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Conserved domains on  [gi|28571787|ref|NP_650920|]
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uncharacterized protein Dmel_CG15695 [Drosophila melanogaster]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 12040939)

alkaline phosphatase family protein is a DUF229 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF229 pfam02995
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ...
 180-656 0e+00

Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.


:

Pssm-ID: 397236  Cd Length: 496  Bit Score: 664.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   180 KKHSYIVCDKSRDMITVNYNVTDSTYRLHKNE-----------NSTCCFKQILRAGTSANADHKYKLGPCVEFHQDFLVP 248
Cdd:pfam02995   1 KPNPLRKCSKDQLLTTKSFNITFGTYRLNIDElakprlnerleNLNCEYREIKRKRDSENRDGYSKLFPLRKLTQSVEVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   249 TEVSAMITYCRRPpFDKVSQKDAFSFVHPRKDQIENP---TTPHRRRPSVLLWGIDSISRMNLELTMPRMYEYLNNQHWF 325
Cdd:pfam02995  81 VGCEILITECWED-FGKIYQKDVFNFLHDRIPPKKPKlssTPAEVRKPSVLILGIDSLSRMNFRRSMPRTYKFLKELGWF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   326 ELQGYNKMGDNTFPNLMAVLTG-FNKTYANARCHPEKVRGLDACPFIWKDFKDKGYTTAFAEDWSKFSTFDYSSRGFFNP 404
Cdd:pfam02995 160 ELQGYNKVGDNTFPNLLPLLTGkFSEPELEADCDPSCNGSLDKCPFIWKDFKDAGYATAFAEDWAKIGTFNYNKPGFRKQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   405 PTDVYGRPLVLAVEKELTILQRGQMPYCLGRKPASEYIYDMGVQFTMVNRNSTFFGMFWTNTFSHNDFSMPSAMDERMVK 484
Cdd:pfam02995 240 PTDHYLRPLILAIEKHLTYSTRFGLNYCLGRRPTHNYLLDYLRQFLPRYRDSPFFGFFWSNSLSHDDFNYASALDEDFLK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   485 YMRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSGFVEERLPFIYIRVPRWIREKYPKLLRNLQMNKNRLTSPYDIHATL 564
Cdd:pfam02995 320 YLKKLHKRGLLDNTIVIFMSDHGLRFGKLRRTSQGMLEERLPLMSIRYPPWFRETYPQAVENLELNANRLTTPFDLHATL 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   565 RHILELDTPKDKLPRP----DGCSSCHSVFEEVDWSRNCSQAGIEDHWCACNSFSDVPTTDPSARSMSTQLVEAINEYVA 640
Cdd:pfam02995 400 KDILHLGELSDKELQDrmkaLDCPRGISLFLPIPDNRTCSDAGIPEHWCTCEPYKEVPTNDTLVQRIARSVVERINEYLK 479

                         490
                  ....*....|....*.
gi 28571787   641 SKKGTKRCSRLKLNRI 656
Cdd:pfam02995 480 THNLSPLCAPLELQKV 495
 
Name Accession Description Interval E-value
DUF229 pfam02995
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ...
 180-656 0e+00

Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.


