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Conserved domains on  [gi|1907068830|ref|XP_036020589|]
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extracellular sulfatase Sulf-1 isoform X2 [Mus musculus]

Protein Classification

G6S and DUF3740 domain-containing protein( domain architecture ID 10888354)

G6S and DUF3740 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
42-384 0e+00

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: 544.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQDVELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE--NCSSPSWQA 119
Cdd:cd16147      1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  120 MHEPRTFAVYLNNTGYRTAFFGKYLNEY----NGSYIPPGWREWLGLIKNSRFYNYTVCrNGIKEKHGFDYAKDYFTDLI 195
Cdd:cd16147     81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  196 TNESINYFKMSKRMypHRPIMMVISHAAPHGPEDSAPQFSKLYPNAS-QHITPSYNYAPNMDKHWIMQYTGPMLPiHMEF 274
Cdd:cd16147    160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLNPT-QIAY 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  275 TNVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSIEPGSI 354
Cdd:cd16147    237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
                          330       340       350
                   ....*....|....*....|....*....|
gi 1907068830  355 VPQIVLNIDLAPTILDIAGLDSPSDVDGKS 384
Cdd:cd16147    317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
DUF3740 pfam12548
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ...
534-678 6.25e-68

Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and 173 amino acids in length. The family is found in association with pfam00884.


:

Pssm-ID: 463628  Cd Length: 142  Bit Score: 224.15  E-value: 6.25e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  534 KPRFVHTRQTRSLSVEFEGEIYDINLEEEeLQVLPPRSIAKRH--DEGHQGFIGHQAAAGDirneMLADSNNAVGLPATV 611
Cdd:pfam12548    1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEE-YQPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPASV 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907068830  612 RVTHKCFILPNDTIHCERELYQSARAWKDHKAYIDKEIEVLQDKIKNLREVRGHLKKRKPEECGCGD 678
Cdd:pfam12548   76 KVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
ALP_like super family cl23718
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
767-808 2.68e-15

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.


The actual alignment was detected with superfamily member cd16147:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 396  Bit Score: 79.13  E-value: 2.68e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907068830  767 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQ 808
Cdd:cd16147    347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQ 388
 
Name Accession Description Interval E-value
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
42-384 0e+00

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: 544.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQDVELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE--NCSSPSWQA 119
Cdd:cd16147      1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  120 MHEPRTFAVYLNNTGYRTAFFGKYLNEY----NGSYIPPGWREWLGLIKNSRFYNYTVCrNGIKEKHGFDYAKDYFTDLI 195
Cdd:cd16147     81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  196 TNESINYFKMSKRMypHRPIMMVISHAAPHGPEDSAPQFSKLYPNAS-QHITPSYNYAPNMDKHWIMQYTGPMLPiHMEF 274
Cdd:cd16147    160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLNPT-QIAY 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  275 TNVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSIEPGSI 354
Cdd:cd16147    237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
                          330       340       350
                   ....*....|....*....|....*....|
gi 1907068830  355 VPQIVLNIDLAPTILDIAGLDSPSDVDGKS 384
Cdd:cd16147    317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
42-414 2.98e-74

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 251.34  E-value: 2.98e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQDVelGSLQVMNKTR-------KIMEQGgATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcsS 114
Cdd:COG3119     23 RPNILFILADDLGY--GDLGCYGNPLiktpnidRLAAEG-VRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEG--Y 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  115 PSWQAMHEPrTFAVYLNNTGYRTAFFGKYLNeyngsyippgwrewlgliknsrfynytvcrngikekhgfdyakdYFTDL 194
Cdd:COG3119     98 NGGLPPDEP-TLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDL 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  195 ITNESINYfkMSKRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYPNasQHITPSYNYAPNMDKHWIMQYtgpmlpihmef 274
Cdd:COG3119    133 LTDKAIDF--LERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR----------- 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  275 tnvLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SIEPGS 353
Cdd:COG3119    198 ---ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPgKIKAGS 274
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068830  354 IVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLdlekpgnrfrTNKKAKiWRDTFLVE 414
Cdd:COG3119    275 VSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLL----------TGEKAE-WRDYLYWE 324
DUF3740 pfam12548
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ...
534-678 6.25e-68

Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and 173 amino acids in length. The family is found in association with pfam00884.


Pssm-ID: 463628  Cd Length: 142  Bit Score: 224.15  E-value: 6.25e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  534 KPRFVHTRQTRSLSVEFEGEIYDINLEEEeLQVLPPRSIAKRH--DEGHQGFIGHQAAAGDirneMLADSNNAVGLPATV 611
Cdd:pfam12548    1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEE-YQPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPASV 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907068830  612 RVTHKCFILPNDTIHCERELYQSARAWKDHKAYIDKEIEVLQDKIKNLREVRGHLKKRKPEECGCGD 678
Cdd:pfam12548   76 KVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
Sulfatase pfam00884
Sulfatase;
43-374 1.64e-48

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 174.92  E-value: 1.64e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQ-DVELGSLQ-VMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNEncsspsWQ 118
Cdd:pfam00884    1 PNVVLVLGESLrAPDLGLYGyPRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------VG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  119 AMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGLIKNSRFYNYTVCRNGIKEKHGfdyakdYFTDLIT 196
Cdd:pfam00884   75 LPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYADPPDVPYNCSGGG------VSDEALL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  197 NESINYfkmskRMYPHRPIMMVISHAAPHGPedsaPQFSKLYPNASQHITPSYNYAPNMDkhwimqytgpmlpihmeftn 276
Cdd:pfam00884  149 DEALEF-----LDNNDKPFFLVLHTLGSHGP----PYYPDRYPEKYATFKPSSCSEEQLL-------------------- 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  277 vlqRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFG--LVKGKSM-PYDFDIRVPFFIRGP-SIEPG 352
Cdd:pfam00884  200 ---NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPgGKAKG 276
                          330       340
                   ....*....|....*....|..
gi 1907068830  353 SIVPQIVLNIDLAPTILDIAGL 374
Cdd:pfam00884  277 QKSEALVSHVDLFPTILDLAGI 298
PRK13759 PRK13759
arylsulfatase; Provisional
42-397 3.36e-28

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 119.77  E-value: 3.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQDVE-LGSL---QVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSspsW 117
Cdd:PRK13759     6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  118 QAMHE-PRTFAvylnNTGYRTAFFGKYlneyngSYIPPgwREWLGLiKNSRFYNYTVCRNGIKEKHGFDYAKDY------ 190
Cdd:PRK13759    83 NYKNTlPQEFR----DAGYYTQCIGKM------HVFPQ--RNLLGF-HNVLLHDGYLHSGRNEDKSQFDFVSDYlawlre 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  191 --------FTDL-----------------------ITNESINYFKmskRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYP 239
Cdd:PRK13759   150 kapgkdpdLTDIgwdcnswvarpwdleerlhptnwVGSESIEFLR---RRDPTKPFFLKMSFARPHSPYDPPKRYFDMYK 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  240 NASQHITPSYNYAPNMDKH-WIMQYTGPMLPIHMEftnVLQRKRLQTLMS---VDDSVERLYNMLVESGELDNTYIIYTA 315
Cdd:PRK13759   227 DADIPDPHIGDWEYAEDQDpEGGSIDALRGNLGEE---YARRARAAYYGLithIDHQIGRFLQALKEFGLLDNTIILFVS 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  316 DHGYHIGQFGLVKgKSMPYDFDIRVPFFIRGPS----IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDL 391
Cdd:PRK13759   304 DHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFG 382

                   ....*.
gi 1907068830  392 EKPGNR 397
Cdd:PRK13759   383 QYEGWR 388
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
767-808 2.68e-15

glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).


