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Conserved domains on  [gi|189571638|ref|NP_001121676|]
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extracellular sulfatase Sulf-1 isoform 1 precursor [Homo sapiens]

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: 542.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQDVELGSLQVMNKTRKIMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE--NCSSPSWQA 119
Cdd:cd16147    1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 120 MHEPRTFAVYLNNTGYRTAFFGKYLNEY----NGSYIPPGWREWLGLIKNSRFYNYTVCrNGIKEKHGFDYAKDYFTDLI 195
Cdd:cd16147   81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 196 TNESINYFKMSKRMypHRPVMMVISHAAPHGPEDSAPQFSKLYPNAS-QHITPSYNYAPNMDKHWIMQYTGPMLPiHMEF 274
Cdd:cd16147  160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLNPT-QIAY 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 275 TNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEPGSI 354
Cdd:cd16147  237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
                        330       340       350
                 ....*....|....*....|....*....|
gi 189571638 355 VPQIVLNIDLAPTILDIAGLDTPPDVDGKS 384
Cdd:cd16147  317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
DUF3740 pfam12548
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ...
534-679 1.93e-69

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: 226.07  E-value: 1.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  534 KPRFVHTRQTRSLSVEFEGEIYDINLEEEEelQVLQPRNIAKRH--DEGHKGPRDLQASSGGnrgrMLADSSNAVGPPTT 611
Cdd:pfam12548   1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEEY--QPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPAS 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189571638  612 VRVTHKCFILPNDSIHCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPEECSCSK 679
Cdd:pfam12548  75 VKVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
ALP_like super family cl23718
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
768-817 1.01e-18

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: 89.15  E-value: 1.01e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 189571638 768 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTV 817
Cdd:cd16147  347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
 
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: 542.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQDVELGSLQVMNKTRKIMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE--NCSSPSWQA 119
Cdd:cd16147    1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 120 MHEPRTFAVYLNNTGYRTAFFGKYLNEY----NGSYIPPGWREWLGLIKNSRFYNYTVCrNGIKEKHGFDYAKDYFTDLI 195
Cdd:cd16147   81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 196 TNESINYFKMSKRMypHRPVMMVISHAAPHGPEDSAPQFSKLYPNAS-QHITPSYNYAPNMDKHWIMQYTGPMLPiHMEF 274
Cdd:cd16147  160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLNPT-QIAY 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 275 TNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEPGSI 354
Cdd:cd16147  237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
                        330       340       350
                 ....*....|....*....|....*....|
gi 189571638 355 VPQIVLNIDLAPTILDIAGLDTPPDVDGKS 384
Cdd:cd16147  317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
42-414 9.64e-73

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 244.02  E-value: 9.64e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQDVelGSLQVMNKTRKIMEH------GGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcsSP 115
Cdd:COG3119   23 RPNILFILADDLGY--GDLGCYGNPLIKTPNidrlaaEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEG--YN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SWQAMHEPrTFAVYLNNTGYRTAFFGKYLNeyngsyippgwrewlgliknsrfynytvcrngikekhgfdyakdYFTDLI 195
Cdd:COG3119   99 GGLPPDEP-TLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDLL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 196 TNESINYfkMSKRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYPNasQHITPSYNYAPNMDKHWIMQYtgpmlpihmeft 275
Cdd:COG3119  134 TDKAIDF--LERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR------------ 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 276 niLQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SVEPGSI 354
Cdd:COG3119  198 --ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPgKIKAGSV 275
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 355 VPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLdpekpgnrfrTNKKAKiWRDTFLVE 414
Cdd:COG3119  276 SDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLL----------TGEKAE-WRDYLYWE 324
DUF3740 pfam12548
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ...
534-679 1.93e-69

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: 226.07  E-value: 1.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  534 KPRFVHTRQTRSLSVEFEGEIYDINLEEEEelQVLQPRNIAKRH--DEGHKGPRDLQASSGGnrgrMLADSSNAVGPPTT 611
Cdd:pfam12548   1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEEY--QPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPAS 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189571638  612 VRVTHKCFILPNDSIHCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPEECSCSK 679
Cdd:pfam12548  75 VKVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
Sulfatase pfam00884
Sulfatase;
43-374 1.93e-46

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 168.37  E-value: 1.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638   43 PNIILVLTDDQ-DVELGSLQ-VMNKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNEncsspsWQ 118
Cdd:pfam00884   1 PNVVLVLGESLrAPDLGLYGyPRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------VG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  119 AMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGLIKNSRFYNYTVCRNGIKEKHGfdyakdYFTDLIT 196
Cdd:pfam00884  75 LPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYADPPDVPYNCSGGG------VSDEALL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  197 NESINYfkmskRMYPHRPVMMVISHAAPHGPedsaPQFSKLYPNASQHITPSYNYAPNMDkhwimqytgpmlpihmeftn 276
Cdd:pfam00884 149 DEALEF-----LDNNDKPFFLVLHTLGSHGP----PYYPDRYPEKYATFKPSSCSEEQLL-------------------- 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  277 ilqRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFG--LVKGKSM-PYDFDIRVPFFIRGPSVEP-G 352
Cdd:pfam00884 200 ---NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKAkG 276
                         330       340
                  ....*....|....*....|..
gi 189571638  353 SIVPQIVLNIDLAPTILDIAGL 374
Cdd:pfam00884 277 QKSEALVSHVDLFPTILDLAGI 298
PRK13759 PRK13759
arylsulfatase; Provisional
42-397 5.47e-28

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 118.62  E-value: 5.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQDVE-LGSL---QVMNKTRKIMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSspsW 117
Cdd:PRK13759   6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 118 QAMHE-PRTFAvylnNTGYRTAFFGKYlneyngSYIPPgwREWLGLiKNSRFYNYTVCRNGIKEKHGFDYAKDY------ 190
Cdd:PRK13759  83 NYKNTlPQEFR----DAGYYTQCIGKM------HVFPQ--RNLLGF-HNVLLHDGYLHSGRNEDKSQFDFVSDYlawlre 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 191 --------FTDL-----------------------ITNESINYFKmskRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYP 239
Cdd:PRK13759 150 kapgkdpdLTDIgwdcnswvarpwdleerlhptnwVGSESIEFLR---RRDPTKPFFLKMSFARPHSPYDPPKRYFDMYK 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 240 NASQHITPSYNYAPNMDKH-WIMQYTGPMLPIHMEFtniLQRKRLQTLMS---VDDSVERLYNMLVETGELENTYIIYTA 315
Cdd:PRK13759 227 DADIPDPHIGDWEYAEDQDpEGGSIDALRGNLGEEY---ARRARAAYYGLithIDHQIGRFLQALKEFGLLDNTIILFVS 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 316 DHGYHIGQFGLVKgKSMPYDFDIRVPFFIRGPS----VEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDP 391
Cdd:PRK13759 304 DHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFG 382

                 ....*.
gi 189571638 392 EKPGNR 397
Cdd:PRK13759 383 QYEGWR 388
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
768-817 1.01e-18

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: 89.15  E-value: 1.01e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 189571638 768 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTV 817
Cdd:cd16147  347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
 
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: 542.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQDVELGSLQVMNKTRKIMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE--NCSSPSWQA 119
Cdd:cd16147    1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPpgGGYPKFWQN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 120 MHEPRTFAVYLNNTGYRTAFFGKYLNEY----NGSYIPPGWREWLGLIKNSRFYNYTVCrNGIKEKHGFDYAKDYFTDLI 195
Cdd:cd16147   81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 196 TNESINYFKMSKRMypHRPVMMVISHAAPHGPEDSAPQFSKLYPNAS-QHITPSYNYAPNMDKHWIMQYTGPMLPiHMEF 274
Cdd:cd16147  160 ANKALDFLRRAAAD--DKPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLNPT-QIAY 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 275 TNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEPGSI 354
Cdd:cd16147  237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
                        330       340       350
                 ....*....|....*....|....*....|
gi 189571638 355 VPQIVLNIDLAPTILDIAGLDTPPDVDGKS 384
Cdd:cd16147  317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRS 346
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
42-414 1.05e-85

