|
Name |
Accession |
Description |
Interval |
E-value |
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
36-528 |
0e+00 |
|
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: 566.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 36 KQPNILFIMADDLGYSDLGAFGGEIHTPNIDNLAQEGRLLTDYHTAPTCSPTRSQLISGTDHHLAGIGAMAELTPehlkG 115
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTMAELAT----G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 116 QPGYEGYLNERSLSIAQVLKDNGYRTYISGKWHLGltpesnahakgfdhsftllqgldhhfkqapsafkrnstytedgqi 195
Cdd:cd16025 77 KPGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG--------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 196 ipisalPDDFFSTNYFTDKLLSYLDSGKNSGKPFFAYAAYTAPHWPIQAPAEYREKYRGVYDVGYDAIRNARISRQKQLG 275
Cdd:cd16025 112 ------PDDYYSTDDLTDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKGKYDAGWDALREERLERQKELG 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 276 IIPANFDAAEPiatqnaPQKYGKWDELTAEQKALEARKMEIYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNGAE 355
Cdd:cd16025 186 LIPADTKLTPR------PPGVPAWDSLSPEEKKLEARRMEVYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGAS 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 356 GFvrggygsesgfdnsvanvgtptsyhyigPRWAEVSAAPFHLWKDTAGEGATTAPAIVKLPNQKKAEAT-NHSFASVLD 434
Cdd:cd16025 260 AE----------------------------PGWANASNTPFRLYKQASHEGGIRTPLIVSWPKGIKAKGGiRHQFAHVID 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 435 VFPTLLEYAHIPVPqGQYNGRAINTPSGISWKPLLENKTDtiRPANFSFADELHGSKYAKQGEWKIALQGRPELGTGTWE 514
Cdd:cd16025 312 IAPTILELAGVEYP-KTVNGVPQLPLDGVSLLPTLDGAAA--PSRRRTQYFELFGNRAIRKGGWKAVALHPPPGWGDQWE 388
|
490
....*....|....
gi 515956550 515 LYNIKLDRGERQNV 528
Cdd:cd16025 389 LYDLAKDPSETHDL 402
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
11-552 |
2.15e-111 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 337.24 E-value: 2.15e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 11 SIALFSLSLAGcndndnQENVVSTPKQPNILFIMADDLGYSDLGAFG-GEIHTPNIDNLAQEGRLLTDYH-TAPTCSPTR 88
Cdd:COG3119 3 RLLLLLLALLA------AAAAAAAAKRPNILFILADDLGYGDLGCYGnPLIKTPNIDRLAAEGVRFTNAYvTSPVCSPSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 89 SQLISGTDHHLAGIGAMAEltpehlkgqpGYEGYLNERSLSIAQVLKDNGYRTYISGKWHLgltpesnahakgfdhsftl 168
Cdd:COG3119 77 ASLLTGRYPHRTGVTDNGE----------GYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 169 lqgldhhfkqapsafkrnstytedgqiipisalpddfFSTNYFTDKLLSYLDSGKNSGKPFFAYAAYTAPHWPIQAPAEY 248
Cdd:COG3119 128 -------------------------------------YLTDLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 249 REKYRGvydvgydairnarisrqkQLGIIPANFDAAEpiatqnapqkygkwdeltaEQKALEARKMEIYAGMVENLDANV 328
Cdd:COG3119 171 LDKYDG------------------KDIPLPPNLAPRD-------------------LTEEELRRARAAYAAMIEEVDDQV 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 329 GRIIQYLKQNNLYDNTLIFFVSDNGAEGFVRGgygsesgfdnsvanvgtptsyhyigprwaevsaapFHLWKDTAGEGAT 408
Cdd:COG3119 214 GRLLDALEELGLADNTIVVFTSDNGPSLGEHG-----------------------------------LRGGKGTLYEGGI 258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 409 TAPAIVKLPNQKKAEATNHSFASVLDVFPTLLEYAHIPVPqgqyngraiNTPSGISWKPLLENKTDTIRPANFSFADELH 488
Cdd:COG3119 259 RVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIP---------EDLDGRSLLPLLTGEKAEWRDYLYWEYPRGG 329
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515956550 489 GSKYAKQGEWKIAlqgRPELGTGTWELYNIKLDRGERQNVAQLYPAKVQELLSVYQKYTEKNGV 552
Cdd:COG3119 330 GNRAIRTGRWKLI---RYYDDDGPWELYDLKNDPGETNNLAADYPEVVAELRALLEAWLKELGD 390
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
38-549 |
6.25e-95 |
|
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: 295.61 E-value: 6.25e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGE-IHTPNIDNLAQEGRLLTDYHTAPTCSPTRSQLISGTDHHLAGIgamaelTPEHLKGQ 116
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPiLKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTGV------WHTILGRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 117 pgyegYLNERSLSIAQVLKDNGYRTYISGKWHLGLTPESNAHAKGFDHSFTLLQGldhHFKQAPS---AFKRNSTYTEDG 193
Cdd:cd16146 75 -----RMRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGG---GIGQYPDywgNDYFDDTYYHNG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 194 QIIpisalPDDFFSTNYFTDKLLSYLDsgKNSGKPFFAYAAYTAPHWPIQAPAEYREKYRgvyDVGYDairnarisrqkq 273
Cdd:cd16146 147 KFV-----KTEGYCTDVFFDEAIDFIE--ENKDKPFFAYLATNAPHGPLQVPDKYLDPYK---DMGLD------------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 274 lgiipanfdaaEPIATqnapqkygkwdeltaeqkalearkmeiYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNG 353
Cdd:cd16146 205 -----------DKLAA---------------------------FYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 354 AEGFVRGGYgsesgfdnsVANV-GTPTSYHyigprwaevsaapfhlwkdtagEGATTAPAIVKLPNQKKAEATNHSFASV 432
Cdd:cd16146 247 PAGGVPKRF---------NAGMrGKKGSVY----------------------EGGHRVPFFIRWPGKILAGKDVDTLTAH 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 433 LDVFPTLLEYAHIPVPQGqyngraiNTPSGISWKPLLENKTDTIRPANF---SFADELHGSKYAK----QGEWKIaLQGR 505
Cdd:cd16146 296 IDLLPTLLDLCGVKLPEG-------IKLDGRSLLPLLKGESDPWPERTLfthSGRWPPPPKKKRNaavrTGRWRL-VSPK 367
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 515956550 506 PElgtgTWELYNIKLDRGERQNVAQLYPAKVQELLSVYQKYTEK 549
Cdd:cd16146 368 GF----QPELYDIENDPGEENDVADEHPEVVKRLKAAYEAWWDD 407
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-546 |
2.88e-93 |
|
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: 291.75 E-value: 2.88e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGEIH-TPNIDNLAQEGRLLTD-YHTAPTCSPTRSQLISG--------TDHhlagIGAMAE 107
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYeTPNIDRLAKEGMRFTQaYAAAPVCSPSRASILTGqyparlgiTDV----IPGRRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 108 LTPEHLKGQPGYEGYLNERSLSIAQVLKDNGYRTYISGKWHLGLTPESNAHAKGFDHSFTllqglDHHFKQAPsafkrnS 187
Cdd:cd16144 77 PPDNTKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIG-----GTGNGGPP------S 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 188 TYTEDGQIIP-ISALPDDFFSTNYFTDKLLSYLDsgKNSGKPFFAYAAYTAPHWPIQAPAEYREKYRGVYDVGYDAIRNA 266
Cdd:cd16144 146 YYFPPGKPNPdLEDGPEGEYLTDRLTDEAIDFIE--QNKDKPFFLYLSHYAVHTPIQARPELIEKYEKKKKGLRKGQKNP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 267 risrqkqlgiipanfdaaepiatqnapqkygkwdeltaeqkalearkmeIYAGMVENLDANVGRIIQYLKQNNLYDNTLI 346
Cdd:cd16144 224 -------------------------------------------------VYAAMIESLDESVGRILDALEELGLADNTLV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 347 FFVSDNGaegfvrggygsesGFDNSvanVGTPTsyhyigprwaevSAAPFHLWKDTAGEGATTAPAIVKLPNQKKAEATN 426
Cdd:cd16144 255 IFTSDNG-------------GLSTR---GGPPT------------SNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGSVS 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 427 HSFASVLDVFPTLLEYAHIPVPQGQyngrainTPSGISWKPLLENKTDTIRPANFSFadelHGSKYAKQ----------G 496
Cdd:cd16144 307 DVPVIGTDLYPTFLELAGGPLPPPQ-------HLDGVSLVPLLKGGEADLPRRALFW----HFPHYHGQggrpasairkG 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 515956550 497 EWKIALQgrpeLGTGTWELYNIKLDRGERQNVAQLYPAKVQELLSVYQKY 546
Cdd:cd16144 376 DWKLIEF----YEDGRVELYNLKNDIGETNNLAAEMPEKAAELKKKLDAW 421
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-533 |
5.71e-79 |
|
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: 254.44 E-value: 5.71e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGE-IHTPNIDNLAQEGRLLTD-YHTAPTCSPTRSQLISG-TDHHLAGIGamaeltpehlK 114
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKkIKTPNLDRLAAEGMRFTQhYAGAPVCAPSRASLLTGlHTGHTRVRG----------N 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 115 GQPGYEGYLNERSLSIAQVLKDNGYRTYISGKWHLG-LTPESNAHAKGFDHSFTLL-QG---------LDHHFKQAPSAF 183
Cdd:cd16145 71 SEPGGQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGgPGTPGHPTKQGFDYFYGYLdQVhahnyypeyLWRNGEKVPLPN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 184 KRNSTYTEDGqiipISALPDDFFSTNYFTDKLLSYLDsgKNSGKPFFAYAAYTAPHWPIQAPAEYREKYRGVYDVGYdai 263
Cdd:cd16145 151 NVIPPLDEGN----NAGGGGGTYSHDLFTDEALDFIR--ENKDKPFFLYLAYTLPHAPLQVPDDGPYKYKPKDPGIY--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 264 rnarisrqkqlgiipanfdaaepiatqnapqKYGKWDELTAEqkalearkmeiYAGMVENLDANVGRIIQYLKQNNLYDN 343
Cdd:cd16145 222 -------------------------------AYLPWPQPEKA-----------YAAMVTRLDRDVGRILALLKELGIDEN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 344 TLIFFVSDNGAEgfvrggygSESGFDNsvanvgTPTSYHyigprwaevSAAPFHLWKDTAGEGATTAPAIVKLPNQKKAE 423
Cdd:cd16145 260 TLVVFTSDNGPH--------SEGGSEH------DPDFFD---------SNGPLRGYKRSLYEGGIRVPFIARWPGKIPAG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 424 AT-NHSFASVlDVFPTLLEYAHIPVPQGqyngraINtpsGISWKPLLENKTDTIRPANFSFADELHGSKYA-KQGEWKIA 501
Cdd:cd16145 317 SVsDHPSAFW-DFMPTLADLAGAEPPED------ID---GISLLPTLLGKPQQQQHDYLYWEFYEGGGAQAvRMGGWKAV 386
|
490 500 510
....*....|....*....|....*....|..