Pssm-ID: 293766 [Multi-domain]  Cd Length: 396  Bit Score: 79.13  E-value: 2.68e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907068830  767 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQ 808
Cdd:cd16147    347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQ 388
 
Name Accession Description Interval E-value
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
42-384 0e+00

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: 544.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQDVELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE--NCSSPSWQA 119
Cdd:cd16147      1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  120 MHEPRTFAVYLNNTGYRTAFFGKYLNEY----NGSYIPPGWREWLGLIKNSRFYNYTVCrNGIKEKHGFDYAKDYFTDLI 195
Cdd:cd16147     81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  196 TNESINYFKMSKRMypHRPIMMVISHAAPHGPEDSAPQFSKLYPNAS-QHITPSYNYAPNMDKHWIMQYTGPMLPiHMEF 274
Cdd:cd16147    160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLNPT-QIAY 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  275 TNVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSIEPGSI 354
Cdd:cd16147    237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
                          330       340       350
                   ....*....|....*....|....*....|
gi 1907068830  355 VPQIVLNIDLAPTILDIAGLDSPSDVDGKS 384
Cdd:cd16147    317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
42-414 9.00e-87

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: 286.73  E-value: 9.00e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQ--DVeLGSLQ-VMNKT---RKIMEQGgATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcSSP 115
Cdd:cd16031      2 RPNIIFILTDDHryDA-LGCYGnPIVKTpniDRLAKEG-VRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP-LFD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  116 SWQamhepRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPPGWREWLGLIKNSRFYNYTVCRNGIKEKHgfdyaKDYFTDLI 195
Cdd:cd16031     79 ASQ-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENGKRVGQ-----KGYVTDII 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  196 TNESINYFKmsKRMyPHRPIMMVISHAAPHGPEDSAPQFSKLYPNAsqHITPSYNYAPN-------------MDKHWIMQ 262
Cdd:cd16031    149 TDKALDFLK--ERD-KDKPFCLSLSFKAPHRPFTPAPRHRGLYEDV--TIPEPETFDDDdyagrpewareqrNRIRGVLD 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  263 YtgpmlPIHMEFTnvLQR--KR-LQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIR 339
Cdd:cd16031    224 G-----RFDTPEK--YQRymKDyLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIR 295
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068830  340 VPFFIRGP-SIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDlekpgnrfrtNKKAKIWRDTFLVE 414
Cdd:cd16031    296 VPLIIRDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLE----------GEKPVDWRKEFYYE 361
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
42-414 2.98e-74

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 251.34  E-value: 2.98e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQDVelGSLQVMNKTR-------KIMEQGgATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcsS 114
Cdd:COG3119     23 RPNILFILADDLGY--GDLGCYGNPLiktpnidRLAAEG-VRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEG--Y 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  115 PSWQAMHEPrTFAVYLNNTGYRTAFFGKYLNeyngsyippgwrewlgliknsrfynytvcrngikekhgfdyakdYFTDL 194
Cdd:COG3119     98 NGGLPPDEP-TLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDL 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  195 ITNESINYfkMSKRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYPNasQHITPSYNYAPNMDKHWIMQYtgpmlpihmef 274
Cdd:COG3119    133 LTDKAIDF--LERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR----------- 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  275 tnvLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SIEPGS 353
Cdd:COG3119    198 ---ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPgKIKAGS 274
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068830  354 IVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLdlekpgnrfrTNKKAKiWRDTFLVE 414
Cdd:COG3119    275 VSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLL----------TGEKAE-WRDYLYWE 324
DUF3740 pfam12548
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ...
534-678 6.25e-68

Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and 173 amino acids in length. The family is found in association with pfam00884.


Pssm-ID: 463628  Cd Length: 142  Bit Score: 224.15  E-value: 6.25e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  534 KPRFVHTRQTRSLSVEFEGEIYDINLEEEeLQVLPPRSIAKRH--DEGHQGFIGHQAAAGDirneMLADSNNAVGLPATV 611
Cdd:pfam12548    1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEE-YQPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPASV 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907068830  612 RVTHKCFILPNDTIHCERELYQSARAWKDHKAYIDKEIEVLQDKIKNLREVRGHLKKRKPEECGCGD 678
Cdd:pfam12548   76 KVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
43-384 3.18e-53

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: 186.10  E-value: 3.18e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQ---DVE-LGSLQVmnKT---RKIMEQGgATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcssp 115
Cdd:cd16022      1 PNILLIMTDDLgydDLGcYGNPDI--KTpnlDRLAAEG-VRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN---- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  116 SWQAMHEPRTFAVYLNNTGYRTAFFGKylneyngsyippgwreWlgliknsrfynytvcrngikekHgfdyakdyftdli 195
Cdd:cd16022     74 GGGLPPDEPTLAELLKEAGYRTALIGK----------------W----------------------H------------- 102
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  196 tNESINYFKmskRMYPHRPIMMVISHAAPHGPedsapqfsklypnasqhitpsYNYAPNMDkhwimqytgpmlpihmeft 275
Cdd:cd16022    103 -DEAIDFIE---RRDKDKPFFLYVSFNAPHPP---------------------FAYYAMVS------------------- 138
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  276 nvlqrkrlqtlmSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SIEPGSI 354
Cdd:cd16022    139 ------------AIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPgKIPAGQV 206
                          330       340       350
                   ....*....|....*....|....*....|
gi 1907068830  355 VPQIVLNIDLAPTILDIAGLDSPSDVDGKS 384
Cdd:cd16022    207 SDALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
42-389 1.22e-52

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: 190.09  E-value: 1.22e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDD---QDveLGSLQVMN-KTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTnneNCSSP 115
Cdd:cd16034      1 KPNILFIFADQhraQA--LGCAGDDPvKTPNLdrLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFG---NDVPL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  116 SwqamHEPRTFAVYLNNTGYRTAFFGKY-LNE-------YNGSYIPP----GWREWLGLIKNSRFYNYTVCRNGIKEKHG 183
Cdd:cd16034     76 P----PDAPTIADVLKDAGYRTGYIGKWhLDGperndgrADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGKRIYI 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  184 FDYAKDYFTDLItnesINYfkMSKRMYPHRPIMMVISHAAPHGPEDSAPQ-FSKLYPNASQHITPsyNYAPNMD-----K 257
Cdd:cd16034    152 KGYSPDAETDLA----IEY--LENQADKDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLLLRP--NVPEDKKeeaglR 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  258 HWIMQYtgpmlpihmeFTNVLqrkrlqtlmSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFD 337
Cdd:cd16034    224 EDLRGY----------YAMIT---------ALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVPYEES 283
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907068830  338 IRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLL 389
Cdd:cd16034    284 IRVPFIIRYPGkIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLL 336
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
43-397 2.10e-49

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: 180.01  E-value: 2.10e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQDVELGSlqVMN---KTRKIME--QGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTN-NENCSSPS 116
Cdd:cd16027      1 PNILWIIADDLSPDLGG--YGGnvvKTPNLDRlaAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLrSRGFPLPD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  117 WQamhepRTFAVYLNNTGYRTAFFGKYlnEYNGSYIPPGWrewlgliknsrFYNYTVCRNGIKEKHGFDYAKDYFTDLIT 196
Cdd:cd16027     79 GV-----KTLPELLREAGYYTGLIGKT--HYNPDAVFPFD-----------DEMRGPDDGGRNAWDYASNAADFLNRAKK 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  197 NE----SINYFkmskrmYPHRPIMMVISHAAPHGPEDsapqfsklypnasqhITPSYNYA--PNMDKHWIMQYTgpmlpi 270
Cdd:cd16027    141 GQpfflWFGFH------DPHRPYPPGDGEEPGYDPEK---------------VKVPPYLPdtPEVREDLADYYD------ 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  271 hmeftnvlqrkrlqTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYhigqfGLVKGKSMPYDFDIRVPFFIRGPS-I 349
Cdd:cd16027    194 --------------EIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkI 254
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1907068830  350 EPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNR 397
Cdd:cd16027    255 KPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGR 302
Sulfatase pfam00884
Sulfatase;
43-374 1.64e-48

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 174.92  E-value: 1.64e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQ-DVELGSLQ-VMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNEncsspsWQ 118
Cdd:pfam00884    1 PNVVLVLGESLrAPDLGLYGyPRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------VG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  119 AMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGLIKNSRFYNYTVCRNGIKEKHGfdyakdYFTDLIT 196
Cdd:pfam00884   75 LPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYADPPDVPYNCSGGG------VSDEALL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  197 NESINYfkmskRMYPHRPIMMVISHAAPHGPedsaPQFSKLYPNASQHITPSYNYAPNMDkhwimqytgpmlpihmeftn 276
Cdd:pfam00884  149 DEALEF-----LDNNDKPFFLVLHTLGSHGP----PYYPDRYPEKYATFKPSSCSEEQLL-------------------- 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  277 vlqRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFG--LVKGKSM-PYDFDIRVPFFIRGP-SIEPG 352
Cdd:pfam00884  200 ---NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPgGKAKG 276
                          330       340
                   ....*....|....*....|..
gi 1907068830  353 SIVPQIVLNIDLAPTILDIAGL 374
Cdd:pfam00884  277 QKSEALVSHVDLFPTILDLAGI 298
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
43-389 7.84e-47