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: 280.18  E-value: 1.05e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQ--DVeLGSLQ-VMNKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcSSPS 116
Cdd:cd16031    2 RPNIIFILTDDHryDA-LGCYGnPIVKTPNIdrLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGP-LFDA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQamhepRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPPGWREWLGLIKNSRFYNYTVCRNGIKEKHgfdyaKDYFTDLIT 196
Cdd:cd16031   80 SQ-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENGKRVGQ-----KGYVTDIIT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 197 NESINYFKmsKRMyPHRPVMMVISHAAPHGPEDSAPQFSKLYPNAsqHITPSYNYAPN-------------MDKHWIMQY 263
Cdd:cd16031  150 DKALDFLK--ERD-KDKPFCLSLSFKAPHRPFTPAPRHRGLYEDV--TIPEPETFDDDdyagrpewareqrNRIRGVLDG 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 264 tgpmlPIHMEFTniLQR--KR-LQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRV 340
Cdd:cd16031  225 -----RFDTPEK--YQRymKDyLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIRV 296
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189571638 341 PFFIRGP-SVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDpekpgnrfrtNKKAKIWRDTFLVE 414
Cdd:cd16031  297 PLIIRDPrLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLE----------GEKPVDWRKEFYYE 361
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
42-414 9.64e-73

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 244.02  E-value: 9.64e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQDVelGSLQVMNKTRKIMEH------GGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcsSP 115
Cdd:COG3119   23 RPNILFILADDLGY--GDLGCYGNPLIKTPNidrlaaEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEG--YN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SWQAMHEPrTFAVYLNNTGYRTAFFGKYLNeyngsyippgwrewlgliknsrfynytvcrngikekhgfdyakdYFTDLI 195
Cdd:COG3119   99 GGLPPDEP-TLAELLKEAGYRTALFGKWHL--------------------------------------------YLTDLL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 196 TNESINYfkMSKRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYPNasQHITPSYNYAPNMDKHWIMQYtgpmlpihmeft 275
Cdd:COG3119  134 TDKAIDF--LERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDG--KDIPLPPNLAPRDLTEEELRR------------ 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 276 niLQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SVEPGSI 354
Cdd:COG3119  198 --ARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPgKIKAGSV 275
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 355 VPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLdpekpgnrfrTNKKAKiWRDTFLVE 414
Cdd:COG3119  276 SDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLL----------TGEKAE-WRDYLYWE 324
DUF3740 pfam12548
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ...
534-679 1.93e-69

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: 226.07  E-value: 1.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  534 KPRFVHTRQTRSLSVEFEGEIYDINLEEEEelQVLQPRNIAKRH--DEGHKGPRDLQASSGGnrgrMLADSSNAVGPPTT 611
Cdd:pfam12548   1 KPRFVRTRQKRSLSVEFEGEVYDIDLEEEY--QPLEPRNLLKRHarDDGEEGEEGEESSGTG----SKRDSSNSVGPPAS 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189571638  612 VRVTHKCFILPNDSIHCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPEECSCSK 679
Cdd:pfam12548  75 VKVTHRCYILANDTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHLKERRPEECDCNK 142
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
43-384 1.88e-51

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: 180.33  E-value: 1.88e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQ---DVE-LGSLQVmnKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENcsspS 116
Cdd:cd16022    1 PNILLIMTDDLgydDLGcYGNPDI--KTPNLdrLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN----G 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQAMHEPRTFAVYLNNTGYRTAFFGKylneyngsyippgwreWlgliknsrfynytvcrngikekHgfdyakdyftdlit 196
Cdd:cd16022   75 GGLPPDEPTLAELLKEAGYRTALIGK----------------W----------------------H-------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 197 NESINYFKmskRMYPHRPVMMVISHAAPHGPedsapqfsklypnasqhitpsYNYAPNMDkhwimqytgpmlpihmeftn 276
Cdd:cd16022  103 DEAIDFIE---RRDKDKPFFLYVSFNAPHPP---------------------FAYYAMVS-------------------- 138
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 277 ilqrkrlqtlmSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGP-SVEPGSIV 355
Cdd:cd16022  139 -----------AIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPgKIPAGQVS 207
                        330       340
                 ....*....|....*....|....*....
gi 189571638 356 PQIVLNIDLAPTILDIAGLDTPPDVDGKS 384
Cdd:cd16022  208 DALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
42-400 2.83e-51

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: 185.08  E-value: 2.83e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDD---QDveLGSLQVMN-KTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTnneNCSSP 115
Cdd:cd16034    1 KPNILFIFADQhraQA--LGCAGDDPvKTPNLdrLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFG---NDVPL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SwqamHEPRTFAVYLNNTGYRTAFFGKY-LNE-------YNGSYIPP----GWREWLGLIKNSRFYNYTVCRNGIKEKHG 183
Cdd:cd16034   76 P----PDAPTIADVLKDAGYRTGYIGKWhLDGperndgrADDYTPPPerrhGFDYWKGYECNHDHNNPHYYDDDGKRIYI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 184 FDYAKDYFTDLItnesINYfkMSKRMYPHRPVMMVISHAAPHGPEDSAPQ-FSKLYPNASQHITPsyNYAPNMD-----K 257
Cdd:cd16034  152 KGYSPDAETDLA----IEY--LENQADKDKPFALVLSWNPPHDPYTTAPEeYLDMYDPKKLLLRP--NVPEDKKeeaglR 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 258 HWIMQYtgpmlpihmeFTNILqrkrlqtlmSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFD 337
Cdd:cd16034  224 EDLRGY----------YAMIT---------ALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM-NKQVPYEES 283
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189571638 338 IRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNRFRT 400
Cdd:cd16034  284 IRVPFIIRYPGKiKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKDDEPDSV 347
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
43-397 1.10e-47

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: 174.23  E-value: 1.10e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQDVELGSlqVMN---KTRKIME--HGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTN-NENCSSPS 116
Cdd:cd16027    1 PNILWIIADDLSPDLGG--YGGnvvKTPNLDRlaAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLrSRGFPLPD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQamhepRTFAVYLNNTGYRTAFFGKYlnEYNGSYIPPGWrewlgliknsrFYNYTVCRNGIKEKHGFDYAKDYFTDLIT 196
Cdd:cd16027   79 GV-----KTLPELLREAGYYTGLIGKT--HYNPDAVFPFD-----------DEMRGPDDGGRNAWDYASNAADFLNRAKK 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 197 NE----SINYFkmskrmYPHRPVMMVISHAAPHGPEDsapqfsklypnasqhITPSYNYA--PNMDKHWIMQYTgpmlpi 270
Cdd:cd16027  141 GQpfflWFGFH------DPHRPYPPGDGEEPGYDPEK---------------VKVPPYLPdtPEVREDLADYYD------ 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 271 hmeftnilqrkrlqTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYhigqfGLVKGKSMPYDFDIRVPFFIRGPS-V 349
Cdd:cd16027  194 --------------EIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkI 254
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 189571638 350 EPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNR 397
Cdd:cd16027  255 KPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGR 302
Sulfatase pfam00884
Sulfatase;
43-374 1.93e-46

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 168.37  E-value: 1.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638   43 PNIILVLTDDQ-DVELGSLQ-VMNKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNEncsspsWQ 118
Cdd:pfam00884   1 PNVVLVLGESLrAPDLGLYGyPRPTTPFLdrLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP------VG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  119 AMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGLIKNSRFYNYTVCRNGIKEKHGfdyakdYFTDLIT 196
Cdd:pfam00884  75 LPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYADPPDVPYNCSGGG------VSDEALL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  197 NESINYfkmskRMYPHRPVMMVISHAAPHGPedsaPQFSKLYPNASQHITPSYNYAPNMDkhwimqytgpmlpihmeftn 276
Cdd:pfam00884 149 DEALEF-----LDNNDKPFFLVLHTLGSHGP----PYYPDRYPEKYATFKPSSCSEEQLL-------------------- 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  277 ilqRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFG--LVKGKSM-PYDFDIRVPFFIRGPSVEP-G 352
Cdd:pfam00884 200 ---NSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGgyLHGGKYDnAPEGGYRVPLLIWSPGGKAkG 276
                         330       340
                  ....*....|....*....|..
gi 189571638  353 SIVPQIVLNIDLAPTILDIAGL 374
Cdd:pfam00884 277 QKSEALVSHVDLFPTILDLAGI 298
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-414 6.84e-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: 170.09  E-value: 6.84e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQDV----ELGSLQVmnKT---RKIMEHGgATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSP 115
Cdd:cd16033    1 PNILFIMTDQQRYdtlgCYGNPIV--KTpniDRLAAEG-VRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SWQAMHEPRTFAVYLNNTGYRTAFFGKylneyngsyippgWRewlgliknsrfynytVCRNGIKEKHGFDY------AKD 189
Cdd:cd16033   78 SRGLPPGVETFSEDLREAGYRNGYVGK-------------WH---------------VGPEETPLDYGFDEylpvetTIE 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 190 YFTDLITNESINYFKMSKRmyphrPVMMVISHAAPHGPEDSAPQFSKLYPNASqhITPSYNYAPNM-DKHWImQYTGPML 268
Cdd:cd16033  130 YFLADRAIEMLEELAADDK-----PFFLRVNFWGPHDPYIPPEPYLDMYDPED--IPLPESFADDFeDKPYI-YRRERKR 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 269 PIHMEFTNILQRKRLQ------TLMsvDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLV-KGKSMpYDFDIRVP 341
Cdd:cd16033  202 WGVDTEDEEDWKEIIAhywgyiTLI--DDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWdKGPFM-YEETYRIP 278
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189571638 342 FFIRGP-SVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNrfrtnkkakiWRDTFLVE 414
Cdd:cd16033  279 LIIKWPgVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQPED----------WRDEVVTE 342
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
43-397 7.26e-46

