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Conserved domains on  [gi|530788254|ref|NP_848638|]
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ectonucleotide pyrophosphatase/phosphodiesterase family member 7 precursor [Homo sapiens]

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

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List of domain hits

 Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 31-396 4.24e-107

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: 318.37  E-value: 4.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  31 NKLLLVSFDGFRWNY-DQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNttSKVKLPY 109
Cdd:cd16018    1 PPLIVISIDGFRWDYlDRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYD--PKTNEEF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 110 HATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLD 189
Cdd:cd16018   79 SDSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPIPLGGYWQPYNDSFPFEERVDTILEWLDLERPD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 190 LVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVdkragdlvefhkfpnft 269
Cdd:cd16018  159 LILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV----------------- 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 270 frdiefelldygpngmllpkegrlekvydalkdahpklhvykkeafpeafhyannprvtpllmysdlgyvihgrinvqfn 349
Cdd:cd16018      --------------------------------------------------------------------------------

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 530788254 350 nGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLG 396
Cdd:cd16018  222 -GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 31-396 4.24e-107

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: 318.37  E-value: 4.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  31 NKLLLVSFDGFRWNY-DQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNttSKVKLPY 109
Cdd:cd16018    1 PPLIVISIDGFRWDYlDRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYD--PKTNEEF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 110 HATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLD 189
Cdd:cd16018   79 SDSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPIPLGGYWQPYNDSFPFEERVDTILEWLDLERPD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 190 LVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVdkragdlvefhkfpnft 269
Cdd:cd16018  159 LILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV----------------- 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 270 frdiefelldygpngmllpkegrlekvydalkdahpklhvykkeafpeafhyannprvtpllmysdlgyvihgrinvqfn 349
Cdd:cd16018      --------------------------------------------------------------------------------

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 530788254 350 nGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLG 396
Cdd:cd16018  222 -GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 33-356 1.47e-90

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: 278.92  E-value: 1.47e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254   33 LLLVSFDGFRWNY-DQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHA 111
Cdd:pfam01663   1 LLVISLDGFRADYlDRFELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  112 TLG-IQRWWDNGsvPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRkeGIAHNYKNETEWRANIDTVM--AWFTEEDL 188
Cdd:pfam01663  81 SDPeDPRWWQGE--PIWDTAAKAGVRAAALFWPGSEVDYSTYYGTPPR--YLKDDYNNSVPFEDRVDTAVlqTWLDLPFA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  189 -------DLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKraGDLVE 261
Cdd:pfam01663 157 dvaaerpDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSD--DKVIF 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  262 FHKFPNFtfrDIEFELLDYGPNGMLLPK--------EGRLEKVYDALKDA--------HPKLHVYKKEAFPEAFHYanNP 325
Cdd:pfam01663 235 LNDYLRE---KGLLHLVDGGPVVAIYPKarelghvpPGEVEEVYAELKEKllglriqdGEHLAVYLKEEIPGRLHY--NP 309

                         330       340       350
                  ....*....|....*....|....*....|....
gi 530788254  326 RVTPLLMYSDLGYVIHGRINVQFNN---GEHGFD 356
Cdd:pfam01663 310 RIPDLVLVADPGWYITGKDGGDKEAaihGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 20-397 4.52e-69

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 224.24  E-value: 4.52e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  20 AGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYY 99
Cdd:COG1524   13 LAAAAAAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 100 NTTSKvKLPYHATLGIQRWWDNGSV---PIWITAQRQGLRAGSFFYPGGNVT--YQGVAVTRSRKEGIAHNYKNETEWRA 174
Cdd:COG1524   93 DPELG-RVVNSLSWVEDGFGSNSLLpvpTIFERARAAGLTTAAVFWPSFEGSglIDAARPYPYDGRKPLLGNPAADRWIA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 175 niDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDK 254
Cdd:COG1524  172 --AAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVPP 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 255 RagdlvefhkFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDahpKLHVYKKEAFpEAFHYaNNPRVTPLLMYS 334
Cdd:COG1524  250 D---------IDLNRLRLAGLLAVRAGESAHLYLKDGADAEVRALLGL---PARVLTREEL-AAGHF-GPHRIGDLVLVA 315

