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Conserved domains on  [gi|262118210|ref|NP_001160022|]
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iduronate 2-sulfatase isoform c [Homo sapiens]

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 ...
5-450 3.94e-167

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: 477.45  E-value: 3.94e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210   5 RRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKVFHPGISsnHTDDSPYSWSFPPYHPSSEKYENTKTCRGP 84
Cdd:cd16030   61 RRPDTTGVYDNNSYFRKVAPDAVTLPQYFKENGYTTAGVGKIFHPGIP--DGDDDPASWDEPPNPPGPEKYPPGKLCPGK 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  85 DGELHANLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPE 164
Cdd:cd16030  139 KGGKGGGGGPAWEAADVPDEAYPDGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPF 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 165 VPDGLPPVAYNPWMDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSD 244
Cdd:cd16030  218 DPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSD 297
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 245 HGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLA 324
Cdd:cd16030  298 HGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTK------------------------PGKVTDALVELVDIYPTLAELA 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 325 GLQVPPrcpvpsfhvelCREGKNLLkhfrfrdleedPYL--PGNPRELIAYSQYPRPSdipqwnsdkpslkdikIMGYSI 402
Cdd:cd16030  354 GLPAPP-----------CLEGKSLV-----------PLLknPSAKWKDAAFSQYPRPS----------------IMGYSI 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 262118210 403 RTIDYRYTVWVgfnpdeflaNFSDIHAGELYFVDSDPLQDHNMYNDSQ 450
Cdd:cd16030  396 RTERYRYTEWV---------DFDKVGAEELYDHKNDPNEWKNLANDPE 434
 
Name Accession Description Interval E-value
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
5-450 3.94e-167

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: 477.45  E-value: 3.94e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210   5 RRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKVFHPGISsnHTDDSPYSWSFPPYHPSSEKYENTKTCRGP 84
Cdd:cd16030   61 RRPDTTGVYDNNSYFRKVAPDAVTLPQYFKENGYTTAGVGKIFHPGIP--DGDDDPASWDEPPNPPGPEKYPPGKLCPGK 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  85 DGELHANLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPE 164
Cdd:cd16030  139 KGGKGGGGGPAWEAADVPDEAYPDGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPF 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 165 VPDGLPPVAYNPWMDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSD 244
Cdd:cd16030  218 DPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSD 297
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 245 HGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLA 324
Cdd:cd16030  298 HGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTK------------------------PGKVTDALVELVDIYPTLAELA 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 325 GLQVPPrcpvpsfhvelCREGKNLLkhfrfrdleedPYL--PGNPRELIAYSQYPRPSdipqwnsdkpslkdikIMGYSI 402
Cdd:cd16030  354 GLPAPP-----------CLEGKSLV-----------PLLknPSAKWKDAAFSQYPRPS----------------IMGYSI 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 262118210 403 RTIDYRYTVWVgfnpdeflaNFSDIHAGELYFVDSDPLQDHNMYNDSQ 450
Cdd:cd16030  396 RTERYRYTEWV---------DFDKVGAEELYDHKNDPNEWKNLANDPE 434
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
5-448 1.72e-53

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 183.93  E-value: 1.72e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210   5 RRPDTTRLYDFNSYWRVH-AGNFSTIPQYFKENGYVTMSVGKVFHpgissnHTDDspyswsfppyhpssekyentktcrg 83
Cdd:COG3119   83 RYPHRTGVTDNGEGYNGGlPPDEPTLAELLKEAGYRTALFGKWHL------YLTD------------------------- 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  84 pdgELhanllcpvdvldvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlapdp 163
Cdd:COG3119  132 ---LL-----------------------TDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDI------ 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 164 EVPDGLPPVAYNPWmdirqredvqalnisvpygpipvdFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTS 243
Cdd:COG3119  180 PLPPNLAPRDLTEE------------------------ELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 244 DHGWALGEHG-EWAKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAG 322
Cdd:COG3119  236 DNGPSLGEHGlRGGKGTLYEGGIRVPLIVRWPGKIK------------------------AGSVSDALVSLIDLLPTLLD 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 323 LAGLQVPPRCpvpsfhvelcrEGKNLLKHFRFRDLEEDPYLpgnpreliaYSQYPRPsdipqwnsdkpslkdikIMGYSI 402
Cdd:COG3119  292 LAGVPIPEDL-----------DGRSLLPLLTGEKAEWRDYL---------YWEYPRG-----------------GGNRAI 334
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 262118210 403 RTIDYRYTVWVGFNPDEflanfsdihagELYFVDSDPLQDHNMYND 448
Cdd:COG3119  335 RTGRWKLIRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
PRK13759 PRK13759
arylsulfatase; Provisional
28-330 9.06e-32

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 126.71  E-value: 9.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  28 TIPQYFKENGYVTMSVGKV-FHPGIS----SNHTDDSPYSWSFPPYHPSseKYENTKTCR--------GPDGEL------ 88
Cdd:PRK13759  87 TLPQEFRDAGYYTQCIGKMhVFPQRNllgfHNVLLHDGYLHSGRNEDKS--QFDFVSDYLawlrekapGKDPDLtdigwd 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  89 -HANLLCPvdvLDVPEGTLPDKQSTEQAIQLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlaPDPEVPD 167
Cdd:PRK13759 165 cNSWVARP---WDLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADI---PDPHIGD 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 168 glppvaynpWmDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGW 247
Cdd:PRK13759 238 ---------W-EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGD 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 248 ALGEHGEWAKYSNFDVATHVPLIFYVPGRTASLPEageklfpyldpfdsasqlmepGRQSMDLVELVSLFPTLAGLAGLQ 327
Cdd:PRK13759 308 MLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGNR---------------------GTVIDQVVELRDIMPTLLDLAGGT 366

                 ...
gi 262118210 328 VPP 330
Cdd:PRK13759 367 IPD 369
Sulfatase pfam00884
Sulfatase;
23-326 5.37e-19

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 87.09  E-value: 5.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210   23 AGNFSTIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDgelhanllcpvdvldvP 102
Cdd:pfam00884  76 PRTEPSLPDLLKRAGYNTGAIGK-WHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNC----------------S 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  103 EGTLPDKQSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpevpdglppvaynpwmdirq 182
Cdd:pfam00884 139 GGGVSDEALLDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKYA----------------------------- 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  183 redvqalnISVPYGpipvDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFD 262
Cdd:pfam00884 187 --------TFKPSS----CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYD 254
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262118210  263 VA----THVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGL 326
Cdd:pfam00884 255 NApeggYRVPLLIWSPGGKA------------------------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 ...
5-450 3.94e-167