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: 170.42  E-value: 7.26e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDD---QDVelgSLQvMNKtrkIME--------HGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYT---- 107
Cdd:cd16144    1 PNIVLILVDDlgwADL---GCY-GSK---FYEtpnidrlaKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDvipg 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 108 ------NNENCSSPSWQAM-HEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYipP---GWREWLGLIKNSRFYNYTVCRN 176
Cdd:cd16144   74 rrgppdNTKLIPPPSTTRLpLEEVTIAEALKDAGYATAHFGKWhLGGEGGYG--PedqGFDVNIGGTGNGGPPSYYFPPG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 177 GIKEKHGFDYAKDYFTDLITNESINYFKMSKRmyphRPVMMVISHAAPHGPEDSAPQFSKLYpnasqhitpsYNYAPNMD 256
Cdd:cd16144  152 KPNPDLEDGPEGEYLTDRLTDEAIDFIEQNKD----KPFFLYLSHYAVHTPIQARPELIEKY----------EKKKKGLR 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 257 KHWIMQYTGPMLpihmeftnilqrkrlqtlMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLV-------KG 329
Cdd:cd16144  218 KGQKNPVYAAMI------------------ESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsnaplrGG 279
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189571638 330 KSMPYDFDIRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILDIAGLDTPP--DVDGKSVLKLL-DPEKPGNR 397
Cdd:cd16144  280 KGSLYEGGIRVPLIVRWPGViKPGSVSDVPVIGTDLYPTFLELAGGPLPPpqHLDGVSLVPLLkGGEADLPR 351
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
43-413 8.23e-39

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: 149.62  E-value: 8.23e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQDVelGSLQVMN----KTRKI--MEHGGATFINaFVTTPMCCPSRSSMLTGKYVHNHNVYTnnencSSPS 116
Cdd:cd16146    1 PNVILILTDDQGY--GDLGFHGnpilKTPNLdrLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRTGVWH-----TILG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQAMH-EPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGL-----------IKNSRFYNyTVCRNGIKEKH 182
Cdd:cd16146   73 RERMRlDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFDEVLGHggggigqypdyWGNDYFDD-TYYHNGKFVKT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 183 gfdyaKDYFTDLITNESINYFKMSKrmypHRPVMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNYApnmdkhwimq 262
Cdd:cd16146  152 -----EGYCTDVFFDEAIDFIEENK----DKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDKLAAFYG---------- 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 263 ytgpMLpihmefTNIlqrkrlqtlmsvDDSVERLYNMLVETGELENTYIIYTADHGYHIG-----QFGLVKGKSMPYDFD 337
Cdd:cd16146  213 ----MI------ENI------------DDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGvpkrfNAGMRGKKGSVYEGG 270
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189571638 338 IRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILDIAGLDTPPDV--DGKSVLKLLdpekpgnrfrTNKKAKiWRDTFLV 413
Cdd:cd16146  271 HRVPFFIRWPGKiLAGKDVDTLTAHIDLLPTLLDLCGVKLPEGIklDGRSLLPLL----------KGESDP-WPERTLF 338
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
74-398 9.47e-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: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 146.92  E-value: 9.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  74 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSpswqamhEPRTFAVYLNNTGYRTAFFGK--YLNEyngsy 151
Cdd:cd16037   36 GTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYDG-------DVPSWGHALRAAGYETVLIGKlhFRGE----- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 152 ippgwrewlgliknsrfynytvcrngiKEKHGFDYakdyfTDLITNESINYFKmsKRMYPHRPVMMVISHAAPHGPEDSA 231
Cdd:cd16037  104 ---------------------------DQRHGFRY-----DRDVTEAAVDWLR--EEAADDKPWFLFVGFVAPHFPLIAP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 232 PQFSKLYpnasqhitpsynyapnmdkhwimqytgpmlpihmeftnilqRKRLQT----LMS-VDDSVERLYNMLVETGEL 306
Cdd:cd16037  150 QEFYDLY-----------------------------------------VRRARAayygLVEfLDENIGRVLDALEELGLL 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 307 ENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVL 386
Cdd:cd16037  189 DNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLL 267
                        330
                 ....*....|..
gi 189571638 387 KLLDPEKPGNRF 398
Cdd:cd16037  268 PLAEGPDDPDRV 279
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
42-397 1.35e-37

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


Pssm-ID: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 145.06  E-value: 1.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQ--DVeLGSL-QVMNKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenCSSPS 116
Cdd:cd16152    1 KPNVIVFFTDQQrwDT-LGCYgQPLDLTPNLdaLAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNG--IPLPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 wqamhEPRTFAVYLNNTGYRTAFFGKylneyngsyippgwreWlgliknsrfynytvcrngikekHGFDYAKDYFTDLit 196
Cdd:cd16152   78 -----DEKTLAHYFRDAGYETGYVGK----------------W----------------------HLAGYRVDALTDF-- 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 197 neSINYfkMSKRMyPHRPVMMVISHAAPH---------GPEDSAPQFSKLYP---------NASQHItPSYnyapnmdkh 258
Cdd:cd16152  113 --AIDY--LDNRQ-KDKPFFLFLSYLEPHhqndrdryvAPEGSAERFANFWVppdlaalpgDWAEEL-PDY--------- 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 259 wimqytgpmlpihmeftnilqrkrLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHigqFGLVKG--KSMPYDF 336
Cdd:cd16152  178 ------------------------LGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHES 230
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189571638 337 DIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNR 397
Cdd:cd16152  231 SIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVEDWR 291
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
42-397 1.61e-37

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


Pssm-ID: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 144.63  E-value: 1.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQDVE----LGSLQVmnKTRKI--MEHGGATFINAFVTTPM----CCPSRSSMLTGKYVHNhnvYTNNEN 111
Cdd:cd16155    2 KPNILFILADDQRADtigaLGNPEI--QTPNLdrLARRGTSFTNAYNMGGWsgavCVPSRAMLMTGRTLFH---APEGGK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 112 CSSPSwqamhEPRTFAVYLNNTGYRTAFFGKYLNEYngsyippgwrewlgliknsrfynytvcrngikekhgfdyakdyf 191
Cdd:cd16155   77 AAIPS-----DDKTWPETFKKAGYRTFATGKWHNGF-------------------------------------------- 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 192 tdliTNESINYFKmsKRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYPnaSQHITPSYNYAPnmdKHwimQYTGPMLPIH 271
Cdd:cd16155  108 ----ADAAIEFLE--EYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYP--PETIPLPENFLP---QH---PFDNGEGTVR 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 272 MEFT--------NIlqRKRLQ----TLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIR 339
Cdd:cd16155  174 DEQLapfprtpeAV--RQHLAeyyaMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM-GKQNLYEHSMR 250
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189571638 340 VPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNR 397
Cdd:cd16155  251 VPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVR 308
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
43-389 2.06e-36