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: 173.88  E-value: 7.84e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDD---QDVelgSLQvMNKtrkIME--------QGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYT---- 107
Cdd:cd16144      1 PNIVLILVDDlgwADL---GCY-GSK---FYEtpnidrlaKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDvipg 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  108 ------NNENCSSPSWQAM-HEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYipP---GWREWLGLIKNSRFYNYTVCRN 176
Cdd:cd16144     74 rrgppdNTKLIPPPSTTRLpLEEVTIAEALKDAGYATAHFGKWhLGGEGGYG--PedqGFDVNIGGTGNGGPPSYYFPPG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  177 GIKEKHGFDYAKDYFTDLITNESINYFKMSKRmyphRPIMMVISHAAPHGPEDSAPQFSKLYpnasqhitpsYNYAPNMD 256
Cdd:cd16144    152 KPNPDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLYLSHYAVHTPIQARPELIEKY----------EKKKKGLR 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  257 KHWIMQYTGPMLpihmeftnvlqrkrlqtlMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLV-------KG 329
Cdd:cd16144    218 KGQKNPVYAAMI------------------ESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGG 279
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907068830  330 KSMPYDFDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLD--SPSDVDGKSVLKLL 389
Cdd:cd16144    280 KGSLYEGGIRVPLIVRWPGvIKPGSVSDVPVIGTDLYPTFLELAGGPlpPPQHLDGVSLVPLL 342
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-414 2.54e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 172.02  E-value: 2.54e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQDV----ELGSLQVmnKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd16033      1 PNILFIMTDQQRYdtlgCYGNPIV--KTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  117 WQAMHEPRTFAVYLNNTGYRTAFFGKylneyngsyippgWRewlgliknsrfynytVCRNGIKEKHGFDY------AKDY 190
Cdd:cd16033     79 RGLPPGVETFSEDLREAGYRNGYVGK-------------WH---------------VGPEETPLDYGFDEylpvetTIEY 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  191 FTDLITNESINYFKMSKRmyphrPIMMVISHAAPHGPEDSAPQFSKLYPNASqhITPSYNYAPNM-DKHWImQYTGPMLP 269
Cdd:cd16033    131 FLADRAIEMLEELAADDK-----PFFLRVNFWGPHDPYIPPEPYLDMYDPED--IPLPESFADDFeDKPYI-YRRERKRW 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  270 IHMEFTNVLQRKRLQ------TLMsvDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLV-KGKSMpYDFDIRVPF 342
Cdd:cd16033    203 GVDTEDEEDWKEIIAhywgyiTLI--DDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIPL 279
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907068830  343 FIRGP-SIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNrfrtnkkakiWRDTFLVE 414
Cdd:cd16033    280 IIKWPgVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPED----------WRDEVVTE 342
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
43-400 1.71e-40

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: 155.02  E-value: 1.71e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQDVelGSLQVMN----KT---RKIMEQGgATFTNaFVTTPMCCPSRSSMLTGKYVHNHNVYTnnencSSP 115
Cdd:cd16146      1 PNVILILTDDQGY--GDLGFHGnpilKTpnlDRLAAES-VRFTN-FHVSPVCAPTRAALLTGRYPFRTGVWH-----TIL 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  116 SWQAMH-EPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGL-----------IKNSRFYNyTVCRNGIKEK 181
Cdd:cd16146     72 GRERMRlDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFDEVLGHggggigqypdyWGNDYFDD-TYYHNGKFVK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  182 HgfdyaKDYFTDLITNESINYFKMSKrmypHRPIMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNYApnmdkhwim 261
Cdd:cd16146    151 T-----EGYCTDVFFDEAIDFIEENK----DKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAFYG--------- 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  262 qytgpMLpihmefTNvlqrkrlqtlmsVDDSVERLYNMLVESGELDNTYIIYTADHGYHIG-----QFGLVKGKSMPYDF 336
Cdd:cd16146    213 -----MI------EN------------IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYEG 269
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907068830  337 DIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDV--DGKSVLKLLDLEKPGNRFRT 400
Cdd:cd16146    270 GHRVPFFIRWPGkILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIklDGRSLLPLLKGESDPWPERT 336
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
74-398 3.31e-40

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: 151.54  E-value: 3.31e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   74 GATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSpswqamhEPRTFAVYLNNTGYRTAFFGK--YLNEyngsy 151
Cdd:cd16037     36 GTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG-------DVPSWGHALRAAGYETVLIGKlhFRGE----- 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  152 ippgwrewlgliknsrfynytvcrngiKEKHGFDYakdyfTDLITNESINYFKmsKRMYPHRPIMMVISHAAPHGPEDSA 231
Cdd:cd16037    104 ---------------------------DQRHGFRY-----DRDVTEAAVDWLR--EEAADDKPWFLFVGFVAPHFPLIAP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  232 PQFSKLYpnasqhitpsynyapnmdkhwimqytgpmlpihmeftnvlqRKRLQT----LMS-VDDSVERLYNMLVESGEL 306
Cdd:cd16037    150 QEFYDLY-----------------------------------------VRRARAayygLVEfLDENIGRVLDALEELGLL 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  307 DNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVL 386
Cdd:cd16037    189 DNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLL 267
                          330
                   ....*....|..
gi 1907068830  387 KLLDLEKPGNRF 398
Cdd:cd16037    268 PLAEGPDDPDRV 279
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
43-389 5.86e-39

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: 150.44  E-value: 5.86e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQDV-ELGSL-QVMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWQ 118
Cdd:cd16145      1 PNIIFILADDLGYgDLGCYgQKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  119 AmhEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYIPP--GWREWLG--------------LIKNSR--FYNYTVCRNGIK 179
Cdd:cd16145     81 P--DDVTLAEVLKKAGYATAAFGKWgLGGPGTPGHPTkqGFDYFYGyldqvhahnyypeyLWRNGEkvPLPNNVIPPLDE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  180 EKHGFDYAKDYFTDLITNESINYFKMSKRmyphRPIMMVISHAAPHGPEDsAPQFSklyPNASQHITPSYNYAPNMDKhw 259
Cdd:cd16145    159 GNNAGGGGGTYSHDLFTDEALDFIRENKD----KPFFLYLAYTLPHAPLQ-VPDDG---PYKYKPKDPGIYAYLPWPQ-- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  260 imqytgpmlpihmeftnvlQRKRLQTLMS-VDDSVERLYNMLVESGELDNTYIIYTADHGYHI-------GQF-----GL 326
Cdd:cd16145    229 -------------------PEKAYAAMVTrLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfdsngPL 289
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907068830  327 VKGK-SMpYDFDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLL 389
Cdd:cd16145    290 RGYKrSL-YEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTL 353
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
42-397 8.29e-39

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: 148.87  E-value: 8.29e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQDVE----LGSLQVmnKTRKI--MEQGGATFTNAFVTTPM----CCPSRSSMLTGKYVHNhnvYTNNEN 111
Cdd:cd16155      2 KPNILFILADDQRADtigaLGNPEI--QTPNLdrLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH---APEGGK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  112 CSSPSwqamhEPRTFAVYLNNTGYRTAFFGKYLNEYngsyippgwrewlgliknsrfynytvcrngikekhgfdyakdyf 191
Cdd:cd16155     77 AAIPS-----DDKTWPETFKKAGYRTFATGKWHNGF-------------------------------------------- 107
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  192 tdliTNESINYFKmsKRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYPnaSQHITPSYNYAPnmdKHwimQYTGPMLPIH 271
Cdd:cd16155    108 ----ADAAIEFLE--EYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYP--PETIPLPENFLP---QH---PFDNGEGTVR 173
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  272 MEFT--------NVlqRKRLQ----TLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIR 339
Cdd:cd16155    174 DEQLapfprtpeAV--RQHLAeyyaMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM-GKQNLYEHSMR 250
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907068830  340 VPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNR 397
Cdd:cd16155    251 VPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVR 308
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
42-397 8.65e-38

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 145.83  E-value: 8.65e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQ--DVeLGSL-QVMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenCSSPS 116
Cdd:cd16152      1 KPNVIVFFTDQQrwDT-LGCYgQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNG--IPLPA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  117 wqamhEPRTFAVYLNNTGYRTAFFGKylneyngsyippgwreWlgliknsrfynytvcrngikekHGFDYAKDYFTDLit 196
Cdd:cd16152     78 -----DEKTLAHYFRDAGYETGYVGK----------------W----------------------HLAGYRVDALTDF-- 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  197 neSINYfkMSKRMyPHRPIMMVISHAAPH---------GPEDSAPQFSKLYP---------NASQHItPSYnyapnmdkh 258
Cdd:cd16152    113 --AIDY--LDNRQ-KDKPFFLFLSYLEPHhqndrdryvAPEGSAERFANFWVppdlaalpgDWAEEL-PDY--------- 177
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  259 wimqytgpmlpihmeftnvlqrkrLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHigqFGLVKG--KSMPYDF 336
Cdd:cd16152    178 ------------------------LGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHES 230
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068830  337 DIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNR 397
Cdd:cd16152    231 SIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVEDWR 291
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
42-390 6.89e-35

