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Conserved domains on  [gi|1958809850|ref|XP_038956468|]
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iduronate 2-sulfatase isoform X1 [Rattus norvegicus]

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 ...
1-411 2.83e-139

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: 405.03  E-value: 2.83e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850   1 MSVGKVFHPGISSNhsDDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHTNLLCPVDVADVPEGTLPDKQSTEEAIRLLE 80
Cdd:cd16030    97 AGVGKIFHPGIPDG--DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYPDGKVADEAIEQLR 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  81 KMKTSVSPFFLAVGYHKPHIPFRYPKEFQKLYPLENMTLaPDPHVPDSLPPVAYNPWMDIREREDVQALNISVPYGPIPV 160
Cdd:cd16030   175 KLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPD 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 161 DFQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYSNFDVTTRVPLMFYVPGKTAll 240
Cdd:cd16030   254 EQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTK-- 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 241 paageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPPwcpipsfhvelCREGHNLQRYLQlhdleeD 320
Cdd:cd16030   332 ----------------------PGKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKSLVPLLK------N 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 321 PylfGNPRELIAYSQYPRPAdfpqwnsdkpslkdikVMGYSIRTIDYRYTVWVgfspteflaNFSDIHAGELYFVDSDPL 400
Cdd:cd16030   373 P---SAKWKDAAFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFDKVGAEELYDHKNDPN 424
                         410
                  ....*....|.
gi 1958809850 401 QDHNVYNDSQH 411
Cdd:cd16030   425 EWKNLANDPEY 435
 
Name Accession Description Interval E-value
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
1-411 2.83e-139

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: 405.03  E-value: 2.83e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850   1 MSVGKVFHPGISSNhsDDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHTNLLCPVDVADVPEGTLPDKQSTEEAIRLLE 80
Cdd:cd16030    97 AGVGKIFHPGIPDG--DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYPDGKVADEAIEQLR 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  81 KMKTSVSPFFLAVGYHKPHIPFRYPKEFQKLYPLENMTLaPDPHVPDSLPPVAYNPWMDIREREDVQALNISVPYGPIPV 160
Cdd:cd16030   175 KLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPD 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 161 DFQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYSNFDVTTRVPLMFYVPGKTAll 240
Cdd:cd16030   254 EQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTK-- 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 241 paageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPPwcpipsfhvelCREGHNLQRYLQlhdleeD 320
Cdd:cd16030   332 ----------------------PGKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKSLVPLLK------N 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 321 PylfGNPRELIAYSQYPRPAdfpqwnsdkpslkdikVMGYSIRTIDYRYTVWVgfspteflaNFSDIHAGELYFVDSDPL 400
Cdd:cd16030   373 P---SAKWKDAAFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFDKVGAEELYDHKNDPN 424
                         410
                  ....*....|.
gi 1958809850 401 QDHNVYNDSQH 411
Cdd:cd16030   425 EWKNLANDPEY 435
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
72-408 1.33e-49

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 172.76  E-value: 1.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSVSPFFLAVGYHKPHIPFRYPKEFQKLYPLENMTLapdphvPDSLPPVAYNPWmdireredvqalni 151
Cdd:COG3119   134 TDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPL------PPNLAPRDLTEE-------------- 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 152 svpygpipvdFQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHG-EWAKYSNFDVTTRVPLM 230
Cdd:COG3119   194 ----------ELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGlRGGKGTLYEGGIRVPLI 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 231 FYVPGKTAllpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPPWCpipsfhvelcrEGHNLQR 310
Cdd:COG3119   264 VRWPGKIK------------------------AGSVSDALVSLIDLLPTLLDLAGVPIPEDL-----------DGRSLLP 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 311 YLQLHDLEEDPYLfgnpreliaYSQYPRPAdfpqwnsdkpslkdikvMGYSIRTIDYRYTVWVGFSPTEflanfsdihag 390
Cdd:COG3119   309 LLTGEKAEWRDYL---------YWEYPRGG-----------------GNRAIRTGRWKLIRYYDDDGPW----------- 351
                         330
                  ....*....|....*...
gi 1958809850 391 ELYFVDSDPLQDHNVYND 408
Cdd:COG3119   352 ELYDLKNDPGETNNLAAD 369
PRK13759 PRK13759
arylsulfatase; Provisional
60-290 9.43e-32

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 125.94  E-value: 9.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  60 DVPEGTLPDKQSTEEAIRLLEKmKTSVSPFFLAVGYHKPHIPFRYPKEFQKLYplENmTLAPDPHVPDslppvaynpWmD 139
Cdd:PRK13759  174 DLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMY--KD-ADIPDPHIGD---------W-E 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 140 IREREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYS 219
Cdd:PRK13759  240 YAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGY 319
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958809850 220 NFDVTTRVPLMFYVPGktALLPAageklfpyqdpfdpaselmGAGRRTEDLVELVSLFPTLAGLAGMPVPP 290
Cdd:PRK13759  320 PYEGSAHIPFIIYDPG--GLLAG-------------------NRGTVIDQVVELRDIMPTLLDLAGGTIPD 369
Sulfatase pfam00884
Sulfatase;
68-286 1.29e-14

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 74.00  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  68 DKQSTEEAIRLLEKMKTsvsPFFLAVGYHKPHIPFRYPKEFQKLYPlenmtlapdphvpdslppvaynpwmdireredvq 147
Cdd:pfam00884 144 DEALLDEALEFLDNNDK---PFFLVLHTLGSHGPPYYPDRYPEKYA---------------------------------- 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 148 alnISVPYGpipvDFQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYSNFDVT--- 224
Cdd:pfam00884 187 ---TFKPSS----CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNApeg 259
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958809850 225 -TRVPLMFYVPGKTAllpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGM 286
Cdd:pfam00884 260 gYRVPLLIWSPGGKA------------------------KGQKSEALVSHVDLFPTILDLAGI 298
 
