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Conserved domains on  [gi|341941059|sp|Q08890|]
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RecName: Full=Iduronate 2-sulfatase; AltName: Full=Alpha-L-iduronate sulfate sulfatase; Flags: Precursor

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 ...
40-543 0e+00

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: 598.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNFS 119
Cdd:cd16030    4 NVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPDAV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 120 TIPQYFKENGYVTMSVGKVFHPGISSNhsDDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHANLLCPVDVADVPEGTLP 199
Cdd:cd16030   84 TLPQYFKENGYTTAGVGKIFHPGIPDG--DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 200 DKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPDSLPPVAYNPWMDIREREDVQ 279
Cdd:cd16030  162 DGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 280 ALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRV 359
Cdd:cd16030  241 ALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 360 PLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPrcpipsfhvelCREGQN 439
Cdd:cd16030  321 PLIIRAPGVTKP------------------------GKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKS 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 440 LQKHLQlhdleeEPDLFGNPReliAYSQYPRPAdfpqwnsdkpslndikVMGYSIRTVDYRYTVWVgfdpseflaNFSDI 519
Cdd:cd16030  366 LVPLLK------NPSAKWKDA---AFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFDKV 411
                        490       500
                 ....*....|....*....|....
gi 341941059 520 HAGELYFVDSDPLQDHNVYNDSQH 543
Cdd:cd16030  412 GAEELYDHKNDPNEWKNLANDPEY 435
 
Name Accession Description Interval E-value
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
40-543 0e+00

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: 598.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNFS 119
Cdd:cd16030    4 NVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPDAV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 120 TIPQYFKENGYVTMSVGKVFHPGISSNhsDDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHANLLCPVDVADVPEGTLP 199
Cdd:cd16030   84 TLPQYFKENGYTTAGVGKIFHPGIPDG--DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 200 DKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPDSLPPVAYNPWMDIREREDVQ 279
Cdd:cd16030  162 DGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 280 ALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRV 359
Cdd:cd16030  241 ALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 360 PLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPrcpipsfhvelCREGQN 439
Cdd:cd16030  321 PLIIRAPGVTKP------------------------GKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKS 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 440 LQKHLQlhdleeEPDLFGNPReliAYSQYPRPAdfpqwnsdkpslndikVMGYSIRTVDYRYTVWVgfdpseflaNFSDI 519
Cdd:cd16030  366 LVPLLK------NPSAKWKDA---AFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFDKV 411
                        490       500
                 ....*....|....*....|....
gi 341941059 520 HAGELYFVDSDPLQDHNVYNDSQH 543
Cdd:cd16030  412 GAEELYDHKNDPNEWKNLANDPEY 435
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
22-540 1.82e-92

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 288.32  E-value: 1.82e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  22 FCIALESAAQGNSATDALNILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPD 100
Cdd:COG3119    7 LLLALLAAAAAAAAAKRPNILFILADDLGYGdLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 101 TTRLYDFNSYWRVH-SGNFSTIPQYFKENGYVTMSVGKVFHpgissnHSDDYpyswsfppyhpssekyentktckgqdgk 179
Cdd:COG3119   87 RTGVTDNGEGYNGGlPPDEPTLAELLKEAGYRTALFGKWHL------YLTDL---------------------------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 180 lhanllcpvdvadvpegtlpdkqSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapdphvpd 259
Cdd:COG3119  133 -----------------------LTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPL-------- 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 260 slpPVAYNPWmdireredvqalnisvpygPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGW 339
Cdd:COG3119  182 ---PPNLAPR-------------------DLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGP 239
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 340 ALGEHG-EWAKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGL 418
Cdd:COG3119  240 SLGEHGlRGGKGTLYEGGIRVPLIVRWPGKIKA------------------------GSVSDALVSLIDLLPTLLDLAGV 295
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 419 PVPPRCpipsfhvelcrEGQNLQKHLQlhdlEEEPDlfgnPRELIaYSQYPRPAdfpqwnsdkpslndikvMGYSIRTVD 498
Cdd:COG3119  296 PIPEDL-----------DGRSLLPLLT----GEKAE----WRDYL-YWEYPRGG-----------------GNRAIRTGR 338
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 341941059 499 YRYTVWVGFDPSEflanfsdihagELYFVDSDPLQDHNVYND 540
Cdd:COG3119  339 WKLIRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
PRK13759 PRK13759
arylsulfatase; Provisional
40-422 1.68e-54

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 191.42  E-value: 1.68e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTT-RLydfnSYWRVHSGN 117
Cdd:PRK13759   8 NIILIMVDQMRgDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHgRV----GYGDVVPWN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 118 FS-TIPQYFKENGYVTMSVGKV-FHP-----GISSNHSDDyPYSWSFPPYHPSSEKY--ENTKTCKGQDGKLHANLL--- 185
Cdd:PRK13759  84 YKnTLPQEFRDAGYYTQCIGKMhVFPqrnllGFHNVLLHD-GYLHSGRNEDKSQFDFvsDYLAWLREKAPGKDPDLTdig 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 186 --CPVDVA---DVPEGTLPDKQSTEEAIRLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlaPDPHVPDs 260
Cdd:PRK13759 163 wdCNSWVArpwDLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADI---PDPHIGD- 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 261 lppvaynpWmDIREREDVQALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWA 340
Cdd:PRK13759 238 --------W-EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDM 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 341 LGEHGEWAKYSNFDVATRVPLMLYVPGRTAPLPaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPV 420
Cdd:PRK13759 309 LGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGN---------------------RGTVIDQVVELRDIMPTLLDLAGGTI 367

                 ..
gi 341941059 421 PP 422
Cdd:PRK13759 368 PD 369
Sulfatase pfam00884
Sulfatase;
40-418 6.64e-37

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 138.71  E-value: 6.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059   40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNsywRVHSGN- 117
Cdd:pfam00884   2 NVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVST---PVGLPRt 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  118 FSTIPQYFKENGYVTMSVGKvFHPGISSNHSDDYPYSWSFPPYHPSSEKYENTKTCKGQDgklhanllcpvdvadvPEGT 197
Cdd:pfam00884  79 EPSLPDLLKRAGYNTGAIGK-WHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNC----------------SGGG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  198 LPDKQSTEEAIRLLEKmktSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdphvpdslppvaynpwmdirered 277
Cdd:pfam00884 142 VSDEALLDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKYA-------------------------------- 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  278 vqalnISVPYGpipeDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVA- 356
Cdd:pfam00884 187 -----TFKPSS----CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNAp 257
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341941059  357 ---TRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGL 418
Cdd:pfam00884 258 eggYRVPLLIWSPGGKAK------------------------GQKSEALVSHVDLFPTILDLAGI 298
 
Name Accession Description Interval E-value
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
40-543 0e+00

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: 598.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNFS 119
Cdd:cd16030    4 NVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPDAV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 120 TIPQYFKENGYVTMSVGKVFHPGISSNhsDDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHANLLCPVDVADVPEGTLP 199
Cdd:cd16030   84 TLPQYFKENGYTTAGVGKIFHPGIPDG--DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 200 DKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPDSLPPVAYNPWMDIREREDVQ 279
Cdd:cd16030  162 DGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 280 ALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATRV 359
Cdd:cd16030  241 ALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 360 PLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPrcpipsfhvelCREGQN 439
Cdd:cd16030  321 PLIIRAPGVTKP------------------------GKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKS 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 440 LQKHLQlhdleeEPDLFGNPReliAYSQYPRPAdfpqwnsdkpslndikVMGYSIRTVDYRYTVWVgfdpseflaNFSDI 519
Cdd:cd16030  366 LVPLLK------NPSAKWKDA---AFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFDKV 411
                        490       500
                 ....*....|....*....|....
gi 341941059 520 HAGELYFVDSDPLQDHNVYNDSQH 543
Cdd:cd16030  412 GAEELYDHKNDPNEWKNLANDPEY 435
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
22-540 1.82e-92

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 288.32  E-value: 1.82e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  22 FCIALESAAQGNSATDALNILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPD 100
Cdd:COG3119    7 LLLALLAAAAAAAAAKRPNILFILADDLGYGdLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 101 TTRLYDFNSYWRVH-SGNFSTIPQYFKENGYVTMSVGKVFHpgissnHSDDYpyswsfppyhpssekyentktckgqdgk 179
Cdd:COG3119   87 RTGVTDNGEGYNGGlPPDEPTLAELLKEAGYRTALFGKWHL------YLTDL---------------------------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 180 lhanllcpvdvadvpegtlpdkqSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapdphvpd 259
Cdd:COG3119  133 -----------------------LTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPL-------- 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 260 slpPVAYNPWmdireredvqalnisvpygPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGW 339
Cdd:COG3119  182 ---PPNLAPR-------------------DLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGP 239
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 340 ALGEHG-EWAKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGL 418
Cdd:COG3119  240 SLGEHGlRGGKGTLYEGGIRVPLIVRWPGKIKA------------------------GSVSDALVSLIDLLPTLLDLAGV 295
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 419 PVPPRCpipsfhvelcrEGQNLQKHLQlhdlEEEPDlfgnPRELIaYSQYPRPAdfpqwnsdkpslndikvMGYSIRTVD 498
Cdd:COG3119  296 PIPEDL-----------DGRSLLPLLT----GEKAE----WRDYL-YWEYPRGG-----------------GNRAIRTGR 338
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 341941059 499 YRYTVWVGFDPSEflanfsdihagELYFVDSDPLQDHNVYND 540
Cdd:COG3119  339 WKLIRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
40-551 1.18e-66