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: 142.73  E-value: 2.06e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQDV-ELGSL-QVMNKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWQ 118
Cdd:cd16145    1 PNIIFILADDLGYgDLGCYgQKKIKTPNLdrLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 119 AmhEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYIPP--GWREWLG--------------LIKNSR--FYNYTVCRNGIK 179
Cdd:cd16145   81 P--DDVTLAEVLKKAGYATAAFGKWgLGGPGTPGHPTkqGFDYFYGyldqvhahnyypeyLWRNGEkvPLPNNVIPPLDE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 180 EKHGFDYAKDYFTDLITNESINYFKMSKRmyphRPVMMVISHAAPHGPEDsAPQFSklyPNASQHITPSYNYAPNMDKhw 259
Cdd:cd16145  159 GNNAGGGGGTYSHDLFTDEALDFIRENKD----KPFFLYLAYTLPHAPLQ-VPDDG---PYKYKPKDPGIYAYLPWPQ-- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 260 imqytgpmlpihmeftnilQRKRLQTLMS-VDDSVERLYNMLVETGELENTYIIYTADHGYHI-------GQF-----GL 326
Cdd:cd16145  229 -------------------PEKAYAAMVTrLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggsehdPDFfdsngPL 289
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189571638 327 VKGK-SMpYDFDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLL 389
Cdd:cd16145  290 RGYKrSL-YEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTL 353
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-387 6.05e-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: 6.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTD----DQdvelgsLQVMNKTRKIMEH------GGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVytnnenc 112
Cdd:cd16148    1 MNVILIVIDslraDH------LGCYGYDRVTTPNldrlaaEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGV------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 113 sspsWQAMHEPR--TFAVYLNNTGYRTAFFGkylneyNGSYIPPGWREWLGliknsrfYNYTVCRNGIKEKHGFDyaKDY 190
Cdd:cd16148   68 ----WGGPLEPDdpTLAEILRKAGYYTAAVS------SNPHLFGGPGFDRG-------FDTFEDFRGQEGDPGEE--GDE 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 191 FTDLITNESINYFKmskRMYPHRPVMMVISHAAPHGPEdsapqfskLYPNAsqhitpsynyapnmdkhwimqytgpmlpI 270
Cdd:cd16148  129 RAERVTDRALEWLD---RNADDDPFFLFLHYFDPHEPY--------LYDAE----------------------------V 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 271 HMeftnilqrkrlqtlmsVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMP-YDFDIRVPFFIRGPSV 349
Cdd:cd16148  170 RY----------------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNlYDEQLHVPLIIRWPGK 233
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 189571638 350 EPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLK 387
Cdd:cd16148  234 EPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
42-397 6.05e-34

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: 135.78  E-value: 6.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQDVELGSL--QVMnKT-------RKimehgGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenc 112
Cdd:cd16030    2 KPNVLFIAVDDLRPWLGCYggHPA-KTpnidrlaAR-----GVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNN--- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 113 sSPSWQAMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYI--PPGWREWLGLIKNSRFYNYTVCRNGIKEKHG------- 183
Cdd:cd16030   73 -SYFRKVAPDAVTLPQYFKENGYTTAGVGKIFHPGIPDGDddPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGgggpawe 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 184 -FDYAKDYFTD-LITNESINYFKMSKRMypHRPVMMVISHAAPHGPEdSAPQ-FSKLYPNASQHITPSYN------YAPN 254
Cdd:cd16030  152 aADVPDEAYPDgKVADEAIEQLRKLKDS--DKPFFLAVGFYKPHLPF-VAPKkYFDLYPLESIPLPNPFDpidlpeVAWN 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 255 mDKHWIMQYTGPMLPIHMEFTNIL----QRKRLQT-LMSV---DDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGL 326
Cdd:cd16030  229 -DLDDLPKYGDIPALNPGDPKGPLpdeqARELRQAyYASVsyvDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGH 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189571638 327 VkGKSMPYDFDIRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLL-DPEKPGNR 397
Cdd:cd16030  308 W-GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLkNPSAKWKD 379
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
72-390 9.39e-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: 132.70  E-value: 9.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  72 HGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNenCSSPSWQamhePrTFAVYLNNTGYRTAFFGKYlneyngsy 151
Cdd:cd16032   34 ARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA--AEFPADI----P-TFAHYLRAAGYRTALSGKM-------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 152 ippgwrewlgliknsRFYnytvcrnGIKEKHGFDY-------AKDYFTDLitnesinyfkmsKRMYPHRPVMMVISHAAP 224
Cdd:cd16032   99 ---------------HFV-------GPDQLHGFDYdeevafkAVQKLYDL------------ARGEDGRPFFLTVSFTHP 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 225 HGPEDSAPQFSKLYPNASQHitpSYnYApnmdkhwIMQYtgpmlpihmeftnilqrkrlqtlmsVDDSVERLYNMLVETG 304
Cdd:cd16032  145 HDPYVIPQEYWDLYVRRARR---AY-YG-------MVSY-------------------------VDDKVGQLLDTLERTG 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 305 ELENTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDV---D 381
Cdd:cd16032  189 LADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVpplD 267

                 ....*....
gi 189571638 382 GKSVLKLLD 390
Cdd:cd16032  268 GRSLLPLLE 276
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
74-411 1.08e-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: 135.46  E-value: 1.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  74 GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNnencSSPswQAMHEPrTFAVYLNNTGYRTAFFGK----------- 142
Cdd:cd16028   36 GVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWN----GTP--LDARHL-TLALELRKAGYDPALFGYtdtspdprgla 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 143 YLNEYNGSY--IPPGWREwlgliknsrfynytVCR-NGIKEKHGfDYAkdYFTDlitnESINYFkmskRMYPHRPVMMVI 219
Cdd:cd16028  109 PLDPRLLSYelAMPGFDP--------------VDRlDEYPAEDS-DTA--FLTD----RAIEYL----DERQDEPWFLHL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 220 SHAAPHGP-EDSAPqFSKLYPNASqhiTPSYNYAPNMD---------KHWIMQYtgPMLPIHMEFTNI-----LQRKRLQ 284
Cdd:cd16028  164 SYIRPHPPfVAPAP-YHALYDPAD---VPPPIRAESLAaeaaqhpllAAFLERI--ESLSFSPGAANAadlddEEVAQMR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 285 T----LMS-VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVPFFIRGPSVE----PGSIV 355
Cdd:cd16028  238 AtylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREadatRGQVV 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189571638 356 PQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNrfrtNKKAKIWRDTF 411
Cdd:cd16028  317 DAFTESVDVMPTILDWLGGEIPHQCDGRSLLPLLAGAQPSD----WRDAVHYEYDF 368
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
43-397 2.62e-32

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


Pssm-ID: 293762 [Multi-domain]  Cd Length: 395  Bit Score: 130.01  E-value: 2.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDqdVELGSLQVMNKTRKI-------MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSP 115
Cdd:cd16143    1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SWqaMHEPR-TFAVYLNNTGYRTAFFGKY---LNEY--NGSYIPPGWRE---WLGLIKNSRFYnytvcrngikekHGFDY 186
Cdd:cd16143   79 PL--IEPDRvTLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKdvdYSKPIKGGPLD------------HGFDY 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 187 akdYFT-------DLITNESINYFKMSKRmyPHRPVMMVISHAAPHGPedsapqfsklypnasqhITPS--YNYAPNMDK 257
Cdd:cd16143  145 ---YFGipasevlPTLTDKAVEFIDQHAK--KDKPFFLYFALPAPHTP-----------------IVPSpeFQGKSGAGP 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 258 H--WIMQytgpmlpihmeftnilqrkrlqtlmsVDDSVERLYNMLVETGELENTYIIYTADHG---YHIGQFGLVKGKSM 332
Cdd:cd16143  203 YgdFVYE--------------------------LDWVVGRILDALKELGLAENTLVIFTSDNGpspYADYKELEKFGHDP 256
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189571638 333 PYDF-----DI-----RVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLK-LLDPEKPGNR 397
Cdd:cd16143  257 SGPLrgmkaDIyegghRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPaLLGPKKQEVR 335
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
42-398 1.77e-31

