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Conserved domains on  [gi|1039796378|ref|XP_017173883|]
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iduronate 2-sulfatase isoform X2 [Mus musculus]

Protein Classification

sulfatase( domain architecture ID 10888136)

sulfatase catalyzes the hydrolysis of sulfate ester bonds of a wide variety of substrates, similar to iduronate 2-sulfatase that hydrolyzes the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate, and heparin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 1-454 9.35e-134

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: 392.71  E-value: 9.35e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378   1 MSVGKVFHPGISSNhsDDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHANLLCPVDVADVPEGTLPDKQSTEEAIRLLE 80
Cdd:cd16030    97 AGVGKIFHPGIPDG--DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYPDGKVADEAIEQLR 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  81 KMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPDSLPPVAYNPWMDIREREDVQALNISVPYGPIPE 160
Cdd:cd16030   175 KLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPD 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 161 DFQhrcsicsililrqsscesswkehllllsrgfqlpsevlclfaeRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNT 240
Cdd:cd16030   254 EQA-------------------------------------------RELRQAYYASVSYVDAQVGRVLDALEELGLADNT 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 241 IIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLF 320
Cdd:cd16030   291 IVVLWSDHGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTKP------------------------GKVTDALVELVDIY 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 321 PTLAGLAGLPVPPrcpipsfhvelCREGQNLQKHLQlhdleeEPDLFGNPReliAYSQYPRPAdfpqwnsdkpslndikV 400
Cdd:cd16030   347 PTLAELAGLPAPP-----------CLEGKSLVPLLK------NPSAKWKDA---AFSQYPRPS----------------I 390

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796378 401 MGYSIRTVDYRYTVWVgfdpseflaNFSDIHAGELYFVDSDPLQDHNVYNDSQH 454
Cdd:cd16030   391 MGYSIRTERYRYTEWV---------DFDKVGAEELYDHKNDPNEWKNLANDPEY 435
 
Name Accession Description Interval E-value
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 1-454 9.35e-134

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: 392.71  E-value: 9.35e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378   1 MSVGKVFHPGISSNhsDDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHANLLCPVDVADVPEGTLPDKQSTEEAIRLLE 80
Cdd:cd16030    97 AGVGKIFHPGIPDG--DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYPDGKVADEAIEQLR 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  81 KMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPDSLPPVAYNPWMDIREREDVQALNISVPYGPIPE 160
Cdd:cd16030   175 KLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPD 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 161 DFQhrcsicsililrqsscesswkehllllsrgfqlpsevlclfaeRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNT 240
Cdd:cd16030   254 EQA-------------------------------------------RELRQAYYASVSYVDAQVGRVLDALEELGLADNT 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 241 IIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLF 320
Cdd:cd16030   291 IVVLWSDHGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTKP------------------------GKVTDALVELVDIY 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 321 PTLAGLAGLPVPPrcpipsfhvelCREGQNLQKHLQlhdleeEPDLFGNPReliAYSQYPRPAdfpqwnsdkpslndikV 400
Cdd:cd16030   347 PTLAELAGLPAPP-----------CLEGKSLVPLLK------NPSAKWKDA---AFSQYPRPS----------------I 390

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796378 401 MGYSIRTVDYRYTVWVgfdpseflaNFSDIHAGELYFVDSDPLQDHNVYNDSQH 454
Cdd:cd16030   391 MGYSIRTERYRYTEWV---------DFDKVGAEELYDHKNDPNEWKNLANDPEY 435
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
72-451 4.10e-44

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 159.27  E-value: 4.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  72 TEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapdphvPDSLPPVAYNPWmdireredvqalni 151
Cdd:COG3119   134 TDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPL------PPNLAPRDLTEE-------------- 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 152 svpygpipedfqhrcsicsililrqsscesswkehllllsrgfqlpsevlclfAERKIRQSYFASVSYLDTQVGHVLSAL 231
Cdd:COG3119   194 -----------------------------------------------------ELRRARAAYAAMIEEVDDQVGRLLDAL 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 232 DDLRLAHNTIIAFTSDHGWALGEHG-EWAKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHT 310
Cdd:COG3119   221 EELGLADNTIVVFTSDNGPSLGEHGlRGGKGTLYEGGIRVPLIVRWPGKIKA------------------------GSVS 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 311 EDLVELVSLFPTLAGLAGLPVPPRCpipsfhvelcrEGQNLQKHLQlhdlEEEPDlfgnPRELIaYSQYPRPAdfpqwns 390
Cdd:COG3119   277 DALVSLIDLLPTLLDLAGVPIPEDL-----------DGRSLLPLLT----GEKAE----WRDYL-YWEYPRGG------- 329

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796378 391 dkpslndikvMGYSIRTVDYRYTVWVGFDPSEflanfsdihagELYFVDSDPLQDHNVYND 451
Cdd:COG3119   330 ----------GNRAIRTGRWKLIRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
PRK13759 PRK13759
arylsulfatase; Provisional
 60-333 2.18e-26