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: 477.45  E-value: 3.94e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210   5 RRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKVFHPGISsnHTDDSPYSWSFPPYHPSSEKYENTKTCRGP 84
Cdd:cd16030   61 RRPDTTGVYDNNSYFRKVAPDAVTLPQYFKENGYTTAGVGKIFHPGIP--DGDDDPASWDEPPNPPGPEKYPPGKLCPGK 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  85 DGELHANLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDPE 164
Cdd:cd16030  139 KGGKGGGGGPAWEAADVPDEAYPDGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPF 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 165 VPDGLPPVAYNPWMDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSD 244
Cdd:cd16030  218 DPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSD 297
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 245 HGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLA 324
Cdd:cd16030  298 HGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTK------------------------PGKVTDALVELVDIYPTLAELA 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 325 GLQVPPrcpvpsfhvelCREGKNLLkhfrfrdleedPYL--PGNPRELIAYSQYPRPSdipqwnsdkpslkdikIMGYSI 402
Cdd:cd16030  354 GLPAPP-----------CLEGKSLV-----------PLLknPSAKWKDAAFSQYPRPS----------------IMGYSI 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 262118210 403 RTIDYRYTVWVgfnpdeflaNFSDIHAGELYFVDSDPLQDHNMYNDSQ 450
Cdd:cd16030  396 RTERYRYTEWV---------DFDKVGAEELYDHKNDPNEWKNLANDPE 434
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
5-448 1.72e-53

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 183.93  E-value: 1.72e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210   5 RRPDTTRLYDFNSYWRVH-AGNFSTIPQYFKENGYVTMSVGKVFHpgissnHTDDspyswsfppyhpssekyentktcrg 83
Cdd:COG3119   83 RYPHRTGVTDNGEGYNGGlPPDEPTLAELLKEAGYRTALFGKWHL------YLTD------------------------- 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  84 pdgELhanllcpvdvldvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlapdp 163
Cdd:COG3119  132 ---LL-----------------------TDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDI------ 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 164 EVPDGLPPVAYNPWmdirqredvqalnisvpygpipvdFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTS 243
Cdd:COG3119  180 PLPPNLAPRDLTEE------------------------ELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 244 DHGWALGEHG-EWAKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAG 322
Cdd:COG3119  236 DNGPSLGEHGlRGGKGTLYEGGIRVPLIVRWPGKIK------------------------AGSVSDALVSLIDLLPTLLD 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 323 LAGLQVPPRCpvpsfhvelcrEGKNLLKHFRFRDLEEDPYLpgnpreliaYSQYPRPsdipqwnsdkpslkdikIMGYSI 402
Cdd:COG3119  292 LAGVPIPEDL-----------DGRSLLPLLTGEKAEWRDYL---------YWEYPRG-----------------GGNRAI 334
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 262118210 403 RTIDYRYTVWVGFNPDEflanfsdihagELYFVDSDPLQDHNMYND 448
Cdd:COG3119  335 RTGRWKLIRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
13-459 7.62e-36

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


Pssm-ID: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 136.97  E-value: 7.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  13 YDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKvFHPGissnhTDDSPYSWSFPPYHPssekYENTKtcrgpdgelhanl 92
Cdd:cd16033   72 ENAGAYSRGLPPGVETFSEDLREAGYRNGYVGK-WHVG-----PEETPLDYGFDEYLP----VETTI------------- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  93 lcpvdvldvpEGTLpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPEVP-DGLPP 171
Cdd:cd16033  129 ----------EYFL-----ADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDfEDKPY 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 172 VAYNpwmdIRQREDVQALNISVpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGE 251
Cdd:cd16033  194 IYRR----ERKRWGVDTEDEED---------WKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGA 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 252 HGEWAK-YSNFDVATHVPLIFYVPGrtaslpeageklfpyldpfdsasqLMEPGRQSMDLVELVSLFPTLAGLAGLQVPP 330
Cdd:cd16033  261 HRLWDKgPFMYEETYRIPLIIKWPG------------------------VIAAGQVVDEFVSLLDLAPTILDLAGVDVPP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 331 RCpvpsfhvelcrEGKNLLKHFRfrdlEEDPylPGNPRELIAysqyprpsdipQWNSDKPSLkdikiMGYSIRTIDYRYT 410
Cdd:cd16033  317 KV-----------DGRSLLPLLR----GEQP--EDWRDEVVT-----------EYNGHEFYL-----PQRMVRTDRYKYV 363
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 262118210 411 vwvgFNPdeflanfSDIhaGELYFVDSDPLQDHNMYNDSQGGDLFQLLM 459
Cdd:cd16033  364 ----FNG-------FDI--DELYDLESDPYELNNLIDDPEYEEILREMR 399
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
112-350 1.63e-32

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


Pssm-ID: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 126.91  E-value: 1.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 112 TEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLapdPEVPDGLPPVAyNPWMDIRqreDVQalni 191
Cdd:cd16155  108 ADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPL---PENFLPQHPFD-NGEGTVR---DEQ---- 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 192 svpYGPIPVDFQ--RKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHVPL 269
Cdd:cd16155  177 ---LAPFPRTPEavRQHLAEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLMGKQNLYEHSMRVPL 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 270 IFYVPGrtasLPeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQVPPRCpvpsfhvelcrEGKNLL 349
Cdd:cd16155  254 IISGPG----IP---------------------KGKRRDALVYLQDVFPTLCELAGIEIPESV-----------EGKSLL 297

                 .
gi 262118210 350 K 350
Cdd:cd16155  298 P 298
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
28-444 5.42e-32

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


Pssm-ID: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 126.14  E-value: 5.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  28 TIPQYFKENGYVTMSVGKvFHpgISSNHTDDSPYSWSFPP-----------------YHPSSEKYENTktcrgpdgelha 90
Cdd:cd16034   81 TIADVLKDAGYRTGYIGK-WH--LDGPERNDGRADDYTPPperrhgfdywkgyecnhDHNNPHYYDDD------------ 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  91 nllcpvDVLDVPEGTLPDKQsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRY-PKEFQKLYPLENITLAPDpevpdgl 169
Cdd:cd16034  146 ------GKRIYIKGYSPDAE-TDLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRPN------- 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 170 ppvaynpwMDIRQREDVQAlnisvpygpipvdfQRKIRQsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWAL 249
Cdd:cd16034  212 --------VPEDKKEEAGL--------------REDLRG-YYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDML 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 250 GEHGEWAKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAGLQVP 329
Cdd:cd16034  269 GSHGLMNKQVPYEESIRVPFIIRYPGK------------------------IKAGRVVDLLINTVDIMPTLLGLCGLPIP 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 330 PrcpvpsfhvelCREGKNLLKHFrfrdLEEDPYLPGNpreliAYSQYPRPSDipQWNSDKPSLKDIkimgysIRTIDYRY 409
Cdd:cd16034  325 D-----------TVEGRDLSPLL----LGGKDDEPDS-----VLLQCFVPFG--GGSARDGGEWRG------VRTDRYTY 376
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 262118210 410 TVWVGfnpDEFLanfsdihageLYFVDSDPLQDHN 444
Cdd:cd16034  377 VRDKN---GPWL----------LFDNEKDPYQLNN 398
PRK13759 PRK13759
arylsulfatase; Provisional
28-330 9.06e-32

