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Conserved domains on  [gi|124174|sp|P22304|]
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RecName: Full=Iduronate 2-sulfatase; AltName: Full=Alpha-L-iduronate sulfate sulfatase; Short=Idursulfase; Contains: RecName: Full=Iduronate 2-sulfatase 42 kDa chain; Contains: RecName: Full=Iduronate 2-sulfatase 14 kDa chain; 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 ...
38-540 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: 600.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFS 117
Cdd:cd16030   4 NVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPDAV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   118 TIPQYFKENGYVTMSVGKVFHPGISsnHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANLLCPVDVLDVPEGTLP 197
Cdd:cd16030  84 TLPQYFKENGYTTAGVGKIFHPGIP--DGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   198 DKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPEVPDGLPPVAYNPWMDIRQREDVQ 277
Cdd:cd16030 162 DGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   278 ALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHV 357
Cdd:cd16030 241 ALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRV 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   358 PLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQVPPrcpvpsfhvelCREGKN 437
Cdd:cd16030 321 PLIIRAPGVTK------------------------PGKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKS 365
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   438 LLkhfrfrdleedPYL--PGNPRELIAYSQYPRPSdipqwnsdkpslkdikIMGYSIRTIDYRYTVWVgfnpdeflaNFS 515
Cdd:cd16030 366 LV-----------PLLknPSAKWKDAAFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFD 409
                       490       500
                ....*....|....*....|....*
gi 124174   516 DIHAGELYFVDSDPLQDHNMYNDSQ 540
Cdd:cd16030 410 KVGAEELYDHKNDPNEWKNLANDPE 434
 
Name Accession Description Interval E-value
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
38-540 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: 600.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFS 117
Cdd:cd16030   4 NVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPDAV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   118 TIPQYFKENGYVTMSVGKVFHPGISsnHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANLLCPVDVLDVPEGTLP 197
Cdd:cd16030  84 TLPQYFKENGYTTAGVGKIFHPGIP--DGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   198 DKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPEVPDGLPPVAYNPWMDIRQREDVQ 277
Cdd:cd16030 162 DGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   278 ALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHV 357
Cdd:cd16030 241 ALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRV 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   358 PLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQVPPrcpvpsfhvelCREGKN 437
Cdd:cd16030 321 PLIIRAPGVTK------------------------PGKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKS 365
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   438 LLkhfrfrdleedPYL--PGNPRELIAYSQYPRPSdipqwnsdkpslkdikIMGYSIRTIDYRYTVWVgfnpdeflaNFS 515
Cdd:cd16030 366 LV-----------PLLknPSAKWKDAAFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFD 409
                       490       500
                ....*....|....*....|....*
gi 124174   516 DIHAGELYFVDSDPLQDHNMYNDSQ 540
Cdd:cd16030 410 KVGAEELYDHKNDPNEWKNLANDPE 434
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
22-538 8.01e-91

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 284.08  E-value: 8.01e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    22 VALGSETQANSTTDALNVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTT 100
Cdd:COG3119   9 LALLAAAAAAAAAKRPNILFILADDLGYGdLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   101 RLYDFNSYWRVH-AGNFSTIPQYFKENGYVTMSVGKVFHpgissnHTDDspyswsfppyhpssekyentktcrgpdgELh 179
Cdd:COG3119  89 GVTDNGEGYNGGlPPDEPTLAELLKEAGYRTALFGKWHL------YLTD----------------------------LL- 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   180 anllcpvdvldvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlapdpEVPDGL 259
Cdd:COG3119 134 ----------------------TDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDI------PLPPNL 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   260 PPVAYNPWmdirqredvqalnisvpygpipvdFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWAL 339
Cdd:COG3119 186 APRDLTEE------------------------ELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSL 241
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   340 GEHG-EWAKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQV 418
Cdd:COG3119 242 GEHGlRGGKGTLYEGGIRVPLIVRWPGKIK------------------------AGSVSDALVSLIDLLPTLLDLAGVPI 297
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   419 PPRCpvpsfhvelcrEGKNLLKHFRFRDLEEDPYLpgnpreliaYSQYPRPsdipqwnsdkpslkdikIMGYSIRTIDYR 498
Cdd:COG3119 298 PEDL-----------DGRSLLPLLTGEKAEWRDYL---------YWEYPRG-----------------GGNRAIRTGRWK 340
                       490       500       510       520
                ....*....|....*....|....*....|....*....|
gi 124174   499 YTVWVGFNPDEflanfsdihagELYFVDSDPLQDHNMYND 538
Cdd:COG3119 341 LIRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
PRK13759 PRK13759
arylsulfatase; Provisional
38-420 5.29e-52

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 184.87  E-value: 5.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174     38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTT-RLydfnSYWRVHAGN 115
Cdd:PRK13759   8 NIILIMVDQMRgDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHgRV----GYGDVVPWN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    116 FS-TIPQYFKENGYVTMSVGKV-FHPGIS----SNHTDDSPYSWSFPPYHPSseKYENTKTCR--------GPDGEL--- 178
Cdd:PRK13759  84 YKnTLPQEFRDAGYYTQCIGKMhVFPQRNllgfHNVLLHDGYLHSGRNEDKS--QFDFVSDYLawlrekapGKDPDLtdi 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    179 ----HANLLCPvdvLDVPEGTLPDKQSTEQAIQLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlaPDPE 254
Cdd:PRK13759 162 gwdcNSWVARP---WDLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADI---PDPH 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    255 VPDglppvaynpWmDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSD 334
Cdd:PRK13759 235 IGD---------W-EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSD 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    335 HGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTASLPEageklfpyldpfdsasqlmepGRQSMDLVELVSLFPTLAGLA 414
Cdd:PRK13759 305 HGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGNR---------------------GTVIDQVVELRDIMPTLLDLA 363

                 ....*.
gi 124174    415 GLQVPP 420
Cdd:PRK13759 364 GGTIPD 369
Sulfatase pfam00884
Sulfatase;
38-416 5.04e-37

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 139.09  E-value: 5.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174      38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSYWRVhAGNF 116
Cdd:pfam00884   2 NVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYV-STPVGL-PRTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174     117 STIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDgelhanllcpvdvldvPEGTL 196
Cdd:pfam00884  80 PSLPDLLKRAGYNTGAIGK-WHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNC----------------SGGGV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174     197 PDKQSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpevpdglppvaynpwmdirqredv 276
Cdd:pfam00884 143 SDEALLDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKYA--------------------------------- 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174     277 qalnISVPYGpipvDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVA-- 354
Cdd:pfam00884 187 ----TFKPSS----CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNApe 258
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124174     355 --THVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGL 416
Cdd:pfam00884 259 ggYRVPLLIWSPGGKA------------------------KGQKSEALVSHVDLFPTILDLAGI 298
 
Name Accession Description Interval E-value
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
38-540 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: 600.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFS 117
Cdd:cd16030   4 NVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPDAV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   118 TIPQYFKENGYVTMSVGKVFHPGISsnHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANLLCPVDVLDVPEGTLP 197
Cdd:cd16030  84 TLPQYFKENGYTTAGVGKIFHPGIP--DGDDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAYP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   198 DKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPEVPDGLPPVAYNPWMDIRQREDVQ 277
Cdd:cd16030 162 DGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDIP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   278 ALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHV 357
Cdd:cd16030 241 ALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATRV 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   358 PLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQVPPrcpvpsfhvelCREGKN 437
Cdd:cd16030 321 PLIIRAPGVTK------------------------PGKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKS 365
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   438 LLkhfrfrdleedPYL--PGNPRELIAYSQYPRPSdipqwnsdkpslkdikIMGYSIRTIDYRYTVWVgfnpdeflaNFS 515
Cdd:cd16030 366 LV-----------PLLknPSAKWKDAAFSQYPRPS----------------IMGYSIRTERYRYTEWV---------DFD 409
                       490       500
                ....*....|....*....|....*
gi 124174   516 DIHAGELYFVDSDPLQDHNMYNDSQ 540
Cdd:cd16030 410 KVGAEELYDHKNDPNEWKNLANDPE 434
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
22-538 8.01e-91

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 284.08  E-value: 8.01e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    22 VALGSETQANSTTDALNVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTT 100
Cdd:COG3119   9 LALLAAAAAAAAAKRPNILFILADDLGYGdLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   101 RLYDFNSYWRVH-AGNFSTIPQYFKENGYVTMSVGKVFHpgissnHTDDspyswsfppyhpssekyentktcrgpdgELh 179
Cdd:COG3119  89 GVTDNGEGYNGGlPPDEPTLAELLKEAGYRTALFGKWHL------YLTD----------------------------LL- 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   180 anllcpvdvldvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlapdpEVPDGL 259
Cdd:COG3119 134 ----------------------TDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDI------PLPPNL 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   260 PPVAYNPWmdirqredvqalnisvpygpipvdFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWAL 339
Cdd:COG3119 186 APRDLTEE------------------------ELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSL 241
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   340 GEHG-EWAKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQV 418
Cdd:COG3119 242 GEHGlRGGKGTLYEGGIRVPLIVRWPGKIK------------------------AGSVSDALVSLIDLLPTLLDLAGVPI 297
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   419 PPRCpvpsfhvelcrEGKNLLKHFRFRDLEEDPYLpgnpreliaYSQYPRPsdipqwnsdkpslkdikIMGYSIRTIDYR 498
Cdd:COG3119 298 PEDL-----------DGRSLLPLLTGEKAEWRDYL---------YWEYPRG-----------------GGNRAIRTGRWK 340
                       490       500       510       520
                ....*....|....*....|....*....|....*....|
gi 124174   499 YTVWVGFNPDEflanfsdihagELYFVDSDPLQDHNMYND 538
Cdd:COG3119 341 LIRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-549 1.54e-60