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: 138.86  E-value: 6.89e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQDVELGSLQvmnktRKIME--------QGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNencs 113
Cdd:cd16030      2 KPNVLFIAVDDLRPWLGCYG-----GHPAKtpnidrlaARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNN---- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  114 SPSWQAMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYI--PPGWREWLGLIKNSRFYNYTVCRNGIKEKHG-------- 183
Cdd:cd16030     73 SYFRKVAPDAVTLPQYFKENGYTTAGVGKIFHPGIPDGDddPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGgggpawea 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  184 FDYAKDYFTD-LITNESINYFKMSKRMypHRPIMMVISHAAPHGPEdSAPQ-FSKLYPNASQHITPSYN------YAPNm 255
Cdd:cd16030    153 ADVPDEAYPDgKVADEAIEQLRKLKDS--DKPFFLAVGFYKPHLPF-VAPKkYFDLYPLESIPLPNPFDpidlpeVAWN- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  256 DKHWIMQYTGPMLPIHMEFTNVL----QRKRLQT-LMSV---DDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLV 327
Cdd:cd16030    229 DLDDLPKYGDIPALNPGDPKGPLpdeqARELRQAyYASVsyvDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHW 308
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907068830  328 kGKSMPYDFDIRVPFFIRGPSI-EPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLD 390
Cdd:cd16030    309 -GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLK 371
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
42-389 6.10e-34

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: 135.38  E-value: 6.10e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQ---DVE-LGSlqVMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKY-----VHNHNVYTNNE 110
Cdd:cd16026      1 KPNIVVILADDLgygDLGcYGS--PLIKTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvgLPGVVGPPGSK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  111 NCSSPSwqamhEPrTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGL----------IKNSRFYNYTVCRNGI 178
Cdd:cd16026     79 GGLPPD-----EI-TIAEVLKKAGYRTALVGKWHLGHQPEFLPTrhGFDEYFGIpysndmwpfpLYRNDPPGPLPPLMEN 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  179 KEKHGFDYAKDYFTDLITNESINYFKMSKrmypHRPIMMVISHAAPHGPEDSAPQFSklypNASQHitpsynyapnmdkh 258
Cdd:cd16026    153 EEVIEQPADQSSLTQRYTDEAVDFIERNK----DQPFFLYLAHTMPHVPLFASEKFK----GRSGA-------------- 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  259 wimqytGPmlpihmeFTNVLQrkrlqtlmSVDDSVERLYNMLVESGELDNTYIIYTADHG--YHIGQFG-----LVKGKS 331
Cdd:cd16026    211 ------GL-------YGDVVE--------ELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsagpLRGGKG 269
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068830  332 MPYDFDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDV--DGKSVLKLL 389
Cdd:cd16026    270 TTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDRviDGKDISPLL 330
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
72-390 7.66e-34

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: 133.09  E-value: 7.66e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   72 QGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenCSSPSWQamhePrTFAVYLNNTGYRTAFFGKYlneyngsy 151
Cdd:cd16032     34 ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA--AEFPADI----P-TFAHYLRAAGYRTALSGKM-------- 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  152 ippgwrewlgliknsRFYnytvcrnGIKEKHGFDY-------AKDYFTDLitnesinyfkmsKRMYPHRPIMMVISHAAP 224
Cdd:cd16032     99 ---------------HFV-------GPDQLHGFDYdeevafkAVQKLYDL------------ARGEDGRPFFLTVSFTHP 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  225 HGPEDSAPQFSKLYPNASQHitpSYnYApnmdkhwIMQYtgpmlpihmeftnvlqrkrlqtlmsVDDSVERLYNMLVESG 304
Cdd:cd16032    145 HDPYVIPQEYWDLYVRRARR---AY-YG-------MVSY-------------------------VDDKVGQLLDTLERTG 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  305 ELDNTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDV---D 381
Cdd:cd16032    189 LADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVpplD 267

                   ....*....
gi 1907068830  382 GKSVLKLLD 390
Cdd:cd16032    268 GRSLLPLLE 276
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-387 8.38e-34

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 131.52  E-value: 8.38e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTD----DQdvelgsLQVMNKTRKIM------EQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVytnnenc 112
Cdd:cd16148      1 MNVILIVIDslraDH------LGCYGYDRVTTpnldrlAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGV------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  113 sspsWQAMHEPR--TFAVYLNNTGYRTAFFGkylneyNGSYIPPGWREWLGliknsrfYNYTVCRNGIKEKHGFDyaKDY 190
Cdd:cd16148     68 ----WGGPLEPDdpTLAEILRKAGYYTAAVS------SNPHLFGGPGFDRG-------FDTFEDFRGQEGDPGEE--GDE 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  191 FTDLITNESINYFKmskRMYPHRPIMMVISHAAPHGPEdsapqfskLYPNAsqhitpsynyapnmdkhwimqytgpmlpI 270
Cdd:cd16148    129 RAERVTDRALEWLD---RNADDDPFFLFLHYFDPHEPY--------LYDAE----------------------------V 169
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  271 HMeftnvlqrkrlqtlmsVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMP-YDFDIRVPFFIRGPSI 349
Cdd:cd16148    170 RY----------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGK 233
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1907068830  350 EPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLK 387
Cdd:cd16148    234 EPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
74-411 1.02e-33

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: 135.85  E-value: 1.02e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   74 GATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNnencSSPswQAMHEPrTFAVYLNNTGYRTAFFGK----------- 142
Cdd:cd16028     36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN----GTP--LDARHL-TLALELRKAGYDPALFGYtdtspdprgla 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  143 YLNEYNGSY--IPPGWREwlgliknsrfynytVCR-NGIKEKHGfDYAkdYFTDlitnESINYFkmskRMYPHRPIMMVI 219
Cdd:cd16028    109 PLDPRLLSYelAMPGFDP--------------VDRlDEYPAEDS-DTA--FLTD----RAIEYL----DERQDEPWFLHL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  220 SHAAPHGP-EDSAPqFSKLYPNASqhiTPSYNYAPNMD---------KHWIMQYtgPMLPIHMEFTNV-----LQRKRLQ 284
Cdd:cd16028    164 SYIRPHPPfVAPAP-YHALYDPAD---VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMR 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  285 T----LMS-VDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSIE----PGSIV 355
Cdd:cd16028    238 AtylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREadatRGQVV 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068830  356 PQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNrfrtNKKAKIWRDTF 411
Cdd:cd16028    317 DAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQPSD----WRDAVHYEYDF 368
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
43-423 1.28e-33

uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293762 [Multi-domain]  Cd Length: 395  Bit Score: 134.25  E-value: 1.28e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDqdVELGSLQVMNKTRKI-------MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSP 115
Cdd:cd16143      1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  116 SWqaMHEPR-TFAVYLNNTGYRTAFFGKY---LNEY--NGSYIPPGWRE---WLGLIKNSRFYnytvcrngikekHGFDY 186
Cdd:cd16143     79 PL--IEPDRvTLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKdvdYSKPIKGGPLD------------HGFDY 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  187 akdYFT-------DLITNESINYFKMSKRmyPHRPIMMVISHAAPHGPedsapqfsklypnasqhITPS--YNYAPNMDK 257
Cdd:cd16143    145 ---YFGipasevlPTLTDKAVEFIDQHAK--KDKPFFLYFALPAPHTP-----------------IVPSpeFQGKSGAGP 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  258 H--WIMQytgpmlpihmeftnvlqrkrlqtlmsVDDSVERLYNMLVESGELDNTYIIYTADHG---YHIGQFGLVKGKSM 332
Cdd:cd16143    203 YgdFVYE--------------------------LDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGHDP 256
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  333 PYDF-----DI-----RVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLLdlekpgnrfr 399
Cdd:cd16143    257 SGPLrgmkaDIyegghRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPAL---------- 326
                          410       420
                   ....*....|....*....|....*..
gi 1907068830  400 TNKKAKIWRDTFLVE--RGKF-LRKKE 423
Cdd:cd16143    327 LGPKKQEVRESLVHHsgNGSFaIRKGD 353
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-386 5.94e-31

