|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
22-500 |
0e+00 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 873.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 22 AYAQKHPHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLGYGKVS 101
Cdd:PRK13759 1 MVQTKKPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 102 PE-YKYEMPQMLKDAGYYTFGIGKMHWHPQRIKHGFEGTLLDE----SGRVEDE---NFTSDYRQWFQTKAPGKNPDATG 173
Cdd:PRK13759 81 PWnYKNTLPQEFRDAGYYTQCIGKMHVFPQRNLLGFHNVLLHDgylhSGRNEDKsqfDFVSDYLAWLREKAPGKDPDLTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 174 IGWNDH--TASIYKLPENLHPTYWTGEMACELISNYDPTnKPLFLKVSFARPHSPYDPPQRYLDMYKDALIPDPAIGDWc 251
Cdd:PRK13759 161 IGWDCNswVARPWDLEERLHPTNWVGSESIEFLRRRDPT-KPFFLKMSFARPHSPYDPPKRYFDMYKDADIPDPHIGDW- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 252 gKYAKKLNPEETAQDAPYGNFGNEYARNSRRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHWRK 331
Cdd:PRK13759 239 -EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 332 TYPYEGSTHVPYIVKWPsANHVTPGKT---DAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKGMETNWRKYLDLEHA 408
Cdd:PRK13759 318 GYPYEGSAHIPFIIYDP-GGLLAGNRGtviDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFGQYEGWRPYLHGEHA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 409 TCYSDDNYwcaLTDGKIKYIWRIHTGTEELFDLTQDPQELHNAVNDKKYRRQLTEMRNEMIRHLSERGEEFVKDGRLVVK 488
Cdd:PRK13759 397 LGYSSDNY---LTDGKWKYIWFSQTGEEQLFDLKKDPHELHNLSPSEKYQPRLREMRKKLVDHLRGREEGFVKDGKLVVG 473
|
490
....*....|..
gi 2176971269 489 EKTMLYGPHYPE 500
Cdd:PRK13759 474 ELVKLYLPHYPK 485
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-478 |
3.88e-127 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 375.76 E-value: 3.88e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 1 MNILINLKYTLAVTAgvcsSFAYAQKHPHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPAR 80
Cdd:COG3119 1 MKRLLLLLLALLAAA----AAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 81 AGLLTGLSPWHHGLLGYGKVS----PEYKYEMPQMLKDAGYYTFGIGKMHwhpqrikhgfegtlldesgrvedenftsdy 156
Cdd:COG3119 77 ASLLTGRYPHRTGVTDNGEGYngglPPDEPTLAELLKEAGYRTALFGKWH------------------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 157 rqwfqtkapgknpdatgigwndhtasiyklpenLHPTYWTGEMACELISNYDPTNKPLFLKVSFARPHSPYDPPQRYLDM 236
Cdd:COG3119 127 ---------------------------------LYLTDLLTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 237 YKDALIPDPAIGDWcgkyakklnpeetaqdapyGNFGNEYARNSRRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFV 316
Cdd:COG3119 174 YDGKDIPLPPNLAP-------------------RDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 317 SDHGDMMGDH-YHWRKTYPYEGSTHVPYIVKWPsaNHVTPGKT-DAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKG 394
Cdd:COG3119 235 SDNGPSLGEHgLRGGKGTLYEGGIRVPLIVRWP--GKIKAGSVsDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 395 METNWRKYLDLEhatcYSDDNYWCALTDGKIKYI-WRIHTGTEELFDLTQDPQELHNAVNDkkYRRQLTEMRNEMIRHLS 473
Cdd:COG3119 313 EKAEWRDYLYWE----YPRGGGNRAIRTGRWKLIrYYDDDGPWELYDLKNDPGETNNLAAD--YPEVVAELRALLEAWLK 386
|
....*
gi 2176971269 474 ERGEE 478
Cdd:COG3119 387 ELGDP 391
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-476 |
2.42e-111 |
|
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: 336.12 E-value: 2.42e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLG----YGKVSPE 103
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNnvenAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 104 YKYEM---PQMLKDAGYYTFGIGKMHWHPQRIKhgfegtlldesgrvedenftSDYrqwfqtkapgknpdatgiGWNDHt 180
Cdd:cd16033 81 LPPGVetfSEDLREAGYRNGYVGKWHVGPEETP--------------------LDY------------------GFDEY- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 181 asiykLPENLHPTYWTGEMACELISNYDPTNKPLFLKVSFARPHSPYDPPQRYLDMYKDALIPDPAigdwcgkyakklNP 260
Cdd:cd16033 122 -----LPVETTIEYFLADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPE------------SF 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 261 EETAQDAPYGN-----------FGNEYARNSRRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHW 329
Cdd:cd16033 185 ADDFEDKPYIYrrerkrwgvdtEDEEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLW 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 330 RKTYP-YEGSTHVPYIVKWPsaNHVTPGKT-DAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKG-METNWRKYLdle 406
Cdd:cd16033 265 DKGPFmYEETYRIPLIIKWP--GVIAAGQVvDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGeQPEDWRDEV--- 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2176971269 407 HATCYSDDNYWC--ALTDGKIKYIWRiHTGTEELFDLTQDPQELHNAVNDKKYRRQLTEMRNEMIRHLSERG 476
Cdd:cd16033 340 VTEYNGHEFYLPqrMVRTDRYKYVFN-GFDIDELYDLESDPYELNNLIDDPEYEEILREMRTRLYEWMEETG 410
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-450 |
3.48e-96 |
|
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: 296.79 E-value: 3.48e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 27 HPHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLGYGKVSPEYKY 106
Cdd:cd16034 1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVPLPPDAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 107 EMPQMLKDAGYYTFGIGKMHWHpqrikhGFEGtlldESGRVEDENFTSDYRQWFQT-KAPGKNPD-ATGIGWNDHTASIY 184
Cdd:cd16034 81 TIADVLKDAGYRTGYIGKWHLD------GPER----NDGRADDYTPPPERRHGFDYwKGYECNHDhNNPHYYDDDGKRIY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 185 klPENLHPTYWTgEMACELISNYDPTNKPLFLKVSFARPHSPYDP-PQRYLDMYKDALIPDPaigdwcgkyakklnpeet 263
Cdd:cd16034 151 --IKGYSPDAET-DLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLR------------------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 264 aQDAPYGNFGNEYARNSRRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHWRKTYPYEGSTHVPY 343
Cdd:cd16034 210 -PNVPEDKKEEAGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLMNKQVPYEESIRVPF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 344 IVKWPSANHvTPGKTDAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKGMETNWRKYLDLE-----HATCYSDDNYWC 418
Cdd:cd16034 289 IIRYPGKIK-AGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKDDEPDSVLLQcfvpfGGGSARDGGEWR 367
|
410 420 430
....*....|....*....|....*....|..
gi 2176971269 419 ALTDGKIKYIwRIHTGTEELFDLTQDPQELHN 450
Cdd:cd16034 368 GVRTDRYTYV-RDKNGPWLLFDNEKDPYQLNN 398
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
28-387 |
1.32e-94 |
|
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: 286.64 E-value: 1.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLGY---GKVSPEY 104
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNvgnGGGLPPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 105 KYEMPQMLKDAGYYTFGIGKMHwhpqrikhgfegtlldesgrvedenftsdyrqwfqtkapgknpdatgigwndhtasiy 184
Cdd:cd16022 81 EPTLAELLKEAGYRTALIGKWH---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 185 klpenlhptywtgEMACELISNYDPtNKPLFLKVSFARPHSPYdppqryldmykdalipdpaigdwcgkyakklnpeeta 264
Cdd:cd16022 103 -------------DEAIDFIERRDK-DKPFFLYVSFNAPHPPF------------------------------------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 265 qdapygnfgneyarnsrrHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYH-WRKTYPYEGSTHVPY 343
Cdd:cd16022 132 ------------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKKGSLYEGGIRVPF 193
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2176971269 344 IVKWPsaNHVTPGKT-DAPVELRDILPTFLDAADVTIPTDMDGRS 387
Cdd:cd16022 194 IVRWP--GKIPAGQVsDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
26-468 |
1.18e-92 |
|
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: 288.66 E-value: 1.18e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 26 KHPHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLGYGKVSPEYK 105
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLFDAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 106 YEM-PQMLKDAGYYTFGIGKmhWHpqrikhgfegtlLDESGRVEDENFtsDYrqWFQTKAPGKNPDATGIGWNDHTasiy 184
Cdd:cd16031 81 QPTyPKLLRKAGYQTAFIGK--WH------------LGSGGDLPPPGF--DY--WVSFPGQGSYYDPEFIENGKRV---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 185 klPENLHPTYWTGEMACELISNYDPtNKPLFLKVSFARPHSPYDPPQRYLDMYKDALIPDPAIGDWcGKYAKKlnpEETA 264
Cdd:cd16031 139 --GQKGYVTDIITDKALDFLKERDK-DKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPETFDD-DDYAGR---PEWA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 265 QDAPYGNFGNEYARNSR--------RHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHWRKTYPYE 336