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 126.71  E-value: 9.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  28 TIPQYFKENGYVTMSVGKV-FHPGIS----SNHTDDSPYSWSFPPYHPSseKYENTKTCR--------GPDGEL------ 88
Cdd:PRK13759  87 TLPQEFRDAGYYTQCIGKMhVFPQRNllgfHNVLLHDGYLHSGRNEDKS--QFDFVSDYLawlrekapGKDPDLtdigwd 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  89 -HANLLCPvdvLDVPEGTLPDKQSTEQAIQLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlaPDPEVPD 167
Cdd:PRK13759 165 cNSWVARP---WDLEERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYKDADI---PDPHIGD 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 168 glppvaynpWmDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGW 247
Cdd:PRK13759 238 ---------W-EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGD 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 248 ALGEHGEWAKYSNFDVATHVPLIFYVPGRTASLPEageklfpyldpfdsasqlmepGRQSMDLVELVSLFPTLAGLAGLQ 327
Cdd:PRK13759 308 MLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGNR---------------------GTVIDQVVELRDIMPTLLDLAGGT 366

                 ...
gi 262118210 328 VPP 330
Cdd:PRK13759 367 IPD 369
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
100-439 9.48e-32

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


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 123.81  E-value: 9.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 100 DVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdpevpdglppvaynpwmd 179
Cdd:cd16037  104 DQRHGFRYDRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY--------------------------- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 180 irqredvqalnisvpygpipvdfQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYS 259
Cdd:cd16037  157 -----------------------VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKST 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 260 NFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCPvpsfhv 339
Cdd:cd16037  214 MYEESVRVPMIISGPGI-------------------------PAGKRVKTPVSLVDLAPTILEAAGAPPPPDLD------ 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 340 elcreGKNLLkhfrfrDLEEDPYlpgnPRELIAYSQYprpsdipqwnsdkpSLKDIKIMGYSIRTIDYRYTVWVGFNPde 419
Cdd:cd16037  263 -----GRSLL------PLAEGPD----DPDRVVFSEY--------------HAHGSPSGAFMLRKGRWKYIYYVGYPP-- 311
                        330       340
                 ....*....|....*....|
gi 262118210 420 flanfsdihagELYFVDSDP 439
Cdd:cd16037  312 -----------QLFDLENDP 320
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
28-458 4.81e-30

unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.


Pssm-ID: 293755 [Multi-domain]  Cd Length: 429  Bit Score: 121.10  E-value: 4.81e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  28 TIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPSSEKYENtKTCRGPDGEL-HANLLCpvdvldvpegtl 106
Cdd:cd16031   83 TYPKLLRKAGYQTAFIGK-WHLGSGGDLPPPGFDYWVSFPGQGSYYDPEF-IENGKRVGQKgYVTDII------------ 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 107 pdkqsTEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAP--DPEVPDGLPPVAYNPWMDIRQRE 184
Cdd:cd16031  149 -----TDKALDFLKERDKD-KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPEtfDDDDYAGRPEWAREQRNRIRGVL 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 185 DVQALNisvpygpiPVDFQRKIRQsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGeWA-KYSNFDV 263
Cdd:cd16031  223 DGRFDT--------PEKYQRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHG-LFdKRLMYEE 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 264 ATHVPLIFYVPGRTaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCpvpsfhvelcr 343
Cdd:cd16031  293 SIRVPLIIRDPRLI------------------------KAGTVVDALVLNIDFAPTILDLAGVPIPEDM----------- 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 344 EGKNLLKHFRFRDleedpylPGNPRE--LIAYSQYPRPSDIPQWnsdkpslkdikimgYSIRTIDYRYTVWVGFNPDEfl 421
Cdd:cd16031  338 QGRSLLPLLEGEK-------PVDWRKefYYEYYEEPNFHNVPTH--------------EGVRTERYKYIYYYGVWDEE-- 394
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 262118210 422 anfsdihagELYFVDSDPLQDHNMYNDSQGGDLFQLL 458
Cdd:cd16031  395 ---------ELYDLKKDPLELNNLANDPEYAEVLKEL 422
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
128-376 2.96e-29

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: 116.91  E-value: 2.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 128 PFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdpevpdglppvaynpwmdirqredvqalnisvpygpipvdfQRKIR 207
Cdd:cd16032  134 PFFLTVSFTHPHDPYVIPQEYWDLY--------------------------------------------------VRRAR 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 208 QSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTAslpeagekl 287
Cdd:cd16032  164 RAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSFFEGSARVPLIISAPGRFA--------- 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 288 fpyldpfdsasqlmePGRQSmDLVELVSLFPTLAGLAGLQVPPRCPVPsfhvelcrEGKNLLKHFRFRDleedpylPGNP 367
Cdd:cd16032  235 ---------------PRRVA-EPVSLVDLLPTLVDLAGGGTAPHVPPL--------DGRSLLPLLEGGD-------SGGE 283

                 ....*....
gi 262118210 368 REliAYSQY 376
Cdd:cd16032  284 DE--VISEY 290
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
105-450 1.45e-28

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 116.95  E-value: 1.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 105 TLPDKQSTEQAIQLLEKMKTSAsPFFLAVGYHKPHIPFRYPKEFQKLYPLEnitLAPdPEVPDGLPpvAYNPWMDIRQRE 184
Cdd:cd16150  111 CDSDEACVRTAIDWLRNRRPDK-PFCLYLPLIFPHPPYGVEEPWFSMIDRE---KLP-PRRPPGLR--AKGKPSMLEGIE 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 185 DvQALNisvpygPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSN-F-D 262
Cdd:cd16150  184 K-QGLD------RWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNtFeD 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 263 VATHVPLIFYVPGRTaslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQVPPrcpvPSFhvelc 342
Cdd:cd16150  257 CLTRVPLIIKPPGGP-------------------------AGGVSDALVELVDIPPTLLDLAGIPLSH----THF----- 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 343 reGKNLLKHFRFRDLEEDPY-------LPGNPReliAYSQYPRPSDIPQWNSDKPSLKDIKIMGYSIRTIDYRYtVWVGF 415
Cdd:cd16150  303 --GRSLLPVLAGETEEHRDAvfseggrLHGEEQ---AMEGGHGPYDLKWPRLLQQEEPPEHTKAVMIRTRRYKY-VYRLY 376
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 262118210 416 NPDeflanfsdihagELYFVDSDPLQDHNMYNDSQ 450
Cdd:cd16150  377 EPD------------ELYDLEADPLELHNLIGDPA 399
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
5-329 2.15e-27

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: 109.45  E-value: 2.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210   5 RRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKvfhpgissNHtddspyswsfppyhpssekyentktcrgp 84
Cdd:cd16022   60 RYPHRHGVRGNVGNGGGLPPDEPTLAELLKEAGYRTALIGK--------WH----------------------------- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  85 dgelhanllcpvdvldvpegtlpdkqstEQAIQLLEKMKTSAsPFFLAVGYHKPHIPFRYpkefqklyplenitlapdpe 164
Cdd:cd16022  103 ----------------------------DEAIDFIERRDKDK-PFFLYVSFNAPHPPFAY-------------------- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 165 vpdglppvaynpwmdirqredvqalnisvpygpipvdfqrkirqsyFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSD 244
Cdd:cd16022  134 ----------------------------------------------YAMVSAIDDQIGRILDALEELGLLDNTLIVFTSD 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 245 HGWALGEHGE-WAKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGL 323
Cdd:cd16022  168 HGDMLGDHGLrGKKGSLYEGGIRVPFIVRWPGK------------------------IPAGQVSDALVSLLDLLPTLLDL 223