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: 220.46  E-value: 1.18e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNFS 119
Cdd:cd16027    2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFPLPDGVK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 120 TIPQYFKENGYVTMSVGKVFHPGissnhsdDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHANllcpvdvadvpegtlP 199
Cdd:cd16027   82 TLPELLREAGYYTGLIGKTHYNP-------DAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRA---------------K 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 200 DKQsteeairllekmktsasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapDPHVPDsLPPVaynpwmdireREDVQ 279
Cdd:cd16027  140 KGQ-----------------PFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKV--PPYLPD-TPEV----------REDLA 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 280 AlnisvpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGehgeWAKYSNFDVATRV 359
Cdd:cd16027  190 D---------------------YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP----RAKGTLYDSGLRV 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 360 PLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPrcpipsfhvELcrEGQN 439
Cdd:cd16027  245 PLIVRWPGKIKP------------------------GSVSDALVSFIDLAPTLLDLAGIEPPE---------YL--QGRS 289
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 440 LqkhlqLHDLEEEPDlfgNPRELIaYSQYPRpadfpqwnsdkpslNDIKVMGY-SIRTVDYRYTVwvgfdpseflaNFSD 518
Cdd:cd16027  290 F-----LPLLKGEKD---PGRDYV-FAERDR--------------HDETYDPIrSVRTGRYKYIR-----------NYMP 335
                        490       500       510
                 ....*....|....*....|....*....|...
gi 341941059 519 IhagELYFVDSDPLQDHNVYNDSQHGGLLHSLR 551
Cdd:cd16027  336 E---ELYDLKNDPDELNNLADDPEYAEVLEELR 365
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-551 6.48e-63

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: 212.08  E-value: 6.48e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY----DFNSYWRVH 114
Cdd:cd16033    2 NILFIMTDQQRyDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLnnveNAGAYSRGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 115 SGNFSTIPQYFKENGYVTMSVGKvFHPGISSNhsddyPYSWSFPPYHPssekYENTKtckgqdgklhanllcpvdvadvp 194
Cdd:cd16033   82 PPGVETFSEDLREAGYRNGYVGK-WHVGPEET-----PLDYGFDEYLP----VETTI----------------------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 195 EGTLpdkqsTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPHVPDSLPPVAYNpwmDIRE 274
Cdd:cd16033  129 EYFL-----ADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYR---RERK 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 275 REDVQALNisvpygpipEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK-YSNF 353
Cdd:cd16033  201 RWGVDTED---------EEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKgPFMY 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 354 DVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPRCpipsfhvel 433
Cdd:cd16033  272 EETYRIPLIIKWPGVIAA------------------------GQVVDEFVSLLDLAPTILDLAGVDVPPKV--------- 318
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 434 crEGQNLQKHLqlhdLEEEPDlfgNPRELIaysqyprpadFPQWNSdkpslNDIKVMGYSIRTVDYRYtVWVGFDpsefl 513
Cdd:cd16033  319 --DGRSLLPLL----RGEQPE---DWRDEV----------VTEYNG-----HEFYLPQRMVRTDRYKY-VFNGFD----- 368
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 341941059 514 anfsdihAGELYFVDSDPLQDHNVYNDSQHGGLLHSLR 551
Cdd:cd16033  369 -------IDELYDLESDPYELNNLIDDPEYEEILREMR 399
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
40-551 6.55e-63

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: 212.39  E-value: 6.55e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNf 118
Cdd:cd16031    4 NIIFILTDDHRyDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLFDASQP- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 119 sTIPQYFKENGYVTMSVGKvFHPGISSNHSD---DYPYSWS-----FPPYHPSSEKYentktcKGQDGklHANLLCpvdv 190
Cdd:cd16031   83 -TYPKLLRKAGYQTAFIGK-WHLGSGGDLPPpgfDYWVSFPgqgsyYDPEFIENGKR------VGQKG--YVTDII---- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 191 advpegtlpdkqsTEEAIRLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPLENI----TLAPDPHvpDSLPPVAY 266
Cdd:cd16031  149 -------------TDKALDFLKERDKD-KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIpepeTFDDDDY--AGRPEWAR 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 267 NPWMDIREREDVQALNisvpygpiPEDFQRKIRQsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGe 346
Cdd:cd16031  213 EQRNRIRGVLDGRFDT--------PEKYQRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHG- 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 347 WA-KYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVPPRCp 425
Cdd:cd16031  283 LFdKRLMYEESIRVPLIIRDPRLIKA------------------------GTVVDALVLNIDFAPTILDLAGVPIPEDM- 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 426 ipsfhvelcrEGQNLQKHLQLHDLEEEPDLFgnpreLIAYSQYPRPADFPQWnsdkpslndikvmgYSIRTVDYRYTVWV 505
Cdd:cd16031  338 ----------QGRSLLPLLEGEKPVDWRKEF-----YYEYYEEPNFHNVPTH--------------EGVRTERYKYIYYY 388
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 341941059 506 GFDPSEflanfsdihagELYFVDSDPLQDHNVYNDSQHGGLLHSLR 551
Cdd:cd16031  389 GVWDEE-----------ELYDLKKDPLELNNLANDPEYAEVLKELR 423
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
40-421 6.26e-59

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: 195.73  E-value: 6.26e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNF 118
Cdd:cd16022    2 NILLIMTDDLGYDdLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPPDE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 119 STIPQYFKENGYVTMSVGKvfhpgissNHsddypyswsfppyhpssekyentktckgqdgklhanllcpvdvadvpegtl 198
Cdd:cd16022   82 PTLAELLKEAGYRTALIGK--------WH--------------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 199 pdkqstEEAIRLLEKMKTSAsPFFLAVGYHKPHIPFRypkefqklyplenitlapdphvpdslppvaynpwmdireredv 278
Cdd:cd16022  103 ------DEAIDFIERRDKDK-PFFLYVSFNAPHPPFA------------------------------------------- 132
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 279 qalnisvpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGE-WAKYSNFDVAT 357
Cdd:cd16022  133 -----------------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKKGSLYEGGI 189
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341941059 358 RVPLMLYVPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVP 421
Cdd:cd16022  190 RVPFIVRWPGKIP------------------------AGQVSDALVSLLDLLPTLLDLAGIEPP 229
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-536 1.00e-58

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: 200.49  E-value: 1.00e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSywRVHSGNF 118
Cdd:cd16034    3 NILFIFADQHRaQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFG-ND--VPLPPDA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 119 STIPQYFKENGYVTMSVGKvFHpgISSNHSDDYPYSWSFPP-----------------YHPSSEKYENTktckgqdgklh 181
Cdd:cd16034   80 PTIADVLKDAGYRTGYIGK-WH--LDGPERNDGRADDYTPPperrhgfdywkgyecnhDHNNPHYYDDD----------- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 182 anllcpvDVADVPEGTLPDKQsTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRY-PKEFQKLYPLENITLAPDphvpds 260
Cdd:cd16034  146 -------GKRIYIKGYSPDAE-TDLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRPN------ 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 261 lppvaynpwmdireredvqalnisVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWA 340
Cdd:cd16034  212 ------------------------VPEDKKEEAGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDM 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 341 LGEHGEWAKYSNFDVATRVPLMLYVPGRtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPV 420
Cdd:cd16034  268 LGSHGLMNKQVPYEESIRVPFIIRYPGK------------------------IKAGRVVDLLINTVDIMPTLLGLCGLPI 323
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 421 PPrcpipsfhvelCREGQNLQKHLqlhdLEEEPDLFGNpreliAYSQYPRPadFPQWNSDKPSLNDIkvmgysIRTVDYR 500
Cdd:cd16034  324 PD-----------TVEGRDLSPLL----LGGKDDEPDS-----VLLQCFVP--FGGGSARDGGEWRG------VRTDRYT 375
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 341941059 501 YTVWVGfdpseflanfsdihaGELYFVD--SDPLQDHN 536
Cdd:cd16034  376 YVRDKN---------------GPWLLFDneKDPYQLNN 398
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-531 1.08e-58