Cdd:cd16031 212 REQRNRIRGVLDGRFDTpekyqrymKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLFDKRLMYE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 337 GSTHVPYIVKWPsaNHVTPGKT-DAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKGME-TNWRKYLDLEHatcYSDD 414
Cdd:cd16031 292 ESIRVPLIIRDP--RLIKAGTVvDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEGEKpVDWRKEFYYEY---YEEP 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 415 NY-----WCALTDGKIKYI-WRIHTGTEELFDLTQDPQELHNAVNDKKYRRQLTEMRNEM 468
Cdd:cd16031 367 NFhnvptHEGVRTERYKYIyYYGVWDEEELYDLKKDPLELNNLANDPEYAEVLKELRKRL 426
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
26-457 |
1.83e-92 |
|
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: 288.32 E-value: 1.83e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 26 KHPHIILIMTDQQRaDAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLGYG----KVS 101
Cdd:cd16030 1 KKPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNsyfrKVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 102 PEYKyEMPQMLKDAGYYTFGIGKMHwHPQRIkhgfegtlldeSGRVEDENFTSDY-RQWFQTKAPGKNPDATGIGWNDHT 180
Cdd:cd16030 80 PDAV-TLPQYFKENGYTTAGVGKIF-HPGIP-----------DGDDDPASWDEPPnPPGPEKYPPGKLCPGKKGGKGGGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 181 ASIY---KLPENLHPTYWTGEMACELISNYDPTNKPLFLKVSFARPHSPYDPPQRYLDMYKDALI-----------PDPA 246
Cdd:cd16030 147 GPAWeaaDVPDEAYPDGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIplpnpfdpidlPEVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 247 IGDWcGKYAKKLNPEETAQDAPYGNFGNEYARNSRRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDH 326
Cdd:cd16030 227 WNDL-DDLPKYGDIPALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 327 YHWRKTYPYEGSTHVPYIVKWPSANHvTPGKTDAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKGMETNWRKYLDLE 406
Cdd:cd16030 306 GHWGKHTLFEEATRVPLIIRAPGVTK-PGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLKNPSAKWKDAAFSQ 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2176971269 407 HATCYSdDNYwcALTDGK---IKYIWRIHTGTEELFDLTQDPQELHNAVNDKKY 457
Cdd:cd16030 385 YPRPSI-MGY--SIRTERyryTEWVDFDKVGAEELYDHKNDPNEWKNLANDPEY 435
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
28-472 |
1.22e-87 |
|
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: 273.62 E-value: 1.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDaVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLG---YGKVSPEY 104
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNV-VKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGlrsRGFPLPDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 105 KYEMPQMLKDAGYYTFGIGKmhwhpqrikhgfegtlldesgrvEDENFTSDYRQWFqtkaPGKNPDATGIGWNDHTASIY 184
Cdd:cd16027 80 VKTLPELLREAGYYTGLIGK-----------------------THYNPDAVFPFDD----EMRGPDDGGRNAWDYASNAA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 185 KlpenlhptyWTgemacelisNYDPTNKPLFLKVSFARPHSPYDPPQRYLDMYKDALIPDPAIG-DwcgkyakklNPEet 263
Cdd:cd16027 133 D---------FL---------NRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPYLpD---------TPE-- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 264 aqdapygnfgneyARNSRRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHyhwrKTYPYEGSTHVPY 343
Cdd:cd16027 184 -------------VREDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFPRA----KGTLYDSGLRVPL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 344 IVKWPsaNHVTPGK-TDAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKGMETNWRKYLDLEHATCysDDNYWC--AL 420
Cdd:cd16027 247 IVRWP--GKIKPGSvSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGRDYVFAERDRH--DETYDPirSV 322
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2176971269 421 TDGKIKYIWRIHtgTEELFDLTQDPQELHNAVNDKKYRRQLTEMRNEMIRHL 472
Cdd:cd16027 323 RTGRYKYIRNYM--PEELYDLKNDPDELNNLADDPEYAEVLEELRAALDAWM 372
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
26-469 |
3.18e-81 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 257.11 E-value: 3.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 26 KHPHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGY---SSCPS-STPARAGLLTGLSPWHHGLLGYGKVS 101
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYnmgGWSGAvCVPSRAMLMTGRTLFHAPEGGKAAIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 102 PEYkYEMPQMLKDAGYYTFGIGKmhWHpqrikhgfegtlldesgrvedenftsdyrqwfqtkapgknpdatgigwNDHTa 181
Cdd:cd16155 81 SDD-KTWPETFKKAGYRTFATGK--WH------------------------------------------------NGFA- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 182 siyklpenlhptywtgEMACELISNYDPTNKPLFLKVSFARPHSPYDPPQRYLDMYKDALIPDPAigdwcgKYAK---KL 258
Cdd:cd16155 109 ----------------DAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPLPE------NFLPqhpFD 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 259 NPEETAQD---APYGnfGNEYA-RNSRRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHWRKTYP 334
Cdd:cd16155 167 NGEGTVRDeqlAPFP--RTPEAvRQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLMGKQNL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 335 YEGSTHVPYIVKWPSanhVTPGKT-DAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKGMETNWRKYLdlehATCYSD 413
Cdd:cd16155 245 YEHSMRVPLIISGPG---IPKGKRrDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVRDTL----YGAYRD 317
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2176971269 414 DNYwcALTDGKIKYIWRIH-TGTEELFDLTQDPQELHNAVNDKKYRRQLTEMRNEMI 469
Cdd:cd16155 318 GQR--AIRDDRWKLIIYVPgVKRTQLFDLKKDPDELNNLADEPEYQERLKKLLAELK 372
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-446 |
1.26e-80 |
|
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: 254.00 E-value: 1.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLGYGKVSPEYKYE 107
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDGDVPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 108 MPQMLKDAGYYTFGIGKMHWHPQRIKHGFEgtlldesgrvEDENFTSDyrqwfqtkapgknpdatgigwndhtasiyklp 187
Cdd:cd16037 81 WGHALRAAGYETVLIGKLHFRGEDQRHGFR----------YDRDVTEA-------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 188 enlhptywtgemACELISNYDPTNKPLFLKVSFARPHSPYDPPQRYLDMYkdalipdpaigdwcgkyakklnpeetaqda 267
Cdd:cd16037 119 ------------AVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY------------------------------ 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 268 pygnfgneyARNSRRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHWRKTYPYEGSTHVPYIVKW 347
Cdd:cd16037 157 ---------VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMYEESVRVPMIISG 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 348 PsaNHVTPGKTDAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKGMEtNWRKYLDLEHATCYSDDnYWCALTDGKIKY 427
Cdd:cd16037 228 P--GIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLAEGPD-DPDRVVFSEYHAHGSPS-GAFMLRKGRWKY 303
|
410 420
....*....|....*....|
gi 2176971269 428 IWriHTG-TEELFDLTQDPQ 446
Cdd:cd16037 304 IY--YVGyPPQLFDLENDPE 321
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
30-471 |
6.98e-78 |
|
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: 251.02 E-value: 6.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 30 IILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLGYGKVSPEYKYEMP 109
Cdd:cd16028 3 VLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGTPLDARHLTLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 110 QMLKDAGYYTFGIGKMHWHP-QRIKHGfegtlLDESGRvedenftsdyrqWFQTKAPGKNPdatgigwNDHTASIyklPE 188
Cdd:cd16028 83 LELRKAGYDPALFGYTDTSPdPRGLAP-----LDPRLL------------SYELAMPGFDP-------VDRLDEY---PA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 189 NLHPTYWTGEMACELISNYDptNKPLFLKVSFARPHSPYDPPQRYLDMYKDALIPDPAigdwcgkyaKKLNPEETAQDAP 268
Cdd:cd16028 136 EDSDTAFLTDRAIEYLDERQ--DEPWFLHLSYIRPHPPFVAPAPYHALYDPADVPPPI---------RAESLAAEAAQHP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 269 -YGNFGNEYARNS-------------------RRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYH 328
Cdd:cd16028 205 lLAAFLERIESLSfspgaanaadlddeevaqmRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 329 WRKTYPYEGSTHVPYIVKWP--SANHVTPGKTDAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKG-METNWRKYLDL 405
Cdd:cd16028 285 WGKDGFFDQAYRVPLIVRDPrrEADATRGQVVDAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGaQPSDWRDAVHY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 406 EHAtcYSDDNY---------------WCALTDGKIKYIWriHTGTEE-LFDLTQDPQELHNAVNDKKYRRQLTEMRNEMI 469
Cdd:cd16028 365 EYD--FRDVSTrrpqealglspdecsLAVIRDERWKYVH--FAALPPlLFDLKNDPGELRDLAADPAYAAVVLRYAQKLL 440
|
..