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530788254 335 DLGYVIHGRInvqfnNGEHGFDNKDmDMKTIFRAVGPSFRAGlevepFESVHVYELMCRLLGI 397
Cdd:COG1524  316 KPGWALDAPL-----KGSHGGLPDE-EMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 31-396 4.24e-107

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: 318.37  E-value: 4.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  31 NKLLLVSFDGFRWNY-DQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNttSKVKLPY 109
Cdd:cd16018    1 PPLIVISIDGFRWDYlDRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYD--PKTNEEF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 110 HATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLD 189
Cdd:cd16018   79 SDSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPIPLGGYWQPYNDSFPFEERVDTILEWLDLERPD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 190 LVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVdkragdlvefhkfpnft 269
Cdd:cd16018  159 LILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV----------------- 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 270 frdiefelldygpngmllpkegrlekvydalkdahpklhvykkeafpeafhyannprvtpllmysdlgyvihgrinvqfn 349
Cdd:cd16018      --------------------------------------------------------------------------------

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 530788254 350 nGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLG 396
Cdd:cd16018  222 -GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 33-356 1.47e-90

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: 278.92  E-value: 1.47e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254   33 LLLVSFDGFRWNY-DQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHA 111
Cdd:pfam01663   1 LLVISLDGFRADYlDRFELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  112 TLG-IQRWWDNGsvPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRkeGIAHNYKNETEWRANIDTVM--AWFTEEDL 188
Cdd:pfam01663  81 SDPeDPRWWQGE--PIWDTAAKAGVRAAALFWPGSEVDYSTYYGTPPR--YLKDDYNNSVPFEDRVDTAVlqTWLDLPFA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  189 -------DLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKraGDLVE 261
Cdd:pfam01663 157 dvaaerpDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSD--DKVIF 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  262 FHKFPNFtfrDIEFELLDYGPNGMLLPK--------EGRLEKVYDALKDA--------HPKLHVYKKEAFPEAFHYanNP 325
Cdd:pfam01663 235 LNDYLRE---KGLLHLVDGGPVVAIYPKarelghvpPGEVEEVYAELKEKllglriqdGEHLAVYLKEEIPGRLHY--NP 309

                         330       340       350
                  ....*....|....*....|....*....|....
gi 530788254  326 RVTPLLMYSDLGYVIHGRINVQFNN---GEHGFD 356
Cdd:pfam01663 310 RIPDLVLVADPGWYITGKDGGDKEAaihGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 20-397 4.52e-69

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 224.24  E-value: 4.52e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  20 AGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYY 99
Cdd:COG1524   13 LAAAAAAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 100 NTTSKvKLPYHATLGIQRWWDNGSV---PIWITAQRQGLRAGSFFYPGGNVT--YQGVAVTRSRKEGIAHNYKNETEWRA 174
Cdd:COG1524   93 DPELG-RVVNSLSWVEDGFGSNSLLpvpTIFERARAAGLTTAAVFWPSFEGSglIDAARPYPYDGRKPLLGNPAADRWIA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 175 niDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDK 254
Cdd:COG1524  172 --AAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDVPP 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 255 RagdlvefhkFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDahpKLHVYKKEAFpEAFHYaNNPRVTPLLMYS 334
Cdd:COG1524  250 D---------IDLNRLRLAGLLAVRAGESAHLYLKDGADAEVRALLGL---PARVLTREEL-AAGHF-GPHRIGDLVLVA 315

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530788254 335 DLGYVIHGRInvqfnNGEHGFDNKDmDMKTIFRAVGPSFRAGlevepFESVHVYELMCRLLGI 397
Cdd:COG1524  316 KPGWALDAPL-----KGSHGGLPDE-EMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 33-250 4.36e-16