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 111.30  E-value: 2.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  60 DVPEGTLPDKQSTEEAIRLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlaPDPHVPDslppvaynpWmD 139
Cdd:PRK13759  174 DLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADI---PDPHIGD---------W-E 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 140 IREREDVQALNISVPYGPIPEDFQHRCsicsililrqsscesswkehllllsrgfqlpsevlclfaerkiRQSYFASVSY 219
Cdd:PRK13759  240 YAEDQDPEGGSIDALRGNLGEEYARRA-------------------------------------------RAAYYGLITH 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 220 LDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGRTAPLPaagqklfpyrdpfdp 299
Cdd:PRK13759  277 IDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGN--------------- 341

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796378 300 asdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPP 333
Cdd:PRK13759  342 ------RGTVIDQVVELRDIMPTLLDLAGGTIPD 369
Sulfatase pfam00884
Sulfatase;
205-329 7.56e-14

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 72.07  E-value: 7.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 205 AERKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVA----TRVPLMLYVPGRT 280
Cdd:pfam00884 194 SEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNApeggYRVPLLIWSPGGK 273

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1039796378 281 APlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGL 329
Cdd:pfam00884 274 AK------------------------GQKSEALVSHVDLFPTILDLAGI 298
 
Name Accession Description Interval E-value
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 1-454 9.35e-134

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: 392.71  E-value: 9.35e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378   1 MSVGKVFHPGISSNhsDDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHANLLCPVDVADVPEGTLPDKQSTEEAIRLLE 80
Cdd:cd16030    97 AGVGKIFHPGIPDG--DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYPDGKVADEAIEQLR 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  81 KMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPDSLPPVAYNPWMDIREREDVQALNISVPYGPIPE 160
Cdd:cd16030   175 KLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPD 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 161 DFQhrcsicsililrqsscesswkehllllsrgfqlpsevlclfaeRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNT 240
Cdd:cd16030   254 EQA-------------------------------------------RELRQAYYASVSYVDAQVGRVLDALEELGLADNT 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 241 IIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLF 320
Cdd:cd16030   291 IVVLWSDHGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTKP------------------------GKVTDALVELVDIY 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 321 PTLAGLAGLPVPPrcpipsfhvelCREGQNLQKHLQlhdleeEPDLFGNPReliAYSQYPRPAdfpqwnsdkpslndikV 400
Cdd:cd16030   347 PTLAELAGLPAPP-----------CLEGKSLVPLLK------NPSAKWKDA---AFSQYPRPS----------------I 390

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796378 401 MGYSIRTVDYRYTVWVgfdpseflaNFSDIHAGELYFVDSDPLQDHNVYNDSQH 454
Cdd:cd16030   391 MGYSIRTERYRYTEWV---------DFDKVGAEELYDHKNDPNEWKNLANDPEY 435
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
72-451 4.10e-44

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 159.27  E-value: 4.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  72 TEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapdphvPDSLPPVAYNPWmdireredvqalni 151
Cdd:COG3119   134 TDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPL------PPNLAPRDLTEE-------------- 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 152 svpygpipedfqhrcsicsililrqsscesswkehllllsrgfqlpsevlclfAERKIRQSYFASVSYLDTQVGHVLSAL 231
Cdd:COG3119   194 -----------------------------------------------------ELRRARAAYAAMIEEVDDQVGRLLDAL 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 232 DDLRLAHNTIIAFTSDHGWALGEHG-EWAKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHT 310
Cdd:COG3119   221 EELGLADNTIVVFTSDNGPSLGEHGlRGGKGTLYEGGIRVPLIVRWPGKIKA------------------------GSVS 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 311 EDLVELVSLFPTLAGLAGLPVPPRCpipsfhvelcrEGQNLQKHLQlhdlEEEPDlfgnPRELIaYSQYPRPAdfpqwns 390
Cdd:COG3119   277 DALVSLIDLLPTLLDLAGVPIPEDL-----------DGRSLLPLLT----GEKAE----WRDYL-YWEYPRGG------- 329

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796378 391 dkpslndikvMGYSIRTVDYRYTVWVGFDPSEflanfsdihagELYFVDSDPLQDHNVYND 451
Cdd:COG3119   330 ----------GNRAIRTGRWKLIRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 7-462 5.97e-33

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: 128.88  E-value: 5.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378   7 FHPGISSNHSDDYPYSWSFPPYHPSsekYENTKTCKGQD----GKLHA-NLLCPVD---VADVPEGTLPDKQSTEEAIRL 78
Cdd:cd16033    63 HEHGVLNNVENAGAYSRGLPPGVET---FSEDLREAGYRngyvGKWHVgPEETPLDygfDEYLPVETTIEYFLADRAIEM 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  79 LEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPHVPDSLPPVAYNpwmDIREREDVQALNisvpygpi 158
Cdd:cd16033   140 LEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYR---RERKRWGVDTED-------- 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 159 pedfqhrcsicsililrqsscESSWKEhllllsrgfqlpsevlclfaerkIRQSYFASVSYLDTQVGHVLSALDDLRLAH 238
Cdd:cd16033   209 ---------------------EEDWKE-----------------------IIAHYWGYITLIDDAIGRILDALEELGLAD 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 239 NTIIAFTSDHGWALGEHGEWAK-YSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELV 317
Cdd:cd16033   245 DTLVIFTSDHGDALGAHRLWDKgPFMYEETYRIPLIIKWPGVIAA------------------------GQVVDEFVSLL 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 318 SLFPTLAGLAGLPVPPRCpipsfhvelcrEGQNLQKHLqlhdLEEEPDlfgNPRELIaysqyprpadFPQWNSdkpslND 397
Cdd:cd16033   301 DLAPTILDLAGVDVPPKV-----------DGRSLLPLL----RGEQPE---DWRDEV----------VTEYNG-----HE 347