gi 2176971269 470 RH 471
Cdd:cd16028 441 SW 442
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
28-474 |
2.60e-70 |
|
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: 231.89 E-value: 2.60e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLGYGKVSPEYKYE 107
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 108 MPQMLKDAGYYTFGIGKmhWHpqrikhgFEGTLLDESGRVEDEnFTSDYrqWFQtkapGKN-----PDATGIGWNDHTAS 182
Cdd:cd16156 81 IGQRLSDNGIHTAYIGK--WH-------LDGGDYFGNGICPQG-WDPDY--WYD----MRNyldelTEEERRKSRRGLTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 183 IYK--LPENLHPTYWTGEMACELISNYdpTNKPLFLKVSFARPHSPYDPPQRYLDMYKDALIP-DPAIGDWCGKyaKKLN 259
Cdd:cd16156 145 LEAegIKEEFTYGHRCTNRALDFIEKH--KDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPkGENAYDDLEN--KPLH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 260 PEETAQDAPYGNFGNEYARNsrRHYYANITFIDEQIGRIIQTLKEKdmYNDALIVFVSDHGDMMGDHYHWRK-TYPYEGS 338
Cdd:cd16156 221 QRLWAGAKPHEDGDKGTIKH--PLYFGCNSFVDYEIGRVLDAADEI--AEDAWVIYTSDHGDMLGAHKLWAKgPAVYDEI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 339 THVPYIVKWPsANHVTPGKTDAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKGMETNWRKYLDLEHATCYSDDNYW- 417
Cdd:cd16156 297 TNIPLIIRGK-GGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIEDPEIPENRGVFVEFGRYEVDHDGFg 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2176971269 418 ------CALTDgkiKYIWRIH-TGTEELFDLTQDPQELHNAVNDKKYRRQLTEMRNEMIRHLSE 474
Cdd:cd16156 376 gfqpvrCVVDG---RYKLVINlLSTDELYDLEKDPYEMHNLIDDPDYADVRDQLHDELLDYMNE 436
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-471 |
3.49e-69 |
|
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: 227.43 E-value: 3.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQ-RADaIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSP-------WHHGLLGYGK 99
Cdd:cd16144 1 PNIVLILVDDLgWAD-LGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYParlgitdVIPGRRGPPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 100 ----VSPEYKYEMP-------QMLKDAGYYTFGIGKmhWH------PQRIKHGFegtlldesgrveDENFTSDyrqwfqt 162
Cdd:cd16144 80 ntklIPPPSTTRLPleevtiaEALKDAGYATAHFGK--WHlggeggYGPEDQGF------------DVNIGGT------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 163 kaPGKNPDATGIGWNDHTASIYKLPENLHPTYWTGEMACELISNYDptNKPLFLKVSFARPHSPYDPPQRYLDmykdali 242
Cdd:cd16144 139 --GNGGPPSYYFPPGKPNPDLEDGPEGEYLTDRLTDEAIDFIEQNK--DKPFFLYLSHYAVHTPIQARPELIE------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 243 pdpaigdwcgKYAKKLNPEETAQDAPygnfgnEYArnsrrhyyANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDM 322
Cdd:cd16144 208 ----------KYEKKKKGLRKGQKNP------VYA--------AMIESLDESVGRILDALEELGLADNTLVIFTSDNGGL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 323 MGDHYHWRKTYP--------YEGSTHVPYIVKWPsaNHVTPGKT-DAPVELRDILPTFLDAADVTIPT--DMDGRSLLPL 391
Cdd:cd16144 264 STRGGPPTSNAPlrggkgslYEGGIRVPLIVRWP--GVIKPGSVsDVPVIGTDLYPTFLELAGGPLPPpqHLDGVSLVPL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 392 AKGMETN-------WrkyldleHATCYSDDNYW--CALTDGKIKYIWRIHTGTEELFDLTQDPQELHNAVNDKKYRRQlt 462
Cdd:cd16144 342 LKGGEADlprralfW-------HFPHYHGQGGRpaSAIRKGDWKLIEFYEDGRVELYNLKNDIGETNNLAAEMPEKAA-- 412
|
....*....
gi 2176971269 463 EMRNEMIRH 471
Cdd:cd16144 413 ELKKKLDAW 421
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
28-446 |
1.80e-68 |
|
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: 222.45 E-value: 1.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPwhHGLLGYGKVSpEYKYE 107
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLP--SRIGAYDNAA-EFPAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 108 MPQM---LKDAGYYTFGIGKMHW-HPQRIkHGFEgtlldesgrvEDENFTSDYRQWFQTKAPGKNPdatgigwndhtasi 183
Cdd:cd16032 78 IPTFahyLRAAGYRTALSGKMHFvGPDQL-HGFD----------YDEEVAFKAVQKLYDLARGEDG-------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 184 yklpenlhptywtgemacelisnydptnKPLFLKVSFARPHSPYDPPQRYLDMYkdalipdpaigdwcgkyakklnpeet 263
Cdd:cd16032 133 ----------------------------RPFFLTVSFTHPHDPYVIPQEYWDLY-------------------------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 264 aqdapygnfgneyARNSRRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHWRKTYPYEGSTHVPY 343
Cdd:cd16032 159 -------------VRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSFFEGSARVPL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 344 IVKWPSANHvtPGKTDAPVELRDILPTFLDAA---DVTIPTDMDGRSLLPLAKGMETNWRKYLDLEH------ATCYsdd 414
Cdd:cd16032 226 IISAPGRFA--PRRVAEPVSLVDLLPTLVDLAgggTAPHVPPLDGRSLLPLLEGGDSGGEDEVISEYlaegavAPCV--- 300
|
410 420 430
....*....|....*....|....*....|..
gi 2176971269 415 nywcALTDGKIKYIWrIHTGTEELFDLTQDPQ 446
Cdd:cd16032 301 ----MIRRGRWKFIY-CPGDPDQLFDLEADPL 327
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-474 |
4.82e-67 |
|
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: 221.72 E-value: 4.82e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPwH-------HGLLgygkv 100
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYP-HvnghrtlHHLL----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 101 sPEYKYEMPQMLKDAGYYTFGIGKMHWHPQRikHGFEGTLLDESGRVEdenftsdyrqwfqtkapgknpdaTGIGWndht 180
Cdd:cd16150 75 -RPDEPNLLKTLKDAGYHVAWAGKNDDLPGE--FAAEAYCDSDEACVR-----------------------TAIDW---- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 181 asiyklpenlhptywtgemacelISNYDPtNKPLFLKVSFARPHSPYDPPQRYLDMYKDALIPD--PAIGDWCGKYAKKL 258
Cdd:cd16150 125 -----------------------LRNRRP-DKPFCLYLPLIFPHPPYGVEEPWFSMIDREKLPPrrPPGLRAKGKPSMLE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 259 NPEetaqdapYGNFG---NEYARNSRRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDH---YHWRKT 332
Cdd:cd16150 181 GIE-------KQGLDrwsEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYglvEKWPNT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 333 YpYEGSTHVPYIVKWPSAnhVTPGKTDAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKGMETNWRKY---------- 402
Cdd:cd16150 254 F-EDCLTRVPLIIKPPGG--PAGGVSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLPVLAGETEEHRDAvfseggrlhg 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 403 ----LDLEHatcYSDDNYWCALT---------------DGKIKYIWRiHTGTEELFDLTQDPQELHNAVNDKKYRRQLTE 463
Cdd:cd16150 331 eeqaMEGGH---GPYDLKWPRLLqqeeppehtkavmirTRRYKYVYR-LYEPDELYDLEADPLELHNLIGDPAYAEIIAE 406
|
490
....*....|.
gi 2176971269 464 MRNEMIRHLSE 474
Cdd:cd16150 407 MKQRLLRWMVE 417
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-474 |
2.58e-60 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 202.84 E-value: 2.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 27 HPHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLGYGKVSPEYKY 106
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNGIPLPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 107 EMPQMLKDAGYYTFGIGKmhWHpqrikhgfegtlldesgrvedenfTSDYRQWFQTkapgknpdatgigwndhtasiykl 186
Cdd:cd16152 81 TLAHYFRDAGYETGYVGK--WH------------------------LAGYRVDALT------------------------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 187 penlhptywtgEMACELISNYDpTNKPLFLKVSFARPH-----SPYDPPQRYLDMYKDALIPD---PAIGDWCGKYAKkl 258
Cdd:cd16152 111 -----------DFAIDYLDNRQ-KDKPFFLFLSYLEPHhqndrDRYVAPEGSAERFANFWVPPdlaALPGDWAEELPD-- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 259 npeetaqdapygnfgneyarnsrrhYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHgdmmGDHYHWR----KTYP 334
Cdd:cd16152 177 -------------------------YLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHFRTRnaeyKRSC 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 335 YEGSTHVPYIVKWPSANHvtpGKT-DAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKGMETNWR------------- 400
Cdd:cd16152 228 HESSIRVPLVIYGPGFNG---GGRvEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVEDWRnevfiqisesqvg 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 401 --------KYldlehATCYSDDNYWcaLTDGKIKYIwrihtgTEELFDLTQDPQELHNAVNDKKYRRQLTEMRNEMIRHL 472
Cdd:cd16152 305 rairtdrwKY-----SVAAPDKDGW--KDSGSDVYV------EDYLYDLEADPYELVNLIGRPEYREVAAELRERLLARM 371
|
..