Name Accession Description Interval E-value
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
1-411 2.83e-139

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: 405.03  E-value: 2.83e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850   1 MSVGKVFHPGISSNhsDDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHTNLLCPVDVADVPEGTLPDKQSTEEAIRLLE 80
Cdd:cd16030    97 AGVGKIFHPGIPDG--DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYPDGKVADEAIEQLR 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  81 KMKTSVSPFFLAVGYHKPHIPFRYPKEFQKLYPLENMTLaPDPHVPDSLPPVAYNPWMDIREREDVQALNISVPYGPIPV 160
Cdd:cd16030   175 KLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPD 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 161 DFQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYSNFDVTTRVPLMFYVPGKTAll 240
Cdd:cd16030   254 EQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTK-- 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 241 paageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPPwcpipsfhvelCREGHNLQRYLQlhdleeD 320
Cdd:cd16030   332 ----------------------PGKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKSLVPLLK------N 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 321 PylfGNPRELIAYSQYPRPAdfpqwnsdkpslkdikVMGYSIRTIDYRYTVWVgfspteflaNFSDIHAGELYFVDSDPL 400
Cdd:cd16030   373 P---SAKWKDAAFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFDKVGAEELYDHKNDPN 424
                         410
                  ....*....|.
gi 1958809850 401 QDHNVYNDSQH 411
Cdd:cd16030   425 EWKNLANDPEY 435
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
72-408 1.33e-49

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 172.76  E-value: 1.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSVSPFFLAVGYHKPHIPFRYPKEFQKLYPLENMTLapdphvPDSLPPVAYNPWmdireredvqalni 151
Cdd:COG3119   134 TDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPL------PPNLAPRDLTEE-------------- 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 152 svpygpipvdFQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHG-EWAKYSNFDVTTRVPLM 230
Cdd:COG3119   194 ----------ELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGlRGGKGTLYEGGIRVPLI 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 231 FYVPGKTAllpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPPWCpipsfhvelcrEGHNLQR 310
Cdd:COG3119   264 VRWPGKIK------------------------AGSVSDALVSLIDLLPTLLDLAGVPIPEDL-----------DGRSLLP 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 311 YLQLHDLEEDPYLfgnpreliaYSQYPRPAdfpqwnsdkpslkdikvMGYSIRTIDYRYTVWVGFSPTEflanfsdihag 390
Cdd:COG3119   309 LLTGEKAEWRDYL---------YWEYPRGG-----------------GNRAIRTGRWKLIRYYDDDGPW----------- 351
                         330
                  ....*....|....*...
gi 1958809850 391 ELYFVDSDPLQDHNVYND 408
Cdd:COG3119   352 ELYDLKNDPGETNNLAAD 369
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
72-419 9.51e-36

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: 135.81  E-value: 9.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSVSPFFLAVGYHKPHIPFRYPKEFQKLYPLENMTLAPDPHVPDSLPPVAYNpwmDIREREDVQALNI 151
Cdd:cd16033   133 ADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYR---RERKRWGVDTEDE 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 152 SVpygpipvdfQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAK-YSNFDVTTRVPLM 230
Cdd:cd16033   210 ED---------WKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKgPFMYEETYRIPLI 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 231 FYVPGKTAllpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPpwcpiPSFHvelcreGHNLQr 310
Cdd:cd16033   281 IKWPGVIA------------------------AGQVVDEFVSLLDLAPTILDLAGVDVP-----PKVD------GRSLL- 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 311 ylqlhdleedPYLFGNPRELIaysqypRPADFPQWNSDKPSLkdikvMGYSIRTIDYRYTVwvgfspteflaNFSDIhaG 390
Cdd:cd16033   325 ----------PLLRGEQPEDW------RDEVVTEYNGHEFYL-----PQRMVRTDRYKYVF-----------NGFDI--D 370
                         330       340
                  ....*....|....*....|....*....
gi 1958809850 391 ELYFVDSDPLQDHNVYNDSQHGGLLLSLR 419
Cdd:cd16033   371 ELYDLESDPYELNNLIDDPEYEEILREMR 399
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
72-328 5.59e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 130.38  E-value: 5.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSVSPFFLAVGYHKPHIPFRYPKEFQKLYPLENMTLaPDPHVPdsLPPVAyNPWMDIRereDVQalni 151
Cdd:cd16155   108 ADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPL-PENFLP--QHPFD-NGEGTVR---DEQ---- 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 152 svpYGPIPVDFQ--RKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYSNFDVTTRVPL 229
Cdd:cd16155   177 ---LAPFPRTPEavRQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLMGKQNLYEHSMRVPL 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 230 MFYVPGKTallpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPPWCPIPSF-----------H 298
Cdd:cd16155   254 IISGPGIP-------------------------KGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLlpvirgekkavR 308
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958809850 299 VELC-----------REGHNLQRY------LQLHDLEEDPY----LFGNPR 328
Cdd:cd16155   309 DTLYgayrdgqrairDDRWKLIIYvpgvkrTQLFDLKKDPDelnnLADEPE 359
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
46-399 4.58e-32