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: 205.53  E-value: 1.54e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY----DFNSYWRVH 112
Cdd:cd16033   2 NILFIMTDQQRyDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLnnveNAGAYSRGL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   113 AGNFSTIPQYFKENGYVTMSVGKvFHPGissnhTDDSPYSWSFPPYHPssekYENTKtcrgpdgelhanllcpvdvldvp 192
Cdd:cd16033  82 PPGVETFSEDLREAGYRNGYVGK-WHVG-----PEETPLDYGFDEYLP----VETTI----------------------- 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   193 EGTLpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPEVP-DGLPPVAYNpwmdIR 271
Cdd:cd16033 129 EYFL-----ADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDfEDKPYIYRR----ER 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   272 QREDVQALNISVpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAK-YSN 350
Cdd:cd16033 200 KRWGVDTEDEED---------WKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKgPFM 270
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   351 FDVATHVPLIFYVPGrtaslpeageklfpyldpfdsasqLMEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCpvpsfhve 430
Cdd:cd16033 271 YEETYRIPLIIKWPG------------------------VIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKV-------- 318
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   431 lcrEGKNLLKHFRfrdlEEDPylPGNPRELIAysqyprpsdipQWNSDKPSLkdikiMGYSIRTIDYRYTvwvgFNPdef 510
Cdd:cd16033 319 ---DGRSLLPLLR----GEQP--EDWRDEVVT-----------EYNGHEFYL-----PQRMVRTDRYKYV----FNG--- 366
                       490       500       510
                ....*....|....*....|....*....|....*....
gi 124174   511 lanfSDIhaGELYFVDSDPLQDHNMYNDSQGGDLFQLLM 549
Cdd:cd16033 367 ----FDI--DELYDLESDPYELNNLIDDPEYEEILREMR 399
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
38-540 8.17e-59

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: 199.66  E-value: 8.17e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFS 117
Cdd:cd16027   2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFPLPDGVK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   118 TIPQYFKENGYVTMSVGKVFHPGissnhtdDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANllcpvdvldvpegtlP 197
Cdd:cd16027  82 TLPELLREAGYYTGLIGKTHYNP-------DAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRA---------------K 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   198 DKQsteqaiqllekmktsasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAP----DPEVpdglppvaynpwmdirqR 273
Cdd:cd16027 140 KGQ-----------------PFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPylpdTPEV-----------------R 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   274 EDVQAlnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGehgeWAKYSNFDV 353
Cdd:cd16027 186 EDLAD---------------------YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP----RAKGTLYDS 240
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   354 ATHVPLIFYVPGRTaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVPPrcpvpsfhvELcr 433
Cdd:cd16027 241 GLRVPLIVRWPGKI------------------------KPGSVSDALVSFIDLAPTLLDLAGIEPPE---------YL-- 285
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   434 EGKNLLkhfrfrDLEEDPYLPGNP-----RELIAYSQYP-RpsdipqwnsdkpslkdikimgySIRTIDYRYTvwvgFNP 507
Cdd:cd16027 286 QGRSFL------PLLKGEKDPGRDyvfaeRDRHDETYDPiR----------------------SVRTGRYKYI----RNY 333
                       490       500       510
                ....*....|....*....|....*....|...
gi 124174   508 DEFlanfsdihagELYFVDSDPLQDHNMYNDSQ 540
Cdd:cd16027 334 MPE----------ELYDLKNDPDELNNLADDPE 356
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
38-419 1.10e-57

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: 192.27  E-value: 1.10e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNF 116
Cdd:cd16022   2 NILLIMTDDLGYDdLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPPDE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   117 STIPQYFKENGYVTMSVGKvfhpgissNHtddspyswsfppyhpssekyentktcrgpdgelhanllcpvdvldvpegtl 196
Cdd:cd16022  82 PTLAELLKEAGYRTALIGK--------WH--------------------------------------------------- 102
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   197 pdkqstEQAIQLLEKMKTSAsPFFLAVGYHKPHIPFRypkefqklyplenitlapdpevpdglppvaynpwmdirqredv 276
Cdd:cd16022 103 ------DEAIDFIERRDKDK-PFFLYVSFNAPHPPFA------------------------------------------- 132
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   277 qalnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGE-WAKYSNFDVAT 355
Cdd:cd16022 133 -----------------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKKGSLYEGGI 189
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124174   356 HVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16022 190 RVPFIVRWPGK------------------------IPAGQVSDALVSLLDLLPTLLDLAGIEPP 229
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-534 6.34e-57

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: 195.48  E-value: 6.34e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLydFNSYWRVHAgNF 116
Cdd:cd16034   3 NILFIFADQHRaQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGV--FGNDVPLPP-DA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   117 STIPQYFKENGYVTMSVGKvFHpgISSNHTDDSPYSWSFPP-----------------YHPSSEKYENTktcrgpdgelh 179
Cdd:cd16034  80 PTIADVLKDAGYRTGYIGK-WH--LDGPERNDGRADDYTPPperrhgfdywkgyecnhDHNNPHYYDDD----------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   180 anllcpvDVLDVPEGTLPDKQsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRY-PKEFQKLYPLENITLAPDpevpdg 258
Cdd:cd16034 146 -------GKRIYIKGYSPDAE-TDLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRPN------ 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   259 lppvaynpwMDIRQREDVQAlnisvpygpipvdfQRKIRQsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWA 338
Cdd:cd16034 212 ---------VPEDKKEEAGL--------------REDLRG-YYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDM 267
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   339 LGEHGEWAKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAGLQV 418
Cdd:cd16034 268 LGSHGLMNKQVPYEESIRVPFIIRYPGK------------------------IKAGRVVDLLINTVDIMPTLLGLCGLPI 323
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   419 PPrcpvpsfhvelCREGKNLLKHFrfrdLEEDPYLPGNpreliAYSQYPRPSDipQWNSDKPSLKDIkimgysIRTIDYR 498
Cdd:cd16034 324 PD-----------TVEGRDLSPLL----LGGKDDEPDS-----VLLQCFVPFG--GGSARDGGEWRG------VRTDRYT 375
                       490       500       510
                ....*....|....*....|....*....|....*.
gi 124174   499 YTVWVGfnpDEFLanfsdihageLYFVDSDPLQDHN 534
Cdd:cd16034 376 YVRDKN---GPWL----------LFDNEKDPYQLNN 398
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-529 4.42e-56

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: 190.83  E-value: 4.42e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWrvhAGNF 116
Cdd:cd16037   2 NILIIMSDEHNPDaMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPY---DGDV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   117 STIPQYFKENGYVTMSVGKvfhpgissnhtddspyswsfppyhpssekyentktcrgpdgeLHANllcpvdVLDVPEGTL 196
Cdd:cd16037  79 PSWGHALRAAGYETVLIGK------------------------------------------LHFR------GEDQRHGFR 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   197 PDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdpevpdglppvaynpwmdirqredv 276
Cdd:cd16037 111 YDRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY---------------------------------- 156
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   277 qalnisvpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATH 356
Cdd:cd16037 157 ----------------VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMYEESVR 220
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   357 VPLIFYVPGRtaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCPvpsfhvelcreGK 436
Cdd:cd16037 221 VPMIISGPGI-------------------------PAGKRVKTPVSLVDLAPTILEAAGAPPPPDLD-----------GR 264
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   437 NLLkhfrfrDLEEDPYlpgnPRELIAYSQYprpsdipqwnsdkpSLKDIKIMGYSIRTIDYRYTVWVGFNPdeflanfsd 516
Cdd:cd16037 265 SLL------PLAEGPD----DPDRVVFSEY--------------HAHGSPSGAFMLRKGRWKYIYYVGYPP--------- 311
                       490
                ....*....|...
gi 124174   517 ihagELYFVDSDP 529
Cdd:cd16037 312 ----QLFDLENDP 320
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
38-548 2.19e-54

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: 189.66  E-value: 2.19e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRvhAGNF 116
Cdd:cd16031   4 NIIFILTDDHRyDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLF--DASQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   117 STIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPSSEKYENtKTCRGPDGEL-HANLLCpvdvldvpegt 195
Cdd:cd16031  82 PTYPKLLRKAGYQTAFIGK-WHLGSGGDLPPPGFDYWVSFPGQGSYYDPEF-IENGKRVGQKgYVTDII----------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   196 lpdkqsTEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAP--DPEVPDGLPPVAYNPWMDIRQR 273
Cdd:cd16031 149 ------TDKALDFLKERDKD-KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPEtfDDDDYAGRPEWAREQRNRIRGV 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   274 EDVQALNisvpygpiPVDFQRKIRQsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGeWA-KYSNFD 352
Cdd:cd16031 222 LDGRFDT--------PEKYQRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHG-LFdKRLMYE 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   353 VATHVPLIFYVPGRTaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCpvpsfhvelc 432
Cdd:cd16031 292 ESIRVPLIIRDPRLI------------------------KAGTVVDALVLNIDFAPTILDLAGVPIPEDM---------- 337
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   433 rEGKNLLKHFRFRDleedpylPGNPRE--LIAYSQYPRPSDIPQWnsdkpslkdikimgYSIRTIDYRYTVWVGFNPDEf 510
Cdd:cd16031 338 -QGRSLLPLLEGEK-------PVDWRKefYYEYYEEPNFHNVPTH--------------EGVRTERYKYIYYYGVWDEE- 394
                       490       500       510
                ....*....|....*....|....*....|....*...
gi 124174   511 lanfsdihagELYFVDSDPLQDHNMYNDSQGGDLFQLL 548
Cdd:cd16031 395 ----------ELYDLKKDPLELNNLANDPEYAEVLKEL 422
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-440 2.57e-53