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: 197.77  E-value: 1.08e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWrvhSGNF 118
Cdd:cd16037    2 NILIIMSDEHNPDaMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPY---DGDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 119 STIPQYFKENGYVTMSVGKVFHPGISSNHSDDYpyswsfppyhpssekyentktckgqdgklhanllcpvdvadvpegtl 198
Cdd:cd16037   79 PSWGHALRAAGYETVLIGKLHFRGEDQRHGFRY----------------------------------------------- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 199 pDKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdphvpdslppvaynpwmdireredv 278
Cdd:cd16037  112 -DRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY---------------------------------- 156
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 279 qalnisvpygpipedfQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVATR 358
Cdd:cd16037  157 ----------------VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMYEESVR 220
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 359 VPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPRCPipsfhvelcreGQ 438
Cdd:cd16037  221 VPMIISGPGIP-------------------------AGKRVKTPVSLVDLAPTILEAAGAPPPPDLD-----------GR 264
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 439 NLQkhlqlhDLEEEPDlfgnPRELIAYSQYprpadfpqwnsdkpSLNDIKVMGYSIRTVDYRYTVWVGFDPseflanfsd 518
Cdd:cd16037  265 SLL------PLAEGPD----DPDRVVFSEY--------------HAHGSPSGAFMLRKGRWKYIYYVGYPP--------- 311
                        490
                 ....*....|...
gi 341941059 519 ihagELYFVDSDP 531
Cdd:cd16037  312 ----QLFDLENDP 320
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-460 6.32e-58

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: 197.40  E-value: 6.32e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAQ----QAVCAPSRVSFLTGRrpdttrlydfnSYWRVH 114
Cdd:cd16155    4 NILFILADDQRAdTIGALGNPEIQTPNLDRLARRGTSFTNAYNMggwsGAVCVPSRAMLMTGR-----------TLFHAP 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 115 SGNFS-------TIPQYFKENGYVTMSVGKvfhpgissnhsddypysWsfppyhpssekyentktckgqdgklHanllcp 187
Cdd:cd16155   73 EGGKAaipsddkTWPETFKKAGYRTFATGK-----------------W-------------------------H------ 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 188 VDVADvpegtlpdkqsteEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPHVPdsLPPVAyN 267
Cdd:cd16155  105 NGFAD-------------AAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPL-PENFLP--QHPFD-N 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 268 PWMDIRereDVQALnisvPYGPIPEDFQRKIRQsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEW 347
Cdd:cd16155  168 GEGTVR---DEQLA----PFPRTPEAVRQHLAE-YYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM 239
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 348 AKYSNFDVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPPRCPIP 427
Cdd:cd16155  240 GKQNLYEHSMRVPLIISGPG-------------------------IPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGK 294
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341941059 428 SF-----------HVELCREGQNLQ-----------------KHLQLHDLEEEP----DLFGNPR 460
Cdd:cd16155  295 SLlpvirgekkavRDTLYGAYRDGQrairddrwkliiyvpgvKRTQLFDLKKDPdelnNLADEPE 359
PRK13759 PRK13759
arylsulfatase; Provisional
40-422 1.68e-54

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 191.42  E-value: 1.68e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTT-RLydfnSYWRVHSGN 117
Cdd:PRK13759   8 NIILIMVDQMRgDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHgRV----GYGDVVPWN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 118 FS-TIPQYFKENGYVTMSVGKV-FHP-----GISSNHSDDyPYSWSFPPYHPSSEKY--ENTKTCKGQDGKLHANLL--- 185
Cdd:PRK13759  84 YKnTLPQEFRDAGYYTQCIGKMhVFPqrnllGFHNVLLHD-GYLHSGRNEDKSQFDFvsDYLAWLREKAPGKDPDLTdig 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 186 --CPVDVA---DVPEGTLPDKQSTEEAIRLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlaPDPHVPDs 260
Cdd:PRK13759 163 wdCNSWVArpwDLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADI---PDPHIGD- 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 261 lppvaynpWmDIREREDVQALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWA 340
Cdd:PRK13759 238 --------W-EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDM 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 341 LGEHGEWAKYSNFDVATRVPLMLYVPGRTAPLPaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPV 420
Cdd:PRK13759 309 LGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGN---------------------RGTVIDQVVELRDIMPTLLDLAGGTI 367

                 ..
gi 341941059 421 PP 422
Cdd:PRK13759 368 PD 369
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-551 9.73e-50

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: 177.04  E-value: 9.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNF 118
Cdd:cd16150    2 NIVIFVADQLRAdSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPDEPNL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 119 StipQYFKENGYVTMSVGKvfhpgissnhSDDYPYSWSFPPYhpssekyentktckgqdgklhanllCPVDVADVpegtl 198
Cdd:cd16150   82 L---KTLKDAGYHVAWAGK----------NDDLPGEFAAEAY-------------------------CDSDEACV----- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 199 pdkqstEEAIRLLEKMKTSAsPFFLAVGYHKPHIPFRYPKEFQKLYPLEnitLAPdPHVPDSLPPVAYNPWMDIREREDV 278
Cdd:cd16150  119 ------RTAIDWLRNRRPDK-PFCLYLPLIFPHPPYGVEEPWFSMIDRE---KLP-PRRPPGLRAKGKPSMLEGIEKQGL 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 279 QALNisvpygpipEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSN-F-DVA 356
Cdd:cd16150  188 DRWS---------EERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNtFeDCL 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 357 TRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPrcpiPSFHVELCRe 436
Cdd:cd16150  259 TRVPLIIKPPGGP-------------------------AGGVSDALVELVDIPPTLLDLAGIPLSH----THFGRSLLP- 308
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 437 gqnlqkhlQLHDLEEEPD---------LFGNPReliAYSQYPRPADFPQWNS---DKPSLNDIKVMgysIRTVDYRYtVW 504
Cdd:cd16150  309 --------VLAGETEEHRdavfseggrLHGEEQ---AMEGGHGPYDLKWPRLlqqEEPPEHTKAVM---IRTRRYKY-VY 373
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 341941059 505 VGFDPSeflanfsdihagELYFVDSDPLQDHNVYNDSQHGGLLHSLR 551
Cdd:cd16150  374 RLYEPD------------ELYDLEADPLELHNLIGDPAYAEIIAEMK 408
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
39-425 1.06e-49

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: 174.30  E-value: 1.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  39 LNILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWrvhSGN 117
Cdd:cd16032    1 PNILLIMADQLTAAaLPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEF---PAD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 118 FSTIPQYFKENGYVTMSVGKVFHPGISSNHSDDYpyswsfppyhpssekyentktckgqdgklhanllcpvdvadvpegt 197
Cdd:cd16032   78 IPTFAHYLRAAGYRTALSGKMHFVGPDQLHGFDY---------------------------------------------- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 198 lpDKQSTEEAIRLLEKMKTSAS--PFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdphvpdslppvaynpwmdirer 275
Cdd:cd16032  112 --DEEVAFKAVQKLYDLARGEDgrPFFLTVSFTHPHDPYVIPQEYWDLY------------------------------- 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 276 edvqalnisvpygpipedfQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDV 355
Cdd:cd16032  159 -------------------VRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSFFEG 219
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 356 ATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdagRHTEDLVELVSLFPTLAGLAGLPVPPRCP 425
Cdd:cd16032  220 SARVPLIISAPGRFAP-------------------------RRVAEPVSLVDLLPTLVDLAGGGTAPHVP 264
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
39-423 1.53e-49

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: 171.96  E-value: 1.53e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  39 LNILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPdttrlydfnSYWRVHSG- 116
Cdd:cd16148    1 MNVILIVIDSLRADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP---------FYHGVWGGp 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 117 ---NFSTIPQYFKENGYVTMsvgkvfhpGISSNhsddyPYSWSFPPYHPSSEKYENTktcKGQDGklhanllcpvdvADV 193
Cdd:cd16148   72 lepDDPTLAEILRKAGYYTA--------AVSSN-----PHLFGGPGFDRGFDTFEDF---RGQEG------------DPG 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 194 PEGTLPDKQSTEEAIRLLEKMKTSaSPFFLAVGYHKPHIPFRYpkefqklyplenitlapDphvpdslppvaynpwmdir 273
Cdd:cd16148  124 EEGDERAERVTDRALEWLDRNADD-DPFFLFLHYFDPHEPYLY-----------------D------------------- 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 274 eredvqalnisvpygpipedfqrkirqsyfASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK-YSN 352
Cdd:cd16148  167 ------------------------------AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGhGSN 216
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341941059 353 F-DVATRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPR 423
Cdd:cd16148  217 LyDEQLHVPLIIRWPGKE-------------------------PGKRVDALVSHIDIAPTLLDLLGVEPPDY 263
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-420 2.72e-49

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: 171.79  E-value: 2.72e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRP-SLGCYGDKL----------VRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFN 108
Cdd:cd16153    3 NILWIITDDQRVdSLSCYNNAHtgksesrlgyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 109 SYWRVHSGNFSTIPQYFKENGYVTMSVGKvfhpgissnhsddypyswsfppyhpssEKYENtktckgqdgklhanllcPV 188
Cdd:cd16153   83 AAHPALDHGLPTFPEVLKKAGYQTASFGK---------------------------SHLEA-----------------FQ 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 189 DVADVPEgtlpdkQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFqklyplenitlapdphvpdslppvaynp 268
Cdd:cd16153  119 RYLKNAN------QSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEF---------------------------- 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 269 wmdiREREDvqalnisvpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAH---NTIIAFTSDHGWALGEHG 345
Cdd:cd16153  165 ----RDRFD------------------------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQG 216
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341941059 346 EWAKYSNFDVATRVPLMLYVPGRtaplpaagqKLFPyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPV 420
Cdd:cd16153  217 ILAKFTFWPQSHRVPLIVVSSDK---------LKAP-------------AGKVRHDFVEFVDLAPTLLAAAGVDV 269
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
40-422 6.01e-48