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


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 123.81  E-value: 4.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  46 GKLHTNllcpvdVADVPEGTLPDKQSTEEAIRLLEKMKTSVSPFFLAVGYHKPHIPFRYPKEFQKLYplenmtlapdphv 125
Cdd:cd16037    96 GKLHFR------GEDQRHGFRYDRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY------------- 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 126 pdslppvaynpwmdireredvqalnisvpygpipvdfQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDH 205
Cdd:cd16037   157 -------------------------------------VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDH 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 206 GWALGEHGEWAKYSNFDVTTRVPLMFYVPGktallpaageklfpyqdpfdpaselMGAGRRTEDLVELVSLFPTLAGLAG 285
Cdd:cd16037   200 GDMLGERGLWGKSTMYEESVRVPMIISGPG-------------------------IPAGKRVKTPVSLVDLAPTILEAAG 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 286 MPVPPWCPipsfhvelcreGHNLQrylqlhDLEEDPYlfgnPRELIAYSQYprpadfpqwnsdkpSLKDIKVMGYSIRTI 365
Cdd:cd16037   255 APPPPDLD-----------GRSLL------PLAEGPD----DPDRVVFSEY--------------HAHGSPSGAFMLRKG 299
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1958809850 366 DYRYTVWVGFSPteflanfsdihagELYFVDSDP 399
Cdd:cd16037   300 RWKYIYYVGYPP-------------QLFDLENDP 320
PRK13759 PRK13759
arylsulfatase; Provisional
60-290 9.43e-32

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 125.94  E-value: 9.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  60 DVPEGTLPDKQSTEEAIRLLEKmKTSVSPFFLAVGYHKPHIPFRYPKEFQKLYplENmTLAPDPHVPDslppvaynpWmD 139
Cdd:PRK13759  174 DLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMY--KD-ADIPDPHIGD---------W-E 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 140 IREREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYS 219
Cdd:PRK13759  240 YAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGY 319
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958809850 220 NFDVTTRVPLMFYVPGktALLPAageklfpyqdpfdpaselmGAGRRTEDLVELVSLFPTLAGLAGMPVPP 290
Cdd:PRK13759  320 PYEGSAHIPFIIYDPG--GLLAG-------------------NRGTVIDQVVELRDIMPTLLDLAGGTIPD 369
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
57-404 1.28e-30

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: 121.52  E-value: 1.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  57 DVADVPEGTLPDKQsTEEAIRLLEKMKTSVSPFFLAVGYHKPHIPFRY-PKEFQKLYPLENMTLAPDphVPdslppvayn 135
Cdd:cd16034   146 GKRIYIKGYSPDAE-TDLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRPN--VP--------- 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 136 PWMDIRERedvqalnisvpygpipvdFQRKIRQsYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEW 215
Cdd:cd16034   214 EDKKEEAG------------------LREDLRG-YYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 216 AKYSNFDVTTRVPLMFYVPGKtallpaageklfpyqdpfdpaselMGAGRRTEDLVELVSLFPTLAGLAGMPVPPWCpip 295
Cdd:cd16034   275 NKQVPYEESIRVPFIIRYPGK------------------------IKAGRVVDLLINTVDIMPTLLGLCGLPIPDTV--- 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 296 sfhvelcrEGHNLQrylqlhdleedPYLFGNPRELIAYSQYPRPADFPQWNSDKPSLKDIkvmgysIRTIDYRYTVWVGf 375
Cdd:cd16034   328 --------EGRDLS-----------PLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRG------VRTDRYTYVRDKN- 381
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958809850 376 spteflanfsdihaGELYFVD--SDPLQDHN 404
Cdd:cd16034   382 --------------GPWLLFDneKDPYQLNN 398
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
72-419 2.56e-30

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: 121.10  E-value: 2.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSvSPFFLAVGYHKPHIPFRYPKEFQKLYPLENM----TLAPDPHvpDSLPPVAYNPWMDIREREDVQ 147
Cdd:cd16031   149 TDKALDFLKERDKD-KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIpepeTFDDDDY--AGRPEWAREQRNRIRGVLDGR 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 148 ALNisvpygpiPVDFQRKIRQsYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGeWA-KYSNFDVTTR 226
Cdd:cd16031   226 FDT--------PEKYQRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHG-LFdKRLMYEESIR 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 227 VPLMFYVPGKTAllpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPpwcpiPSFHvelcreGH 306
Cdd:cd16031   296 VPLIIRDPRLIK------------------------AGTVVDALVLNIDFAPTILDLAGVPIP-----EDMQ------GR 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 307 NLqryLQLHDLEEDPylfgNPRE--LIAYSQYPRPADFPQWnsdkpslkdikvmgYSIRTIDYRYTVWVGFSPTEflanf 384
Cdd:cd16031   341 SL---LPLLEGEKPV----DWRKefYYEYYEEPNFHNVPTH--------------EGVRTERYKYIYYYGVWDEE----- 394
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1958809850 385 sdihagELYFVDSDPLQDHNVYNDSQHGGLLLSLR 419
Cdd:cd16031   395 ------ELYDLKKDPLELNNLANDPEYAEVLKELR 423
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
88-293 7.21e-30

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: 118.06  E-value: 7.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  88 PFFLAVGYHKPHIPFRYPKEFQKLYplenmtlapdphvpdslppvaynpwmdireredvqalnisvpygpipvdfQRKIR 167
Cdd:cd16032   134 PFFLTVSFTHPHDPYVIPQEYWDLY--------------------------------------------------VRRAR 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 168 QSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYSNFDVTTRVPLMFYVPGKTallpaagekl 247
Cdd:cd16032   164 RAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSFFEGSARVPLIISAPGRF---------- 233
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958809850 248 fpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPPWCP 293
Cdd:cd16032   234 ---------------APRRVAEPVSLVDLLPTLVDLAGGGTAPHVP 264
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
88-419 8.18e-29