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: 185.08  E-value: 2.57e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQ----QAVCAPSRVSFLTGRrpdttrlydfnSYWRVH 112
Cdd:cd16155   4 NILFILADDQRAdTIGALGNPEIQTPNLDRLARRGTSFTNAYNMggwsGAVCVPSRAMLMTGR-----------TLFHAP 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   113 AGNFS-------TIPQYFKENGYVTMSVGKvfhpgissNHTDdspyswsfppyhpssekyentktcrgpdgelHANllcp 185
Cdd:cd16155  73 EGGKAaipsddkTWPETFKKAGYRTFATGK--------WHNG-------------------------------FAD---- 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   186 vdvldvpegtlpdkqsteQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapdPEVPDGLPPVAyN 265
Cdd:cd16155 110 ------------------AAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPL---PENFLPQHPFD-N 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   266 PWMDIRqreDVQalnisvpYGPIPVDFQ--RKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHG 343
Cdd:cd16155 168 GEGTVR---DEQ-------LAPFPRTPEavRQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHG 237
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   344 EWAKYSNFDVATHVPLIFYVPGrtasLPeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQVPPRCp 423
Cdd:cd16155 238 LMGKQNLYEHSMRVPLIISGPG----IP---------------------KGKRRDALVYLQDVFPTLCELAGIEIPESV- 291
                       410
                ....*....|....*..
gi 124174   424 vpsfhvelcrEGKNLLK 440
Cdd:cd16155 292 ----------EGKSLLP 298
PRK13759 PRK13759
arylsulfatase; Provisional
38-420 5.29e-52

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 184.87  E-value: 5.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174     38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTT-RLydfnSYWRVHAGN 115
Cdd:PRK13759   8 NIILIMVDQMRgDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHgRV----GYGDVVPWN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    116 FS-TIPQYFKENGYVTMSVGKV-FHPGIS----SNHTDDSPYSWSFPPYHPSseKYENTKTCR--------GPDGEL--- 178
Cdd:PRK13759  84 YKnTLPQEFRDAGYYTQCIGKMhVFPQRNllgfHNVLLHDGYLHSGRNEDKS--QFDFVSDYLawlrekapGKDPDLtdi 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    179 ----HANLLCPvdvLDVPEGTLPDKQSTEQAIQLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlaPDPE 254
Cdd:PRK13759 162 gwdcNSWVARP---WDLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADI---PDPH 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    255 VPDglppvaynpWmDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSD 334
Cdd:PRK13759 235 IGD---------W-EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSD 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    335 HGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTASLPEageklfpyldpfdsasqlmepGRQSMDLVELVSLFPTLAGLA 414
Cdd:PRK13759 305 HGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGNR---------------------GTVIDQVVELRDIMPTLLDLA 363

                 ....*.
gi 124174    415 GLQVPP 420
Cdd:PRK13759 364 GGTIPD 369
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
37-421 2.66e-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: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 173.89  E-value: 2.66e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    37 LNVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPdttrlydfnSYWRVHAG- 114
Cdd:cd16148   1 MNVILIVIDSLRADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP---------FYHGVWGGp 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   115 ---NFSTIPQYFKENGYVTMSVGkvfhpgissnhtdDSPYSWSFPPYHPSSEKYENTktcRGPDGElhanllcpvdvlDV 191
Cdd:cd16148  72 lepDDPTLAEILRKAGYYTAAVS-------------SNPHLFGGPGFDRGFDTFEDF---RGQEGD------------PG 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   192 PEGTLPDKQSTEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYpkefqklyplenitlapDpevpdglppvaynpwmdir 271
Cdd:cd16148 124 EEGDERAERVTDRALEWLDRNADD-DPFFLFLHYFDPHEPYLY-----------------D------------------- 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   272 qredvqalnisvpygpipvdfqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAK-YSN 350
Cdd:cd16148 167 ------------------------------AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGhGSN 216
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124174   351 F-DVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVPPR 421
Cdd:cd16148 217 LyDEQLHVPLIIRWPGK-------------------------EPGKRVDALVSHIDIAPTLLDLLGVEPPDY 263
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-418 5.79e-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: 171.02  E-value: 5.79e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRP-SLGCYGDKL----------VRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFN 106
Cdd:cd16153   3 NILWIITDDQRVdSLSCYNNAHtgksesrlgyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   107 SYWRVHAGNFSTIPQYFKENGYVTMSVGKvfhpgissnhtddspyswsfppyhpssEKYENtktcrgpdgelhanllcPV 186
Cdd:cd16153  83 AAHPALDHGLPTFPEVLKKAGYQTASFGK---------------------------SHLEA-----------------FQ 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   187 DVLDVPEgtlpdkQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFqklyplenitlapdpevpdglppvaynp 266
Cdd:cd16153 119 RYLKNAN------QSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEF---------------------------- 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   267 wmdiRQREDvqalnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLAN---STIIAFTSDHGWALGEHG 343
Cdd:cd16153 165 ----RDRFD------------------------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQG 216
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124174   344 EWAKYSNFDVATHVPLIFYVPGRtaslpeageKLFPyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQV 418
Cdd:cd16153 217 ILAKFTFWPQSHRVPLIVVSSDK---------LKAP-------------AGKVRHDFVEFVDLAPTLLAAAGVDV 269
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
37-466 1.43e-48

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: 171.22  E-value: 1.43e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    37 LNVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfnsywrvHAGN 115
Cdd:cd16032   1 PNILLIMADQLTAAaLPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYD-------NAAE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   116 FS----TIPQYFKENGYVTMSVGKVfhpgissnHtddspyswsFPpyhpssekyentktcrGPDgELHanllcpvdvldv 191
Cdd:cd16032  74 FPadipTFAHYLRAAGYRTALSGKM--------H---------FV----------------GPD-QLH------------ 107
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   192 peGTLPDKQSTEQAIQLLEKMKTSAS--PFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdpevpdglppvaynpwmd 269
Cdd:cd16032 108 --GFDYDEEVAFKAVQKLYDLARGEDgrPFFLTVSFTHPHDPYVIPQEYWDLY--------------------------- 158
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   270 irqredvqalnisvpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYS 349
Cdd:cd16032 159 -----------------------VRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMS 215
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   350 NFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSmDLVELVSLFPTLAGLAGLQVPPRCPVPsfhv 429
Cdd:cd16032 216 FFEGSARVPLIISAPGRFA------------------------PRRVA-EPVSLVDLLPTLVDLAGGGTAPHVPPL---- 266
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 124174   430 elcrEGKNLLKHFRFRDleedpylPGNPREliAYSQY 466
Cdd:cd16032 267 ----DGRSLLPLLEGGD-------SGGEDE--VISEY 290
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
38-420 8.05e-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: 171.57  E-value: 8.05e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNF 116
Cdd:cd16144   2 NIVLILVDDLgWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDNT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   117 S---------------TIPQYFKENGYVTMSVGKvFHPGISSNHT--------DDSPYSWSFPPYHPSSEKYENTKTCRG 173
Cdd:cd16144  82 KlipppsttrlpleevTIAEALKDAGYATAHFGK-WHLGGEGGYGpedqgfdvNIGGTGNGGPPSYYFPPGKPNPDLEDG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   174 PDGElHanllcPVDVLdvpegtlpdkqsTEQAIQLLEkmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdP 253
Cdd:cd16144 161 PEGE-Y-----LTDRL------------TDEAIDFIE--QNKDKPFFLYLSHYAVHTPIQARPELIEKY----------E 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   254 EVPDGLPPVAYNPwmdirqredvqalnisvpygpipvdfqrkirqSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTS 333
Cdd:cd16144 211 KKKKGLRKGQKNP--------------------------------VYAAMIESLDESVGRILDALEELGLADNTLVIFTS 258
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   334 DHGwALGEHGEWA---------KYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELV 404
Cdd:cd16144 259 DNG-GLSTRGGPPtsnaplrggKGSLYEGGIRVPLIVRWPGVIK------------------------PGSVSDVPVIGT 313
                       410
                ....*....|....*.
gi 124174   405 SLFPTLAGLAGLQVPP 420
Cdd:cd16144 314 DLYPTFLELAGGPLPP 329
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-540 8.65e-48