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 122.73  E-value: 5.94e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQDV----ELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNV-----YTNNENCS 113
Cdd:cd16149      1 PNILFILTDDQGPwalgCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  114 SP-SWQAMHEprTFAVYLNNTGYRTAFFGKylneyngsyippgwreW-LGliknsrfynytvcrngikekhgfDYAKDYF 191
Cdd:cd16149     81 KPeGYLEGQT--TLPEVLQDAGYRCGLSGK----------------WhLG-----------------------DDAADFL 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  192 TDLITNEsinyfkmskrmyphRPIMMVISHAAPHGPedsapqfsklypnasqhitpsynyapnmdkhWimQYtgpmlpih 271
Cdd:cd16149    120 RRRAEAE--------------KPFFLSVNYTAPHSP-------------------------------W--GY-------- 144
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  272 meftnvlqrkrLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGlVKGK-------SMpYDFDIRVPFFI 344
Cdd:cd16149    145 -----------FAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNSVKVPFII 211
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1907068830  345 RGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVD--GKSVL 386
Cdd:cd16149    212 RWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFA 256
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-378 9.42e-31

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 123.86  E-value: 9.42e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQ----DVELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYtnnENCSSPS-W 117
Cdd:cd16035      1 PNILLILTDQEryppPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMqP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  118 QAMHEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYippgwrewlgliknsrfynytvcrngikekhgfdYAKDyftDLIT 196
Cdd:cd16035     78 LLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAAGGG----------------------------------YKRD---PGIA 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  197 NESINY-FKMSKRMYPHRPIMMVISHAAPHgpeDsapqfsklypnasqhItpsyNYAPNMDKHWImqytgpmlpihmeft 275
Cdd:cd16035    121 AQAVEWlRERGAKNADGKPWFLVVSLVNPH---D---------------I----MFPPDDEERWR--------------- 163
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  276 nVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSIEP-GSI 354
Cdd:cd16035    164 -RFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFGtGQT 242
                          330       340
                   ....*....|....*....|....
gi 1907068830  355 VPQIVLNIDLAPTILDIAGLDSPS 378
Cdd:cd16035    243 TDALTSHIDLLPTLLGLAGVDAEA 266
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
42-388 1.24e-30

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: 125.63  E-value: 1.24e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDqdveLG-----------------SLQvmnktrkimeQGGATFTNaFVTTPMCCPSRSSMLTGKYVHNHN 104
Cdd:cd16025      2 RPNILLILADD----LGfsdlgcfggeiptpnldALA----------AEGLRFTN-FHTTALCSPTRAALLTGRNHHQVG 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  105 VYTNNENCSS-PSWQAMHEPR--TFAVYLNNTGYRTAFFGKYlneYNGsyiPPGWrewlgliknsrfynytvcrngikek 181
Cdd:cd16025     67 MGTMAELATGkPGYEGYLPDSaaTIAEVLKDAGYHTYMSGKW---HLG---PDDY------------------------- 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  182 hgfdyakdYFTDLITNESINYFKMSKRmyPHRPIMMVISHAAPHGPedsapqfsklypnasQHitpsynyAPnmdKHWIM 261
Cdd:cd16025    116 --------YSTDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAP---------------LQ-------AP---KEWID 160
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  262 QYTG---------------------------PMLPIHMEFT--NVL---QRKRLQTLMSV--------DDSVERLYNMLV 301
Cdd:cd16025    161 KYKGkydagwdalreerlerqkelglipadtKLTPRPPGVPawDSLspeEKKLEARRMEVyaamvehmDQQIGRLIDYLK 240
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  302 ESGELDNTYIIYTADHG--YHIG--QFG---LVKGKSMPYDFDIRVPFFIRGPS--IEPGSIVPQIVLNIDLAPTILDIA 372
Cdd:cd16025    241 ELGELDNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKgiKAKGGIRHQFAHVIDIAPTILELA 320
                          410
                   ....*....|....*.
gi 1907068830  373 GLDSPSDVDGKSVLKL 388
Cdd:cd16025    321 GVEYPKTVNGVPQLPL 336
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
43-418 7.97e-30

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: 124.42  E-value: 7.97e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQD---VELGSLQVMnKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSw 117
Cdd:cd16156      1 KQFIFIMTDTQRwdmVGCYGNKAM-KTPNLdrLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNV- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  118 qamhepRTFAVYLNNTGYRTAFFGKY-LN--EYNGSYI-PPGWRE--WLGL-----------IKNSRFYNYTVCRNGIKE 180
Cdd:cd16156     79 ------KTIGQRLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDPdyWYDMrnyldelteeeRRKSRRGLTSLEAEGIKE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  181 KhgFDYAKDyftdlITNESINYFkmskRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYN----YAPNMD 256
Cdd:cd16156    153 E--FTYGHR-----CTNRALDFI----EKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAYddleNKPLHQ 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  257 KHWIMQYTGP----MLPIHMEFtnvlqrkrLQTLMSVDDSVERLYNMLVEsgELDNTYIIYTADHGYHIGQFGL-VKGKS 331
Cdd:cd16156    222 RLWAGAKPHEdgdkGTIKHPLY--------FGCNSFVDYEIGRVLDAADE--IAEDAWVIYTSDHGDMLGAHKLwAKGPA 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  332 MpYDFDIRVPFFIRGPSIEPGSIVPQI-VLNIDLAPTILDIAGLDSPSDVDGKSVLKLLdlekpgnrfrTNKKAKIwRDT 410
Cdd:cd16156    292 V-YDEITNIPLIIRGKGGEKAGTVTDTpVSHIDLAPTILDYAGIPQPKVLEGESILATI----------EDPEIPE-NRG 359

                   ....*...
gi 1907068830  411 FLVERGKF 418
Cdd:cd16156    360 VFVEFGRY 367
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-389 2.34e-28

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: 118.47  E-value: 2.34e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQDVE-LGSL-QVMNKTRKI--MEQGGATFTNAFvTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPswq 118
Cdd:cd16151      1 PNIILIMADDLGYEcIGCYgGESYKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQK--- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  119 amheprTFAVYLNNTGYRTAFFGK---YLNEYNGSYIPP-GWREWL-------GLIKNSRFYNYTVCRNGIKEKhgfDYA 187
Cdd:cd16151     77 ------TFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHEfGFDEYClwqltetGEKYSRPATPTFNIRNGKLLE---TTE 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  188 KDYFTDLITNESINYFKMSKR-----MYPhrpimMVIshaaPHGPEDSAPQFSKLYPnasqhitPSYNYAPNMDKHWIM- 261
Cdd:cd16151    148 GDYGPDLFADFLIDFIERNKDqpffaYYP-----MVL----VHDPFVPTPDSPDWDP-------DDKRKKDDPEYFPDMv 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  262 QYTgpmlpihmeftnvlqrkrlqtlmsvDDSVERLYNMLVESGELDNTYIIYTADHGYHIG-----QFGLVKG-KSMPYD 335
Cdd:cd16151    212 AYM-------------------------DKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTD 266
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907068830  336 FDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLL 389
Cdd:cd16151    267 AGTHVPLIVNWPGlIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQL 323
PRK13759 PRK13759
arylsulfatase; Provisional
42-397 3.36e-28

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 119.77  E-value: 3.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQDVE-LGSL---QVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSspsW 117
Cdd:PRK13759     6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  118 QAMHE-PRTFAvylnNTGYRTAFFGKYlneyngSYIPPgwREWLGLiKNSRFYNYTVCRNGIKEKHGFDYAKDY------ 190
Cdd:PRK13759    83 NYKNTlPQEFR----DAGYYTQCIGKM------HVFPQ--RNLLGF-HNVLLHDGYLHSGRNEDKSQFDFVSDYlawlre 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  191 --------FTDL-----------------------ITNESINYFKmskRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYP 239
Cdd:PRK13759   150 kapgkdpdLTDIgwdcnswvarpwdleerlhptnwVGSESIEFLR---RRDPTKPFFLKMSFARPHSPYDPPKRYFDMYK 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  240 NASQHITPSYNYAPNMDKH-WIMQYTGPMLPIHMEftnVLQRKRLQTLMS---VDDSVERLYNMLVESGELDNTYIIYTA 315
Cdd:PRK13759   227 DADIPDPHIGDWEYAEDQDpEGGSIDALRGNLGEE---YARRARAAYYGLithIDHQIGRFLQALKEFGLLDNTIILFVS 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  316 DHGYHIGQFGLVKgKSMPYDFDIRVPFFIRGPS----IEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDL 391
Cdd:PRK13759   304 DHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFG 382

                   ....*.
gi 1907068830  392 EKPGNR 397
Cdd:PRK13759   383 QYEGWR 388
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
43-385 1.89e-27