gi 2176971269 473 SE 474
Cdd:cd16152 372 AE 373
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
28-467 |
3.21e-58 |
|
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: 198.16 E-value: 3.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSScPSSTPARAGLLTGLSPW----HHGLLGYGKVSPE 103
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFrtgvWHTILGRERMRLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 104 yKYEMPQMLKDAGYYTFGIGKMH------WHPQRikHGFEGTLLDESGRVedenftsdyrqwfqtkapGKNPDATGigwN 177
Cdd:cd16146 80 -ETTLAEVFKDAGYRTGIFGKWHlgdnypYRPQD--RGFDEVLGHGGGGI------------------GQYPDYWG---N 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 178 DHTASIYKLPENLHPT--Y----WTgEMACELISnyDPTNKPLFLKVSFARPHSPYDPPQRYLDMYKDALIPDPaigdwc 251
Cdd:cd16146 136 DYFDDTYYHNGKFVKTegYctdvFF-DEAIDFIE--ENKDKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDK------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 252 gkyakklnpeetaqdapygnfgneyarnsRRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHW-- 329
Cdd:cd16146 207 -----------------------------LAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRFna 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 330 ----RKTYPYEGSTHVPYIVKWPsaNHVTPGK-TDAPVELRDILPTFLDAADVTIPT--DMDGRSLLPLAKGMETNWR-K 401
Cdd:cd16146 258 gmrgKKGSVYEGGHRVPFFIRWP--GKILAGKdVDTLTAHIDLLPTLLDLCGVKLPEgiKLDGRSLLPLLKGESDPWPeR 335
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2176971269 402 YLDLEHATCYSDDNYW--CALTDGKIKYIWRiHTGTEELFDLTQDPQELHNAVndKKYRRQLTEMRNE 467
Cdd:cd16146 336 TLFTHSGRWPPPPKKKrnAAVRTGRWRLVSP-KGFQPELYDIENDPGEENDVA--DEHPEVVKRLKAA 400
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-390 |
1.49e-56 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 189.68 E-value: 1.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGllGYGKVSPEYKYE 107
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHG--VWGGPLEPDDPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 108 MPQMLKDAGYYTFGIGKMHWHPQRikHGFegtlldesgrveDENFTSDYRQWFQTKAPGKNPDatgigwndhtasiyklp 187
Cdd:cd16148 79 LAEILRKAGYYTAAVSSNPHLFGG--PGF------------DRGFDTFEDFRGQEGDPGEEGD----------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 188 enlHPTYWTGEMACELISNYDPtNKPLFLKVSFARPHSPYdppqryldmykdalipdpaigdwcgkyakklnpeetaqda 267
Cdd:cd16148 128 ---ERAERVTDRALEWLDRNAD-DDPFFLFLHYFDPHEPY---------------------------------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 268 pygnfgneyarnsrrHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHWRKTYP--YEGSTHVPYIV 345
Cdd:cd16148 164 ---------------LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSnlYDEQLHVPLII 228
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2176971269 346 KWPSanhVTPGKT-DAPVELRDILPTFLDAADVTIPTDMDGRSLLP 390
Cdd:cd16148 229 RWPG---KEPGKRvDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-450 |
1.46e-54 |
|
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: 188.57 E-value: 1.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDqqraD----AIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHhgllGYGKVSPE 103
Cdd:cd16145 1 PNIIFILAD----DlgygDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGH----TRVRGNSE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 104 YKYEMP---------QMLKDAGYYTFGIGKMHW-------HPQriKHGFegtlldesgrvedenftsDYrqWFqtkapgk 167
Cdd:cd16145 73 PGGQDPlppddvtlaEVLKKAGYATAAFGKWGLggpgtpgHPT--KQGF------------------DY--FY------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 168 npdatgiGWNDHTAS-------------IYKLPENLHPTYWTGEMACELISNYDPT--------------NKPLFLKVSF 220
Cdd:cd16145 124 -------GYLDQVHAhnyypeylwrngeKVPLPNNVIPPLDEGNNAGGGGGTYSHDlftdealdfirenkDKPFFLYLAY 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 221 ARPHSPYDPPQRYLDMYKDALIPDPAIGDWcgkyakklnpeetaqdapygnfgneyaRNSRRHYYANITFIDEQIGRIIQ 300
Cdd:cd16145 197 TLPHAPLQVPDDGPYKYKPKDPGIYAYLPW---------------------------PQPEKAYAAMVTRLDRDVGRILA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 301 TLKEKDMYNDALIVFVSDHGDMM-----GDHYHWRKTYP--------YEGSTHVPYIVKWPsaNHVTPGKT-DAPVELRD 366
Cdd:cd16145 250 LLKELGIDENTLVVFTSDNGPHSeggseHDPDFFDSNGPlrgykrslYEGGIRVPFIARWP--GKIPAGSVsDHPSAFWD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 367 ILPTFLDAADVTIPTDMDGRSLLPLAKGMETNWR-KYLDLEhatcYSDDNYWCALTDGKIKYIwRIHTGTE--ELFDLTQ 443
Cdd:cd16145 328 FMPTLADLAGAEPPEDIDGISLLPTLLGKPQQQQhDYLYWE----FYEGGGAQAVRMGGWKAV-RHGKKDGpfELYDLST 402
|
....*..
gi 2176971269 444 DPQELHN 450
Cdd:cd16145 403 DPGETNN 409
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-450 |
2.03e-51 |
|
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: 179.70 E-value: 2.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDqqraDA----IGCMGNDAVIS-PNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGL-----LGY 97
Cdd:cd16143 1 PNIVIILAD----DLgygdISCYNPDSKIPtPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLkggvlGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 98 GK--VSPEyKYEMPQMLKDAGYYTFGIGKmhWHpqrikHGFEGTLLDESGRVEDENFTSDYRQWFqtkAPGknPDATGIg 175
Cdd:cd16143 77 SPplIEPD-RVTLAKMLKQAGYRTAMVGK--WH-----LGLDWKKKDGKKAATGTGKDVDYSKPI---KGG--PLDHGF- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 176 wnDHTasiYKLPENLHPTYWTGEmACELISNYDPTNKPLFLKVSFARPHSPYDPPQRyldmykdalipdpaigdWCGKYa 255
Cdd:cd16143 143 --DYY---FGIPASEVLPTLTDK-AVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPE-----------------FQGKS- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 256 kKLNPeetaqdapYGNFgneyarnsrrhyyanITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHG-------DMMGDH-- 326
Cdd:cd16143 199 -GAGP--------YGDF---------------VYELDWVVGRILDALKELGLAENTLVIFTSDNGpspyadyKELEKFgh 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 327 ---YHWR--KTYPYEGSTHVPYIVKWPsaNHVTPGKT-DAPVELRDILPTFLDAADVTIPTD--MDGRSLLPLAKGmetn 398
Cdd:cd16143 255 dpsGPLRgmKADIYEGGHRVPFIVRWP--GKIPAGSVsDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPALLG---- 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2176971269 399 wRKYLDLEHATCYSDDNYWCALTDGKIKYIwrIHTGT----------------EELFDLTQDPQELHN 450
Cdd:cd16143 329 -PKKQEVRESLVHHSGNGSFAIRKGDWKLI--DGTGSggfsyprgkeklglppGQLYNLSTDPGESNN 393
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
28-377 |
2.56e-48 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 168.76 E-value: 2.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLGYGKVSPEYKYE 107
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVGLPRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 108 -MPQMLKDAGYYTFGIGKMH--WHPQRI--KHGFEGTLldesGRVEDENFTSDYrqwfqtkapgKNPDATGIGWNDHTAS 182
Cdd:pfam00884 81 sLPDLLKRAGYNTGAIGKWHlgWYNNQSpcNLGFDKFF----GRNTGSDLYADP----------PDVPYNCSGGGVSDEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 183 IYKlpenlhptywtgemacELISNYDPTNKPLFLKVSFARPHSPYDPPQRYldmykdalipdpaigdwcgkyakklnPEE 262
Cdd:pfam00884 147 LLD----------------EALEFLDNNDKPFFLVLHTLGSHGPPYYPDRY--------------------------PEK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 263 TAQDAPYGNFGNEYARNsrrhYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGD---HYHWRKTY-PYEGS 338
Cdd:pfam00884 185 YATFKPSSCSEEQLLNS----YDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEgggYLHGGKYDnAPEGG 260
|
330 340 350
....*....|....*....|....*....|....*....
gi 2176971269 339 THVPYIVKWPSANHvTPGKTDAPVELRDILPTFLDAADV 377
Cdd:pfam00884 261 YRVPLLIWSPGGKA-KGQKSEALVSHVDLFPTILDLAGI 298
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
28-450 |
3.33e-48 |
|
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: 171.19 E-value: 3.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSScPSSTPARAGLLTGLSPWHHGLLGYGKVSPEYKY- 106
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEPYGl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 107 -----EMPQMLKDAGYYTFGIGKmhWH----------PQRikhGFE---GTLLDESG---RVEDENFTSDYRQWFQTKAP 165
Cdd:cd16029 80 plnetLLPQYLKELGYATHLVGK--WHlgfytweytpTNR---GFDsfyGYYGGAEDyytHTSGGANDYGNDDLRDNEEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 166 GKNpdatgiGWNDHTASIYklpenlhptywtGEMACELISNYDPTnKPLFLKVSFARPHSPYDPPQRYLDMYKDAL--IP 243
Cdd:cd16029 155 AWD------YNGTYSTDLF------------TDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYEDKFahIK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 244 DPaigdwcgkyakklnpeetaqdapygnfgneyarnSRRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHG-DM 322
Cdd:cd16029 216 DE----------------------------------DRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGgPT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 323 MGDHYHW------RKTYPYEGSTHVPYIVKWPSANHVTPGKTDAPVELRDILPTFLDAA--DVTIPTDMDGRSLLPLAKG 394
Cdd:cd16029 262 GGGDGGSnyplrgGKNTLWEGGVRVPAFVWSPLLPPKRGTVSDGLMHVTDWLPTLLSLAggDPDDLPPLDGVDQWDALSG 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2176971269 395 METNWRKylDLEHAtcYSDDNYWC---ALTDGKIKYIwrihTGTeELFDLTQDPQELHN 450
Cdd:cd16029 342 GAPSPRT--EILLN--IDDITRTTggaAIRVGDWKLI----VGK-PLFNIENDPCERND 391
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-388 |
3.91e-48 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 167.55 E-value: 3.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGN----------DAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLGY 97
Cdd:cd16153 2 PNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 98 GKV--SPEYKYEM-PQMLKDAGYYTFGIGKMHwhpqrikhgfegtlLDESGRVEDENFTSDYRQWFQtkaPGKNPDatgi 174
Cdd:cd16153 82 EAAhpALDHGLPTfPEVLKKAGYQTASFGKSH--------------LEAFQRYLKNANQSYKSFWGK---IAKGAD---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 175 gwndhtasiyklpenlhptywtgemacelisnydpTNKPLFLKVSFARPHSPYDPPQRYLDMYKdalipdpaigdwcgky 254
Cdd:cd16153 141 -----------------------------------SDKPFFVRLSFLQPHTPVLPPKEFRDRFD---------------- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 255 akklnpeetaqdapygnfgneyarnsrrhYYANITFIDEQIGRIIQTLK---EKDMYNDALIVFVSDHGDMMGDHYHWRK 331
Cdd:cd16153 170 -----------------------------YYAFCAYGDAQVGRAVEAFKaysLKQDRDYTIVYVTGDHGWHLGEQGILAK 220
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 332 TYPYEGSTHVPYIVKWPSANHVTPGKT-DAPVELRDILPTFLDAA--DVTIPTDMDGRSL 388
Cdd:cd16153 221 FTFWPQSHRVPLIVVSSDKLKAPAGKVrHDFVEFVDLAPTLLAAAgvDVDAPDYLDGRDL 280
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
26-450 |
4.78e-48 |
|
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: 170.70 E-value: 4.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 26 KHPHIILIMTDqqraD----AIGCMGNDaVISPNLDALAAEGTLFMNGYSScPSSTPARAGLLTGLspWHH--------- 92
Cdd:cd16025 1 GRPNILLILAD----DlgfsDLGCFGGE-IPTPNLDALAAEGLRFTNFHTT-ALCSPTRAALLTGR--NHHqvgmgtmae 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 93 ---GLLGYGKVSPEYKYEMPQMLKDAGYYTFGIGKmhWHpqrikHGFEGtlldesgrvedenftsdyrqWFQTKApgknp 169
Cdd:cd16025 73 latGKPGYEGYLPDSAATIAEVLKDAGYHTYMSGK--WH-----LGPDD--------------------YYSTDD----- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 170 datgigWNDHtasiyklpenlhptywtgemACELISNYDPTNKPLFLKVSFARPHSPYDPPQRYLDMYK-------DA-- 240
Cdd:cd16025 121 ------LTDK--------------------AIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKgkydagwDAlr 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 241 -----------LIP--------DPAIGDWcgkyaKKLNPEETAQDApygnfgneyarnsRR--HYYANITFIDEQIGRII 299
Cdd:cd16025 175 eerlerqkelgLIPadtkltprPPGVPAW-----DSLSPEEKKLEA-------------RRmeVYAAMVEHMDQQIGRLI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 300 QTLKEKDMYNDALIVFVSDHG--------DMMGDHYHWRKTYPYEGSTHVPYIVKWPSANHVTPGKTDAPVELRDILPTF 371
Cdd:cd16025 237 DYLKELGELDNTLIIFLSDNGasaepgwaNASNTPFRLYKQASHEGGIRTPLIVSWPKGIKAKGGIRHQFAHVIDIAPTI 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 372 LDAADVTIPTD--------MDGRSLLPLakgmetnwrkyldLEHATCYSDDNYWC-------ALTDGKIKYIWRIHTGTE 436
Cdd:cd16025 317 LELAGVEYPKTvngvpqlpLDGVSLLPT-------------LDGAAAPSRRRTQYfelfgnrAIRKGGWKAVALHPPPGW 383
|
490
....*....|....*...