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: 171.65  E-value: 8.65e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNF 116
Cdd:cd16150   2 NIVIFVADQLRAdSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPDEPNL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   117 StipQYFKENGYVTMSVGKvfhpgissNHTDDSPYSWsfppyhpssEKYEntktcrgpdgelhanllcpvdvldvpegtL 196
Cdd:cd16150  82 L---KTLKDAGYHVAWAGK--------NDDLPGEFAA---------EAYC-----------------------------D 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   197 PDKQSTEQAIQLLEKMKTSAsPFFLAVGYHKPHIPFRYPKEFQKLYPLEnitLAPdPEVPDGLPpvAYNPWMDIRQREDv 276
Cdd:cd16150 113 SDEACVRTAIDWLRNRRPDK-PFCLYLPLIFPHPPYGVEEPWFSMIDRE---KLP-PRRPPGLR--AKGKPSMLEGIEK- 184
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   277 QALNisvpygPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSN-F-DVA 354
Cdd:cd16150 185 QGLD------RWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNtFeDCL 258
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   355 THVPLIFYVPGRTaslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQVPPrcpvPSFhvelcre 434
Cdd:cd16150 259 TRVPLIIKPPGGP-------------------------AGGVSDALVELVDIPPTLLDLAGIPLSH----THF------- 302
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   435 GKNLLKHFRFRDLEEDPY-------LPGNPReliAYSQYPRPSDIPQWNS---DKPSLKDIKIMgysIRTIDYRYtVWVG 504
Cdd:cd16150 303 GRSLLPVLAGETEEHRDAvfseggrLHGEEQ---AMEGGHGPYDLKWPRLlqqEEPPEHTKAVM---IRTRRYKY-VYRL 375
                       490       500       510
                ....*....|....*....|....*....|....*.
gi 124174   505 FNPDeflanfsdihagELYFVDSDPLQDHNMYNDSQ 540
Cdd:cd16150 376 YEPD------------ELYDLEADPLELHNLIGDPA 399
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
38-469 4.04e-47

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: 170.52  E-value: 4.04e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRrpdttrlYDFN--SYWR---V 111
Cdd:cd16028   2 NVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGR-------YLMNhrSVWNgtpL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   112 HAGnFSTIPQYFKENGYVTMSVGKvfhpgissnhTDDSPYSWSFPPYHPSSEKYENtktcrgpdgelhanLLCPVDVLDV 191
Cdd:cd16028  75 DAR-HLTLALELRKAGYDPALFGY----------TDTSPDPRGLAPLDPRLLSYEL--------------AMPGFDPVDR 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   192 PEGtLPDKQS-----TEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITL---APDPEVPDGLPPVa 263
Cdd:cd16028 130 LDE-YPAEDSdtaflTDRAIEYLDERQDE--PWFLHLSYIRPHPPFVAPAPYHALYDPADVPPpirAESLAAEAAQHPL- 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   264 YNPWMDIRQREDVQALNISVPYGPIPVdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHG 343
Cdd:cd16028 206 LAAFLERIESLSFSPGAANAADLDDEE--VAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHW 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   344 EWAKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfDSASqlmepGRQSMDLVELVSLFPTLAGLAGLQVPPRCp 423
Cdd:cd16028 284 LWGKDGFFDQAYRVPLIVRDPRREA----------------DATR-----GQVVDAFTESVDVMPTILDWLGGEIPHQC- 341
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 124174   424 vpsfhvelcrEGKNLLKHfrfrdLEEDPylPGNPRELIAYSQYPRP 469
Cdd:cd16028 342 ----------DGRSLLPL-----LAGAQ--PSDWRDAVHYEYDFRD 370
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
38-419 2.69e-42

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: 156.18  E-value: 2.69e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAG-- 114
Cdd:cd16026   3 NIVVILADDLGYGdLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGGlp 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   115 -NFSTIPQYFKENGYVTMSVGKvFHPGISSNH--TD---DS----PYS---WSFPPYHPSSEKYEntktcrgpdgelhAN 181
Cdd:cd16026  83 pDEITIAEVLKKAGYRTALVGK-WHLGHQPEFlpTRhgfDEyfgiPYSndmWPFPLYRNDPPGPL-------------PP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   182 LLCPVDVLDVPegtlPD-----KQSTEQAIQLLEKMKTsaSPFFLAVGYHKPHIPFRYPKEFqklyplENITLApdpevp 256
Cdd:cd16026 149 LMENEEVIEQP----ADqssltQRYTDEAVDFIERNKD--QPFFLYLAHTMPHVPLFASEKF------KGRSGA------ 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   257 dGLppvaynpwmdirqredvqalnisvpYGpipvdfqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:cd16026 211 -GL-------------------------YG---------------DVVEELDWSVGRILDALKELGLEENTLVIFTSDNG 249
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   337 WALGEHGEW--------AKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFP 408
Cdd:cd16026 250 PWLEYGGHGgsagplrgGKGTTWEGGVRVPFIAWWPGV------------------------IPAGTVSDELASTMDLLP 305
                       410
                ....*....|.
gi 124174   409 TLAGLAGLQVP 419
Cdd:cd16026 306 TLAALAGAPLP 316
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-427 2.49e-41

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: 149.31  E-value: 2.49e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRV----- 111
Cdd:cd16149   2 NILFILTDDQGPwALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHgktkk 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   112 ---HAGNFSTIPQYFKENGYVTMSVGKvFHPGissnhtddspyswsfppyhpssekyentktcrgpdgelhanllcpvdv 188
Cdd:cd16149  82 pegYLEGQTTLPEVLQDAGYRCGLSGK-WHLG------------------------------------------------ 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   189 ldvpegtlpdkqstEQAIQLLEKMKTSASPFFLAVGYHKPHipfrypkefqklyplenitlapdpevpdglppvayNPWm 268
Cdd:cd16149 113 --------------DDAADFLRRRAEAEKPFFLSVNYTAPH-----------------------------------SPW- 142
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   269 dirqredvqalnisvpygpipvdfqrkirqSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAK- 347
Cdd:cd16149 143 ------------------------------GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKg 192
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   348 -----YSNFDVATHVPLIFYVPGRTaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVP--P 420
Cdd:cd16149 193 ngtfpLNMYDNSVKVPFIIRWPGVV------------------------PAGRVVDSLVSAYDFFPTLLELAGVDPPadP 248

                ....*..
gi 124174   421 RCPVPSF 427
Cdd:cd16149 249 RLPGRSF 255
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
38-534 7.95e-40

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


Pssm-ID: 293765 [Multi-domain]  Cd Length: 409  Bit Score: 149.62  E-value: 7.95e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNaFAQQAVCAPSRVSFLTGRRPDTTRLydfnsyWRVHAG-- 114
Cdd:cd16146   2 NVILILTDDQgYGDLGFHGNPILKTPNLDRLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRTGV------WHTILGre 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   115 ----NFSTIPQYFKENGYVTMSVGKvFHPGissnhtDDSPY----------------SWSFPPYHPSSEKYENTKTCRGP 174
Cdd:cd16146  75 rmrlDETTLAEVFKDAGYRTGIFGK-WHLG------DNYPYrpqdrgfdevlghgggGIGQYPDYWGNDYFDDTYYHNGK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   175 ----DGelhanlLCPvDVLdvpegtlpdkqsTEQAIQLLEKMKTsaSPFFLAVGYHKPHIPFRYPKEFQKLYplenitla 250
Cdd:cd16146 148 fvktEG------YCT-DVF------------FDEAIDFIEENKD--KPFFAYLATNAPHGPLQVPDKYLDPY-------- 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   251 PDPEVPDGlppvaynpwmdirqredvqalnisvpygpipvdfqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIA 330
Cdd:cd16146 199 KDMGLDDK--------------------------------------LAAFYGMIENIDDNVGRLLAKLKELGLEENTIVI 240
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   331 FTSDHGWALGEHGEW------AKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELV 404
Cdd:cd16146 241 FMSDNGPAGGVPKRFnagmrgKKGSVYEGGHRVPFFIRWPGKIL------------------------AGKDVDTLTAHI 296
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   405 SLFPTLAGLAGLQVPPrcpvpsfHVELcrEGKNLLKhfrfrdLEEDPYLPGNPRELIAYSQYPRPSDIPQWNSdkpslkd 484
Cdd:cd16146 297 DLLPTLLDLCGVKLPE-------GIKL--DGRSLLP------LLKGESDPWPERTLFTHSGRWPPPPKKKRNA------- 354
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|
gi 124174   485 ikimgySIRTIDYRYTVWVGFNPdeflanfsdihagELYFVDSDPLQDHN 534
Cdd:cd16146 355 ------AVRTGRWRLVSPKGFQP-------------ELYDIENDPGEEND 385
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
38-421 2.99e-39