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: 116.11  E-value: 1.89e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQ---DVEL-GSLQVmnKTRKIME--QGGATFTNAFVTtPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd16029      1 PHIVFILADDLgwnDVGFhGSDQI--KTPNLDAlaADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEPY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  117 WQAMHEPrTFAVYLNNTGYRTAFFGKY-LNEYNGSYIPPGwR-------EWLGLI-----KNSRFYNYTVCRNGIKEKHG 183
Cdd:cd16029     78 GLPLNET-LLPQYLKELGYATHLVGKWhLGFYTWEYTPTN-RgfdsfygYYGGAEdyythTSGGANDYGNDDLRDNEEPA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  184 FDYAKDYFTDLITNESINYFKMSKrmyPHRPIMMVISHAAPHGPEDSAPQFSKLYPNASQHITPsynyapnmdkhwimqy 263
Cdd:cd16029    156 WDYNGTYSTDLFTDRAVDIIENHD---PSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKD---------------- 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  264 tgpmlpihmeftnvLQRKRLQTLMS-VDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFG------LVKGKSMPYDF 336
Cdd:cd16029    217 --------------EDRRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggsnypLRGGKNTLWEG 282
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907068830  337 DIRVPFFIRGPSIEP--GSIVPQIVLNIDLAPTILDIAGLDSPS--DVDGKSV 385
Cdd:cd16029    283 GVRVPAFVWSPLLPPkrGTVSDGLMHVTDWLPTLLSLAGGDPDDlpPLDGVDQ 335
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
42-387 3.18e-23

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 100.91  E-value: 3.18e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQDVElgSLQVMNKTRKIMEQG----------------GATFTNAFVTTPMCCPSRSSMLTGKYVHNHNV 105
Cdd:cd16153      1 KPNILWIITDDQRVD--SLSCYNNAHTGKSESrlgyvespnidalaaeGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  106 YtNNENcsspSWQAMHE-PRTFAVYLNNTGYRTAFFGKylneyngsyipPGWREWLGLIKNSrfyNYTVCRNGIKEKHGF 184
Cdd:cd16153     79 Y-GFEA----AHPALDHgLPTFPEVLKKAGYQTASFGK-----------SHLEAFQRYLKNA---NQSYKSFWGKIAKGA 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  185 DYAKdyftdlitnesinyfkmskrmyphrPIMMVISHAAPHGPedsapqfsklypnasqhITPSYNYAPNMDKHWIMQYt 264
Cdd:cd16153    140 DSDK-------------------------PFFVRLSFLQPHTP-----------------VLPPKEFRDRFDYYAFCAY- 176
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  265 gpmlpihmeftnvlqrkrlqtlmsVDDSVERLYNMLVESGEL---DNTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVP 341
Cdd:cd16153    177 ------------------------GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVP 231
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907068830  342 FFIRGPSIEP---GSIVPQIVLNIDLAPTILDIAGLD--SPSDVDGKSVLK 387
Cdd:cd16153    232 LIVVSSDKLKapaGKVRHDFVEFVDLAPTLLAAAGVDvdAPDYLDGRDLFE 282
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
74-390 7.61e-23

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 102.70  E-value: 7.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   74 GATFTNAFVTTPMCCPSRSSMLTGKY--VHNHNVYTNnencsspsWQAMHEPrTFAVYLNNTGYRTAFFGKylneyNGSY 151
Cdd:cd16150     36 GVRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLHH--------LLRPDEP-NLLKTLKDAGYHVAWAGK-----NDDL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  152 IPPGWREwlgliknsrfyNYTVCrngikekhgfDYAkdyftdlITNESINYFKmskRMYPHRPIMMVISHAAPHGP-EDS 230
Cdd:cd16150    102 PGEFAAE-----------AYCDS----------DEA-------CVRTAIDWLR---NRRPDKPFCLYLPLIFPHPPyGVE 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  231 APQFSKLYPNASQHITPSynyapnmdKHWIMQYtgPMLPIHMEFTNvLQR---KRLQTL--------MSVDDSVERLYNM 299
Cdd:cd16150    151 EPWFSMIDREKLPPRRPP--------GLRAKGK--PSMLEGIEKQG-LDRwseERWRELratylgmvSRLDHQFGRLLEA 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  300 LVESGELDNTYIIYTADHGYHIGQFGLV-KGKSMPYDFDIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPS 378
Cdd:cd16150    220 LKETGLYDDTAVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSH 299
                          330
                   ....*....|..
gi 1907068830  379 DVDGKSVLKLLD 390
Cdd:cd16150    300 THFGRSLLPVLA 311
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-389 2.63e-22

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 100.12  E-value: 2.63e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQDVE------LGSLQVMNKTRKIMEQGGATFTNAFVTtPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd16154      1 PNILLIIADDQGLDssaqysLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  117 wqamHE-PRTFAVYLNNTGYRTAFFGKYL--NEYNGSYIPPGWREWLGLIKN--SRFYNYTVCRNGIKEKHGfDYAKDYF 191
Cdd:cd16154     80 ----ETlLQLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNST-EYATTKL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  192 TDL----ITNEsinyfkmskrmypHRPIMMVISHAAPHGPedsapqFsklypnasqHITPSYNYAPNMdkhwimqyTGPM 267
Cdd:cd16154    155 TNLaidwIDQQ-------------TKPWFLWLAYNAPHTP------F---------HLPPAELHSRSL--------LGDS 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  268 LPIHMEftnvlqrKR---LQTLMSVDDSVERLYNMLVESgELDNTYIIYTADHGYHiGQ-----FGLVKGKSMPYDFDIR 339
Cdd:cd16154    199 ADIEAN-------PRpyyLAAIEAMDTEIGRLLASIDEE-ERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGGIN 269
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907068830  340 VPFFIRGPSIEPGSIVPQIVLNI-DLAPTILDIAGLDSPSDVDGKSVLKLL 389
Cdd:cd16154    270 VPLIVSGAGVERANERESALVNAtDLYATIAELAGVDAAEIHDSVSFKPLL 320
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
42-389 1.63e-21

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: 99.04  E-value: 1.63e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDqdVELGSLQVM-NKTRKI-----MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYtnNENCSSP 115
Cdd:cd16160      1 KPNIVLFFADD--MGYGDLASYgHPTQERgpiddMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--GGTRVFL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  116 SWQAMHEPR---TFAVYLNNTGYRTAFFGKY---LNEYN---GSYIPpgwrewlgliknsrfynytvcrngikEKHGFDY 186
Cdd:cd16160     77 PWDIGGLPKtevTMAEALKEAGYTTGMVGKWhlgINENNhsdGAHLP--------------------------SHHGFDF 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  187 A---------------------KD------YFTDLITNESINYFKMSKRMYP----------HRPIMMVISHAAPHGPED 229
Cdd:cd16160    131 VgtnlpftnswacddtgrhvdfPDrsacflYYNDTIVEQPIQHEHLTETLVGdaksfiednqENPFFLYFSFPQTHTPLF 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  230 SAPQFSklypNASQHitpsYNYAPNMDKhwimqytgpmlpihmeftnvlqrkrlqtlMSVddSVERLYNMLVESGELDNT 309
Cdd:cd16160    211 ASKRFK----GKSKR----GRYGDNINE-----------------------------MSW--AVGEVLDTLVDTGLDQNT 251
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  310 YIIYTADHGYHI------GQFGLVKG-KSMPYDFDIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--V 380
Cdd:cd16160    252 LVFFLSDHGPHVeyclegGSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDriY 331

                   ....*....
gi 1907068830  381 DGKSVLKLL 389
Cdd:cd16160    332 DGLSITDLL 340
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
42-422 2.87e-19

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 93.18  E-value: 2.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLtddqdVElgSLQ--VMNKT----------RKIMEQGgATFTNAFVTTPMCCPSRSSMLTGKY-VHNHNVYTN 108
Cdd:COG1368    234 KPNVVVIL-----LE--SFSdfFIGALgngkdvtpflDSLAKES-LYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKR 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  109 NencsspswqAMHEPRTFAVYLNNTGYRTAFFgkylneYNGsyippgwrewlglikNSRFYNytvcRNGIKEKHGFD--Y 186
Cdd:COG1368    306 P---------GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGFDefY 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  187 AKDYFTDLITN-----------ESINYFKMSKRmyphrPIMMVISHAAPHGPedsapqfsklypnasqhitpsynYAPNM 255
Cdd:COG1368    352 DREDFDDPFDGgwgvsdedlfdKALEELEKLKK-----PFFAFLITLSNHGP-----------------------YTLPE 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  256 DKHWIMQYTGPMLpihmeftnvlqRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGyhigqfGLVKGKSmPYD 335
Cdd:COG1368    404 EDKKIPDYGKTTL-----------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYE 465
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  336 FDI---RVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVD-GKSvlkLLDLEKPGNRFR-----TNKKAKI 406
Cdd:COG1368    466 NPLeryRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAfGRD---LLSPDTDPFAFRnggfiTDDYVYV 542
                          410
                   ....*....|....*.
gi 1907068830  407 WRDTFLVERGKFLRKK 422
Cdd:COG1368    543 LKTGELTEEDKELEEE 558
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
43-373 8.24e-19