Pssm-ID: 397236  Cd Length: 496  Bit Score: 664.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   180 KKHSYIVCDKSRDMITVNYNVTDSTYRLHKNE-----------NSTCCFKQILRAGTSANADHKYKLGPCVEFHQDFLVP 248
Cdd:pfam02995   1 KPNPLRKCSKDQLLTTKSFNITFGTYRLNIDElakprlnerleNLNCEYREIKRKRDSENRDGYSKLFPLRKLTQSVEVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   249 TEVSAMITYCRRPpFDKVSQKDAFSFVHPRKDQIENP---TTPHRRRPSVLLWGIDSISRMNLELTMPRMYEYLNNQHWF 325
Cdd:pfam02995  81 VGCEILITECWED-FGKIYQKDVFNFLHDRIPPKKPKlssTPAEVRKPSVLILGIDSLSRMNFRRSMPRTYKFLKELGWF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   326 ELQGYNKMGDNTFPNLMAVLTG-FNKTYANARCHPEKVRGLDACPFIWKDFKDKGYTTAFAEDWSKFSTFDYSSRGFFNP 404
Cdd:pfam02995 160 ELQGYNKVGDNTFPNLLPLLTGkFSEPELEADCDPSCNGSLDKCPFIWKDFKDAGYATAFAEDWAKIGTFNYNKPGFRKQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   405 PTDVYGRPLVLAVEKELTILQRGQMPYCLGRKPASEYIYDMGVQFTMVNRNSTFFGMFWTNTFSHNDFSMPSAMDERMVK 484
Cdd:pfam02995 240 PTDHYLRPLILAIEKHLTYSTRFGLNYCLGRRPTHNYLLDYLRQFLPRYRDSPFFGFFWSNSLSHDDFNYASALDEDFLK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   485 YMRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSGFVEERLPFIYIRVPRWIREKYPKLLRNLQMNKNRLTSPYDIHATL 564
Cdd:pfam02995 320 YLKKLHKRGLLDNTIVIFMSDHGLRFGKLRRTSQGMLEERLPLMSIRYPPWFRETYPQAVENLELNANRLTTPFDLHATL 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   565 RHILELDTPKDKLPRP----DGCSSCHSVFEEVDWSRNCSQAGIEDHWCACNSFSDVPTTDPSARSMSTQLVEAINEYVA 640
Cdd:pfam02995 400 KDILHLGELSDKELQDrmkaLDCPRGISLFLPIPDNRTCSDAGIPEHWCTCEPYKEVPTNDTLVQRIARSVVERINEYLK 479

                         490
                  ....*....|....*.
gi 28571787   641 SKKGTKRCSRLKLNRI 656
Cdd:pfam02995 480 THNLSPLCAPLELQKV 495
ALP_like cd16021
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ...
 293-571 3.58e-133

uncharacterized Alkaline phosphatase subfamily; 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.


Pssm-ID: 293745  Cd Length: 278  Bit Score: 394.19  E-value: 3.58e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 293 PSVLLWGIDSISRMNLELTMPRMYEYL-NNQHWFELQGYNKMGDNTFPNLMAVLTGFN-KTYANARCHPEKVRGLDACPF 370
Cdd:cd16021   1 PNVLILGIDSVSRLNFKRSLPKTLKFLkSELGAVEFKGYNKVGDNTFPNLLPLLTGKSeEELPEARRKESCKGYLDNCPF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 371 IWKDFKDKGYTTAFAEDWSKFSTFDYSSRGFFNPPTDVYGRPLVLAVEKELTILQRGqmpYCLGRKPASEYIYDMGVQFT 450
Cdd:cd16021  81 IWKDFKKAGYVTAFAEDWPKIGTFNYRKKGFKKPPTDHYLRPFWLAAEKTTSYSTKS---YCTGCRPSHKALLDYLEDFI 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 451 MVNRNSTFFGMFWTNTFSHNDFSMPSAMDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSGFVEERLPFIYI 530
Cdd:cd16021 158 EAYKDRPKFSFFWLSELTHDYLNGLSLADEDLLEFLKRLKENGLLDNTFVIFMSDHGLRFGKIRETLQGKLEERLPFLSI 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 28571787 531 RVPRWIREKYPKLLRNLQMNKNRLTSPYDIHATLRHILELD 571
Cdd:cd16021 238 SLPKWFREKYPEAVANLKKNSNRLTTPFDLHATLLDILNLQ 278
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 334-575 1.00e-08

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 58.51  E-value: 1.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 334 GDNTFPNLMAVLTGFNKTYANArchPEKVRGLDACPFIWKDFKDKGYTTAF----AEDWSKFSTFdYSSRGFfnppTDVY 409
Cdd:COG1368 280 GGRTSRGEFAVLTGLPPLPGGS---PYKRPGQNNFPSLPSILKKQGYETSFfhggDGSFWNRDSF-YKNLGF----DEFY 351

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 410 GRplvlaveKELTILQRGQMPYClgrkpaSEYIYDMGVQfTMVNRNSTFFGMFWTNTfSHNDFSMP-----------SAM 478
Cdd:COG1368 352 DR-------EDFDDPFDGGWGVS------DEDLFDKALE-ELEKLKKPFFAFLITLS-NHGPYTLPeedkkipdygkTTL 416