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


Pssm-ID: 293764 [Multi-domain]  Cd Length: 415  Bit Score: 148.13  E-value: 2.99e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSY---WRVHA 113
Cdd:cd16145   2 NIIFILADDLGYGdLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPggqDPLPP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   114 GNfSTIPQYFKENGYVTMSVGKVfhpGISSNHTDDSPYS----------------WSFPPYhpsseKYENTKTcrgpdgE 177
Cdd:cd16145  82 DD-VTLAEVLKKAGYATAAFGKW---GLGGPGTPGHPTKqgfdyfygyldqvhahNYYPEY-----LWRNGEK------V 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   178 LHANLLCPVDVLDVPEGTLPDKQS----TEQAIQLLEKMKtsASPFFLAVGYHKPHIPFRYPKefqklyplenitLAPDP 253
Cdd:cd16145 147 PLPNNVIPPLDEGNNAGGGGGTYShdlfTDEALDFIRENK--DKPFFLYLAYTLPHAPLQVPD------------DGPYK 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   254 EVPDGLPPVAYNPWMDIRQRedvqalnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTS 333
Cdd:cd16145 213 YKPKDPGIYAYLPWPQPEKA--------------------------YAAMVTRLDRDVGRILALLKELGIDENTLVVFTS 266
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   334 DHGwALGEHGEWAKYSNFDVA--------------THVPLIFYVPGRTaslpeageklfpyldpfdsasqlmEPGRQSMD 399
Cdd:cd16145 267 DNG-PHSEGGSEHDPDFFDSNgplrgykrslyeggIRVPFIARWPGKI------------------------PAGSVSDH 321
                       410       420
                ....*....|....*....|..
gi 124174   400 LVELVSLFPTLAGLAGLQVPPR 421
Cdd:cd16145 322 PSAFWDFMPTLADLAGAEPPED 343
Sulfatase pfam00884
Sulfatase;
38-416 5.04e-37

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 139.09  E-value: 5.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174      38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSYWRVhAGNF 116
Cdd:pfam00884   2 NVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYV-STPVGL-PRTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174     117 STIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDgelhanllcpvdvldvPEGTL 196
Cdd:pfam00884  80 PSLPDLLKRAGYNTGAIGK-WHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNC----------------SGGGV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174     197 PDKQSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpevpdglppvaynpwmdirqredv 276
Cdd:pfam00884 143 SDEALLDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKYA--------------------------------- 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174     277 qalnISVPYGpipvDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVA-- 354
Cdd:pfam00884 187 ----TFKPSS----CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNApe 258
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124174     355 --THVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGL 416
Cdd:pfam00884 259 ggYRVPLLIWSPGGKA------------------------KGQKSEALVSHVDLFPTILDLAGI 298
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-534 7.77e-36

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


Pssm-ID: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 137.73  E-value: 7.77e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAqQAVCAPSRVSFLTGRRPDTTrlYDFNSYWrvHAGNf 116
Cdd:cd16151   2 NIILIMADDLGYeCIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRN--YVVFGYL--DPKQ- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   117 STIPQYFKENGYVTMSVGKvfhPGISSNhTDDSPYS-------WSFPPYHPSSEKYENTKTcrgPDGELHANllcpVDVL 189
Cdd:cd16151  76 KTFGHLLKDAGYATAIAGK---WQLGGG-RGDGDYPhefgfdeYCLWQLTETGEKYSRPAT---PTFNIRNG----KLLE 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   190 DVPEGTLPDkQSTEQAIQLLEKMKtsASPFFLavgY------HKPHIPFrypkefqklyplenitlaPDPEvpdglppva 263
Cdd:cd16151 145 TTEGDYGPD-LFADFLIDFIERNK--DQPFFA---YypmvlvHDPFVPT------------------PDSP--------- 191
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   264 ynPWMDIRQRedvqalnisvpygpipvdfqRKIRQSYF-ASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEH 342
Cdd:cd16151 192 --DWDPDDKR--------------------KKDDPEYFpDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPIT 249
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   343 GEW-------AKYSNFDVATHVPLIFYVPGrtaslpeageklfpyldpfdsasqLMEPGRQSMDLVELVSLFPTLAGLAG 415
Cdd:cd16151 250 SRTngrevrgGKGKTTDAGTHVPLIVNWPG------------------------LIPAGGVSDDLVDFSDFLPTLAELAG 305
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   416 LQVPPRCPVpsfhvelcrEGKNLLkhfrfrdleedPYL---PGNPRELIAYsqyprpsdipqWNSDKPSLKDIKimgYSI 492
Cdd:cd16151 306 APLPEDYPL---------DGRSFA-----------PQLlgkTGSPRREWIY-----------WYYRNPHKKFGS---RFV 351
                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 124174   493 RTIDYRYtvwvgfnpdeflanFSDihaGELYFVDSDPLQDHN 534
Cdd:cd16151 352 RTKRYKL--------------YAD---GRFFDLREDPLEKNP 376
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
38-536 1.16e-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: 131.94  E-value: 1.16e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRP-SLGCYGDK-LVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRrpdttrlYDFNSY--WRVhA 113
Cdd:cd16143   2 NIVIILADDLGYgDISCYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGR-------YPWRSRlkGGV-L 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   114 GNFS---------TIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDgelHANLLC 184
Cdd:cd16143  74 GGFSppliepdrvTLAKMLKQAGYRTAMVGK-WHLGLDWKKKDGKKAATGTGKDVDYSKPIKGGPLDHGFD---YYFGIP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   185 PVDVLDvpegTLpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKlyplenitlapdpevpdglppvay 264
Cdd:cd16143 150 ASEVLP----TL-----TDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQG------------------------ 196
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   265 npwmdirqredVQALNisvPYGpipvDFqrkIRQsyfasvsyLDTQVGRLLSALDDLQLANSTIIAFTSDHG-------W 337
Cdd:cd16143 197 -----------KSGAG---PYG----DF---VYE--------LDWVVGRILDALKELGLAENTLVIFTSDNGpspyadyK 247
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   338 ALGEHGEWA-------KYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTL 410
Cdd:cd16143 248 ELEKFGHDPsgplrgmKADIYEGGHRVPFIVRWPGKIP------------------------AGSVSDQLVSLTDLFATL 303
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   411 AGLAGLQVPPRCPVPSFhvelcregkNLLkhfrfrdleedPYLPGNPreliaySQYPRPSDIPQWNSDkpslkdikimGY 490
Cdd:cd16143 304 AAIVGQKLPDNAAEDSF---------SFL-----------PALLGPK------KQEVRESLVHHSGNG----------SF 347
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*...
gi 124174   491 SIRTIDYRYTVWVGF--NPDEFLANFSDIHAGELYFVDSDPLQDHNMY 536
Cdd:cd16143 348 AIRKGDWKLIDGTGSggFSYPRGKEKLGLPPGQLYNLSTDPGESNNLY 395
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
38-452 2.94e-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: 132.12  E-value: 2.94e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTtrlydfNSYWR---VHA 113
Cdd:cd16156   2 QFIFIMTDTQRWDmVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHT------NGSWTncmALG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   114 GNFSTIPQYFKENGYVTMSVGK-------VFHPGISSNHTDdSPYSWSFPPYHPSSEKYENTKTCRGPDgELHANllcpv 186
Cdd:cd16156  76 DNVKTIGQRLSDNGIHTAYIGKwhldggdYFGNGICPQGWD-PDYWYDMRNYLDELTEEERRKSRRGLT-SLEAE----- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   187 dvlDVPEGTLPDKQSTEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYplENITLAPDPEVPDGLP--PVAY 264
Cdd:cd16156 149 ---GIKEEFTYGHRCTNRALDFIEKHKDE--DFFLVVSYDEPHHPFLCPKPYASMY--KDFEFPKGENAYDDLEnkPLHQ 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   265 NPWMDIRQREDVQALNISVPYgpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLqLANSTIIaFTSDHGWALGEHGE 344
Cdd:cd16156 222 RLWAGAKPHEDGDKGTIKHPL--------------YFGCNSFVDYEIGRVLDAADEI-AEDAWVI-YTSDHGDMLGAHKL 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   345 WAK-YSNFDVATHVPLIFYVPGrtaslpeaGEKLFPYLD-PfdsasqlmepgrqsmdlVELVSLFPTLAGLAGLQVPPRC 422
Cdd:cd16156 286 WAKgPAVYDEITNIPLIIRGKG--------GEKAGTVTDtP-----------------VSHIDLAPTILDYAGIPQPKVL 340
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124174   423 P----VPSFHVELCREGK----------------------------------NLLKHFRFRDLEEDPY 452
Cdd:cd16156 341 EgesiLATIEDPEIPENRgvfvefgryevdhdgfggfqpvrcvvdgryklviNLLSTDELYDLEKDPY 408
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-539 9.59e-33

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


Pssm-ID: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 128.89  E-value: 9.59e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRP-SLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSywRVHAGNF 116
Cdd:cd16152   3 NVIVFFTDQQRWdTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFR-NG--IPLPADE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   117 STIPQYFKENGYVTMSVGKvfhpgissnhtddspysWSFPPYHpssekyentktcrgpdgelhanllcpVDVLdvpegtl 196
Cdd:cd16152  80 KTLAHYFRDAGYETGYVGK-----------------WHLAGYR--------------------------VDAL------- 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   197 pdkqsTEQAIQLLEKmKTSASPFFLAVGYHKPHIP---FRY--PKEFQKLYplenitlaPDPEVPdglppvaynpwmdir 271
Cdd:cd16152 110 -----TDFAIDYLDN-RQKDKPFFLFLSYLEPHHQndrDRYvaPEGSAERF--------ANFWVP--------------- 160
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   272 qrEDVQALnisvpygpiPVDFQRKIrQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHgwalGEH-----GEWa 346
Cdd:cd16152 161 --PDLAAL---------PGDWAEEL-PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHfrtrnAEY- 223
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   347 KYSNFDVATHVPLIFYVPGrtaslpeageklfpyldpFDSasqlmepGRQSMDLVELVSLFPTLAGLAGLQVPprcpvPS 426
Cdd:cd16152 224 KRSCHESSIRVPLVIYGPG------------------FNG-------GGRVEELVSLIDLPPTLLDAAGIDVP-----EE 273
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   427 FHvelcreGKNLLkhfrfrdleedpylpgnprELIAYSQYPRPSDIPqwnsdkpslkdIKI----MGYSIRTIDYRYTVw 502
Cdd:cd16152 274 MQ------GRSLL-------------------PLVDGKVEDWRNEVF-----------IQIsesqVGRAIRTDRWKYSV- 316
                       490       500       510
                ....*....|....*....|....*....|....*...
gi 124174   503 VGFNPDEFLANFSDIHAGE-LYFVDSDPLQDHNMYNDS 539
Cdd:cd16152 317 AAPDKDGWKDSGSDVYVEDyLYDLEADPYELVNLIGRP 354
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
38-424 1.00e-32