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: 171.96  E-value: 6.01e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNF 118
Cdd:cd16144    2 NIVLILVDDLgWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDNT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 119 S---------------TIPQYFKENGYVTMSVGKvFHPGISSNHS-DDYPYSWSF-------PPYHPSSEKYENTKTCKG 175
Cdd:cd16144   82 KlipppsttrlpleevTIAEALKDAGYATAHFGK-WHLGGEGGYGpEDQGFDVNIggtgnggPPSYYFPPGKPNPDLEDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 176 QDGKlhanllcpvdvadvpegTLPDKqSTEEAIRLLEkmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdp 255
Cdd:cd16144  161 PEGE-----------------YLTDR-LTDEAIDFIE--QNKDKPFFLYLSHYAVHTPIQARPELIEKY----------- 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 256 hvpdslppvaynpwmdireredvqalnisvpYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTS 335
Cdd:cd16144  210 -------------------------------EKKKKGLRKGQKNPVYAAMIESLDESVGRILDALEELGLADNTLVIFTS 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 336 DHGwALGEHGEWA---------KYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELV 406
Cdd:cd16144  259 DNG-GLSTRGGPPtsnaplrggKGSLYEGGIRVPLIVRWPGVIKP------------------------GSVSDVPVIGT 313
                        410
                 ....*....|....*.
gi 341941059 407 SLFPTLAGLAGLPVPP 422
Cdd:cd16144  314 DLYPTFLELAGGPLPP 329
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
40-509 4.02e-46

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: 167.82  E-value: 4.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRrpdttrlYDFN--SYW----- 111
Cdd:cd16028    2 NVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGR-------YLMNhrSVWngtpl 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 112 RVHsgnFSTIPQYFKENGYVTMSVGK---VFHP-GISSNHsddyPYSWSfppYHPSSEKYEntktckgqdgklhanllcP 187
Cdd:cd16028   75 DAR---HLTLALELRKAGYDPALFGYtdtSPDPrGLAPLD----PRLLS---YELAMPGFD------------------P 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 188 VDVADvpegTLPDKQS-----TEEAIRLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITL---APDPHVPD 259
Cdd:cd16028  127 VDRLD----EYPAEDSdtaflTDRAIEYLDERQDE--PWFLHLSYIRPHPPFVAPAPYHALYDPADVPPpirAESLAAEA 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 260 SLPPVaYNPWMDIREREDVQALNIsvPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGW 339
Cdd:cd16028  201 AQHPL-LAAFLERIESLSFSPGAA--NAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGE 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 340 ALGEHGEWAKYSNFDVATRVPLMLYVPGRTAplpaagqklfpyrdpfDPASdwmdaGRHTEDLVELVSLFPTLAGLAGLP 419
Cdd:cd16028  278 QLGDHWLWGKDGFFDQAYRVPLIVRDPRREA----------------DATR-----GQVVDAFTESVDVMPTILDWLGGE 336
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 420 VPPRCpipsfhvelcrEGQNLQKHLQlhdlEEEPdlfGNPRELIAYSQYPRPADFPQW------NSDKPSLNdikvmgyS 493
Cdd:cd16028  337 IPHQC-----------DGRSLLPLLA----GAQP---SDWRDAVHYEYDFRDVSTRRPqealglSPDECSLA-------V 391
                        490
                 ....*....|....*.
gi 341941059 494 IRTVDYRYTVWVGFDP 509
Cdd:cd16028  392 IRDERWKYVHFAALPP 407
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
40-540 1.24e-43

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: 160.02  E-value: 1.24e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNaFAQQAVCAPSRVSFLTGRRPDTTRLydfnsyWRVHSG-- 116
Cdd:cd16146    2 NVILILTDDQgYGDLGFHGNPILKTPNLDRLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRTGV------WHTILGre 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 117 ----NFSTIPQYFKENGYVTMSVGKvFHPGissnhsDDYPY----------------SWSFPPYHPSSEKYENTKTCKGQ 176
Cdd:cd16146   75 rmrlDETTLAEVFKDAGYRTGIFGK-WHLG------DNYPYrpqdrgfdevlghgggGIGQYPDYWGNDYFDDTYYHNGK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 177 DGKLhanllcpvdvadvpEGTLPDKQsTEEAIRLLEKMKTsaSPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdph 256
Cdd:cd16146  148 FVKT--------------EGYCTDVF-FDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPYK----------- 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 257 vpdslppvaynpwmDIREREDVQAlnisvpygpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSD 336
Cdd:cd16146  200 --------------DMGLDDKLAA---------------------FYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSD 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 337 HGWALGEHGEW------AKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFP 410
Cdd:cd16146  245 NGPAGGVPKRFnagmrgKKGSVYEGGHRVPFFIRWPGKILA------------------------GKDVDTLTAHIDLLP 300
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 411 TLAGLAGLPVPPRCPIpsfhvelcrEGQNLQKHLQlHDLEEEPDlfgnpRELIAYSQYPRPADFPQWNSdkpslndikvm 490
Cdd:cd16146  301 TLLDLCGVKLPEGIKL---------DGRSLLPLLK-GESDPWPE-----RTLFTHSGRWPPPPKKKRNA----------- 354
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 341941059 491 gySIRTVDYRYtVWVGFDPSeflanfsdihagELYFVDSDPLQDHNVYND 540
Cdd:cd16146  355 --AVRTGRWRL-VSPKGFQP------------ELYDIENDPGEENDVADE 389
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
40-421 3.12e-43

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: 158.88  E-value: 3.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSG-- 116
Cdd:cd16026    3 NIVVILADDLGYGdLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGGlp 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 117 -NFSTIPQYFKENGYVTMSVGKvFHPGISS-----NHSDDY----PYS---WSFPPYHPSSEkyentktckGQDGKLHAN 183
Cdd:cd16026   83 pDEITIAEVLKKAGYRTALVGK-WHLGHQPeflptRHGFDEyfgiPYSndmWPFPLYRNDPP---------GPLPPLMEN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 184 LLCPVDVADVPEGTlpdKQSTEEAIRLLEKMKTsaSPFFLAVGYHKPHIPfrypkefqkLYPlenitlapdphvpdslpp 263
Cdd:cd16026  153 EEVIEQPADQSSLT---QRYTDEAVDFIERNKD--QPFFLYLAHTMPHVP---------LFA------------------ 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 264 vaynpwmdireredvqalnisvpygpiPEDFQ-RKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALG 342
Cdd:cd16026  201 ---------------------------SEKFKgRSGAGLYGDVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLE 253
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 343 EHGEW--------AKYSNFDVATRVPLMLYVPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAG 414
Cdd:cd16026  254 YGGHGgsagplrgGKGTTWEGGVRVPFIAWWPGVIP------------------------AGTVSDELASTMDLLPTLAA 309

                 ....*..
gi 341941059 415 LAGLPVP 421
Cdd:cd16026  310 LAGAPLP 316
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-429 1.25e-40

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


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 147.77  E-value: 1.25e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRV----- 113
Cdd:cd16149    2 NILFILTDDQGPwALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHgktkk 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 114 ---HSGNFSTIPQYFKENGYVTMSVGKvFHPGissnhsddypyswsfppyhpssekyentktckgqdgklhanllcpvdv 190
Cdd:cd16149   82 pegYLEGQTTLPEVLQDAGYRCGLSGK-WHLG------------------------------------------------ 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 191 advpegtlpdkqstEEAIRLLEKMKTSASPFFLAVGYHKPHipfrypkefqklyplenitlapdphvpdslppvayNPWm 270
Cdd:cd16149  113 --------------DDAADFLRRRAEAEKPFFLSVNYTAPH-----------------------------------SPW- 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 271 direredvqalnisvpygpipedfqrkirqSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAK- 349
Cdd:cd16149  143 ------------------------------GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKg 192
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 350 -----YSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGLPVP--P 422
Cdd:cd16149  193 ngtfpLNMYDNSVKVPFIIRWPGVVPA------------------------GRVVDSLVSAYDFFPTLLELAGVDPPadP 248

                 ....*..
gi 341941059 423 RCPIPSF 429
Cdd:cd16149  249 RLPGRSF 255
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
40-423 1.62e-40