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: 116.07  E-value: 8.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  88 PFFLAVGYHKPHIPFRYPKEFQKLYPLENMTLapDPHVPDsLPPVaynpwmdireREDVQAlnisvpygpipvdfqrkir 167
Cdd:cd16027   143 PFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKV--PPYLPD-TPEV----------REDLAD------------------- 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 168 qsYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGehgeWAKYSNFDVTTRVPLMFYVPGKTAllpaagekl 247
Cdd:cd16027   191 --YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP----RAKGTLYDSGLRVPLIVRWPGKIK--------- 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 248 fpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPPWcpipsfhvelcREGHNLQRYLQLHDLEEDPYLFGNp 327
Cdd:cd16027   256 ---------------PGSVSDALVSFIDLAPTLLDLAGIEPPEY-----------LQGRSFLPLLKGEKDPGRDYVFAE- 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 328 RELIAYSQYP-RpadfpqwnsdkpslkdikvmgySIRTIDYRYTVwvgfspteflaNFSDIhagELYFVDSDPLQDHNVY 406
Cdd:cd16027   309 RDRHDETYDPiR----------------------SVRTGRYKYIR-----------NYMPE---ELYDLKNDPDELNNLA 352
                         330
                  ....*....|...
gi 1958809850 407 NDSQHGGLLLSLR 419
Cdd:cd16027   353 DDPEYAEVLEELR 365
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
88-419 1.56e-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: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 110.40  E-value: 1.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  88 PFFLAVGYHKPHIPFRYPKEFQKLYPLEnmtLAPdPHVPDSLPPVAYNPWMDIREREDVQALNisvpygpipVDFQRKIR 167
Cdd:cd16150   133 PFCLYLPLIFPHPPYGVEEPWFSMIDRE---KLP-PRRPPGLRAKGKPSMLEGIEKQGLDRWS---------EERWRELR 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 168 QSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYSN-F-DVTTRVPLMFYVPGKTallpaage 245
Cdd:cd16150   200 ATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNtFeDCLTRVPLIIKPPGGP-------- 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 246 klfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPPwcpiPSFHVELCReghnlqrylQLHDLEEDP--YL 323
Cdd:cd16150   272 -----------------AGGVSDALVELVDIPPTLLDLAGIPLSH----THFGRSLLP---------VLAGETEEHrdAV 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 324 FG----NPRELIAYSQYPRPADFPQWNS---DKPSLKDIKVMgysIRTIDYRYtVWVGFSPTeflanfsdihagELYFVD 396
Cdd:cd16150   322 FSeggrLHGEEQAMEGGHGPYDLKWPRLlqqEEPPEHTKAVM---IRTRRYKY-VYRLYEPD------------ELYDLE 385
                         330       340
                  ....*....|....*....|...
gi 1958809850 397 SDPLQDHNVYNDSQHGGLLLSLR 419
Cdd:cd16150   386 ADPLELHNLIGDPAYAEIIAEMK 408
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
73-292 4.77e-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: 105.21  E-value: 4.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  73 EEAIRLLEKMKTSvSPFFLAVGYHKPHIPFRYpkefqklyplenmtlapdphvpdslppvaynpwmdireredvqalnis 152
Cdd:cd16022   103 DEAIDFIERRDKD-KPFFLYVSFNAPHPPFAY------------------------------------------------ 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 153 vpygpipvdfqrkirqsyFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGE-WAKYSNFDVTTRVPLMF 231
Cdd:cd16022   134 ------------------YAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKKGSLYEGGIRVPFIV 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958809850 232 YVPGKtallpaageklfpyqdpfdpaselMGAGRRTEDLVELVSLFPTLAGLAGMPVPPWC 292
Cdd:cd16022   196 RWPGK------------------------IPAGQVSDALVSLLDLLPTLLDLAGIEPPEGL 232
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
72-408 5.24e-22

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: 97.24  E-value: 5.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSvsPFFLAVGYHKPHIPFRYPKEFQKLYplENMTLAPDphvpdslppvaynpwmdireredvqalni 151
Cdd:cd16146   160 FDEAIDFIEENKDK--PFFAYLATNAPHGPLQVPDKYLDPY--KDMGLDDK----------------------------- 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 152 svpygpipvdfqrkiRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEW------AKYSNFDVTT 225
Cdd:cd16146   207 ---------------LAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRFnagmrgKKGSVYEGGH 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 226 RVPLMFYVPGKTAllpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPPWCPIpsfhvelcrEG 305
Cdd:cd16146   272 RVPFFIRWPGKIL------------------------AGKDVDTLTAHIDLLPTLLDLCGVKLPEGIKL---------DG 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 306 HNLQRYLQlhdLEEDPYlfgNPRELIAYSQYPRPADFPQWNSdkpslkdikvmgySIRTIDYRYTVWVGFSPteflanfs 385
Cdd:cd16146   319 RSLLPLLK---GESDPW---PERTLFTHSGRWPPPPKKKRNA-------------AVRTGRWRLVSPKGFQP-------- 371
                         330       340
                  ....*....|....*....|...
gi 1958809850 386 dihagELYFVDSDPLQDHNVYND 408
Cdd:cd16146   372 -----ELYDIENDPGEENDVADE 389
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
72-313 7.63e-22