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039796378 398 IKVMGYSIRTVDYRYtVWVGFDpseflanfsdihAGELYFVDSDPLQDHNVYNDSQHGGLLHSLR 462
Cdd:cd16033   348 FYLPQRMVRTDRYKY-VFNGFD------------IDELYDLESDPYELNNLIDDPEYEEILREMR 399
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 72-371 3.86e-31

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


Pssm-ID: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 123.06  E-value: 3.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  72 TEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPdsLPPVAyNPWMDIRereDVQalni 151
Cdd:cd16155   108 ADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPL-PENFLP--QHPFD-NGEGTVR---DEQ---- 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 152 svpYGPIPEDfqhrcsicsililrqsscesswkehllllsrgfqlPSEVlclfaeRKIRQSYFASVSYLDTQVGHVLSAL 231
Cdd:cd16155   177 ---LAPFPRT-----------------------------------PEAV------RQHLAEYYAMITHLDAQIGRILDAL 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 232 DDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTE 311
Cdd:cd16155   213 EASGELDNTIIVFTSDHGLAVGSHGLMGKQNLYEHSMRVPLIISGPG-------------------------IPKGKRRD 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 312 DLVELVSLFPTLAGLAGLPVPPRCPIPSF-----------HVELCREGQNLQ-----------------KHLQLHDLEEE 363
Cdd:cd16155   268 ALVYLQDVFPTLCELAGIEIPESVEGKSLlpvirgekkavRDTLYGAYRDGQrairddrwkliiyvpgvKRTQLFDLKKD 347

                         330
                  ....*....|..
gi 1039796378 364 P----DLFGNPR 371
Cdd:cd16155   348 PdelnNLADEPE 359
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 46-442 1.07e-28

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


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 115.33  E-value: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  46 GKLHANllcpvdVADVPEGTLPDKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdphv 125
Cdd:cd16037    96 GKLHFR------GEDQRHGFRYDRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY------------- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 126 pdslppvaynpwmdireredvqalnisvpygpipedfqhrcsicsililrqsscesswkehllllsrgfqlpsevlclfa 205
Cdd:cd16037       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 206 ERKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGRTaplpa 285
Cdd:cd16037   157 VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMYEESVRVPMIISGPGIP----- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 286 agqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPRCPipsfhvelcreGQNLQkhlqlhDLEEEPD 365
Cdd:cd16037   232 --------------------AGKRVKTPVSLVDLAPTILEAAGAPPPPDLD-----------GRSLL------PLAEGPD 274

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796378 366 lfgnPRELIAYSQYprpadfpqwnsdkpSLNDIKVMGYSIRTVDYRYTVWVGFDPseflanfsdihagELYFVDSDP 442
Cdd:cd16037   275 ----DPDRVVFSEY--------------HAHGSPSGAFMLRKGRWKYIYYVGYPP-------------QLFDLENDP 320
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
 207-336 1.42e-28

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: 114.98  E-value: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 207 RKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGRTAPlpaa 286
Cdd:cd16032   160 RRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSFFEGSARVPLIISAPGRFAP---- 235

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039796378 287 gqklfpyrdpfdpasdwmdagRHTEDLVELVSLFPTLAGLAGLPVPPRCP 336
Cdd:cd16032   236 ---------------------RRVAEPVSLVDLLPTLVDLAGGGTAPHVP 264
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
 72-462 6.24e-27

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: 112.24  E-value: 6.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  72 TEEAIRLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPLENI----TLAPDPHvpDSLPPVAYNPWMDIREREDVQ 147
Cdd:cd16031   149 TDKALDFLKERDKD-KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIpepeTFDDDDY--AGRPEWAREQRNRIRGVLDGR 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 148 ALNisvpygpiPEDFQHRCsicsililrqsscesswkehllllsrgfqlpsevlclfaerkirQSYFASVSYLDTQVGHV 227
Cdd:cd16031   226 FDT--------PEKYQRYM--------------------------------------------KDYLRTVTGVDDNVGRI 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 228 LSALDDLRLAHNTIIAFTSDHGWALGEHGeWA-KYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmda 306
Cdd:cd16031   254 LDYLEEQGLADNTIIIYTSDNGFFLGEHG-LFdKRLMYEESIRVPLIIRDPRLIKA------------------------ 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 307 GRHTEDLVELVSLFPTLAGLAGLPVPPRCpipsfhvelcrEGQNLQKHLQLHDLEEEPDLFgnpreLIAYSQYPRPADFP 386
Cdd:cd16031   309 GTVVDALVLNIDFAPTILDLAGVPIPEDM-----------QGRSLLPLLEGEKPVDWRKEF-----YYEYYEEPNFHNVP 372

