS 150
|
170
....*....|....*.
gi 1958663166 166 QDDRPFFLYVALHDPH 181
Cdd:cd16161 151 AKDRPFFLYAALAHVH 166
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
24-129 |
1.29e-17 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 84.72 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFES-GVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlHQDVhhfNSFD 102
Cdd:PRK13759 8 NIILIMVDQMRGDClGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVG-YGDV---VPWN 83
|
90 100
....*....|....*....|....*..
gi 1958663166 103 KVQSLPLLLSQAGVRTGIIGKKHVGPE 129
Cdd:PRK13759 84 YKNTLPQEFRDAGYYTQCIGKMHVFPQ 110
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
24-181 |
1.20e-16 |
|
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: 81.06 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGF-ESGVYNNTAINTPHLDALARHSLIFRNAFTSvSSCSPSRASLLTGLPQHQNGMYG--LHQDVHHFNS 100
Cdd:cd16029 2 HIVFILADDLGWnDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHgvILAGEPYGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 101 FDKVQsLPLLLSQAGVRTGIIGKKHVG--------------------------------PETVYPFDFAFTEENSSVLQV 148
Cdd:cd16029 81 LNETL-LPQYLKELGYATHLVGKWHLGfytweytptnrgfdsfygyyggaedyythtsgGANDYGNDDLRDNEEPAWDYN 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1958663166 149 GRNITRI-KQLVRKFLQTQD-DRPFFLYVALHDPH 181
Cdd:cd16029 160 GTYSTDLfTDRAVDIIENHDpSKPLFLYLAFQAVH 194
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
24-190 |
1.14e-15 |
|
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: 78.36 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDggfESGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDvhhFNSFDK 103
Cdd:cd16147 3 NIVLILTDD---QDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPP---GGGYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 104 VQS-------LPLLLSQAGVRTGIIGK------KHVGPETVYP-FD-FAFTEENSS----VLQVGRNITR---------- 154
Cdd:cd16147 77 FWQnglerstLPVWLQEAGYRTAYAGKylngygVPGGVSYVPPgWDeWDGLVGNSTyynyTLSNGGNGKHgvsypgdylt 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958663166 155 --IKQLVRKFLQT--QDDRPFFLYVALHDPHRCGHSQPQY 190
Cdd:cd16147 157 dvIANKALDFLRRaaADDKPFFLVVAPPAPHGPFTPAPRY 196
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
24-209 |
1.55e-15 |
|
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: 78.26 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGF-ESGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMY-GLhqdvhhfnsF 101
Cdd:cd16158 3 NIVLLFADDLGYgDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYpGV---------F 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 102 DKVQS--LPL-------LLSQAGVRTGIIGKKH--VGPETVY-PFDFAFTE----------------------------- 140
Cdd:cd16158 74 YPGSRggLPLnettiaeVLKTVGYQTAMVGKWHlgVGLNGTYlPTHQGFDHylgipyshdqgpcqnltcfppnipcfggc 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 141 ----------ENSSVLQVGRNITRIKQLVRKFLQ------TQDDRPFFLYVALHDPHrcghsQPQYGAfcEKFGnGESGM 204
Cdd:cd16158 154 dqgevpcplfYNESIVQQPVDLLTLEERYAKFAKdfiadnAKEGKPFFLYYASHHTH-----YPQFAG--QKFA-GRSSR 225
|
....*
gi 1958663166 205 GRIPD 209
Cdd:cd16158 226 GPFGD 230
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-175 |
1.96e-15 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 77.19 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGF-ESGVYNNTAIN---TPHLDALARHSLIFRNaFTSVSSCSPSRASLLTG---------LPQHQNGMYG 90
Cdd:cd16142 2 NILVILGDDIGWgDLGCYGGGIGRgapTPNIDRLAKEGLRFTS-FYVEPSCTPGRAAFITGrhpirtgltTVGLPGSPGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 91 LHQDVHhfnsfdkvqSLPLLLSQAGVRTGIIGKKHVG--PE---TVYPFDFAFTEENSSVLQ--VGRNITRIKQlvrkfl 163
Cdd:cd16142 81 LPPWEP---------TLAELLKDAGYATAQFGKWHLGdeDGrlpTDHGFDEFYGNLYHTIDEeiVDKAIDFIKR------ 145
|
170
....*....|..