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: 96.94  E-value: 7.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSvsPFFLAVGYHKPHIPFRYPKEFQKLYPLENMTL---APDPHVPDSLPPVaYNPWMDIREREDVQA 148
Cdd:cd16028   144 TDRAIEYLDERQDE--PWFLHLSYIRPHPPFVAPAPYHALYDPADVPPpirAESLAAEAAQHPL-LAAFLERIESLSFSP 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 149 LNISVPYGPIPVdfQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYSNFDVTTRVP 228
Cdd:cd16028   221 GAANAADLDDEE--VAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLWGKDGFFDQAYRVP 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 229 LMFYVPGKTAllpaageklfpyqdpfDPASelmgaGRRTEDLVELVSLFPTLAGLAGMPVPPWCpipsfhvelcrEGHNL 308
Cdd:cd16028   299 LIVRDPRREA----------------DATR-----GQVVDAFTESVDVMPTILDWLGGEIPHQC-----------DGRSL 346

                  ....*
gi 1958809850 309 QRYLQ 313
Cdd:cd16028   347 LPLLA 351
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
170-290 3.81e-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: 92.23  E-value: 3.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 170 YFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAK-YSNF-DVTTRVPLMFYVPGKTallpaagekl 247
Cdd:cd16148   165 YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGhGSNLyDEQLHVPLIIRWPGKE---------- 234
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958809850 248 fpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPP 290
Cdd:cd16148   235 ---------------PGKRVDALVSHIDIAPTLLDLLGVEPPD 262
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
68-288 8.48e-20

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: 88.59  E-value: 8.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  68 DKQSTEEAIRLLEKMKTSVSPFFLAVGYHKPHIPFRYPKEFqklyplenmtlapdphvpdslppvaynpwmdiREREDvq 147
Cdd:cd16153   124 ANQSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEF--------------------------------RDRFD-- 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 148 alnisvpygpipvdfqrkirqsYFASVSYLDTQVGHLLSALDDLRLAH---NTIIAFMSDHGWALGEHGEWAKYSNFDVT 224
Cdd:cd16153   170 ----------------------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQGILAKFTFWPQS 227
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958809850 225 TRVPLMFYVPGKTAllpaageklfpyqdpfdpaselMGAGRRTEDLVELVSLFPTLAGLAGMPV 288
Cdd:cd16153   228 HRVPLIVVSSDKLK----------------------APAGKVRHDFVEFVDLAPTLLAAAGVDV 269
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
170-297 3.17e-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: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 83.83  E-value: 3.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 170 YFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAK------YSNFDVTTRVPLMFYVPGKTAllpaa 243
Cdd:cd16149   144 YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKgngtfpLNMYDNSVKVPFIIRWPGVVP----- 218
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958809850 244 geklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVP--PWCPIPSF 297
Cdd:cd16149   219 -------------------AGRVVDSLVSAYDFFPTLLELAGVDPPadPRLPGRSF 255
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
72-322 1.24e-17

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: 84.14  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSVSPFFLAVGYHKPHIPFRYPKEFQKLYPleNMTLAP-----------DPHVPDSLPPvaynPWMDI 140
Cdd:cd16147   160 ANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFP--NVTAPPrpppnnpdvsdKPHWLRRLPP----LNPTQ 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 141 REREDvqalnisvpygpipvDFQRKIRQSyFASVsylDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHG-EWAKYS 219
Cdd:cd16147   234 IAYID---------------ELYRKRLRT-LQSV---DDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRlPPGKRT 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 220 NFDVTTRVPLMFYVPGktallpaageklfpyqdpfdpaselMGAGRRTEDLVELVSLFPTLAGLAGMPVPPW-------- 291
Cdd:cd16147   295 PYEEDIRVPLLVRGPG-------------------------IPAGVTVDQLVSNIDLAPTILDLAGAPPPSDmdgrscgd 349
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958809850 292 CPIPSFH-VELCREGHNLQ------RYLQLHDLEEDPY 322
Cdd:cd16147   350 SNNNTYKcVRTVDDTYNLLyfewctGFRELYDLTTDPY 387
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
55-290 1.34e-16

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: 81.05  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  55 PVDVADVPEGTLPDKQSTEEAIRLLEKMKTSvsPFFLAVGYHKPHIPFRYPKEFQKLYplenmtlapdphvpdslppvay 134
Cdd:cd16144   154 NPDLEDGPEGEYLTDRLTDEAIDFIEQNKDK--PFFLYLSHYAVHTPIQARPELIEKY---------------------- 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 135 npwmdireredvqalnisvpYGPIPVDFQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGwALGEHGE 214
Cdd:cd16144   210 --------------------EKKKKGLRKGQKNPVYAAMIESLDESVGRILDALEELGLADNTLVIFTSDNG-GLSTRGG 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 215 WA---------KYSNFDVTTRVPLMFYVPGKTAllpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAG 285
Cdd:cd16144   269 PPtsnaplrggKGSLYEGGIRVPLIVRWPGVIK------------------------PGSVSDVPVIGTDLYPTFLELAG 324

                  ....*
gi 1958809850 286 MPVPP 290
Cdd:cd16144   325 GPLPP 329
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
68-289 6.97e-16