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: 127.68  E-value: 1.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQ---DVE-LGSlqVMNKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKY-----VHNHNVYTNNE 110
Cdd:cd16026    1 KPNIVVILADDLgygDLGcYGS--PLIKTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYpvrvgLPGVVGPPGSK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 111 NCSSPSwqamhEPrTFAVYLNNTGYRTAFFGKYLNEYNGSYIPP--GWREWLGL----------IKNSRFYNYTVCRNGI 178
Cdd:cd16026   79 GGLPPD-----EI-TIAEVLKKAGYRTALVGKWHLGHQPEFLPTrhGFDEYFGIpysndmwpfpLYRNDPPGPLPPLMEN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 179 KEKHGFDYAKDYFTDLITNESINYFKMSKrmypHRPVMMVISHAAPHGPedsapqfskLYPNasqhitpsynyapnmdkh 258
Cdd:cd16026  153 EEVIEQPADQSSLTQRYTDEAVDFIERNK----DQPFFLYLAHTMPHVP---------LFAS------------------ 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 259 wimqytgpmlpihMEFTNILQRKRL-QTLMSVDDSVERLYNMLVETGELENTYIIYTADHG--YHIGQFG-----LVKGK 330
Cdd:cd16026  202 -------------EKFKGRSGAGLYgDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwLEYGGHGgsagpLRGGK 268
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189571638 331 SMPYDFDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPDV--DGKSVLKLL--DPEKPGNRF 398
Cdd:cd16026  269 GTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDRviDGKDISPLLlgGSKSPPHPF 341
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
43-397 1.45e-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: 126.34  E-value: 1.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQD---VELGSLQVMnKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSw 117
Cdd:cd16156    1 KQFIFIMTDTQRwdmVGCYGNKAM-KTPNLdrLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGDNV- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 118 qamhepRTFAVYLNNTGYRTAFFGKY-LN--EYNGSYI-PPGWRE--WLGL-----------IKNSRFYNYTVCRNGIKE 180
Cdd:cd16156   79 ------KTIGQRLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDPdyWYDMrnyldelteeeRRKSRRGLTSLEAEGIKE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 181 KhgFDYAKDyftdlITNESINYFkmskRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNyaPNMDKHWI 260
Cdd:cd16156  153 E--FTYGHR-----CTNRALDFI----EKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAY--DDLENKPL 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 261 MQ--YTGPMLPIHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETgeLENTYIIYTADHGYHIGQFGL-VKGKSMpYDFD 337
Cdd:cd16156  220 HQrlWAGAKPHEDGDKGTIKHPLYFGCNSFVDYEIGRVLDAADEI--AEDAWVIYTSDHGDMLGAHKLwAKGPAV-YDEI 296
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189571638 338 IRVPFFIRGPSVEPGSIVPQI-VLNIDLAPTILDIAGLDTPPDVDGKSVLKLL-DPEKPGNR 397
Cdd:cd16156  297 TNIPLIIRGKGGEKAGTVTDTpVSHIDLAPTILDYAGIPQPKVLEGESILATIeDPEIPENR 358
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-375 1.59e-29

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


Pssm-ID: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 119.62  E-value: 1.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQ----DVELGSLQVMNKTRKIMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYtnnENCSSPS-W 117
Cdd:cd16035    1 PNILLILTDQEryppPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPMqP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 118 QAMHEPRTFAVYLNNTGYRTAFFGKY-LNEYNGSYippgwrewlgliknsrfynytvcrngikekhgfdYAKDyftDLIT 196
Cdd:cd16035   78 LLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAAGGG----------------------------------YKRD---PGIA 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 197 NESINY-FKMSKRMYPHRPVMMVISHAAPH----GPEDSapqfsklypnasqhitPSYNYAPNMdkhwimqYtgpmlpih 271
Cdd:cd16035  121 AQAVEWlRERGAKNADGKPWFLVVSLVNPHdimfPPDDE----------------ERWRRFRNF-------Y-------- 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 272 meftnilqrkrLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEP 351
Cdd:cd16035  170 -----------YNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNAYEEALHVPLIISHPDLFG 238
                        330       340
                 ....*....|....*....|....*
gi 189571638 352 -GSIVPQIVLNIDLAPTILDIAGLD 375
Cdd:cd16035  239 tGQTTDALTSHIDLLPTLLGLAGVD 263
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-386 9.25e-29

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


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 116.18  E-value: 9.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQ-----------DVELGSLQVMNKTrkimehgGATFINAFVTTPMCCPSRSSMLTGKYVHNHNV-----Y 106
Cdd:cd16149    1 PNILFILTDDQgpwalgcygnsEAVTPNLDRLAAE-------GVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 107 TNNENCSSP-SWQAMHEprTFAVYLNNTGYRTAFFGKylneyngsyippgwreW-LGliknsrfynytvcrngikekhgf 184
Cdd:cd16149   74 GSHGKTKKPeGYLEGQT--TLPEVLQDAGYRCGLSGK----------------WhLG----------------------- 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 185 DYAKDYFTDLITNEsinyfkmskrmyphRPVMMVISHAAPHGPedsapqfsklypnasqhitpsynyapnmdkhWimQYt 264
Cdd:cd16149  113 DDAADFLRRRAEAE--------------KPFFLSVNYTAPHSP-------------------------------W--GY- 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 265 gpmlpihmeftnilqrkrLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGlVKGK-------SMpYDFD 337
Cdd:cd16149  145 ------------------FAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngtfplNM-YDNS 204
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189571638 338 IRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVD--GKSVL 386
Cdd:cd16149  205 VKVPFIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFA 256
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
42-388 5.30e-28

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: 117.54  E-value: 5.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDqdveLG-----------------SLQvmnktrkimeHGGATFiNAFVTTPMCCPSRSSMLTGKYVHNHN 104
Cdd:cd16025    2 RPNILLILADD----LGfsdlgcfggeiptpnldALA----------AEGLRF-TNFHTTALCSPTRAALLTGRNHHQVG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 105 VYTNNENCSS-PSWQAMHEPR--TFAVYLNNTGYRTAFFGKYlneYNGsyiPPGWrewlgliknsrfynytvcrngikek 181
Cdd:cd16025   67 MGTMAELATGkPGYEGYLPDSaaTIAEVLKDAGYHTYMSGKW---HLG---PDDY------------------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 182 hgfdyakdYFTDLITNESINYFKMSKRmyPHRPVMMVISHAAPHGPedsapqfsklypnasQHitpsynyAPnmdKHWIM 261
Cdd:cd16025  116 --------YSTDDLTDKAIEYIDEQKA--PDKPFFLYLAFGAPHAP---------------LQ-------AP---KEWID 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 262 QYTG---------------------------PMLPIHMEFT--NIL---QRKRLQTLMSV--------DDSVERLYNMLV 301
Cdd:cd16025  161 KYKGkydagwdalreerlerqkelglipadtKLTPRPPGVPawDSLspeEKKLEARRMEVyaamvehmDQQIGRLIDYLK 240
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 302 ETGELENTYIIYTADHG--YHIG--QFG---LVKGKSMPYDFDIRVPFFIRGPSV--EPGSIVPQIVLNIDLAPTILDIA 372
Cdd:cd16025  241 ELGELDNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKGikAKGGIRHQFAHVIDIAPTILELA 320
                        410
                 ....*....|....*.
gi 189571638 373 GLDTPPDVDGKSVLKL 388
Cdd:cd16025  321 GVEYPKTVNGVPQLPL 336
PRK13759 PRK13759
arylsulfatase; Provisional
42-397 5.47e-28

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 118.62  E-value: 5.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQDVE-LGSL---QVMNKTRKIMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSspsW 117
Cdd:PRK13759   6 KPNIILIMVDQMRGDcLGCNgnkAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 118 QAMHE-PRTFAvylnNTGYRTAFFGKYlneyngSYIPPgwREWLGLiKNSRFYNYTVCRNGIKEKHGFDYAKDY------ 190
Cdd:PRK13759  83 NYKNTlPQEFR----DAGYYTQCIGKM------HVFPQ--RNLLGF-HNVLLHDGYLHSGRNEDKSQFDFVSDYlawlre 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 191 --------FTDL-----------------------ITNESINYFKmskRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYP 239
Cdd:PRK13759 150 kapgkdpdLTDIgwdcnswvarpwdleerlhptnwVGSESIEFLR---RRDPTKPFFLKMSFARPHSPYDPPKRYFDMYK 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 240 NASQHITPSYNYAPNMDKH-WIMQYTGPMLPIHMEFtniLQRKRLQTLMS---VDDSVERLYNMLVETGELENTYIIYTA 315
Cdd:PRK13759 227 DADIPDPHIGDWEYAEDQDpEGGSIDALRGNLGEEY---ARRARAAYYGLithIDHQIGRFLQALKEFGLLDNTIILFVS 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 316 DHGYHIGQFGLVKgKSMPYDFDIRVPFFIRGPS----VEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDP 391
Cdd:PRK13759 304 DHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFG 382

                 ....*.
gi 189571638 392 EKPGNR 397
Cdd:PRK13759 383 QYEGWR 388
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
43-385 1.55e-26