gi 1958663166 164 QTQDDRPFFLYV 175
Cdd:cd16142 146 NAKADKPFFLYV 157
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
24-203 |
5.32e-12 |
|
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: 67.45 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGF-ESGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNS-- 100
Cdd:cd16160 3 NIVLFFADDMGYgDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRVFLPWDIgg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 101 --FDKVqSLPLLLSQAGVRTGIIGKKHVG------------PE--------TVYPF-------------DFA-----FTE 140
Cdd:cd16160 83 lpKTEV-TMAEALKEAGYTTGMVGKWHLGinennhsdgahlPShhgfdfvgTNLPFtnswacddtgrhvDFPdrsacFLY 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663166 141 ENSSVLQVGRNITRIKQLVR----KFLQTQDDRPFFLYVALHDPHrcghsQPQYGA--FCEKFGNGESG 203
Cdd:cd16160 162 YNDTIVEQPIQHEHLTETLVgdakSFIEDNQENPFFLYFSFPQTH-----TPLFASkrFKGKSKRGRYG 225
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-181 |
5.47e-12 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 66.46 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVAD-DGGFESGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMYglhqDVHHFNSF- 101
Cdd:cd16035 2 NILLILTDqERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT----DTLGSPMQp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 102 ---DKVQSLPLLLSQAGVRTGIIGKKHV--GPETVYPFDFAFTEENSSVLQvgrnitrikqlvRKFLQTQDDRPFFLYVA 176
Cdd:cd16035 78 llsPDVPTLGHMLRAAGYYTAYKGKWHLsgAAGGGYKRDPGIAAQAVEWLR------------ERGAKNADGKPWFLVVS 145
|
....*
gi 1958663166 177 LHDPH 181
Cdd:cd16035 146 LVNPH 150
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-127 |
2.07e-11 |
|
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: 65.06 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGFES-GVYN--NTAINTPHLDALARHSLIFRNAFtSVSSCSPSRASLLTglpqhqnGMYGLHQDVHHF-- 98
Cdd:cd16154 2 NILLIIADDQGLDSsAQYSlsSDLPVTPTLDSLANSGIVFDNLW-ATPACSPTRATILT-------GKYGFRTGVLAVpd 73
|
90 100 110
....*....|....*....|....*....|...
gi 1958663166 99 NSFDKVQSLPLLL----SQAGVRTGIIGKKHVG 127
Cdd:cd16154 74 ELLLSEETLLQLLikdaTTAGYSSAVIGKWHLG 106
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
23-186 |
2.83e-10 |
|
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: 60.13 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 23 RNVLLIVADDGGF-ESGVYNNTAINTPHLDALARHSLIFR-NAFTSVSSCSPSRASLLTGLPQHQ-----NGMYGLHQDV 95
Cdd:cd00016 1 KHVVLIVLDGLGAdDLGKAGNPAPTTPNLKRLASEGATFNfRSVSPPTSSAPNHAALLTGAYPTLhgytgNGSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 96 HHFNSFDKVQSLPLLLSQAGVRTGIIGkkhvgpetvypfdfafteenssvlqvgrnitrikqlVRKFL-QTQDDRPFFLY 174
Cdd:cd00016 81 RAAGKDEDGPTIPELLKQAGYRTGVIG------------------------------------LLKAIdETSKEKPFVLF 124
|
170
....*....|..
gi 1958663166 175 VALHDPHRCGHS 186
Cdd:cd00016 125 LHFDGPDGPGHA 136
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
24-127 |
2.92e-10 |
|
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: 61.92 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVADDGGF-ESGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHQNGMyGLHQDVHHFNSFD 102
Cdd:cd16159 3 NIVLFMADDLGIgDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGM-ASSHGMRVILFTA 81
|
90 100 110
....*....|....*....|....*....|..
gi 1958663166 103 KVQSLP-------LLLSQAGVRTGIIGKKHVG 127
Cdd:cd16159 82 SSGGLPpnettfaEVLKQQGYSTALIGKWHLG 113
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
356-409 |
3.45e-07 |
|
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: 48.40 E-value: 3.45e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958663166 356 YKnLQHYYYR-ERWELYDISRDPRETRNLAAEPDFAQVLEVLKAQLVKWQWETHD 409
Cdd:pfam16347 50 YK-LIHFYNDiDEWELYDLQKDPKEMNNVYGDPEYAEVQAELKEELEELRKQYKD 103
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
24-181 |
4.74e-05 |
|
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: 45.22 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 24 NVLLIVAD--DGGFeSGVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLPQHqngmygLHQDVHHFNSF 101
Cdd:cd16171 2 NVVMVMSDsfDGRL-TFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTH------LTESWNNYKGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 102 DK-VQSLPLLLSQAGVRTGIIGKKHV--GPETVYPFDFAFTEENSSVL-QVGR---NITRIKQLVRKFL---QTQD---- 167
Cdd:cd16171 75 DPnYPTWMDRLEKHGYHTQKYGKLDYtsGHHSVSNRVEAWTRDVPFLLrQEGRptvNLVGDRSTVRVMLkdwQNTDkavh 154
|
170 180
....*....|....*....|...