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: 88.12  E-value: 8.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVL-----TDDQDVELGSLQVMNKTRKIMEQGgATFTNAFVTTPMCCPSRS--SMLTGkyvhnhnVYTNNENCSSP 115
Cdd:cd16015      1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKEG-LYFGNFYSPGFGGGTANGefEVLTG-------LPPLPLGSGSY 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  116 SWQAMHEPRTFAVYLNNTGYRTAFFgkylneYNGsyippgwrewlglikNSRFYNytvcRNGIKEKHGFD--YAKDYFTD 193
Cdd:cd16015     73 TLYKLNPLPSLPSILKEQGYETIFI------HGG---------------DASFYN----RDSVYPNLGFDefYDLEDFPD 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  194 LITNESINY------FKMSKRMY---PHRPIMMVISHAAPHGPedsapqfsklypnasqhitpsYNYAPNMDKhwimqyt 264
Cdd:cd16015    128 DEKETNGWGvsdeslFDQALEELeelKKKPFFIFLVTMSNHGP---------------------YDLPEEKKD------- 179
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  265 gpmLPIHMEFTNVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFdiRVPFFI 344
Cdd:cd16015    180 ---EPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLI 254
                          330       340
                   ....*....|....*....|....*....
gi 1907068830  345 RGPSIEPGSIVPQIVLNIDLAPTILDIAG 373
Cdd:cd16015    255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
43-389 1.33e-18

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: 89.14  E-value: 1.33e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQDVELgSLQVMNKTRKI-----MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYtNNENCSSPSW 117
Cdd:cd16171      1 PNVVMVMSDSFDGRL-TFRPGNQVVDLpyinfMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW-NNYKGLDPNY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  118 QamheprTFAVYLNNTGYRTAFFGKyLNEYNGSYIPPGWRE-WlgliknSRFYNYTVCRNGIKEkhgfdyakdyfTDLIT 196
Cdd:cd16171     79 P------TWMDRLEKHGYHTQKYGK-LDYTSGHHSVSNRVEaW------TRDVPFLLRQEGRPT-----------VNLVG 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  197 NESinyfkmskrmypHRPIMMvishaaphgpedsapqfsKLYPNASQHITPSYNYAPNMDKHWIMqYTGPMLPiHMEFTN 276
Cdd:cd16171    135 DRS------------TVRVML------------------KDWQNTDKAVHWIRKEAPNLTQPFAL-YLGLNLP-HPYPSP 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  277 VLQrkrlQTLMSVDDSVERLYNMLVE--------------SGELDNTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPF 342
Cdd:cd16171    183 SMG----ENFGSIRNIRAFYYAMCAEtdamlgeiisalkdTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPL 257
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1907068830  343 FIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLL 389
Cdd:cd16171    258 LIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLL 304
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
42-389 1.01e-17

galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.


Pssm-ID: 293776 [Multi-domain]  Cd Length: 466  Bit Score: 87.52  E-value: 1.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQDV-ELGSLQVMNK-TRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNN---ENCSS 114
Cdd:cd16157      1 KPNIILMLMDDMGWgDLGVFGEPSReTPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNahaRNAYT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  115 PSWQAMHEPRT---FAVYLNNTGYRTAFFGKYLNEYNGSYIP--PGWREWLG-------LIKNSRFYNYTVCRNgikEKH 182
Cdd:cd16157     81 PQNIVGGIPDSeilLPELLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWFGapnchfgPYDNKAYPNIPVYRD---WEM 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  183 GFDYAKDYFTDLITNESiNYfkmsKRMYPHRPIMMVISHAAPHgpedsAPQFSKLYPNASQhiTPSYNYAPnmdkhwimq 262
Cdd:cd16157    158 IGRYYEEFKIDKKTGES-NL----TQIYLQEALEFIEKQHDAQ-----KPFFLYWAPDATH--APVYASKP--------- 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  263 ytgpmlpihmeFTNVLQRKRL-QTLMSVDDSVERLYNMLVESGELDNTYIIYTADHG---YHIGQFG-----LVKGKSMP 333
Cdd:cd16157    217 -----------FLGTSQRGLYgDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgsngpFLCGKQTT 285
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907068830  334 YDFDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLL 389
Cdd:cd16157    286 FEGGMREPAIAWWPGhIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDraIDGIDLLPVL 344
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
43-397 2.99e-17

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: 85.96  E-value: 2.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQDV-ELG-----SLQVMNKTRkiMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSpS 116
Cdd:cd16158      2 PNIVLLFADDLGYgDLGcyghpSSSTPNLDR--LAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGS-R 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  117 WQAMHEPRTFAVYLNNTGYRTAFFGKY---LNEyNGSYIPP--GWREWLGL---------IKNSRFYNYTVCRNGIKEkh 182
Cdd:cd16158     79 GGLPLNETTIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPThqGFDHYLGIpyshdqgpcQNLTCFPPNIPCFGGCDQ-- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  183 GFDYAKDYFTDLITNESINYFKMSKRM--YPHRpimmVISHAAphgpEDSAPQFskLYpNASQHItpsynYAPnmdkhwi 260
Cdd:cd16158    156 GEVPCPLFYNESIVQQPVDLLTLEERYakFAKD----FIADNA----KEGKPFF--LY-YASHHT-----HYP------- 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  261 mQYTGpmlpihMEFTNVLQRKRL-QTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHI------GQFGLVK-GKSM 332
Cdd:cd16158    213 -QFAG------QKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGT 285
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907068830  333 PYDFDIRVPFFIRGPS-IEPGsIVPQIVLNIDLAPTILDIAGLDSPS-DVDGKSVLKLLDLEKPGNR 397
Cdd:cd16158    286 TYEGGVREPAIAYWPGrIKPG-VTHELASTLDILPTIAKLAGAPLPNvTLDGVDMSPILFEQGKSPR 351
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
43-379 4.05e-17

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: 84.51  E-value: 4.05e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQDV-ELGS----LQVMNKTRKI--MEQGGATFTNAFVTtPMCCPSRSSMLTGKYVhnhnvytNNENCSSP 115
Cdd:cd16142      1 PNILVILGDDIGWgDLGCygggIGRGAPTPNIdrLAKEGLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTGLTTV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  116 SWQ-AMH----EPRTFAVYLNNTGYRTAFFGK-YLNEYNGSYipP---GWREWLGliknsrFYNYTVcrngikEKHGFDY 186
Cdd:cd16142     73 GLPgSPGglppWEPTLAELLKDAGYATAQFGKwHLGDEDGRL--PtdhGFDEFYG------NLYHTI------DEEIVDK 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  187 AKDYFTDLITNE-----SINYFKMSKRMYPHrpimmvishaaphgpEDSAPQFSKLYPNASqhitpsynyapnmdkhwim 261
Cdd:cd16142    139 AIDFIKRNAKADkpfflYVNFTKMHFPTLPS---------------PEFEGKSSGKGKYAD------------------- 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  262 qytgpmlpihmeftnvlqrkrlqTLMSVDDSVERLYNMLVESGELDNTYIIYTADHG-----YHIGQFGLVKG-KSMPYD 335
Cdd:cd16142    185 -----------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKGTTWE 241
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1907068830  336 FDIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD 379
Cdd:cd16142    242 GGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPKD 286
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
42-389 9.25e-17

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: 84.65  E-value: 9.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDDQDV-ELGSLQvmNKTRK-----IMEQGGATFTNAFVTTPMCCPSRSSMLTGKY------VHNHNVYTNN 109
Cdd:cd16159      1 KPNIVLFMADDLGIgDVGCFG--NDTIRtpnidRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmASSHGMRVIL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  110 ENCSS---PSWQAmheprTFAVYLNNTGYRTAFFGKY----------------LN-----------------------EY 147
Cdd:cd16159     79 FTASSgglPPNET-----TFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNhgfdyfyglpltnlkdcgdgsngEY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  148 NGSYIPP------------------------GWRE--------------WLGLIKNSRFYNYTVCRNG-IKEKhgfDYAK 188
Cdd:cd16159    154 DLSFDPLfplltafvlitaltiflllylgavSKRFfvfllilsllfislFFLLLITNRYFNCILMRNHeVVEQ---PMSL 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  189 DYFTDLITNESINYFKMSKRmyphRPIMMVISHAAPHGPEDSAPQFSklypNASQHitpsYNYAPNmdkhwimqytgpml 268
Cdd:cd16159    231 ENLTQRLTKEAISFLERNKE----RPFLLVMSFLHVHTALFTSKKFK----GRSKH----GRYGDN-------------- 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  269 pihmeftnvlqrkrlqtLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHI-----------GQFGLVKGKSMP-YDF 336
Cdd:cd16159    285 -----------------VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIYGGKKMGgWEG 347
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068830  337 DIRVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLL 389
Cdd:cd16159    348 GIRVPTIVRWPGvIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLL 403
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
767-808 2.68e-15

glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).