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796378 387 QWnsdkpslndikvmgYSIRTVDYRYTVWVGFDPSEflanfsdihagELYFVDSDPLQDHNVYNDSQHGGLLHSLR 462
Cdd:cd16031   373 TH--------------EGVRTERYKYIYYYGVWDEE-----------ELYDLKKDPLELNNLANDPEYAEVLKELR 423
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 57-447 1.81e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 110.35  E-value: 1.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  57 DVADVPEGTLPDKQsTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRY-PKEFQKLYPLENITLAPDphvpdslppvayn 135
Cdd:cd16034   146 GKRIYIKGYSPDAE-TDLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRPN------------- 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 136 pwmdireredvqalnisVPYGPIPEDFQHRCsicsililrqsscesswkehllllsrgfqlpsevlclfaerkIRQsYFA 215
Cdd:cd16034   212 -----------------VPEDKKEEAGLRED------------------------------------------LRG-YYA 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 216 SVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGRtaplpaagqklfpyrd 295
Cdd:cd16034   232 MITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLMNKQVPYEESIRVPFIIRYPGK---------------- 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 296 pfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPPrcpipsfhvelCREGQNLQKHLqlhdLEEEPDLFGNpreliA 375
Cdd:cd16034   296 --------IKAGRVVDLLINTVDIMPTLLGLCGLPIPD-----------TVEGRDLSPLL----LGGKDDEPDS-----V 347

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796378 376 YSQYPRPadFPQWNSDKPSLNDIkvmgysIRTVDYRYTVWVGfdpseflanfsdihaGELYFVD--SDPLQDHN 447
Cdd:cd16034   348 LLQCFVP--FGGGSARDGGEWRG------VRTDRYTYVRDKN---------------GPWLLFDneKDPYQLNN 398
PRK13759 PRK13759
arylsulfatase; Provisional
 60-333 2.18e-26

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 111.30  E-value: 2.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  60 DVPEGTLPDKQSTEEAIRLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlaPDPHVPDslppvaynpWmD 139
Cdd:PRK13759  174 DLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADI---PDPHIGD---------W-E 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 140 IREREDVQALNISVPYGPIPEDFQHRCsicsililrqsscesswkehllllsrgfqlpsevlclfaerkiRQSYFASVSY 219
Cdd:PRK13759  240 YAEDQDPEGGSIDALRGNLGEEYARRA-------------------------------------------RAAYYGLITH 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 220 LDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGRTAPLPaagqklfpyrdpfdp 299
Cdd:PRK13759  277 IDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGN--------------- 341

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796378 300 asdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPP 333
Cdd:PRK13759  342 ------RGTVIDQVVELRDIMPTLLDLAGGTIPD 369
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 213-332 3.46e-26

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: 105.98  E-value: 3.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 213 YFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGE-WAKYSNFDVATRVPLMLYVPGRTAplpaagqklf 291
Cdd:cd16022   133 YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKKGSLYEGGIRVPFIVRWPGKIP---------- 202

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039796378 292 pyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVP 332
Cdd:cd16022   203 --------------AGQVSDALVSLLDLLPTLLDLAGIEPP 229
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 88-462 3.61e-24

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: 103.36  E-value: 3.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  88 PFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapDPHVPDsLPPVaynpwmdireREDvqalnisvpygpipedfqhrcs 167
Cdd:cd16027   143 PFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKV--PPYLPD-TPEV----------RED---------------------- 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 168 icsililrqsscesswkehllllsrgfqlpsevlclFAErkirqsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSD 247
Cdd:cd16027   188 ------------------------------------LAD------YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSD 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 248 HGWALGehgeWAKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLA 327
Cdd:cd16027   226 HGMPFP----RAKGTLYDSGLRVPLIVRWPGKIKP------------------------GSVSDALVSFIDLAPTLLDLA 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 328 GLPVPPrcpipsfhvELcrEGQNLqkhlqLHDLEEEPDlfgNPRELIaYSQYPRpadfpqwnsdkpslNDIKVMGY-SIR 406
Cdd:cd16027   278 GIEPPE---------YL--QGRSF-----LPLLKGEKD---PGRDYV-FAERDR--------------HDETYDPIrSVR 323

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796378 407 TVDYRYTVwvgfdpseflaNFSDIhagELYFVDSDPLQDHNVYNDSQHGGLLHSLR 462
Cdd:cd16027   324 TGRYKYIR-----------NYMPE---ELYDLKNDPDELNNLADDPEYAEVLEELR 365
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 207-462 1.18e-23

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 102.70  E-value: 1.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 207 RKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSN-F-DVATRVPLMLYVPGRTaplp 284
Cdd:cd16150   196 RELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNtFeDCLTRVPLIIKPPGGP---- 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 285 aagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPrcpiPSFHVELCRegqnlqkhlQLHDLEEEP 364
Cdd:cd16150   272 ---------------------AGGVSDALVELVDIPPTLLDLAGIPLSH----THFGRSLLP---------VLAGETEEH 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 365 D---------LFGNPReliAYSQYPRPADFPQWNS---DKPSLNDIKVMgysIRTVDYRYtVWVGFDPSeflanfsdiha 432
Cdd:cd16150   318 RdavfseggrLHGEEQ---AMEGGHGPYDLKWPRLlqqEEPPEHTKAVM---IRTRRYKY-VYRLYEPD----------- 379