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: 151.59  E-value: 1.62e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSY---WRVHS 115
Cdd:cd16145    2 NIIFILADDLGYGdLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPggqDPLPP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 116 GNfSTIPQYFKENGYVTMSVGK-----VFHPGISSNHSDDYPYSWS--------FPPYhpsseKYENTKTcKGQDGKLHA 182
Cdd:cd16145   82 DD-VTLAEVLKKAGYATAAFGKwglggPGTPGHPTKQGFDYFYGYLdqvhahnyYPEY-----LWRNGEK-VPLPNNVIP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 183 NLLCPVDVADVPEGTLPDKqSTEEAIRLLEKMKtsASPFFLAVGYHKPHIPFRYPKefqklyplenitLAPDPHVPDSLP 262
Cdd:cd16145  155 PLDEGNNAGGGGGTYSHDL-FTDEALDFIRENK--DKPFFLYLAYTLPHAPLQVPD------------DGPYKYKPKDPG 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 263 PVAYNPWmdireredvqalnisvpygpipedfqRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGwALG 342
Cdd:cd16145  220 IYAYLPW--------------------------PQPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNG-PHS 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 343 EHGEWAKYSNFDVA--------------TRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSL 408
Cdd:cd16145  273 EGGSEHDPDFFDSNgplrgykrslyeggIRVPFIARWPGKIPA------------------------GSVSDHPSAFWDF 328
                        410
                 ....*....|....*
gi 341941059 409 FPTLAGLAGLPVPPR 423
Cdd:cd16145  329 MPTLADLAGAEPPED 343
Sulfatase pfam00884
Sulfatase;
40-418 6.64e-37

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 138.71  E-value: 6.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059   40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNsywRVHSGN- 117
Cdd:pfam00884   2 NVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVST---PVGLPRt 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  118 FSTIPQYFKENGYVTMSVGKvFHPGISSNHSDDYPYSWSFPPYHPSSEKYENTKTCKGQDgklhanllcpvdvadvPEGT 197
Cdd:pfam00884  79 EPSLPDLLKRAGYNTGAIGK-WHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNC----------------SGGG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  198 LPDKQSTEEAIRLLEKmktSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdphvpdslppvaynpwmdirered 277
Cdd:pfam00884 142 VSDEALLDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKYA-------------------------------- 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  278 vqalnISVPYGpipeDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVA- 356
Cdd:pfam00884 187 -----TFKPSS----CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNAp 257
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341941059  357 ---TRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLFPTLAGLAGL 418
Cdd:pfam00884 258 eggYRVPLLIWSPGGKAK------------------------GQKSEALVSHVDLFPTILDLAGI 298
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-536 7.32e-37

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


Pssm-ID: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 140.43  E-value: 7.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAqQAVCAPSRVSFLTGRRPDTTrlYDFNSYWrvHSGNf 118
Cdd:cd16151    2 NIILIMADDLGYeCIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRN--YVVFGYL--DPKQ- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 119 STIPQYFKENGYVTMSVGKvfhPGISSNHSD-DYPY-----SWSFPPYHPSSEKYENTKTCKG--QDGKLhanllcpvdV 190
Cdd:cd16151   76 KTFGHLLKDAGYATAIAGK---WQLGGGRGDgDYPHefgfdEYCLWQLTETGEKYSRPATPTFniRNGKL---------L 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 191 ADVPEGTLPDkQSTEEAIRLLEKMKtsASPFFLavgYhkphipfrYPkefqklyplenITLAPDPHV--PDSLppvaynP 268
Cdd:cd16151  144 ETTEGDYGPD-LFADFLIDFIERNK--DQPFFA---Y--------YP-----------MVLVHDPFVptPDSP------D 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 269 WMDIRERedvqalnisvpygpipedfqRKIRQSYF-ASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEW 347
Cdd:cd16151  193 WDPDDKR--------------------KKDDPEYFpDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRT 252
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 348 -------AKYSNFDVATRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmDAGRHTEDLVELVSLFPTLAGLAGLPV 420
Cdd:cd16151  253 ngrevrgGKGKTTDAGTHVPLIVNWPGLI------------------------PAGGVSDDLVDFSDFLPTLAELAGAPL 308
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 421 PPRCPIpsfhvelcrEGQNLQkhlqlhdleeePDLFGNP----RELIAYsqYPRpadfPQWNSDKPslndikvmgYSIRT 496
Cdd:cd16151  309 PEDYPL---------DGRSFA-----------PQLLGKTgsprREWIYW--YYR----NPHKKFGS---------RFVRT 353
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 341941059 497 VDYRYtvwvgfdpseflanFSDihaGELYFVDSDPLQDHN 536
Cdd:cd16151  354 KRYKL--------------YAD---GRFFDLREDPLEKNP 376
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
40-426 1.84e-35

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: 136.91  E-value: 1.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQaVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSG-- 116
Cdd:cd16029    2 HIVFILADDLGWNdVGFHGSDQIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGRYPIHTGMQHGVILAGEPYGlp 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 117 -NFSTIPQYFKENGYVTMSVGKvFHPGIssnhsddypYSWSFPP----------YHPSSEKYENTKTCKGQDgklhanll 185
Cdd:cd16029   81 lNETLLPQYLKELGYATHLVGK-WHLGF---------YTWEYTPtnrgfdsfygYYGGAEDYYTHTSGGAND-------- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 186 CPVDVADVPEGTLPDKQS-------TEEAIRLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlAPDPHVP 258
Cdd:cd16029  143 YGNDDLRDNEEPAWDYNGtystdlfTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYE------DKFAHIK 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 259 DslppvaynpwmdireredvqalnisvpygpipedfqrKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHG 338
Cdd:cd16029  216 D-------------------------------------EDRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 339 wALGEHGEWA--------KYSNFDVATRVPLMLYVPGRTaplPAAGQKlfpYRDPFDpASDWmdagrhtedlvelvslFP 410
Cdd:cd16029  259 -GPTGGGDGGsnyplrggKNTLWEGGVRVPAFVWSPLLP---PKRGTV---SDGLMH-VTDW----------------LP 314
                        410
                 ....*....|....*.
gi 341941059 411 TLAGLAGLPVPPRCPI 426
Cdd:cd16029  315 TLLSLAGGDPDDLPPL 330
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
40-422 8.70e-35

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: 135.37  E-value: 8.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPSLGCYGD--KLVRspnidQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPD----TTRLYDFNSYWRV 113
Cdd:cd16147    3 NIVLILTDDQDVELGSMDPmpKTKK-----LLADQGTTFTNAFVTTPLCCPSRASILTGQYAHnhgvTNNSPPGGGYPKF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 114 HSGNF--STIPQYFKENGYVTMSVGKVFHpGISSNHSDDYP---YSWSFPPYHPSseKYENTKTCKGQDGKLHANLlcpv 188
Cdd:cd16147   78 WQNGLerSTLPVWLQEAGYRTAYAGKYLN-GYGVPGGVSYVppgWDEWDGLVGNS--TYYNYTLSNGGNGKHGVSY---- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 189 dvadvPEGTLPDKqSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPleNITLAPDPHVPDslPPVAYNP 268
Cdd:cd16147  151 -----PGDYLTDV-IANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFP--NVTAPPRPPPNN--PDVSDKP 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 269 -WmdIREREDVQALNISVpygpIPEDFQRKIR--QSyfasvsyLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHG 345
Cdd:cd16147  221 hW--LRRLPPLNPTQIAY----IDELYRKRLRtlQS-------VDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHR 287
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341941059 346 -EWAKYSNFDVATRVPLMLYVPGrtapLPaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPP 422
Cdd:cd16147  288 lPPGKRTPYEEDIRVPLLVRGPG----IP---------------------AGVTVDQLVSNIDLAPTILDLAGAPPPS 340
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-551 9.62e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 131.97  E-value: 9.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSywRVHSGNF 118
Cdd:cd16152    3 NVIVFFTDQQRWdTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFR-NG--IPLPADE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 119 STIPQYFKENGYVTMSVGKvfhpgissnhsddypysWSFPPYHpssekyentktckgqdgklhanllcpVDVAdvpegtl 198
Cdd:cd16152   80 KTLAHYFRDAGYETGYVGK-----------------WHLAGYR--------------------------VDAL------- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 199 pdkqsTEEAIRLLEKmKTSASPFFLAVGYHKPHIP---FRY--PKEFQKLYplenitlaPDPHVPdslppvaynpwmdir 273
Cdd:cd16152  110 -----TDFAIDYLDN-RQKDKPFFLFLSYLEPHHQndrDRYvaPEGSAERF--------ANFWVP--------------- 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 274 erEDVQALnisvpygpiPEDFQRKIrQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHgwalGEH-----GEWa 348
Cdd:cd16152  161 --PDLAAL---------PGDWAEEL-PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHfrtrnAEY- 223
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 349 KYSNFDVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPprcpiPS 428
Cdd:cd16152  224 KRSCHESSIRVPLVIYGPG-------------------------FNGGGRVEELVSLIDLPPTLLDAAGIDVP-----EE 273
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 429 FHvelcreGQNLQKhlqlhDLEEEPDlfgnPRELIAYSQyprpadfpqwnsdkpsLNDIKVmGYSIRTVDYRYTVwVGFD 508
Cdd:cd16152  274 MQ------GRSLLP-----LVDGKVE----DWRNEVFIQ----------------ISESQV-GRAIRTDRWKYSV-AAPD 320
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 341941059 509 PSEFLANFSDIHAGE-LYFVDSDPLQDHNVYNDSQHGGLLHSLR 551
Cdd:cd16152  321 KDGWKDSGSDVYVEDyLYDLEADPYELVNLIGRPEYREVAAELR 364
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
40-421 2.11e-33

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


Pssm-ID: 293762 [Multi-domain]  Cd Length: 395  Bit Score: 131.17  E-value: 2.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRP-SLGCYGDK-LVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNsyWRVHSG- 116
Cdd:cd16143    2 NIVIILADDLGYgDISCYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGV--LGGFSPp 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 117 ----NFSTIPQYFKENGYVTMSVGKvFHPGIssnhsdDYPYSWSFPPYHPSSEKYENTKTCKgqDGklhanllcPVDV-- 190
Cdd:cd16143   80 liepDRVTLAKMLKQAGYRTAMVGK-WHLGL------DWKKKDGKKAATGTGKDVDYSKPIK--GG--------PLDHgf 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 191 --------ADVpegtlpDKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKlyplenitlapdphvpdslp 262
Cdd:cd16143  143 dyyfgipaSEV------LPTLTDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQG-------------------- 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 263 pvaynpwmdireredVQALNisvPYGpipeDFqrkIRQsyfasvsyLDTQVGHVLSALDDLRLAHNTIIAFTSDHG---- 338
Cdd:cd16143  197 ---------------KSGAG---PYG----DF---VYE--------LDWVVGRILDALKELGLAENTLVIFTSDNGpspy 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 339 ---WALGEHGEWA-------KYSNFDVATRVPLMLYVPGRTaplpaagqklfpyrdpfdpasdwmDAGRHTEDLVELVSL 408
Cdd:cd16143  244 adyKELEKFGHDPsgplrgmKADIYEGGHRVPFIVRWPGKI------------------------PAGSVSDQLVSLTDL 299
                        410
                 ....*....|...
gi 341941059 409 FPTLAGLAGLPVP 421
Cdd:cd16143  300 FATLAAIVGQKLP 312
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
40-422 2.60e-33

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: 132.51  E-value: 2.60e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTtrlydfNSYWR---VHS 115
Cdd:cd16156    2 QFIFIMTDTQRWDmVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHT------NGSWTncmALG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 116 GNFSTIPQYFKENGYVTMSVGKVfhpgissnHSD--DY------PYSWSfPPYHPSSEKYENTKTckGQDGKLHANLLCP 187
Cdd:cd16156   76 DNVKTIGQRLSDNGIHTAYIGKW--------HLDggDYfgngicPQGWD-PDYWYDMRNYLDELT--EEERRKSRRGLTS 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 188 VDVADVPEGTLPDKQSTEEAIRLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYplENITLAPDPHVPDSLP--PVA 265
Cdd:cd16156  145 LEAEGIKEEFTYGHRCTNRALDFIEKHKDE--DFFLVVSYDEPHHPFLCPKPYASMY--KDFEFPKGENAYDDLEnkPLH 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 266 YNPWMDIREREDVQALNISVPYgpipedfqrkirqsYFASVSYLDTQVGHVLSALDDLrlAHNTIIAFTSDHGWALGEHG 345
Cdd:cd16156  221 QRLWAGAKPHEDGDKGTIKHPL--------------YFGCNSFVDYEIGRVLDAADEI--AEDAWVIYTSDHGDMLGAHK 284
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341941059 346 EWAK-YSNFDVATRVPLMLYVPGRtapLPAAGQKLFPyrdpfdpasdwmdagrhtedlVELVSLFPTLAGLAGLPVPP 422
Cdd:cd16156  285 LWAKgPAVYDEITNIPLIIRGKGG---EKAGTVTDTP---------------------VSHIDLAPTILDYAGIPQPK 338
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
40-422 3.93e-30

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: 121.49  E-value: 3.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPS-LGCYGDKLVR---SPNIDQLASHSVLFQNAFAQQAvCAPSRVSFLTGRRPdttrlydfnsywrVHS 115
Cdd:cd16142    2 NILVILGDDIGWGdLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHP-------------IRT 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 116 GNFS---------------TIPQYFKENGYVTMSVGKvfhpgissNHSDDYPYSWsfppyhpssekyentktckgqdgkl 180
Cdd:cd16142   68 GLTTvglpgspgglppwepTLAELLKDAGYATAQFGK--------WHLGDEDGRL------------------------- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 181 hanllcPVDVA-DVPEGTLP---DKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdph 256
Cdd:cd16142  115 ------PTDHGfDEFYGNLYhtiDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSS----------- 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 257 vpdslppvAYNPWMDireredvqalnisvpygpipedfqrkirqsyfaSVSYLDTQVGHVLSALDDLRLAHNTIIAFTSD 336
Cdd:cd16142  178 --------GKGKYAD---------------------------------SMVELDDHVGQILDALDELGIADNTIVIFTTD 216
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 337 HG-----WALGEHGEW--AKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRHTEDLVELVSLF 409
Cdd:cd16142  217 NGpeqdvWPDGGYTPFrgEKGTTWEGGVRVPAIVRWPGKIKP------------------------GRVSNEIVSHLDWF 272
                        410
                 ....*....|...
gi 341941059 410 PTLAGLAGLPVPP 422
Cdd:cd16142  273 PTLAALAGAPDPK 285
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
40-421 1.32e-28

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


Pssm-ID: 293749 [Multi-domain]  Cd Length: 402  Bit Score: 117.54  E-value: 1.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPS-LGCYGDkLVRSPNIDQLASHSVLFQNaFAQQAVCAPSRVSFLTGRRP-------DTTRLYDFNSYW 111
Cdd:cd16025    4 NILLILADDLGFSdLGCFGG-EIPTPNLDALAAEGLRFTN-FHTTALCSPTRAALLTGRNHhqvgmgtMAELATGKPGYE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 112 RVHSGNFSTIPQYFKENGYVTMSVGKvfhpgissnhsddypysW--SFPPYHpSSEKYentktckgqdgklhanllcpvd 189
Cdd:cd16025   82 GYLPDSAATIAEVLKDAGYHTYMSGK-----------------WhlGPDDYY-STDDL---------------------- 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 190 vadvpegtlpdkqsTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEF----------------------QK---LY 244
Cdd:cd16025  122 --------------TDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkykgkydagwdalreerlerQKelgLI 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 245 PlENITLAPDPH-VP--DSLPPvaynpwmdirEREDVQALNISVpygpipedfqrkirqsYFASVSYLDTQVGHVLSALD 321
Cdd:cd16025  188 P-ADTKLTPRPPgVPawDSLSP----------EEKKLEARRMEV----------------YAAMVEHMDQQIGRLIDYLK 240
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 322 DLRLAHNTIIAFTSDHGwALGEHGeWAKYSNfdvaTrvPLMLYvpgrtaplpaagqKLFPY----RDPF--DPASDWMDA 395
Cdd:cd16025  241 ELGELDNTLIIFLSDNG-ASAEPG-WANASN----T--PFRLY-------------KQASHeggiRTPLivSWPKGIKAK 299
                        410       420
                 ....*....|....*....|....*.
gi 341941059 396 GRHTEDLVELVSLFPTLAGLAGLPVP 421
Cdd:cd16025  300 GGIRHQFAHVIDIAPTILELAGVEYP 325
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-423 2.51e-27

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: 112.30  E-value: 2.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYD-FNSYWRVH-SG 116
Cdd:cd16035    2 NILLILTDQERyPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDtLGSPMQPLlSP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 117 NFSTIPQYFKENGYVTMSVGKvfhpgissnhsddypysWsfppyHPSSekyentktckgqdgklHANllcpvdvadvpEG 196
Cdd:cd16035   82 DVPTLGHMLRAAGYYTAYKGK-----------------W-----HLSG----------------AAG-----------GG 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 197 TLPDKQSTEEAIRLLEKMKTSAS---PFFLAVGYHKPHipfrypkefqklyplenitlapdphvpdslppvaynpwmdir 273
Cdd:cd16035  113 YKRDPGIAAQAVEWLRERGAKNAdgkPWFLVVSLVNPH------------------------------------------ 150
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 274 ereDVQalnisvpYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSN- 352
Cdd:cd16035  151 ---DIM-------FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNa 220
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341941059 353 FDVATRVPLMLYVPGrtaplpaagqkLFPyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGLPVPPR 423
Cdd:cd16035  221 YEEALHVPLIISHPD-----------LFG-------------TGQTTDALTSHIDLLPTLLGLAGVDAEAR 267
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
40-422 1.43e-24

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: 105.32  E-value: 1.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPSLGCY-GDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRlyDFNSYWRVHSgNF 118
Cdd:cd16171    2 NVVMVMSDSFDGRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTE--SWNNYKGLDP-NY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 119 STIPQYFKENGYVTMSVGKVFHpgISSNHS-DDYPYSWSfppyhpssekyENTKTCKGQDGKLHANLLCPVDVADVpegT 197
Cdd:cd16171   79 PTWMDRLEKHGYHTQKYGKLDY--TSGHHSvSNRVEAWT-----------RDVPFLLRQEGRPTVNLVGDRSTVRV---M 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 198 LPDKQSTEEAIRLLEKMKTSAS-PFFLAVGYHKPHiPFRYPkefqklypleniTLAPDphvpdslppvaynpwmdirere 276
Cdd:cd16171  143 LKDWQNTDKAVHWIRKEAPNLTqPFALYLGLNLPH-PYPSP------------SMGEN---------------------- 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 277 dvqalnisvpYGPIpedfqRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYSNFDVA 356
Cdd:cd16171  188 ----------FGSI-----RNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMYEGS 252
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341941059 357 TRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAGLPVPP 422
Cdd:cd16171  253 SHVPLLIMGPG-------------------------IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
40-421 2.46e-24

