NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1270232598|gb|PHQ37247.1|]
View 

arylsulfatase [Rhodopirellula bahusiensis]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 10888406)

alkaline phosphatase (ALP) family protein may catalyze the hydrolysis of substrates; the ALP superfamily includes alkaline phosphatases and sulfatases

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
48-427 0e+00

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: 616.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGMTNKRNYVKFGMLDRKQTTFAH 127
Cdd:cd16151     1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQKTFGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 128 LLKSAGYRTCIAGKWQLGS---ELDSPRHFGFEESLLWQHTRGRMDSQKRDTRYPNprlERNGTKEDYDEGEFSSDLFAD 204
Cdd:cd16151    81 LLKDAGYATAIAGKWQLGGgrgDGDYPHEFGFDEYCLWQLTETGEKYSRPATPTFN---IRNGKLLETTEGDYGPDLFAD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 205 FLCDFMETNRDQPFLAYYPMALVHCPFCPTPDSEDWDPTShgsKTYKGQPEYFGDMVAYVDKIVGRIDQKLGDLGIRENT 284
Cdd:cd16151   158 FLIDFIERNKDQPFFAYYPMVLVHDPFVPTPDSPDWDPDD---KRKKDDPEYFPDMVAYMDKLVGKLVDKLEELGLRENT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 285 LLIFTGDNGTDKPIVTQTRFGEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPANLTI 364
Cdd:cd16151   235 IIIFTGDNGTHRPITSRTNGREVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPL 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270232598 365 DGQSFLPVLQGIEGQGRESMFMWYERNGRPNKAREFARNQRYKLYGDGSFFDVEMDRNEKSPL 427
Cdd:cd16151   315 DGRSFAPQLLGKTGSPRREWIYWYYRNPHKKFGSRFVRTKRYKLYADGRFFDLREDPLEKNPL 377
 
Name Accession Description Interval E-value
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
48-427 0e+00

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: 616.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGMTNKRNYVKFGMLDRKQTTFAH 127
Cdd:cd16151     1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQKTFGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 128 LLKSAGYRTCIAGKWQLGS---ELDSPRHFGFEESLLWQHTRGRMDSQKRDTRYPNprlERNGTKEDYDEGEFSSDLFAD 204
Cdd:cd16151    81 LLKDAGYATAIAGKWQLGGgrgDGDYPHEFGFDEYCLWQLTETGEKYSRPATPTFN---IRNGKLLETTEGDYGPDLFAD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 205 FLCDFMETNRDQPFLAYYPMALVHCPFCPTPDSEDWDPTShgsKTYKGQPEYFGDMVAYVDKIVGRIDQKLGDLGIRENT 284
Cdd:cd16151   158 FLIDFIERNKDQPFFAYYPMVLVHDPFVPTPDSPDWDPDD---KRKKDDPEYFPDMVAYMDKLVGKLVDKLEELGLRENT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 285 LLIFTGDNGTDKPIVTQTRFGEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPANLTI 364
Cdd:cd16151   235 IIIFTGDNGTHRPITSRTNGREVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPL 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270232598 365 DGQSFLPVLQGIEGQGRESMFMWYERNGRPNKAREFARNQRYKLYGDGSFFDVEMDRNEKSPL 427
Cdd:cd16151   315 DGRSFAPQLLGKTGSPRREWIYWYYRNPHKKFGSRFVRTKRYKLYADGRFFDLREDPLEKNPL 377
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
22-449 3.01e-100

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 305.26  E-value: 3.01e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  22 ILACSLAFTAASVPADEPspqrsgDRPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRV 100
Cdd:COG3119     4 LLLLLLALLAAAAAAAAA------KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTsPVCSPSRA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 101 KLMTGMTNKRNYV------KFGMLDRKQTTFAHLLKSAGYRTCIAGKWQLgseldsprhfgfeesllwqhtrgrmdsqkr 174
Cdd:COG3119    78 SLLTGRYPHRTGVtdngegYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------------ 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 175 dtrypnprlerngtkedydegeFSSDLFADFLCDFMETNR--DQPFLAYYPMALVHCPFCPTPDSED------------W 240
Cdd:COG3119   128 ----------------------YLTDLLTDKAIDFLERQAdkDKPFFLYLAFNAPHAPYQAPEEYLDkydgkdiplppnL 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 241 DPTSHGSKTYKGQPEYFGDMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGtdkpivtqTRFGE--VVGAKGEMVDAG 318
Cdd:COG3119   186 APRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNG--------PSLGEhgLRGGKGTLYEGG 257
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 319 NHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPANLtiDGQSFLPVLQGIEGQGRESMFMWYERNGrPNKAr 398
Cdd:COG3119   258 IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDL--DGRSLLPLLTGEKAEWRDYLYWEYPRGG-GNRA- 333
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1270232598 399 efARNQRYKL------YGDGSFFDVEMDRNEkspLQSLTDDQKEIRSKLQAKIDSFA 449
Cdd:COG3119   334 --IRTGRWKLiryyddDGPWELYDLKNDPGE---TNNLAADYPEVVAELRALLEAWL 385
Sulfatase pfam00884
Sulfatase;
48-356 4.76e-44

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 156.43  E-value: 4.76e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKRNYVKFGMLD---RKQT 123
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSgGTLTAPSRFALLTGLPPHNFGSYVSTPVglpRTEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 124 TFAHLLKSAGYRTCIAGKWQLG-SELDSPRHFGFEESLLWQHtrGRMDSQKRDTRYPNPRLerngtkedydeGEFSSDLF 202
Cdd:pfam00884  81 SLPDLLKRAGYNTGAIGKWHLGwYNNQSPCNLGFDKFFGRNT--GSDLYADPPDVPYNCSG-----------GGVSDEAL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 203 ADFLCDFmETNRDQPFLAYY-PMAlVHCPFcptPDSEDWDPTSHGSKTYKG----QPEYFGDMVAYVDKIVGRIDQKLGD 277
Cdd:pfam00884 148 LDEALEF-LDNNDKPFFLVLhTLG-SHGPP---YYPDRYPEKYATFKPSSCseeqLLNSYDNTLLYTDDAIGRVLDKLEE 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270232598 278 LGIRENTLLIFTGDNGtdkPIVTQTRFGEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADA 356
Cdd:pfam00884 223 NGLLDNTLVVYTSDHG---ESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
PRK13759 PRK13759
arylsulfatase; Provisional
47-446 2.25e-37

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 142.50  E-value: 2.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMTNKRNyvkfGMLDRKQ--- 122
Cdd:PRK13759    6 KPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAvPSCTPARAALLTGLSQWHH----GRVGYGDvvp 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 123 ----TTFAHLLKSAGYRT-CIaGKWQLGSEldSPRHfGFEESLL---WQHTrGRMDSQKR-----DTRY--------PNP 181
Cdd:PRK13759   82 wnykNTLPQEFRDAGYYTqCI-GKMHVFPQ--RNLL-GFHNVLLhdgYLHS-GRNEDKSQfdfvsDYLAwlrekapgKDP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 182 RLERNGTKE--------DYDEGEFSSDLFADFLCDFMET-NRDQPFLAYYPMALVHCPF--------------CPTPDSE 238
Cdd:PRK13759  157 DLTDIGWDCnswvarpwDLEERLHPTNWVGSESIEFLRRrDPTKPFFLKMSFARPHSPYdppkryfdmykdadIPDPHIG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 239 DW------DPTSHGSKTYKGQ-PE---------YFGDMvAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNgtdkpivtqt 302
Cdd:PRK13759  237 DWeyaedqDPEGGSIDALRGNlGEeyarraraaYYGLI-THIDHQIGRFLQALKEFGLLDNTIILFVSDH---------- 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 303 rfGEVVG-----AKGEMVDAGNHVTCIAKWPG-VIQPQRLTS--QIIDFSDFLPTMCEVADAEVPAnlTIDGQSFLPVLQ 374
Cdd:PRK13759  306 --GDMLGdhylfRKGYPYEGSAHIPFIIYDPGgLLAGNRGTVidQVVELRDIMPTLLDLAGGTIPD--DVDGRSLKNLIF 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 375 GIEGQGRESM----FMWYERNGRPNKARE----FARNQRYKLygdgsfFDVEMDRNEKSPLQSLTDDQKEIRSKLQAKID 446
Cdd:PRK13759  382 GQYEGWRPYLhgehALGYSSDNYLTDGKWkyiwFSQTGEEQL------FDLKKDPHELHNLSPSEKYQPRLREMRKKLVD 455
 
Name Accession Description Interval E-value
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
48-427 0e+00

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: 616.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGMTNKRNYVKFGMLDRKQTTFAH 127
Cdd:cd16151     1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQKTFGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 128 LLKSAGYRTCIAGKWQLGS---ELDSPRHFGFEESLLWQHTRGRMDSQKRDTRYPNprlERNGTKEDYDEGEFSSDLFAD 204
Cdd:cd16151    81 LLKDAGYATAIAGKWQLGGgrgDGDYPHEFGFDEYCLWQLTETGEKYSRPATPTFN---IRNGKLLETTEGDYGPDLFAD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 205 FLCDFMETNRDQPFLAYYPMALVHCPFCPTPDSEDWDPTShgsKTYKGQPEYFGDMVAYVDKIVGRIDQKLGDLGIRENT 284
Cdd:cd16151   158 FLIDFIERNKDQPFFAYYPMVLVHDPFVPTPDSPDWDPDD---KRKKDDPEYFPDMVAYMDKLVGKLVDKLEELGLRENT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 285 LLIFTGDNGTDKPIVTQTRFGEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPANLTI 364
Cdd:cd16151   235 IIIFTGDNGTHRPITSRTNGREVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPL 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270232598 365 DGQSFLPVLQGIEGQGRESMFMWYERNGRPNKAREFARNQRYKLYGDGSFFDVEMDRNEKSPL 427
Cdd:cd16151   315 DGRSFAPQLLGKTGSPRREWIYWYYRNPHKKFGSRFVRTKRYKLYADGRFFDLREDPLEKNPL 377
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
22-449 3.01e-100