gi 515956550 502 lqgRPELGTGTWELYNIKLDRGERQNVAQLYP 533
Cdd:cd16145 387 ---RHGKKDGPFELYDLSTDPGETNNLAAQHP 415
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
37-529 |
1.29e-76 |
|
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: 247.48 E-value: 1.29e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 37 QPNILFIMADDLGYSDLGAFGGE-IHTPNIDNLAQEGRLLTDYH-TAPTCSPTRSQLISGTDHHLAGIGamaeltpeHLK 114
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPlIKTPNIDRLAAEGVRFTDFYaAAPVCSPSRAALLTGRYPVRVGLP--------GVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 115 GQPGYEGYLNERSLSIAQVLKDNGYRTYISGKWHLGLTPES--NAHakGFDHSFTLLQGLDH----HFKQAPSAFKRNST 188
Cdd:cd16026 73 GPPGSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFlpTRH--GFDEYFGIPYSNDMwpfpLYRNDPPGPLPPLM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 189 YTEDgqiipISALPDDFFS-TNYFTDKLLSYLDsgKNSGKPFFAYAAYTAPHWPIQAPAEYREKY-RGVY-DVgydairn 265
Cdd:cd16026 151 ENEE-----VIEQPADQSSlTQRYTDEAVDFIE--RNKDQPFFLYLAHTMPHVPLFASEKFKGRSgAGLYgDV------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 266 arisrqkqlgiipanfdaaepiatqnapqkygkwdeltaeqkalearkmeiyagmVENLDANVGRIIQYLKQNNLYDNTL 345
Cdd:cd16026 217 -------------------------------------------------------VEELDWSVGRILDALKELGLEENTL 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 346 IFFVSDNGAegfvRGGYGSESGfdnsvanvgtptsyhyigprwaevSAAPFHLWKDTAGEGATTAPAIVKLPNQKKAEAT 425
Cdd:cd16026 242 VIFTSDNGP----WLEYGGHGG------------------------SAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTV 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 426 NHSFASVLDVFPTLLEYAHIPVPQgqynGRAINtpsGISWKPLLENKTDTIRPANFSFADELHGsKYAKQGEWKIALQ-- 503
Cdd:cd16026 294 SDELASTMDLLPTLAALAGAPLPE----DRVID---GKDISPLLLGGSKSPPHPFFYYYDGGDL-QAVRSGRWKLHLPtt 365
|
490 500 510
....*....|....*....|....*....|....
gi 515956550 504 --------GRPELGTGTWELYNIKLDRGERQNVA 529
Cdd:cd16026 366 yrtgtdpgGLDPTKLEPPLLYDLEEDPGETYNVA 399
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-529 |
2.84e-64 |
|
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: 215.14 E-value: 2.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGE--IHTPNIDNLAQEGRLLTDYHT-APTCSPTRSQLISGTDHHLAGigamaeltpehLK 114
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDskIPTPNIDRLAAEGMRFTDAHSpSSVCTPSRYGLLTGRYPWRSR-----------LK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 115 GQ--PGYEGYLNERS-LSIAQVLKDNGYRTYISGKWHLGLT-------PESNAHAKGFDHSFTLL-----QGLDHHFkqa 179
Cdd:cd16143 70 GGvlGGFSPPLIEPDrVTLAKMLKQAGYRTAMVGKWHLGLDwkkkdgkKAATGTGKDVDYSKPIKggpldHGFDYYF--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 180 psafkrnstytedgqIIPISALPDDFfstnyfTDKLLSYLDSGKNSGKPFFAYAAYTAPHWPIQAPaeyrEKYRGVYDVG 259
Cdd:cd16143 147 ---------------GIPASEVLPTL------TDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPS----PEFQGKSGAG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 260 ydairnarisrqkqlgiipanfdaaepiatqnapqKYGkwDeltaeqkalearkmeiyagMVENLDANVGRIIQYLKQNN 339
Cdd:cd16143 202 -----------------------------------PYG--D-------------------FVYELDWVVGRILDALKELG 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 340 LYDNTLIFFVSDNGAEGFVRGGYGSESGFDnsvanvgtpTSYHYIGprwaevsaapfhlWKDTAGEGATTAPAIVKLPNQ 419
Cdd:cd16143 226 LAENTLVIFTSDNGPSPYADYKELEKFGHD---------PSGPLRG-------------MKADIYEGGHRVPFIVRWPGK 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 420 KKAEATNHSFASVLDVFPTLLEYAHIPVPQGQyngrainTPSGISWKP-LLENKTDTIRPanfSFADELHGSKYA-KQGE 497
Cdd:cd16143 284 IPAGSVSDQLVSLTDLFATLAAIVGQKLPDNA-------AEDSFSFLPaLLGPKKQEVRE---SLVHHSGNGSFAiRKGD 353
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 515956550 498 WKIALQG----------RPELGTGTWELYNIKLDRGERQNVA 529
Cdd:cd16143 354 WKLIDGTgsggfsyprgKEKLGLPPGQLYNLSTDPGESNNLY 395
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
38-529 |
1.42e-62 |
|
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: 210.08 E-value: 1.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGEIH----TPNIDNLAQEGRLLTDYHTAPTCSPTRSQLISGTDHHLAGIgamaeLTPehl 113
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGrgapTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGL-----TTV--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 114 kGQPGYEGYLNERSLSIAQVLKDNGYRTYISGKWHLGLTPESNAHAKGFDHsftllqgldhhfkqapsaFKRNSTYTEDG 193
Cdd:cd16142 73 -GLPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDE------------------FYGNLYHTIDE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 194 qiipisalpddffstnYFTDKLLSYLDSGKNSGKPFFAYAAYTAPHWPIQAPAEYREKYRGVYdvgydairnarisrqkq 273
Cdd:cd16142 134 ----------------EIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSSGKG----------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 274 lgiipanfdaaepiatqnapqKYGkwdeltaeqkalearkmeiyAGMVEnLDANVGRIIQYLKQNNLYDNTLIFFVSDNG 353
Cdd:cd16142 181 ---------------------KYA--------------------DSMVE-LDDHVGQILDALDELGIADNTIVIFTTDNG 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 354 AEGFV--RGGYGsesgfdnsvanvgtptsyhyigprwaevsaaPFHLWKDTAGEGATTAPAIVKLPNQKKAEATNHSFAS 431
Cdd:cd16142 219 PEQDVwpDGGYT-------------------------------PFRGEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVS 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 432 VLDVFPTLLEYAHIPVP--QGQYNGRAINtpsGISWKPLLENKTDTIRPANFSF--ADELHGSKYakqGEWKIALQGRPE 507
Cdd:cd16142 268 HLDWFPTLAALAGAPDPkdKLLGKDRHID---GVDQSPFLLGKSEKSRRSEFFYfgEGELGAVRW---KNWKVHFKAQED 341
|
490 500 510
....*....|....*....|....*....|.
gi 515956550 508 LGTGTWE---------LYNIKLDRGERQNVA 529
Cdd:cd16142 342 TGGPTGEpfyvltfplIFNLRRDPKERYDVT 372
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
38-529 |
2.00e-62 |
|
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: 210.10 E-value: 2.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGaFGG--EIHTPNIDNLAQEGRLLTDYHTAPTCSPTRSQLISGTDHHLAGIGAMAeLTPEHLKG 115
Cdd:cd16029 1 PHIVFILADDLGWNDVG-FHGsdQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHGV-ILAGEPYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 116 QPgyegyLNERSLsiAQVLKDNGYRTYISGKWHLGL-TPESNAHAKGFDHSFTLLQGLDHHFKQAPSAFKRNSTYTEDGQ 194
Cdd:cd16029 79 LP-----LNETLL--PQYLKELGYATHLVGKWHLGFyTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGGANDYGNDDLRDN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 195 IIPISALPDDfFSTNYFTDKLLSYLDSgKNSGKPFFAYAAYTAPHWPIQAPAEYREKYRGvydvgydairnarisrqkql 274
Cdd:cd16029 152 EEPAWDYNGT-YSTDLFTDRAVDIIEN-HDPSKPLFLYLAFQAVHAPLQVPPEYADPYED-------------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 275 giipanfdaaepiatqnapQKYGKWDeltaeqkalEARKMeiYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNGA 354
Cdd:cd16029 210 -------------------KFAHIKD---------EDRRT--YAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 355 eGFVRGGYGSesgfdNsvanvgtptsyhyigprWaevsaaPFHLWKDTAGEGATTAPAIVKLPN-QKKAEATNHSFASVL 433
Cdd:cd16029 260 -PTGGGDGGS-----N-----------------Y------PLRGGKNTLWEGGVRVPAFVWSPLlPPKRGTVSDGLMHVT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 434 DVFPTLLEYAhipvpqgqyNGRAINTPS--GIS-WKPLLENK----TDTIRPANFSFADELHGSkyAKQGEWKIaLQGRP 506
Cdd:cd16029 311 DWLPTLLSLA---------GGDPDDLPPldGVDqWDALSGGApsprTEILLNIDDITRTTGGAA--IRVGDWKL-IVGKP 378
|
490 500
....*....|....*....|...
gi 515956550 507 elgtgtweLYNIKLDRGERQNVA 529
Cdd:cd16029 379 --------LFNIENDPCERNDLA 393
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
38-530 |
1.43e-59 |
|
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: 201.97 E-value: 1.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGEIHTPNIDNLAQEGRLLTDYH-TAPTCSPTRSQLISGTDHHLAGIGAMAELtpehlkgq 116
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFtTAPVCSPSRSALLTGLYPHQNGAHGLRSR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 117 pgyEGYLNERSLSIAQVLKDNGYRTYISGKWHlgltpESNAHAKGFDHSFTLLQGLDHHFKQAPSAFKrnstytedgqii 196
Cdd:cd16027 73 ---GFPLPDGVKTLPELLREAGYYTGLIGKTH-----YNPDAVFPFDDEMRGPDDGGRNAWDYASNAA------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 197 pisalpdDFFSTnyftdkllsyldsgKNSGKPFFAYAAYTAPHWPIQAPAEYREKYRgVYDVgydairnarisrqkqlgI 276
Cdd:cd16027 133 -------DFLNR--------------AKKGQPFFLWFGFHDPHRPYPPGDGEEPGYD-PEKV-----------------K 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 277 IPANFdaaepiatQNAPqkygkwdeltaeqkalEARK-MEIYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNGAe 355
Cdd:cd16027 174 VPPYL--------PDTP----------------EVREdLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM- 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 356 GFVRGgygsesgfdnsvanvgtptsyhyigprwaevsaapfhlwKDTAGEGATTAPAIVKLPNQKKAEATNHSFASVLDV 435
Cdd:cd16027 229 PFPRA---------------------------------------KGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDL 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 436 FPTLLEYAHIPVPQG-QyngraintpsGISWKPLLENKTDTIRPANFSFADElHGSKYAKQ-----GEWKIALQGRPElg 509
Cdd:cd16027 270 APTLLDLAGIEPPEYlQ----------GRSFLPLLKGEKDPGRDYVFAERDR-HDETYDPIrsvrtGRYKYIRNYMPE-- 336
|
490 500
....*....|....*....|.