                         250       260       270
                  ....*....|....*....|....*....|
gi 1039796378 433 gELYFVDSDPLQDHNVYNDSQHGGLLHSLR 462
Cdd:cd16150   380 -ELYDLEADPLELHNLIGDPAYAEIIAEMK 408
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 213-334 1.70e-21

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 93.77  E-value: 1.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 213 YFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK-YSNF-DVATRVPLMLYVPGRTaplpaagqkl 290
Cdd:cd16148   165 YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGhGSNLyDEQLHVPLIIRWPGKE---------- 234

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039796378 291 fpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPR 334
Cdd:cd16148   235 ---------------PGKRVDALVSHIDIAPTLLDLLGVEPPDY 263
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
 72-420 2.87e-21

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: 95.79  E-value: 2.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  72 TEEAIRLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdphvPDSLPPVAYNPWMDIREREDvqalni 151
Cdd:cd16028   144 TDRAIEYLDERQDE--PWFLHLSYIRPHPPFVAPAPYHALYD------------PADVPPPIRAESLAAEAAQH------ 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 152 svpygPIPEDFqhrcsicsililRQSSCESSWKEHLLLLSRgfqLPSEVLclfaeRKIRQSYFASVSYLDTQVGHVLSAL 231
Cdd:cd16028   204 -----PLLAAF------------LERIESLSFSPGAANAAD---LDDEEV-----AQMRATYLGLIAEVDDHLGRLFDYL 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 232 DDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGRTAplpaagqklfpyrdpfDPASdwmdaGRHTE 311
Cdd:cd16028   259 KETGQWDDTLIVFTSDHGEQLGDHWLWGKDGFFDQAYRVPLIVRDPRREA----------------DATR-----GQVVD 317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 312 DLVELVSLFPTLAGLAGLPVPPRCpipsfhvelcrEGQNLQKHLQlhdlEEEPdlfGNPRELIAYSQYPRPADFPQW--- 388
Cdd:cd16028   318 AFTESVDVMPTILDWLGGEIPHQC-----------DGRSLLPLLA----GAQP---SDWRDAVHYEYDFRDVSTRRPqea 379

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1039796378 389 ---NSDKPSLNdikvmgySIRTVDYRYTVWVGFDP 420
Cdd:cd16028   380 lglSPDECSLA-------VIRDERWKYVHFAALPP 407
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 213-340 5.70e-19

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


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 86.14  E-value: 5.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 213 YFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK------YSNFDVATRVPLMLYVPGRTAPlpaa 286
Cdd:cd16149   144 YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKgngtfpLNMYDNSVKVPFIIRWPGVVPA---- 219

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796378 287 gqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVP--PRCPIPSF 340
Cdd:cd16149   220 --------------------GRVVDSLVSAYDFFPTLLELAGVDPPadPRLPGRSF 255
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
 194-451 1.04e-18

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: 87.61  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 194 FQLPSEVLCLFAERKI---RQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEW------AKYSNF 264
Cdd:cd16146   188 LQVPDKYLDPYKDMGLddkLAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRFnagmrgKKGSVY 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 265 DVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPRCPIpsfhvel 344
Cdd:cd16146   268 EGGHRVPFFIRWPGKILA------------------------GKDVDTLTAHIDLLPTLLDLCGVKLPEGIKL------- 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 345 crEGQNLQKHLQlHDLEEEPDlfgnpRELIAYSQYPRPADFPQWNSdkpslndikvmgySIRTVDYRYtVWVGFDPSefl 424
Cdd:cd16146   317 --DGRSLLPLLK-GESDPWPE-----RTLFTHSGRWPPPPKKKRNA-------------AVRTGRWRL-VSPKGFQP--- 371

                         250       260
                  ....*....|....*....|....*..
gi 1039796378 425 anfsdihagELYFVDSDPLQDHNVYND 451
Cdd:cd16146   372 ---------ELYDIENDPGEENDVADE 389
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 188-331 7.07e-18

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: 83.58  E-value: 7.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 188 LLLSRGFQLPSEVLCLFAERKIRQSYFASVSYLDTQVGHVLSALDDLRLAH---NTIIAFTSDHGWALGEHGEWAKYSNF 264
Cdd:cd16153   145 FFVRLSFLQPHTPVLPPKEFRDRFDYYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQGILAKFTFW 224

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796378 265 DVATRVPLMLYVPGRtaplpaagqKLFPyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPV 331
Cdd:cd16153   225 PQSHRVPLIVVSSDK---------LKAP-------------AGKVRHDFVEFVDLAPTLLAAAGVDV 269
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 204-337 8.39e-16

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: 78.76  E-value: 8.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 204 FAERKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEW--------AKYSNFDVATRVPLMLY 275
Cdd:cd16026   204 FKGRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHGgsagplrgGKGTTWEGGVRVPFIAW 283