gi 2176971269 437 ----ELFDLTQDPQELHN 450
Cdd:cd16025 384 gdqwELYDLAKDPSETHD 401
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
27-450 |
2.66e-46 |
|
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: 166.20 E-value: 2.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 27 HPHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSP------WHHGLLGYGKV 100
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPvrvglpGVVGPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 101 SPEYKYEMPQMLKDAGYYTFGIGKMH------WHPQRikHGFEgtlldesgrvedenftsdyrQWFQTkaPGKN-PDATG 173
Cdd:cd16026 81 LPPDEITIAEVLKKAGYRTALVGKWHlghqpeFLPTR--HGFD--------------------EYFGI--PYSNdMWPFP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 174 IGWNDHTASIYKLPENL----HPT-------YWTGEmACELIsnYDPTNKPLFLKVSFARPHSPYDPPQRYldmykdali 242
Cdd:cd16026 137 LYRNDPPGPLPPLMENEevieQPAdqssltqRYTDE-AVDFI--ERNKDQPFFLYLAHTMPHVPLFASEKF--------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 243 pdpaigdwcgkyakklnpEETAQDAPYGNFGNEyarnsrrhyyanitfIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDM 322
Cdd:cd16026 205 ------------------KGRSGAGLYGDVVEE---------------LDWSVGRILDALKELGLEENTLVIFTSDNGPW 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 323 MGDHYHW--------RKTYPYEGSTHVPYIVKWPSanHVTPGKT-DAPVELRDILPTFLDAADVTIPTD--MDGRSLLPL 391
Cdd:cd16026 252 LEYGGHGgsagplrgGKGTTWEGGVRVPFIAWWPG--VIPAGTVsDELASTMDLLPTLAALAGAPLPEDrvIDGKDISPL 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2176971269 392 AKGMETNWRKYLDLehatcYSDDNYWCALTDGKIKYI--------------WRIHTGTEELFDLTQDPQELHN 450
Cdd:cd16026 330 LLGGSKSPPHPFFY-----YYDGGDLQAVRSGRWKLHlpttyrtgtdpgglDPTKLEPPLLYDLEEDPGETYN 397
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-450 |
3.03e-46 |
|
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: 165.47 E-value: 3.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSScPSSTPARAGLLTGLSPWHHGLLGYGKVSPEYKYe 107
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNYVVFGYLDPKQKTF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 108 mPQMLKDAGYYTFGIGKmhW----------HPQriKHGFegtllDES---GRVEDENFTSDYRQWFQTKAPGKNPDATGi 174
Cdd:cd16151 79 -GHLLKDAGYATAIAGK--WqlgggrgdgdYPH--EFGF-----DEYclwQLTETGEKYSRPATPTFNIRNGKLLETTE- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 175 GW------NDHtasiyklpenlhptywtgemACELISNYdpTNKPLFLKVSFARPHSPYDPpqryldmykdalIPDPaiG 248
Cdd:cd16151 148 GDygpdlfADF--------------------LIDFIERN--KDQPFFAYYPMVLVHDPFVP------------TPDS--P 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 249 DWcgkyakklNPEETAQDAPYGNFGneyarnsrrhyyANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYH 328
Cdd:cd16151 192 DW--------DPDDKRKKDDPEYFP------------DMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 329 WR-------KTYPYEGSTHVPYIVKWPSanHVTPGK-TDAPVELRDILPTFLDAADVTIPTD--MDGRSLLPLAKGMETN 398
Cdd:cd16151 252 TNgrevrggKGKTTDAGTHVPLIVNWPG--LIPAGGvSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQLLGKTGS 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2176971269 399 WRKYldlehATCYSDDNYWCALTDGKIKY-IWRIHtGTEELFDLTQDPQELHN 450
Cdd:cd16151 330 PRRE-----WIYWYYRNPHKKFGSRFVRTkRYKLY-ADGRFFDLREDPLEKNP 376
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-390 |
2.98e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 156.63 E-value: 2.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLL------GYGKVS 101
Cdd:cd16149 1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHdwivegSHGKTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 102 PEYKY-----EMPQMLKDAGYYTFGIGKmhWHpqrikhgfegtlldesgrvedenftsdyrqwfqtkapgknpdatgigw 176
Cdd:cd16149 81 KPEGYlegqtTLPEVLQDAGYRCGLSGK--WH------------------------------------------------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 177 ndhtasiyklpenlhptywTGEMACELISNYDPTNKPLFLKVSFARPHSPYDppqryldmykdalipdpaigdwcgkyak 256
Cdd:cd16149 111 -------------------LGDDAADFLRRRAEAEKPFFLSVNYTAPHSPWG---------------------------- 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 257 klnpeetaqdapygnfgneyarnsrrhYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHWRK---TY 333
Cdd:cd16149 144 ---------------------------YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKgngTF 196
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2176971269 334 P---YEGSTHVPYIVKWPsaNHVTPG-KTDAPVELRDILPTFLDAADVTIPTDMD--GRSLLP 390
Cdd:cd16149 197 PlnmYDNSVKVPFIIRWP--GVVPAGrVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFAD 257
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
28-454 |
1.48e-42 |
|
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: 155.79 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADaigcMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLL-------GYGKV 100
Cdd:cd16147 2 PNIVLILTDDQDVE----LGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTnnsppggGYPKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 101 SpEYKYE---MPQMLKDAGYYTFGIGKmhwhpqrikhgfegtLLDESGRVEDENFT-SDYRQWFqtkAPGKNpdATGIGW 176
Cdd:cd16147 78 W-QNGLErstLPVWLQEAGYRTAYAGK---------------YLNGYGVPGGVSYVpPGWDEWD---GLVGN--STYYNY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 177 NDHTASIYKLPENLHPTYWT---GEMACELISNYDPTNKPLFLKVSFARPHSPYDPPQRYLDMYKDALIP------DPAI 247
Cdd:cd16147 137 TLSNGGNGKHGVSYPGDYLTdviANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPprpppnNPDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 248 GD---WCGKYAKkLNPEETAqdapygnFGNEYARNSRRHYYAnitfIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMG 324
Cdd:cd16147 217 SDkphWLRRLPP-LNPTQIA-------YIDELYRKRLRTLQS----VDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 325 DH-YHWRKTYPYEGSTHVPYIVKWPsanHVTPGKT-DAPVELRDILPTFLDAADVTIPTDMDGRSllplakgmetnwrky 402
Cdd:cd16147 285 QHrLPPGKRTPYEEDIRVPLLVRGP---GIPAGVTvDQLVSNIDLAPTILDLAGAPPPSDMDGRS--------------- 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2176971269 403 ldlehatCYSDDN--YWCA--LTDGKIKYIWRIHTGTEELFDLTQDPQELHNAVND 454
Cdd:cd16147 347 -------CGDSNNntYKCVrtVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGD 395
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-398 |
2.02e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 150.44 E-value: 2.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGY-SSCPSStPARAGLLTGLSPWHHGL---LGYGkVSPE 103
Cdd:cd16035 1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYtAACMCS-PSRSTLYTGLHPQQTGVtdtLGSP-MQPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 104 YKYEMPQ---MLKDAGYYTFGIGKmhWHpqrIKHGFEGtlldesGRVEDENFTSDYRQWFQTKAPGKNPDatgigwndht 180
Cdd:cd16035 79 LSPDVPTlghMLRAAGYYTAYKGK--WH---LSGAAGG------GYKRDPGIAAQAVEWLRERGAKNADG---------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 181 asiyklpenlhptywtgemacelisnydptnKPLFLKVSFARPHspydppqryldmykDALIPDPAIGDWCgkyakklnp 260
Cdd:cd16035 138 -------------------------------KPWFLVVSLVNPH--------------DIMFPPDDEERWR--------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 261 eetaqdapygnfgneYARNsrrhYYAN-ITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHWRKTY-PYEGS 338
Cdd:cd16035 164 ---------------RFRN----FYYNlIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFnAYEEA 224
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2176971269 339 THVPYIVKWPSANHvTPGKTDAPVELRDILPTFLDAADVTIPT------DMDGRSLLPLAKGMETN 398
Cdd:cd16035 225 LHVPLIISHPDLFG-TGQTTDALTSHIDLLPTLLGLAGVDAEArateapPLPGRDLSPLLTDADAD 289
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
27-391 |
3.07e-31 |
|
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: 125.62 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 27 HPHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLLGYGKVS----- 101
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRVFlpwdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 102 ---PEYKYEMPQMLKDAGYYTFGIGKmhWH--------------PQriKHGFE--GTLLDesgrvedenFTSdyrQWF-- 160
Cdd:cd16160 81 gglPKTEVTMAEALKEAGYTTGMVGK--WHlginennhsdgahlPS--HHGFDfvGTNLP---------FTN---SWAcd 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 161 --QTKAPGKNPDATGIGWNDhtaSIYKLPENlhPTYWTGEM---ACELIsnYDPTNKPLFLKVSFARPHSPydppqryld 235
Cdd:cd16160 145 dtGRHVDFPDRSACFLYYND---TIVEQPIQ--HEHLTETLvgdAKSFI--EDNQENPFFLYFSFPQTHTP--------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 236 MYKDAlipdpaigDWCGKyakklnpeetaqdapygnfgneyarnSRRHYYA-NITFIDEQIGRIIQTLKEKDMYNDALIV 314
Cdd:cd16160 209 LFASK--------RFKGK--------------------------SKRGRYGdNINEMSWAVGEVLDTLVDTGLDQNTLVF 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 315 FVSDHGDMM------GDHYHWR--KTYPYEGSTHVPYIVKWPSAnhVTPGKTDAPVELRDILPTFLDAADVTIPTD--MD 384
Cdd:cd16160 255 FLSDHGPHVeyclegGSTGGLKggKGNSWEGGIRVPFIAYWPGT--IKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriYD 332
|
....*..
