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Conserved domains on  [gi|23503267|ref|NP_699174|]
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glycerophosphocholine cholinephosphodiesterase ENPP6 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 ...
24-397 4.64e-100

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: 299.50  E-value: 4.64e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267  24 RKLLVFLLDGFRSDYISDeaLESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPTTNKSF 103
Cdd:cd16018   1 PPLIVISIDGFRWDYLDR--AGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 104 DigvNKDSLMPLWWNGSEPLWVTLTKAKRKVYMYYWPGCEVEILGVRPTYClEYKNVPTDINFANAVSDALDS----FKS 179
Cdd:cd16018  79 S---DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPI-PLGGYWQPYNDSFPFEERVDTilewLDL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 180 GRADLAAIYHERIDVEGHHYGPASPQRKDALKAVDTVLKYMTKWIQERGLQDRLNVIIFSDHGMTDIfwmdkvielnkyi 259
Cdd:cd16018 155 ERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV------------- 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 260 slndlqqvkdrgpvvslwpapgkhseiynklstvehmtvyekeaipsrfyykkgkfvspltlvadegwfitenremlpfw 339
Cdd:cd16018     --------------------------------------------------------------------------------
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23503267 340 mnstgrregwqrGWHGYDNELMDMRGIFLAFGPDFKSNFRAAPIRSVDVYNVMCNVVG 397
Cdd:cd16018 222 ------------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
24-397 4.64e-100

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: 299.50  E-value: 4.64e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267  24 RKLLVFLLDGFRSDYISDeaLESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPTTNKSF 103
Cdd:cd16018   1 PPLIVISIDGFRWDYLDR--AGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 104 DigvNKDSLMPLWWNGSEPLWVTLTKAKRKVYMYYWPGCEVEILGVRPTYClEYKNVPTDINFANAVSDALDS----FKS 179
Cdd:cd16018  79 S---DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPI-PLGGYWQPYNDSFPFEERVDTilewLDL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 180 GRADLAAIYHERIDVEGHHYGPASPQRKDALKAVDTVLKYMTKWIQERGLQDRLNVIIFSDHGMTDIfwmdkvielnkyi 259
Cdd:cd16018 155 ERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV------------- 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 260 slndlqqvkdrgpvvslwpapgkhseiynklstvehmtvyekeaipsrfyykkgkfvspltlvadegwfitenremlpfw 339
Cdd:cd16018     --------------------------------------------------------------------------------
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23503267 340 mnstgrregwqrGWHGYDNELMDMRGIFLAFGPDFKSNFRAAPIRSVDVYNVMCNVVG 397
Cdd:cd16018 222 ------------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
26-357 1.46e-95

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: 290.86  E-value: 1.46e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267    26 LLVFLLDGFRSDYISDeaLESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPTTNK--SF 103
Cdd:pfam01663   1 LLVISLDGFRADYLDR--FELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEylVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267   104 DIGvnkDSLMPLWWNGsEPLWVTLTKAKRKVYMYYWPGCEVEI---LGVRPTYCLEYKN--VPTDINFANAVSDAL--DS 176
Cdd:pfam01663  79 VIS---DPEDPRWWQG-EPIWDTAAKAGVRAAALFWPGSEVDYstyYGTPPRYLKDDYNnsVPFEDRVDTAVLQTWldLP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267   177 FK---SGRADLAAIYHERIDVEGHHYGPASPQRKDALKAVDTVLKYMTKWIQERGLQDRLNVIIFSDHGMTDIFwMDKVI 253
Cdd:pfam01663 155 FAdvaAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVS-DDKVI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267   254 ELNKYISLNDLQQVKDRGPVVSLWP--------APGKHSEIYNKLS---------TVEHMTVYEKEAIPSRFYYkkGKFV 316
Cdd:pfam01663 234 FLNDYLREKGLLHLVDGGPVVAIYPkarelghvPPGEVEEVYAELKekllglriqDGEHLAVYLKEEIPGRLHY--NPRI 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 23503267   317 SPLTLVADEGWFITENREMLPFWMnstgrregwQRGWHGYD 357
Cdd:pfam01663 312 PDLVLVADPGWYITGKDGGDKEAA---------IHGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
18-398 4.77e-67