gi 515956550 510 tgtwELYNIKLDRGERQNVAQ 530
Cdd:cd16027 337 ----ELYDLKNDPDELNNLAD 353
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
38-450 |
8.29e-59 |
|
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: 195.35 E-value: 8.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGG-EIHTPNIDNLAQEGRLLTD-YHTAPTCSPTRSQLISGTDHHLAGIGamaeltpehlkG 115
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNpDIKTPNLDRLAAEGVRFTNaYVASPVCSPSRASLLTGRYPHRHGVR-----------G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 116 QPGYEGYLNERSLSIAQVLKDNGYRTYISGKWHlgltpesnahakgfdhsftllqgldhhfkqapsafkrnstytedgqi 195
Cdd:cd16022 70 NVGNGGGLPPDEPTLAELLKEAGYRTALIGKWH----------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 196 ipisalpddffstnyftDKLLSYLDSgKNSGKPFFAYAAYTAPHWPIqapaeyrekyrgvydvgydairnarisrqkqlg 275
Cdd:cd16022 103 -----------------DEAIDFIER-RDKDKPFFLYVSFNAPHPPF--------------------------------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 276 iipanfdaaepiatqnapqkygkwdeltaeqkalearkmeIYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNGAE 355
Cdd:cd16022 132 ----------------------------------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDM 171
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 356 GFVRGGYGsesgfdnsvanvgtptsyhyigprwaevsaapfhlWKDTAGEGATTAPAIVKLPNQKKAEATNHSFASVLDV 435
Cdd:cd16022 172 LGDHGLRG-----------------------------------KKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDL 216
|
410
....*....|....*
gi 515956550 436 FPTLLEYAHIPVPQG 450
Cdd:cd16022 217 LPTLLDLAGIEPPEG 231
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-527 |
7.63e-58 |
|
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: 198.18 E-value: 7.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 37 QPNILFIMADDLGYSDLGAFGGE-IHTPNIDNLAQEGRLLTD-YHTAPTCSPTRSQLISGTDHHLAGIgamaeltpehlk 114
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDpVKTPNLDRLAKEGVVFTNaVSNYPVCSPYRASLLTGQYPLTNGV------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 115 gqpgyegYLNERSLS-----IAQVLKDNGYRT-YIsGKWHLGLTPESNAHAK----------GFDHSFTLLQGlDHHFkq 178
Cdd:cd16034 69 -------FGNDVPLPpdaptIADVLKDAGYRTgYI-GKWHLDGPERNDGRADdytppperrhGFDYWKGYECN-HDHN-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 179 apsafkrNSTY-TEDGQIIPISAlpddfFSTNYFTDKLLSYLDSGKNSGKPFFAYAAYTAPHWP-IQAPAEYREKYrgvy 256
Cdd:cd16034 138 -------NPHYyDDDGKRIYIKG-----YSPDAETDLAIEYLENQADKDKPFALVLSWNPPHDPyTTAPEEYLDMY---- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 257 dvgydairnarisRQKQLGIIPanfdaaepiatqNAPqkygkwdeLTAEQKALEARKMEIYAGMVENLDANVGRIIQYLK 336
Cdd:cd16034 202 -------------DPKKLLLRP------------NVP--------EDKKEEAGLREDLRGYYAMITALDDNIGRLLDALK 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 337 QNNLYDNTLIFFVSDNGaegfvrggygsESGFDNSVANVGTPtsyhyigprWAEVSAAPFhlwkdtagegattapaIVKL 416
Cdd:cd16034 249 ELGLLENTIVVFTSDHG-----------DMLGSHGLMNKQVP---------YEESIRVPF----------------IIRY 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 417 PNQKKAEATNHSFASVLDVFPTLLEYAHIPVPQgqyngrainTPSGISWKPLLENKTDTI-RPANFSFADELHGSKYAKQ 495
Cdd:cd16034 293 PGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPD---------TVEGRDLSPLLLGGKDDEpDSVLLQCFVPFGGGSARDG 363
|
490 500 510
....*....|....*....|....*....|....*
gi 515956550 496 GEWKIALQGRPEL---GTGTWELYNIKLDRGERQN 527
Cdd:cd16034 364 GEWRGVRTDRYTYvrdKNGPWLLFDNEKDPYQLNN 398
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
36-541 |
1.74e-57 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 196.63 E-value: 1.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 36 KQPNILFIMADDLGYSDLGAFGG-EIHTPNIDNLAQEGRLLTDYHTA-----PTCSPTRSQLISG-TDHHLAGIGAMAEl 108
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNpEIQTPNLDRLARRGTSFTNAYNMggwsgAVCVPSRAMLMTGrTLFHAPEGGKAAI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 109 tpehlkgqpgyegylNERSLSIAQVLKDNGYRTYISGKWHlgltpesnahakgfdhsftllqgldhhfkqapsafkrnst 188
Cdd:cd16155 80 ---------------PSDDKTWPETFKKAGYRTFATGKWH---------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 189 ytedgqiipisalpddffstNYFTDKLLSYLDSGKNSGKPFFAYAAYTAPHWPIQAPAEYREKYrgvydvGYDAIRnari 268
Cdd:cd16155 105 --------------------NGFADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMY------PPETIP---- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 269 srqkqlgiIPANFDAAEPIatQNAPQKYGkwDELTA----EQKALEARKMEIYAgMVENLDANVGRIIQYLKQNNLYDNT 344
Cdd:cd16155 155 --------LPENFLPQHPF--DNGEGTVR--DEQLApfprTPEAVRQHLAEYYA-MITHLDAQIGRILDALEASGELDNT 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 345 LIFFVSDNGaegfvrggygsesgfdnsvANVGtptSYHYIGprwaevsaapfhlwKDTAGEGATTAPAIVKLPNQKKAEA 424
Cdd:cd16155 222 IIVFTSDHG-------------------LAVG---SHGLMG--------------KQNLYEHSMRVPLIISGPGIPKGKR 265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 425 TNHsFASVLDVFPTLLEYAHIPVPQgqyngrainTPSGISWKPLLENKTDTIRPANF-SFADelhGSKYAKQGEWKIALQ 503
Cdd:cd16155 266 RDA-LVYLQDVFPTLCELAGIEIPE---------SVEGKSLLPVIRGEKKAVRDTLYgAYRD---GQRAIRDDRWKLIIY 332
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 515956550 504 GRpelGTGTWELYNIKLDRGERQNVAQL--YPAKVQELLS 541
Cdd:cd16155 333 VP---GVKRTQLFDLKKDPDELNNLADEpeYQERLKKLLA 369
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-527 |
1.47e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 191.66 E-value: 1.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGE-IHTPNIDNLAQEGRLLTDYHTAPTCSPTRSQLISGTDHHLAGIGAmaeltpehlkgq 116
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGEsYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 117 pgyeGYLNERSLSIAQVLKDNGYRTYISGKWHLG---LTPESNAHAkGFDHsFTLLQGldHHFKQAPSAFKRNSTYTEDG 193
Cdd:cd16151 69 ----GYLDPKQKTFGHLLKDAGYATAIAGKWQLGggrGDGDYPHEF-GFDE-YCLWQL--TETGEKYSRPATPTFNIRNG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 194 QIIPISAlpdDFFSTNYFTDKLLSYLDsgKNSGKPFFAYAAYTAPHWPIQApaeyrekyrgvydvgydairnarisrqkq 273
Cdd:cd16151 141 KLLETTE---GDYGPDLFADFLIDFIE--RNKDQPFFAYYPMVLVHDPFVP----------------------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 274 lgiIPANFDAAEPIATQNAPQKYgkwdeltaeqkalearkmeiYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNG 353
Cdd:cd16151 187 ---TPDSPDWDPDDKRKKDDPEY--------------------FPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 354 aegfvrggygsesgfdnsvanvgTPTSYHYigpRW--AEVSAApfhlwKDTAGEGATTAPAIVKLPNQKKAEATNHSFAS 431
Cdd:cd16151 244 -----------------------THRPITS---RTngREVRGG-----KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVD 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 432 VLDVFPTLLEYAHIPVPqgqyNGRAINtpsGISWKPLLENKTDTIRPANFSFADELHGSKYAKQ----GEWKIALQGRpe 507
Cdd:cd16151 293 FSDFLPTLAELAGAPLP----EDYPLD---GRSFAPQLLGKTGSPRREWIYWYYRNPHKKFGSRfvrtKRYKLYADGR-- 363
|
490 500
....*....|....*....|
gi 515956550 508 lgtgtweLYNIKLDRGERQN 527
Cdd:cd16151 364 -------FFDLREDPLEKNP 376
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
36-539 |
3.70e-55 |
|
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: 191.97 E-value: 3.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 36 KQPNILFIMADDLGYSDLGAFGGEI-HTPNIDNLAQEGRLLTD-YHTAPTCSPTRSQLISGTdhHlagigamaeltpEHL 113
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIvKTPNIDRLAKEGVRFDNaFVTTSICAPSRASILTGQ--Y------------SHR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 114 KGQPGYEGYLNERSL-SIAQVLKDNGYRTYISGKWHLGLtpESNAHAKGFDHSFtllqgldhhfkqapsAFKRNSTYTED 192
Cdd:cd16031 67 HGVTDNNGPLFDASQpTYPKLLRKAGYQTAFIGKWHLGS--GGDLPPPGFDYWV---------------SFPGQGSYYDP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 193 GQIIPISALPDDFFSTNYFTDKLLSYLDSGKNSgKPFFAYAAYTAPHwpiqAPAEYREKYRGVYDvgydairNARISRqk 272