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 305.26  E-value: 3.01e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  22 ILACSLAFTAASVPADEPspqrsgDRPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRV 100
Cdd:COG3119     4 LLLLLLALLAAAAAAAAA------KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTsPVCSPSRA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 101 KLMTGMTNKRNYV------KFGMLDRKQTTFAHLLKSAGYRTCIAGKWQLgseldsprhfgfeesllwqhtrgrmdsqkr 174
Cdd:COG3119    78 SLLTGRYPHRTGVtdngegYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------------ 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 175 dtrypnprlerngtkedydegeFSSDLFADFLCDFMETNR--DQPFLAYYPMALVHCPFCPTPDSED------------W 240
Cdd:COG3119   128 ----------------------YLTDLLTDKAIDFLERQAdkDKPFFLYLAFNAPHAPYQAPEEYLDkydgkdiplppnL 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 241 DPTSHGSKTYKGQPEYFGDMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGtdkpivtqTRFGE--VVGAKGEMVDAG 318
Cdd:COG3119   186 APRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNG--------PSLGEhgLRGGKGTLYEGG 257
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 319 NHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPANLtiDGQSFLPVLQGIEGQGRESMFMWYERNGrPNKAr 398
Cdd:COG3119   258 IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDL--DGRSLLPLLTGEKAEWRDYLYWEYPRGG-GNRA- 333
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1270232598 399 efARNQRYKL------YGDGSFFDVEMDRNEkspLQSLTDDQKEIRSKLQAKIDSFA 449
Cdd:COG3119   334 --IRTGRWKLiryyddDGPWELYDLKNDPGE---TNNLAADYPEVVAELRALLEAWL 385
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
47-427 2.16e-90

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: 280.22  E-value: 2.16e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKRNyvkfGM-------- 117
Cdd:cd16026     1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAaAPVCSPSRAALLTGRYPVRV----GLpgvvgppg 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 118 ----LDRKQTTFAHLLKSAGYRTCIAGKWQLGSELDS-PRHFGFEE--SLLWQHTRGRMDSQKRDTRYPNPRLERNGTKE 190
Cdd:cd16026    77 skggLPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFlPTRHGFDEyfGIPYSNDMWPFPLYRNDPPGPLPPLMENEEVI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 191 DYDEGEFS-SDLFADFLCDFMETNRDQPFLAYYPMALVHCP-FCptpdSEDWDPTSHGSKtykgqpeyFGDMVAYVDKIV 268
Cdd:cd16026   157 EQPADQSSlTQRYTDEAVDFIERNKDQPFFLYLAHTMPHVPlFA----SEKFKGRSGAGL--------YGDVVEELDWSV 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 269 GRIDQKLGDLGIRENTLLIFTGDNGtdkPIVTQTRF----GEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFS 344
Cdd:cd16026   225 GRILDALKELGLEENTLVIFTSDNG---PWLEYGGHggsaGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGTVSDELASTM 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 345 DFLPTMCEVADAEVPANLTIDGQSFLPVLQGIEGQGRESMFmWYERNGRPNKarefARNQRYKL-----YGDGSFFDVEM 419
Cdd:cd16026   302 DLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFF-YYYDGGDLQA----VRSGRWKLhlpttYRTGTDPGGLD 376

                  ....*...
gi 1270232598 420 DRNEKSPL 427
Cdd:cd16026   377 PTKLEPPL 384
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
48-446 8.01e-89

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: 276.35  E-value: 8.01e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGMTNKRN-----YVKFGMLDRKQ 122
Cdd:cd16146     1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTgvwhtILGRERMRLDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 123 TTFAHLLKSAGYRTCIAGKWQLGselDSPRHF----GFEESL-----LWQHTRGRMDSQkrdtrYPNPRLERNGTKEDYd 193
Cdd:cd16146    81 TTLAEVFKDAGYRTGIFGKWHLG---DNYPYRpqdrGFDEVLghgggGIGQYPDYWGND-----YFDDTYYHNGKFVKT- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 194 EGeFSSDLFADFLCDFMETNRDQPFLAYYPMALVHCPF-CPTpdsEDWDPtshgsktYKGQ------PEYFGdMVAYVDK 266
Cdd:cd16146   152 EG-YCTDVFFDEAIDFIEENKDKPFFAYLATNAPHGPLqVPD---KYLDP-------YKDMglddklAAFYG-MIENIDD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 267 IVGRIDQKLGDLGIRENTLLIFTGDNGTDKPivTQTRF-GEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSD 345
Cdd:cd16146   220 NVGRLLAKLKELGLEENTIVIFMSDNGPAGG--VPKRFnAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHID 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 346 FLPTMCEVADAEVPANLTIDGQSFLPVLQGIEGQGRESMFMWY--ERNGRPNKAREFA-RNQRYKLYGDGSF----FDVE 418
Cdd:cd16146   298 LLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTLFTHsgRWPPPPKKKRNAAvRTGRWRLVSPKGFqpelYDIE 377
                         410       420
                  ....*....|....*....|....*...
gi 1270232598 419 MDRNEKsplQSLTDDQKEIRSKLQAKID 446
Cdd:cd16146   378 NDPGEE---NDVADEHPEVVKRLKAAYE 402
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
48-448 3.95e-88

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: 275.19  E-value: 3.95e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMT------------NKRNYVK 114
Cdd:cd16144     1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAaAPVCSPSRASILTGQYparlgitdvipgRRGPPDN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 115 FGM--------LDRKQTTFAHLLKSAGYRTCIAGKWQLG-SELDSPRHFGFEESLlwqHTRGrmdsQKRDTRYPNPRLER 185
Cdd:cd16144    81 TKLipppsttrLPLEEVTIAEALKDAGYATAHFGKWHLGgEGGYGPEDQGFDVNI---GGTG----NGGPPSYYFPPGKP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 186 NGTKEDYDEGEFSSDLFADFLCDFMETNRDQPFLAYYPMALVHCPFCPTPDSEDwDPTSHGSKTYKGQ--PEYFGdMVAY 263
Cdd:cd16144   154 NPDLEDGPEGEYLTDRLTDEAIDFIEQNKDKPFFLYLSHYAVHTPIQARPELIE-KYEKKKKGLRKGQknPVYAA-MIES 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 264 VDKIVGRIDQKLGDLGIRENTLLIFTGDNG---TDKPIVTQT---RFGevvgaKGEMVDAGNHVTCIAKWPGVIQPQRLT 337
Cdd:cd16144   232 LDESVGRILDALEELGLADNTLVIFTSDNGglsTRGGPPTSNaplRGG-----KGSLYEGGIRVPLIVRWPGVIKPGSVS 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 338 SQIIDFSDFLPTMCEVADAEVPANLTIDGQSFLPVLQGIEGQ-GRESMFmWYERNGRPNKAREFA--RNQRYKL---YGD 411
Cdd:cd16144   307 DVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADlPRRALF-WHFPHYHGQGGRPASaiRKGDWKLiefYED 385
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1270232598 412 GSF--FDVEMDRNEKsplQSLTDDQKEIRSKLQAKIDSF 448
Cdd:cd16144   386 GRVelYNLKNDIGET---NNLAAEMPEKAAELKKKLDAW 421
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
48-424 2.06e-85

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: 267.92  E-value: 2.06e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGM----TNKR-NYVKFGM--LD 119
Cdd:cd16145     1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAgAPVCAPSRASLLTGLhtghTRVRgNSEPGGQdpLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 120 RKQTTFAHLLKSAGYRTCIAGKWQLGSELD--SPRHFGFEESLlwqhtrGRMDSQKRDTRYPnPRLERNGTKEDYDE--- 194
Cdd:cd16145    81 PDDVTLAEVLKKAGYATAAFGKWGLGGPGTpgHPTKQGFDYFY------GYLDQVHAHNYYP-EYLWRNGEKVPLPNnvi 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 195 -------------GEFSSDLFADFLCDFMETNRDQPFLAYYPMALVHCPFCPTPDSEDWD-PTSHGSKTYKGQPE---YF 257
Cdd:cd16145   154 ppldegnnaggggGTYSHDLFTDEALDFIRENKDKPFFLYLAYTLPHAPLQVPDDGPYKYkPKDPGIYAYLPWPQpekAY 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 258 GDMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGTDK---PIVTQTRF---GEVVGAKGEMVDAGNHVTCIAKWPGVI 331
Cdd:cd16145   234 AAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeggSEHDPDFFdsnGPLRGYKRSLYEGGIRVPFIARWPGKI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 332 QPQRLTSQIIDFSDFLPTMCEVADAEVPANltIDGQSFLPVLQGIEGQGRESMFMWYERNGRPNKArefARNQRYKLY-- 409
Cdd:cd16145   314 PAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYLYWEFYEGGGAQA---VRMGGWKAVrh 388
                         410
                  ....*....|....*....
gi 1270232598 410 --GDGSF--FDVEMDRNEK 424
Cdd:cd16145   389 gkKDGPFelYDLSTDPGET 407
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
48-386 5.67e-71

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: 229.78  E-value: 5.67e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGS-NGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKRNYVKFG--------M 117
Cdd:cd16143     1 PNIVIILADDLGYGDISCyNPDSKIPTPNIDRLAAEGMRFTDAHSpSSVCTPSRYGLLTGRYPWRSRLKGGvlggfsppL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 118 LDRKQTTFAHLLKSAGYRTCIAGKWqlgseldsprHFGFEESLLWQHTRGRMDSQKRD-TRYPnprleRNGTKE---DYD 193
Cdd:cd16143    81 IEPDRVTLAKMLKQAGYRTAMVGKW----------HLGLDWKKKDGKKAATGTGKDVDySKPI-----KGGPLDhgfDYY 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 194 EGEFSS---DLFADFLCDFMETNR--DQPFLAYYPMALVHCPFCPtpdSEDWDPTSHGSKtykgqpeyFGDMVAYVDKIV 268
Cdd:cd16143   146 FGIPASevlPTLTDKAVEFIDQHAkkDKPFFLYFALPAPHTPIVP---SPEFQGKSGAGP--------YGDFVYELDWVV 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 269 GRIDQKLGDLGIRENTLLIFTGDNGTDKPIVTQTRF-------GEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQII 341
Cdd:cd16143   215 GRILDALKELGLAENTLVIFTSDNGPSPYADYKELEkfghdpsGPLRGMKADIYEGGHRVPFIVRWPGKIPAGSVSDQLV 294
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1270232598 342 DFSDFLPTMCEVADAEVPANLTIDGQSFLPVLQGIEGQ-GRESMFM 386
Cdd:cd16143   295 SLTDLFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQeVRESLVH 340
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
46-443 6.81e-71