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: 112.64  E-value: 1.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQ---DVEL-GSLQVmnKT---RKIMEHGgaTFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSP 115
Cdd:cd16029    1 PHIVFILADDLgwnDVGFhGSDQI--KTpnlDALAADG--VILNNYYVQPICTPSRAALMTGRYPIHTGMQHGVILAGEP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SWQAMHEPrTFAVYLNNTGYRTAFFGKY-LNEYNGSYIPPGwR-------EWLGLI-----KNSRFYNYTVCRNGIKEKH 182
Cdd:cd16029   77 YGLPLNET-LLPQYLKELGYATHLVGKWhLGFYTWEYTPTN-RgfdsfygYYGGAEdyythTSGGANDYGNDDLRDNEEP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 183 GFDYAKDYFTDLITNESINYFKMSKrmyPHRPVMMVISHAAPHGPEDSAPQFSKLYPNASQHITPsynyapnmdkhwimq 262
Cdd:cd16029  155 AWDYNGTYSTDLFTDRAVDIIENHD---PSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKD--------------- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 263 ytgpmlpihmeftniLQRKRLQTLMS-VDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFG------LVKGKSMPYD 335
Cdd:cd16029  217 ---------------EDRRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDggsnypLRGGKNTLWE 281
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189571638 336 FDIRVPFFIRGPSVEP--GSIVPQIVLNIDLAPTILDIAGLDTP--PDVDGKSV 385
Cdd:cd16029  282 GGVRVPAFVWSPLLPPkrGTVSDGLMHVTDWLPTLLSLAGGDPDdlPPLDGVDQ 335
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-389 2.60e-26

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


Pssm-ID: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 111.92  E-value: 2.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQDVE-LGSL-QVMNKTRKI--MEHGGATFINAFvTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPswq 118
Cdd:cd16151    1 PNIILIMADDLGYEcIGCYgGESYKTPNIdaLAAEGVRFNNAY-AQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQK--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 119 amheprTFAVYLNNTGYRTAFFGK---YLNEYNGSYIPP-GWREWL-------GLIKNSRFYNYTVCRNGIKEKhgfDYA 187
Cdd:cd16151   77 ------TFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHEfGFDEYClwqltetGEKYSRPATPTFNIRNGKLLE---TTE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 188 KDYFTDLITNESINYFKMSKR-----MYPhrpvmMVIshaaPHGPEDSAPQFSKLYPnasqhitPSYNYAPNMDKHWIM- 261
Cdd:cd16151  148 GDYGPDLFADFLIDFIERNKDqpffaYYP-----MVL----VHDPFVPTPDSPDWDP-------DDKRKKDDPEYFPDMv 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 262 QYTgpmlpihmeftnilqrkrlqtlmsvDDSVERLYNMLVETGELENTYIIYTADHGYHIG-----QFGLVKG-KSMPYD 335
Cdd:cd16151  212 AYM-------------------------DKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTD 266
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189571638 336 FDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLKLL 389
Cdd:cd16151  267 AGTHVPLIVNWPGlIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDypLDGRSFAPQL 323
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
74-397 7.86e-24

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 105.39  E-value: 7.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  74 GATFINAFVTTPMCCPSRSSMLTGKY--VHNHNVYTNnencsspsWQAMHEPrTFAVYLNNTGYRTAFFGKylneyNGSY 151
Cdd:cd16150   36 GVRFSNAYCQNPVCSPSRCSFLTGWYphVNGHRTLHH--------LLRPDEP-NLLKTLKDAGYHVAWAGK-----NDDL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 152 IPPGWREwlgliknsrfyNYTVCrngikekhgfDYAkdyftdlITNESINYFKmskRMYPHRPVMMVISHAAPHGP-EDS 230
Cdd:cd16150  102 PGEFAAE-----------AYCDS----------DEA-------CVRTAIDWLR---NRRPDKPFCLYLPLIFPHPPyGVE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 231 APQFSKLYPNASQHITPSynyapnmdKHWIMQYtgPMLPIHMEFTNiLQR---KRLQTL--------MSVDDSVERLYNM 299
Cdd:cd16150  151 EPWFSMIDREKLPPRRPP--------GLRAKGK--PSMLEGIEKQG-LDRwseERWRELratylgmvSRLDHQFGRLLEA 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 300 LVETGELENTYIIYTADHGYHIGQFGLV-KGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPP 378
Cdd:cd16150  220 LKETGLYDDTAVFFFSDHGDYTGDYGLVeKWPNTFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSH 299
                        330       340
                 ....*....|....*....|
gi 189571638 379 DVDGKSVLKLL-DPEKPGNR 397
Cdd:cd16150  300 THFGRSLLPVLaGETEEHRD 319
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
42-387 1.16e-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: 101.68  E-value: 1.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQDVElgSLQVMNKTR---KIMEHG-------------GATFINAFVTTPMCCPSRSSMLTGKYVHNHNV 105
Cdd:cd16153    1 KPNILWIITDDQRVD--SLSCYNNAHtgkSESRLGyvespnidalaaeGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 106 YtNNENcsspSWQAMHE-PRTFAVYLNNTGYRTAFFGKylneyngsyipPGWREWLGLIKNSrfyNYTVCRNGIKEKHGF 184
Cdd:cd16153   79 Y-GFEA----AHPALDHgLPTFPEVLKKAGYQTASFGK-----------SHLEAFQRYLKNA---NQSYKSFWGKIAKGA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 185 DYAKdyftdlitnesinyfkmskrmyphrPVMMVISHAAPHGPedsapqfsklypnasqhITPSYNYAPNMDKHWIMQYt 264
Cdd:cd16153  140 DSDK-------------------------PFFVRLSFLQPHTP-----------------VLPPKEFRDRFDYYAFCAY- 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 265 gpmlpihmeftnilqrkrlqtlmsVDDSVERLYNMLVETGEL---ENTYIIYTADHGYHIGQFGLVkGKSMPYDFDIRVP 341
Cdd:cd16153  177 ------------------------GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGIL-AKFTFWPQSHRVP 231
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189571638 342 FFIRGPSVEP---GSIVPQIVLNIDLAPTILDIAGLD--TPPDVDGKSVLK 387
Cdd:cd16153  232 LIVVSSDKLKapaGKVRHDFVEFVDLAPTLLAAAGVDvdAPDYLDGRDLFE 282
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
43-400 5.47e-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: 98.96  E-value: 5.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQDVE------LGSLQVMNKTRKIMEHGGATFINAFVTtPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd16154    1 PNILLIIADDQGLDssaqysLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLSE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 wqamHE-PRTFAVYLNNTGYRTAFFGKYL--NEYNGSYIPPGWREWLGLIKN--SRFYNYTVCRNGIKEKHGfDYAKDYF 191
Cdd:cd16154   80 ----ETlLQLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNST-EYATTKL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 192 TDL----ITNESINYFkmskrmyphrpvmMVISHAAPHGPedsapqFsKLYPNA--SQHITPSYnyapnmdkhwimqytg 265
Cdd:cd16154  155 TNLaidwIDQQTKPWF-------------LWLAYNAPHTP------F-HLPPAElhSRSLLGDS---------------- 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 266 pmlpihmefTNILQRKR---LQTLMSVDDSVERLYNMLVETgELENTYIIYTADHGYHiGQ-----FGLVKGKSMPYDFD 337
Cdd:cd16154  199 ---------ADIEANPRpyyLAAIEAMDTEIGRLLASIDEE-ERENTIIIFIGDNGTP-GQvvdlpYTRNHAKGSLYEGG 267
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189571638 338 IRVPFFIRGPSVEPGSIVPQIVLNI-DLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNRFRT 400
Cdd:cd16154  268 INVPLIVSGAGVERANERESALVNAtDLYATIAELAGVDAAEIHDSVSFKPLLSDVNASTRQYN 331
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
42-394 1.18e-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: 1.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDqdVELGSLQVMNKTRKimEHG--------GATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYtnNENCS 113
Cdd:cd16160    1 KPNIVLFFADD--MGYGDLASYGHPTQ--ERGpiddmaaeGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMY--GGTRV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 114 SPSWQAMHEPR---TFAVYLNNTGYRTAFFGKY---LNEYN---GSYIPpgwrewlgliknsrfynytvcrngikEKHGF 184
Cdd:cd16160   75 FLPWDIGGLPKtevTMAEALKEAGYTTGMVGKWhlgINENNhsdGAHLP--------------------------SHHGF 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 185 DYA---------------------KD------YFTDLITNESINYFKMSKRMYP----------HRPVMMVISHAAPHGP 227
Cdd:cd16160  129 DFVgtnlpftnswacddtgrhvdfPDrsacflYYNDTIVEQPIQHEHLTETLVGdaksfiednqENPFFLYFSFPQTHTP 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 228 EDSAPQFSklypNASQHitpsYNYAPNMDKhwimqytgpmlpihmeftnilqrkrlqtlMSVddSVERLYNMLVETGELE 307
Cdd:cd16160  209 LFASKRFK----GKSKR----GRYGDNINE-----------------------------MSW--AVGEVLDTLVDTGLDQ 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 308 NTYIIYTADHGYHI------GQFGLVKG-KSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPD- 379
Cdd:cd16160  250 NTLVFFLSDHGPHVeyclegGSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTDr 329
                        410
                 ....*....|....*.
gi 189571638 380 -VDGKSVLKLLDPEKP 394
Cdd:cd16160  330 iYDGLSITDLLLGEAD 345
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
43-389 1.87e-19