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796378 276 VPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPRCPI 337
Cdd:cd16026   284 WPGVIP------------------------AGTVSDELASTMDLLPTLAALAGAPLPEDRVI 321
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 207-334 5.59e-15

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: 75.32  E-value: 5.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 207 RKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSN-FDVATRVPLMLYVPGrtaplpa 285
Cdd:cd16035   163 RRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNaYEEALHVPLIISHPD------- 235

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1039796378 286 agqkLFPyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPR 334
Cdd:cd16035   236 ----LFG-------------TGQTTDALTSHIDLLPTLLGLAGVDAEAR 267
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
 207-333 5.86e-15

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: 76.04  E-value: 5.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 207 RKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRVPLMLYVPGrtaplpaa 286
Cdd:cd16171   192 RNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMYEGSSHVPLLIMGPG-------- 263

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1039796378 287 gqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPP 333
Cdd:cd16171   264 -----------------IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 206-447 6.14e-15

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: 76.10  E-value: 6.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 206 ERKIRQSYF-ASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEW-------AKYSNFDVATRVPLMLYVP 277
Cdd:cd16151   199 RKKDDPEYFpDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTngrevrgGKGKTTDAGTHVPLIVNWP 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 278 GRTaplpaagqklfpyrdpfdpasdwmDAGRHTEDLVELVSLFPTLAGLAGLPVPPRCPIpsfhvelcrEGQNLQkhlql 357
Cdd:cd16151   279 GLI------------------------PAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPL---------DGRSFA----- 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 358 hdleeePDLFGNP----RELIAYsqYPRpadfPQWNSDKPslndikvmgYSIRTVDYRYtvwvgfdpseflanFSDihaG 433
Cdd:cd16151   321 ------PQLLGKTgsprREWIYW--YYR----NPHKKFGS---------RFVRTKRYKL--------------YAD---G 362

                         250
                  ....*....|....
gi 1039796378 434 ELYFVDSDPLQDHN 447
Cdd:cd16151   363 RFFDLREDPLEKNP 376
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 213-462 1.42e-14

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


Pssm-ID: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 74.96  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 213 YFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHgwalGEH-----GEWaKYSNFDVATRVPLMLYVPGrtaplpaag 287
Cdd:cd16152   177 YLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHfrtrnAEY-KRSCHESSIRVPLVIYGPG--------- 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 288 qklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPprcpiPSFHvelcreGQNLQKhlqlhDLEEEPDlf 367
Cdd:cd16152   243 ----------------FNGGGRVEELVSLIDLPPTLLDAAGIDVP-----EEMQ------GRSLLP-----LVDGKVE-- 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 368 gnPRELIAYSQyprpadfpqwnsdkpsLNDIKVmGYSIRTVDYRYTVwVGFDPSEFLANFSDIHAGE-LYFVDSDPLQDH 446
Cdd:cd16152   289 --DWRNEVFIQ----------------ISESQV-GRAIRTDRWKYSV-AAPDKDGWKDSGSDVYVEDyLYDLEADPYELV 348

                         250
                  ....*....|....*.
gi 1039796378 447 NVYNDSQHGGLLHSLR 462
Cdd:cd16152   349 NLIGRPEYREVAAELR 364
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 72-333 3.27e-14

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: 74.12  E-value: 3.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  72 TEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPleNITLAPDPHVPDslPPVAYNP-WmdIREREDVQALN 150
Cdd:cd16147   160 ANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFP--NVTAPPRPPPNN--PDVSDKPhW--LRRLPPLNPTQ 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 151 ISVpygpIPEDFQHRCsicsililrQSscesswkehllLLSrgfqlpsevlclfaerkirqsyfasvsyLDTQVGHVLSA 230
Cdd:cd16147   234 IAY----IDELYRKRL---------RT-----------LQS----------------------------VDDLVERLVNT 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 231 LDDLRLAHNTIIAFTSDHGWALGEHG-EWAKYSNFDVATRVPLMLYVPGrtapLPaagqklfpyrdpfdpasdwmdAGRH 309
Cdd:cd16147   262 LEATGQLDNTYIIYTSDNGYHLGQHRlPPGKRTPYEEDIRVPLLVRGPG----IP---------------------AGVT 316

                         250       260
                  ....*....|....*....|....
gi 1039796378 310 TEDLVELVSLFPTLAGLAGLPVPP 333
Cdd:cd16147   317 VDQLVSNIDLAPTILDLAGAPPPS 340
Sulfatase pfam00884
Sulfatase;
205-329 7.56e-14

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 72.07  E-value: 7.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 205 AERKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVA----TRVPLMLYVPGRT 280
Cdd:pfam00884 194 SEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNApeggYRVPLLIWSPGGK 273

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1039796378 281 APlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGL 329
Cdd:pfam00884 274 AK------------------------GQKSEALVSHVDLFPTILDLAGI 298
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 204-333 7.85e-13

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: 69.48  E-value: 7.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 204 FAERKIRQSYFA-SVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHG-----WALGEHGEW--AKYSNFDVATRVPLMLY 275
Cdd:cd16142   172 FEGKSSGKGKYAdSMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFrgEKGTTWEGGVRVPAIVR 251