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: 77.46  E-value: 4.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  33 LLLVSFDGFRWNYDQD-----VDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTskvkL 107
Cdd:cd00016    3 VVLIVLDGLGADDLGKagnpaPTTPNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPE----L 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 108 PYHATlgiqRWWDNGsVPIWITAQRQGLRAGSFFypggnvtyqgvavtrsrkegiahnyknetewranIDTVMAWFTEED 187
Cdd:cd00016   79 PSRAA----GKDEDG-PTIPELLKQAGYRTGVIG----------------------------------LLKAIDETSKEK 119

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530788254 188 LDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMT 250
Cdd:cd00016  120 PFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGI 182
COG3379 COG3379
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ...
 28-254 1.20e-09

Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];


Pssm-ID: 442606 [Multi-domain]  Cd Length: 472  Bit Score: 60.30  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  28 GSQNKLLLVSFDG------FRWNydQDVDTPNLDAMARDGVKARyMTPAFVTMTSPCHFTLVTGKYIENHGVvhnmyYNT 101
Cdd:COG3379    2 GDMPRVLVIGLDGappdllDPWI--ARGELPNLARLAEEGAYGR-LRSTIPPITPPAWTSMMTGRNPGEHGV-----YGF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 102 TSKVKLPYHATLGIQRwwDNGSVPIWITAQRQGLRAGSFFYPggnVTY-----QGVAVT-----------------RSRK 159
Cdd:COG3379   74 RDREPGSYDTRVANSR--DVRAPTLWDILSRAGKRVTVLNVP---VTYpprpvNGVMVSgfltpdllgdatyppelADEL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 160 EGIAHNY----------KNETEWRANI-DTVMAWFT-------EEDLDLVTLYFGEPDSTGH-----------RYGPESP 210
Cdd:COG3379  149 EALVGDYridvnaklrpDDKEELLEDLyETLEKRFEaarhlleEDDWDLFMVVFMGTDRVQHflwhyydpdhpLYDPDGP 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 530788254 211 ERREMV---RQVDRTVGYLREsiarnHLTDRLNLIITSDHGMTTVDK 254
Cdd:COG3379  229 YRDAILdyyRALDRYIGELLE-----LAGDDTTVVVVSDHGFGPLDG 270
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 45-249 2.20e-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: 59.06  E-value: 2.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  45 YDQDVDTPNLDAMARDGVkaRYmTPAFVT--MTSPCHFTLVTGKYIENHGVVHN--MYYNTTSKVK-LP-------YHAT 112
Cdd:cd16027   19 GGNVVKTPNLDRLAAEGV--RF-TNAFTTapVCSPSRSALLTGLYPHQNGAHGLrsRGFPLPDGVKtLPellreagYYTG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 113 LgIQRWWDNGSVPiwitaqrqglraGSFFYPGGNVTYQGvavtrsrkEGIAHNYKNETEWRANIDTVMAWFteedldlvt 192
Cdd:cd16027   96 L-IGKTHYNPDAV------------FPFDDEMRGPDDGG--------RNAWDYASNAADFLNRAKKGQPFF--------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 193 LYFGEPDStgHR---------------------YGPESPERRE-------MVRQVDRTVGYLRESIARNHLTDrlN-LII 243
Cdd:cd16027  146 LWFGFHDP--HRpyppgdgeepgydpekvkvppYLPDTPEVREdladyydEIERLDQQVGEILDELEEDGLLD--NtIVI 221