Cdd:cd16031 130 EFIENGKRVGQKGYVTDIITDKALDFLKERDKD-KPFCLSLSFKAPH----RPFTPAPRHRGLYE-------DVTIPE-- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 273 qlgiiPANFD----AAEPIATQNAPQK---YGKWDELTAE--QkaleaRKMEIYAGMVENLDANVGRIIQYLKQNNLYDN 343
Cdd:cd16031 196 -----PETFDdddyAGRPEWAREQRNRirgVLDGRFDTPEkyQ-----RYMKDYLRTVTGVDDNVGRILDYLEEQGLADN 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 344 TLIFFVSDNgaeGFVRGGYGsesgfdnsvanvgtptsyhYIGPRWA-EVSAapfhlwkdtagegatTAPAIVKLPNQKKA 422
Cdd:cd16031 266 TIIIYTSDN---GFFLGEHG-------------------LFDKRLMyEESI---------------RVPLIIRDPRLIKA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 423 EATNHSFASVLDVFPTLLEYAHIPVPQgQYNGRaintpsgiSWKPLLENKTDTIRPANFSFadELHGSKYAKQ------- 495
Cdd:cd16031 309 GTVVDALVLNIDFAPTILDLAGVPIPE-DMQGR--------SLLPLLEGEKPVDWRKEFYY--EYYEEPNFHNvpthegv 377
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 515956550 496 --GEWK-IALQGRPelgtGTWELYNIKLDRGERQNVA--QLYPAKVQEL 539
Cdd:cd16031 378 rtERYKyIYYYGVW----DEEELYDLKKDPLELNNLAndPEYAEVLKEL 422
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
38-445 |
2.73e-50 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 174.92 E-value: 2.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGEIH-TPNIDNLAQEGRLLTDYH-TAPTCSPTRSQLISGTDHHLAGIGAMaeltpehlkg 115
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPtTPFLDRLAEEGLLFSNFYsGGTLTAPSRFALLTGLPPHNFGSYVS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 116 qpgYEGYLNERSLSIAQVLKDNGYRTYISGKWHLGLTPESNAHAKGFDHSFTLLQGLDhhfkqapsafkrNSTYTEDGQI 195
Cdd:pfam00884 71 ---TPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFDKFFGRNTGSD------------LYADPPDVPY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 196 IPisalPDDFFSTNYFTDKLLSYLDsgkNSGKPFFAYAAYTAPHWPIQAPAEYREKYRGVYDvgydairnarisrqkqlg 275
Cdd:pfam00884 136 NC----SGGGVSDEALLDEALEFLD---NNDKPFFLVLHTLGSHGPPYYPDRYPEKYATFKP------------------ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 276 iipanfdaaepiatqnapqkygkwdeltaeQKALEARKMEIYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNGAE 355
Cdd:pfam00884 191 ------------------------------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGES 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 356 gfvrggygsesgfdnsvanVGTPTSYHYIGPRWaevsaapfhlwkdTAGEGATTAPAIVKLPNQKKAEATNHSFASVLDV 435
Cdd:pfam00884 241 -------------------LGEGGGYLHGGKYD-------------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDL 288
|
410
....*....|
gi 515956550 436 FPTLLEYAHI 445
Cdd:pfam00884 289 FPTILDLAGI 298
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-539 |
9.20e-47 |
|
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: 168.94 E-value: 9.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGEI-HTPNIDNLAQEGRLLTD-YHTAPTCSPTRSQLISGTDHHLAGI-------GAMAEL 108
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIvKTPNIDRLAAEGVRFTNaYTPSPVCCPARASLLTGLYPHEHGVlnnvenaGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 109 TPehlkgqPGYEGYLnerslsiaQVLKDNGYRTYISGKWHLGltPESNAhakgfdhsftllqgLDHHFKQapsafkrnst 188
Cdd:cd16033 81 LP------PGVETFS--------EDLREAGYRNGYVGKWHVG--PEETP--------------LDYGFDE---------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 189 ytedgqiipisALPDDFFSTNYFTDKLLSYLDSGKNSGKPFFAYAAYTAPHWPIQAPAEYrekyrgvydvgYDAIRNARI 268
Cdd:cd16033 121 -----------YLPVETTIEYFLADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPY-----------LDMYDPEDI 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 269 SRqkqlgiiPANFD---AAEPIATQNAPQKYGKWDELTAEQKALEARkmeiYAGMVENLDANVGRIIQYLKQNNLYDNTL 345
Cdd:cd16033 179 PL-------PESFAddfEDKPYIYRRERKRWGVDTEDEEDWKEIIAH----YWGYITLIDDAIGRILDALEELGLADDTL 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 346 IFFVSDNG----AEGFVRGGYgseSGFDnsvanvgtpTSYHyigprwaevsaapfhlwkdtagegattAPAIVKLPNQKK 421
Cdd:cd16033 248 VIFTSDHGdalgAHRLWDKGP---FMYE---------ETYR---------------------------IPLIIKWPGVIA 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 422 AEATNHSFASVLDVFPTLLEYAHIPVPqgqyngraiNTPSGISWKPLLENKTDT-IRPANFSfadELHGSKY------AK 494
Cdd:cd16033 289 AGQVVDEFVSLLDLAPTILDLAGVDVP---------PKVDGRSLLPLLRGEQPEdWRDEVVT---EYNGHEFylpqrmVR 356
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 515956550 495 QGEWKIALQgrpelGTGTWELYNIKLDRGERQNVAQL--YPAKVQEL 539
Cdd:cd16033 357 TDRYKYVFN-----GFDIDELYDLESDPYELNNLIDDpeYEEILREM 398
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
36-530 |
4.49e-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: 4.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 36 KQPNILFIMADDLGySDLGAFGGE-IHTPNIDNLAQEGRLLTDYHT-APTCSPTRSQLISGtdhhlagigamaeLTPEHL 113
Cdd:cd16030 1 KKPNVLFIAVDDLR-PWLGCYGGHpAKTPNIDRLAARGVLFTNAYCqQPVCGPSRASLLTG-------------RRPDTT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 114 K--GQPGYEGYLNERSLSIAQVLKDNGYRTYISGK-WHlGLTPESNAHAKGFDHSFTLlQGLDHHFKQAPSAFKRNSTYT 190
Cdd:cd16030 67 GvyDNNSYFRKVAPDAVTLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPPNP-PGPEKYPPGKLCPGKKGGKGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 191 EDGQIIPISALPDDFFSTNYFTDKLLSYLDSGKNSGKPFFAYAAYTAPHWPIQAPAEYREKYRgvydvgydairnarisr 270
Cdd:cd16030 145 GGGPAWEAADVPDEAYPDGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYP----------------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 271 qkqlgiiPANFDAAEPIATQNAP-QKYGKWDELTAEQKALEARKMEIYAGMVENL---------------DANVGRIIQY 334
Cdd:cd16030 208 -------LESIPLPNPFDPIDLPeVAWNDLDDLPKYGDIPALNPGDPKGPLPDEQarelrqayyasvsyvDAQVGRVLDA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 335 LKQNNLYDNTLIFFVSDNGaegfvrggygsesgfdnsvanvgtptsYHyIGP--RWAEVSaapfhLWkdtagEGATTAPA 412
Cdd:cd16030 281 LEELGLADNTIVVLWSDHG---------------------------WH-LGEhgHWGKHT-----LF-----EEATRVPL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 413 IVKLPNQKKAEATNHSFASVLDVFPTLLEYAHIPVPQgqyngraiNTpSGISWKPLLENKTDTIRPANFS-FADELHGSk 491
Cdd:cd16030 323 IIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPP--------CL-EGKSLVPLLKNPSAKWKDAAFSqYPRPSIMG- 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 515956550 492 YA---KQG---EWkialqgRPELGTGTWELYNIKLDRGERQNVAQ 530
Cdd:cd16030 393 YSirtERYrytEW------VDFDKVGAEELYDHKNDPNEWKNLAN 431
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
37-454 |
1.40e-40 |
|
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: 151.08 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 37 QPNILFIMADDLGYSDLGAFGGE--IHTPNIDNLAQEGRLLTDYHTA-PTCSPTRSQLISGTDHHLAGIGAmaELTPEHL 113
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPnaILTPNLDKLAAEGTRFVDWYSAaSVCSPSRASLMTGRLGLRNGVGH--NFLPTSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 114 KGQPgyegyLNERSLsiAQVLKDNGYRTYISGKWHLGLTPESNAHAKGFDHSFTllqgldhhfkqapsafkrnstytedg 193
Cdd:cd16161 79 GGLP-----LNETTL--AEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFG-------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 194 qiIPISalpDDFFSTNYFTDKLLSYLDSGKNSGKPFFAYAAYTAPHWPIQAPAEYrekyrgvydvgydairnarisrqkq 273
Cdd:cd16161 126 --IPFS---HDSSLADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRF------------------------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 274 lgiipanfdaaepiatQNAPQKYGkwdeltaeqkalearkmeIYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNG 353
Cdd:cd16161 176 ----------------QSPTSGRG------------------PYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNG 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 354 AEgfvrgGYGSESGfdnsvANVGTptsyhyigprWAEVSAAPFHLWKDTAGEGATTAPAIVKLPNQKKAEATNHSFASVL 433
Cdd:cd16161 222 PW-----EVKCELA-----VGPGT----------GDWQGNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTL 281
|
410 420
....*....|....*....|..