                 ....*.
gi 262118210 324 AGLQVP 329
Cdd:cd16022  224 AGIEPP 229
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
28-330 4.79e-27

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: 111.45  E-value: 4.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  28 TIPQYFKENGYVTMSVGKVFHPGissnhtdDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANllcpvdvldvpegtlP 107
Cdd:cd16027   82 TLPELLREAGYYTGLIGKTHYNP-------DAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRA---------------K 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 108 DKQsteqaiqllekmktsasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAP----DPEVpdglppvaynpwmdirqR 183
Cdd:cd16027  140 KGQ-----------------PFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPylpdTPEV-----------------R 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 184 EDVQAlnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGehgeWAKYSNFDV 263
Cdd:cd16027  186 EDLAD---------------------YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP----RAKGTLYDS 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262118210 264 ATHVPLIFYVPGRTaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVPP 330
Cdd:cd16027  241 GLRVPLIVRWPGKI------------------------KPGSVSDALVSFIDLAPTLLDLAGIEPPE 283
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
15-331 5.83e-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: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 109.17  E-value: 5.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  15 FNSYWRVHAG----NFSTIPQYFKENGYVTMSVGkvfhpgissnhtdDSPYSWSFPPYHPSSEKYENTktcRGPDGElha 90
Cdd:cd16148   61 YPFYHGVWGGplepDDPTLAEILRKAGYYTAAVS-------------SNPHLFGGPGFDRGFDTFEDF---RGQEGD--- 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  91 nllcpvdvlDVPEGTLPDKQSTEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYpkefqklyplenitlapdpevpdglp 170
Cdd:cd16148  122 ---------PGEEGDERAERVTDRALEWLDRNADD-DPFFLFLHYFDPHEPYLY-------------------------- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 171 pvaynpwmdirqredvqalnisvpygpipvDfqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALG 250
Cdd:cd16148  166 ------------------------------D----------AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFG 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 251 EHGEWAK-YSNF-DVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQV 328
Cdd:cd16148  206 EHGLYWGhGSNLyDEQLHVPLIIRWPGK-------------------------EPGKRVDALVSHIDIAPTLLDLLGVEP 260

                 ...
gi 262118210 329 PPR 331
Cdd:cd16148  261 PDY 263
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
128-379 6.57e-24

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: 103.49  E-value: 6.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 128 PFFLAVGYHKPHIPFRYPKEFQKLYPLENITL---APDPEVPDGLPPVaYNPWMDIRQREDVQALNISVPYGPIPVdfQR 204
Cdd:cd16028  158 PWFLHLSYIRPHPPFVAPAPYHALYDPADVPPpirAESLAAEAAQHPL-LAAFLERIESLSFSPGAANAADLDDEE--VA 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 205 KIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTAslpeag 284
Cdd:cd16028  235 QMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLWGKDGFFDQAYRVPLIVRDPRREA------ 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 285 eklfpyldpfDSASqlmepGRQSMDLVELVSLFPTLAGLAGLQVPPRCpvpsfhvelcrEGKNLLKHfrfrdLEEDPylP 364
Cdd:cd16028  309 ----------DATR-----GQVVDAFTESVDVMPTILDWLGGEIPHQC-----------DGRSLLPL-----LAGAQ--P 355
                        250
                 ....*....|....*
gi 262118210 365 GNPRELIAYSQYPRP 379
Cdd:cd16028  356 SDWRDAVHYEYDFRD 370
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
5-328 2.03e-22

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


Pssm-ID: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 96.68  E-value: 2.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210   5 RRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKvfhpgissnhtddspyswsfppyhpssEKYENtktcrgp 84
Cdd:cd16153   71 RYPHRTGVYGFEAAHPALDHGLPTFPEVLKKAGYQTASFGK---------------------------SHLEA------- 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  85 dgelhanllcPVDVLDVPEgtlpdkQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFqklyplenitlapdpe 164
Cdd:cd16153  117 ----------FQRYLKNAN------QSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEF---------------- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 165 vpdglppvaynpwmdiRQREDvqalnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLAN---STIIAF 241
Cdd:cd16153  165 ----------------RDRFD------------------------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYV 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 242 TSDHGWALGEHGEWAKYSNFDVATHVPLIFYVPGRtaslpeageKLFPyldpfdsasqlmePGRQSMDLVELVSLFPTLA 321
Cdd:cd16153  205 TGDHGWHLGEQGILAKFTFWPQSHRVPLIVVSSDK---------LKAP-------------AGKVRHDFVEFVDLAPTLL 262

                 ....*..
gi 262118210 322 GLAGLQV 328
Cdd:cd16153  263 AAAGVDV 269
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
2-330 6.55e-22

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: 97.61  E-value: 6.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210   2 PLRRRPDTTRLYDFNSYWRVHAGNFsTIPQYFKENGYVTMSVGKvFHPGISSNHT--------DDSPYSWSFPPYHPSSE 73
Cdd:cd16144   73 GRRGPPDNTKLIPPPSTTRLPLEEV-TIAEALKDAGYATAHFGK-WHLGGEGGYGpedqgfdvNIGGTGNGGPPSYYFPP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  74 KYENTKTCRGPDGElHanllcPVDVLdvpegtlpdkqsTEQAIQLLEKmkTSASPFFLAVGYHKPHIPFRYPKEFQKLYP 153
Cdd:cd16144  151 GKPNPDLEDGPEGE-Y-----LTDRL------------TDEAIDFIEQ--NKDKPFFLYLSHYAVHTPIQARPELIEKYE 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 154 lenitlapdpEVPDGLPPVAYNPwmdirqredvqalnisvpygpipvdfqrkirqSYFASVSYLDTQVGRLLSALDDLQL 233
Cdd:cd16144  211 ----------KKKKGLRKGQKNP--------------------------------VYAAMIESLDESVGRILDALEELGL 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 234 ANSTIIAFTSDHGwALGEHGEWA---------KYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePG 304
Cdd:cd16144  249 ADNTLVIFTSDNG-GLSTRGGPPtsnaplrggKGSLYEGGIRVPLIVRWPGVIK------------------------PG 303
                        330       340
                 ....*....|....*....|....*.
gi 262118210 305 RQSMDLVELVSLFPTLAGLAGLQVPP 330
Cdd:cd16144  304 SVSDVPVIGTDLYPTFLELAGGPLPP 329
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
28-329 1.44e-21