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: 91.06  E-value: 1.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQDVELgSLQVMNKTRKI-----MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYtNNENCSSPSW 117
Cdd:cd16171    1 PNVVMVMSDSFDGRL-TFRPGNQVVDLpyinfMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW-NNYKGLDPNY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 118 QamheprTFAVYLNNTGYRTAFFGKyLNEYNGSYIPPGWRE-WlgliknSRFYNYTVCRNGIKEkhgfdyakdyfTDLIT 196
Cdd:cd16171   79 P------TWMDRLEKHGYHTQKYGK-LDYTSGHHSVSNRVEaW------TRDVPFLLRQEGRPT-----------VNLVG 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 197 NESinyfkmskrmypHRPVMMvishaaphgpedsapqfsKLYPNASQHITPSYNYAPNMDKHWIMqYTGPMLP------- 269
Cdd:cd16171  135 DRS------------TVRVML------------------KDWQNTDKAVHWIRKEAPNLTQPFAL-YLGLNLPhpypsps 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 270 IHMEFTNILQRKRLQTLM--SVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMpYDFDIRVPFFIRGP 347
Cdd:cd16171  184 MGENFGSIRNIRAFYYAMcaETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSM-YEGSSHVPLLIMGP 262
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 189571638 348 SVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLL 389
Cdd:cd16171  263 GIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLL 304
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
768-817 1.01e-18

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: 89.15  E-value: 1.01e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 189571638 768 CTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTV 817
Cdd:cd16147  347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
42-422 8.84e-18

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 87.79  E-value: 8.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLtddqdVElgSLQ--VMNKT----------RKIMEHGgATFINAFVTTPMCCPSRSSMLTGKY-VHNHNVYTN 108
Cdd:COG1368  234 KPNVVVIL-----LE--SFSdfFIGALgngkdvtpflDSLAKES-LYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKR 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 109 NencsspswqAMHEPRTFAVYLNNTGYRTAFFgkylneYNGsyippgwrewlglikNSRFYNytvcRNGIKEKHGFD--Y 186
Cdd:COG1368  306 P---------GQNNFPSLPSILKKQGYETSFF------HGG---------------DGSFWN----RDSFYKNLGFDefY 351
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 187 AKDYFTDLITN-----------ESINYFKMSKRmyphrPVMMVISHAAPHGPedsapqfsklypnasqhitpsynYAPNM 255
Cdd:COG1368  352 DREDFDDPFDGgwgvsdedlfdKALEELEKLKK-----PFFAFLITLSNHGP-----------------------YTLPE 403
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 256 DKHWIMQYTGPMLpihmeftnilqRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGyhigqfGLVKGKSmPYD 335
Cdd:COG1368  404 EDKKIPDYGKTTL-----------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYE 465
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 336 FDI---RVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVD-GKSvlkLLDPEKPGNRFR-----TNKKAKI 406
Cdd:COG1368  466 NPLeryRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAfGRD---LLSPDTDPFAFRnggfiTDDYVYV 542
                        410
                 ....*....|....*.
gi 189571638 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 2.87e-17

Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.


Pssm-ID: 293739 [Multi-domain]  Cd Length: 283  Bit Score: 83.12  E-value: 2.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVL-----TDDQDVELGSLQVMNKTRKIMEHGgATFINAFVTTPMCCPSRS--SMLTGkyvhnhnVYTNNENCSSP 115
Cdd:cd16015    1 PNVIVILlesfsDPYIDKDVGGEDLTPNLNKLAKEG-LYFGNFYSPGFGGGTANGefEVLTG-------LPPLPLGSGSY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SWQAMHEPRTFAVYLNNTGYRTAFFgkylneYNGsyippgwrewlglikNSRFYNytvcRNGIKEKHGFD--YAKDYFTD 193
Cdd:cd16015   73 TLYKLNPLPSLPSILKEQGYETIFI------HGG---------------DASFYN----RDSVYPNLGFDefYDLEDFPD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 194 LITNESINY------FKMSKRMY---PHRPVMMVISHAAPHGPedsapqfsklypnasqhitpsYNYAPNMDKhwimqyt 264
Cdd:cd16015  128 DEKETNGWGvsdeslFDQALEELeelKKKPFFIFLVTMSNHGP---------------------YDLPEEKKD------- 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 265 gpmLPIHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFdiRVPFFI 344
Cdd:cd16015  180 ---EPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLI 254
                        330       340
                 ....*....|....*....|....*....
gi 189571638 345 RGPSVEPGSIVPQIVLNIDLAPTILDIAG 373
Cdd:cd16015  255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
42-389 8.00e-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: 84.06  E-value: 8.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDQDV-ELGSLQVMNK-TRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNE---NCSS 114
Cdd:cd16157    1 KPNIILMLMDDMGWgDLGVFGEPSReTPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharNAYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 115 PSWQAMHEPRT---FAVYLNNTGYRTAFFGKYLNEYNGSYIP--PGWREWLG-------LIKNSRFYNYTVCRNgikEKH 182
Cdd:cd16157   81 PQNIVGGIPDSeilLPELLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWFGapnchfgPYDNKAYPNIPVYRD---WEM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 183 GFDYAKDYFTDLITNESiNYfkmsKRMYPHRPVMMVISHAAPHgpedsAPQFSKLYPNASQhiTPSYNYAPnmdkhwimq 262
Cdd:cd16157  158 IGRYYEEFKIDKKTGES-NL----TQIYLQEALEFIEKQHDAQ-----KPFFLYWAPDATH--APVYASKP--------- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 263 ytgpmlpihmeFTNILQRKRL-QTLMSVDDSVERLYNMLVETGELENTYIIYTADHG---YHIGQFG-----LVKGKSMP 333
Cdd:cd16157  217 -----------FLGTSQRGLYgDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPEQGgsngpFLCGKQTT 285
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189571638 334 YDFDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLKLL 389
Cdd:cd16157  286 FEGGMREPAIAWWPGhIKPGQVSHQLGSLMDLFTTSLALAGLPIPSDraIDGIDLLPVL 344
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
43-397 6.88e-16

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: 81.34  E-value: 6.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQDV-ELG-----SLQVMNKTRkiMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSpS 116
Cdd:cd16158    2 PNIVLLFADDLGYgDLGcyghpSSSTPNLDR--LAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGS-R 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQAMHEPRTFAVYLNNTGYRTAFFGKY---LNEyNGSYIPP--GWREWLGL---------IKNSRFYNYTVCRNGIKEkh 182
Cdd:cd16158   79 GGLPLNETTIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPThqGFDHYLGIpyshdqgpcQNLTCFPPNIPCFGGCDQ-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 183 GFDYAKDYFTDLITNESINYFKMSKRM--YPHRpvmmVISHAAphgpEDSAPQFskLYpNASQHItpsynYAPnmdkhwi 260
Cdd:cd16158  156 GEVPCPLFYNESIVQQPVDLLTLEERYakFAKD----FIADNA----KEGKPFF--LY-YASHHT-----HYP------- 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 261 mQYTGpmlpihMEFTNILQRKRL-QTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHI------GQFGLVK-GKSM 332
Cdd:cd16158  213 -QFAG------QKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGLLKcGKGT 285
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189571638 333 PYDFDIRVPFFIRGPS-VEPGsIVPQIVLNIDLAPTILDIAGLDTPP-DVDGKSVLKLLDPEKPGNR 397
Cdd:cd16158  286 TYEGGVREPAIAYWPGrIKPG-VTHELASTLDILPTIAKLAGAPLPNvTLDGVDMSPILFEQGKSPR 351
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
43-379 1.42e-15

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


Pssm-ID: 293761 [Multi-domain]  Cd Length: 372  Bit Score: 79.50  E-value: 1.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQDV-ELGS----LQVMNKTRKI--MEHGGATFINAFVTtPMCCPSRSSMLTGKYVhnhnvytNNENCSSP 115
Cdd:cd16142    1 PNILVILGDDIGWgDLGCygggIGRGAPTPNIdrLAKEGLRFTSFYVE-PSCTPGRAAFITGRHP-------IRTGLTTV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 116 SWQ-AMH----EPRTFAVYLNNTGYRTAFFGK-YLNEYNGSYipP---GWREWLGliknsrFYNYTVcrngikEKHGFDY 186
Cdd:cd16142   73 GLPgSPGglppWEPTLAELLKDAGYATAQFGKwHLGDEDGRL--PtdhGFDEFYG------NLYHTI------DEEIVDK 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 187 AKDYFTDLITNE-----SINYFKMSKRMYPHrpvmmvishaaphgpEDSAPQFSKLYPNASqhitpsynyapnmdkhwim 261
Cdd:cd16142  139 AIDFIKRNAKADkpfflYVNFTKMHFPTLPS---------------PEFEGKSSGKGKYAD------------------- 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 262 qytgpmlpihmeftnilqrkrlqTLMSVDDSVERLYNMLVETGELENTYIIYTADHG-----YHIGQFGLVKG-KSMPYD 335
Cdd:cd16142  185 -----------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeKGTTWE 241
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 189571638 336 FDIRVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPD 379
Cdd:cd16142  242 GGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPKD 286
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
42-389 2.11e-14