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: 78.02  E-value: 6.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  68 DKQSTEEAIRLLEKMKTSVS---PFFLAVGYHKPHipfrypkefqklyplenmtlapdphvpdslppvaynpwmdirere 144
Cdd:cd16035   116 DPGIAAQAVEWLRERGAKNAdgkPWFLVVSLVNPH--------------------------------------------- 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 145 DVQalnisvpYGPIPVDFQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYSN-FDV 223
Cdd:cd16035   151 DIM-------FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNaYEE 223
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958809850 224 TTRVPLMFYVPgktallpaageklfpyqdpfdpasELMGAGRRTEDLVELVSLFPTLAGLAGMPVP 289
Cdd:cd16035   224 ALHVPLIISHP------------------------DLFGTGQTTDALTSHIDLLPTLLGLAGVDAE 265
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
112-345 2.00e-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: 77.25  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 112 YPlenMTLAPDPHV--PDSLPpvaynpWMDIRERedvqalnisvpygpipvdfqRKIRQSYF-ASVSYLDTQVGHLLSAL 188
Cdd:cd16151   175 YP---MVLVHDPFVptPDSPD------WDPDDKR--------------------KKDDPEYFpDMVAYMDKLVGKLVDKL 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 189 DDLRLAHNTIIAFMSDHGWALGEHGEW-------AKYSNFDVTTRVPLMFYVPGKTAllpaageklfpyqdpfdpaselm 261
Cdd:cd16151   226 EELGLRENTIIIFTGDNGTHRPITSRTngrevrgGKGKTTDAGTHVPLIVNWPGLIP----------------------- 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 262 gAGRRTEDLVELVSLFPTLAGLAGMPVPPWCPIpsfhvelcrEGHNLqrYLQLH---DLEEDPYLFGNPRELiAYSQYPR 338
Cdd:cd16151   283 -AGGVSDDLVDFSDFLPTLAELAGAPLPEDYPL---------DGRSF--APQLLgktGSPRREWIYWYYRNP-HKKFGSR 349

                  ....*..
gi 1958809850 339 PADFPQW 345
Cdd:cd16151   350 FVRTKRY 356
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
72-290 2.80e-15

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: 77.42  E-value: 2.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSvsPFFLAVGYHKPHIPFRYPKEFQKLYplENMTLAPDPHVPDSLP--PVAYNPWMDIREREDVQAL 149
Cdd:cd16156   161 TNRALDFIEKHKDE--DFFLVVSYDEPHHPFLCPKPYASMY--KDFEFPKGENAYDDLEnkPLHQRLWAGAKPHEDGDKG 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 150 NISVPYgpipvdfqrkirqsYFASVSYLDTQVGHLLSALDDLrlAHNTIIAFMSDHGWALGEHGEWAK-YSNFDVTTRVP 228
Cdd:cd16156   237 TIKHPL--------------YFGCNSFVDYEIGRVLDAADEI--AEDAWVIYTSDHGDMLGAHKLWAKgPAVYDEITNIP 300
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958809850 229 LMFYVPGKtallpaaGEKLFPYQDPfdpaselmgagrrtedlVELVSLFPTLAGLAGMPVPP 290
Cdd:cd16156   301 LIIRGKGG-------EKAGTVTDTP-----------------VSHIDLAPTILDYAGIPQPK 338
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
72-419 5.14e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 76.11  E-value: 5.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKmKTSVSPFFLAVGYHKPHIP---FRY--PKEFQKLYPlenmtlapDPHVPdslppvaynpwmdirerEDV 146
Cdd:cd16152   110 TDFAIDYLDN-RQKDKPFFLFLSYLEPHHQndrDRYvaPEGSAERFA--------NFWVP-----------------PDL 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 147 QALnisvpygpiPVDFQRKIrQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHgwalGEH-----GEWaKYSNF 221
Cdd:cd16152   164 AAL---------PGDWAEEL-PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHfrtrnAEY-KRSCH 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 222 DVTTRVPLMFYVPGktallpaageklfpyqdpFDpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPpwcpiPSFHvel 301
Cdd:cd16152   229 ESSIRVPLVIYGPG------------------FN-------GGGRVEELVSLIDLPPTLLDAAGIDVP-----EEMQ--- 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 302 creGHNLQRYLQLHDleedpylfgNPRELIAYSQyprpadfpqwnsdkpslkdIK--VMGYSIRTIDYRYTVwvgFSPTE 379
Cdd:cd16152   276 ---GRSLLPLVDGKV---------EDWRNEVFIQ-------------------ISesQVGRAIRTDRWKYSV---AAPDK 321
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1958809850 380 --FLANFSDIHAGE-LYFVDSDPLQDHNVYNDSQHGGLLLSLR 419
Cdd:cd16152   322 dgWKDSGSDVYVEDyLYDLEADPYELVNLIGRPEYREVAAELR 364
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
72-289 5.79e-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: 293764 [Multi-domain]  Cd Length: 415  Bit Score: 76.09  E-value: 5.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSvsPFFLAVGYHKPHIPFRYPKefqklyplenmtLAPDPHVPDSLPPVAYNPWmdireredvqalni 151
Cdd:cd16145   175 TDEALDFIRENKDK--PFFLYLAYTLPHAPLQVPD------------DGPYKYKPKDPGIYAYLPW-------------- 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 152 svpygpipvdfqRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGwALGEHGEWAKYSNFDVT------- 224
Cdd:cd16145   227 ------------PQPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNG-PHSEGGSEHDPDFFDSNgplrgyk 293
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958809850 225 -------TRVPLMFYVPGKTAllpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVP 289
Cdd:cd16145   294 rslyeggIRVPFIARWPGKIP------------------------AGSVSDHPSAFWDFMPTLADLAGAEPP 341
Sulfatase pfam00884
Sulfatase;
68-286 1.29e-14

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 74.00  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  68 DKQSTEEAIRLLEKMKTsvsPFFLAVGYHKPHIPFRYPKEFQKLYPlenmtlapdphvpdslppvaynpwmdireredvq 147
Cdd:pfam00884 144 DEALLDEALEFLDNNDK---PFFLVLHTLGSHGPPYYPDRYPEKYA---------------------------------- 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 148 alnISVPYGpipvDFQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYSNFDVT--- 224
Cdd:pfam00884 187 ---TFKPSS----CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNApeg 259
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958809850 225 -TRVPLMFYVPGKTAllpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGM 286
Cdd:pfam00884 260 gYRVPLLIWSPGGKA------------------------KGQKSEALVSHVDLFPTILDLAGI 298
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
72-289 2.71e-13