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796378 276 VPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPP 333
Cdd:cd16142   252 WPGKIKP------------------------GRVSNEIVSHLDWFPTLAALAGAPDPK 285
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 213-333 9.30e-13

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: 69.88  E-value: 9.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 213 YFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwALGEHGEWA---------KYSNFDVATRVPLMLYVPGRTAPl 283
Cdd:cd16144   225 YAAMIESLDESVGRILDALEELGLADNTLVIFTSDNG-GLSTRGGPPtsnaplrggKGSLYEGGIRVPLIVRWPGVIKP- 302

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039796378 284 paagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPP 333
Cdd:cd16144   303 -----------------------GSVSDVPVIGTDLYPTFLELAGGPLPP 329
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 207-334 4.19e-12

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: 67.62  E-value: 4.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 207 RKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwALGEHGEWAKYSNFDVA--------------TRVPL 272
Cdd:cd16145   227 PQPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNG-PHSEGGSEHDPDFFDSNgplrgykrslyeggIRVPF 305

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796378 273 MLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPR 334
Cdd:cd16145   306 IARWPGKIPA------------------------GSVSDHPSAFWDFMPTLADLAGAEPPED 343
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 72-333 6.25e-12

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: 67.41  E-value: 6.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  72 TEEAIRLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdphvpDSLPPVAYNPWMDIRERedvqalni 151
Cdd:cd16156   161 TNRALDFIEKHKDE--DFFLVVSYDEPHHPFLCPKPYASMYK-------------DFEFPKGENAYDDLENK-------- 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 152 svpygpipedfqhrcsicsililrqsscesswKEHLLLLSRGFQLPSEvlclfAERKIR-QSYFASVSYLDTQVGHVLSA 230
Cdd:cd16156   218 --------------------------------PLHQRLWAGAKPHEDG-----DKGTIKhPLYFGCNSFVDYEIGRVLDA 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 231 LDDLrlAHNTIIAFTSDHGWALGEHGEWAK-YSNFDVATRVPLMLYVPGRtapLPAAGQKLFPyrdpfdpasdwmdagrh 309
Cdd:cd16156   261 ADEI--AEDAWVIYTSDHGDMLGAHKLWAKgPAVYDEITNIPLIIRGKGG---EKAGTVTDTP----------------- 318

                         250       260
                  ....*....|....*....|....
gi 1039796378 310 tedlVELVSLFPTLAGLAGLPVPP 333
Cdd:cd16156   319 ----VSHIDLAPTILDYAGIPQPK 338
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
 208-281 2.59e-11

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: 65.70  E-value: 2.59e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796378 208 KIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGE--WAKYSNF-DVATRVPLMLYVPGRTA 281
Cdd:COG3083   424 PFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQnyWGHNSNFsRYQLQVPLVIHWPGTPP 500
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 202-327 4.43e-11

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: 62.82  E-value: 4.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 202 CLFAERKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYS----NFDVATRVPLMLYVP 277
Cdd:cd00016   133 PGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADgkadKSHTGMRVPFIAYGP 212

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039796378 278 GrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLA 327
Cdd:cd00016   213 G-------------------------VKKGGVKHELISQYDIAPTLADLL 237
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 220-332 2.74e-10

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: 61.83  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 220 LDTQVGHVLSALDDLRLAHNTIIAFTSDHG-------WALGEHGEWA-------KYSNFDVATRVPLMLYVPGRTaplpa 285
Cdd:cd16143   210 LDWVVGRILDALKELGLAENTLVIFTSDNGpspyadyKELEKFGHDPsgplrgmKADIYEGGHRVPFIVRWPGKI----- 284

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1039796378 286 agqklfpyrdpfdpasdwmDAGRHTEDLVELVSLFPTLAGLAGLPVP 332
Cdd:cd16143   285 -------------------PAGSVSDQLVSLTDLFATLAAIVGQKLP 312
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
 213-332 7.93e-10

Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.


Pssm-ID: 293778 [Multi-domain]  Cd Length: 521  Bit Score: 60.76  E-value: 7.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 213 YFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWAL------GEHGEW-------AKYSNFDVATRVPLMLYVPGR 279
Cdd:cd16159   281 YGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvgGEYGGGnggiyggKKMGGWEGGIRVPTIVRWPGV 360

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796378 280 TAPlpaaGQKLfpyrdpfDPASDWMDagrhtedlvelvsLFPTLAGLAGLPVP 332
Cdd:cd16159   361 IPP----GSVI-------DEPTSLMD-------------IFPTVAALAGAPLP 389
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
 210-337 1.92e-08

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: 56.02  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 210 RQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwALGEHGEWA--------KYSNFDVATRVPLMLYVPGRTa 281
Cdd:cd16029   219 RRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG-GPTGGGDGGsnyplrggKNTLWEGGVRVPAFVWSPLLP- 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796378 282 plPAAGQKlfpYRDPFDpASDWmdagrhtedlvelvslFPTLAGLAGLPVPPRCPI 337
Cdd:cd16029   297 --PKRGTV---SDGLMH-VTDW----------------LPTLLSLAGGDPDDLPPL 330
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 206-333 5.44e-08

