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Conserved domains on  [gi|108935978|sp|Q58D68|]
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RecName: Full=Glycerophosphocholine cholinephosphodiesterase ENPP6; Short=GPC-Cpde; AltName: Full=Choline-specific glycerophosphodiester phosphodiesterase; AltName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 6; Short=E-NPP 6; Short=NPP-6; Flags: Precursor

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 ...
24-397 1.72e-97

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: 292.95  E-value: 1.72e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978  24 RKLLVFLLDGFRSDYISDeaLESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPATNKSF 103
Cdd:cd16018    1 PPLIVISIDGFRWDYLDR--AGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 104 DigvNRDSLMPLWWNGSEPLWITLTKAKRKVYMYYWPGCEVEILGVRPTYClEYKNVPTDINFANAVSDALD----FFKS 179
Cdd:cd16018   79 S---DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPI-PLGGYWQPYNDSFPFEERVDtileWLDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 180 GQADLAAIYHERIDVEGHHFGPSSPQRRDALKAVDTVLKYMTEWIQERELQDDLNVIIFSDHGMTDIfwmdkvielnkyi 259
Cdd:cd16018  155 ERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV------------- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 260 slndlqqvkdrgpvvslwpapgkhseiynklrrvehmtvyekeaipsrfyykkgkfvspltlvadegwfitenrellpfw 339
Cdd:cd16018      --------------------------------------------------------------------------------
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 108935978 340 mnstgkregwqrGWHGYDNELRDMRGIFLAFGPDFKSNFRAAPIRSVDVYNVMCSVAG 397
Cdd:cd16018  222 ------------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
24-397 1.72e-97

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: 292.95  E-value: 1.72e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978  24 RKLLVFLLDGFRSDYISDeaLESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPATNKSF 103
Cdd:cd16018    1 PPLIVISIDGFRWDYLDR--AGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 104 DigvNRDSLMPLWWNGSEPLWITLTKAKRKVYMYYWPGCEVEILGVRPTYClEYKNVPTDINFANAVSDALD----FFKS 179
Cdd:cd16018   79 S---DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPI-PLGGYWQPYNDSFPFEERVDtileWLDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 180 GQADLAAIYHERIDVEGHHFGPSSPQRRDALKAVDTVLKYMTEWIQERELQDDLNVIIFSDHGMTDIfwmdkvielnkyi 259
Cdd:cd16018  155 ERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV------------- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 260 slndlqqvkdrgpvvslwpapgkhseiynklrrvehmtvyekeaipsrfyykkgkfvspltlvadegwfitenrellpfw 339
Cdd:cd16018      --------------------------------------------------------------------------------
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 108935978 340 mnstgkregwqrGWHGYDNELRDMRGIFLAFGPDFKSNFRAAPIRSVDVYNVMCSVAG 397
Cdd:cd16018  222 ------------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
26-357 8.04e-96

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: 291.63  E-value: 8.04e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978   26 LLVFLLDGFRSDYISDeaLESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPATNK--SF 103
Cdd:pfam01663   1 LLVISLDGFRADYLDR--FELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEylVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978  104 DIGvnrDSLMPLWWNGsEPLWITLTKAKRKVYMYYWPGCEVEI---LGVRPTYCLEYKN--VPTDINFANAVSDAL---- 174
Cdd:pfam01663  79 VIS---DPEDPRWWQG-EPIWDTAAKAGVRAAALFWPGSEVDYstyYGTPPRYLKDDYNnsVPFEDRVDTAVLQTWldlp 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978  175 -DFFKSGQADLAAIYHERIDVEGHHFGPSSPQRRDALKAVDTVLKYMTEWIQERELQDDLNVIIFSDHGMTDIFwMDKVI 253
Cdd:pfam01663 155 fADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVS-DDKVI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978  254 ELNKYISLNDLQQVKDRGPVVSLWP--------APGKHSEIYNKLRRV---------EHMTVYEKEAIPSRFYYkkGKFV 316
Cdd:pfam01663 234 FLNDYLREKGLLHLVDGGPVVAIYPkarelghvPPGEVEEVYAELKEKllglriqdgEHLAVYLKEEIPGRLHY--NPRI 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 108935978  317 SPLTLVADEGWFITENRELLPFWMnstgkregwQRGWHGYD 357
Cdd:pfam01663 312 PDLVLVADPGWYITGKDGGDKEAA---------IHGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
1-398 1.37e-67