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: 230.49  E-value: 6.81e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  46 DRPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCY-SQPICTPSRVKLMTGMTNKRNYVKFG---MLDRK 121
Cdd:cd16031     1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFvTTSICAPSRASILTGQYSHRHGVTDNngpLFDAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 122 QTTFAHLLKSAGYRTCIAGKWQLGSELDSPR-HFGFEESLLWQHTrgrmdsqkrdtrYPNPRLERNGtKEDYDEGeFSSD 200
Cdd:cd16031    81 QPTYPKLLRKAGYQTAFIGKWHLGSGGDLPPpGFDYWVSFPGQGS------------YYDPEFIENG-KRVGQKG-YVTD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 201 LFADFLCDFMETNR-DQPFLAYYPMALVHCPFCPTP-------DSEDWDPTSHGSKTYKGQPEYFGD------------- 259
Cdd:cd16031   147 IITDKALDFLKERDkDKPFCLSLSFKAPHRPFTPAPrhrglyeDVTIPEPETFDDDDYAGRPEWAREqrnrirgvldgrf 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 260 ---------------MVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNG--------TDKpivtqtRFgevvgakgeMVD 316
Cdd:cd16031   227 dtpekyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGfflgehglFDK------RL---------MYE 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 317 AGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPANltIDGQSFLPVLQGIEGQGRESMFM--WYERNGRP 394
Cdd:cd16031   292 ESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDWRKEFYyeYYEEPNFH 369
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270232598 395 NKAREFA-RNQRYKL---YGDGSF---FDVEMDRNEkspLQSLTDD------QKEIRSKLQA 443
Cdd:cd16031   370 NVPTHEGvRTERYKYiyyYGVWDEeelYDLKKDPLE---LNNLANDpeyaevLKELRKRLEE 428
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
48-368 6.11e-69

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: 219.23  E-value: 6.11e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMTNKR-----NYVKFGMLDRK 121
Cdd:cd16022     1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVAsPVCSPSRASLLTGRYPHRhgvrgNVGNGGGLPPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 122 QTTFAHLLKSAGYRTCIAGKWqlgseldsprhfgfeesllwqHTRGrmdsqkrdtrypnprlerngtkedydegefssdl 201
Cdd:cd16022    81 EPTLAELLKEAGYRTALIGKW---------------------HDEA---------------------------------- 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 202 fadflCDFMETN-RDQPFLAYYPMALVHCPFcptpdsedwdptshgsktykgqpEYFGdMVAYVDKIVGRIDQKLGDLGI 280
Cdd:cd16022   106 -----IDFIERRdKDKPFFLYVSFNAPHPPF-----------------------AYYA-MVSAIDDQIGRILDALEELGL 156
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 281 RENTLLIFTGDNGtDKPIVTQTRFGevvgaKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPA 360
Cdd:cd16022   157 LDNTLIVFTSDHG-DMLGDHGLRGK-----KGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEPPE 230

                  ....*...
gi 1270232598 361 nlTIDGQS 368
Cdd:cd16022   231 --GLDGRS 236
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
48-448 1.66e-68

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: 222.77  E-value: 1.66e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDyQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGM---TNK--RNYVKFGMLDRK 121
Cdd:cd16027     1 PNILWIIADDLSPDLGGYGGNVV-KTPNLDRLAAEGVRFTNAFTtAPVCSPSRSALLTGLyphQNGahGLRSRGFPLPDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 122 QTTFAHLLKSAGYRTCIAGKWqlgseldsprHFGFEESLLWQHtrgrmdsqkrdtrYPNPRLERNGTKEDYdegefsSDL 201
Cdd:cd16027    80 VKTLPELLREAGYYTGLIGKT----------HYNPDAVFPFDD-------------EMRGPDDGGRNAWDY------ASN 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 202 FADFLcdfMETNRDQPFLAYYPMALVHcpfcptpdsEDWDPTSHGSKTYKGQ----PEYFGD-------------MVAYV 264
Cdd:cd16027   131 AADFL---NRAKKGQPFFLWFGFHDPH---------RPYPPGDGEEPGYDPEkvkvPPYLPDtpevredladyydEIERL 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 265 DKIVGRIDQKLGDLGIRENTLLIFTGDNGTDKPivtqtrfgevvGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFS 344
Cdd:cd16027   199 DQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP-----------RAKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFI 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 345 DFLPTMCEVADAEVPANLtiDGQSFLPVLQGIEGQGRESMFMWYERNG-RPNKAReFARNQRYKL---YGDGSFFDVEMD 420
Cdd:cd16027   268 DLAPTLLDLAGIEPPEYL--QGRSFLPLLKGEKDPGRDYVFAERDRHDeTYDPIR-SVRTGRYKYirnYMPEELYDLKND 344
                         410       420       430
                  ....*....|....*....|....*....|
gi 1270232598 421 RNEkspLQSLTDD--QKEIRSKLQAKIDSF 448
Cdd:cd16027   345 PDE---LNNLADDpeYAEVLEELRAALDAW 371
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
48-389 2.30e-66

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: 217.02  E-value: 2.30e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGS---LDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGmtnkRNYVKFGM------- 117
Cdd:cd16142     1 PNILVILGDDIGWGDLGCYGGgigRGAPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITG----RHPIRTGLttvglpg 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 118 ----LDRKQTTFAHLLKSAGYRTCIAGKWQLGselDSPRHF----GFEEslLWQHTRGRMDsqkrdtrypnprlerngtk 189
Cdd:cd16142    77 spggLPPWEPTLAELLKDAGYATAQFGKWHLG---DEDGRLptdhGFDE--FYGNLYHTID------------------- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 190 edydegefssDLFADFLCDFMETNR--DQPFLAYYPMALVHCPFCPTPDSEdwdptshGSKTYKGQpeyFGDMVAYVDKI 267
Cdd:cd16142   133 ----------EEIVDKAIDFIKRNAkaDKPFFLYVNFTKMHFPTLPSPEFE-------GKSSGKGK---YADSMVELDDH 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 268 VGRIDQKLGDLGIRENTLLIFTGDNGTDK---PIVTQTRFGevvGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFS 344
Cdd:cd16142   193 VGQILDALDELGIADNTIVIFTTDNGPEQdvwPDGGYTPFR---GEKGTTWEGGVRVPAIVRWPGKIKPGRVSNEIVSHL 269
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1270232598 345 DFLPTMCEVADAEVPANLT------IDGQSFLPVLQGIEGQGRESMFMWYE 389
Cdd:cd16142   270 DWFPTLAALAGAPDPKDKLlgkdrhIDGVDQSPFLLGKSEKSRRSEFFYFG 320
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
48-427 7.50e-59

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: 198.16  E-value: 7.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGmtnkRNYVKFGM---------- 117
Cdd:cd16029     1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTG----RYPIHTGMqhgvilagep 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 118 --LDRKQTTFAHLLKSAGYRTCIAGKWQLG--SELDSPRHFGFEESLL--------WQHTRGrmdsqkRDTRYPNPRLER 185
Cdd:cd16029    77 ygLPLNETLLPQYLKELGYATHLVGKWHLGfyTWEYTPTNRGFDSFYGyyggaedyYTHTSG------GANDYGNDDLRD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 186 NGTKEDYDEGEFSSDLFADFLCDFMET-NRDQPFLAYYPMALVHCP-------FCPTPDSEDWDPTsHGSKTYKGqpeyf 257
Cdd:cd16029   151 NEEPAWDYNGTYSTDLFTDRAVDIIENhDPSKPLFLYLAFQAVHAPlqvppeyADPYEDKFAHIKD-EDRRTYAA----- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 258 gdMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGtdkpivTQTRFGEVV------GAKGEMVDAGNHVTCIAkWPGVI 331
Cdd:cd16029   225 --MVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG------GPTGGGDGGsnyplrGGKNTLWEGGVRVPAFV-WSPLL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 332 QPQRLTS--QIIDFSDFLPTMCEVADAEVPANLTIDGQSFLPVLQGIEGQGRESMFmwYERNGRPNKAREFA-RNQRYKL 408
Cdd:cd16029   296 PPKRGTVsdGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEIL--LNIDDITRTTGGAAiRVGDWKL 373
                         410
                  ....*....|....*....
gi 1270232598 409 YGDGSFFDVEMDRNEKSPL 427
Cdd:cd16029   374 IVGKPLFNIENDPCERNDL 392
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
46-423 2.51e-55

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: 189.19  E-value: 2.51e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  46 DRPNIVLIMADDMGFECIGSNGSlDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGMTNKRNYVKF---------- 115
Cdd:cd16025     1 GRPNILLILADDLGFSDLGCFGG-EIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTmaelatgkpg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 116 --GMLDRKQTTFAHLLKSAGYRTCIAGKWQLGseldsprhfgfeesllwqhtrgrmdsqkrdtrypnprlerngtKEDYd 193
Cdd:cd16025    80 yeGYLPDSAATIAEVLKDAGYHTYMSGKWHLG-------------------------------------------PDDY- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 194 egeFSSDLFADFLCDFMETNR--DQPFLAYYPMALVHCPF---------------------------------------- 231
Cdd:cd16025   116 ---YSTDDLTDKAIEYIDEQKapDKPFFLYLAFGAPHAPLqapkewidkykgkydagwdalreerlerqkelglipadtk 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 232 -CPTPDS-EDWD-PTSHGSKTYKGQPEYFGDMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGTDkpivtqtrfGEV- 307
Cdd:cd16025   193 lTPRPPGvPAWDsLSPEEKKLEARRMEVYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGAS---------AEPg 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 308 ---VGA------KGEMVDAGNHVTCIAKWPGVI-QPQRLTSQIIDFSDFLPTMCEVADAEVPAN------LTIDGQSFLP 371
Cdd:cd16025   264 wanASNtpfrlyKQASHEGGIRTPLIVSWPKGIkAKGGIRHQFAHVIDIAPTILELAGVEYPKTvngvpqLPLDGVSLLP 343
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270232598 372 VLQGIEGQGRESmFMWYERNGrpNKArefARNQRYKL------YGDGSF---FDVEMDRNE 423
Cdd:cd16025   344 TLDGAAAPSRRR-TQYFELFG--NRA---IRKGGWKAvalhppPGWGDQwelYDLAKDPSE 398
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
47-428 3.43e-55