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: 129.21  E-value: 1.00e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAQQaVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAG-- 114
Cdd:cd16029   2 HIVFILADDLGWNdVGFHGSDQIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGRYPIHTGMQHGVILAGEPYGlp 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   115 -NFSTIPQYFKENGYVTMSVGKvFHPGISS-NHTD-----DSPYSwsfppYHPSSEKYENTKTCRGPDgelhanllCPVD 187
Cdd:cd16029  81 lNETLLPQYLKELGYATHLVGK-WHLGFYTwEYTPtnrgfDSFYG-----YYGGAEDYYTHTSGGAND--------YGND 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   188 VLDVPEGTLPDKQS-------TEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpevpdglp 260
Cdd:cd16029 147 DLRDNEEPAWDYNGtystdlfTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYE----------------- 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   261 pvaynpwmdirqredVQALNISvpygpipvDFQRKIrqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGwALG 340
Cdd:cd16029 209 ---------------DKFAHIK--------DEDRRT---YAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG-GPT 261
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   341 EHGEWAkySNFdvathvPLifyvPGRTASLPEAGEKlfpyLDPFDSASQL-MEPGRQSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16029 262 GGGDGG--SNY------PL----RGGKNTLWEGGVR----VPAFVWSPLLpPKRGTVSDGLMHVTDWLPTLLSLAGGDPD 325

                ....*
gi 124174   420 PRCPV 424
Cdd:cd16029 326 DLPPL 330
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
38-452 3.21e-31

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: 124.97  E-value: 3.21e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPSLGCYGD--KLVRspnidQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPD----TTRLYDFNSYWRV 111
Cdd:cd16147   3 NIVLILTDDQDVELGSMDPmpKTKK-----LLADQGTTFTNAFVTTPLCCPSRASILTGQYAHnhgvTNNSPPGGGYPKF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   112 HAGNF--STIPQYFKENGYVTMSVGKVFHpGISSNHTDDSP---YSWSFPPYHPSseKYENTKTCRGPDGELHANllCPV 186
Cdd:cd16147  78 WQNGLerSTLPVWLQEAGYRTAYAGKYLN-GYGVPGGVSYVppgWDEWDGLVGNS--TYYNYTLSNGGNGKHGVS--YPG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   187 ----DVLdvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPleNITLAP-----DPEVPD 257
Cdd:cd16147 153 dyltDVI------------ANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFP--NVTAPPrpppnNPDVSD 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   258 G--------LPPVAYNPWMDIRQREDVQALnisvpygpipvdfqrkirqsyfASVsylDTQVGRLLSALDDLQLANSTII 329
Cdd:cd16147 219 KphwlrrlpPLNPTQIAYIDELYRKRLRTL----------------------QSV---DDLVERLVNTLEATGQLDNTYI 273
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   330 AFTSDHGWALGEHG-EWAKYSNFDVATHVPLIFYVPGrtasLPeageklfpyldpfdsasqlmePGRQSMDLVELVSLFP 408
Cdd:cd16147 274 IYTSDNGYHLGQHRlPPGKRTPYEEDIRVPLLVRGPG----IP---------------------AGVTVDQLVSNIDLAP 328
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 124174   409 TLAGLAGLQVPP--------RCPVPSFH-VELCREGKNLLKHF---RFR---DLEEDPY 452
Cdd:cd16147 329 TILDLAGAPPPSdmdgrscgDSNNNTYKcVRTVDDTYNLLYFEwctGFRelyDLTTDPY 387
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
38-420 5.86e-31

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: 123.80  E-value: 5.86e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPS-LGCYGDKLVR---SPNIDQLASHSLLFQNAFAQQAvCAPSRVSFLTGRRPDTTRLYdfnsywRV-- 111
Cdd:cd16142   2 NILVILGDDIGWGdLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLT------TVgl 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   112 -HAGNF-----STIPQYFKENGYVTMSVGKvfhpgissNHTDDSPYSWsfPpyhpssekyentkTCRGPDgELHANLLcp 185
Cdd:cd16142  75 pGSPGGlppwePTLAELLKDAGYATAQFGK--------WHLGDEDGRL--P-------------TDHGFD-EFYGNLY-- 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   186 vdvldvpegTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpevpdglppvAYN 265
Cdd:cd16142 129 ---------HTIDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSS-------------------GKG 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   266 PWMDirqredvqalnisvpygpipvdfqrkirqsyfaSVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG-----WALG 340
Cdd:cd16142 181 KYAD---------------------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDG 227
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   341 EHGEW--AKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAGLQV 418
Cdd:cd16142 228 GYTPFrgEKGTTWEGGVRVPAIVRWPGK------------------------IKPGRVSNEIVSHLDWFPTLAALAGAPD 283

                ..
gi 124174   419 PP 420
Cdd:cd16142 284 PK 285
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
38-419 7.41e-29

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: 118.31  E-value: 7.41e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPS-LGCYGDkLVRSPNIDQLASHSLLFQNaFAQQAVCAPSRVSFLTGRRP-------DTTRLYDFNSYW 109
Cdd:cd16025   4 NILLILADDLGFSdLGCFGG-EIPTPNLDALAAEGLRFTN-FHTTALCSPTRAALLTGRNHhqvgmgtMAELATGKPGYE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   110 RVHAGNFSTIPQYFKENGYVTMSVGKvfhpgissnhtddspysW--SFPPYHpSSEKYentktcrgpdgelhanllcpvd 187
Cdd:cd16025  82 GYLPDSAATIAEVLKDAGYHTYMSGK-----------------WhlGPDDYY-STDDL---------------------- 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   188 vldvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEF----------------------QK---LY 242
Cdd:cd16025 122 --------------TDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkykgkydagwdalreerlerQKelgLI 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   243 PlENITLAP-DPEVPdglppvaynPWMDIRQRE-DVQALNISVpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDD 320
Cdd:cd16025 188 P-ADTKLTPrPPGVP---------AWDSLSPEEkKLEARRMEV----------------YAAMVEHMDQQIGRLIDYLKE 241
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   321 LQLANSTIIAFTSDHGwALGEHGeWAKYSN-----FDVATH-----VPLIfyvpgrtASLPEAGEKlfpyldpfdsasql 390
Cdd:cd16025 242 LGELDNTLIIFLSDNG-ASAEPG-WANASNtpfrlYKQASHeggirTPLI-------VSWPKGIKA-------------- 298
                       410       420
                ....*....|....*....|....*....
gi 124174   391 mePGRQSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16025 299 --KGGIRHQFAHVIDIAPTILELAGVEYP 325
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-416 1.30e-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: 113.07  E-value: 1.30e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYD-FNSYWRVHAGN 115
Cdd:cd16035   2 NILLILTDQERyPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDtLGSPMQPLLSP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   116 -FSTIPQYFKENGYVTMSVGKvfhpgissnhtddspysWsfppyHPSSekyentktcrgpdgelHANllcpvdvldvpEG 194
Cdd:cd16035  82 dVPTLGHMLRAAGYYTAYKGK-----------------W-----HLSG----------------AAG-----------GG 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   195 TLPDKQSTEQAIQLLEKMKTSAS---PFFLAVGYHKPHipfrypkefqklyplenitlapdpevpdglppvaynpwmdir 271
Cdd:cd16035 113 YKRDPGIAAQAVEWLRERGAKNAdgkPWFLVVSLVNPH------------------------------------------ 150
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   272 qreDVQalnisvpYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSN- 350
Cdd:cd16035 151 ---DIM-------FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNa 220
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124174   351 FDVATHVPLIFYVPGrtaslpeagekLFPyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGL 416
Cdd:cd16035 221 YEEALHVPLIISHPD-----------LFG-------------TGQTTDALTSHIDLLPTLLGLAGV 262
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
38-420 2.99e-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: 104.55  E-value: 2.99e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPSLGCY-GDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRlyDFNSYWRVHAgNF 116
Cdd:cd16171   2 NVVMVMSDSFDGRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTE--SWNNYKGLDP-NY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   117 STIPQYFKENGYVTMSVGKVFHpgiSSNHtddspyswsfppyHPSSEKYE----NTKTCRGPDGELHANLLCPVDVLDVp 192
Cdd:cd16171  79 PTWMDRLEKHGYHTQKYGKLDY---TSGH-------------HSVSNRVEawtrDVPFLLRQEGRPTVNLVGDRSTVRV- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   193 egTLPDKQSTEQAIQLLEKMKTSAS-PFFLAVGYHKPHiPFRYPkefqklypleniTLAPDpevpdglppvaynpwmdir 271
Cdd:cd16171 142 --MLKDWQNTDKAVHWIRKEAPNLTqPFALYLGLNLPH-PYPSP------------SMGEN------------------- 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   272 qredvqalnisvpYGPIpvdfqRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNF 351
Cdd:cd16171 188 -------------FGSI-----RNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMY 249
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124174   352 DVATHVPLIFYVPGrtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAGLQVPP 420
Cdd:cd16171 250 EGSSHVPLLIMGPG-------------------------IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
38-419 6.55e-22