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 219.62  E-value: 1.37e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978   1 MAMKFGALLLVLVLSLAQPASGRRKLLVFLLDGFRSDYISDEaleSLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMT 80
Cdd:COG1524    1 MKRGLSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLLERA---HAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978  81 GRHCEVHQMIGNYMWDPATNKSFDI--GVNRDSLMPLWWNGsEPLWITLTKAKRKVYMYYWPGCEVE--ILGVRPTYC-- 154
Cdd:COG1524   78 GLYPGEHGIVGNGWYDPELGRVVNSlsWVEDGFGSNSLLPV-PTIFERARAAGLTTAAVFWPSFEGSglIDAARPYPYdg 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 155 --LEYKNVPTDINFANAVSDALdffKSGQADLAAIYHERIDVEGHHFGPSSPQRRDALKAVDTVLKYMTEWIQERELQDD 232
Cdd:COG1524  157 rkPLLGNPAADRWIAAAALELL---REGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 233 LNVIIFSDHGMTDIfwmDKVIELNKyISLNDLQQVKDrGPVVSLWPAPGKHSEIYNKLRrvEHMTVYEKEAIpsrfyyKK 312
Cdd:COG1524  234 TLVIVTADHGMVDV---PPDIDLNR-LRLAGLLAVRA-GESAHLYLKDGADAEVRALLG--LPARVLTREEL------AA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 313 GKFVSP----LTLVADEGWFITENrellpfwmnstgkregwQRGWHGYDNElRDMRGIFLAFGPDFKSNFRAapirsVDV 388
Cdd:COG1524  301 GHFGPHrigdLVLVAKPGWALDAP-----------------LKGSHGGLPD-EEMRVPLLASGPGFRPGVRN-----VDV 357
                        410
                 ....*....|
gi 108935978 389 YNVMCSVAGI 398
Cdd:COG1524  358 APTIARLLGL 367
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
24-397 1.72e-97

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: 292.95  E-value: 1.72e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978  24 RKLLVFLLDGFRSDYISDeaLESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPATNKSF 103
Cdd:cd16018    1 PPLIVISIDGFRWDYLDR--AGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 104 DigvNRDSLMPLWWNGSEPLWITLTKAKRKVYMYYWPGCEVEILGVRPTYClEYKNVPTDINFANAVSDALD----FFKS 179
Cdd:cd16018   79 S---DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPI-PLGGYWQPYNDSFPFEERVDtileWLDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 180 GQADLAAIYHERIDVEGHHFGPSSPQRRDALKAVDTVLKYMTEWIQERELQDDLNVIIFSDHGMTDIfwmdkvielnkyi 259
Cdd:cd16018  155 ERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV------------- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 260 slndlqqvkdrgpvvslwpapgkhseiynklrrvehmtvyekeaipsrfyykkgkfvspltlvadegwfitenrellpfw 339
Cdd:cd16018      --------------------------------------------------------------------------------
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 108935978 340 mnstgkregwqrGWHGYDNELRDMRGIFLAFGPDFKSNFRAAPIRSVDVYNVMCSVAG 397
Cdd:cd16018  222 ------------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
26-357 8.04e-96

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: 291.63  E-value: 8.04e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978   26 LLVFLLDGFRSDYISDeaLESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPATNK--SF 103
Cdd:pfam01663   1 LLVISLDGFRADYLDR--FELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEylVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978  104 DIGvnrDSLMPLWWNGsEPLWITLTKAKRKVYMYYWPGCEVEI---LGVRPTYCLEYKN--VPTDINFANAVSDAL---- 174
Cdd:pfam01663  79 VIS---DPEDPRWWQG-EPIWDTAAKAGVRAAALFWPGSEVDYstyYGTPPRYLKDDYNnsVPFEDRVDTAVLQTWldlp 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978  175 -DFFKSGQADLAAIYHERIDVEGHHFGPSSPQRRDALKAVDTVLKYMTEWIQERELQDDLNVIIFSDHGMTDIFwMDKVI 253
Cdd:pfam01663 155 fADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVS-DDKVI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978  254 ELNKYISLNDLQQVKDRGPVVSLWP--------APGKHSEIYNKLRRV---------EHMTVYEKEAIPSRFYYkkGKFV 316
Cdd:pfam01663 234 FLNDYLREKGLLHLVDGGPVVAIYPkarelghvPPGEVEEVYAELKEKllglriqdgEHLAVYLKEEIPGRLHY--NPRI 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 108935978  317 SPLTLVADEGWFITENRELLPFWMnstgkregwQRGWHGYD 357
Cdd:pfam01663 312 PDLVLVADPGWYITGKDGGDKEAA---------IHGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
1-398 1.37e-67