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: 188.06  E-value: 3.43e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  47 RPNIVLIMADDMGFECIGSNGS-LDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMTNKRNYV-------KFGM 117
Cdd:cd16161     1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAaSVCSPSRASLMTGRLGLRNGVghnflptSVGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 118 LDRKQTTFAHLLKSAGYRTCIAGKWQLGseldsprhfgfeesllwqhtrgrmdsqKRDTRYPNPRlerngtKEDYDEG-E 196
Cdd:cd16161    81 LPLNETTLAEVLRQAGYATGMIGKWHLG---------------------------QREAYLPNSR------GFDYYFGiP 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 197 FSSDL-----FADFLCDFME--TNRDQPFLAYYPMALVHCPFCPTPDSEDwdPTSHGSKtykgqpeyFGDMVAYVDKIVG 269
Cdd:cd16161   128 FSHDSsladrYAQFATDFIQraSAKDRPFFLYAALAHVHVPLANLPRFQS--PTSGRGP--------YGDALQEMDDLVG 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 270 RIDQKLGDLGIRENTLLIFTGDNG--------TDKPIVTQTR-FGEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQI 340
Cdd:cd16161   198 QIMDAVKHAGLKDNTLTWFTSDNGpwevkcelAVGPGTGDWQgNLGGSVAKASTWEGGHREPAIVYWPGRIPANSTSAAL 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 341 IDFSDFLPTMCEVADAEVPANLTIDGQSFLPVLQGIEGQGRESMFMWyerNGRPNKAREF--ARNQRYKLY--------G 410
Cdd:cd16161   278 VSTLDIFPTVVALAGASLPPGRIYDGKDLSPVLFGGSKTGHRCLFHP---NSGAAGAGALsaVRCGDYKAHyatggalaC 354
                         410       420
                  ....*....|....*....|....*....
gi 1270232598 411 DGSF-----------FDVEMDRNEKSPLQ 428
Cdd:cd16161   355 CGSTgpklyhdppllFDLEVDPAESFPLT 383
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
47-428 5.69e-55

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: 188.16  E-value: 5.69e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGM---TNK--RNYVkfgMLDR 120
Cdd:cd16034     1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNyPVCSPYRASLLTGQyplTNGvfGNDV---PLPP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 121 KQTTFAHLLKSAGYRTCIAGKWQL-GSELDSPRH----------FGFEEsllWqhtRGRMdsqkRDTRYPNPRLERNGTK 189
Cdd:cd16034    78 DAPTIADVLKDAGYRTGYIGKWHLdGPERNDGRAddytppperrHGFDY---W---KGYE----CNHDHNNPHYYDDDGK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 190 EDYDEGeFSSDLFADFLCDFMET--NRDQPFLAYYPMALVHCPF--CPTPDSEDWDP---------------TSHGSKTY 250
Cdd:cd16034   148 RIYIKG-YSPDAETDLAIEYLENqaDKDKPFALVLSWNPPHDPYttAPEEYLDMYDPkklllrpnvpedkkeEAGLREDL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 251 KGqpeYFGdMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNgtdkpivtqtrfGEVVGAKGEM-----VDAGNHVTCIA 325
Cdd:cd16034   227 RG---YYA-MITALDDNIGRLLDALKELGLLENTIVVFTSDH------------GDMLGSHGLMnkqvpYEESIRVPFII 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 326 KWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPAnlTIDGQSFLPVLQGIEGQGRESM-FMWYERNGRPN----KAREF 400
Cdd:cd16034   291 RYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPD--TVEGRDLSPLLLGGKDDEPDSVlLQCFVPFGGGSardgGEWRG 368
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1270232598 401 ARNQRYKLY----GDGSFFDvemdrNEKSPLQ 428
Cdd:cd16034   369 VRTDRYTYVrdknGPWLLFD-----NEKDPYQ 395
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
48-431 1.28e-52

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: 183.80  E-value: 1.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKRNYVKFGMLD------- 119
Cdd:cd16158     2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSsSPVCSPSRAALLTGRYQVRSGVYPGVFYpgsrggl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 120 -RKQTTFAHLLKSAGYRTCIAGKWQLGSELDS---PRHFGFEESLLWQHTRGRMDSQKRdTRYPnPRLERNGTkedYDEG 195
Cdd:cd16158    82 pLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGtylPTHQGFDHYLGIPYSHDQGPCQNL-TCFP-PNIPCFGG---CDQG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 196 EFSSDLFAD-------------------FLCDFMETN--RDQPFLAYYPMALVHCPfcptpdsedwdptSHGSKTYKGQP 254
Cdd:cd16158   157 EVPCPLFYNesivqqpvdlltleeryakFAKDFIADNakEGKPFFLYYASHHTHYP-------------QFAGQKFAGRS 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 255 EY--FGDMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGtdkPIVTQTRFGEVVG----AKGEMVDAGNHVTCIAKWP 328
Cdd:cd16158   224 SRgpFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNG---PSTMRKSRGGNAGllkcGKGTTYEGGVREPAIAYWP 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 329 GVIQPQRlTSQIIDFSDFLPTMCEVADAEVPaNLTIDGQSFLPVLQGIEGQGRESMFmWYERNGRPNKAREFARNQRYK- 407
Cdd:cd16158   301 GRIKPGV-THELASTLDILPTIAKLAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFF-YYPTSPDPDKGVFAVRWGKYKa 377
                         410       420
                  ....*....|....*....|....*
gi 1270232598 408 -LYGDGSFFDVEMDRNEKSPLQSLT 431
Cdd:cd16158   378 hFYTQGAAHSGTTPDKDCHPSAELT 402
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
47-454 2.36e-48

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: 173.24  E-value: 2.36e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMT-------GMTNKRNYVKF--- 115
Cdd:cd16159     1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAaAPLCTPSRAAFLTgrypirsGMASSHGMRVIlft 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 116 ---GMLDRKQTTFAHLLKSAGYRTCIAGKWQLG----SELD---SPRHFGF-----------------EESLLWQ----- 163
Cdd:cd16159    81 assGGLPPNETTFAEVLKQQGYSTALIGKWHLGlhceSRNDfchHPLNHGFdyfyglpltnlkdcgdgSNGEYDLsfdpl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 164 -------------HTRGRMDSQKRDTR------------------------YPNPRLERNgtkEDYDEGEFSSDLFADFL 206
Cdd:cd16159   161 fplltafvlitalTIFLLLYLGAVSKRffvfllilsllfislfflllitnrYFNCILMRN---HEVVEQPMSLENLTQRL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 207 CD----FMETNRDQPFLAYYPMALVHCPFCPTPdsEDWDPTSHGsktykgqpEYfGDMVAYVDKIVGRIDQKLGDLGIRE 282
Cdd:cd16159   238 TKeaisFLERNKERPFLLVMSFLHVHTALFTSK--KFKGRSKHG--------RY-GDNVEEMDWSVGQILDALDELGLKD 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 283 NTLLIFTGDNGtdkPIVTQTRFGEVV---------GAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEV 353
Cdd:cd16159   307 NTFVYFTSDNG---GHLEEISVGGEYgggnggiygGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAAL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 354 ADAEVPANLTIDGQSFLPVLQGIEGQG-RESMFM----------WYERNGR---------PNKAREFARNQRYKL---YG 410
Cdd:cd16159   384 AGAPLPSDRIIDGRDLMPLLTGQEKRSpHEFLFHycgaelhavrYRPRDGGavwkahyftPNFYPGTEGCCGTLLcrcFG 463
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1270232598 411 DGS-------FFDVEMDRNEKSPLQSLTDDQKEIRSKLQAKIDSFANIIPP 454
Cdd:cd16159   464 DSVthhdpplLFDLSADPSESNPLDPTDEPYQEIIKKILEAVAEHQSSIEP 514
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
48-444 5.54e-46

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: 164.32  E-value: 5.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKR-----NYVKFGMLDRK 121
Cdd:cd16033     1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTpSPVCCPARASLLTGLYPHEhgvlnNVENAGAYSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 122 ----QTTFAHLLKSAGYRTCIAGKWQLGSElDSPRHFGFEEsllwqhtrgrmdsqkrdtrypnprlerNGTKEDYDEGeF 197
Cdd:cd16033    81 lppgVETFSEDLREAGYRNGYVGKWHVGPE-ETPLDYGFDE---------------------------YLPVETTIEY-F 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 198 SSDLFADFLCDFMEtnRDQPFLAYY----PmalvHCPFCPTPDSEDW-DPTS---HGS--KTYKGQPE------------ 255
Cdd:cd16033   132 LADRAIEMLEELAA--DDKPFFLRVnfwgP----HDPYIPPEPYLDMyDPEDiplPESfaDDFEDKPYiyrrerkrwgvd 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 256 -------------YFGdMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNgtdkpivtqtrfGEVVGAKGeMVDAGN--- 319
Cdd:cd16033   206 tedeedwkeiiahYWG-YITLIDDAIGRILDALEELGLADDTLVIFTSDH------------GDALGAHR-LWDKGPfmy 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 320 ----HVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPanLTIDGQSFLPVLQG-IEGQGRESMFMwyERNGrp 394
Cdd:cd16033   272 eetyRIPLIIKWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVP--PKVDGRSLLPLLRGeQPEDWRDEVVT--EYNG-- 345
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270232598 395 nkaREF------ARNQRYKL-YGDGSF---FDVEMDRNEkspLQSLTDDQ--KEIRSKLQAK 444
Cdd:cd16033   346 ---HEFylpqrmVRTDRYKYvFNGFDIdelYDLESDPYE---LNNLIDDPeyEEILREMRTR 401
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
47-373 7.18e-46

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: 164.91  E-value: 7.18e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGmtnkRNYVKFGM-------- 117
Cdd:cd16160     1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSaDSVCTPSRAALLTG----RLPIRSGMyggtrvfl 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 118 ------LDRKQTTFAHLLKSAGYRTCIAGKWQLG-SELDS------PRHFGFE-------ESLLWQhtrgrMDSQKRDTR 177
Cdd:cd16160    77 pwdiggLPKTEVTMAEALKEAGYTTGMVGKWHLGiNENNHsdgahlPSHHGFDfvgtnlpFTNSWA-----CDDTGRHVD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 178 YPNPRLERNGTKEDYDEGEFSSDLFADFLCD----FMETNRDQPFLAYYPMALVHCP-FCptpdSEDWDPTSHgsktyKG 252
Cdd:cd16160   152 FPDRSACFLYYNDTIVEQPIQHEHLTETLVGdaksFIEDNQENPFFLYFSFPQTHTPlFA----SKRFKGKSK-----RG 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 253 QpeyFGDMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGTDKPIV-TQTRFGEVVGAKGEMVDAGNHVTCIAKWPGVI 331
Cdd:cd16160   223 R---YGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEYClEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTI 299
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1270232598 332 QPQRlTSQIIDFSDFLPTMCEVADAEVPANLTIDGQSFLPVL 373
Cdd:cd16160   300 KPRV-SHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLL 340
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
48-424 1.62e-44