gi 515956550 434 DVFPTLLEYAHIPVPQGQ-YNG 454
Cdd:cd16161 282 DIFPTVVALAGASLPPGRiYDG 303
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
38-476 |
4.47e-40 |
|
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: 151.26 E-value: 4.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFG-GEIHTPNIDNLAQEGRLLTDYHT-APTCSPTRSQLISGtdHHLAGIGAMAELTPehlkg 115
Cdd:cd16028 1 RNVLFITADQWRADCLSCLGhPLVKTPNLDRLAAEGVRFRNHYTqAAPCGPSRASLYTG--RYLMNHRSVWNGTP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 116 qpgyegyLNERSLSIAQVLKDNGYRTYISGKWHLGLTPESnAHAKGFD--HSFTLLQGLDHHFkqapsafkRNSTYtedg 193
Cdd:cd16028 74 -------LDARHLTLALELRKAGYDPALFGYTDTSPDPRG-LAPLDPRllSYELAMPGFDPVD--------RLDEY---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 194 qiipisalPDDFFSTNYFTDKLLSYLDSGKNsgKPFFAYAAYTAPHWPIQAPAEYREKYRGvyDVGYDAIRNARISRQKQ 273
Cdd:cd16028 134 --------PAEDSDTAFLTDRAIEYLDERQD--EPWFLHLSYIRPHPPFVAPAPYHALYDP--ADVPPPIRAESLAAEAA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 274 LGIIPANFdaAEPIATQNAPQKYGKWDELTAEQKAlEARKmeIYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNG 353
Cdd:cd16028 202 QHPLLAAF--LERIESLSFSPGAANAADLDDEEVA-QMRA--TYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 354 aegfvrggygsesgfdnsvanvgtptsyHYIGPRWaevsaapfhLW-KDTAGEGATTAPAIVKLPNQkKAEAT----NHS 428
Cdd:cd16028 277 ----------------------------EQLGDHW---------LWgKDGFFDQAYRVPLIVRDPRR-EADATrgqvVDA 318
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 515956550 429 FASVLDVFPTLLEYAHIPVPQgQYNGRaintpsgiSWKPLLENKTDTI 476
Cdd:cd16028 319 FTESVDVMPTILDWLGGEIPH-QCDGR--------SLLPLLAGAQPSD 357
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
37-529 |
5.54e-40 |
|
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: 151.47 E-value: 5.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 37 QPNILFIMADDLGYSDLGAFGgEIH--TPNIDNLAQEGRLLTDYHTA-PTCSPTRSQLISG----------TDHHlagig 103
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFG-EPSreTPNLDRMAAEGMLFTDFYSAnPLCSPSRAALLTGrlpirngfytTNAH----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 104 AMAELTPEHL-KGQPGYEGYLNErslsiaqVLKDNGYRTYISGKWHLGLTPESNAHAKGFDHSFTllqGLDHHF-----K 177
Cdd:cd16157 75 ARNAYTPQNIvGGIPDSEILLPE-------LLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWFG---APNCHFgpydnK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 178 QAPS-AFKRNST----YTEDGQIIPISALPDdffSTNYFTDKLLSYLDSGKNSGKPFFAYAAYTAPHWPIQAPAEYREKY 252
Cdd:cd16157 145 AYPNiPVYRDWEmigrYYEEFKIDKKTGESN---LTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFLGTS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 253 -RGVYDvgyDAIRnarisrqkqlgiipanfdaaepiatqnapqkygkwdeltaeqkalearkmeiyagmveNLDANVGRI 331
Cdd:cd16157 222 qRGLYG---DAVM----------------------------------------------------------ELDSSVGKI 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 332 IQYLKQNNLYDNTLIFFVSDNGAEGFVRGGYGSESGfdnsvanvgtptsyhyigprwaevsaaPFHLWKDTAGEGATTAP 411
Cdd:cd16157 241 LESLKSLGIENNTFVFFSSDNGAALISAPEQGGSNG---------------------------PFLCGKQTTFEGGMREP 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 412 AIVKLPNQKKAEATNHSFASVLDVFPTLLEYAHIPVPqgqyNGRAINtpsGISWKPLLENKTDTIRPANFSFADEL---- 487
Cdd:cd16157 294 AIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIP----SDRAID---GIDLLPVLLNGKEKDRPIFYYRGDELmavr 366
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 515956550 488 HGSKYAKQGEWkialqgrpelgTGTWELYNIKLDRGERQNVA 529
Cdd:cd16157 367 LGQYKAHFWTW-----------SNSWEEFRKGINFCPGQNVP 397
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
35-545 |
8.45e-39 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 148.28 E-value: 8.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 35 PKQPNILFIMADDLGYSDLGAFGGE-IHTPNIDNLAQEGRLLTD-YHTAPTCSPTRSQLISGtdhhlagigamaeLTPEH 112
Cdd:PRK13759 4 TKKPNIILIMVDQMRGDCLGCNGNKaVETPNLDMLASEGYNFENaYSAVPSCTPARAALLTG-------------LSQWH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 113 lKGQPGYE-----GYLNErslsIAQVLKDNGYRTYISGKWHlgLTPESNAHakGFDHsfTLL-QGLDHH----------- 175
Cdd:PRK13759 71 -HGRVGYGdvvpwNYKNT----LPQEFRDAGYYTQCIGKMH--VFPQRNLL--GFHN--VLLhDGYLHSgrnedksqfdf 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 176 -------FK-QAPSafkRNSTYTEDG-----QIIPISALPDDFFSTNYFTDKLLSYLdSGKNSGKPFFAYAAYTAPHWPI 242
Cdd:PRK13759 140 vsdylawLReKAPG---KDPDLTDIGwdcnsWVARPWDLEERLHPTNWVGSESIEFL-RRRDPTKPFFLKMSFARPHSPY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 243 QAPAEYREKYRgvydvgyDA-IRNARISRQKQlgiipanfdAAEPIATQNAPQK-YGKWdeltaeQKALEARKMEIYAGM 320
Cdd:PRK13759 216 DPPKRYFDMYK-------DAdIPDPHIGDWEY---------AEDQDPEGGSIDAlRGNL------GEEYARRARAAYYGL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 321 VENLDANVGRIIQYLKQNNLYDNTLIFFVSDNGaegfvrggygsESGFDNsvanvgtptsyhyigprwaevsaapfHLWK 400
Cdd:PRK13759 274 ITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG-----------DMLGDH--------------------------YLFR 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 401 DT-AGEGATTAPAIVKLPNQKKAEATNHSFASVL---DVFPTLLEYAHIPVPqgqyngraiNTPSGISWKPLLENKTDTI 476
Cdd:PRK13759 317 KGyPYEGSAHIPFIIYDPGGLLAGNRGTVIDQVVelrDIMPTLLDLAGGTIP---------DDVDGRSLKNLIFGQYEGW 387
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515956550 477 RPanfsfadELHG--------SKYAKQGEWKIALQgrpeLGTGTWELYNIKLDRGERQNVAQlyPAKVQELLSVYQK 545
Cdd:PRK13759 388 RP-------YLHGehalgyssDNYLTDGKWKYIWF----SQTGEEQLFDLKKDPHELHNLSP--SEKYQPRLREMRK 451
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-529 |
3.76e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 145.46 E-value: 3.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGE-IHTPNIDNLAQEGRLLTDYHTA-PTCSPTRSQLISGTDHHLAGIGAMAELTPEHlkg 115
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPaAVTPNLDALAAEGVRFSNAYCQnPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 116 QPgyegylnerslSIAQVLKDNGYRTYISGKWHLgltpesnahakgfdhsftllqgldhhfkqAPSAFKRNSTYTEDGQI 195
Cdd:cd16150 78 EP-----------NLLKTLKDAGYHVAWAGKNDD-----------------------------LPGEFAAEAYCDSDEAC 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 196 IpisalpddffstnyftDKLLSYLDSgKNSGKPFFAYAAYTAPHWPIQAPaeyrEKYRGVYDvgydaiRNARISRQKQLG 275
Cdd:cd16150 118 V----------------RTAIDWLRN-RRPDKPFCLYLPLIFPHPPYGVE----EPWFSMID------REKLPPRRPPGL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 276 IIPANFDAAEPIATQNapqkygkWDELTaeqkalEARKMEI---YAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDN 352
Cdd:cd16150 171 RAKGKPSMLEGIEKQG-------LDRWS------EERWRELratYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDH 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 353 GaeGFVrGGYG-SE---SGFDNSVANVgtptsyhyigprwaevsaapfhlwkdtagegattaPAIVKLPNQKKAEATNHs 428
Cdd:cd16150 238 G--DYT-GDYGlVEkwpNTFEDCLTRV-----------------------------------PLIIKPPGGPAGGVSDA- 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 429 FASVLDVFPTLLEYAHIPVPQGQYngraintpsGISWKPLLENKTDTIRPANFSFADELHGSKYA-------KQGEWKIA 501
Cdd:cd16150 279 LVELVDIPPTLLDLAGIPLSHTHF---------GRSLLPVLAGETEEHRDAVFSEGGRLHGEEQAmegghgpYDLKWPRL 349
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 515956550 502 LQGR--PELG------TGTW----------ELYNIKLDRGERQNVA 529
Cdd:cd16150 350 LQQEepPEHTkavmirTRRYkyvyrlyepdELYDLEADPLELHNLI 395
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-457 |
1.84e-37 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 138.91 E-value: 1.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFG-GEIHTPNIDNLAQEGRLLTDYHTA-PTCSPTRSQLISGT---DHhlagiGAMAELTPEH 112
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGnSEAVTPNLDRLAAEGVRFENFFCTsPVCSPARASLLTGRmpsQH-----GIHDWIVEGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 113 LKGQPGYEGYLNERSlSIAQVLKDNGYRTYISGKWHLGltpesnahakgfdhsftllqgldhhfkqapsafkrnstyted 192
Cdd:cd16149 76 HGKTKKPEGYLEGQT-TLPEVLQDAGYRCGLSGKWHLG------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 193 gqiipisalpddffstnyftDKLLSYLDSGKNSGKPFFAYAAYTAPHWPiqapaeyrekyrgvydvgydairnarisrqk 272
Cdd:cd16149 113 --------------------DDAADFLRRRAEAEKPFFLSVNYTAPHSP------------------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 273 qlgiipanfdaaepiatqnapqkygkWDeltaeqkalearkmeiYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDN 352
Cdd:cd16149 142 --------------------------WG----------------YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDN 179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 353 gaeGFVRGGYGsesgfdnsVANVGTPTSyhyigprwaevsaaPFHLWkdtagEGATTAPAIVKLPNQKKAEATNHSFASV 432
Cdd:cd16149 180 ---GFNMGHHG--------IWGKGNGTF--------------PLNMY-----DNSVKVPFIIRWPGVVPAGRVVDSLVSA 229
|
410 420
....*....|....*....|....*.
gi 515956550 433 LDVFPTLLEYAHIPVPQGQ-YNGRAI 457
Cdd:cd16149 230 YDFFPTLLELAGVDPPADPrLPGRSF 255
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
38-546 |
1.07e-36 |
|
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: 142.20 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGgeiH----TPNIDNLAQEGRLLTD-YHTAPTCSPTRSQLISGTDHHLAGI--GAMaeltp 110
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYG---HpsssTPNLDRLAANGLRFTDfYSSSPVCSPSRAALLTGRYQVRSGVypGVF----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 111 ehlkgQPGYEGYLNERSLSIAQVLKDNGYRTYISGKWHLGLTPESN--AHAKGFDHSFTLLQGLDHHFKQAPSAFKRN-S 187
Cdd:cd16158 74 -----YPGSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGTylPTHQGFDHYLGIPYSHDQGPCQNLTCFPPNiP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 188 TY-TEDGQIIP--------ISALPDDFFSTNYFTDKLL-SYLDSGKNSGKPFFAYAAYTAPHWPIQAPAEYREKY-RGVY 256
Cdd:cd16158 149 CFgGCDQGEVPcplfynesIVQQPVDLLTLEERYAKFAkDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSsRGPF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 257 DvgyDAIrnarisrqkqlgiipanfdaaepiatqnapqkygkwdeltaeqkalearkMEiyagmvenLDANVGRIIQYLK 336
Cdd:cd16158 229 G---DAL--------------------------------------------------AE--------LDGSVGELLQTLK 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 337 QNNLYDNTLIFFVSDNGAEgFVRGGYGSESGfdnsVANVGTPTSYhyigprwaevsaapfhlwkdtagEGATTAPAIVKL 416
Cdd:cd16158 248 ENGIDNNTLVFFTSDNGPS-TMRKSRGGNAG----LLKCGKGTTY-----------------------EGGVREPAIAYW 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 417 PNQKKAEATnHSFASVLDVFPTLLEYAHIPVPQGQYNgraintpsGISWKPLLENKTDTIRPANF---SFADELHGSKYA 493
Cdd:cd16158 300 PGRIKPGVT-HELASTLDILPTIAKLAGAPLPNVTLD--------GVDMSPILFEQGKSPRQTFFyypTSPDPDKGVFAV 370
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515956550 494 KQGEWKIAL--QGRPELGTG-----------TWE----LYNIKLDRGERQNVAQL--YPAKVQELLSVYQKY 546
Cdd:cd16158 371 RWGKYKAHFytQGAAHSGTTpdkdchpsaelTSHdpplLFDLSQDPSENYNLLGLpeYNQVLKQIQQVKERF 442
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
37-515 |
1.52e-33 |
|
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: 133.95 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 37 QPNILFIMADDLGYSDLGAFGGE-IHTPNIDNLAQEGRLLTdYHTAPT--CSPTRSQLI-------SGTDHHLAG----- 101
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGNDtIRTPNIDRLAKEGVKLT-HHLAAAplCTPSRAAFLtgrypirSGMASSHGMrvilf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 102 IGAMAELTPehlkgqpgyegylNErsLSIAQVLKDNGYRTYISGKWHLGLTPESNahaKGFDHsFTLLQGLDHHFKQAPS 181
Cdd:cd16159 80 TASSGGLPP-------------NE--TTFAEVLKQQGYSTALIGKWHLGLHCESR---NDFCH-HPLNHGFDYFYGLPLT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 182 AFKRNStyTEDGQIIPISALPDDFFSTNY---FTDKLLSYLDSGKNSGKPFFAYAAYTAPHWpiqapaeyrekyrGVYDV 258
Cdd:cd16159 141 NLKDCG--DGSNGEYDLSFDPLFPLLTAFvliTALTIFLLLYLGAVSKRFFVFLLILSLLFI-------------SLFFL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 259 GYdaIRNARIsrqkqLGIIPANFDAAE-PIATQNAPQKygkwdeLTAE-QKALEARKME--------------------- 315
Cdd:cd16159 206 LL--ITNRYF-----NCILMRNHEVVEqPMSLENLTQR------LTKEaISFLERNKERpfllvmsflhvhtalftskkf 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 316 -------IYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNGA------EGFVRGGYgsESGFdnsvanvgtptsyh 382
Cdd:cd16159 273 kgrskhgRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGhleeisVGGEYGGG--NGGI-------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 383 YIGPrwaevsaapfhlwKDTAGEGATTAPAIVKLP-----NQKKAEATNHsfasvLDVFPTLLEYAHIPVPqgqyNGRAI 457
Cdd:cd16159 337 YGGK-------------KMGGWEGGIRVPTIVRWPgvippGSVIDEPTSL-----MDIFPTVAALAGAPLP----SDRII 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515956550 458 NtpsGISWKPLLENKTdTIRPANFSF---ADELHGSKYakqgewkialqgRPELGTGTWEL 515
Cdd:cd16159 395 D---GRDLMPLLTGQE-KRSPHEFLFhycGAELHAVRY------------RPRDGGAVWKA 439
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-521 |
3.54e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 126.12 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGE-IHTPNIDNLAQEGRLLTD-YHTAPTCSPTRSQLISGTDHHLAGIGAMAeltpehlkg 115
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPvVRTPNLDRLAARGTRFENaYTPSPICVPSRASFLTGRYVHETGVWDNA--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 116 qpgyeGYLNERSLSIAQVLKDNGYRTYISGKWHlgltpesnAHAKGFDHSFtllqgldhhfkqapsafkrnsTYTEDgqi 195
Cdd:cd16037 72 -----DPYDGDVPSWGHALRAAGYETVLIGKLH--------FRGEDQRHGF---------------------RYDRD--- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 196 ipisalpddffstnyFTDKLLSYLDSGKNSGKPFFAYAAYTAPHWPIQAPAEYREKYRgvydvgydaiRNARISrqkqlg 275
Cdd:cd16037 115 ---------------VTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLYV----------RRARAA------ 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 276 iipanfdaaepiatqnapqkygkwdeltaeqkalearkmeiYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNGae 355
Cdd:cd16037 164 -----------------------------------------YYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHG-- 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 356 gfvrggygsesgfdnsvANVGTptsyHYIgprWaevsaapfhlWKDTAGEGATTAPAIVKLPNQKKAEaTNHSFASVLDV 435
Cdd:cd16037 201 -----------------DMLGE----RGL---W----------GKSTMYEESVRVPMIISGPGIPAGK-RVKTPVSLVDL 245
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 436 FPTLLEYAHIPVPQGQyngraintpSGISWKPLLENKTDTIRPAnFSfadELH------GSKYAKQGEWK-IALQGRPEl 508
Cdd:cd16037 246 APTILEAAGAPPPPDL---------DGRSLLPLAEGPDDPDRVV-FS---EYHahgspsGAFMLRKGRWKyIYYVGYPP- 311
|
490
....*....|...
gi 515956550 509 gtgtwELYNIKLD 521
Cdd:cd16037 312 -----QLFDLEND 319
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
37-500 |
1.21e-30 |
|
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: 124.46 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 37 QPNILFIMADDLGYSDLGAFGGEIHTPN-IDNLAQEG-RLLTDYHTAPTCSPTRSQLISGTDHHLAGI-GAMAELTPEHL 113
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGpIDDMAAEGiRFTQAYSADSVCTPSRAALLTGRLPIRSGMyGGTRVFLPWDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 114 KGQPGYEgylnersLSIAQVLKDNGYRTYISGKWHLGLTPESNA------HAKGFDH-----SFTLLQGLDHHFKQAPSA 182
Cdd:cd16160 81 GGLPKTE-------VTMAEALKEAGYTTGMVGKWHLGINENNHSdgahlpSHHGFDFvgtnlPFTNSWACDDTGRHVDFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 183 fKRNSTYTEDGQiiPISALPddfFSTNYFTDKLL----SYLDSgkNSGKPFFAYAAYTAPHWPIQAPAEYREK-YRGVYD 257
Cdd:cd16160 154 -DRSACFLYYND--TIVEQP---IQHEHLTETLVgdakSFIED--NQENPFFLYFSFPQTHTPLFASKRFKGKsKRGRYG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 258 vgyDAIRnarisrqkqlgiipanfdaaepiatqnapqkygkwdeltaeqkalearkmeiyagmveNLDANVGRIIQYLKQ 337
Cdd:cd16160 226 ---DNIN----------------------------------------------------------EMSWAVGEVLDTLVD 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 338 NNLYDNTLIFFVSDNG--AEGFVRGGygsesgfdnsvanvgtptsyhyigprwaevSAAPFHLWKDTAGEGATTAPAIVK 415
Cdd:cd16160 245 TGLDQNTLVFFLSDHGphVEYCLEGG------------------------------STGGLKGGKGNSWEGGIRVPFIAY 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 416 LPNQKKAEATnHSFASVLDVFPTLLEYAHIPVPqgqyNGRAINtpsGISWKP-LLENKTDTIRPANFSFADELHGSKYak 494
Cdd:cd16160 295 WPGTIKPRVS-HEVVSTMDIFPTFVDLAGGTLP----TDRIYD---GLSITDlLLGEADSPHDDILYYCCSRLMAVRY-- 364
|
....*.
gi 515956550 495 qGEWKI 500
Cdd:cd16160 365 -GSYKI 369
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-521 |
3.01e-29 |
|
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: 118.99 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFG-GEIH--TPNIDNLAQEGRLLTDYHTAPTCSPTRSQLISGTDHHLAGIgamaeltpehlk 114
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSlSSDLpvTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGV------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 115 GQPGYEGYLNERSLSIAQVLKDN--GYRTYISGKWHLGLTPESNAHAKGFDHSFTLLQGldhhfkQAPSAFkrNSTYTED 192
Cdd:cd16154 69 LAVPDELLLSEETLLQLLIKDATtaGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGILGG------GVQDYY--NWNLTNN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 193 GQIIPIsalpdDFFSTNYFTDKLLSYLDsgkNSGKPFFAYAAYTAPHWPIQAPAeyrekyrgvydvgydairNARISRqk 272
Cdd:cd16154 141 GQTTNS-----TEYATTKLTNLAIDWID---QQTKPWFLWLAYNAPHTPFHLPP------------------AELHSR-- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 273 qlgiipanfdaaepiatqnapqkygkwdELTAEQKALEARKMEIYAGMVENLDANVGRIIQYLKQNNLyDNTLIFFVSDN 352
Cdd:cd16154 193 ----------------------------SLLGDSADIEANPRPYYLAAIEAMDTEIGRLLASIDEEER-ENTIIIFIGDN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 353 gaegfvrggygsesgfdnsvanvGTPTSyhyIGPRWAEVSAApfhlwKDTAGEGATTAPAIVKLPNQKKAEATNHSFASV 432
Cdd:cd16154 244 -----------------------GTPGQ---VVDLPYTRNHA-----KGSLYEGGINVPLIVSGAGVERANERESALVNA 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 433 LDVFPTLLEYAhipvpqgqyNGRAINTPSGISWKPLLENKTDTIRPANFSFADELHGSKYAKQGEWKIALqgrpELGTGT 512
Cdd:cd16154 293 TDLYATIAELA---------GVDAAEIHDSVSFKPLLSDVNASTRQYNYTEYESPTTTGWATRNQYYKLI----ESENGQ 359
|
....*....
gi 515956550 513 WELYNIKLD 521
Cdd:cd16154 360 EELYDLIND 368
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-529 |
1.01e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 111.94 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 37 QPNILFIMADDLGYSDLGAFGGEIH-TPNIDNLAQEGRLLTDYHTA-PTCSPTRSQLISG-----TDHHLAGIGamaelt 109
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDlTPNLDALAEEGVLFENAFTPqPVCGPARACLQTGlypteTGCFRNGIP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 110 pehlkgqpgyegyLNERSLSIAQVLKDNGYRT-YIsGKWHLgltpesnahakgfdhsftllqgldhhfkqapsafkrnST 188
Cdd:cd16152 75 -------------LPADEKTLAHYFRDAGYETgYV-GKWHL-------------------------------------AG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 189 YTEDgqiipisalpddffstnYFTDKLLSYLDSgKNSGKPFFAYAAYTAPH-----WPIQAPAEYREKYRGVYdvgydai 263
Cdd:cd16152 104 YRVD-----------------ALTDFAIDYLDN-RQKDKPFFLFLSYLEPHhqndrDRYVAPEGSAERFANFW------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 264 rnarisrqkqlgiIPANFDAAEpiatqnapqkyGKWDELTAEqkalearkmeiYAGMVENLDANVGRIIQYLKQNNLYDN 343
Cdd:cd16152 159 -------------VPPDLAALP-----------GDWAEELPD-----------YLGCCERLDENVGRIRDALKELGLYDN 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 344 TLIFFVSDNGAEGFVRggygsesgfdnsvanvgtPTSYhyigprwaevsaapfhlwKDTAGEGATTAPAIVKLPNQKKAE 423
Cdd:cd16152 204 TIIVFTSDHGCHFRTR------------------NAEY------------------KRSCHESSIRVPLVIYGPGFNGGG 247
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 424 ATNHsFASVLDVFPTLLEYAHIPVPqgqyngraiNTPSGISWKPLLENKTDTIRPANFSFADELHGSKYAKQGEWKIA-- 501
Cdd:cd16152 248 RVEE-LVSLIDLPPTLLDAAGIDVP---------EEMQGRSLLPLVDGKVEDWRNEVFIQISESQVGRAIRTDRWKYSva 317
|
490 500 510
....*....|....*....|....*....|....