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: 71.06  E-value: 2.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSvsPFFLAVGYHKPHIPFRYPKEFQKlyplenmtlapdphvpdslppvaynpwmdireredvqalni 151
Cdd:cd16026   170 TDEAVDFIERNKDQ--PFFLYLAHTMPHVPLFASEKFKG----------------------------------------- 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 152 svpygpipvdfqRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEW--------AKYSNFDV 223
Cdd:cd16026   207 ------------RSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLEYGGHGgsagplrgGKGTTWEG 274
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958809850 224 TTRVPLMFYVPGKTAllpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVP 289
Cdd:cd16026   275 GVRVPFIAWWPGVIP------------------------AGTVSDELASTMDLLPTLAALAGAPLP 316
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
164-290 3.65e-13

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: 70.26  E-value: 3.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 164 RKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYSNFDVTTRVPLMFYVPGktallpaa 243
Cdd:cd16171   192 RNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMYEGSSHVPLLIMGPG-------- 263
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958809850 244 geklfpyqdpfdpaselMGAGRRTEDLVELVSLFPTLAGLAGMPVPP 290
Cdd:cd16171   264 -----------------IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
72-294 1.05e-11

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: 66.03  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSvSPFFLAVGYHKPHIPFRYPKEFQKLYPlenmtlAPDPHVPDslppvaynpwmdireredvqalni 151
Cdd:cd16029   168 TDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYE------DKFAHIKD------------------------ 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 152 svpygpipvdfqrKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGwALGEHGEWA--------KYSNFDV 223
Cdd:cd16029   217 -------------EDRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG-GPTGGGDGGsnyplrggKNTLWEG 282
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958809850 224 TTRVPLMFYVPgktaLLPAAgeklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPPWCPI 294
Cdd:cd16029   283 GVRVPAFVWSP----LLPPK-------------------RGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPL 330
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
170-290 4.13e-11

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: 64.09  E-value: 4.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 170 YFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHG-----WALGEHGEW--AKYSNFDVTTRVPLMFYVPGKTAllpa 242
Cdd:cd16142   182 YADSMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFrgEKGTTWEGGVRVPAIVRWPGKIK---- 257
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958809850 243 ageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPP 290
Cdd:cd16142   258 --------------------PGRVSNEIVSHLDWFPTLAALAGAPDPK 285
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
167-284 5.43e-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: 62.44  E-value: 5.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 167 RQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYS----NFDVTTRVPLMFYVPGktallpa 242
Cdd:cd00016   141 TPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADgkadKSHTGMRVPFIAYGPG------- 213
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958809850 243 ageklfpyqdpfdpaselMGAGRRTEDLVELVSLFPTLAGLA 284
Cdd:cd00016   214 ------------------VKKGGVKHELISQYDIAPTLADLL 237
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
72-289 1.85e-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: 62.22  E-value: 1.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSVSPFFLAVGYHKPHIPFRYPKEFQKLYpleNMTlapdphvpdslppvaynpwmdireredvqalni 151
Cdd:cd16143   158 TDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQGKS---GAG--------------------------------- 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 152 svPYGpipvDFqrkIRQsyfasvsyLDTQVGHLLSALDDLRLAHNTIIAFMSDHG-------WALGEHGEWA-------K 217
Cdd:cd16143   202 --PYG----DF---VYE--------LDWVVGRILDALKELGLAENTLVIFTSDNGpspyadyKELEKFGHDPsgplrgmK 264
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958809850 218 YSNFDVTTRVPLMFYVPGKTallpaageklfpyqdpfdpaselmGAGRRTEDLVELVSLFPTLAGLAGMPVP 289
Cdd:cd16143   265 ADIYEGGHRVPFIVRWPGKI------------------------PAGSVSDQLVSLTDLFATLAAIVGQKLP 312
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
68-238 2.34e-10

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: 62.23  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  68 DKQSTEEAIRLLEKMKTSvSPFFLAVGYHKPHIPFRYPKEFQKLYPLENMTLAPDPHVPDSLPpvaynpwmdireredvq 147
Cdd:COG3083   363 DRQITAQWLQWLDQRDSD-RPWFSYLFLDAPHAYSFPADYPKPFQPSEDCNYLALDNESDPTP----------------- 424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 148 alnisvpygpipvdfqrkIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGE--WAKYSNF-DVT 224
Cdd:COG3083   425 ------------------FKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQnyWGHNSNFsRYQ 486
                         170
                  ....*....|....
gi 1958809850 225 TRVPLMFYVPGKTA 238
Cdd:COG3083   487 LQVPLVIHWPGTPP 500
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
72-220 1.28e-09

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: 59.76  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  72 TEEAIRLLEKMKTSVSPFFLAVGYHKPHIPFRYPKEF----------------------QK---LYPlENMTLAPDPH-V 125
Cdd:cd16025   122 TDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkykgkydagwdalreerlerQKelgLIP-ADTKLTPRPPgV 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 126 P--DSLPPvaynpwmdirEREDVQALNISVpygpipvdfqrkirqsYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMS 203
Cdd:cd16025   201 PawDSLSP----------EEKKLEARRMEV----------------YAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLS 254
                         170
                  ....*....|....*..
gi 1958809850 204 DHGwALGEHGeWAKYSN 220
Cdd:cd16025   255 DNG-ASAEPG-WANASN 269
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
66-291 1.81e-08