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: 159.44  E-value: 1.62e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIG--SNGSLDYQTPNIDRIASEGLRFEHCYSQPICTPSRVKLMTGMTNKRNYVKF--GMLDRKQT 123
Cdd:cd16154     1 PNILLIIADDQGLDSSAqySLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGVLAvpDELLLSEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 124 TFAHLLK----SAGYRTCIAGKWQLGSELDSPRHFGfeeslLWQHTRGRMDSQKRDtrYPNPRLERNGTKEDYDE--GEF 197
Cdd:cd16154    81 TLLQLLIkdatTAGYSSAVIGKWHLGGNDNSPNNPG-----GIPYYAGILGGGVQD--YYNWNLTNNGQTTNSTEyaTTK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 198 SSDLFADFLcdfmeTNRDQPFLAYypMALV--HCPFcPTPDSEDWDPTSHGSKTYKGQP--EYFGDMVAYVDKIVGRIDQ 273
Cdd:cd16154   154 LTNLAIDWI-----DQQTKPWFLW--LAYNapHTPF-HLPPAELHSRSLLGDSADIEANprPYYLAAIEAMDTEIGRLLA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 274 KLgDLGIRENTLLIFTGDNGTDKPiVTQTRFgEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEV 353
Cdd:cd16154   226 SI-DEEERENTIIIFIGDNGTPGQ-VVDLPY-TRNHAKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAEL 302
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270232598 354 ADAEVPAnlTIDGQSFLPVLQGIEGQGRESMFMWYERNGRPNKARefaRNQRYKL--YGDG--SFFDVEMDRNEK 424
Cdd:cd16154   303 AGVDAAE--IHDSVSFKPLLSDVNASTRQYNYTEYESPTTTGWAT---RNQYYKLieSENGqeELYDLINDPSEQ 372
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
48-371 3.42e-44

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: 155.78  E-value: 3.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMAD----DMgfecIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMTNKRNYVKFGMLDRKQ 122
Cdd:cd16148     1 MNVILIVIDslraDH----LGCYGYDRVTTPNLDRLAAEGVVFDNHYSGsNPTLPSRFSLFTGLYPFYHGVWGGPLEPDD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 123 TTFAHLLKSAGYRTCIAGkwqlgselDSPRHFGFeesllWQHTRGRmdsqkrDTRYPNPRLERNGTKEDYdegEFSSDLF 202
Cdd:cd16148    77 PTLAEILRKAGYYTAAVS--------SNPHLFGG-----PGFDRGF------DTFEDFRGQEGDPGEEGD---ERAERVT 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 203 ADFLcDFMETN-RDQPFLAYypmalVHCpfcptpdsedWDPtsHGSKTYKGQpeyfgdmVAYVDKIVGRIDQKLGDLGIR 281
Cdd:cd16148   135 DRAL-EWLDRNaDDDPFFLF-----LHY----------FDP--HEPYLYDAE-------VRYVDEQIGRLLDKLKELGLL 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 282 ENTLLIFTGDNGTDkpivtqtrFGEvvgaKGEMVDAGN-------HVTCIAKWPGVIQPQR---LTSQIidfsDFLPTMC 351
Cdd:cd16148   190 EDTLVIVTSDHGEE--------FGE----HGLYWGHGSnlydeqlHVPLIIRWPGKEPGKRvdaLVSHI----DIAPTLL 253
                         330       340
                  ....*....|....*....|
gi 1270232598 352 EVADAEVPAnlTIDGQSFLP 371
Cdd:cd16148   254 DLLGVEPPD--YSDGRSLLP 271
Sulfatase pfam00884
Sulfatase;
48-356 4.76e-44

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 156.43  E-value: 4.76e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKRNYVKFGMLD---RKQT 123
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSgGTLTAPSRFALLTGLPPHNFGSYVSTPVglpRTEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 124 TFAHLLKSAGYRTCIAGKWQLG-SELDSPRHFGFEESLLWQHtrGRMDSQKRDTRYPNPRLerngtkedydeGEFSSDLF 202
Cdd:pfam00884  81 SLPDLLKRAGYNTGAIGKWHLGwYNNQSPCNLGFDKFFGRNT--GSDLYADPPDVPYNCSG-----------GGVSDEAL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 203 ADFLCDFmETNRDQPFLAYY-PMAlVHCPFcptPDSEDWDPTSHGSKTYKG----QPEYFGDMVAYVDKIVGRIDQKLGD 277
Cdd:pfam00884 148 LDEALEF-LDNNDKPFFLVLhTLG-SHGPP---YYPDRYPEKYATFKPSSCseeqLLNSYDNTLLYTDDAIGRVLDKLEE 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270232598 278 LGIRENTLLIFTGDNGtdkPIVTQTRFGEVVGAKGEMVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADA 356
Cdd:pfam00884 223 NGLLDNTLVVYTSDHG---ESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
47-444 2.27e-43

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: 156.57  E-value: 2.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-----PICTPSRVKLMTGMTNKRNYVKFGM-LDR 120
Cdd:cd16155     2 KPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMggwsgAVCVPSRAMLMTGRTLFHAPEGGKAaIPS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 121 KQTTFAHLLKSAGYRTCIAGKWqlgseldsprHfgfeesllwqhtrgrmdsqkrdtrypnprlerNGtkedydegefssd 200
Cdd:cd16155    82 DDKTWPETFKKAGYRTFATGKW----------H--------------------------------NG------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 201 lFADFLCDFME--TNRDQPFLAYYPMALVHCPFCPTPDSED-WDPTSHG-SKTYKGQ-PEYFGD---------------- 259
Cdd:cd16155   107 -FADAAIEFLEeyKDGDKPFFMYVAFTAPHDPRQAPPEYLDmYPPETIPlPENFLPQhPFDNGEgtvrdeqlapfprtpe 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 260 -----------MVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGTdkpivtqtrfgeVVGAKG-----EMVDAGNHVTC 323
Cdd:cd16155   186 avrqhlaeyyaMITHLDAQIGRILDALEASGELDNTIIVFTSDHGL------------AVGSHGlmgkqNLYEHSMRVPL 253
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 324 IAKWPGvIQPQRLTSQIIDFSDFLPTMCEVADAEVPAnlTIDGQSFLPVLQGIEGQGRESMFMWYERNGRPnkarefARN 403
Cdd:cd16155   254 IISGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPE--SVEGKSLLPVIRGEKKAVRDTLYGAYRDGQRA------IRD 324
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1270232598 404 QRYKL--YGDGSF----FDVEMDRNEKSPLQSLTDDQKEIRsKLQAK 444
Cdd:cd16155   325 DRWKLiiYVPGVKrtqlFDLKKDPDELNNLADEPEYQERLK-KLLAE 370
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
47-373 2.54e-43

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


Pssm-ID: 293776 [Multi-domain]  Cd Length: 466  Bit Score: 158.40  E-value: 2.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKRN-------------- 111
Cdd:cd16157     1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSaNPLCSPSRAALLTGRLPIRNgfyttnaharnayt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 112 --YVKFGMLDRKQtTFAHLLKSAGYRTCIAGKWQLG-SELDSPRHFGFEEsllWQHTRGRMDSQKRDTRYPNPRLERNGT 188
Cdd:cd16157    81 pqNIVGGIPDSEI-LLPELLKKAGYRNKIVGKWHLGhRPQYHPLKHGFDE---WFGAPNCHFGPYDNKAYPNIPVYRDWE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 189 ---------KEDYDEGEFS-SDLFADFLCDFMET--NRDQPFLAYYPMALVHCPFcptpdsedwdptsHGSKTYKG--QP 254
Cdd:cd16157   157 migryyeefKIDKKTGESNlTQIYLQEALEFIEKqhDAQKPFFLYWAPDATHAPV-------------YASKPFLGtsQR 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 255 EYFGDMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNG--TDKPIVTQTRFGEVVGAKGEMVDAGNHVTCIAKWPGVIQ 332
Cdd:cd16157   224 GLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaaLISAPEQGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIK 303
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1270232598 333 PQRLTSQIIDFSDFLPTMCEVADAEVPANLTIDGQSFLPVL 373
Cdd:cd16157   304 PGQVSHQLGSLMDLFTTSLALAGLPIPSDRAIDGIDLLPVL 344
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
48-420 6.52e-42

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: 151.16  E-value: 6.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGM--TNKRNYVKFGMLDRKQTT 124
Cdd:cd16037     1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPsPICVPSRASFLTGRyvHETGVWDNADPYDGDVPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 125 FAHLLKSAGYRTCIAGKwqlgseldsprhfgfeesllwQHTRGRMDsqkrdtrypnprleRNGTkeDYDEgefssdLFAD 204
Cdd:cd16037    81 WGHALRAAGYETVLIGK---------------------LHFRGEDQ--------------RHGF--RYDR------DVTE 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 205 FLCDFMETN--RDQPFLAYYPMALVHCPFCPTPdsEDWDPTSHGSKTykgqpEYFGdMVAYVDKIVGRIDQKLGDLGIRE 282
Cdd:cd16037   118 AAVDWLREEaaDDKPWFLFVGFVAPHFPLIAPQ--EFYDLYVRRARA-----AYYG-LVEFLDENIGRVLDALEELGLLD 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 283 NTLLIFTGDNgtdkpivtqtrfGEVVGAKG-----EMVDAGNHVTCIAKWPGVIQPQRlTSQIIDFSDFLPTMCEVADAE 357
Cdd:cd16037   190 NTLIIYTSDH------------GDMLGERGlwgksTMYEESVRVPMIISGPGIPAGKR-VKTPVSLVDLAPTILEAAGAP 256
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270232598 358 VPANLtiDGQSFLPVLQGIEGQGRE--SMFMWyerNGRPNKAReFARNQRYKL---YGDGS-FFDVEMD 420
Cdd:cd16037   257 PPPDL--DGRSLLPLAEGPDDPDRVvfSEYHA---HGSPSGAF-MLRKGRWKYiyyVGYPPqLFDLEND 319
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
48-371 1.36e-40