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 479 DERM--VKY--------MRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSGFVEERLPFIyIRVPRWIREKypkllrnlq 548
Cdd:COG1368 417 NNYLnaVRYadqalgefIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENPLERYRVPLL-IYSPGLKKPK--------- 486

                       250       260
                ....*....|....*....|....*..
gi 28571787 549 mNKNRLTSPYDIHATLRHILELDTPKD 575
Cdd:COG1368 487 -VIDTVGSQIDIAPTLLDLLGIDYPSY 512
PRK13759 PRK13759
arylsulfatase; Provisional
 479-511 3.45e-03

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 40.42  E-value: 3.45e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 28571787  479 DERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFG 511
Cdd:PRK13759 278 DHQIGRFLQALKEFGLLDNTIILFVSDHGDMLG 310
 
Name Accession Description Interval E-value
DUF229 pfam02995
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ...
 180-656 0e+00

Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.


Pssm-ID: 397236  Cd Length: 496  Bit Score: 664.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   180 KKHSYIVCDKSRDMITVNYNVTDSTYRLHKNE-----------NSTCCFKQILRAGTSANADHKYKLGPCVEFHQDFLVP 248
Cdd:pfam02995   1 KPNPLRKCSKDQLLTTKSFNITFGTYRLNIDElakprlnerleNLNCEYREIKRKRDSENRDGYSKLFPLRKLTQSVEVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   249 TEVSAMITYCRRPpFDKVSQKDAFSFVHPRKDQIENP---TTPHRRRPSVLLWGIDSISRMNLELTMPRMYEYLNNQHWF 325
Cdd:pfam02995  81 VGCEILITECWED-FGKIYQKDVFNFLHDRIPPKKPKlssTPAEVRKPSVLILGIDSLSRMNFRRSMPRTYKFLKELGWF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   326 ELQGYNKMGDNTFPNLMAVLTG-FNKTYANARCHPEKVRGLDACPFIWKDFKDKGYTTAFAEDWSKFSTFDYSSRGFFNP 404
Cdd:pfam02995 160 ELQGYNKVGDNTFPNLLPLLTGkFSEPELEADCDPSCNGSLDKCPFIWKDFKDAGYATAFAEDWAKIGTFNYNKPGFRKQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   405 PTDVYGRPLVLAVEKELTILQRGQMPYCLGRKPASEYIYDMGVQFTMVNRNSTFFGMFWTNTFSHNDFSMPSAMDERMVK 484
Cdd:pfam02995 240 PTDHYLRPLILAIEKHLTYSTRFGLNYCLGRRPTHNYLLDYLRQFLPRYRDSPFFGFFWSNSLSHDDFNYASALDEDFLK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   485 YMRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSGFVEERLPFIYIRVPRWIREKYPKLLRNLQMNKNRLTSPYDIHATL 564
Cdd:pfam02995 320 YLKKLHKRGLLDNTIVIFMSDHGLRFGKLRRTSQGMLEERLPLMSIRYPPWFRETYPQAVENLELNANRLTTPFDLHATL 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   565 RHILELDTPKDKLPRP----DGCSSCHSVFEEVDWSRNCSQAGIEDHWCACNSFSDVPTTDPSARSMSTQLVEAINEYVA 640
Cdd:pfam02995 400 KDILHLGELSDKELQDrmkaLDCPRGISLFLPIPDNRTCSDAGIPEHWCTCEPYKEVPTNDTLVQRIARSVVERINEYLK 479

                         490
                  ....*....|....*.
gi 28571787   641 SKKGTKRCSRLKLNRI 656
Cdd:pfam02995 480 THNLSPLCAPLELQKV 495
ALP_like cd16021
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ...
 293-571 3.58e-133

uncharacterized Alkaline phosphatase subfamily; 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.


Pssm-ID: 293745  Cd Length: 278  Bit Score: 394.19  E-value: 3.58e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 293 PSVLLWGIDSISRMNLELTMPRMYEYL-NNQHWFELQGYNKMGDNTFPNLMAVLTGFN-KTYANARCHPEKVRGLDACPF 370
Cdd:cd16021   1 PNVLILGIDSVSRLNFKRSLPKTLKFLkSELGAVEFKGYNKVGDNTFPNLLPLLTGKSeEELPEARRKESCKGYLDNCPF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 371 IWKDFKDKGYTTAFAEDWSKFSTFDYSSRGFFNPPTDVYGRPLVLAVEKELTILQRGqmpYCLGRKPASEYIYDMGVQFT 450
Cdd:cd16021  81 IWKDFKKAGYVTAFAEDWPKIGTFNYRKKGFKKPPTDHYLRPFWLAAEKTTSYSTKS---YCTGCRPSHKALLDYLEDFI 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 451 MVNRNSTFFGMFWTNTFSHNDFSMPSAMDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSGFVEERLPFIYI 530
Cdd:cd16021 158 EAYKDRPKFSFFWLSELTHDYLNGLSLADEDLLEFLKRLKENGLLDNTFVIFMSDHGLRFGKIRETLQGKLEERLPFLSI 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 28571787 531 RVPRWIREKYPKLLRNLQMNKNRLTSPYDIHATLRHILELD 571
Cdd:cd16021 238 SLPKWFREKYPEAVANLKKNSNRLTTPFDLHATLLDILNLQ 278
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 293-568 1.37e-39

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: 146.03  E-value: 1.37e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 293 PSVLLWGIDSISRMNLELTM------PRMYEYLNNQHWFELQGYNKMGdNTFPNLMAVLTGFNKTYANARCHPEKVRGL- 365
Cdd:cd00016   1 KHVVLIVLDGLGADDLGKAGnpapttPNLKRLASEGATFNFRSVSPPT-SSAPNHAALLTGAYPTLHGYTGNGSADPELp 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 366 -------DACPFIWKDFKDKGYTTAFAedwskfstfdyssrgffnpptdvygrplvlavekeltilqrgqmpyclgrkpa 438
Cdd:cd00016  80 sraagkdEDGPTIPELLKQAGYRTGVI----------------------------------------------------- 106

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 439 seYIYDMGVQFTMvnrNSTFFGMFWTNTFSHNDFS----------MPSAMDERMVKYMRTLDKNGIMDNTIIIFFSDHGS 508
Cdd:cd00016 107 --GLLKAIDETSK---EKPFVLFLHFDGPDGPGHAygpntpeyydAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG 181

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571787 509 RFGPLRNL-------DSGFVEERLPFIYIRVPRWIrekypkllrnlQMNKNRLTSPYDIHATLRHIL 568
Cdd:cd00016 182 IDKGHGGDpkadgkaDKSHTGMRVPFIAYGPGVKK-----------GGVKHELISQYDIAPTLADLL 237
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 476-575 1.57e-09

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: 60.21  E-value: 1.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 476 SAMDERMVKYMRTLDKNGIMDNTIIIFFSDHGsrfGPL----RNL-DSGFveeRLPFIyIRVPrwirEKYPKLLRNlqmn 550
Cdd:cd16027 196 ERLDQQVGEILDELEEDGLLDNTIVIFTSDHG---MPFprakGTLyDSGL---RVPLI-VRWP----GKIKPGSVS---- 260

                        90       100
                ....*....|....*....|....*
gi 28571787 551 kNRLTSPYDIHATLRHILELDTPKD 575
Cdd:cd16027 261 -DALVSFIDLAPTLLDLAGIEPPEY 284
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
 376-575 5.89e-09

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: 58.69  E-value: 5.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 376 KDKGYTTAFA-------EDWSKFSTFDYSSRG-----FFNPP--------------TDVYGRplvLAVE--KEltilQRG 427
Cdd:cd16031  89 RKAGYQTAFIgkwhlgsGGDLPPPGFDYWVSFpgqgsYYDPEfiengkrvgqkgyvTDIITD---KALDflKE----RDK 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 428 QMPYCL-----------GRKPASEYIYDmGVQF----TMVNRN----STFF---GMFWTNTFShNDFSMPSAMDERMVKY 485
Cdd:cd16031 162 DKPFCLslsfkaphrpfTPAPRHRGLYE-DVTIpepeTFDDDDyagrPEWAreqRNRIRGVLD-GRFDTPEKYQRYMKDY 239

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 486 MRT--------------LDKNGIMDNTIIIFFSDHGSRFGplrnlDSGFVEERLPfiY---IRVPRWIRekYPKLLRNLQ 548
Cdd:cd16031 240 LRTvtgvddnvgrildyLEEQGLADNTIIIYTSDNGFFLG-----EHGLFDKRLM--YeesIRVPLIIR--DPRLIKAGT 310

                       250       260       270
                ....*....|....*....|....*....|
gi 28571787 549 MNKNrLTSPYDIHATlrhILEL---DTPKD 575
Cdd:cd16031 311 VVDA-LVLNIDFAPT---ILDLagvPIPED 336
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 472-575 7.61e-09

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: 58.35  E-value: 7.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 472 FSMPSAMDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFGplrnlDSGFVEERLPFIY-IRVPRWIRekYPKLLRNlQMN 550
Cdd:cd16034 230 YAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLG-----SHGLMNKQVPYEEsIRVPFIIR--YPGKIKA-GRV 301

                        90       100
                ....*....|....*....|....*
gi 28571787 551 KNRLTSPYDIHATLRHILELDTPKD 575
Cdd:cd16034 302 VDLLINTVDIMPTLLGLCGLPIPDT 326
Sulfatase pfam00884
Sulfatase;
343-564 9.18e-09

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 57.43  E-value: 9.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   343 AVLTGFNKTYANARCHPEKVRGLDaCPFIWKDFKDKGYTTAFAEDWSKF--STFDYSSRGFfnppTDVYGRPLVLAVEKE 420
Cdd:pfam00884  55 ALLTGLPPHNFGSYVSTPVGLPRT-EPSLPDLLKRAGYNTGAIGKWHLGwyNNQSPCNLGF----DKFFGRNTGSDLYAD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   421 LTILQrgqmPYCLGRKPASEYIYDMGVQFTMVNRNSTFF--------GMFW--------TNTFSHNDFSMPSAMDE--RM 482
Cdd:pfam00884 130 PPDVP----YNCSGGGVSDEALLDEALEFLDNNDKPFFLvlhtlgshGPPYypdrypekYATFKPSSCSEEQLLNSydNT 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787   483 VKYM--------RTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSGFVEERLPFIYIRVPRWIRekYPKLLRNLQMNKnRL 554
Cdd:pfam00884 206 LLYTddaigrvlDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNAPEGGYRVPLLIW--SPGGKAKGQKSE-AL 282

                         250
                  ....*....|
gi 28571787   555 TSPYDIHATL 564
Cdd:pfam00884 283 VSHVDLFPTI 292
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 334-575 1.00e-08

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 58.51  E-value: 1.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 334 GDNTFPNLMAVLTGFNKTYANArchPEKVRGLDACPFIWKDFKDKGYTTAF----AEDWSKFSTFdYSSRGFfnppTDVY 409
Cdd:COG1368 280 GGRTSRGEFAVLTGLPPLPGGS---PYKRPGQNNFPSLPSILKKQGYETSFfhggDGSFWNRDSF-YKNLGF----DEFY 351

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 410 GRplvlaveKELTILQRGQMPYClgrkpaSEYIYDMGVQfTMVNRNSTFFGMFWTNTfSHNDFSMP-----------SAM 478
Cdd:COG1368 352 DR-------EDFDDPFDGGWGVS------DEDLFDKALE-ELEKLKKPFFAFLITLS-NHGPYTLPeedkkipdygkTTL 416

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 479 DERM--VKY--------MRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSGFVEERLPFIyIRVPRWIREKypkllrnlq 548
Cdd:COG1368 417 NNYLnaVRYadqalgefIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENPLERYRVPLL-IYSPGLKKPK--------- 486

                       250       260
                ....*....|....*....|....*..
gi 28571787 549 mNKNRLTSPYDIHATLRHILELDTPKD 575
Cdd:COG1368 487 -VIDTVGSQIDIAPTLLDLLGIDYPSY 512
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 476-584 2.57e-08

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: 55.14  E-value: 2.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 476 SAMDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSG--FVEE--RLPFIyIRVPRWIREKypkllrnlqMNK 551
Cdd:cd16022 138 SAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKgsLYEGgiRVPFI-VRWPGKIPAG---------QVS 207

                        90       100       110
                ....*....|....*....|....*....|...
gi 28571787 552 NRLTSPYDIHATLRHILELDTPKDklprPDGCS 584
Cdd:cd16022 208 DALVSLLDLLPTLLDLAGIEPPEG----LDGRS 236
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 311-575 1.23e-07

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 53.71  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 311 TMPRMYEYLNNQHWFElQGYnkMGDN-TFPNLMAVLTGFNKTYANARCHPEKVRGldacPFIWKDFKDKGYTTA----FA 385
Cdd:cd16148  25 TTPNLDRLAAEGVVFD-NHY--SGSNpTLPSRFSLFTGLYPFYHGVWGGPLEPDD----PTLAEILRKAGYYTAavssNP 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 386 EDWSKFsTFDyssRGFFnppTDVYGRPLVLAVEKEltilqrgqmpyclgRKPASEYIYDMGVQFtmVNRNST---FFGmf 462
Cdd:cd16148  98 HLFGGP-GFD---RGFD---TFEDFRGQEGDPGEE--------------GDERAERVTDRALEW--LDRNADddpFFL-- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 463 WTNTFS-HNDF------SMpsaMDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFGplrnlDSGFVEERLPFIY---IRV 532
Cdd:cd16148 153 FLHYFDpHEPYlydaevRY---VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFG-----EHGLYWGHGSNLYdeqLHV 224

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 28571787 533 PRWIRekYPKLLRnlQMNKNRLTSPYDIHATLRHILELDTPKD 575
Cdd:cd16148 225 PLIIR--WPGKEP--GKRVDALVSHIDIAPTLLDLLGVEPPDY 263
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 375-584 1.61e-07

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: 54.09  E-value: 1.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 375 FKDKGYTTAF---------AEDWSKFSTFDYSSRGFFNPPTDVYGRPlvlavekeltilqRGQMPYCLGRKPASEYIYD- 444
Cdd:cd16144 103 LKDAGYATAHfgkwhlggeGGYGPEDQGFDVNIGGTGNGGPPSYYFP-------------PGKPNPDLEDGPEGEYLTDr 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 445 ---MGVQFTMVNRNSTFFGMFWT-----------------------NTFSHND---FSMPSAMDE---RMVKYmrtLDKN 492
Cdd:cd16144 170 ltdEAIDFIEQNKDKPFFLYLSHyavhtpiqarpeliekyekkkkgLRKGQKNpvyAAMIESLDEsvgRILDA---LEEL 246

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 493 GIMDNTIIIFFSDHGSRF---------GPLRnldsgfveERLPFIY---IRVP---RWirekyPKLLRNLQMNkNRLTSP 557
Cdd:cd16144 247 GLADNTLVIFTSDNGGLStrggpptsnAPLR--------GGKGSLYeggIRVPlivRW-----PGVIKPGSVS-DVPVIG 312

                       250       260
                ....*....|....*....|....*..
gi 28571787 558 YDIHATLRHILELDTPKDKLprPDGCS 584
Cdd:cd16144 313 TDLYPTFLELAGGPLPPPQH--LDGVS 337
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 476-577 1.83e-07

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


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 53.01  E-value: 1.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 476 SAMDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFG------------PLRNLDSGFveeRLPFIyIRVPrwirEKYPKL 543
Cdd:cd16149 149 TGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGhhgiwgkgngtfPLNMYDNSV---KVPFI-IRWP----GVVPAG 220

                        90       100       110
                ....*....|....*....|....*....|....
gi 28571787 544 LRNLQmnknrLTSPYDIHATLRHILELDTPKDKL 577
Cdd:cd16149 221 RVVDS-----LVSAYDFFPTLLELAGVDPPADPR 249
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
476-536 1.15e-06

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 51.42  E-value: 1.15e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28571787 476 SAMDE---RMVKYmrtLDKNGIMDNTIIIFFSDHGSRFGplrnlDSGFVEE---------RLPFIyIRVPRWI 536
Cdd:COG3119 207 EEVDDqvgRLLDA---LEELGLADNTIVVFTSDNGPSLG-----EHGLRGGkgtlyeggiRVPLI-VRWPGKI 270
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 478-568 3.76e-06

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: 49.22  E-value: 3.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 478 MDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDsgfveERLPFIYIRVPRWIREKYPKLLRnlqmNKNRLTSP 557
Cdd:cd16015 201 TDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDET-----DEDPLDLYRTPLLIYSPGLKKPK----KIDRVGSQ 271

                        90
                ....*....|.
gi 28571787 558 YDIHATLRHIL 568
Cdd:cd16015 272 IDIAPTLLDLL 282
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
 443-584 8.67e-06

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: 48.70  E-value: 8.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 443 YDMGVqftmVNRNSTFFGMFwTNtfshndfsmpsaMDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSGF-- 520
Cdd:cd16146 199 KDMGL----DDKLAAFYGMI-EN------------IDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRFNAGMrg 261

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571787 521 ----VEE---RLPFiYIRVPrwirekypkllRNLQMNK--NRLTSPYDIHATLrhiLEL-DTPKDKLPRPDGCS 584
Cdd:cd16146 262 kkgsVYEgghRVPF-FIRWP-----------GKILAGKdvDTLTAHIDLLPTL---LDLcGVKLPEGIKLDGRS 320
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 478-564 1.23e-05

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: 47.97  E-value: 1.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 478 MDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSGFV--EE--RLPFIyIRVPRwirekYPKLLRNLQMnknr 553
Cdd:cd16035 176 VDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNayEEalHVPLI-ISHPD-----LFGTGQTTDA---- 245

                        90
                ....*....|.
gi 28571787 554 LTSPYDIHATL 564
Cdd:cd16035 246 LTSHIDLLPTL 256
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 472-507 1.85e-05

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: 47.56  E-value: 1.85e-05
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 28571787 472 FSMPSAMDERMVKYMRTLDKNGIMDNTIIIFFSDHG 507
Cdd:cd16155 195 YAMITHLDAQIGRILDALEASGELDNTIIVFTSDHG 230
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 476-584 5.12e-05

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: 46.45  E-value: 5.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 476 SAMDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSGFV--EErlpfIYiRVPRWIreKYPKLLRNLQMNkNR 553
Cdd:cd16033 224 TLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKGPFmyEE----TY-RIPLII--KWPGVIAAGQVV-DE 295

                        90       100       110
                ....*....|....*....|....*....|.
gi 28571787 554 LTSPYDIHATLRHILELDTPkdklPRPDGCS 584
Cdd:cd16033 296 FVSLLDLAPTILDLAGVDVP----PKVDGRS 322
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 486-575 5.93e-05

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: 46.04  E-value: 5.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 486 MRTLDKNGIMDNTIIIFFSDHGSRF---------------GPLRNLDSGFVE--ERLPFIYirvpRWirekyPKLLRNLQ 548
Cdd:cd16143 218 LDALKELGLAENTLVIFTSDNGPSPyadykelekfghdpsGPLRGMKADIYEggHRVPFIV----RW-----PGKIPAGS 288

                        90       100
                ....*....|....*....|....*..
gi 28571787 549 MNkNRLTSPYDIHATLRHILELDTPKD 575
Cdd:cd16143 289 VS-DQLVSLTDLFATLAAIVGQKLPDN 314
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 472-510 7.67e-05

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: 45.68  E-value: 7.67e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 28571787 472 FSMPSAMDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRF 510
Cdd:cd16152 178 LGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGCHF 216
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 447-576 1.41e-04

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: 44.86  E-value: 1.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 447 VQFTMVNRNSTFFgMFWTNTFSHN------DFSMPSA----------MDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRF 510
Cdd:cd16026 174 VDFIERNKDQPFF-LYLAHTMPHVplfaseKFKGRSGaglygdvveeLDWSVGRILDALKELGLEENTLVIFTSDNGPWL 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 511 ---------GPLR-----NLDSGFveeRLPFIYirvpRWirekyPKLLRNLQMNkNRLTSPYDIHATLRHILELDTPKDK 576
Cdd:cd16026 253 eygghggsaGPLRggkgtTWEGGV---RVPFIA----WW-----PGVIPAGTVS-DELASTMDLLPTLAALAGAPLPEDR 319
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 474-536 1.81e-04

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: 44.53  E-value: 1.81e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28571787 474 MPSAMDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFGplrnlDSGFVEE----------RLPFIyIRVPRWI 536
Cdd:cd16150 205 MVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTG-----DYGLVEKwpntfedcltRVPLI-IKPPGGP 271
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 477-537 4.43e-04

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: 43.31  E-value: 4.43e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28571787 477 AMDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFGplrnldsgfvEERLPF----IY---IRVPRWIR 537
Cdd:cd16147 250 SVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLG----------QHRLPPgkrtPYeedIRVPLLVR 307
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
 472-507 4.78e-04

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: 42.95  E-value: 4.78e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 28571787 472 FSMPSAMDERMVKYMRTLDKNGIMDNTIIIFFSDHG 507
Cdd:cd16032 167 YGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHG 202
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 473-584 5.55e-04

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: 42.97  E-value: 5.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 473 SMPSAMDERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSGFVEERLPF------IY---IRVP---RWireky 540
Cdd:cd16145 235 AMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHSEGGSEHDPDFFDSNGPLrgykrsLYeggIRVPfiaRW----- 309

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 28571787 541 PKLLRNLQMNkNRLTSPYDIHATLRHILELDTPKDKlprpDGCS 584
Cdd:cd16145 310 PGKIPAGSVS-DHPSAFWDFMPTLADLAGAEPPEDI----DGIS 348
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
 486-573 9.68e-04

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: 42.58  E-value: 9.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571787 486 MRTLDKNGIMDNTIIIFFSDHGSRFGPLRNLDSG----FVEERL--PFIyIRVPrwirEKYPKLLrnlqmnkNRLTSPYD 559
Cdd:COG3083 444 LDTLEQRGLLENTIVIITADHGEEFNENGQNYWGhnsnFSRYQLqvPLV-IHWP----GTPPQVI-------SKLTSHLD 511

                        90
                ....*....|....*
gi 28571787 560 IHATL-RHILELDTP 573
Cdd:COG3083 512 IVPTLmQRLLGVQNP 526
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 472-507 1.16e-03

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: 41.76  E-value: 1.16e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 28571787 472 FSMPSAMDERMVKYMRTLDKNGIMDNTIIIFFSDHG 507
Cdd:cd16037 165 YGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHG 200
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 476-507 1.52e-03

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: 41.79  E-value: 1.52e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 28571787 476 SAMDERMVKYMRTLDKNGIMDNTIIIFFSDHG 507
Cdd:cd16030 268 SYVDAQVGRVLDALEELGLADNTIVVLWSDHG 299
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 478-507 2.03e-03

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: 41.05  E-value: 2.03e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 28571787 478 MDeRMV-KYMRTLDKNGIMDNTIIIFFSDHG 507
Cdd:cd16151 214 MD-KLVgKLVDKLEELGLRENTIIIFTGDNG 243
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
 473-514 3.14e-03

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: 40.61  E-value: 3.14e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 28571787 473 SMPSAMDE---RMVKymrTLDKNGIMDNTIIIFFSDHG--SRFG------PLR 514
Cdd:cd16029 224 AMVSALDEsvgNVVD---ALKAKGMLDNTLIVFTSDNGgpTGGGdggsnyPLR 273
PRK13759 PRK13759
arylsulfatase; Provisional
 479-511 3.45e-03

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 40.42  E-value: 3.45e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 28571787  479 DERMVKYMRTLDKNGIMDNTIIIFFSDHGSRFG 511
Cdd:PRK13759 278 DHQIGRFLQALKEFGLLDNTIILFVSDHGDMLG 310
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
 474-508 4.77e-03

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: 40.12  E-value: 4.77e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 28571787 474 MPSAMDERMVKYMRTLDKNGIMDNTIIIFFSDHGS 508
Cdd:cd16025 224 MVEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGA 258
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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