gi 2176971269 385 GRSLLPL 391
Cdd:cd16160 333 GLSITDL 339
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
28-445 |
2.50e-29 |
|
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: 118.80 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSP-----WHHgllgYGKVSP 102
Cdd:cd16171 1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFThltesWNN----YKGLDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 103 EYKYEMPQMLKDaGYYTFGIGKMHWhpqriKHGFEgtllDESGRVE----DENFTsdYRQWFQTKapgknPDATGigwND 178
Cdd:cd16171 77 NYPTWMDRLEKH-GYHTQKYGKLDY-----TSGHH----SVSNRVEawtrDVPFL--LRQEGRPT-----VNLVG---DR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 179 HTASIYKLPenlhptyWTG-EMACELISNYDPT-NKPLFLKVSFARPHsPYdppqryldmykdaliPDPAIGDwcgkyak 256
Cdd:cd16171 137 STVRVMLKD-------WQNtDKAVHWIRKEAPNlTQPFALYLGLNLPH-PY---------------PSPSMGE------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 257 klnpeetaqdapygNFGNeyARNSRRHYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHWRKTYPYE 336
Cdd:cd16171 187 --------------NFGS--IRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMYE 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 337 GSTHVPYIVKWPSanhVTPGK-TDAPVELRDILPTFLDAADVTIPTDMDGRSLLPL----------AKGMETNWrkYLDL 405
Cdd:cd16171 251 GSSHVPLLIMGPG---IKAGQqVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLlsessikespSRVPHPDW--VLSE 325
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2176971269 406 EHATCYSDDNYwcALTDGKIKYIwRIHTGTE---ELFDLTQDP 445
Cdd:cd16171 326 FHGCNVNASTY--MLRTNSWKYI-AYADGNSvppQLFDLSKDP 365
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-450 |
5.72e-29 |
|
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: 117.63 E-value: 5.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVI---SPNLDALAAEGTLFMNGYSScPSSTPARAGLLTGLSPWHHGLL-----GYGK 99
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVE-PSCTPGRAAFITGRHPIRTGLTtvglpGSPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 100 VSPEYKYEMPQMLKDAGYYTFGIGKmhWH----PQR--IKHGFegtllDEsgrvedenftsdyrqWFqtkapgknpdatg 173
Cdd:cd16142 80 GLPPWEPTLAELLKDAGYATAQFGK--WHlgdeDGRlpTDHGF-----DE---------------FY------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 174 iGWNDHTASIYklpenlhptywTGEMACELISNYDPTNKPLFLKVSFARPHSPYDPPQRYLDMYKDAlipdpaigdwcGK 253
Cdd:cd16142 125 -GNLYHTIDEE-----------IVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSSGK-----------GK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 254 YAKKLnpeetAQdapygnfgneyarnsrrhyyanitfIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMgDHYH----- 328
Cdd:cd16142 182 YADSM-----VE-------------------------LDDHVGQILDALDELGIADNTIVIFTTDNGPEQ-DVWPdggyt 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 329 -WRKTY--PYEGSTHVPYIVKWPsaNHVTPG-KTDAPVELRDILPTFLDAADVTIPTD--------MDGRSLLPLAKGME 396
Cdd:cd16142 231 pFRGEKgtTWEGGVRVPAIVRWP--GKIKPGrVSNEIVSHLDWFPTLAALAGAPDPKDkllgkdrhIDGVDQSPFLLGKS 308
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2176971269 397 TNWRkyldlEHATCYSDDNYWCALTDGKIKYIWRIHTGTEE-------------LFDLTQDPQELHN 450
Cdd:cd16142 309 EKSR-----RSEFFYFGEGELGAVRWKNWKVHFKAQEDTGGptgepfyvltfplIFNLRRDPKERYD 370
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
28-473 |
2.33e-27 |
|
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: 115.08 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLT-------GLSPWHHGLLGYGKV 100
Cdd:cd16159 2 PNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTgrypirsGMASSHGMRVILFTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 101 S----PEYKYEMPQMLKDAGYYTFGIGKMH------------WHPqrIKHGFE---G---TLLDESGRVEDENFTSDYRQ 158
Cdd:cd16159 82 SsgglPPNETTFAEVLKQQGYSTALIGKWHlglhcesrndfcHHP--LNHGFDyfyGlplTNLKDCGDGSNGEYDLSFDP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 159 WFQTKAPGKNPDATGIGWNDHTASIYKLP-------ENLHPTYW------TGEMACELISNYD----P------------ 209
Cdd:cd16159 160 LFPLLTAFVLITALTIFLLLYLGAVSKRFfvfllilSLLFISLFflllitNRYFNCILMRNHEvveqPmslenltqrltk 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 210 ---------TNKPLFLKVSFARPHSPYDPPQRYLdmykdalipdpaigdwcGKyakklnpeetAQDAPYGnfgneyarns 280
Cdd:cd16159 240 eaisflernKERPFLLVMSFLHVHTALFTSKKFK-----------------GR----------SKHGRYG---------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 281 rrhyyANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHG---------DMMGDH----YHWRKTYPYEGSTHVPYIVKW 347
Cdd:cd16159 283 -----DNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGghleeisvgGEYGGGnggiYGGKKMGGWEGGIRVPTIVRW 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 348 PSanHVTPGKT-DAPVELRDILPTFLDAADVTIPTD--MDGRSLLPLAKGMETNW-RKYL-----DLEHATCY---SDDN 415
Cdd:cd16159 358 PG--VIPPGSViDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLLTGQEKRSpHEFLfhycgAELHAVRYrprDGGA 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 416 YWcaltdgKIKYIW-RIHTGTE---------------------ELFDLTQDPQEL-HNAVNDKKYRRQLTEMRNEMIRHL 472
Cdd:cd16159 436 VW------KAHYFTpNFYPGTEgccgtllcrcfgdsvthhdppLLFDLSADPSESnPLDPTDEPYQEIIKKILEAVAEHQ 509
|
.
gi 2176971269 473 S 473
Cdd:cd16159 510 S 510
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
28-391 |
5.95e-27 |
|
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: 113.33 E-value: 5.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLL---GYGKVS--- 101
Cdd:cd16157 2 PNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYttnAHARNAytp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 102 -------PEYKYEMPQMLKDAGYYTFGIGKMH------WHPqrIKHGFegtlldesgrveDENFTS---DYRQWFQTKAP 165
Cdd:cd16157 82 qnivggiPDSEILLPELLKKAGYRNKIVGKWHlghrpqYHP--LKHGF------------DEWFGApncHFGPYDNKAYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 166 G----KNPDATGIGWNDHTASIYKLPENLHPTYWtgEMACELISNYDPTNKPLFLKVSFARPHSPYdppqryldmykdal 241
Cdd:cd16157 148 NipvyRDWEMIGRYYEEFKIDKKTGESNLTQIYL--QEALEFIEKQHDAQKPFFLYWAPDATHAPV-------------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 242 ipdpaigdwcgkYAKKlnpeetaqdapygnfgnEYARNSRRHYYAN-ITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHG 320
Cdd:cd16157 212 ------------YASK-----------------PFLGTSQRGLYGDaVMELDSSVGKILESLKSLGIENNTFVFFSSDNG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 321 D-MMGDHYHWRKTYP--------YEGSTHVPYIVKWPSanHVTPGKTDAPV-ELRDILPTFLDAADVTIPTD--MDGRSL 388
Cdd:cd16157 263 AaLISAPEQGGSNGPflcgkqttFEGGMREPAIAWWPG--HIKPGQVSHQLgSLMDLFTTSLALAGLPIPSDraIDGIDL 340
|
...