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


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 145.84  E-value: 1.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCY-SQPICTPSRVKLMTGM-------------TNKRNYV 113
Cdd:cd16149     1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFcTSPVCSPARASLLTGRmpsqhgihdwiveGSHGKTK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 114 KFGMLDRKQTTFAHLLKSAGYRTCIAGKWQLGSELdsprhfgfeesllwqhtrgrmdsqkrdtrypnprlerngtkedyd 193
Cdd:cd16149    81 KPEGYLEGQTTLPEVLQDAGYRCGLSGKWHLGDDA--------------------------------------------- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 194 egefssdlfADFLCDfmETNRDQPFLAYYPMALVHCPFcptpdsedwdptshgsktykgqpEYFGDMVAyVDKIVGRIDQ 273
Cdd:cd16149   116 ---------ADFLRR--RAEAEKPFFLSVNYTAPHSPW-----------------------GYFAAVTG-VDRNVGRLLD 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 274 KLGDLGIRENTLLIFTGDNGTDkpivtqtrfgevVG-----AKG------EMVDAGNHVTCIAKWPGVIQPQRLTSQIID 342
Cdd:cd16149   161 ELEELGLTENTLVIFTSDNGFN------------MGhhgiwGKGngtfplNMYDNSVKVPFIIRWPGVVPAGRVVDSLVS 228
                         330       340
                  ....*....|....*....|....*....
gi 1270232598 343 FSDFLPTMCEVADAEVPANLTIDGQSFLP 371
Cdd:cd16149   229 AYDFFPTLLELAGVDPPADPRLPGRSFAD 257
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
48-420 1.21e-39

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: 145.41  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMTNKRNyvkfGMLDR------ 120
Cdd:cd16032     1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNsPLCAPSRASMMTGRLPSRI----GAYDNaaefpa 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 121 KQTTFAHLLKSAGYRTCIAGKwqlgseldspRHF-------GFeesllwqhtrgrmdsqkrdtrypnprlerngtkeDYD 193
Cdd:cd16032    77 DIPTFAHYLRAAGYRTALSGK----------MHFvgpdqlhGF----------------------------------DYD 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 194 -EGEFSSdlfADFLCDFMETNRDQPFLAYYPMALVHCPFCPTPdsEDWD----PTSHGsktykgqpeYFGdMVAYVDKIV 268
Cdd:cd16032   113 eEVAFKA---VQKLYDLARGEDGRPFFLTVSFTHPHDPYVIPQ--EYWDlyvrRARRA---------YYG-MVSYVDDKV 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 269 GRIDQKLGDLGIRENTLLIFTGDNgtdkpivtqtrfGEVVGAKG---EMV--DAGNHVTCIAKWPGVIQPQRLtSQIIDF 343
Cdd:cd16032   178 GQLLDTLERTGLADDTIVIFTSDH------------GDMLGERGlwyKMSffEGSARVPLIISAPGRFAPRRV-AEPVSL 244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 344 SDFLPTMCEVADAEVPANLT-IDGQSFLPVLQGIEGQGRESMFMWYERNGRPNKAReFARNQRYKL---YGDGS-FFDVE 418
Cdd:cd16032   245 VDLLPTLVDLAGGGTAPHVPpLDGRSLLPLLEGGDSGGEDEVISEYLAEGAVAPCV-MIRRGRWKFiycPGDPDqLFDLE 323

                  ..
gi 1270232598 419 MD 420
Cdd:cd16032   324 AD 325
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
46-406 4.17e-38

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: 143.48  E-value: 4.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  46 DRPNIVLIMADDMGFEcIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGM--TNKRNYVkFGMLDRKQ 122
Cdd:cd16030     1 KKPNVLFIAVDDLRPW-LGCYGGHPAKTPNIDRLAARGVLFTNAYCQqPVCGPSRASLLTGRrpDTTGVYD-NNSYFRKV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 123 ----TTFAHLLKSAGYRTCIAGK---WQLGSELDSPRHFgfeeSLLWQHTRGRMDSQKRDTRYPNPRLERNGTK----ED 191
Cdd:cd16030    79 apdaVTLPQYFKENGYTTAGVGKifhPGIPDGDDDPASW----DEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPaweaAD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 192 YDEGEFSSDLFADFLCDFMET--NRDQP-FLA---YYPmalvHCPF-CPT------PDSE------------------DW 240
Cdd:cd16030   155 VPDEAYPDGKVADEAIEQLRKlkDSDKPfFLAvgfYKP----HLPFvAPKkyfdlyPLESiplpnpfdpidlpevawnDL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 241 -DPTSHGSKTYKGQPEYFGDM---------------VAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGtdkpivtqtrF 304
Cdd:cd16030   231 dDLPKYGDIPALNPGDPKGPLpdeqarelrqayyasVSYVDAQVGRVLDALEELGLADNTIVVLWSDHG----------W 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 305 --GEvvgaKGE-----MVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPANLtiDGQSFLPVLQGIE 377
Cdd:cd16030   301 hlGE----HGHwgkhtLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPPCL--EGKSLVPLLKNPS 374
                         410       420
                  ....*....|....*....|....*....
gi 1270232598 378 GQGRESMFMWYERNGRPNKArefARNQRY 406
Cdd:cd16030   375 AKWKDAAFSQYPRPSIMGYS---IRTERY 400
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
48-445 1.27e-37

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


Pssm-ID: 293769 [Multi-domain]  Cd Length: 423  Bit Score: 141.99  E-value: 1.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMtnkrnY--VK-----FGMLD 119
Cdd:cd16150     1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQnPVCSPSRCSFLTGW-----YphVNghrtlHHLLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 120 RKQTTFAHLLKSAGYRTCIAGKwqlgseldspRHFgfeesllwqhtrgrmdsqkrdtrypnprLERNGTKEDYdegEFSS 199
Cdd:cd16150    76 PDEPNLLKTLKDAGYHVAWAGK----------NDD----------------------------LPGEFAAEAY---CDSD 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 200 DLFADFLCDFMET-NRDQPFLAYYPMALVHCPF-CPTP-----DSEDWDPTSHGSKTYKGQPE----------------- 255
Cdd:cd16150   115 EACVRTAIDWLRNrRPDKPFCLYLPLIFPHPPYgVEEPwfsmiDREKLPPRRPPGLRAKGKPSmlegiekqgldrwseer 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 256 -------YFGdMVAYVDKIVGRIDQKLGDLGIRENTLLIF-------TGDNG-TDKpivTQTRFGEVVgakgemvdagNH 320
Cdd:cd16150   195 wrelratYLG-MVSRLDHQFGRLLEALKETGLYDDTAVFFfsdhgdyTGDYGlVEK---WPNTFEDCL----------TR 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 321 VTCIAKWPGVIqPQRLTSQIIDFSDFLPTMCEVADaeVPANLTIDGQSFLPVLQGIEGQGRESMF------------Mwy 388
Cdd:cd16150   261 VPLIIKPPGGP-AGGVSDALVELVDIPPTLLDLAG--IPLSHTHFGRSLLPVLAGETEEHRDAVFseggrlhgeeqaM-- 335
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270232598 389 ERNGRPN---KAREFA-------------RNQRYK----LYGDGSFFDVEMDRNEkspLQSLTDDQ--KEIRSKLQAKI 445
Cdd:cd16150   336 EGGHGPYdlkWPRLLQqeeppehtkavmiRTRRYKyvyrLYEPDELYDLEADPLE---LHNLIGDPayAEIIAEMKQRL 411
PRK13759 PRK13759
arylsulfatase; Provisional
47-446 2.25e-37

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 142.50  E-value: 2.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  47 RPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMTNKRNyvkfGMLDRKQ--- 122
Cdd:PRK13759    6 KPNIILIMVDQMRGDCLGCNGNKAVETPNLDMLASEGYNFENAYSAvPSCTPARAALLTGLSQWHH----GRVGYGDvvp 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 123 ----TTFAHLLKSAGYRT-CIaGKWQLGSEldSPRHfGFEESLL---WQHTrGRMDSQKR-----DTRY--------PNP 181
Cdd:PRK13759   82 wnykNTLPQEFRDAGYYTqCI-GKMHVFPQ--RNLL-GFHNVLLhdgYLHS-GRNEDKSQfdfvsDYLAwlrekapgKDP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 182 RLERNGTKE--------DYDEGEFSSDLFADFLCDFMET-NRDQPFLAYYPMALVHCPF--------------CPTPDSE 238
Cdd:PRK13759  157 DLTDIGWDCnswvarpwDLEERLHPTNWVGSESIEFLRRrDPTKPFFLKMSFARPHSPYdppkryfdmykdadIPDPHIG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 239 DW------DPTSHGSKTYKGQ-PE---------YFGDMvAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNgtdkpivtqt 302
Cdd:PRK13759  237 DWeyaedqDPEGGSIDALRGNlGEeyarraraaYYGLI-THIDHQIGRFLQALKEFGLLDNTIILFVSDH---------- 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 303 rfGEVVG-----AKGEMVDAGNHVTCIAKWPG-VIQPQRLTS--QIIDFSDFLPTMCEVADAEVPAnlTIDGQSFLPVLQ 374
Cdd:PRK13759  306 --GDMLGdhylfRKGYPYEGSAHIPFIIYDPGgLLAGNRGTVidQVVELRDIMPTLLDLAGGTIPD--DVDGRSLKNLIF 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 375 GIEGQGRESM----FMWYERNGRPNKARE----FARNQRYKLygdgsfFDVEMDRNEKSPLQSLTDDQKEIRSKLQAKID 446
Cdd:PRK13759  382 GQYEGWRPYLhgehALGYSSDNYLTDGKWkyiwFSQTGEEQL------FDLKKDPHELHNLSPSEKYQPRLREMRKKLVD 455
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
48-445 5.98e-33