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: 106.60  E-value: 2.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSY----WRVH 114
Cdd:cd16159    3 NIVLFMADDLGiGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMrvilFTAS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 115 SG----NFSTIPQYFKENGYVTMSVGKvFHPGISSNHSDDYpyswsfpPYHPSSEKYE--------NTKTCkgQDGKLHA 182
Cdd:cd16159   83 SGglppNETTFAEVLKQQGYSTALIGK-WHLGLHCESRNDF-------CHHPLNHGFDyfyglpltNLKDC--GDGSNGE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 183 NLLCPVDVADVPEGTLPDKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPL--ENITLAPDPHVPDS 260
Cdd:cd16159  153 YDLSFDPLFPLLTAFVLITALTIFLLLYLGAVSKRFFVFLLILSLLFISLFFLLLITNRYFNCIlmRNHEVVEQPMSLEN 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 261 LPP---VAYNPWMDIRERED----VQALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAF 333
Cdd:cd16159  233 LTQrltKEAISFLERNKERPfllvMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYF 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 334 TSDHGWAL------GEHGEW-------AKYSNFDVATRVPLMLYVPGRTAPlpaaGQKLfpyrdpfDPASDWMDagrhte 400
Cdd:cd16159  313 TSDNGGHLeeisvgGEYGGGnggiyggKKMGGWEGGIRVPTIVRWPGVIPP----GSVI-------DEPTSLMD------ 375
                        410       420
                 ....*....|....*....|.
gi 341941059 401 dlvelvsLFPTLAGLAGLPVP 421
Cdd:cd16159  376 -------IFPTVAALAGAPLP 389
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
40-421 4.33e-20

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: 93.28  E-value: 4.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSG-- 116
Cdd:cd16158    3 NIVLLFADDLgYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGGlp 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 117 -NFSTIPQYFKENGYVTMSVGKvFHPGISSNHS--------DDY---PYSWSFPPYHPSSEKYENTKTCKGQDGKLhanL 184
Cdd:cd16158   83 lNETTIAEVLKTVGYQTAMVGK-WHLGVGLNGTylpthqgfDHYlgiPYSHDQGPCQNLTCFPPNIPCFGGCDQGE---V 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 185 LCPVDVADVPEGTLPD-----KQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQklyplenitlapdphvpd 259
Cdd:cd16158  159 PCPLFYNESIVQQPVDlltleERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFA------------------ 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 260 slppvaynpwmdireredvqalnisvpygpipedfQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGW 339
Cdd:cd16158  221 -----------------------------------GRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGP 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 340 AL------GEHG--EWAKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaGRhTEDLVELVSLFPT 411
Cdd:cd16158  266 STmrksrgGNAGllKCGKGTTYEGGVREPAIAYWPGRIKP------------------------GV-THELASTLDILPT 320
                        410
                 ....*....|
gi 341941059 412 LAGLAGLPVP 421
Cdd:cd16158  321 IAKLAGAPLP 330
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
40-421 1.10e-18

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: 88.68  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSywrvHSGNF 118
Cdd:cd16157    3 NIILMLMDDMGwGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNA----HARNA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 119 ST--------------IPQYFKENGYVTMSVGKvFHPGissnHSddypyswsfPPYHP---SSEKYENTKTC--KGQDGK 179
Cdd:cd16157   79 YTpqnivggipdseilLPELLKKAGYRNKIVGK-WHLG----HR---------PQYHPlkhGFDEWFGAPNChfGPYDNK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 180 LHANLlcPVDVADVPEGTLPDKQS--------------TEEAIRLLEKMKTSASPFFLAVGYHKPHIPfrypkefqkLYp 245
Cdd:cd16157  145 AYPNI--PVYRDWEMIGRYYEEFKidkktgesnltqiyLQEALEFIEKQHDAQKPFFLYWAPDATHAP---------VY- 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 246 lenitlapdphvpdslppvAYNPWMDIREREdvqalnisvpygpipedfqrkirqSYFASVSYLDTQVGHVLSALDDLRL 325
Cdd:cd16157  213 -------------------ASKPFLGTSQRG------------------------LYGDAVMELDSSVGKILESLKSLGI 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 326 AHNTIIAFTSDHGWAL-------GEHGEW--AKYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdaG 396
Cdd:cd16157  250 ENNTFVFFSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPGHIKP------------------------G 305
                        410       420
                 ....*....|....*....|....*
gi 341941059 397 RHTEDLVELVSLFPTLAGLAGLPVP 421
Cdd:cd16157  306 QVSHQLGSLMDLFTTSLALAGLPIP 330
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
40-422 2.24e-18

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: 87.14  E-value: 2.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLR-PSLGCYGDKLVR-SPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSYWRVHSG- 116
Cdd:cd16161    3 NFLLLFADDLGwGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGH-NFLPTSVGGl 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 117 --NFSTIPQYFKENGYVTMSVGKvFHPGISSNhsddypyswsfppYHPSSekyentktcKGQDGKLHANLLCPVDVADvp 194
Cdd:cd16161   82 plNETTLAEVLRQAGYATGMIGK-WHLGQREA-------------YLPNS---------RGFDYYFGIPFSHDSSLAD-- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 195 egtlpdkQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPkefqklyplenitlaPDPHVPDSlppvaynpwmdire 274
Cdd:cd16161  137 -------RYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANL---------------PRFQSPTS-------------- 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 275 redvqalnISVPYGpipedfqrkirqsyfASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHG-WALG-------EHGE 346
Cdd:cd16161  181 --------GRGPYG---------------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpWEVKcelavgpGTGD 237
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 347 W--------AKYSNFDVATRVPLMLYVPGRTAplpaagqklfpyrdpfdpasdwmdAGRHTEDLVELVSLFPTLAGLAGL 418
Cdd:cd16161  238 WqgnlggsvAKASTWEGGHREPAIVYWPGRIP------------------------ANSTSAALVSTLDIFPTVVALAGA 293

                 ....
gi 341941059 419 PVPP 422
Cdd:cd16161  294 SLPP 297
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
40-417 2.67e-18

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: 87.49  E-value: 2.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRpslgcYGDKLV-------RSPnIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY--DFNSY 110
Cdd:cd16160    3 NIVLFFADDMG-----YGDLASyghptqeRGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYggTRVFL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 111 WRVHSG---NFSTIPQYFKENGYVTMSVGKvFHPGISSNHSDDypySWSFPPYH---------PssekYENTKTCkgQDG 178
Cdd:cd16160   77 PWDIGGlpkTEVTMAEALKEAGYTTGMVGK-WHLGINENNHSD---GAHLPSHHgfdfvgtnlP----FTNSWAC--DDT 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 179 KLHanllcpVDVADVPEGTLPDK-QSTEEAIR---LLEKMKTSA---------SPFFLAVGYHKPHIPFRYPKEFQklyp 245
Cdd:cd16160  147 GRH------VDFPDRSACFLYYNdTIVEQPIQhehLTETLVGDAksfiednqeNPFFLYFSFPQTHTPLFASKRFK---- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 246 lenitlapdphvpdslppvaynpwmdireredvqalNISVpygpipedfqrkiRQSYFASVSYLDTQVGHVLSALDDLRL 325
Cdd:cd16160  217 ------------------------------------GKSK-------------RGRYGDNINEMSWAVGEVLDTLVDTGL 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 326 AHNTIIAFTSDHGWAL---GEHGEWA-----KYSNFDVATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdagR 397
Cdd:cd16160  248 DQNTLVFFLSDHGPHVeycLEGGSTGglkggKGNSWEGGIRVPFIAYWPGTIKP-------------------------R 302
                        410       420
                 ....*....|....*....|
gi 341941059 398 HTEDLVELVSLFPTLAGLAG 417
Cdd:cd16160  303 VSHEVVSTMDIFPTFVDLAG 322
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
28-422 2.99e-17