gi 1958663166 168 ---------DRPFFLYVALHDPH 181
Cdd:cd16171 155 wirkeapnlTQPFALYLGLNLPH 177
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
23-269 |
4.78e-05 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 45.80 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 23 RNVLLIVAddggfES------GVYNNTAINTPHLDALARHSLIFRNAFTSVSSCSPSRASLLTGLP-QHQNGMYGLHQDV 95
Cdd:COG1368 235 PNVVVILL-----ESfsdffiGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKRPGQN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 96 HHFnsfdkvqSLPLLLSQAGVRTGIIgkkHVGPET------VYP---FDFAFTEENSSVLQVGRNITRIKQLVRKFLQT- 165
Cdd:COG1368 310 NFP-------SLPSILKKQGYETSFF---HGGDGSfwnrdsFYKnlgFDEFYDREDFDDPFDGGWGVSDEDLFDKALEEl 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 166 -QDDRPFFLYV---ALHDP------------HRCGHSQPQYGA----------FCEKFgnGESGM-------------GR 206
Cdd:COG1368 380 eKLKKPFFAFLitlSNHGPytlpeedkkipdYGKTTLNNYLNAvryadqalgeFIEKL--KKSGWydntifviygdhgPR 457
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958663166 207 IPDWTPQIYDPQDVMVPYFV--PD--TPAARADLAAQYttigrmdqDLTPTILDWFSIPYPSYAIFG 269
Cdd:COG1368 458 SPGKTDYENPLERYRVPLLIysPGlkKPKVIDTVGSQI--------DIAPTLLDLLGIDYPSYYAFG 516
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
23-192 |
1.20e-04 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 43.97 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 23 RNVLLIVADdgGFESGVYnnTAINTPHLDALARHSLIFRNAFTSVSSCS-PSRASLLTGLP--QHQ---NGMY------- 89
Cdd:COG1524 24 KKVVLILVD--GLRADLL--ERAHAPNLAALAARGVYARPLTSVFPSTTaPAHTTLLTGLYpgEHGivgNGWYdpelgrv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 90 ----GLHQDVHHFNSFDKVQSLPLLLSQAGVRTGIIG-KKHVGPETV-YPFDFAFTEENSSVLQVGRNITRIKQLVRkfl 163
Cdd:COG1524 100 vnslSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFwPSFEGSGLIdAARPYPYDGRKPLLGNPAADRWIAAAALE--- 176
|
170 180 190
....*....|....*....|....*....|...
gi 1958663166 164 QTQDDRPFFLYVALHDP----HRCGHSQPQYGA 192
Cdd:COG1524 177 LLREGRPDLLLVYLPDLdyagHRYGPDSPEYRA 209
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
47-187 |
1.68e-04 |
|
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: 43.56 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 47 TPHLDALARHSLIFRNAFTSV-SSCSPSRASLLTGLPQHQNGMYG-----------LHQDVHHFNSFDKVQSLPLL--LS 112
Cdd:pfam01663 20 TPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVGntfydpktgeyLVFVISDPEDPRWWQGEPIWdtAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 113 QAGVRTGII----GKKHVGPETVYPFDFAFTEENSSVLQVGRNITRIKQ--LVRKFLQTQDDRPFFLYVALHDPHRCGHS 186
Cdd:pfam01663 100 KAGVRAAALfwpgSEVDYSTYYGTPPRYLKDDYNNSVPFEDRVDTAVLQtwLDLPFADVAAERPDLLLVYLEEPDYAGHR 179
|
.
gi 1958663166 187 Q 187
Cdd:pfam01663 180 Y 180
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
23-118 |
6.58e-04 |
|
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: 41.51 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 23 RNVLLIVAddggfESgvYNNTAIN--------TPHLDALARHSLIFRNAFTSVSSCSPSRA--SLLTGLPQHQNGMYGLH 92
Cdd:cd16015 1 PNVIVILL-----ES--FSDPYIDkdvggedlTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYT 73
|
90 100
....*....|....*....|....*.
gi 1958663166 93 QDVHHfnsfdKVQSLPLLLSQAGVRT 118
Cdd:cd16015 74 LYKLN-----PLPSLPSILKEQGYET 94
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
23-191 |
8.71e-04 |
|
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: 41.03 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 23 RNVLLIVADdgGFESGvYNNTAINTPHLDALARHSLIF---RNAFTSVSScsPSRASLLTGLP--QHQ---NGMY----- 89
Cdd:cd16018 1 PPLIVISID--GFRWD-YLDRAGLTPNLKRLAEEGVRAkyvKPVFPTLTF--PNHYSIVTGLYpeSHGivgNYFYdpktn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663166 90 --GLHQDVHHFNSFDKVQSLPLLLSQAGVRTGII------GKKHVGPETVYPFDFAFTEENSSVLqvgrNITRIKQLVRK 161
Cdd:cd16018 76 eeFSDSDWVWDPWWIGGEPIWVTAEKAGLKTASYfwpgseVAIIGYNPTPIPLGGYWQPYNDSFP----FEERVDTILEW 151
|
170 180 190
....*....|....*....|....*....|
gi 1958663166 162 FlqtQDDRPFFLYVALHDPHRCGHsqpQYG 191
Cdd:cd16018 152 L---DLERPDLILLYFEEPDSAGH---KYG 175
|
|
| Sulfatase_C |
pfam14707 |
C-terminal region of aryl-sulfatase; |
370-405 |
7.87e-03 |
|
C-terminal region of aryl-sulfatase;
Pssm-ID: 405407 [Multi-domain] Cd Length: 122 Bit Score: 36.14 E-value: 7.87e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1958663166 370 LYDISRDPRETRNLAAE-PDFAQVLEVLKAQLVKWQW 405
Cdd:pfam14707 54 LFDLERDPSEKYPLSPDsPEYPEVLAEIKAAVEEHKA 90
|
|
| |