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: 99.28  E-value: 6.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYwRV----- 111
Cdd:cd16159   3 NIVLFMADDLGiGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGM-RVilfta 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   112 -HAG---NFSTIPQYFKENGYVTMSVGKvFHPGISSNHTDDSpyswsfpPYHPSSEKYE--------NTKTCRGPDGElh 179
Cdd:cd16159  82 sSGGlppNETTFAEVLKQQGYSTALIGK-WHLGLHCESRNDF-------CHHPLNHGFDyfyglpltNLKDCGDGSNG-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   180 ANLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKL--------------YPLE 245
Cdd:cd16159 152 EYDLSFDPLFPLLTAFVLITALTIFLLLYLGAVSKRFFVFLLILSLLFISLFFLLLITNRYFncilmrnhevveqpMSLE 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   246 NITLAPDPEVPDGL------PPVAYNPWmdirqredvqaLNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALD 319
Cdd:cd16159 232 NLTQRLTKEAISFLernkerPFLLVMSF-----------LHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALD 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   320 DLQLANSTIIAFTSDHGWAL------GEHGEW-------AKYSNFDVATHVPLIFYVPGRtasLPeageklfpyldpfdS 386
Cdd:cd16159 301 ELGLKDNTFVYFTSDNGGHLeeisvgGEYGGGnggiyggKKMGGWEGGIRVPTIVRWPGV---IP--------------P 363
                       410       420       430
                ....*....|....*....|....*....|...
gi 124174   387 ASQLMEPGRQsMDlvelvsLFPTLAGLAGLQVP 419
Cdd:cd16159 364 GSVIDEPTSL-MD------IFPTVAALAGAPLP 389
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
38-420 1.23e-19

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: 90.99  E-value: 1.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLR-PSLGCYGDKLVR-SPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDfNSYWRVHAG- 114
Cdd:cd16161   3 NFLLLFADDLGwGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGH-NFLPTSVGGl 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   115 --NFSTIPQYFKENGYVTMSVGKvFHPGissnHTDdspyswsfpPYHPSSekyentktcRGPDgelhanllcpvDVLDVP 192
Cdd:cd16161  82 plNETTLAEVLRQAGYATGMIGK-WHLG----QRE---------AYLPNS---------RGFD-----------YYFGIP 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   193 ---EGTLPDKQStEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQklyplenitlapdpevpdglppvaynpwmd 269
Cdd:cd16161 128 fshDSSLADRYA-QFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQ------------------------------ 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   270 irqredvQALNISVPYGpipvdfqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG-WALG-------E 341
Cdd:cd16161 177 -------SPTSGRGPYG---------------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpWEVKcelavgpG 234
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   342 HGEW--------AKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGL 413
Cdd:cd16161 235 TGDWqgnlggsvAKASTWEGGHREPAIVYWPGR------------------------IPANSTSAALVSTLDIFPTVVAL 290

                ....*..
gi 124174   414 AGLQVPP 420
Cdd:cd16161 291 AGASLPP 297
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
38-419 2.77e-19

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: 90.97  E-value: 2.77e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAG-- 114
Cdd:cd16158   3 NIVLLFADDLgYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGGlp 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   115 -NFSTIPQYFKENGYVTMSVGKvFHPGISSN-----------HTDDSPYSWSFPPYHPSSEKYENTK---TCRgpDGELH 179
Cdd:cd16158  83 lNETTIAEVLKTVGYQTAMVGK-WHLGVGLNgtylpthqgfdHYLGIPYSHDQGPCQNLTCFPPNIPcfgGCD--QGEVP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   180 ANLLCPVDVLDVPeGTLPD--KQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQklyplenitlapdpevpd 257
Cdd:cd16158 160 CPLFYNESIVQQP-VDLLTleERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFA------------------ 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   258 glppvaynpwmdirqredvqalnisvpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGW 337
Cdd:cd16158 221 -----------------------------------GRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGP 265
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   338 AL------GEHG--EWAKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRqSMDLVELVSLFPT 409
Cdd:cd16158 266 STmrksrgGNAGllKCGKGTTYEGGVREPAIAYWPGRIK------------------------PGV-THELASTLDILPT 320
                       410
                ....*....|
gi 124174   410 LAGLAGLQVP 419
Cdd:cd16158 321 IAKLAGAPLP 330
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
38-419 8.11e-19

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: 89.06  E-value: 8.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLR-PSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSywrvHAGNF 116
Cdd:cd16157   3 NIILMLMDDMGwGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNA----HARNA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   117 ST--------------IPQYFKENGYVTMSVGK-------VFHPgisSNHTDD----SPySWSFPPY----HPSSEKYEN 167
Cdd:cd16157  79 YTpqnivggipdseilLPELLKKAGYRNKIVGKwhlghrpQYHP---LKHGFDewfgAP-NCHFGPYdnkaYPNIPVYRD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   168 TKTCrgpdGELHANLlcPVDvLDVPEGTLpDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPfrypkefqkLYpleni 247
Cdd:cd16157 155 WEMI----GRYYEEF--KID-KKTGESNL-TQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAP---------VY----- 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   248 tlapdpevpdglppvAYNPWMDIRQREdvqalnisvpygpipvdfqrkirqSYFASVSYLDTQVGRLLSALDDLQLANST 327
Cdd:cd16157 213 ---------------ASKPFLGTSQRG------------------------LYGDAVMELDSSVGKILESLKSLGIENNT 253
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   328 IIAFTSDHGWAL-------GEHGEW--AKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSM 398
Cdd:cd16157 254 FVFFSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPGH------------------------IKPGQVSH 309
                       410       420
                ....*....|....*....|.
gi 124174   399 DLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16157 310 QLGSLMDLFTTSLALAGLPIP 330
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
38-419 1.28e-17

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: 84.71  E-value: 1.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDL-RPSLGCY--GDKLVRSPNIDQLASHSLLFQNAFAqQAVCAPSRVSFLTGRrpdttrlYDFN----SYWR 110
Cdd:cd16154   2 NILLIIADDQgLDSSAQYslSSDLPVTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGK-------YGFRtgvlAVPD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   111 VHAGNFSTIPQYFKEN----GYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPS--SEKYENTKTCRGPDGELHanllc 184
Cdd:cd16154  74 ELLLSEETLLQLLIKDattaGYSSAVIGK-WHLGGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNST----- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   185 pvdvldvpegTLPDKQSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPkefqklyP--LENITLAPDpevpdgLPPV 262
Cdd:cd16154 148 ----------EYATTKLTNLAIDWIDQ---QTKPWFLWLAYNAPHTPFHLP-------PaeLHSRSLLGD------SADI 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   263 AYNPwmdirqredvqalnisvpygpipvdfqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIaFTSDHG------ 336
Cdd:cd16154 202 EANP------------------------------RPYYLAAIEAMDTEIGRLLASIDEEERENTIII-FIGDNGtpgqvv 250
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   337 --WALGEHgewAKYSNFDVATHVPLIFyvpgrtaslpeageklfpyldpfdSASQLMEPGRQSMDLVELVSLFPTLAGLA 414
Cdd:cd16154 251 dlPYTRNH---AKGSLYEGGINVPLIV------------------------SGAGVERANERESALVNATDLYATIAELA 303

                ....*
gi 124174   415 GLQVP 419
Cdd:cd16154 304 GVDAA 308
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
38-419 4.98e-17

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: 83.63  E-value: 4.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRpslgcYGDKLV-------RSPnIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLY--DFNSY 108
Cdd:cd16160   3 NIVLFFADDMG-----YGDLASyghptqeRGP-IDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYggTRVFL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   109 WRVHAG---NFSTIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYswsFPPYH---------PssekYENTKTCrgPDG 176
Cdd:cd16160  77 PWDIGGlpkTEVTMAEALKEAGYTTGMVGK-WHLGINENNHSDGAH---LPSHHgfdfvgtnlP----FTNSWAC--DDT 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   177 ELHanllcpVDVLDVPEGTLPDK-QSTEQAIQ---LLEKMKTSA---------SPFFLAVGYHKPHIPFRYPKEFQklyp 243
Cdd:cd16160 147 GRH------VDFPDRSACFLYYNdTIVEQPIQhehLTETLVGDAksfiednqeNPFFLYFSFPQTHTPLFASKRFK---- 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   244 lenitlapdpevpdglppvaynpwmdirqredvqalNISVpygpipvdfqrkiRQSYFASVSYLDTQVGRLLSALDDLQL 323
Cdd:cd16160 217 ------------------------------------GKSK-------------RGRYGDNINEMSWAVGEVLDTLVDTGL 247
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   324 ANSTIIAFTSDHGWAL---GEHGEWA-----KYSNFDVATHVPLIFYVPGRTaslpeageklfpyldpfdsasqlmePGR 395
Cdd:cd16160 248 DQNTLVFFLSDHGPHVeycLEGGSTGglkggKGNSWEGGIRVPFIAYWPGTI-------------------------KPR 302
                       410       420
                ....*....|....*....|....
gi 124174   396 QSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16160 303 VSHEVVSTMDIFPTFVDLAGGTLP 326
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
26-439 4.99e-17