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: 76.94  E-value: 2.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDDqdveLG----------SLQVMNKTR------KIMEHGGATfinafvttPMCCPSRSSMLTGKY------ 99
Cdd:cd16159    1 KPNIVLFMADD----LGigdvgcfgndTIRTPNIDRlakegvKLTHHLAAA--------PLCTPSRAAFLTGRYpirsgm 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 100 VHNHNVYTNNENCSS---PSWQAmheprTFAVYLNNTGYRTAFFGKY----------------LN--------------- 145
Cdd:cd16159   69 ASSHGMRVILFTASSgglPPNET-----TFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNhgfdyfyglpltnlk 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 146 --------EYNGSYIPP------------------------GWRE--------------WLGLIKNSRFYNYTVCRNG-I 178
Cdd:cd16159  144 dcgdgsngEYDLSFDPLfplltafvlitaltiflllylgavSKRFfvfllilsllfislFFLLLITNRYFNCILMRNHeV 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 179 KEKhgfDYAKDYFTDLITNESINYFKMSKRmyphRPVMMVISHAAPHGPEDSAPQFSklypNASQHitpsYNYAPNmdkh 258
Cdd:cd16159  224 VEQ---PMSLENLTQRLTKEAISFLERNKE----RPFLLVMSFLHVHTALFTSKKFK----GRSKH----GRYGDN---- 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 259 wimqytgpmlpihmeftnilqrkrlqtLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHI-----------GQFGLV 327
Cdd:cd16159  285 ---------------------------VEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeyggGNGGIY 337
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189571638 328 KGKSMP-YDFDIRVPFFIRGPSV-EPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLKLL 389
Cdd:cd16159  338 GGKKMGgWEGGIRVPTIVRWPGViPPGSVIDEPTSLMDIFPTVAALAGAPLPSDriIDGRDLMPLL 403
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
42-389 1.19e-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: 73.66  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  42 RPNIILVLTDD---QDVELGSLQVMNKTRKI--MEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVyTNNENCSSPS 116
Cdd:cd16161    1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTSVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQAMHEPrTFAVYLNNTGYRTAFFGKYLNEYNGSYIPpgwrewlglikNSRFYNYTVcrnGIKEKHGFDYAKDYF---TD 193
Cdd:cd16161   80 GLPLNET-TLAEVLRQAGYATGMIGKWHLGQREAYLP-----------NSRGFDYYF---GIPFSHDSSLADRYAqfaTD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 194 LITNESINyfkmskrmypHRPVMMVISHAAPHGPEDSAPQFsklyPNASQHITPsynyapnmdkhwimqyTGpmlpihme 273
Cdd:cd16161  145 FIQRASAK----------DRPFFLYAALAHVHVPLANLPRF----QSPTSGRGP----------------YG-------- 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 274 ftnilqrkrlQTLMSVDDSVERLYNMLVETGELENTYIIYTAD---------------HGYHIGQFGLVKGKSMPYDFDI 338
Cdd:cd16161  187 ----------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGH 256
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189571638 339 RVPFFIRGPS-VEPGSIVPQIVLNIDLAPTILDIAGLDTPPD--VDGKSVLKLL 389
Cdd:cd16161  257 REPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVL 310
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
43-372 2.63e-13

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: 70.53  E-value: 2.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638  43 PNIILVLTDDQDVELGSLQVMNKTR----KIMEHGGATFiNAFVTTPMC--CPSRSSMLTGKYVHNHNVYTNNENCSSPS 116
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPAPTtpnlKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 117 WQAMHEP---RTFAVYLNNTGYRTAFFG--KYLNEyngsyippgwrewlgliknsrfynytvcrnGIKEKHGFDYakdyf 191
Cdd:cd00016   80 SRAAGKDedgPTIPELLKQAGYRTGVIGllKAIDE------------------------------TSKEKPFVLF----- 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 192 tdlitnesINYfkmskrmyphrpvmmvishAAPHGPEDSAPQFSKLYPNASQHItpsynyapnmdkhwimqytgpmlpih 271
Cdd:cd00016  125 --------LHF-------------------DGPDGPGHAYGPNTPEYYDAVEEI-------------------------- 151
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 272 meftnilqrkrlqtlmsvDDSVERLYNMLVETGELENTYIIYTADHG---YHIGQFGLVKGKSMPYDFDIRVPFFIRGPS 348
Cdd:cd00016  152 ------------------DERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPG 213
                        330       340
                 ....*....|....*....|....
gi 189571638 349 VEPGSIVPQIVLNIDLAPTILDIA 372
Cdd:cd00016  214 VKKGGVKHELISQYDIAPTLADLL 237
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
284-373 1.35e-07

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


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 53.74  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 284 QTLMSVDDSVERLYNMLVETGELENTYIIYTADHGY-----HiGQFglvkgksmPYDFDIRVPFFIRGPSVEPGSIVPQI 358
Cdd:cd16018  183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GYD--------NELPDMRAIFIARGPAFKKGKKLGPF 253
                         90
                 ....*....|....*
gi 189571638 359 vLNIDLAPTILDIAG 373
Cdd:cd16018  254 -RNVDIYPLMCNLLG 267
COG3379 COG3379
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ...
342-390 2.90e-06

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


Pssm-ID: 442606 [Multi-domain]  Cd Length: 472  Bit Score: 50.67  E-value: 2.90e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 189571638 342 FFIRGPSVEPGSIVPQIVLnIDLAPTILDIAGLDTPPDVDGKSVLKLLD 390
Cdd:COG3379  422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAFA 469
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
229-378 7.78e-06

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: 49.52  E-value: 7.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 229 DSAPQFSKLYPNASQhitPSYNYAPNMDKHWIMQYTGPMLPIHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETGELEN 308
Cdd:COG3083  379 SDRPWFSYLFLDAPH---AYSFPADYPKPFQPSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLEN 455
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 309 TYIIYTADHGY-----------HIGQFGlvkgksmpyDFDIRVPFFIRGPSVEPGSIvPQIVLNIDLAPTIL-DIAGLDT 376
Cdd:COG3083  456 TIVIITADHGEefnengqnywgHNSNFS---------RYQLQVPLVIHWPGTPPQVI-SKLTSHLDIVPTLMqRLLGVQN 525

                 ..
gi 189571638 377 PP 378
Cdd:COG3083  526 PA 527
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
289-387 2.20e-03

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 41.63  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 289 VDDSVERLYNMLVETGeleNTYIIyTADHG-------YHIGQfglvkgksmPY------DfdirVPFFIRGPSV---EPG 352
Cdd:PRK05434 417 VDECLGRVVDAVLKVG---GTLLI-TADHGnaeqmidPETGQ---------PHtahttnP----VPFILVGGKAlrlEGG 479
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 189571638 353 SIvpqivlnIDLAPTILDIAGLDTPPDVDGKSVLK 387
Cdd:PRK05434 480 KL-------ADIAPTILDLLGLEQPAEMTGKSLIE 507
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
290-375 4.07e-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: 40.30  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 290 DDSVERLYNMLVETGEleNTYIIYTADHGYHIGQFGlVKGKSMPYDFD--IRVPFFI--------RGPSVEPGSIVPQIV 359
Cdd:cd16017  196 DYVLSQIIERLKKKDK--DAALIYFSDHGESLGENG-LYLHGAPYAPKeqYHVPFIIwssdsykqRYPVERLRANKDRPF 272
                         90
                 ....*....|....*.
gi 189571638 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 5.31e-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: 5.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571638 283 LQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGyhIGQFGLVKGKSmpyDFDIRVPFF-----IRGPSVEPGSI--- 354
Cdd:cd16020  182 LENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHG--MTDWGSHGDGS---PDETETPFIawgagIKHPTPGRGPSfsa 256
                         90       100
                 ....*....|....*....|.
gi 189571638 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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