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 85.09  E-value: 2.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  28 SAAQGNSATDALNILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGrrpdttrLYD 106
Cdd:COG1368  224 PTPNPFGPAKKPNVVVILLESFsDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTG-------LPP 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 107 FNS---YWRVHSGNFSTIPQYFKENGYVTMsvgkVFHPGissnhsddYPYSWSFPPYHPSsEKYENTKtckGQDgklhan 183
Cdd:COG1368  297 LPGgspYKRPGQNNFPSLPSILKKQGYETS----FFHGG--------DGSFWNRDSFYKN-LGFDEFY---DRE------ 354
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 184 llcpvDVADVPEGT--LPDKQSTEEAIRLLEKMKtsaSPFFLAV----GyhkpHIPFRYPKEFQKLYPLENITLapdphv 257
Cdd:COG1368  355 -----DFDDPFDGGwgVSDEDLFDKALEELEKLK---KPFFAFLitlsN----HGPYTLPEEDKKIPDYGKTTL------ 416
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 258 pdslppvaynpwmdireredvqalnisvpygpipedfqrkirQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDH 337
Cdd:COG1368  417 ------------------------------------------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDH 454
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 338 GwalGEHGEWAKYSNFDVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLAG 417
Cdd:COG1368  455 G---PRSPGKTDYENPLERYRVPLLIYSPG-------------------------LKKPKVIDTVGSQIDIAPTLLDLLG 506

                 ....*
gi 341941059 418 LPVPP 422
Cdd:COG1368  507 IDYPS 511
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
40-417 1.70e-15

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: 76.95  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVC--APSRVSFLTGRRPDTTRLYDFNSYwrvHSG 116
Cdd:cd16015    2 NVIVILLESFsDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGgtANGEFEVLTGLPPLPLGSGSYTLY---KLN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 117 NFSTIPQYFKENGYVTMSvgkvFHPGissnhsddYPYSWSFPPYHP--------SSEKYENTKTCKGQDGklhanllcpv 188
Cdd:cd16015   79 PLPSLPSILKEQGYETIF----IHGG--------DASFYNRDSVYPnlgfdefyDLEDFPDDEKETNGWG---------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 189 dvadvpegtLPDKQSTEEAIRLLEKMKtsASPFFLAVgyhkphipfrypkefqklyplenITLapDPHVPDSLPPVAYNP 268
Cdd:cd16015  137 ---------VSDESLFDQALEELEELK--KKPFFIFL-----------------------VTM--SNHGPYDLPEEKKDE 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 269 wmdireredvqalnisvpygPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWA 348
Cdd:cd16015  181 --------------------PLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDET 240
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341941059 349 KYSNFDvATRVPLMLYVPGRTAPlpaagqklfpyrdpfdpasdwmdagRHTEDLVELVSLFPTLAGLAG 417
Cdd:cd16015  241 DEDPLD-LYRTPLLIYSPGLKKP-------------------------KKIDRVGSQIDIAPTLLDLLG 283
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
40-421 2.48e-14

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


Pssm-ID: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 74.69  E-value: 2.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDL-RPSLGCY--GDKLVRSPNIDQLASHSVLFQNAFAqQAVCAPSRVSFLTGRrpdttrlYDFN----SYWR 112
Cdd:cd16154    2 NILLIIADDQgLDSSAQYslSSDLPVTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGK-------YGFRtgvlAVPD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 113 VHSGNFSTIPQYFKEN----GYVTMSVGKvFHPGISSNHSDDYPYSWSFPPYHPS--SEKYENTKTCKGQdgklhanllc 186
Cdd:cd16154   74 ELLLSEETLLQLLIKDattaGYSSAVIGK-WHLGGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQ---------- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 187 pvdvaDVPEGTLPDKQSTEEAIRLLEKmktSASPFFLAVGYHKPHIPFRYPkefqklyP--LENITLAPDphvpdsLPPV 264
Cdd:cd16154  143 -----TTNSTEYATTKLTNLAIDWIDQ---QTKPWFLWLAYNAPHTPFHLP-------PaeLHSRSLLGD------SADI 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 265 AYNPwmdireredvqalnisvpygpipedfqrkiRQSYFASVSYLDTQVGHVLSALDDLRLAhNTIIAFTSDHG------ 338
Cdd:cd16154  202 EANP------------------------------RPYYLAAIEAMDTEIGRLLASIDEEERE-NTIIIFIGDNGtpgqvv 250
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 339 --WALGEHgewAKYSNFDVATRVPLMlyvpgrtaplpAAGQKLfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLA 416
Cdd:cd16154  251 dlPYTRNH---AKGSLYEGGINVPLI-----------VSGAGV-------------ERANERESALVNATDLYATIAELA 303

                 ....*
gi 341941059 417 GLPVP 421
Cdd:cd16154  304 GVDAA 308
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
40-416 9.48e-13

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 67.83  E-value: 9.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQnAFAQQAVC--APSRVSFLTGRRPDttrlydfnsywrvhsg 116
Cdd:cd00016    2 HVVLIVLDGLGADdLGKAGNPAPTTPNLKRLASEGATFN-FRSVSPPTssAPNHAALLTGAYPT---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 117 nfstipqyfkENGYVTMSVGKVFHPGISSNHSDDYPyswSFPpyhpssekyentktckgqdgklhanllcpvdvadvpeG 196
Cdd:cd00016   65 ----------LHGYTGNGSADPELPSRAAGKDEDGP---TIP-------------------------------------E 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 197 TLPDKQSTEEAIRLLE--KMKTSASPFFLAVGYHKPHIPFrypkefqklyplenitlapdpHVPDSLPPvaynpwmdire 274
Cdd:cd00016   95 LLKQAGYRTGVIGLLKaiDETSKEKPFVLFLHFDGPDGPG---------------------HAYGPNTP----------- 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 275 redvqalnisvpygpipedfqrkirqSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGEWAKYS--- 351
Cdd:cd00016  143 --------------------------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADgka 196
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341941059 352 -NFDVATRVPLMLYVPGrtaplpaagqklfpyrdpfdpasdwMDAGRHTEDLVELVSLFPTLAGLA 416
Cdd:cd00016  197 dKSHTGMRVPFIAYGPG-------------------------VKKGGVKHELISQYDIAPTLADLL 237
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
200-370 3.27e-12

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: 69.16  E-value: 3.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 200 DKQSTEEAIRLLEKmKTSASPFFLAVGYHKPHIpFRYPKEFQKLYplenitlapdphvpdslppvaynpwmdireredvQ 279
Cdd:COG3083  363 DRQITAQWLQWLDQ-RDSDRPWFSYLFLDAPHA-YSFPADYPKPF----------------------------------Q 406
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 280 ALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWALGEHGE--WAKYSNF-DVA 356
Cdd:COG3083  407 PSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQnyWGHNSNFsRYQ 486
                        170
                 ....*....|....
gi 341941059 357 TRVPLMLYVPGRTA 370
Cdd:COG3083  487 LQVPLVIHWPGTPP 500
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
40-418 2.03e-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: 43.38  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  40 NILLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSVLFQNAFAqqavCAPS-RVS---FLTGR-RPDTTRLYDFNSywrv 113
Cdd:cd16017    4 NVVLVIGESARRDhMSLYGYPRDTTPFLSKLKKNLIVFDNVIS----CGTStAVSlpcMLSFAnRENYDRAYYQEN---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 114 hsgnfstIPQYFKENGYvtmsvgKVFHpgISsNHSDDYPYSWSFPPYHPSSEKYENTKTCKGQ---DGKLhanllcpvdv 190
Cdd:cd16017   76 -------LIDLAKKAGY------KTYW--IS-NQGGCGGYDTRISAIAKIETVFTNKGSCNSSncyDEAL---------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 191 advpegtLPDkqsteeairLLEKMKTSASPFFLAV---GyhkPHIPF--RYPKEFQKLYPlenitlapdphvpdslppva 265
Cdd:cd16017  130 -------LPL---------LDEALADSSKKKLIVLhlmG---SHGPYydRYPEEFAKFTP-------------------- 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059 266 ynpwmdireredvqalnisVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSALDdlRLAHNTIIAFTSDHGWALGEHG 345
Cdd:cd16017  171 -------------------DCDNELQSCSKEELINAYDNSILYTDYVLSQIIERLK--KKDKDAALIYFSDHGESLGENG 229
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341941059 346 EW--AKYSNFDVATRVPLMLYVPGRTAPLPAAGQKLFPYRDPFDpaSDWmdagrhtedlvelvsLFPTLAGLAGL 418
Cdd:cd16017  230 LYlhGAPYAPKEQYHVPFIIWSSDSYKQRYPVERLRANKDRPFS--HDN---------------LFHTLLGLLGI 287
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
304-367 2.36e-04

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


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 42.96  E-value: 2.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341941059 304 ASVSYLDTQVGHVLSALDDLRLAHNTIIAFTSDHGWA-LGEHGewakYSNFDVATRVPLMLYVPG 367
Cdd:cd16018  183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHG----YDNELPDMRAIFIARGPA 243
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
19-112 3.96e-03

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 39.73  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941059  19 LGSFCIALESAAQGNSATDALNILLIIVDDLRPslgcygDKLVR--SPNIDQLASHSVLFQNAfaqQAVC----APSRVS 92
Cdd:COG1524    4 GLSLLLASLLAAAAAAAPPAKKVVLILVDGLRA------DLLERahAPNLAALAARGVYARPL---TSVFpsttAPAHTT 74
                         90       100
                 ....*....|....*....|
gi 341941059  93 FLTGRRPDTTRLYDFNSYWR 112
Cdd:COG1524   75 LLTGLYPGEHGIVGNGWYDP 94
 
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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