gi 515956550 502 ---LQGRPELGTGT---WELYNIKLDRGERQNVA 529
Cdd:cd16152 318 apdKDGWKDSGSDVyveDYLYDLEADPYELVNLI 351
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
38-527 |
5.80e-26 |
|
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: 110.93 E-value: 5.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGG-EIHTPNIDNLAQEG-RLLTDYHTAPTCSPTRSQLISGTDHHLAGIGA--MAeltpehl 113
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNkAMKTPNLDRLAAEGvRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTncMA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 114 kgqpgyegyLNERSLSIAQVLKDNGYRT-YIsGKWHL--------GLTPEsnahakGFD--HSFTLLQGLDHHFKQAPSA 182
Cdd:cd16156 74 ---------LGDNVKTIGQRLSDNGIHTaYI-GKWHLdggdyfgnGICPQ------GWDpdYWYDMRNYLDELTEEERRK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 183 FKR--NSTYTEDgqiipisaLPDDFFSTNYFTDKLLSYLDsgKNSGKPFFAYAAYTAPHWPIQAPAEYREKYRGVYdvgy 260
Cdd:cd16156 138 SRRglTSLEAEG--------IKEEFTYGHRCTNRALDFIE--KHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFE---- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 261 dairnarisrqkqLGIIPANFDAAEpiatqNAPQKYGKWdeltAEQKALEAR-----KMEIYAGMVENLDANVGRIIQYL 335
Cdd:cd16156 204 -------------FPKGENAYDDLE-----NKPLHQRLW----AGAKPHEDGdkgtiKHPLYFGCNSFVDYEIGRVLDAA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 336 KQNnlYDNTLIFFVSDNGaegfvrggygsESGFDNSVANVGtPTSYHyigprwaEVSAAPFhlwkdtagegattapaIVK 415
Cdd:cd16156 262 DEI--AEDAWVIYTSDHG-----------DMLGAHKLWAKG-PAVYD-------EITNIPL----------------IIR 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 416 LPNQKKAEATNHSFASVLDVFPTLLEYAHIPVPQgQYNGRAIntpsgiswkplLENKTDTIRPANFSFADELHgsKY--- 492
Cdd:cd16156 305 GKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPK-VLEGESI-----------LATIEDPEIPENRGVFVEFG--RYevd 370
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 515956550 493 ------------AKQGEWKIALQgrpelGTGTWELYNIKLDRGERQN 527
Cdd:cd16156 371 hdgfggfqpvrcVVDGRYKLVIN-----LLSTDELYDLEKDPYEMHN 412
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
38-521 |
1.55e-25 |
|
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: 107.28 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGEI-HTPNIDNLAQEGRLLTD-YHTAPTCSPTRSQLISGtdhHLAG-IGAM---AELTPE 111
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVvKTPNLDRLAARGVVFDNaYCNSPLCAPSRASMMTG---RLPSrIGAYdnaAEFPAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 112 hlkgQPGYEGYLneRSLsiaqvlkdnGYRTYISGKWHLgLTPEsNAHakGFDHsftllqgldhhfkqapsafkrnstyte 191
Cdd:cd16032 78 ----IPTFAHYL--RAA---------GYRTALSGKMHF-VGPD-QLH--GFDY--------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 192 dgqiipisalpDD---FFSTNYFTDKllsyldSGKNSGKPFFAYAAYTAPHWPIQAPAEYREKYrgvydvgydaIRNARI 268
Cdd:cd16032 112 -----------DEevaFKAVQKLYDL------ARGEDGRPFFLTVSFTHPHDPYVIPQEYWDLY----------VRRARR 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 269 SrqkqlgiipanfdaaepiatqnapqkygkwdeltaeqkalearkmeiYAGMVENLDANVGRIIQYLKQNNLYDNTLIFF 348
Cdd:cd16032 165 A-----------------------------------------------YYGMVSYVDDKVGQLLDTLERTGLADDTIVIF 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 349 VSDNG---AEgfvRGgygsesgfdnsvanvgtptsyhyigprwaevsaapfhLW-KDTAGEGATTAPAIVKLPNQKKAE- 423
Cdd:cd16032 198 TSDHGdmlGE---RG-------------------------------------LWyKMSFFEGSARVPLIISAPGRFAPRr 237
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 424 -ATNhsfASVLDVFPTLLEYAHIPVPQgqyngrAINTPSGISWKPLLENKTDTIRPANFS-FADElhGSkYA-----KQG 496
Cdd:cd16032 238 vAEP---VSLVDLLPTLVDLAGGGTAP------HVPPLDGRSLLPLLEGGDSGGEDEVISeYLAE--GA-VApcvmiRRG 305
|
490 500
....*....|....*....|....*.
gi 515956550 497 EWK-IALQGRPELgtgtweLYNIKLD 521
Cdd:cd16032 306 RWKfIYCPGDPDQ------LFDLEAD 325
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
37-449 |
2.57e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 105.54 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 37 QPNILFIMADDLGYSDLGAFG-----------GEIHTPNIDNLAQEGRLLTD-YHTAPTCSPTRSQLISGtdhhlagiga 104
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNnahtgksesrlGYVESPNIDALAAEGVLFTNaYCNSPVCVPSRTSMLTG---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 105 maelTPEHLKGQPGYEGYLN---ERSLSIAQVLKDNGYRTYISGKWHLGltpesnahakgfdhSFTLlqgldhHFKQAPS 181
Cdd:cd16153 71 ----RYPHRTGVYGFEAAHPaldHGLPTFPEVLKKAGYQTASFGKSHLE--------------AFQR------YLKNANQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 182 AFKRNSTYTEDGqiipisalPDdffstnyftdkllsyldsgknSGKPFFAYAAYTAPHWPIQAPAEYREKYRgvydvgyd 261
Cdd:cd16153 127 SYKSFWGKIAKG--------AD---------------------SDKPFFVRLSFLQPHTPVLPPKEFRDRFD-------- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 262 airnarisrqkqlgiipanfdaaepiatqnapqkygkwdeltaeqkalearkmeiYAGMVENLDANVGRIIQYLKQNNLY 341
Cdd:cd16153 170 -------------------------------------------------------YYAFCAYGDAQVGRAVEAFKAYSLK 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 342 ---DNTLIFFVSDNGAEgfvRGGYGSESGFdnsvanVGTPTSYHyigprwaevsaapfhlwkdtagegattAPAIVKLPN 418
Cdd:cd16153 195 qdrDYTIVYVTGDHGWH---LGEQGILAKF------TFWPQSHR---------------------------VPLIVVSSD 238
|
410 420 430
....*....|....*....|....*....|...
gi 515956550 419 QKKAEAT--NHSFASVLDVFPTLLEYAHIPVPQ 449
Cdd:cd16153 239 KLKAPAGkvRHDFVEFVDLAPTLLAAAGVDVDA 271
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
37-353 |
1.20e-23 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 103.01 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 37 QPNILFIMADDLgysDLGAFGGEIHTPNIDNLAQEGRLLTDYHTA-PTCSPTRSQLISG--------TDHHLAGIGAMAE 107
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPMPKTKKLLADQGTTFTNAFVTtPLCCPSRASILTGqyahnhgvTNNSPPGGGYPKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 108 ltpehlkgqpgYEGYLNERSLSIAqvLKDNGYRTYISGKwHL---GLTPESNAHAKGFDHSFTLLQgldhhfkqaPSAFk 184
Cdd:cd16147 78 -----------WQNGLERSTLPVW--LQEAGYRTAYAGK-YLngyGVPGGVSYVPPGWDEWDGLVG---------NSTY- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 185 RNSTYTEDGQIIPISALPDDFfSTNYFTDKLLSYLDSGKNSGKPFFAYAAYTAPHWPIQAPAEYREKYRGVYDvgydair 264
Cdd:cd16147 134 YNYTLSNGGNGKHGVSYPGDY-LTDVIANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFPNVTA------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 265 narisrqkqlgiiPANFDAAEPIATQNAPqkygkW----DELTAEQkalEARKMEIYAGMVENL---DANVGRIIQYLKQ 337
Cdd:cd16147 206 -------------PPRPPPNNPDVSDKPH-----WlrrlPPLNPTQ---IAYIDELYRKRLRTLqsvDDLVERLVNTLEA 264
|
330
....*....|....*.
gi 515956550 338 NNLYDNTLIFFVSDNG 353
Cdd:cd16147 265 TGQLDNTYIIYTSDNG 280
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-451 |
4.84e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 98.77 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGE-IHTPNIDNLAQEGRLLTD-YHTAPTCSPTRSQLISGTDHHLAGIgamaeltpehlkg 115
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDrVTTPNLDRLAAEGVVFDNhYSGSNPTLPSRFSLFTGLYPFYHGV------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 116 qpgYEGYLNERSLSIAQVLKDNGYRT-YISGKWHLGLTPESNahaKGFDHS-FTLLQGLDHHFKQAPSAFKRnstytedg 193
Cdd:cd16148 68 ---WGGPLEPDDPTLAEILRKAGYYTaAVSSNPHLFGGPGFD---RGFDTFeDFRGQEGDPGEEGDERAERV-------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 194 qiipisalpddffstnyfTDKLLSYLDSGKNSgKPFFAYAAYTAPHWPiqapaeYRekyrgvydvgydairnarisrqkq 273
Cdd:cd16148 134 ------------------TDRALEWLDRNADD-DPFFLFLHYFDPHEP------YL------------------------ 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 274 lgiipanfdaaepiatqnapqkygkwdeltaeqkalearkmeiYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNG 353
Cdd:cd16148 165 -------------------------------------------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 354 AEGFVRGGYGSE-SGFDNSVANVgtptsyhyigprwaevsaapfhlwkdtagegattaPAIVKLPNQKKAEATNHsFASV 432
Cdd:cd16148 202 EEFGEHGLYWGHgSNLYDEQLHV-----------------------------------PLIIRWPGKEPGKRVDA-LVSH 245
|
410 420
....*....|....*....|..
gi 515956550 433 LDVFPTLLEYAHIPVP---QGQ 451
Cdd:cd16148 246 IDIAPTLLDLLGVEPPdysDGR 267
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
38-440 |
8.96e-16 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 77.08 E-value: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFGGEI-HTPNIDNLAQEGRLLTDYHTAPTCS--PTRSQLISGTDHHLAGIGAMAELTPEhlk 114
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPApTTPNLKRLASEGATFNFRSVSPPTSsaPNHAALLTGAYPTLHGYTGNGSADPE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 115 gQPGYEGYLNERSLSIAQVLKDNGYRTyisgkwhlgltpesnahakgfdhsftLLQGLDHHFKQapsafkrnstytedgq 194
Cdd:cd00016 78 -LPSRAAGKDEDGPTIPELLKQAGYRT--------------------------GVIGLLKAIDE---------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 195 iipisalpddffstnyftdkllsyldsgKNSGKPFFAYAAYTAPHWPIQAPAeyrekyrgvydvgydairnarisrqkql 274
Cdd:cd00016 115 ----------------------------TSKEKPFVLFLHFDGPDGPGHAYG---------------------------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 275 giipanfdaaepiatqnapqkygkwdeltaeqkaleaRKMEIYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNGA 354
Cdd:cd00016 139 -------------------------------------PNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG 181
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 355 EGFVRGGYGSESgfdnsvanvGTPTSYHYiGPRwaevsaAPFHLWKDTAgegattapaivklpnqkKAEATNHSFASVLD 434
Cdd:cd00016 182 IDKGHGGDPKAD---------GKADKSHT-GMR------VPFIAYGPGV-----------------KKGGVKHELISQYD 228
|
....*.
gi 515956550 435 VFPTLL 440
Cdd:cd00016 229 IAPTLA 234
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-479 |
6.22e-14 |
|
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: 72.63 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLGYSDLGAFG-GEIHTPNIDNLAQEGRLLTDYHTAPT-CSPTRSQLISGtdHHLAGIGaMAELTPehlkg 115
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGwAALNLPARERLAANGLSFENHYTAACmCSPSRSTLYTG--LHPQQTG-VTDTLG----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 116 qPGYEGYLNERSLSIAQVLKDNGYRTYISGKWHLgltpesNAHAKGfdhsftllqgldhhfkqapsAFKRNSTYTEDGQI 195
Cdd:cd16035 73 -SPMQPLLSPDVPTLGHMLRAAGYYTAYKGKWHL------SGAAGG--------------------GYKRDPGIAAQAVE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 196 ipisalpddffstnyftdkLLSYLDSGKNSGKPFFAYAAYTAPH---WPIQAPAEYREKyrgvydvgydairnarisrqk 272
Cdd:cd16035 126 -------------------WLRERGAKNADGKPWFLVVSLVNPHdimFPPDDEERWRRF--------------------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 273 qlgiipANFdaaepiatqnapqkygkwdeltaeqkalearkmeiYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDN 352
Cdd:cd16035 166 ------RNF-----------------------------------YYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDH 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 353 G----AEGFVRGGYgsesgfdnsvanvgtptsyhyigprwaevsaapfhlwkdTAGEGATTAPAIVKLPNQKKAEATNHS 428
Cdd:cd16035 205 GemggAHGLRGKGF---------------------------------------NAYEEALHVPLIISHPDLFGTGQTTDA 245
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 515956550 429 FASVLDVFPTLLEYAHIPVPQGQYNGRAIntpSGISWKPLLENK-TDTIRPA 479
Cdd:cd16035 246 LTSHIDLLPTLLGLAGVDAEARATEAPPL---PGRDLSPLLTDAdADAVRDG 294
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
23-455 |
7.14e-14 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 74.30 E-value: 7.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 23 NDNDNQENVVSTPKQPNILFIMADDLGYSDLGAFGGEIH-TPNIDNLAQEGrLLTDYHTAPTCSPTRSQLISgtdhhLAG 101
Cdd:COG1368 220 KSNRPTPNPFGPAKKPNVVVILLESFSDFFIGALGNGKDvTPFLDSLAKES-LYFGNFYSQGGRTSRGEFAV-----LTG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 102 IGAMAELTPEHLKGQPGYEgylnerslSIAQVLKDNGYRT-YISGkwhlgltpesnaHAKGFD--HSFTLLQGLDHhfkq 178
Cdd:COG1368 294 LPPLPGGSPYKRPGQNNFP--------SLPSILKKQGYETsFFHG------------GDGSFWnrDSFYKNLGFDE---- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 179 apsafkrnstytedgqIIPISALPDDFFST-----NYFTDKLLSYLDsgkNSGKPFFAYAAYTAPHWPiqapaeyrekyr 253
Cdd:COG1368 350 ----------------FYDREDFDDPFDGGwgvsdEDLFDKALEELE---KLKKPFFAFLITLSNHGP------------ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 254 gvYDVgydairnarisrqkqlgiipanfdaaepiatqnaPQKYGKWDEltaeqkaLEARKMEIYAGMVENLDANVGRIIQ 333
Cdd:COG1368 399 --YTL----------------------------------PEEDKKIPD-------YGKTTLNNYLNAVRYADQALGEFIE 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 334 YLKQNNLYDNTLIFFVSDngaegfvrggygsesgfdnsvanvgtptsyHYI---GPRWAEVSAAPFHLwkdtagegatta 410
Cdd:COG1368 436 KLKKSGWYDNTIFVIYGD------------------------------HGPrspGKTDYENPLERYRV------------ 473
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 515956550 411 PAIVKLPNQKKAEaTNHSFASVLDVFPTLLEYAHIPVPQGQYNGR 455
Cdd:COG1368 474 PLLIYSPGLKKPK-VIDTVGSQIDIAPTLLDLLGIDYPSYYAFGR 517
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
38-444 |
1.17e-10 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 62.70 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDLG--YSDLGAFGGEIhTPNIDNLAQEGRLLTDYHTAPTCSPT-RSQLISgtdhhLAGIgamaeltPEHLK 114
Cdd:cd16015 1 PNVIVILLESFSdpYIDKDVGGEDL-TPNLNKLAKEGLYFGNFYSPGFGGGTaNGEFEV-----LTGL-------PPLPL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 115 GQPGYEGYLNERSLSIAQVLKDNGYRTYIsgkWHlgltpesnAHAKGFD--HSFTLLQGLDHhfkqapsaFKRNSTYTED 192
Cdd:cd16015 68 GSGSYTLYKLNPLPSLPSILKEQGYETIF---IH--------GGDASFYnrDSVYPNLGFDE--------FYDLEDFPDD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 193 GQIIPISALPDDffstnYFTDKLLSYLDsgKNSGKPFFAYAAYTAPHWPIQAPAEYREKYRGVYDvgydairnarisrqk 272
Cdd:cd16015 129 EKETNGWGVSDE-----SLFDQALEELE--ELKKKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEE--------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 273 qlgiipanfdaaepiatqnapqkygkwdeltaeqkalEARKMEIYAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDN 352
Cdd:cd16015 187 -------------------------------------DKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDH 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 353 GAegfvrggygseSGFDNSVANVGTPTSYHYIgprwaevsaapfhlwkdtagegattaPAIVKLPNQKKAEaTNHSFASV 432
Cdd:cd16015 230 LP-----------SLGSDYDETDEDPLDLYRT--------------------------PLLIYSPGLKKPK-KIDRVGSQ 271
|
410
....*....|..
gi 515956550 433 LDVFPTLLEYAH 444
Cdd:cd16015 272 IDIAPTLLDLLG 283
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
38-499 |
7.40e-10 |
|
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: 61.02 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 38 PNILFIMADDL-GYSDLGAFGGEIHTPNIDNLAQEGRL-LTDYHTAPTCSPTRSQLISGTDHHLAGigamaelTPEHLKG 115
Cdd:cd16171 1 PNVVMVMSDSFdGRLTFRPGNQVVDLPYINFMKQHGSVfLNAYTNSPICCPSRAAMWSGLFTHLTE-------SWNNYKG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 116 -QPGYEGYLNerslsiaqVLKDNGYRTYISGK--WHLGLTPESN-AHAKGFDHSFTLLQgldhhfKQAPSA-FKRNSTYT 190
Cdd:cd16171 74 lDPNYPTWMD--------RLEKHGYHTQKYGKldYTSGHHSVSNrVEAWTRDVPFLLRQ------EGRPTVnLVGDRSTV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 191 E----DGQIipisalpddffstnyfTDKLLSYL-DSGKNSGKPFFAYAAYTAPHwpiqapaEYREKYRGVydvGYDAIRN 265
Cdd:cd16171 140 RvmlkDWQN----------------TDKAVHWIrKEAPNLTQPFALYLGLNLPH-------PYPSPSMGE---NFGSIRN 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 266 ARisrqkqlgiipanfdaaepiatqnapqkygkwdeltaeqkalearkmEIYAGMVENLDANVGRIIQYLKQNNLYDNTL 345
Cdd:cd16171 194 IR-----------------------------------------------AFYYAMCAETDAMLGEIISALKDTGLLDKTY 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 346 IFFVSDNGaegfvrggygsesgfdnsvanvgtptsyhyigprwaEVSAAPFHLWKDTAGEGATTAPAIVKLPNQKKAEAT 425
Cdd:cd16171 227 VFFTSDHG------------------------------------ELAMEHRQFYKMSMYEGSSHVPLLIMGPGIKAGQQV 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515956550 426 NhSFASVLDVFPTLLEYAHIPVPQGQyngraintpSGISWKPLLENKTDTIRPA-----NFSFAdELHG-----SKYA-K 494
Cdd:cd16171 271 S-DVVSLVDIYPTMLDIAGVPQPQNL---------SGYSLLPLLSESSIKESPSrvphpDWVLS-EFHGcnvnaSTYMlR 339
|
....*
gi 515956550 495 QGEWK 499
Cdd:cd16171 340 TNSWK 344
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
320-354 |
1.60e-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: 43.95 E-value: 1.60e-04
10 20 30
....*....|....*....|....*....|....*
gi 515956550 320 MVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNGA 354
Cdd:pfam01663 190 ALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGM 224
|
|
| DUF4994 |
pfam16385 |
Domain of unknown function; This family around 100 residues locates in the C-terminal of some ... |
515-539 |
1.71e-04 |
|
Domain of unknown function; This family around 100 residues locates in the C-terminal of some uncharacterized proteins in various Bacteroides and Prevotella species. The function of this family remains unknown.
Pssm-ID: 406720 [Multi-domain] Cd Length: 98 Bit Score: 40.74 E-value: 1.71e-04
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
320-353 |
9.79e-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: 9.79e-04
10 20 30
....*....|....*....|....*....|....
gi 515956550 320 MVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNG 353
Cdd:cd16018 184 ALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG 217
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
317-353 |
1.21e-03 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 41.27 E-value: 1.21e-03
10 20 30
....*....|....*....|....*....|....*..
gi 515956550 317 YAGMVENLDANVGRIIQYLKQNNLYDNTLIFFVSDNG 353
Cdd:COG1524 207 YRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| |