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 219.62  E-value: 1.37e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978   1 MAMKFGALLLVLVLSLAQPASGRRKLLVFLLDGFRSDYISDEaleSLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMT 80
Cdd:COG1524    1 MKRGLSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLLERA---HAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978  81 GRHCEVHQMIGNYMWDPATNKSFDI--GVNRDSLMPLWWNGsEPLWITLTKAKRKVYMYYWPGCEVE--ILGVRPTYC-- 154
Cdd:COG1524   78 GLYPGEHGIVGNGWYDPELGRVVNSlsWVEDGFGSNSLLPV-PTIFERARAAGLTTAAVFWPSFEGSglIDAARPYPYdg 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 155 --LEYKNVPTDINFANAVSDALdffKSGQADLAAIYHERIDVEGHHFGPSSPQRRDALKAVDTVLKYMTEWIQERELQDD 232
Cdd:COG1524  157 rkPLLGNPAADRWIAAAALELL---REGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 233 LNVIIFSDHGMTDIfwmDKVIELNKyISLNDLQQVKDrGPVVSLWPAPGKHSEIYNKLRrvEHMTVYEKEAIpsrfyyKK 312
Cdd:COG1524  234 TLVIVTADHGMVDV---PPDIDLNR-LRLAGLLAVRA-GESAHLYLKDGADAEVRALLG--LPARVLTREEL------AA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 313 GKFVSP----LTLVADEGWFITENrellpfwmnstgkregwQRGWHGYDNElRDMRGIFLAFGPDFKSNFRAapirsVDV 388
Cdd:COG1524  301 GHFGPHrigdLVLVAKPGWALDAP-----------------LKGSHGGLPD-EEMRVPLLASGPGFRPGVRN-----VDV 357
                        410
                 ....*....|
gi 108935978 389 YNVMCSVAGI 398
Cdd:COG1524  358 APTIARLLGL 367
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
26-247 9.99e-14

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: 70.53  E-value: 9.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978  26 LLVFLLDGFRSDYISD--EALESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPATNKSF 103
Cdd:cd00016    3 VVLIVLDGLGADDLGKagNPAPTTPNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELPSRA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108935978 104 DIgvnrdslmplWWNGSEPLWITLTKAKRKVYMYYwpgceveilgvrptycleyknvptdinfanaVSDALDFFKSGQAD 183
Cdd:cd00016   83 AG----------KDEDGPTIPELLKQAGYRTGVIG-------------------------------LLKAIDETSKEKPF 121
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 108935978 184 LAAIYHERIDVEGHHFGPSSPQRRDALKAVDTVL-KYMtEWIQERELQDDLNVIIFSDHGMTDIF 247
Cdd:cd00016  122 VLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIgKVL-DALKKAGDADDTVIIVTADHGGIDKG 185
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
196-245 5.98e-07

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: 50.64  E-value: 5.98e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 108935978 196 GHHFGPSSPQRRDALKAVDTVLKYMTEWIQERELqddlnVIIFSDHGMTD 245
Cdd:cd16023  174 GHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTL-----LLVFGDHGMTE 218
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
196-245 1.34e-04

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: 43.32  E-value: 1.34e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 108935978 196 GHHFGPSSPQRRDALKAVDTVLKYMTEWIQERELQDDLNVIIFSDHGMTD 245
Cdd:cd16024  159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQSSNNPTLLVVCGDHGMTD 208
 
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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