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 55.04  E-value: 5.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 206 ERKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwalGEHGEWAKYSNFDVATRVPLMLYVPGrtaplpa 285
Cdd:COG1368   412 GKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG---PRSPGKTDYENPLERYRVPLLIYSPG------- 481

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796378 286 agqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPP 333
Cdd:COG1368   482 ------------------LKKPKVIDTVGSQIDIAPTLLDLLGIDYPS 511
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
 209-333 8.12e-08

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: 54.01  E-value: 8.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 209 IRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHG-WALG-------EHGEW--------AKYSNFDVATRVPL 272
Cdd:cd16161   181 GRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpWEVKcelavgpGTGDWqgnlggsvAKASTWEGGHREPA 260

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796378 273 MLYVPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPP 333
Cdd:cd16161   261 IVYWPGRIP------------------------ANSTSAALVSTLDIFPTVVALAGASLPP 297
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
 204-332 2.51e-07

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: 52.83  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 204 FAERKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWAL------GEHG--EWAKYSNFDVATRVPLMLY 275
Cdd:cd16158   219 FAGRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGllKCGKGTTYEGGVREPAIAY 298

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796378 276 VPGRTAPlpaagqklfpyrdpfdpasdwmdaGRhTEDLVELVSLFPTLAGLAGLPVP 332
Cdd:cd16158   299 WPGRIKP------------------------GV-THELASTLDILPTIAKLAGAPLP 330
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 204-332 2.51e-07

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: 52.85  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 204 FAERKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWAL-------GEHGEW--AKYSNFDVATRVPLML 274
Cdd:cd16157   217 FLGTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIA 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796378 275 YVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVP 332
Cdd:cd16157   297 WWPGHIKP------------------------GQVSHQLGSLMDLFTTSLALAGLPIP 330
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
 204-328 3.44e-07

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: 52.43  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 204 FAERKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWAL---GEHGEWA-----KYSNFDVATRVPLMLY 275
Cdd:cd16160   215 FKGKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVeycLEGGSTGglkggKGNSWEGGIRVPFIAY 294

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796378 276 VPGRTAPlpaagqklfpyrdpfdpasdwmdagRHTEDLVELVSLFPTLAGLAG 328
Cdd:cd16160   295 WPGTIKP-------------------------RVSHEVVSTMDIFPTFVDLAG 322
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 213-328 5.10e-07

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: 51.14  E-value: 5.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 213 YFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDvATRVPLMLYVPGRTAPlpaagqklfp 292
Cdd:cd16015   194 YLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLD-LYRTPLLIYSPGLKKP---------- 262

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039796378 293 yrdpfdpasdwmdagRHTEDLVELVSLFPTLAGLAG 328
Cdd:cd16015   263 ---------------KKIDRVGSQIDIAPTLLDLLG 283
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
 72-332 2.51e-06

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: 49.36  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378  72 TEEAIRLLEKMKTSASPFFLAVGYHKPHIPFrypkefqklyplenitlapdpHVPDSlppvaynpWMD------------ 139
Cdd:cd16025   122 TDKAIEYIDEQKAPDKPFFLYLAFGAPHAPL---------------------QAPKE--------WIDkykgkydagwda 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 140 IRER--EDVQALNIsvpygpIPEDFQhrcsicsiLILRQSScESSWKEhllllsrgfqLPSEvlclfaERKI---RQSYF 214
Cdd:cd16025   173 LREErlERQKELGL------IPADTK--------LTPRPPG-VPAWDS----------LSPE------EKKLearRMEVY 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 215 AS-VSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwALGEHGeWAKYSNfdvaTrvPLMLYvpgrtaplpaagqKLFPY 293
Cdd:cd16025   222 AAmVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNG-ASAEPG-WANASN----T--PFRLY-------------KQASH 280

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039796378 294 ----RDPF--DPASDWMDAGRHTEDLVELVSLFPTLAGLAGLPVP 332
Cdd:cd16025   281 eggiRTPLivSWPKGIKAKGGIRHQFAHVIDIAPTILELAGVEYP 325
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 215-278 1.84e-04

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


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 42.96  E-value: 1.84e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039796378 215 ASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWA-LGEHGewakYSNFDVATRVPLMLYVPG 278
Cdd:cd16018   183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHG----YDNELPDMRAIFIARGPA 243
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 206-329 1.69e-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: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796378 206 ERKIRQSYFASVSYLDTQVGHVLSALDdlRLAHNTIIAFTSDHGWALGEHGEW--AKYSNFDVATRVPLMLYVPGRTAPL 283
Cdd:cd16017   181 KEELINAYDNSILYTDYVLSQIIERLK--KKDKDAALIYFSDHGESLGENGLYlhGAPYAPKEQYHVPFIIWSSDSYKQR 258

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039796378 284 PAAGQKLFPYRDPFDpaSDWmdagrhtedlvelvsLFPTLAGLAGL 329
Cdd:cd16017   259 YPVERLRANKDRPFS--HDN---------------LFHTLLGLLGI 287
 
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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