                 ....*..
gi 530788254 244 -TSDHGM 249
Cdd:cd16027  222 fTSDHGM 228
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 32-248 1.35e-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: 49.85  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  32 KLLLVSFDGFRW------NYDQDVdTPNLDAMARDGVK-ARYMTPAFVTMTSpcHFTLVTGKYIENHGVVhnmyynttsK 104
Cdd:cd16148    2 NVILIVIDSLRAdhlgcyGYDRVT-TPNLDRLAAEGVVfDNHYSGSNPTLPS--RFSLFTGLYPFYHGVW---------G 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 105 VKLPYHATLGIQRWWDNGsvpiWITAqrqGLRAGSFFYPGGNVtYQGV-AVTRSRKEGIAHNYKNETEWRANIDTVMAWF 183
Cdd:cd16148   70 GPLEPDDPTLAEILRKAG----YYTA---AVSSNPHLFGGPGF-DRGFdTFEDFRGQEGDPGEEGDERAERVTDRALEWL 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530788254 184 TEEDLD----LVTLYFgEPdstgH---RYgpesperREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHG 248
Cdd:cd16148  142 DRNADDdpffLFLHYF-DP----HepyLY-------DAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG 201
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 46-96 2.06e-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: 46.79  E-value: 2.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530788254  46 DQDVDTPNLDAMARDGVkarYMTPAFVTM--TSPCHFTLVTGKYIENHGVVHN 96
Cdd:cd16034   22 DDPVKTPNLDRLAKEGV---VFTNAVSNYpvCSPYRASLLTGQYPLTNGVFGN 71
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
 31-96 2.46e-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: 46.48  E-value: 2.46e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530788254  31 NKLLLVSFDGFRWNY-----DQDVDTPNLDAMARDGVKaryMTPAFVTMTsPC---HFTLVTGKYIENHGVVHN 96
Cdd:cd16028    1 RNVLFITADQWRADClsclgHPLVKTPNLDRLAAEGVR---FRNHYTQAA-PCgpsRASLYTGRYLMNHRSVWN 70
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 199-251 2.55e-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: 46.01  E-value: 2.55e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530788254 199 DSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLtdrlnLIITSDHGMTT 251
Cdd:cd16023  171 DHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTL-----LLVFGDHGMTE 218
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 48-101 5.87e-05

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: 44.35  E-value: 5.87e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530788254  48 DVDTPNLDAMARDGVKaryMTPAFVT--MTSPCHFTLVTGKYIENHGVVHNMYYNT 101
Cdd:cd16022   23 DIKTPNLDRLAAEGVR---FTNAYVAspVCSPSRASLLTGRYPHRHGVRGNVGNGG 75
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
48-248 7.54e-05

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 44.87  E-value: 7.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  48 DVDTPNLDAMARDGVKaryMTPAFVT--MTSPCHFTLVTGKYIENHGVVHNMYYnttskvklpyhatlgiQRWWDNGSVP 125
Cdd:COG3119   46 LIKTPNIDRLAAEGVR---FTNAYVTspVCSPSRASLLTGRYPHRTGVTDNGEG----------------YNGGLPPDEP 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 126 IWITA-QRQGLRAGSF----FYPGGNVTYQGVA-VTRSRKEG------IAHN-----YKNETEWRANidtvmawFTEEDL 188
Cdd:COG3119  107 TLAELlKEAGYRTALFgkwhLYLTDLLTDKAIDfLERQADKDkpfflyLAFNaphapYQAPEEYLDK-------YDGKDI 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 189 DLVTlYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHG 248
Cdd:COG3119  180 PLPP-NLAPRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNG 238
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 31-96 8.47e-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: 44.53  E-value: 8.47e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530788254  31 NKLLLVSfDGFRWN----YDQDVD-TPNLDAMARDGVKARYM-TPAFVtmTSPCHFTLVTGKYIENHGVVHN 96
Cdd:cd16152    3 NVIVFFT-DQQRWDtlgcYGQPLDlTPNLDALAEEGVLFENAfTPQPV--CGPARACLQTGLYPTETGCFRN 71
Sulfatase pfam00884
Sulfatase;
30-248 1.45e-04

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 43.57  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254   30 QNKLLLVSfDGFRWNY-----DQDVDTPNLDAMARDGV-KARYMTPAfvTMTSPCHFTLVTGKYIENHGVVHNmyyntTS 103
Cdd:pfam00884   1 PNVVLVLG-ESLRAPDlglygYPRPTTPFLDRLAEEGLlFSNFYSGG--TLTAPSRFALLTGLPPHNFGSYVS-----TP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  104 KVKLPYHATL-------GIQR---------WWDNGSVPIWitaqrqglragSFFYPGGNVTYQgvavtrsrkEGIAHNYK 167
Cdd:pfam00884  73 VGLPRTEPSLpdllkraGYNTgaigkwhlgWYNNQSPCNL-----------GFDKFFGRNTGS---------DLYADPPD 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254  168 NETEWRAN--IDTVMAWFTEEDLD---------LVTL-------YFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRES 229
Cdd:pfam00884 133 VPYNCSGGgvSDEALLDEALEFLDnndkpfflvLHTLgshgppyYPDRYPEKYATFKPSSCSEEQLLNSYDNTLLYTDDA 212

                         250       260
                  ....*....|....*....|....*...
gi 530788254  230 IARnhLTDRLN---------LIITSDHG 248
Cdd:pfam00884 213 IGR--VLDKLEenglldntlVVYTSDHG 238
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
 46-96 1.71e-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: 1.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530788254  46 DQDVDTPNLDAMARDGVkarYMTPAFVTmTSPC---HFTLVTGKYIENHGVVHN 96
Cdd:cd16031   23 NPIVKTPNIDRLAKEGV---RFDNAFVT-TSICapsRASILTGQYSHRHGVTDN 72
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 49-98 3.54e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 42.59  E-value: 3.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530788254  49 VDTPNLDAMARDGVkarYMTPAFVTMT--SPCHFTLVTGKYIENHGVVHNMY 98
Cdd:cd16033   24 VKTPNIDRLAAEGV---RFTNAYTPSPvcCPARASLLTGLYPHEHGVLNNVE 72
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 184-250 4.46e-04

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: 41.96  E-value: 4.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530788254 184 TEEDLDLVTLYFGEPDSTGHRYG-PESPERREMVRQVDRtvgYLRESIarNHLTDRLNLIITSDHGMT 250
Cdd:cd16019  149 YYDNWDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDN---LIRDIY--DRMDNDTLLVVVSDHGMN 211
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 49-108 8.16e-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: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 41.21  E-value: 8.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530788254  49 VDTPNLDAMARDGV---KARYMTPAFVtmtsPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLP 108
Cdd:cd16153   35 VESPNIDALAAEGVlftNAYCNSPVCV----PSRTSMLTGRYPHRTGVYGFEAAHPALDHGLP 93
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
 189-270 8.66e-04

SPAP is a subclass of alkaline phosphatase (AP); 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. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.


Pssm-ID: 293740 [Multi-domain]  Cd Length: 457  Bit Score: 41.75  E-value: 8.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 189 DLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVG----YLRESIARNHLTdrlnLIITSDHGmttvdkrAGDLVEF-- 262
Cdd:cd16016  208 DLLAVSFSATDYIGHAFGPNSVEMEDTYLRLDRDLArlldALDKKVGKGNYL----VFLTADHG-------AADNPEFlk 276


                 ....*....
gi 530788254 263 -HKFPNFTF 270
Cdd:cd16016  277 dHKIPAGRF 285
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 175-250 6.34e-03

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


Pssm-ID: 293748 [Multi-domain]  Cd Length: 274  Bit Score: 38.31  E-value: 6.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788254 175 NIDTVMAwftEEDLDLVTL-YFGEpDSTGHRYGPESPE----RREMVRQVDRTVGYLRESIARNHLTdrlnLIITSDHGM 249
Cdd:cd16024  135 HLDSELS---RDDWDVLILhYLGL-DHIGHLEGPKSPLmppkLKEMDDVIKRIYESLEEQSSNNPTL----LVVCGDHGM 206


                 .
gi 530788254 250 T 250
Cdd:cd16024  207 T 207
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 47-95 6.40e-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: 38.73  E-value: 6.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530788254  47 QDVDTPNLDAMARDGVKAR--YMTPafvtMTSPCHFTLVTGKYIENHGVVH 95
Cdd:cd16151   22 ESYKTPNIDALAAEGVRFNnaYAQP----LCTPSRVQLMTGKYNFRNYVVF 68
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 199-250 6.53e-03

GPI ethanolamine phosphate transferase 1; PIG-N; 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: 293744  Cd Length: 294  Bit Score: 38.34  E-value: 6.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530788254 199 DSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMT 250
Cdd:cd16020  168 DTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMT 219
 
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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