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 56.20  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  66 LPDKQSTEEAIRLLEKMKtsvSPFFLAV----GyhkpHIPFRYPKEFQKLYPLENMTLapdphvpdslppvaynpwmdir 141
Cdd:COG1368   366 VSDEDLFDKALEELEKLK---KPFFAFLitlsN----HGPYTLPEEDKKIPDYGKTTL---------------------- 416
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 142 eredvqalnisvpygpipvdfqrkirQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDH-GWALGEHGEWAKYSN 220
Cdd:COG1368   417 --------------------------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHgPRSPGKTDYENPLER 470
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958809850 221 FdvttRVPLMFYVPGktallpaageklfpyqdpfdpaselMGAGRRTEDLVELVSLFPTLAGLAGMPVPPW 291
Cdd:COG1368   471 Y----RVPLLIYSPG-------------------------LKKPKVIDTVGSQIDIAPTLLDLLGIDYPSY 512
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
170-289 5.05e-08

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: 54.99  E-value: 5.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 170 YFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWAL------GEHGEW-------AKYSNFDVTTRVPLMFYVPGK 236
Cdd:cd16159   281 YGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvgGEYGGGnggiyggKKMGGWEGGIRVPTIVRWPGV 360
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958809850 237 talLPAAGEklfpyqdpFDPASELMgagrrtedlvelvSLFPTLAGLAGMPVP 289
Cdd:cd16159   361 ---IPPGSV--------IDEPTSLM-------------DIFPTVAALAGAPLP 389
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
157-285 5.22e-08

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: 53.84  E-value: 5.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 157 PIPVDFQRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHGEWAKYSNFDVtTRVPLMFYVPGK 236
Cdd:cd16015   181 PLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDL-YRTPLLIYSPGL 259
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958809850 237 TallpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAG 285
Cdd:cd16015   260 K-------------------------KPKKIDRVGSQIDIAPTLLDLLG 283
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
167-289 3.59e-06

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: 48.97  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 167 RQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWAL---GEHGEWA-----KYSNFDVTTRVPLMFYVPGKTa 238
Cdd:cd16160   221 RGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVeycLEGGSTGglkggKGNSWEGGIRVPFIAYWPGTI- 299
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958809850 239 llpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVP 289
Cdd:cd16160   300 ------------------------KPRVSHEVVSTMDIFPTFVDLAGGTLP 326
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
166-290 1.06e-05

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: 47.46  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 166 IRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHG-WALG-------EHGEW--------AKYSNFDVTTRVPL 229
Cdd:cd16161   181 GRGPYGDALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpWEVKcelavgpGTGDWqgnlggsvAKASTWEGGHREPA 260
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958809850 230 MFYVPGKTAllpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVPP 290
Cdd:cd16161   261 IVYWPGRIP------------------------ANSTSAALVSTLDIFPTVVALAGASLPP 297
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
167-289 8.67e-05

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: 44.77  E-value: 8.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 167 RQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWAL-------GEHGEW--AKYSNFDVTTRVPLMFYVPGKT 237
Cdd:cd16157   223 RGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPGHI 302
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958809850 238 AllpaageklfpyqdpfdpaselmgAGRRTEDLVELVSLFPTLAGLAGMPVP 289
Cdd:cd16157   303 K------------------------PGQVSHQLGSLMDLFTTSLALAGLPIP 330
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
172-235 1.21e-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: 43.34  E-value: 1.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958809850 172 ASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWA-LGEHGewakYSNFDVTTRVPLMFYVPG 235
Cdd:cd16018   183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHG----YDNELPDMRAIFIARGPA 243
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
99-286 3.56e-04

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: 42.23  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850  99 HIPF--RYPKEFQKLYPlenmtlapdphvpdslppvaynpwmdireredvqalnisVPYGPIPVDFQRKIRQSYFASVSY 176
Cdd:cd16017   154 HGPYydRYPEEFAKFTP---------------------------------------DCDNELQSCSKEELINAYDNSILY 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 177 LDTQVGHLLSALDdlRLAHNTIIAFMSDHGWALGEHGEW--AKYSNFDVTTRVPLMFYVPGKTALLPAAGEKLFPYQDPF 254
Cdd:cd16017   195 TDYVLSQIIERLK--KKDKDAALIYFSDHGESLGENGLYlhGAPYAPKEQYHVPFIIWSSDSYKQRYPVERLRANKDRPF 272
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958809850 255 dpaselmgagrRTEDlvelvsLFPTLAGLAGM 286
Cdd:cd16017   273 -----------SHDN------LFHTLLGLLGI 287
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
164-289 8.27e-04

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: 41.66  E-value: 8.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958809850 164 RKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWAL------GEHG--EWAKYSNFDVTTRVPLMFYVPG 235
Cdd:cd16158   222 RSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGllKCGKGTTYEGGVREPAIAYWPG 301
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958809850 236 KtallpaageklfpyqdpFDPAselmgagrRTEDLVELVSLFPTLAGLAGMPVP 289
Cdd:cd16158   302 R-----------------IKPG--------VTHELASTLDILPTIAKLAGAPLP 330
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
163-213 8.20e-03

Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441797 [Multi-domain]  Cd Length: 537  Bit Score: 38.30  E-value: 8.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958809850 163 QRKIRQSYFASVSYLDTQVGHLLSALDDLRLAHNTIIAFMSDHGWALGEHG 213
Cdd:COG2194   407 REELVNAYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENG 457
 
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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