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 84.32  E-value: 4.99e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    26 SETQANSTTDALNVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGrrpdttrLYD 104
Cdd:COG1368 224 PTPNPFGPAKKPNVVVILLESFsDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTG-------LPP 296
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   105 FNS---YWRVHAGNFSTIPQYFKENGYVTMsvgkVFHPGissnhtddSPYSWSFPPYHP--------SSEKYENTKTcrG 173
Cdd:COG1368 297 LPGgspYKRPGQNNFPSLPSILKKQGYETS----FFHGG--------DGSFWNRDSFYKnlgfdefyDREDFDDPFD--G 362
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   174 PDGelhanllcpvdvldvpegtLPDKQSTEQAIQLLEKMKtsaSPFFLAV----GyhkpHIPFRYPKEFQKLYPLENITL 249
Cdd:COG1368 363 GWG-------------------VSDEDLFDKALEELEKLK---KPFFAFLitlsN----HGPYTLPEEDKKIPDYGKTTL 416
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   250 apdpevpdglppvaynpwmdirqredvqalnisvpygpipvdfqrkirQSYFASVSYLDTQVGRLLSALDDLQLANSTII 329
Cdd:COG1368 417 ------------------------------------------------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIF 448
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   330 AFTSDHGwalGEHGEWAKYSNFDVATHVPLIFYVPGRTAslPEAGEKLfpyldpfdsASQlmepgrqsMDlvelvsLFPT 409
Cdd:COG1368 449 VIYGDHG---PRSPGKTDYENPLERYRVPLLIYSPGLKK--PKVIDTV---------GSQ--------ID------IAPT 500
                       410       420       430
                ....*....|....*....|....*....|
gi 124174   410 LAGLAGLQVPPRcpvPSFhvelcreGKNLL 439
Cdd:COG1368 501 LLDLLGIDYPSY---YAF-------GRDLL 520
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
38-415 4.67e-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: 75.80  E-value: 4.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDL-RPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVC--APSRVSFLTGRRPDTTRLYDFNSYwrvHAG 114
Cdd:cd16015   2 NVIVILLESFsDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGgtANGEFEVLTGLPPLPLGSGSYTLY---KLN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   115 NFSTIPQYFKENGYVTMSvgkvFHPGissnhtddSPYSWSFPPYHP--------SSEKYENTKTCRGPDGelhanllcpv 186
Cdd:cd16015  79 PLPSLPSILKEQGYETIF----IHGG--------DASFYNRDSVYPnlgfdefyDLEDFPDDEKETNGWG---------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   187 dvldvpegtLPDKQSTEQAIQLLEKMKtsASPFFLAV----GyhkpHIPFRYPKEFQKLyplenitlapdpevpdglppv 262
Cdd:cd16015 137 ---------VSDESLFDQALEELEELK--KKPFFIFLvtmsN----HGPYDLPEEKKDE--------------------- 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   263 aynpwmdirqredvqalnisvpygPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEH 342
Cdd:cd16015 181 ------------------------PLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSD 236
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124174   343 GEWAKYSNFDvATHVPLIFYVPGrtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAG 415
Cdd:cd16015 237 YDETDEDPLD-LYRTPLLIYSPG-------------------------LKKPKKIDRVGSQIDIAPTLLDLLG 283
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
38-414 7.16e-14

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


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 71.30  E-value: 7.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQnAFAQQAVC--APSRVSFLTGRRPDttrlydfnsywrvhag 114
Cdd:cd00016   2 HVVLIVLDGLGADdLGKAGNPAPTTPNLKRLASEGATFN-FRSVSPPTssAPNHAALLTGAYPT---------------- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   115 nfstipqyfkENGYVTMSVGKVFHPGISSNHTDDSPyswSFPpyhpssekyentktcrgpdgelhanllcpvdvldvpeG 194
Cdd:cd00016  65 ----------LHGYTGNGSADPELPSRAAGKDEDGP---TIP-------------------------------------E 94
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   195 TLPDKQSTEQAIQLLE--KMKTSASPFFLAVGYHKPHIPFRypkefqklyplenitlAPDPEVPdglppvaynpwmdirq 272
Cdd:cd00016  95 LLKQAGYRTGVIGLLKaiDETSKEKPFVLFLHFDGPDGPGH----------------AYGPNTP---------------- 142
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   273 redvqalnisvpygpipvdfqrkirqSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYS--- 349
Cdd:cd00016 143 --------------------------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADgka 196
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124174   350 -NFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmepGRQSMDLVELVSLFPTLAGLA 414
Cdd:cd00016 197 dKSHTGMRVPFIAYGPGVKK-------------------------GGVKHELISQYDIAPTLADLL 237
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
302-365 2.26e-06

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: 49.12  E-value: 2.26e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124174   302 ASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWA-LGEHGewakYSNFDVATHVPLIFYVPG 365
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHG----YDNELPDMRAIFIARGPA 243
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
38-417 4.76e-05

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: 45.31  E-value: 4.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    38 NVLLIIVDDLRPS-LGCYGDKLVRSPNIDQLASHSLLFQNAFAqqavCAPS-RVS---FLTGR-RPDTTRLYDFNSywrv 111
Cdd:cd16017   4 NVVLVIGESARRDhMSLYGYPRDTTPFLSKLKKNLIVFDNVIS----CGTStAVSlpcMLSFAnRENYDRAYYQEN---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   112 hagnfstIPQYFKENGYvtmsvgKVF----HPGISSNHTDDSPYSWSFppYHPSSEKYENTKTCrgPDGELhanllcpvd 187
Cdd:cd16017  76 -------LIDLAKKAGY------KTYwisnQGGCGGYDTRISAIAKIE--TVFTNKGSCNSSNC--YDEAL--------- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   188 vldvpegtLPdkqsteqaiQLLEKMKTSASPFFLAV---GyhkPHIPF--RYPKEFQKLYPlenitlapdpevpdglppv 262
Cdd:cd16017 130 --------LP---------LLDEALADSSKKKLIVLhlmG---SHGPYydRYPEEFAKFTP------------------- 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   263 aynpwmdirqredvqalnisVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQlaNSTIIAFTSDHGWALGEH 342
Cdd:cd16017 171 --------------------DCDNELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKD--KDAALIYFSDHGESLGEN 228
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124174   343 GEW--AKYSNFDVATHVPLIFYVPGRTASLPEAGEKLFPYLDPFdsasqlmepgrqSMDLvelvsLFPTLAGLAGLQ 417
Cdd:cd16017 229 GLYlhGAPYAPKEQYHVPFIIWSSDSYKQRYPVERLRANKDRPF------------SHDN-----LFHTLLGLLGIK 288
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
13-336 2.03e-04

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 43.58  E-value: 2.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    13 LGLVLSSVCVALGSETQANSttdalNVLLIIVDDLRPslgcygDKLVR--SPNIDQLASHSLLFQNAfaqQAVC----AP 86
Cdd:COG1524   5 LSLLLASLLAAAAAAAPPAK-----KVVLILVDGLRA------DLLERahAPNLAALAARGVYARPL---TSVFpsttAP 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174    87 SRVSFLTGRRPDTTRLYDFNSYWRVHAGNFS------------------TIPQYFKENGyvtMSVGKVFHPGissnhTDD 148
Cdd:COG1524  71 AHTTLLTGLYPGEHGIVGNGWYDPELGRVVNslswvedgfgsnsllpvpTIFERARAAG---LTTAAVFWPS-----FEG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   149 SPYSWSFPPYHPSSEKYentktcrgpdgelhanllcpvdVLDVPEGtlpDKQSTEQAIQLLEKmktsaspfflavgyHKP 228
Cdd:COG1524 143 SGLIDAARPYPYDGRKP----------------------LLGNPAA---DRWIAAAALELLRE--------------GRP 183
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   229 HIpfrypkefqkLYplenitlapdpevpdglppvAYNPWMD-IRQRedvqalnisvpYGPipvdfqrkirQS--YFASVS 305
Cdd:COG1524 184 DL----------LL--------------------VYLPDLDyAGHR-----------YGP----------DSpeYRAALR 212
                       330       340       350
                ....*....|....*....|....*....|.
gi 124174   306 YLDTQVGRLLSALDDLQLANSTIIAFTSDHG 336
Cdd:COG1524 213 EVDAALGRLLDALKARGLYEGTLVIVTADHG 243
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
306-419 2.66e-03

GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293748 [Multi-domain]  Cd Length: 274  Bit Score: 39.86  E-value: 2.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124174   306 YLDTQVGRLLSALDDLQLANSTIIAFTSDHGW-ALGEHGEwAKYSNfdvaTHVPLIFYVPGrtaslpeageklfpyldpF 384
Cdd:cd16024 175 EMDDVIKRIYESLEEQSSNNPTLLVVCGDHGMtDAGNHGG-SSPGE----TSVPLLFISPK------------------F 231
                        90       100       110
                ....*....|....*....|....*....|....*
gi 124174   385 DSASQLMEPGRQSMDLVELVSLFPTLAGLAGLQVP 419
Cdd:cd16024 232 SSKPSNADGELSYYETVQQVDLAPTLALLLGLPIP 266
 
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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