Pssm-ID: 293766 [Multi-domain]  Cd Length: 396  Bit Score: 79.13  E-value: 2.68e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907068830  767 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQ 808
Cdd:cd16147    347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQ 388
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
43-372 2.79e-14

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: 73.61  E-value: 2.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   43 PNIILVLTDDQDVELGSLQVMNKTR----KIMEQGGATFtNAFVTTPMC--CPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd00016      1 KHVVLIVLDGLGADDLGKAGNPAPTtpnlKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  117 WQAMHEP---RTFAVYLNNTGYRTAFFG--KYLNEyngsyippgwrewlgliknsrfynytvcrnGIKEKHGFDYakdyf 191
Cdd:cd00016     80 SRAAGKDedgPTIPELLKQAGYRTGVIGllKAIDE------------------------------TSKEKPFVLF----- 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  192 tdlitnesINYfkmskrmyphrpimmvishAAPHGPedsapqfsklypnasqhitpSYNYAPNMDkhwimqytgpmlpih 271
Cdd:cd00016    125 --------LHF-------------------DGPDGP--------------------GHAYGPNTP--------------- 142
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  272 mEFTNVLQRkrlqtlmsVDDSVERLYNMLVESGELDNTYIIYTADHG---YHIGQFGLVKGKSMPYDFDIRVPFFIRGPS 348
Cdd:cd00016    143 -EYYDAVEE--------IDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPG 213
                          330       340
                   ....*....|....*....|....
gi 1907068830  349 IEPGSIVPQIVLNIDLAPTILDIA 372
Cdd:cd00016    214 VKKGGVKHELISQYDIAPTLADLL 237
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
42-389 2.18e-13

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: 73.27  E-value: 2.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   42 RPNIILVLTDD---QDVELGSLQVMNKTRKI--MEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVyTNNENCSSPS 116
Cdd:cd16161      1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTSVG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  117 WQAMHEPrTFAVYLNNTGYRTAFFGKYLNEYNGSYIPpgwrewlglikNSRFYNYTVcrnGIKEKHGFDYAKDYF---TD 193
Cdd:cd16161     80 GLPLNET-TLAEVLRQAGYATGMIGKWHLGQREAYLP-----------NSRGFDYYF---GIPFSHDSSLADRYAqfaTD 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  194 LITNESINyfkmskrmypHRPIMMVISHAAPHGPEDSAPQFsklyPNASQHITPsynyapnmdkhwimqyTGpmlpihme 273
Cdd:cd16161    145 FIQRASAK----------DRPFFLYAALAHVHVPLANLPRF----QSPTSGRGP----------------YG-------- 186
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  274 ftnvlqrkrlQTLMSVDDSVERLYNMLVESGELDNTYIIYTAD---------------HGYHIGQFGLVKGKSMPYDFDI 338
Cdd:cd16161    187 ----------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGH 256
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907068830  339 RVPFFIRGPS-IEPGSIVPQIVLNIDLAPTILDIAGLDSPSD--VDGKSVLKLL 389
Cdd:cd16161    257 REPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVL 310
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
67-373 2.91e-08

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 56.05  E-value: 2.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830   67 RKIMEQGGATF--TNAFVT-TpmcCPSRSSMLTGKYVHNHNVYTN-------NENCSSPSWqaMHEPR-----TFAVYLN 131
Cdd:cd16018     26 KRLAEEGVRAKyvKPVFPTlT---FPNHYSIVTGLYPESHGIVGNyfydpktNEEFSDSDW--VWDPWwiggePIWVTAE 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  132 NTGYRTA-FFGKY-LNEYNGSYIPPGWREWLGLIKNSRFynytvcrngikekhGFDYAKDYFtdlitnesINYFKMSkrm 209
Cdd:cd16018    101 KAGLKTAsYFWPGsEVAIIGYNPTPIPLGGYWQPYNDSF--------------PFEERVDTI--------LEWLDLE--- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  210 yphRPIMMVISHAAPhgpeDSApqfsklypnasQHitpsyNYAPNmdkhwimqytgpmlpiHMEFTNVLQRkrlqtlmsV 289
Cdd:cd16018    156 ---RPDLILLYFEEP----DSA-----------GH-----KYGPD----------------SPEVNEALKR--------V 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  290 DDSVERLYNMLVESGELDNTYIIYTADHGY-----HiGQFglvkgksmPYDFDIRVPFFIRGPSIEPGSIVPQIvLNIDL 364
Cdd:cd16018    189 DRRLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GYD--------NELPDMRAIFIARGPAFKKGKKLGPF-RNVDI 258

                   ....*....
gi 1907068830  365 APTILDIAG 373
Cdd:cd16018    259 YPLMCNLLG 267
COG3379 COG3379
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ...
342-390 2.17e-06

Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];


Pssm-ID: 442606 [Multi-domain]  Cd Length: 472  Bit Score: 51.44  E-value: 2.17e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1907068830  342 FFIRGPSIEPGSIVPQIVLnIDLAPTILDIAGLDSPSDVDGKSVLKLLD 390
Cdd:COG3379    422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFA 469
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
229-369 1.34e-05

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: 49.13  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  229 DSAPQFSKLYPNASQhitPSYNYAPNMDKHWIMQYTGPMLPIHMEFTNVLQRKRLQTLMSVDDSVERLYNMLVESGELDN 308
Cdd:COG3083    379 SDRPWFSYLFLDAPH---AYSFPADYPKPFQPSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLEN 455
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068830  309 TYIIYTADHGYhigQFGLVKGKSMPY-----DFDIRVPFFIRGPSIEPGSIvPQIVLNIDLAPTIL 369
Cdd:COG3083    456 TIVIITADHGE---EFNENGQNYWGHnsnfsRYQLQVPLVIHWPGTPPQVI-SKLTSHLDIVPTLM 517
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
272-383 1.05e-03

SPAP is a subclass of alkaline phosphatase (AP); 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. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.


Pssm-ID: 293740 [Multi-domain]  Cd Length: 457  Bit Score: 42.90  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  272 MEFTNVLQ---RKRLQTLMSVDDSVERLYNMLV--ESGEL---------DNTYIIYTADHGyhigqfglvkgksMPYDFD 337
Cdd:cd16016    342 LQMPGVAAaytADELLAGPEPTGIRERLRNGYNpkRSGDLivvlkpgwiEGDGSGKGTTHG-------------SPYDYD 408
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907068830  338 IRVPFFIRGPSIEPGSIV--PQIVlniDLAPTILDIAGLDSPSDVDGK 383
Cdd:cd16016    409 THVPLLFYGWGIKPGEIPrpVEIT---DIAPTLAALLGIQPPNGCIGK 453
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
290-375 5.92e-03

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: 39.91  E-value: 5.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  290 DDSVERLYNMLVESGEldNTYIIYTADHGYHIGQFGlVKGKSMPYDFD--IRVPFFI--------RGPSIEPGSIVPQIV 359
Cdd:cd16017    196 DYVLSQIIERLKKKDK--DAALIYFSDHGESLGENG-LYLHGAPYAPKeqYHVPFIIwssdsykqRYPVERLRANKDRPF 272
                           90
                   ....*....|....*.
gi 1907068830  360 LNIDLAPTILDIAGLD 375
Cdd:cd16017    273 SHDNLFHTLLGLLGIK 288
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
283-368 7.39e-03

GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293744  Cd Length: 294  Bit Score: 39.88  E-value: 7.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068830  283 LQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGyhIGQFGLVKGKSmpyDFDIRVPFF-----IRGPSIEPGSI--- 354
Cdd:cd16020    182 LENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHG--MTDWGSHGDGS---PDETETPFIawgagIKHPTPGRGPSfsa 256
                           90       100
                   ....*....|....*....|.
gi 1907068830  355 ------VPQIVLN-IDLAPTI 368
Cdd:cd16020    257 nwgglrLPRHDLDqADLAPLM 277
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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