gi 2176971269 389 LPL 391
Cdd:cd16157 341 LPV 343
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
28-496 |
1.85e-23 |
|
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: 103.29 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLlgY-GKVSPEYKY 106
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGV--YpGVFYPGSRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 107 EMP-------QMLKDAGYYTFGIGKmhWHpqrIKHGFEGTLLdesgrveDENFTSDYR---QWFQTKAPGKN-----PDA 171
Cdd:cd16158 80 GLPlnettiaEVLKTVGYQTAMVGK--WH---LGVGLNGTYL-------PTHQGFDHYlgiPYSHDQGPCQNltcfpPNI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 172 TGIG------------WNDhtaSIYKLPEN---LHPTYwtGEMACELISNYDPTNKPLFLKVSFARPHSPYDPPQRYldm 236
Cdd:cd16158 148 PCFGgcdqgevpcplfYNE---SIVQQPVDlltLEERY--AKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKF--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 237 ykdalipdpaigdwcgkyakklnpeetAQDAPYGNFGNEYARnsrrhyyanitfIDEQIGRIIQTLKEKDMYNDALIVFV 316
Cdd:cd16158 220 ---------------------------AGRSSRGPFGDALAE------------LDGSVGELLQTLKENGIDNNTLVFFT 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 317 SDHG-DMMgdhyhWR------------KTYPYEGSTHVPYIVKWPSanHVTPGKTDAPVELRDILPTFLDAADVTIP-TD 382
Cdd:cd16158 261 SDNGpSTM-----RKsrggnagllkcgKGTTYEGGVREPAIAYWPG--RIKPGVTHELASTLDILPTIAKLAGAPLPnVT 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 383 MDGRSLLPLAkgMETNWRKYLDLEHATCYSDDNYWC-ALTDGKIK--YIWR--IHTGTEE-----------------LFD 440
Cdd:cd16158 334 LDGVDMSPIL--FEQGKSPRQTFFYYPTSPDPDKGVfAVRWGKYKahFYTQgaAHSGTTPdkdchpsaeltshdpplLFD 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2176971269 441 LTQDPQELHNAVNDKKYRRQLTEMRNEMIRHlsergeefvkdgrlvvkEKTMLYGP 496
Cdd:cd16158 412 LSQDPSENYNLLGLPEYNQVLKQIQQVKERF-----------------EASMKFGE 450
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
28-391 |
4.10e-21 |
|
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: 95.23 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVI-SPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPWHHGLL-GYGKVS---- 101
Cdd:cd16161 2 PNFLLLFADDLGWGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGhNFLPTSvggl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 102 PEYKYEMPQMLKDAGYYTFGIGKMH------WHPQriKHGFegtlldesgrveDENFTSDYRQwfqtkapgknpdatgig 175
Cdd:cd16161 82 PLNETTLAEVLRQAGYATGMIGKWHlgqreaYLPN--SRGF------------DYYFGIPFSH----------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 176 wNDHTASIYklpenlhptywtGEMACELISNYDPTNKPLFLKVSFARPHSPydppqryldmykDALIPDPaigdwcgkya 255
Cdd:cd16161 131 -DSSLADRY------------AQFATDFIQRASAKDRPFFLYAALAHVHVP------------LANLPRF---------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 256 kklnPEETAQDAPYGNFGNEyarnsrrhyyanitfIDEQIGRIIQTLKEKDMYNDALIVFVSD---------------HG 320
Cdd:cd16161 176 ----QSPTSGRGPYGDALQE---------------MDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTG 236
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2176971269 321 DMMGDHYhWR--KTYPYEGSTHVPYIVKWPsaNHVTPGKTD-APVELRDILPTFLDAADVTIPTD--MDGRSLLPL 391
Cdd:cd16161 237 DWQGNLG-GSvaKASTWEGGHREPAIVYWP--GRIPANSTSaALVSTLDIFPTVVALAGASLPPGriYDGKDLSPV 309
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-447 |
5.27e-21 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 94.72 E-value: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIG--CMGNDAVISPNLDALAAEGTLFMNGYSScPSSTPARAGLLTGLSPWHHGLLGYGKVSPEYK 105
Cdd:cd16154 1 PNILLIIADDQGLDSSAqySLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 106 YEMPQMLK----DAGYYTFGIGKmhWHpqrikhgFEGTLLDESGRVEDENFT-------SDYRQWFQTKApGKNPDATgi 174
Cdd:cd16154 80 ETLLQLLIkdatTAGYSSAVIGK--WH-------LGGNDNSPNNPGGIPYYAgilgggvQDYYNWNLTNN-GQTTNST-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 175 gwndhtasIYklpenlHPTYWTgEMACELISNydpTNKPLFLKVSFARPHSPYD-PPQrylDMYKDALIPD-PAIGDwcg 252
Cdd:cd16154 148 --------EY------ATTKLT-NLAIDWIDQ---QTKPWFLWLAYNAPHTPFHlPPA---ELHSRSLLGDsADIEA--- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 253 kyakklnpeetaqdapygnfgneyarNSRRHYYANITFIDEQIGRIIQTLKEKDMYNdALIVFVSDHG--DMMGDHYHWR 330
Cdd:cd16154 204 --------------------------NPRPYYLAAIEAMDTEIGRLLASIDEEEREN-TIIIFIGDNGtpGQVVDLPYTR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 331 ---KTYPYEGSTHVPYIVKWPSANHVTPgKTDAPVELRDILPTFLDAADVTIPTDMDGRSLLPLAKGMETNWRK--YLDL 405
Cdd:cd16154 257 nhaKGSLYEGGINVPLIVSGAGVERANE-RESALVNATDLYATIAELAGVDAAEIHDSVSFKPLLSDVNASTRQynYTEY 335
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2176971269 406 EHATCYSDdnywcaLTDGKIKYIWRIHTGTEELFDLTQDPQE 447
Cdd:cd16154 336 ESPTTTGW------ATRNQYYKLIESENGQEELYDLINDPSE 371
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
9-320 |
2.31e-19 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 89.81 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 9 YTLAVTAGVCSSFAYAQKHPHIILIMTDQQRADAIgcmgnDAVISPNLDALAAEGTLFMNGYSSCPSST-PARAGLLTGL 87
Cdd:COG1524 5 LSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFPSTTaPAHTTLLTGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 88 SPWHHGLLGYGKVSPEYKYEMpqmlkdagYYTFGIGKMHWHPQRIKHgfeGTLLDesgRVEDENFTSDYRQWFQTKAPGK 167
Cdd:COG1524 80 YPGEHGIVGNGWYDPELGRVV--------NSLSWVEDGFGSNSLLPV---PTIFE---RARAAGLTTAAVFWPSFEGSGL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 168 NpDATGIGWNDHTASIYKLPENlhpTYWTGEMACELISNYDPTnkplflkVSFArphspydppqrYLdmykdaliPDPai 247
Cdd:COG1524 146 I-DAARPYPYDGRKPLLGNPAA---DRWIAAAALELLREGRPD-------LLLV-----------YL--------PDL-- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2176971269 248 gDWCGKYakklnpeetaqdapYGNFGNEYArnsrrhyyANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHG 320
Cdd:COG1524 194 -DYAGHR--------------YGPDSPEYR--------AALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
28-375 |
5.96e-19 |
|
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: 85.94 E-value: 5.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLF-MNGYSSCPSSTPARAGLLTGLSPWHHGLLGYGKVSPEYKY 106
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 107 E----------MPQMLKDAGYYTFGIGkmhwhpqrikhgfegtLLDesgrvedenftsdyrqwfqtkapgknpdatgigw 176
Cdd:cd00016 81 RaagkdedgptIPELLKQAGYRTGVIG----------------LLK---------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 177 ndhtasiyklpenlhptywtgemACELISNydptNKPLFLKVSFARPHspydppqryldmykdalipdpaigdWCGKYAK 256
Cdd:cd00016 111 -----------------------AIDETSK----EKPFVLFLHFDGPD-------------------------GPGHAYG 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 257 KLNPEetaqdapygnfgneyarnsrrhYYANITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHWRKTY--- 333
Cdd:cd00016 139 PNTPE----------------------YYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADgka 196
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2176971269 334 -PYEGSTHVPYIVKWPSANHvtPGKTDAPVELRDILPTFLDAA 375
Cdd:cd00016 197 dKSHTGMRVPFIAYGPGVKK--GGVKHELISQYDIAPTLADLL 237
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
26-389 |
1.93e-18 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 88.17 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 26 KHPHIILIMTDQQRADAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSPwhhglLGYGKVSPEYK 105
Cdd:COG1368 233 KKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPP-----LPGGSPYKRPG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 106 YE----MPQMLKDAGYYTFGIgkmhwhpqrikHGFEGT------LLDESG--RVEDENftsDYrqwfqtkapgKNPDATG 173
Cdd:COG1368 308 QNnfpsLPSILKKQGYETSFF-----------HGGDGSfwnrdsFYKNLGfdEFYDRE---DF----------DDPFDGG 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 174 IGWNDHtaSIYKlpenlhptywtgemacELISNYDPTNKPLFLKVSFARPHSPYDPPQryldmyKDALIPDpaigdwcgk 253
Cdd:COG1368 364 WGVSDE--DLFD----------------KALEELEKLKKPFFAFLITLSNHGPYTLPE------EDKKIPD--------- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 254 yakklnpeetaqdapygnFGNEYARNSRRH-YYAnitfiDEQIGRIIQTLKEKDMYNDALIVFVSDHGdmmGDHYHWRKT 332