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


Pssm-ID: 293775 [Multi-domain]  Cd Length: 468  Bit Score: 129.81  E-value: 5.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGMTNKRNyvkfGM------LDR 120
Cdd:cd16156     1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTtQPVCGPARSGLFTGLYPHTN----GSwtncmaLGD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 121 KQTTFAHLLKSAGYRTCIAGKWQLgselDSPRHFGFEE------SLLWQHTRGRMDSQKRDTRY----PNPRLERNGTKE 190
Cdd:cd16156    77 NVKTIGQRLSDNGIHTAYIGKWHL----DGGDYFGNGIcpqgwdPDYWYDMRNYLDELTEEERRksrrGLTSLEAEGIKE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 191 DYDEGEFSSDLfadfLCDFMETNRDQPFLayypmaLV------HCPF-CPTPDSE------------DWD-----PTSH- 245
Cdd:cd16156   153 EFTYGHRCTNR----ALDFIEKHKDEDFF------LVvsydepHHPFlCPKPYASmykdfefpkgenAYDdlenkPLHQr 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 246 ----------GSKTYKGQPEYFGdMVAYVDKIVGRIDQKLGDlgIRENTLLIFTGDNGtdkpivtqtrfgEVVGA----- 310
Cdd:cd16156   223 lwagakphedGDKGTIKHPLYFG-CNSFVDYEIGRVLDAADE--IAEDAWVIYTSDHG------------DMLGAhklwa 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 311 KGE-MVDAGNHVTCIAKWPGVIQPQRLTSQIIDFSDFLPTMCEVADAEVPANLtiDGQSFLPVLQGIEGQGRESMFM--- 386
Cdd:cd16156   288 KGPaVYDEITNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVL--EGESILATIEDPEIPENRGVFVefg 365
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270232598 387 WYERNGRPNKAREFAR---NQRYK----LYGDGSFFDVEMDRNEkspLQSLTDDQ--KEIRSKLQAKI 445
Cdd:cd16156   366 RYEVDHDGFGGFQPVRcvvDGRYKlvinLLSTDELYDLEKDPYE---MHNLIDDPdyADVRDQLHDEL 430
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
47-385 9.71e-33

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


Pssm-ID: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 127.34  E-value: 9.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  47 RPNIVLIMADDMGFECIGSNGS-LDYqTPNIDRIASEGLRFEHCYS-QPICTPSRVKLMTGM--TNKRNYVKFGMLDRKQ 122
Cdd:cd16152     1 KPNVIVFFTDQQRWDTLGCYGQpLDL-TPNLDALAEEGVLFENAFTpQPVCGPARACLQTGLypTETGCFRNGIPLPADE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 123 TTFAHLLKSAGYRTCIAGKWQLgseldsprhfgfeesllwqhtrgrmdsqkrdtrypnprlerngtkedydeGEFSSDLF 202
Cdd:cd16152    80 KTLAHYFRDAGYETGYVGKWHL--------------------------------------------------AGYRVDAL 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 203 ADFLCDFMET-NRDQPFLAYYPMALVHcpfcptpDSEDWD--PTSHGSK------------------TYKGQPEYFGdMV 261
Cdd:cd16152   110 TDFAIDYLDNrQKDKPFFLFLSYLEPH-------HQNDRDryVAPEGSAerfanfwvppdlaalpgdWAEELPDYLG-CC 181
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 262 AYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGTDkpivTQTRFGEVvgaKGEMVDAGNHVTCIAKWPGVIQPQRLTsQII 341
Cdd:cd16152   182 ERLDENVGRIRDALKELGLYDNTIIVFTSDHGCH----FRTRNAEY---KRSCHESSIRVPLVIYGPGFNGGGRVE-ELV 253
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1270232598 342 DFSDFLPTMCEVADAEVPAnlTIDGQSFLPVLQGIEGQGRESMF 385
Cdd:cd16152   254 SLIDLPPTLLDAAGIDVPE--EMQGRSLLPLVDGKVEDWRNEVF 295
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
47-368 5.06e-32

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: 126.13  E-value: 5.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  47 RPNIVLIMADDMGFECigsnGSLDYQTPNIDRIASEGLRFEHCY-SQPICTPSRVKLMTGM----TNKRN-------YVK 114
Cdd:cd16147     1 RPNIVLILTDDQDVEL----GSMDPMPKTKKLLADQGTTFTNAFvTTPLCCPSRASILTGQyahnHGVTNnsppgggYPK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 115 FGMLDRKQTTFAHLLKSAGYRTCIAGK----WQLGSELDS-PRhfGFEESLLWQHTRgrmdsqkRDTRYpNPRLERNGTK 189
Cdd:cd16147    77 FWQNGLERSTLPVWLQEAGYRTAYAGKylngYGVPGGVSYvPP--GWDEWDGLVGNS-------TYYNY-TLSNGGNGKH 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 190 EDYDEGEFSSDLFADFLCDFMET--NRDQPFLAYYPMALVHCPFCPTPDSED-------------WDPTSHGSKTY-KGQ 253
Cdd:cd16147   147 GVSYPGDYLTDVIANKALDFLRRaaADDKPFFLVVAPPAPHGPFTPAPRYANlfpnvtapprpppNNPDVSDKPHWlRRL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 254 PEYFGDMVAY--------------VDKIVGRIDQKLGDLGIRENTLLIFTGDNG---------TDKpivtQTRFGEVVga 310
Cdd:cd16147   227 PPLNPTQIAYidelyrkrlrtlqsVDDLVERLVNTLEATGQLDNTYIIYTSDNGyhlgqhrlpPGK----RTPYEEDI-- 300
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270232598 311 kgemvdagnHVTCIAKWPGVIQPQR---LTSQIidfsDFLPTMCEVADAEVPANLtiDGQS 368
Cdd:cd16147   301 ---------RVPLLVRGPGIPAGVTvdqLVSNI----DLAPTILDLAGAPPPSDM--DGRS 346
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
48-427 7.62e-32

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: 126.60  E-value: 7.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGM--TNKRNYVKFGMLDRKQTT 124
Cdd:cd16028     1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQaAPCGPSRASLYTGRylMNHRSVWNGTPLDARHLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 125 FAHLLKSAGYRTCIAGKWQLGSELD--SPRHfgfeESLLWQHT-RGRMDSQKRDTRYPnprlerngtKEDYDegefsSDL 201
Cdd:cd16028    81 LALELRKAGYDPALFGYTDTSPDPRglAPLD----PRLLSYELaMPGFDPVDRLDEYP---------AEDSD-----TAF 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 202 FADFLCDFMETNRDQPF---LAYY----------PMALVHCP------------------------FCPTPDSEDWDPTS 244
Cdd:cd16028   143 LTDRAIEYLDERQDEPWflhLSYIrphppfvapaPYHALYDPadvpppiraeslaaeaaqhpllaaFLERIESLSFSPGA 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 245 HGSKTYKG------QPEYFGdMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNgtdkpivtqtrfGEVVG-----AKGE 313
Cdd:cd16028   223 ANAADLDDeevaqmRATYLG-LIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDH------------GEQLGdhwlwGKDG 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 314 MVDAGNHVTCIAKWPGVIQPQRLTSQIIDFS---DFLPTMCEVADAEVPAnlTIDGQSFLPVLQGIEGQGRESMFMWYER 390
Cdd:cd16028   290 FFDQAYRVPLIVRDPRREADATRGQVVDAFTesvDVMPTILDWLGGEIPH--QCDGRSLLPLLAGAQPSDWRDAVHYEYD 367
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1270232598 391 NG-------------RPNKAREFA-RNQRYKL--YGDGS--FFDVEMDRNEKSPL 427
Cdd:cd16028   368 FRdvstrrpqealglSPDECSLAViRDERWKYvhFAALPplLFDLKNDPGELRDL 422
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
47-366 9.57e-25

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: 103.22  E-value: 9.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  47 RPNIVLIMADDM---GFECIG------SNGSLDY-QTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTGMTNKRNYV-K 114
Cdd:cd16153     1 KPNILWIITDDQrvdSLSCYNnahtgkSESRLGYvESPNIDALAAEGVLFTNAYCNsPVCVPSRTSMLTGRYPHRTGVyG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 115 FGM----LDRKQTTFAHLLKSAGYRTCIAGKwqlgseldsprhFGFEESLLWqhtrgrmdsqkrdTRYPNPRLERNGTKE 190
Cdd:cd16153    81 FEAahpaLDHGLPTFPEVLKKAGYQTASFGK------------SHLEAFQRY-------------LKNANQSYKSFWGKI 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 191 dydegefssdlfadflcdFMETNRDQPFLAYYPMALVHCPFCPtpdsedwdptshgSKTYKGQPEYFGdMVAYVDKIVGR 270
Cdd:cd16153   136 ------------------AKGADSDKPFFVRLSFLQPHTPVLP-------------PKEFRDRFDYYA-FCAYGDAQVGR 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 271 IDQKLGDLGI---RENTLLIFTGDNGtdkpivtqTRFGEV-VGAKGEMVDAGNHVTCIAKWPGVIQPQRLT--SQIIDFS 344
Cdd:cd16153   184 AVEAFKAYSLkqdRDYTIVYVTGDHG--------WHLGEQgILAKFTFWPQSHRVPLIVVSSDKLKAPAGKvrHDFVEFV 255
                         330       340
                  ....*....|....*....|..
gi 1270232598 345 DFLPTMCEVADAEVPANLTIDG 366
Cdd:cd16153   256 DLAPTLLAAAGVDVDAPDYLDG 277
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
48-390 1.52e-21

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


Pssm-ID: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 94.58  E-value: 1.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFE-HCYSQPICTPSRVKLMTG-------MTNKRNYVKFGMLD 119
Cdd:cd16035     1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFEnHYTAACMCSPSRSTLYTGlhpqqtgVTDTLGSPMQPLLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 120 RKQTTFAHLLKSAGYRTCIAGKWQLGSeldsprhfgfeesllwqHTRGrmdsqkrdtrypnprlernGTKEDydegefss 199
Cdd:cd16035    81 PDVPTLGHMLRAAGYYTAYKGKWHLSG-----------------AAGG-------------------GYKRD-------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 200 DLFADFLCDFMET-----NRDQPFLAYypMALV--HCPFCPTPDSEDWdptshgsktyKGQPEYFGDMVAYVDKIVGRID 272
Cdd:cd16035   117 PGIAAQAVEWLRErgaknADGKPWFLV--VSLVnpHDIMFPPDDEERW----------RRFRNFYYNLIRDVDRQIGRVL 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 273 QKLGDLGIRENTLLIFTGDNgtdkpivtqtrfGEVVGAKGEMVDAGN------HVtciakwPGVI-------QPQR---L 336
Cdd:cd16035   185 DALDASGLADNTIVVFTSDH------------GEMGGAHGLRGKGFNayeealHV------PLIIshpdlfgTGQTtdaL 246
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1270232598 337 TSQIidfsDFLPTMCEVADAEVPANLTID----GQSFLPVLQGIEG-QGRESMFMWYER 390
Cdd:cd16035   247 TSHI----DLLPTLLGLAGVDAEARATEApplpGRDLSPLLTDADAdAVRDGILFTYDR 301
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
48-395 2.38e-20