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: 96.09  E-value: 1.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  28 TIPQYFKENGYVTMSVGKvFHPGISSNH--TD---DS----PYS---WSFPPYHPSSEKYEntktcrgpdgelhANLLCP 95
Cdd:cd16026   87 TIAEVLKKAGYRTALVGK-WHLGHQPEFlpTRhgfDEyfgiPYSndmWPFPLYRNDPPGPL-------------PPLMEN 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  96 VDVLDVPegtlPD-----KQSTEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFqklyplENITLApdpevpdGLp 170
Cdd:cd16026  153 EEVIEQP----ADqssltQRYTDEAVDFIERNKDQ--PFFLYLAHTMPHVPLFASEKF------KGRSGA-------GL- 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 171 pvaynpwmdirqredvqalnisvpYGpipvdfqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALG 250
Cdd:cd16026  213 ------------------------YG---------------DVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLE 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 251 EHGEW--------AKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAG 322
Cdd:cd16026  254 YGGHGgsagplrgGKGTTWEGGVRVPFIAWWPGV------------------------IPAGTVSDELASTMDLLPTLAA 309

                 ....*..
gi 262118210 323 LAGLQVP 329
Cdd:cd16026  310 LAGAPLP 316
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
28-444 1.96e-20

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: 93.00  E-value: 1.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  28 TIPQYFKENGYVTMSVGKvFHPGissnhtDDSPY----------------SWSFPPYHPSSEKYENTKTCRGP----DGe 87
Cdd:cd16146   82 TLAEVFKDAGYRTGIFGK-WHLG------DNYPYrpqdrgfdevlghgggGIGQYPDYWGNDYFDDTYYHNGKfvktEG- 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  88 lhanlLCPvDVLdvpegtlpdkqsTEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapDPEVPD 167
Cdd:cd16146  154 -----YCT-DVF------------FDEAIDFIEENKDK--PFFAYLATNAPHGPLQVPDKYLDPYK--------DMGLDD 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 168 GlppvaynpwmdirqredvqalnisvpygpipvdfqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGW 247
Cdd:cd16146  206 K--------------------------------------LAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGP 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 248 ALGEHGEW------AKYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLA 321
Cdd:cd16146  248 AGGVPKRFnagmrgKKGSVYEGGHRVPFFIRWPGKIL------------------------AGKDVDTLTAHIDLLPTLL 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 322 GLAGLQVPPrcpvpsfHVELcrEGKNLLKhfrfrdLEEDPYLPGNPRELIAYSQYPRPSDIPQWNSdkpslkdikimgyS 401
Cdd:cd16146  304 DLCGVKLPE-------GIKL--DGRSLLP------LLKGESDPWPERTLFTHSGRWPPPPKKKRNA-------------A 355
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 262118210 402 IRTIDYRYTVWVGFNPdeflanfsdihagELYFVDSDPLQDHN 444
Cdd:cd16146  356 VRTGRWRLVSPKGFQP-------------ELYDIENDPGEEND 385
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
210-337 6.12e-20

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


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 88.84  E-value: 6.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 210 YFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAK------YSNFDVATHVPLIFYVPGRTaslpea 283
Cdd:cd16149  144 YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKgngtfpLNMYDNSVKVPFIIRWPGVV------ 217
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 262118210 284 geklfpyldpfdsasqlmEPGRQSMDLVELVSLFPTLAGLAGLQVP--PRCPVPSF 337
Cdd:cd16149  218 ------------------PAGRVVDSLVSAYDFFPTLLELAGVDPPadPRLPGRSF 255
Sulfatase pfam00884
Sulfatase;
23-326 5.37e-19

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 87.09  E-value: 5.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210   23 AGNFSTIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDgelhanllcpvdvldvP 102
Cdd:pfam00884  76 PRTEPSLPDLLKRAGYNTGAIGK-WHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNC----------------S 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  103 EGTLPDKQSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpevpdglppvaynpwmdirq 182
Cdd:pfam00884 139 GGGVSDEALLDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKYA----------------------------- 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  183 redvqalnISVPYGpipvDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFD 262
Cdd:pfam00884 187 --------TFKPSS----CSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYD 254
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262118210  263 VA----THVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGL 326
Cdd:pfam00884 255 NApeggYRVPLLIWSPGGKA------------------------KGQKSEALVSHVDLFPTILDLAGI 298
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
25-362 8.06e-19

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: 88.59  E-value: 8.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  25 NFSTIPQYFKENGYVTMSVGK-------VFHPGISSNHTDdSPYSWSFPPYHPSSEKYENTKTCRGPDgELHANllcpvd 97
Cdd:cd16156   77 NVKTIGQRLSDNGIHTAYIGKwhldggdYFGNGICPQGWD-PDYWYDMRNYLDELTEEERRKSRRGLT-SLEAE------ 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  98 vlDVPEGTLPDKQSTEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYplENITLAPDPEVPDGLP--PVAYN 175
Cdd:cd16156  149 --GIKEEFTYGHRCTNRALDFIEKHKDE--DFFLVVSYDEPHHPFLCPKPYASMY--KDFEFPKGENAYDDLEnkPLHQR 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 176 PWMDIRQREDVQALNISVPYgpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLqLANSTIIaFTSDHGWALGEHGEW 255
Cdd:cd16156  223 LWAGAKPHEDGDKGTIKHPL--------------YFGCNSFVDYEIGRVLDAADEI-AEDAWVI-YTSDHGDMLGAHKLW 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 256 AK-YSNFDVATHVPLIFYVPGrtaslpeaGEKLFPYLD-PfdsasqlmepgrqsmdlVELVSLFPTLAGLAGLQVPPRCP 333
Cdd:cd16156  287 AKgPAVYDEITNIPLIIRGKG--------GEKAGTVTDtP-----------------VSHIDLAPTILDYAGIPQPKVLE 341
                        330       340       350
                 ....*....|....*....|....*....|...
gi 262118210 334 ----VPSFHVELCREGKNLLKHFRFRDLEEDPY 362
Cdd:cd16156  342 gesiLATIEDPEIPENRGVFVEFGRYEVDHDGF 374
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
108-326 4.06e-18

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


Pssm-ID: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 84.57  E-value: 4.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 108 DKQSTEQAIQLLEKMKTSAS---PFFLAVGYHKPHipfrypkefqklyplenitlapdpevpdglppvaynpwmdirqre 184
Cdd:cd16035  116 DPGIAAQAVEWLRERGAKNAdgkPWFLVVSLVNPH--------------------------------------------- 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 185 DVQalnisvpYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSN-FDV 263
Cdd:cd16035  151 DIM-------FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNaYEE 223
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262118210 264 ATHVPLIFYVPGrtaslpeagekLFPyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGL 326
Cdd:cd16035  224 ALHVPLIISHPD-----------LFG-------------TGQTTDALTSHIDLLPTLLGLAGV 262
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
27-362 1.41e-17

glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).


Pssm-ID: 293766 [Multi-domain]  Cd Length: 396  Bit Score: 84.14  E-value: 1.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  27 STIPQYFKENGYVTMSVGKVFHpGISSNHTDDSP---YSWSFPPYHPSseKYENTKTCRGPDGELHANllCPV----DVL 99
Cdd:cd16147   85 STLPVWLQEAGYRTAYAGKYLN-GYGVPGGVSYVppgWDEWDGLVGNS--TYYNYTLSNGGNGKHGVS--YPGdyltDVI 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 100 dvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPleNITLAP-----DPEVPDG------ 168
Cdd:cd16147  160 ------------ANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFP--NVTAPPrpppnNPDVSDKphwlrr 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 169 --LPPVAYNPWMDIRQREDVQALnisvpygpipvdfqrkirqsyfASVsylDTQVGRLLSALDDLQLANSTIIAFTSDHG 246
Cdd:cd16147  226 lpPLNPTQIAYIDELYRKRLRTL----------------------QSV---DDLVERLVNTLEATGQLDNTYIIYTSDNG 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 247 WALGEHG-EWAKYSNFDVATHVPLIFYVPGrtasLPeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAG 325
Cdd:cd16147  281 YHLGQHRlPPGKRTPYEEDIRVPLLVRGPG----IP---------------------AGVTVDQLVSNIDLAPTILDLAG 335
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 262118210 326 LQVPP--------RCPVPSFH-VELCREGKNLLKHF---RFR---DLEEDPY 362
Cdd:cd16147  336 APPPSdmdgrscgDSNNNTYKcVRTVDDTYNLLYFEwctGFRelyDLTTDPY 387
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
28-331 4.56e-17

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: 83.03  E-value: 4.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  28 TIPQYFKENGYVTMSVGKVfhpGISSNHTDDSPYS----------------WSFPPYhpsseKYENTKTcrgpdgELHAN 91
Cdd:cd16145   85 TLAEVLKKAGYATAAFGKW---GLGGPGTPGHPTKqgfdyfygyldqvhahNYYPEY-----LWRNGEK------VPLPN 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  92 LLCPVDVLDVPEGTLPDKQS----TEQAIQLLEKMKtsASPFFLAVGYHKPHIPFRYPKefqklyplenitLAPDPEVPD 167
Cdd:cd16145  151 NVIPPLDEGNNAGGGGGTYShdlfTDEALDFIRENK--DKPFFLYLAYTLPHAPLQVPD------------DGPYKYKPK 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 168 GLPPVAYNPWMDIRQRedvqalnisvpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGw 247
Cdd:cd16145  217 DPGIYAYLPWPQPEKA--------------------------YAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNG- 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 248 ALGEHGEWAKYSNFDVA--------------THVPLIFYVPGRTaslpeageklfpyldpfdsasqlmEPGRQSMDLVEL 313
Cdd:cd16145  270 PHSEGGSEHDPDFFDSNgplrgykrslyeggIRVPFIARWPGKI------------------------PAGSVSDHPSAF 325
                        330
                 ....*....|....*...
gi 262118210 314 VSLFPTLAGLAGLQVPPR 331
Cdd:cd16145  326 WDFMPTLADLAGAEPPED 343
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
192-444 2.83e-16

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


Pssm-ID: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 79.95  E-value: 2.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 192 SVPYGPIPVDFQRkiRQSYF-ASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEW-------AKYSNFDV 263
Cdd:cd16151  190 SPDWDPDDKRKKD--DPEYFpDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTngrevrgGKGKTTDA 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 264 ATHVPLIFYVPGrtaslpeageklfpyldpfdsasqLMEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCPVpsfhvelcr 343
Cdd:cd16151  268 GTHVPLIVNWPG------------------------LIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPL--------- 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 344 EGKNLLkhfrfrdleedPYL---PGNPRELIAYsqyprpsdipqWNSDKPSLKDIKimgYSIRTIDYRYtvwvgfnpdef 420
Cdd:cd16151  315 DGRSFA-----------PQLlgkTGSPRREWIY-----------WYYRNPHKKFGS---RFVRTKRYKL----------- 358
                        250       260
                 ....*....|....*....|....
gi 262118210 421 lanFSDihaGELYFVDSDPLQDHN 444
Cdd:cd16151  359 ---YAD---GRFFDLREDPLEKNP 376
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
204-330 3.05e-16

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: 79.89  E-value: 3.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 204 RKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHVPLIFYVPGrtaslpea 283
Cdd:cd16171  192 RNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMYEGSSHVPLLIMGPG-------- 263
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 262118210 284 geklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAGLQVPP 330
Cdd:cd16171  264 -----------------IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
25-334 7.26e-16

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: 79.13  E-value: 7.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  25 NFSTIPQYFKENGYVTMSVGKvFHPGISS-NHTD-----DSPYSwsfppYHPSSEKYENTKTCRGPDgelhanllCPVDV 98
Cdd:cd16029   82 NETLLPQYLKELGYATHLVGK-WHLGFYTwEYTPtnrgfDSFYG-----YYGGAEDYYTHTSGGAND--------YGNDD 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  99 LDVPEGTLPDKQS-------TEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpevpdglpp 171
Cdd:cd16029  148 LRDNEEPAWDYNGtystdlfTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYE------------------ 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 172 vaynpwmdirqredVQALNISvpygpipvDFQRKIrqsYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGwALGE 251
Cdd:cd16029  209 --------------DKFAHIK--------DEDRRT---YAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG-GPTG 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 252 HGEWAkySNFdvathvPLifyvPGRTASLPEAGEKlfpyLDPFDSASQL-MEPGRQSMDLVELVSLFPTLAGLAGLQVPP 330
Cdd:cd16029  263 GGDGG--SNY------PL----RGGKNTLWEGGVR----VPAFVWSPLLpPKRGTVSDGLMHVTDWLPTLLSLAGGDPDD 326

                 ....
gi 262118210 331 RCPV 334
Cdd:cd16029  327 LPPL 330
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
28-330 9.75e-16

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


Pssm-ID: 293761 [Multi-domain]  Cd Length: 372  Bit Score: 78.34  E-value: 9.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  28 TIPQYFKENGYVTMSVGKvfhpgissNHTDDSPYSWsfppyhPssekyentkTCRGPDgELHANLLcpvdvldvpegTLP 107
Cdd:cd16142   87 TLAELLKDAGYATAQFGK--------WHLGDEDGRL------P---------TDHGFD-EFYGNLY-----------HTI 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 108 DKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdpevpdglppvAYNPWMDirqredvq 187
Cdd:cd16142  132 DEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSS-------------------GKGKYAD-------- 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 188 alnisvpygpipvdfqrkirqsyfaSVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG-----WALGEHGEW--AKYSN 260
Cdd:cd16142  185 -------------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFrgEKGTT 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 261 FDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAGLQVPP 330
Cdd:cd16142  240 WEGGVRVPAIVRWPGK------------------------IKPGRVSNEIVSHLDWFPTLAALAGAPDPK 285
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
28-329 1.06e-14

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: 75.32  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  28 TIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDgelHANLLCPVDVLDvpegTLp 107
Cdd:cd16143   87 TLAKMLKQAGYRTAMVGK-WHLGLDWKKKDGKKAATGTGKDVDYSKPIKGGPLDHGFD---YYFGIPASEVLP----TL- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 108 dkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKlyplenitlapdpevpdglppvaynpwmdirqredVQ 187
Cdd:cd16143  158 ----TDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQG-----------------------------------KS 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 188 ALNisvPYGpipvDFqrkIRQsyfasvsyLDTQVGRLLSALDDLQLANSTIIAFTSDHG-------WALGEHGEWA---- 256
Cdd:cd16143  199 GAG---PYG----DF---VYE--------LDWVVGRILDALKELGLAENTLVIFTSDNGpspyadyKELEKFGHDPsgpl 260
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262118210 257 ---KYSNFDVATHVPLIFYVPGRTAslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLFPTLAGLAGLQVP 329
Cdd:cd16143  261 rgmKADIYEGGHRVPFIVRWPGKIP------------------------AGSVSDQLVSLTDLFATLAAIVGQKLP 312
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
112-449 1.69e-14

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


Pssm-ID: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 74.57  E-value: 1.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 112 TEQAIQLLEKmKTSASPFFLAVGYHKPHIP---FRY--PKEFQKLYPlenitlapDPEVPdglppvaynpwmdirqrEDV 186
Cdd:cd16152  110 TDFAIDYLDN-RQKDKPFFLFLSYLEPHHQndrDRYvaPEGSAERFA--------NFWVP-----------------PDL 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 187 QALnisvpygpiPVDFQRKIrQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHgwalGEH-----GEWaKYSNF 261
Cdd:cd16152  164 AAL---------PGDWAEEL-PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHfrtrnAEY-KRSCH 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 262 DVATHVPLIFYVPGrtaslpeageklfpyldpFDSasqlmepGRQSMDLVELVSLFPTLAGLAGLQVPprcpvPSFHvel 341
Cdd:cd16152  229 ESSIRVPLVIYGPG------------------FNG-------GGRVEELVSLIDLPPTLLDAAGIDVP-----EEMQ--- 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 342 creGKNLLkhfrfrdleedpylpgnprELIAYSQYPRPSDIPqwnsdkpslkdIKI----MGYSIRTIDYRYTVwVGFNP 417
Cdd:cd16152  276 ---GRSLL-------------------PLVDGKVEDWRNEVF-----------IQIsesqVGRAIRTDRWKYSV-AAPDK 321
                        330       340       350
                 ....*....|....*....|....*....|...
gi 262118210 418 DEFLANFSDIHAGE-LYFVDSDPLQDHNMYNDS 449
Cdd:cd16152  322 DGWKDSGSDVYVEDyLYDLEADPYELVNLIGRP 354
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
28-329 4.73e-12

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: 67.47  E-value: 4.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  28 TIPQYFKENGYVTMSVGKvfhpgissnhtddspysW--SFPPYHpSSEKYentktcrgpdgelhanllcpvdvldvpegt 105
Cdd:cd16025   90 TIAEVLKDAGYHTYMSGK-----------------WhlGPDDYY-STDDL------------------------------ 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 106 lpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEF----------------------QK---LYPlENITLA 160
Cdd:cd16025  122 ------TDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkykgkydagwdalreerlerQKelgLIP-ADTKLT 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 161 P-DPEVPdglppvaynPWMDIRQRE-DVQALNISVpygpipvdfqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTI 238
Cdd:cd16025  195 PrPPGVP---------AWDSLSPEEkKLEARRMEV----------------YAAMVEHMDQQIGRLIDYLKELGELDNTL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 239 IAFTSDHGwALGEHGeWAKYSN-----FDVATH-----VPLIfyvpgrtASLPEAGEKlfpyldpfdsasqlmePGRQSM 308
Cdd:cd16025  250 IIFLSDNG-ASAEPG-WANASNtpfrlYKQASHeggirTPLI-------VSWPKGIKA----------------KGGIRH 304
                        330       340
                 ....*....|....*....|.
gi 262118210 309 DLVELVSLFPTLAGLAGLQVP 329
Cdd:cd16025  305 QFAHVIDIAPTILELAGVEYP 325
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
207-324 7.46e-12

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: 65.13  E-value: 7.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 207 RQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYS----NFDVATHVPLIFYVPGRTAslpe 282
Cdd:cd00016  141 TPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADgkadKSHTGMRVPFIAYGPGVKK---- 216
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 262118210 283 ageklfpyldpfdsasqlmepGRQSMDLVELVSLFPTLAGLA 324
Cdd:cd00016  217 ---------------------GGVKHELISQYDIAPTLADLL 237
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
25-330 8.18e-11

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: 63.64  E-value: 8.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  25 NFSTIPQYFKENGYVTMSVGKvFHPGissnHTDDspyswsfppYHPSSekyentktcRGPDgelhanllcpvDVLDVP-- 102
Cdd:cd16161   84 NETTLAEVLRQAGYATGMIGK-WHLG----QREA---------YLPNS---------RGFD-----------YYFGIPfs 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 103 -EGTLPDKQStEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQklyplenitlapdpevpdglppvaynpwmdir 181
Cdd:cd16161  130 hDSSLADRYA-QFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQ-------------------------------- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 182 qredvQALNISVPYGpipvdfqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG-WALG-------EHG 253
Cdd:cd16161  177 -----SPTSGRGPYG---------------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpWEVKcelavgpGTG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 254 EW--------AKYSNFDVATHVPLIFYVPGRtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAG 325
Cdd:cd16161  237 DWqgnlggsvAKASTWEGGHREPAIVYWPGR------------------------IPANSTSAALVSTLDIFPTVVALAG 292

                 ....*
gi 262118210 326 LQVPP 330
Cdd:cd16161  293 ASLPP 297
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
25-349 9.21e-10

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 60.82  E-value: 9.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  25 NFSTIPQYFKENGYVTMsvgkVFHPGissnhtddSPYSWSFPPYHP--------SSEKYENTKTcrGPDGelhanllcpv 96
Cdd:COG1368  310 NFPSLPSILKKQGYETS----FFHGG--------DGSFWNRDSFYKnlgfdefyDREDFDDPFD--GGWG---------- 365
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  97 dvldvpegtLPDKQSTEQAIQLLEKMKtsaSPFFLAV----GyhkpHIPFRYPKEFQKLYPLENITLapdpevpdglppv 172
Cdd:COG1368  366 ---------VSDEDLFDKALEELEKLK---KPFFAFLitlsN----HGPYTLPEEDKKIPDYGKTTL------------- 416
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 173 aynpwmdirqredvqalnisvpygpipvdfqrkirQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGwalGEH 252
Cdd:COG1368  417 -----------------------------------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG---PRS 458
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 253 GEWAKYSNFDVATHVPLIFYVPGRTAslPEAGEKLfpyldpfdsASQlmepgrqsMDlvelvsLFPTLAGLAGLQVPPRc 332
Cdd:COG1368  459 PGKTDYENPLERYRVPLLIYSPGLKK--PKVIDTV---------GSQ--------ID------IAPTLLDLLGIDYPSY- 512
                        330
                 ....*....|....*..
gi 262118210 333 pvPSFhvelcreGKNLL 349
Cdd:COG1368  513 --YAF-------GRDLL 520
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
25-325 7.10e-09