Cdd:COG1368 411 ------------------YGKTTLNNYLNAvRYA-----DQALGEFIEKLKKSGWYDNTIFVIYGDHG---PRSPGKTDY 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2176971269 333 YPYEGSTHVPYIVKwpSANHVTPGKTDAPVELRDILPTFLDAADVTIPTD-MDGRSLL 389
Cdd:COG1368 465 ENPLERYRVPLLIY--SPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYyAFGRDLL 520
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
28-376 |
4.32e-17 |
|
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: 81.58 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 28 PHIILIM----TDqqraDAIGCMGNDAVISPNLDALAAEGTLFMNGYSSCPSSTPARA--GLLTGLSPWHHGLLGYGKVS 101
Cdd:cd16015 1 PNVIVILlesfSD----PYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 102 PEYKYEMPQMLKDAGYYTFGIgkmhwhpqrikHGFEGTLldesgrvedENFTSDYRQ------WFQTKAPGKNPDATGIG 175
Cdd:cd16015 77 LNPLPSLPSILKEQGYETIFI-----------HGGDASF---------YNRDSVYPNlgfdefYDLEDFPDDEKETNGWG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 176 WNDHTasiyklpenlhptywTGEMACELISNYDPtnKPLFLKVSFARPHSPYDPPQRYLDMYKDALIPDPAIGDwcgkYA 255
Cdd:cd16015 137 VSDES---------------LFDQALEELEELKK--KPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTELEN----YL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 256 KKLNpeetaqdapygnfgneyarnsrrhyYAnitfiDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDHYHWRKTYPY 335
Cdd:cd16015 196 NAIH-------------------------YT-----DKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPL 245
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2176971269 336 EgSTHVPYIVKWPSAnhVTPGKTDAPVELRDILPTFLDAAD 376
Cdd:cd16015 246 D-LYRTPLLIYSPGL--KKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
20-372 |
5.06e-14 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 74.56 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 20 SFAYAQKHPHIILIMTDQQRADAIgcmgnDAVISPNLDALAAEGTLFMNGYSSCPSSTPARAGLLTGLSP--WHhGLLGy 97
Cdd:COG3083 237 QFSDPAKPPNILLIVVDSLRADML-----DPEVMPNLYAFAQRSLRFTNHYSSGNSTRAGLFGLFYGLPGnyWD-SILA- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 98 GKVSPEYkyeMPQMLKDAgyYTFGIgkmhwhpqrikhgfegtlldesgrvedenFTSD------YRQWFQTKAPGKNPDA 171
Cdd:COG3083 310 ERTPPVL---IDALQQQG--YQFGL-----------------------------FSSAgfnsplFRQTIFSDVSLPRLHT 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 172 TGIGWNDHTASIYKLPEnlhptyWtgemacelISNYDPtNKPLFLKVSFARPHSPYDPPQryldmykdalipdpaigdwc 251
Cdd:COG3083 356 PGGPAQRDRQITAQWLQ------W--------LDQRDS-DRPWFSYLFLDAPHAYSFPAD-------------------- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 252 gkYAKKLNPEEtaqDAPYGNFGNEYARNSRRHYYAN-ITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGDMMGDH--YH 328
Cdd:COG3083 401 --YPKPFQPSE---DCNYLALDNESDPTPFKNRYRNaVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENgqNY 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2176971269 329 WRKTYPY-EGSTHVPYIVKWPSAnhvTPGKTDAPVELRDILPTFL 372
Cdd:COG3083 476 WGHNSNFsRYQLQVPLVIHWPGT---PPQVISKLTSHLDIVPTLM 517
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
379-470 |
3.15e-09 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 54.18 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 379 IPTDMDGRSLLPLAKG-METNWRKYL-------DLEHAT--CY--SDDNYwcaltdgK-IKYIWRIHTGteELFDLTQDP 445
Cdd:pfam16347 1 IPADMQGKSFLPLLKGkKPKNWRDALyyhyyeyPAEHAVkrHYgvRTERY-------KlIHFYNDIDEW--ELYDLQKDP 71
|
90 100
....*....|....*....|....*
gi 2176971269 446 QELHNAVNDKKYRRQLTEMRNEMIR 470
Cdd:pfam16347 72 KEMNNVYGDPEYAEVQAELKEELEE 96
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
288-389 |
1.72e-08 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 56.65 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 288 ITFIDEQIGRIIQTLKEKDMyndALIVfVSDHG--DMMGDhyhwrktyPYEGSTH-------VPYIVkwpsanhVTPGKT 358
Cdd:cd16010 409 VEAVDECLGRIVEAVLENGG---TLLI-TADHGnaEEMID--------PETGGPHtahttnpVPFII-------VDPGLK 469
|
90 100 110
....*....|....*....|....*....|....
gi 2176971269 359 DAPVE---LRDILPTFLDAADVTIPTDMDGRSLL 389
Cdd:cd16010 470 RKLLKdggLADVAPTILDLLGIEKPKEMTGKSLI 503
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
285-378 |
4.13e-08 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 54.55 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 285 YAN-ITFIDEQIGRIIQTLKEKDmyNDALIVFVSDHGDMMGDHYHWR--KTYPYEGSTHVPYIVkW--PSANHVTPGKT- 358
Cdd:cd16017 188 YDNsILYTDYVLSQIIERLKKKD--KDAALIYFSDHGESLGENGLYLhgAPYAPKEQYHVPFII-WssDSYKQRYPVERl 264
|
90 100
....*....|....*....|....
gi 2176971269 359 ----DAPVELRDILPTFLDAADVT 378
Cdd:cd16017 265 rankDRPFSHDNLFHTLLGLLGIK 288
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
288-389 |
1.20e-07 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 53.95 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 288 ITFIDEQIGRIIQTLKEKDmyNDALIVfvSDHG--DMMGDhyhwrktyPYEGSTH-------VPYIVKWPSANHVTPGKt 358
Cdd:PRK05434 414 VEAVDECLGRVVDAVLKVG--GTLLIT--ADHGnaEQMID--------PETGQPHtahttnpVPFILVGGKALRLEGGK- 480
|
90 100 110
....*....|....*....|....*....|.
gi 2176971269 359 dapveLRDILPTFLDAADVTIPTDMDGRSLL 389
Cdd:PRK05434 481 -----LADIAPTILDLLGLEQPAEMTGKSLI 506
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
31-373 |
1.75e-07 |
|
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: 53.19 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 31 ILIMTDQQRADAIgcmgNDAVISPNLDALAAEGTLFMNGYSSCPSST-PARAGLLTGLSPWHHGLLGYGKVSPEYKYEMP 109
Cdd:pfam01663 2 LVISLDGFRADYL----DRFELTPNLAALAKEGVSAPNLTPVFPTLTfPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 110 QMLKDAGYYTFgigkmhWHPQRIkhgfegtlLDESGRvedENFTSDYRQWfqtkaPGKNPDATgiGWNDHTASIYKLPEN 189
Cdd:pfam01663 78 FVISDPEDPRW------WQGEPI--------WDTAAK---AGVRAAALFW-----PGSEVDYS--TYYGTPPRYLKDDYN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 190 LHPTYWtGEMACELISNydptnkplFLKVSFArpHSPYDPPQRYLdmykdALIPDPaigDWCGKYakklnpeetaqdapY 269
Cdd:pfam01663 134 NSVPFE-DRVDTAVLQT--------WLDLPFA--DVAAERPDLLL-----VYLEEP---DYAGHR--------------Y 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 270 GNFGNEYARNSRRhyyanitfIDEQIGRIIQTLKEKDMYNDALIVFVSDHG--DMMGDH-------------YHWRKTYP 334
Cdd:pfam01663 181 GPDSPEVEDALRR--------VDRAIGDLLEALDERGLFEDTNVIVVSDHGmtPVSDDKviflndylrekglLHLVDGGP 252
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2176971269 335 YEGSThvpyiVKWPSANHVTPGKTDA-PVELRDILPTFLD 373
Cdd:pfam01663 253 VVAIY-----PKARELGHVPPGEVEEvYAELKEKLLGLRI 287
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
288-373 |
7.72e-07 |
|
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: 50.66 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 288 ITFIDEQIGRIIQTLKEKDMYNDALIVFVSDHGdMM--GDH-YHwrktyPYEGSTHVPYIVKWPSanhVTPGKTDAPVEL 364
Cdd:cd16018 185 LKRVDRRLGYLIEALKERGLLDDTNIIVVSDHG-MTdvGTHgYD-----NELPDMRAIFIARGPA---FKKGKKLGPFRN 255
|
....*....
gi 2176971269 365 RDILPTFLD 373
Cdd:cd16018 256 VDIYPLMCN 264
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
291-389 |
2.28e-06 |
|
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-independent), AlkP superfamily is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440460 Cd Length: 511 Bit Score: 50.05 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 291 IDEQIGRIIQTLKEKDMyndALIVfVSDHG--DMMGDhyhwrktyPYEGSTH-------VPYIVkwpsanhVTPGKTdap 361
Cdd:COG0696 418 VDECLGRVVDAVLAAGG---TLLI-TADHGnaEQMID--------PDTGGPHtahttnpVPFIL-------VGGDKG--- 475
|
90 100 110
....*....|....*....|....*....|....
gi 2176971269 362 VELR------DILPTFLDAADVTIPTDMDGRSLL 389
Cdd:COG0696 476 VKLRedgrlaDIAPTILELMGLPQPAEMTGKSLI 509
|
|
| PRK09598 |
PRK09598 |
phosphoethanolamine--lipid A transferase EptA; |
285-381 |
9.46e-04 |
|
phosphoethanolamine--lipid A transferase EptA;
Pssm-ID: 236581 [Multi-domain] Cd Length: 522 Bit Score: 41.69 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176971269 285 YAN-ITFIDEQIGRIIQTLKEkdMYNDALIVFVSDHGDMMGDHYHWRKTYPY----EGSTHVPYIVkWPSANHV---TPG 356
Cdd:PRK09598 406 YDNtIFYNDYLLDKIISMLKN--LKQPALMIYLSDHGESLGEGAFYLHGIPKsiapKEQYEIPFIV-WASDSFKkqhSII 482
|
90 100
....*....|....*....|....*
gi 2176971269 357 KTDAPVELRDILPTFLDAADVTIPT 381
Cdd:PRK09598 483 QTQTPINQNVIFHSVLGVFDFKNPS 507
|
|
| |