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: 92.22  E-value: 2.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQ-PICTPSRVKLMTG----MTNKRNyvKFGMLDRKQ 122
Cdd:cd16171     1 PNVVMVMSDSFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTNsPICCPSRAAMWSGlfthLTESWN--NYKGLDPNY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 123 TTFAHLLKSAGYRTCIAGKWQLGSELDSprhfgfeesllwqhTRGRMDSQKRDTRY-------PNPRLERNGTKEDYDEG 195
Cdd:cd16171    79 PTWMDRLEKHGYHTQKYGKLDYTSGHHS--------------VSNRVEAWTRDVPFllrqegrPTVNLVGDRSTVRVMLK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 196 EFSSDLFADFLCDFMETNRDQPFLAYYPMALVHcPFcPTPDSedwDPTSHGSKTYKgqpEYFGDMVAYVDKIVGRIDQKL 275
Cdd:cd16171   145 DWQNTDKAVHWIRKEAPNLTQPFALYLGLNLPH-PY-PSPSM---GENFGSIRNIR---AFYYAMCAETDAMLGEIISAL 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 276 GDLGIRENTLLIFTGDNGtdKPIVTQTRFgevvgAKGEMVDAGNHVTCIAKWPGvIQPQRLTSQIIDFSDFLPTMCEVAD 355
Cdd:cd16171   217 KDTGLLDKTYVFFTSDHG--ELAMEHRQF-----YKMSMYEGSSHVPLLIMGPG-IKAGQQVSDVVSLVDIYPTMLDIAG 288
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1270232598 356 AEVPANLTidGQSFLPVLQgiegqgRESMFMWYERNGRPN 395
Cdd:cd16171   289 VPQPQNLS--GYSLLPLLS------ESSIKESPSRVPHPD 320
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
48-354 2.82e-20

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: 89.40  E-value: 2.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFE--HCYSQPICTPSRVKLMTG------------MTNKRNYV 113
Cdd:cd00016     1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNfrSVSPPTSSAPNHAALLTGayptlhgytgngSADPELPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 114 KFGMLDRKQTTFAHLLKSAGYRTCIAGkwqlgseldsprhfgfeeslLWQHtrgrmdsqkrdtrypnprlerngtkedyd 193
Cdd:cd00016    81 RAAGKDEDGPTIPELLKQAGYRTGVIG--------------------LLKA----------------------------- 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 194 egefssdlfadflcdFMETNRDQPFLAYypmalVHCpfcptpDSEDWDPTSHGSKTykgqPEYFgDMVAYVDKIVGRIDQ 273
Cdd:cd00016   112 ---------------IDETSKEKPFVLF-----LHF------DGPDGPGHAYGPNT----PEYY-DAVEEIDERIGKVLD 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 274 KLGDLGIRENTLLIFTGDNG-TDKPIVTQTRFGEVVGAKGemvdAGNHVTCIAKWPGVIQPQ---RLTSQIidfsDFLPT 349
Cdd:cd00016   161 ALKKAGDADDTVIIVTADHGgIDKGHGGDPKADGKADKSH----TGMRVPFIAYGPGVKKGGvkhELISQY----DIAPT 232

                  ....*
gi 1270232598 350 MCEVA 354
Cdd:cd00016   233 LADLL 237
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
36-350 1.01e-14

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 76.23  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  36 ADEPSPQRSGDRPNIVLIMADDMGFECIGSNGSLDYQTPNIDRIASEGLRFEHCYSQpicTPSRVK----LMTGM--TNK 109
Cdd:COG1368   223 RPTPNPFGPAKKPNVVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQ---GGRTSRgefaVLTGLppLPG 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 110 RNYVKfGMLDRKQTTFAHLLKSAGYRTciagkwqlgseldsprHF--GFEESllwqhtrgrmdSQKRDTRYPNprlerNG 187
Cdd:COG1368   300 GSPYK-RPGQNNFPSLPSILKKQGYET----------------SFfhGGDGS-----------FWNRDSFYKN-----LG 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 188 TKEDYDEGEFSS-----------DLFADFLcDFMETNrDQPFLAYYpMALV-HCPFcpTPDSEDWDPTSHGSKTYKgqpE 255
Cdd:COG1368   347 FDEFYDREDFDDpfdggwgvsdeDLFDKAL-EELEKL-KKPFFAFL-ITLSnHGPY--TLPEEDKKIPDYGKTTLN---N 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 256 YFGdMVAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGtdkPIVTQTRFGEVVGAKgemvdagNHVTCIAKWPGVIQPQ- 334
Cdd:COG1368   419 YLN-AVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG---PRSPGKTDYENPLER-------YRVPLLIYSPGLKKPKv 487
                         330
                  ....*....|....*...
gi 1270232598 335 --RLTSQIidfsDFLPTM 350
Cdd:COG1368   488 idTVGSQI----DIAPTL 501
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
48-355 1.30e-14

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: 73.87  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  48 PNIVLIMADDMGFECIGS-NGSLDYqTPNIDRIASEGLRFEHCYSQPICTPSrVK----LMTG--MTNKRNYVKFGMLDR 120
Cdd:cd16015     1 PNVIVILLESFSDPYIDKdVGGEDL-TPNLNKLAKEGLYFGNFYSPGFGGGT-ANgefeVLTGlpPLPLGSGSYTLYKLN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 121 KQTTFAHLLKSAGYRTC--IAGK---WQLGSELdspRHFGFEESLlwqhtrgrmdsQKRDTRYPNPRLERNGTkedYDEg 195
Cdd:cd16015    79 PLPSLPSILKEQGYETIfiHGGDasfYNRDSVY---PNLGFDEFY-----------DLEDFPDDEKETNGWGV---SDE- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 196 efssDLFaDFLCDFMETNRDQPFLAYypmaLV----HCPFcptPDSEDWDPTSHGSKTYKGQPEYFGDMVAYVDKIVGRI 271
Cdd:cd16015   141 ----SLF-DQALEELEELKKKPFFIF----LVtmsnHGPY---DLPEEKKDEPLKVEEDKTELENYLNAIHYTDKALGEF 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 272 DQKLGDLGIRENTLLIFTGDNgtdkpivtQTRFGEVVGAKGEMVDAGNHVTCIAKWPGVIQPQ---RLTSQIidfsDFLP 348
Cdd:cd16015   209 IEKLKKSGLYENTIIVIYGDH--------LPSLGSDYDETDEDPLDLYRTPLLIYSPGLKKPKkidRVGSQI----DIAP 276

                  ....*..
gi 1270232598 349 TMCEVAD 355
Cdd:cd16015   277 TLLDLLG 283
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
42-350 2.75e-08

Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 442317 [Multi-domain]  Cd Length: 603  Bit Score: 56.07  E-value: 2.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  42 QRSGDRPNIVLIMADDMGFEcigsngSLDYQT-PNIDRIASEGLRFEHCYSQPICTpsrvklMTGMTN-----KRNYVkF 115
Cdd:COG3083   239 SDPAKPPNILLIVVDSLRAD------MLDPEVmPNLYAFAQRSLRFTNHYSSGNST------RAGLFGlfyglPGNYW-D 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 116 GMLD-RKQTTFAHLLKSAGYRTCIAGkwqlGSELDSPRhfgFEESLLwqhtrgrmdsqkrdTRYPNPRLERNGTKEDYDe 194
Cdd:COG3083   306 SILAeRTPPVLIDALQQQGYQFGLFS----SAGFNSPL---FRQTIF--------------SDVSLPRLHTPGGPAQRD- 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 195 gefsSDLFADFLCDFMETNRDQPFLAYYPMALVH---------CPFCPTPDSEDWDPTSHGSKT-----YKGQpeyfgdm 260
Cdd:COG3083   364 ----RQITAQWLQWLDQRDSDRPWFSYLFLDAPHaysfpadypKPFQPSEDCNYLALDNESDPTpfknrYRNA------- 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 261 VAYVDKIVGRIDQKLGDLGIRENTLLIFTGDNGTDkpivtqtrFGEV----VGAKGEMVDAGNHVTCIAKWPGvIQPQ-- 334
Cdd:COG3083   433 VHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEE--------FNENgqnyWGHNSNFSRYQLQVPLVIHWPG-TPPQvi 503
                         330
                  ....*....|....*..
gi 1270232598 335 -RLTSQIidfsDFLPTM 350
Cdd:COG3083   504 sKLTSHL----DIVPTL 516
DUF4976 pfam16347
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ...
358-446 2.80e-03

Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.


Pssm-ID: 406689 [Multi-domain]  Cd Length: 103  Bit Score: 37.23  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598 358 VPANltIDGQSFLPVLQGIEGQG-RESMFM-WYERNGRPNKAREFA-RNQRYKL---YGD---GSFFDVEMDRNEkspLQ 428
Cdd:pfam16347   1 IPAD--MQGKSFLPLLKGKKPKNwRDALYYhYYEYPAEHAVKRHYGvRTERYKLihfYNDideWELYDLQKDPKE---MN 75
                          90       100
                  ....*....|....*....|
gi 1270232598 429 SLTDDQK--EIRSKLQAKID 446
Cdd:pfam16347  76 NVYGDPEyaEVQAELKEELE 95
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
46-136 4.22e-03

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


Pssm-ID: 293741 [Multi-domain]  Cd Length: 288  Bit Score: 39.14  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270232598  46 DRPNIVLIM-----ADDMGfecigSNGsldYQ---TPNIDRIASEGLRFEHCYSQ-PICTPSrVKLM-TGMTNKrNYVKF 115
Cdd:cd16017     1 KPKNVVLVIgesarRDHMS-----LYG---YPrdtTPFLSKLKKNLIVFDNVISCgTSTAVS-LPCMlSFANRE-NYDRA 70
                          90       100
                  ....*....|....*....|.
gi 1270232598 116 gmldRKQTTFAHLLKSAGYRT 136
Cdd:cd16017    71 ----YYQENLIDLAKKAGYKT 87
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH