NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1321103867|ref|NP_001346503|]
View 

ectonucleotide pyrophosphatase/phosphodiesterase family member 7 precursor [Mus musculus]

Protein Classification

ectonucleotide pyrophosphatase/phosphodiesterase( domain architecture ID 10887878)

ectonucleotide pyrophosphatase/phosphodiesterase (ENPPs) hydrolyzes 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 28-393 6.23e-104

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


:

Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 309.52  E-value: 6.23e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  28 HKLLLVSFDGFRWNY-DQDVDTPNLDSMAQEGVKAQYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMFYNttSTVRLPY 106
Cdd:cd16018     1 PPLIVISIDGFRWDYlDRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYD--PKTNEEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 107 HATLGIQRWWDNGSIPIWITAQRQGLKTGSFFYPGGNVTYQGEAVTMSRKEGVLHNYKNETEWRGNVDTVMKWFLEEDVS 186
Cdd:cd16018    79 SDSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPIPLGGYWQPYNDSFPFEERVDTILEWLDLERPD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 187 LVTLYFGEPDSTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLSDSLNLIITSDHGMTTVnkkasdlvefhkfsnft 266
Cdd:cd16018   159 LILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV----------------- 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 267 fqdiqfelldygpigmlipkegmlekvysvlkdahprlhvykkedfpknfhyannpritpllmysdlgyvihgrvnvqfn 346
Cdd:cd16018       --------------------------------------------------------------------------------

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1321103867 347 nGEHGFNNQDMDMKTIFRAVGPSFKAGLEVEPFESVHVYELMCQLLG 393
Cdd:cd16018   222 -GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 28-393 6.23e-104

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


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 309.52  E-value: 6.23e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  28 HKLLLVSFDGFRWNY-DQDVDTPNLDSMAQEGVKAQYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMFYNttSTVRLPY 106
Cdd:cd16018     1 PPLIVISIDGFRWDYlDRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYD--PKTNEEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 107 HATLGIQRWWDNGSIPIWITAQRQGLKTGSFFYPGGNVTYQGEAVTMSRKEGVLHNYKNETEWRGNVDTVMKWFLEEDVS 186
Cdd:cd16018    79 SDSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPIPLGGYWQPYNDSFPFEERVDTILEWLDLERPD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 187 LVTLYFGEPDSTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLSDSLNLIITSDHGMTTVnkkasdlvefhkfsnft 266
Cdd:cd16018   159 LILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV----------------- 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 267 fqdiqfelldygpigmlipkegmlekvysvlkdahprlhvykkedfpknfhyannpritpllmysdlgyvihgrvnvqfn 346
Cdd:cd16018       --------------------------------------------------------------------------------

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1321103867 347 nGEHGFNNQDMDMKTIFRAVGPSFKAGLEVEPFESVHVYELMCQLLG 393
Cdd:cd16018   222 -GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 30-353 4.82e-88

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 271.60  E-value: 4.82e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  30 LLLVSFDGFRWNY-DQDVDTPNLDSMAQEGVKAQYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMFYNTTSTVRLPYHA 108
Cdd:pfam01663   1 LLVISLDGFRADYlDRFELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 109 TLG-IQRWWDNGsiPIWITAQRQGLKTGSFFYPGGNVTYQGEAVTmsRKEGVLHNYKNETEWRGNVDTVM--KWF----- 180
Cdd:pfam01663  81 SDPeDPRWWQGE--PIWDTAAKAGVRAAALFWPGSEVDYSTYYGT--PPRYLKDDYNNSVPFEDRVDTAVlqTWLdlpfa 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 181 --LEEDVSLVTLYFGEPDSTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLSDSLNLIITSDHGMTTVNKKasDLVE 258
Cdd:pfam01663 157 dvAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDD--KVIF 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 259 FHKFsnFTFQDIqFELLDYGPIGMLIPK--------EGMLEKVYSVLKDA--------HPRLHVYKKEDFPKNFHYanNP 322
Cdd:pfam01663 235 LNDY--LREKGL-LHLVDGGPVVAIYPKarelghvpPGEVEEVYAELKEKllglriqdGEHLAVYLKEEIPGRLHY--NP 309

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1321103867 323 RITPLLMYSDLGYVIHGRVNVQFNN---GEHGFN 353
Cdd:pfam01663 310 RIPDLVLVADPGWYITGKDGGDKEAaihGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 1-394 1.93e-68

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 221.93  E-value: 1.93e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867   1 MGHSAVLLCVALAILPAcvtgAPVQRQHKLLLVSFDGFRWNYDQDVDTPNLDSMAQEGVKAQYMTPAFVTMTSPCHFTLV 80
Cdd:COG1524     1 MKRGLSLLLASLLAAAA----AAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  81 TGKYIENHGVVHNMFYNTTsTVRLPYHATLGIQRWWDNGSI---PIWITAQRQGLKTGSFFYPGGNVT--YQGEAVTMSR 155
Cdd:COG1524    77 TGLYPGEHGIVGNGWYDPE-LGRVVNSLSWVEDGFGSNSLLpvpTIFERARAAGLTTAAVFWPSFEGSglIDAARPYPYD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 156 KEGVLHNYKNETEWRgnVDTVMKWFLEEDVSLVTLYFGEPDSTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLSDS 235
Cdd:COG1524   156 GRKPLLGNPAADRWI--AAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEG 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 236 LNLIITSDHGMTTVNkkasdlvefHKFSNFTFQDIQFELLDYGPIGMLIPKEGMLEKVYSVLKDahpRLHVYKKEDFpKN 315
Cdd:COG1524   234 TLVIVTADHGMVDVP---------PDIDLNRLRLAGLLAVRAGESAHLYLKDGADAEVRALLGL---PARVLTREEL-AA 300

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1321103867 316 FHYaNNPRITPLLMYSDLGYVIHGRVnvqfnNGEHGFNNQDmDMKTIFRAVGPSFKAGlevepFESVHVYELMCQLLGI 394
Cdd:COG1524   301 GHF-GPHRIGDLVLVAKPGWALDAPL-----KGSHGGLPDE-EMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 28-393 6.23e-104

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


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 309.52  E-value: 6.23e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  28 HKLLLVSFDGFRWNY-DQDVDTPNLDSMAQEGVKAQYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMFYNttSTVRLPY 106
Cdd:cd16018     1 PPLIVISIDGFRWDYlDRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYD--PKTNEEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 107 HATLGIQRWWDNGSIPIWITAQRQGLKTGSFFYPGGNVTYQGEAVTMSRKEGVLHNYKNETEWRGNVDTVMKWFLEEDVS 186
Cdd:cd16018    79 SDSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPIPLGGYWQPYNDSFPFEERVDTILEWLDLERPD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 187 LVTLYFGEPDSTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLSDSLNLIITSDHGMTTVnkkasdlvefhkfsnft 266
Cdd:cd16018   159 LILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV----------------- 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 267 fqdiqfelldygpigmlipkegmlekvysvlkdahprlhvykkedfpknfhyannpritpllmysdlgyvihgrvnvqfn 346
Cdd:cd16018       --------------------------------------------------------------------------------

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1321103867 347 nGEHGFNNQDMDMKTIFRAVGPSFKAGLEVEPFESVHVYELMCQLLG 393
Cdd:cd16018   222 -GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 30-353 4.82e-88

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 271.60  E-value: 4.82e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  30 LLLVSFDGFRWNY-DQDVDTPNLDSMAQEGVKAQYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMFYNTTSTVRLPYHA 108
Cdd:pfam01663   1 LLVISLDGFRADYlDRFELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 109 TLG-IQRWWDNGsiPIWITAQRQGLKTGSFFYPGGNVTYQGEAVTmsRKEGVLHNYKNETEWRGNVDTVM--KWF----- 180
Cdd:pfam01663  81 SDPeDPRWWQGE--PIWDTAAKAGVRAAALFWPGSEVDYSTYYGT--PPRYLKDDYNNSVPFEDRVDTAVlqTWLdlpfa 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 181 --LEEDVSLVTLYFGEPDSTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLSDSLNLIITSDHGMTTVNKKasDLVE 258
Cdd:pfam01663 157 dvAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDD--KVIF 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 259 FHKFsnFTFQDIqFELLDYGPIGMLIPK--------EGMLEKVYSVLKDA--------HPRLHVYKKEDFPKNFHYanNP 322
Cdd:pfam01663 235 LNDY--LREKGL-LHLVDGGPVVAIYPKarelghvpPGEVEEVYAELKEKllglriqdGEHLAVYLKEEIPGRLHY--NP 309

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1321103867 323 RITPLLMYSDLGYVIHGRVNVQFNN---GEHGFN 353
Cdd:pfam01663 310 RIPDLVLVADPGWYITGKDGGDKEAaihGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 1-394 1.93e-68

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 221.93  E-value: 1.93e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867   1 MGHSAVLLCVALAILPAcvtgAPVQRQHKLLLVSFDGFRWNYDQDVDTPNLDSMAQEGVKAQYMTPAFVTMTSPCHFTLV 80
Cdd:COG1524     1 MKRGLSLLLASLLAAAA----AAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  81 TGKYIENHGVVHNMFYNTTsTVRLPYHATLGIQRWWDNGSI---PIWITAQRQGLKTGSFFYPGGNVT--YQGEAVTMSR 155
Cdd:COG1524    77 TGLYPGEHGIVGNGWYDPE-LGRVVNSLSWVEDGFGSNSLLpvpTIFERARAAGLTTAAVFWPSFEGSglIDAARPYPYD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 156 KEGVLHNYKNETEWRgnVDTVMKWFLEEDVSLVTLYFGEPDSTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLSDS 235
Cdd:COG1524   156 GRKPLLGNPAADRWI--AAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEG 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 236 LNLIITSDHGMTTVNkkasdlvefHKFSNFTFQDIQFELLDYGPIGMLIPKEGMLEKVYSVLKDahpRLHVYKKEDFpKN 315
Cdd:COG1524   234 TLVIVTADHGMVDVP---------PDIDLNRLRLAGLLAVRAGESAHLYLKDGADAEVRALLGL---PARVLTREEL-AA 300

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1321103867 316 FHYaNNPRITPLLMYSDLGYVIHGRVnvqfnNGEHGFNNQDmDMKTIFRAVGPSFKAGlevepFESVHVYELMCQLLGI 394
Cdd:COG1524   301 GHF-GPHRIGDLVLVAKPGWALDAPL-----KGSHGGLPDE-EMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 30-247 1.06e-18

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: 84.78  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  30 LLLVSFDGFRWNYDQD-----VDTPNLDSMAQEGVKAQYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMFYNTTSTVRl 104
Cdd:cd00016     3 VVLIVLDGLGADDLGKagnpaPTTPNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELPSR- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 105 PYHatlgiqrwWDNGSIPIWITAQRQGLKTGSFFypggnvtyqgeavtmsrkegvlhnyknetewrgnVDTVMKWFLEED 184
Cdd:cd00016    82 AAG--------KDEDGPTIPELLKQAGYRTGVIG----------------------------------LLKAIDETSKEK 119

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1321103867 185 VSLVTLYFGEPDSTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLSDSLNLIITSDHGMT 247
Cdd:cd00016   120 PFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGI 182
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 42-246 1.21e-08

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: 56.36  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  42 YDQDVDTPNLDSMAQEGVKaqyMTPAFVT--MTSPCHFTLVTGKYIENHGVVHNMFYNTTSTVRLP----------YHAT 109
Cdd:cd16027    19 GGNVVKTPNLDRLAAEGVR---FTNAFTTapVCSPSRSALLTGLYPHQNGAHGLRSRGFPLPDGVKtlpellreagYYTG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 110 LgIQRWWDNGSipiwitaqrqglKTGSFFYPGGNVTYQGEAVTmsrkegvlHNYKNETEWRGNVDTVMKWFLeedvsLVT 189
Cdd:cd16027    96 L-IGKTHYNPD------------AVFPFDDEMRGPDDGGRNAW--------DYASNAADFLNRAKKGQPFFL-----WFG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 190 L-------YFGEPDSTGHK--------YGPESQE-RKDM------VKQVDRTVGYLRDSIKRHHLSDslN-LII-TSDHG 245
Cdd:cd16027   150 FhdphrpyPPGDGEEPGYDpekvkvppYLPDTPEvREDLadyydeIERLDQQVGEILDELEEDGLLD--NtIVIfTSDHG 227


                  .
gi 1321103867 246 M 246
Cdd:cd16027   228 M 228
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
45-245 5.11e-07

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: 5.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  45 DVDTPNLDSMAQEGVKaqyMTPAFVT--MTSPCHFTLVTGKYIENHGVVHNmfyNTTSTVRLPYHATlgiqrwwdngSIP 122
Cdd:COG3119    46 LIKTPNIDRLAAEGVR---FTNAYVTspVCSPSRASLLTGRYPHRTGVTDN---GEGYNGGLPPDEP----------TLA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 123 IWItaQRQGLKTGSF----FYPGGNVTyqGEAVTMsrkegvLHNYKNETEwrgnvdtvmKWFL--------------EED 184
Cdd:COG3119   110 ELL--KEAGYRTALFgkwhLYLTDLLT--DKAIDF------LERQADKDK---------PFFLylafnaphapyqapEEY 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 185 VSL-------VTLYFGEPDSTGHKYGPESQERKDMVKQVDRTVGYLRDSIKRHHLSDslNLII--TSDHG 245
Cdd:COG3119   171 LDKydgkdipLPPNLAPRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLAD--NTIVvfTSDNG 238
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 29-245 1.31e-06

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: 49.47  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  29 KLLLVSFDGFRW------NYDQDVdTPNLDSMAQEGVK-AQYMTPAFVTMTSpcHFTLVTGKYIENHGVVHnmfynttst 101
Cdd:cd16148     2 NVILIVIDSLRAdhlgcyGYDRVT-TPNLDRLAAEGVVfDNHYSGSNPTLPS--RFSLFTGLYPFYHGVWG--------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 102 vrlpyhatlgiqrWWDNGSIPIWITA-QRQGLKTG---SFFYPGGNVTY-QG-EAVTMSRKEGVLHNYKNETEWRGNVDT 175
Cdd:cd16148    70 -------------GPLEPDDPTLAEIlRKAGYYTAavsSNPHLFGGPGFdRGfDTFEDFRGQEGDPGEEGDERAERVTDR 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1321103867 176 VMKWF----LEEDVSLVTLYFgEPdstgH---KYGPEsqerkdmVKQVDRTVGYLRDSIKRHHLSDSLNLIITSDHG 245
Cdd:cd16148   137 ALEWLdrnaDDDPFFLFLHYF-DP----HepyLYDAE-------VRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG 201
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 45-245 8.31e-06

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: 46.66  E-value: 8.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  45 DVDTPNLDSMAQEGVKaqyMTPAFVT--MTSPCHFTLVTGKYIENHGVVhnmfYNTTSTVRLPYHATLgiqrwwdngsip 122
Cdd:cd16022    23 DIKTPNLDRLAAEGVR---FTNAYVAspVCSPSRASLLTGRYPHRHGVR----GNVGNGGGLPPDEPT------------ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 123 IWITAQRQGLKTGSFfypggnvtyqgeavtmsrkeGVLHNyknetewrgnvDTVmkWFLEEDVS----LVTLYFGEPDST 198
Cdd:cd16022    84 LAELLKEAGYRTALI--------------------GKWHD-----------EAI--DFIERRDKdkpfFLYVSFNAPHPP 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1321103867 199 GHKYGpesqerkdMVKQVDRTVGYLRDSIKRHHLSDslNLII--TSDHG 245
Cdd:cd16022   131 FAYYA--------MVSAIDDQIGRILDALEELGLLD--NTLIvfTSDHG 169
Sulfatase pfam00884
Sulfatase;
30-296 1.10e-05

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 47.03  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  30 LLLVSFDGFRWNY-----DQDVDTPNLDSMAQEGV-KAQYMTPAfvTMTSPCHFTLVTGKYIENHGVVHNmfyntTSTVR 103
Cdd:pfam00884   3 VVLVLGESLRAPDlglygYPRPTTPFLDRLAEEGLlFSNFYSGG--TLTAPSRFALLTGLPPHNFGSYVS-----TPVGL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 104 LPYHATL-------GIQRWWDNGSIPIWITaqRQGLKTGSFFYPGGNVTYQgEAVTMSRKEGVLHNYKNE------TEWR 170
Cdd:pfam00884  76 PRTEPSLpdllkraGYNTGAIGKWHLGWYN--NQSPCNLGFDKFFGRNTGS-DLYADPPDVPYNCSGGGVsdeallDEAL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 171 GNVDTVMK-WFLeedvSLVTL-------YFGEPDSTGHKYGPESQERKDMVKQVDRTVGYLRDSIKR-------HHLSDS 235
Cdd:pfam00884 153 EFLDNNDKpFFL----VLHTLgshgppyYPDRYPEKYATFKPSSCSEEQLLNSYDNTLLYTDDAIGRvldkleeNGLLDN 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1321103867 236 LNLIITSDHGMTTVNKKASDLveFHKFSNFTFQDIQFELLDYGPIGmlIPKEGMLEKVYSV 296
Cdd:pfam00884 229 TLVVYTSDHGESLGEGGGYLH--GGKYDNAPEGGYRVPLLIWSPGG--KAKGQKSEALVSH 285
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 43-93 1.17e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 47.18  E-value: 1.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1321103867  43 DQDVDTPNLDSMAQEGVkaqYMTPAFVTM--TSPCHFTLVTGKYIENHGVVHN 93
Cdd:cd16034    22 DDPVKTPNLDRLAKEGV---VFTNAVSNYpvCSPYRASLLTGQYPLTNGVFGN 71
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 196-248 1.31e-05

GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293747  Cd Length: 289  Bit Score: 46.78  E-value: 1.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1321103867 196 DSTGHKYGPESQERKDMVKQVDRtvgYLRDSIKRHHlSDSLnLIITSDHGMTT 248
Cdd:cd16023   171 DHVGHRYGPNHPEMARKLTQMDQ---FIRDIIERLD-DDTL-LLVFGDHGMTE 218
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
 30-93 3.75e-05

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: 45.71  E-value: 3.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1321103867  30 LLLVSFDGFRWNY-----DQDVDTPNLDSMAQEGVKaqyMTPAFVTMTsPC---HFTLVTGKYIENHGVVHN 93
Cdd:cd16028     3 VLFITADQWRADClsclgHPLVKTPNLDRLAAEGVR---FRNHYTQAA-PCgpsRASLYTGRYLMNHRSVWN 70
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 45-246 5.33e-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: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 44.54  E-value: 5.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  45 DVDTPNLDSMAQEGVKaqyMTPAFVT--MTSPCHFTLVTGKYIENHGvVHNmfynttstvrlpyhatlgiqrwwdngsip 122
Cdd:cd16149    23 EAVTPNLDRLAAEGVR---FENFFCTspVCSPARASLLTGRMPSQHG-IHD----------------------------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 123 iWITAQRQGLKTGSFFYPGGNVTYQgeavtmsrkeGVLHNYKNETEWRGnvdtvmKW--------FLEEDVS-----LVT 189
Cdd:cd16149    70 -WIVEGSHGKTKKPEGYLEGQTTLP----------EVLQDAGYRCGLSG------KWhlgddaadFLRRRAEaekpfFLS 132

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1321103867 190 LYFGEPDSTgHKYGPEsqerkdmVKQVDRTVGYLRDSIKRHHLSDSLNLIITSDHGM 246
Cdd:cd16149   133 VNYTAPHSP-WGYFAA-------VTGVDRNVGRLLDELEELGLTENTLVIFTSDNGF 181
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 46-106 6.28e-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: 44.90  E-value: 6.28e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1321103867  46 VDTPNLDSMAQEGVkaqYMTPAFVTMT--SPCHFTLVTGKYIENHGVVHNMfYNTTSTVRLPY 106
Cdd:cd16033    24 VKTPNIDRLAAEGV---RFTNAYTPSPvcCPARASLLTGLYPHEHGVLNNV-ENAGAYSRGLP 82
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 182-247 7.42e-05

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


Pssm-ID: 293743 [Multi-domain]  Cd Length: 292  Bit Score: 44.27  E-value: 7.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1321103867 182 EEDVSLVTLYFGEPDSTGHKYG-PESQERKDMVKQVDRtvgYLRDSIKRhhLSDSLNLIITSDHGMT 247
Cdd:cd16019   150 YDNWDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDN---LIRDIYDR--MDNDTLLVVVSDHGMN 211
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
 43-93 1.77e-04

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: 43.67  E-value: 1.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1321103867  43 DQDVDTPNLDSMAQEGVkaqYMTPAFVTmTSPC---HFTLVTGKYIENHGVVHN 93
Cdd:cd16031    23 NPIVKTPNIDRLAKEGV---RFDNAFVT-TSICapsRASILTGQYSHRHGVTDN 72
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 48-245 2.27e-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: 293762 [Multi-domain]  Cd Length: 395  Bit Score: 43.34  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  48 TPNLDSMAQEGVKAqymTPAFVT--MTSPCHFTLVTGKY---IENHGVVHNMFYNT---TSTVRLP-------YHaT--- 109
Cdd:cd16143    27 TPNIDRLAAEGMRF---TDAHSPssVCTPSRYGLLTGRYpwrSRLKGGVLGGFSPPliePDRVTLAkmlkqagYR-Tamv 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 110 ----LGIQrWWDNGSIPIWITAQR-----QGLKTG--------SFFYPGGNVtyqgeAVTMSRK-EGVLHNYKNETewrg 171
Cdd:cd16143   103 gkwhLGLD-WKKKDGKKAATGTGKdvdysKPIKGGpldhgfdyYFGIPASEV-----LPTLTDKaVEFIDQHAKKD---- 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 172 nvdtvmKWFLeedvslvtLYFGEPD--------------STGHKYGpesqerkDMVKQVDRTVGYLRDSIKRHHLSDSLN 237
Cdd:cd16143   173 ------KPFF--------LYFALPAphtpivpspefqgkSGAGPYG-------DFVYELDWVVGRILDALKELGLAENTL 231


                  ....*...
gi 1321103867 238 LIITSDHG 245
Cdd:cd16143   232 VIFTSDNG 239
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 36-93 3.57e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 42.60  E-value: 3.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1321103867  36 DGFRWN----YDQDVD-TPNLDSMAQEGVKAQYM-TPAFVtmTSPCHFTLVTGKYIENHGVVHN 93
Cdd:cd16152    10 DQQRWDtlgcYGQPLDlTPNLDALAEEGVLFENAfTPQPV--CGPARACLQTGLYPTETGCFRN 71
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 43-135 8.33e-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: 41.38  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  43 DQDVDTPNLDSM-------AQEGVkaqYMTPAFVTmTSPC---HFTLVTGKYIENHGVVHNmfynttstvRLPYHatlGI 112
Cdd:cd16147    11 DQDVELGSMDPMpktkkllADQGT---TFTNAFVT-TPLCcpsRASILTGQYAHNHGVTNN---------SPPGG---GY 74

                          90       100
                  ....*....|....*....|....*..
gi 1321103867 113 QRWWDNG----SIPIWItaQRQGLKTG 135
Cdd:cd16147    75 PKFWQNGlersTLPVWL--QEAGYRTA 99
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 44-245 1.02e-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: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  44 QDVDTPNLDSMAQEGVKAQ--YMTPafvtMTSPCHFTLVTGKYIENHGVVH-----------NMF----YNT-------- 98
Cdd:cd16151    22 ESYKTPNIDALAAEGVRFNnaYAQP----LCTPSRVQLMTGKYNFRNYVVFgyldpkqktfgHLLkdagYATaiagkwql 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867  99 -TSTVRLPYHATLGiqrwWDNGSipIWitaqrQGLKTGSFFYPGGNVTYQGEavtmsrkEGVLHNYKNetEWRGN---VD 174
Cdd:cd16151    98 gGGRGDGDYPHEFG----FDEYC--LW-----QLTETGEKYSRPATPTFNIR-------NGKLLETTE--GDYGPdlfAD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321103867 175 TVMKwFLEED----------VSLV-TLYFGEPDSTGHKYGPESQER-----KDMVKQVDRTVGYLRDSIKRHHLSDSLNL 238
Cdd:cd16151   158 FLID-FIERNkdqpffayypMVLVhDPFVPTPDSPDWDPDDKRKKDdpeyfPDMVAYMDKLVGKLVDKLEELGLRENTII 236


                  ....*..
gi 1321103867 239 IITSDHG 245
Cdd:cd16151   237 IFTGDNG 243
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 46-105 1.24e-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: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 40.44  E-value: 1.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1321103867  46 VDTPNLDSMAQEGV---KAQYMTPAFVtmtsPCHFTLVTGKYIENHGVVHNMFYNTTSTVRLP 105
Cdd:cd16153    35 VESPNIDALAAEGVlftNAYCNSPVCV----PSRTSMLTGRYPHRTGVYGFEAAHPALDHGLP 93
 
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