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: 56.92  E-value: 7.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  25 NFSTIPQYFKENGYVTMSvgkvFHPGissnhtddSPYSWSFPPYHP--------SSEKYENTKTCRGPDGelhanllcpv 96
Cdd:cd16015   79 PLPSLPSILKEQGYETIF----IHGG--------DASFYNRDSVYPnlgfdefyDLEDFPDDEKETNGWG---------- 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  97 dvldvpegtLPDKQSTEQAIQLLEKMKtsASPFFLAV----GyhkpHIPFRYPKEFQKLyplenitlapdpevpdglppv 172
Cdd:cd16015  137 ---------VSDESLFDQALEELEELK--KKPFFIFLvtmsN----HGPYDLPEEKKDE--------------------- 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 173 aynpwmdirqredvqalnisvpygPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEH 252
Cdd:cd16015  181 ------------------------PLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSD 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262118210 253 GEWAKYSNFDvATHVPLIFYVPGrtaslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAG 325
Cdd:cd16015  237 YDETDEDPLD-LYRTPLLIYSPG-------------------------LKKPKKIDRVGSQIDIAPTLLDLLG 283
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
210-329 7.15e-09

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: 57.68  E-value: 7.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 210 YFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWAL------GEHGEW-------AKYSNFDVATHVPLIFYVPGR 276
Cdd:cd16159  281 YGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvgGEYGGGnggiyggKKMGGWEGGIRVPTIVRWPGV 360
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 262118210 277 tasLPeageklfpyldpfdSASQLMEPGRQsMDlvelvsLFPTLAGLAGLQVP 329
Cdd:cd16159  361 ---IP--------------PGSVIDEPTSL-MD------IFPTVAALAGAPLP 389
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
207-329 4.55e-07

galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.


Pssm-ID: 293776 [Multi-domain]  Cd Length: 466  Bit Score: 52.08  E-value: 4.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 207 RQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWAL-------GEHGEW--AKYSNFDVATHVPLIFYVPGRt 277
Cdd:cd16157  223 RGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPGH- 301
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 262118210 278 aslpeageklfpyldpfdsasqlMEPGRQSMDLVELVSLFPTLAGLAGLQVP 329
Cdd:cd16157  302 -----------------------IKPGQVSHQLGSLMDLFTTSLALAGLPIP 330
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
110-329 7.95e-07

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: 50.81  E-value: 7.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 110 QSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPkefqklyP--LENITLAPDpevpdgLPPVAYNPwmdirqredvq 187
Cdd:cd16154  153 KLTNLAIDWIDQ---QTKPWFLWLAYNAPHTPFHLP-------PaeLHSRSLLGD------SADIEANP----------- 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 188 alnisvpygpipvdfqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIaFTSDHG--------WALGEHgewAKYS 259
Cdd:cd16154  206 -------------------RPYYLAAIEAMDTEIGRLLASIDEEERENTIII-FIGDNGtpgqvvdlPYTRNH---AKGS 262
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 260 NFDVATHVPLIFyvpgrtaslpeageklfpyldpfdSASQLMEPGRQSMDLVELVSLFPTLAGLAGLQVP 329
Cdd:cd16154  263 LYEGGINVPLIV------------------------SGAGVERANERESALVNATDLYATIAELAGVDAA 308
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
212-275 2.83e-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: 48.74  E-value: 2.83e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262118210 212 ASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWA-LGEHGewakYSNFDVATHVPLIFYVPG 275
Cdd:cd16018  183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHG----YDNELPDMRAIFIARGPA 243
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
28-329 1.65e-05

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: 47.04  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  28 TIPQYFKENGYVTMSVGKvFHPGISSNHTDDSPYswsFPPYH---------PssekYENTKTCrgPDGELHanllcpVDV 98
Cdd:cd16160   89 TMAEALKEAGYTTGMVGK-WHLGINENNHSDGAH---LPSHHgfdfvgtnlP----FTNSWAC--DDTGRH------VDF 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210  99 LDVPEGTLPDK-QSTEQAIQ---LLEKMKTSA---------SPFFLAVGYHKPHIPFRYPKEFQklyplenitlapdpev 165
Cdd:cd16160  153 PDRSACFLYYNdTIVEQPIQhehLTETLVGDAksfiednqeNPFFLYFSFPQTHTPLFASKRFK---------------- 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 166 pdglppvaynpwmdirqredvqalNISVpygpipvdfqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDH 245
Cdd:cd16160  217 ------------------------GKSK-------------RGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDH 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 246 GWAL---GEHGEWA-----KYSNFDVATHVPLIFYVPGRTaslpeageklfpyldpfdsasqlmePGRQSMDLVELVSLF 317
Cdd:cd16160  260 GPHVeycLEGGSTGglkggKGNSWEGGIRVPFIAYWPGTI-------------------------KPRVSHEVVSTMDIF 314
                        330
                 ....*....|..
gi 262118210 318 PTLAGLAGLQVP 329
Cdd:cd16160  315 PTFVDLAGGTLP 326
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
204-329 6.44e-05

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: 45.13  E-value: 6.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 204 RKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWAL------GEHG--EWAKYSNFDVATHVPLIFYVPG 275
Cdd:cd16158  222 RSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGllKCGKGTTYEGGVREPAIAYWPG 301
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 262118210 276 RTAslpeageklfpyldpfdsasqlmePGRqSMDLVELVSLFPTLAGLAGLQVP 329
Cdd:cd16158  302 RIK------------------------PGV-THELASTLDILPTIAKLAGAPLP 330
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
139-327 1.12e-04

Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.


Pssm-ID: 293741 [Multi-domain]  Cd Length: 288  Bit Score: 43.77  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 139 HIPF--RYPKEFQKLYPlenitlapdpevpdglppvaynpwmdirqredvqalnisVPYGPIPVDFQRKIRQSYFASVSY 216
Cdd:cd16017  154 HGPYydRYPEEFAKFTP---------------------------------------DCDNELQSCSKEELINAYDNSILY 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 217 LDTQVGRLLSALDDLQlaNSTIIAFTSDHGWALGEHGEW--AKYSNFDVATHVPLIFYVPGRTASLPEAGEKLFPYLDPF 294
Cdd:cd16017  195 TDYVLSQIIERLKKKD--KDAALIYFSDHGESLGENGLYlhGAPYAPKEQYHVPFIIWSSDSYKQRYPVERLRANKDRPF 272
                        170       180       190
                 ....*....|....*....|....*....|...
gi 262118210 295 dsasqlmepgrqSMDLvelvsLFPTLAGLAGLQ 327
Cdd:cd16017  273 ------------SHDN-----LFHTLLGLLGIK 288
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
210-246 4.28e-04

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 42.43  E-value: 4.28e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 262118210 210 YFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHG 246
Cdd:COG1524  207 YRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
216-329 2.29e-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: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118210 216 YLDTQVGRLLSALDDLQLANSTIIAFTSDHGW-ALGEHGEwAKYSNfdvaTHVPLIFYVPGrtaslpeageklfpyldpF 294
Cdd:cd16024  175 EMDDVIKRIYESLEEQSSNNPTLLVVCGDHGMtDAGNHGG-SSPGE----TSVPLLFISPK------------------F 231
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 262118210 295 DSASQLMEPGRQSMDLVELVSLFPTLAGLAGLQVP 329
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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