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 218.46  E-value: 4.77e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267  18 QPASARRKLLVFLLDGFRSDYISDEaleSLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDP 97
Cdd:COG1524  18 AAAPPAKKVVLILVDGLRADLLERA---HAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDP 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267  98 TTNKSFDI--GVNKDSLMPLWWNGsEPLWVTLTKAKRKVYMYYWPGCEVE--ILGVRPTYC----LEYKNVPTDINFANA 169
Cdd:COG1524  95 ELGRVVNSlsWVEDGFGSNSLLPV-PTIFERARAAGLTTAAVFWPSFEGSglIDAARPYPYdgrkPLLGNPAADRWIAAA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 170 VSDALdsfKSGRADLAAIYHERIDVEGHHYGPASPQRKDALKAVDTVLKYMTKWIQERGLQDRLNVIIFSDHGMTDIfwm 249
Cdd:COG1524 174 ALELL---REGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDV--- 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 250 DKVIELNKyISLNDLQQVKDrGPVVSLWPAPGKHSEIYNKLStvEHMTVYEKEAIpsrfyyKKGKFVSP----LTLVADE 325
Cdd:COG1524 248 PPDIDLNR-LRLAGLLAVRA-GESAHLYLKDGADAEVRALLG--LPARVLTREEL------AAGHFGPHrigdLVLVAKP 317
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23503267 326 GWfiTENREMlpfwmnstgrregwqRGWHGYDNELmDMRGIFLAFGPDFKSNFRAapirsVDVYNVMCNVVGI 398
Cdd:COG1524 318 GW--ALDAPL---------------KGSHGGLPDE-EMRVPLLASGPGFRPGVRN-----VDVAPTIARLLGL 367
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
24-397 4.64e-100

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: 299.50  E-value: 4.64e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267  24 RKLLVFLLDGFRSDYISDeaLESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPTTNKSF 103
Cdd:cd16018   1 PPLIVISIDGFRWDYLDR--AGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 104 DigvNKDSLMPLWWNGSEPLWVTLTKAKRKVYMYYWPGCEVEILGVRPTYClEYKNVPTDINFANAVSDALDS----FKS 179
Cdd:cd16018  79 S---DSDWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPI-PLGGYWQPYNDSFPFEERVDTilewLDL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 180 GRADLAAIYHERIDVEGHHYGPASPQRKDALKAVDTVLKYMTKWIQERGLQDRLNVIIFSDHGMTDIfwmdkvielnkyi 259
Cdd:cd16018 155 ERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV------------- 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 260 slndlqqvkdrgpvvslwpapgkhseiynklstvehmtvyekeaipsrfyykkgkfvspltlvadegwfitenremlpfw 339
Cdd:cd16018     --------------------------------------------------------------------------------
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23503267 340 mnstgrregwqrGWHGYDNELMDMRGIFLAFGPDFKSNFRAAPIRSVDVYNVMCNVVG 397
Cdd:cd16018 222 ------------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
26-357 1.46e-95

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: 290.86  E-value: 1.46e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267    26 LLVFLLDGFRSDYISDeaLESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPTTNK--SF 103
Cdd:pfam01663   1 LLVISLDGFRADYLDR--FELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEylVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267   104 DIGvnkDSLMPLWWNGsEPLWVTLTKAKRKVYMYYWPGCEVEI---LGVRPTYCLEYKN--VPTDINFANAVSDAL--DS 176
Cdd:pfam01663  79 VIS---DPEDPRWWQG-EPIWDTAAKAGVRAAALFWPGSEVDYstyYGTPPRYLKDDYNnsVPFEDRVDTAVLQTWldLP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267   177 FK---SGRADLAAIYHERIDVEGHHYGPASPQRKDALKAVDTVLKYMTKWIQERGLQDRLNVIIFSDHGMTDIFwMDKVI 253
Cdd:pfam01663 155 FAdvaAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVS-DDKVI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267   254 ELNKYISLNDLQQVKDRGPVVSLWP--------APGKHSEIYNKLS---------TVEHMTVYEKEAIPSRFYYkkGKFV 316
Cdd:pfam01663 234 FLNDYLREKGLLHLVDGGPVVAIYPkarelghvPPGEVEEVYAELKekllglriqDGEHLAVYLKEEIPGRLHY--NPRI 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 23503267   317 SPLTLVADEGWFITENREMLPFWMnstgrregwQRGWHGYD 357
Cdd:pfam01663 312 PDLVLVADPGWYITGKDGGDKEAA---------IHGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
18-398 4.77e-67

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 218.46  E-value: 4.77e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267  18 QPASARRKLLVFLLDGFRSDYISDEaleSLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDP 97
Cdd:COG1524  18 AAAPPAKKVVLILVDGLRADLLERA---HAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDP 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267  98 TTNKSFDI--GVNKDSLMPLWWNGsEPLWVTLTKAKRKVYMYYWPGCEVE--ILGVRPTYC----LEYKNVPTDINFANA 169
Cdd:COG1524  95 ELGRVVNSlsWVEDGFGSNSLLPV-PTIFERARAAGLTTAAVFWPSFEGSglIDAARPYPYdgrkPLLGNPAADRWIAAA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 170 VSDALdsfKSGRADLAAIYHERIDVEGHHYGPASPQRKDALKAVDTVLKYMTKWIQERGLQDRLNVIIFSDHGMTDIfwm 249
Cdd:COG1524 174 ALELL---REGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDV--- 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 250 DKVIELNKyISLNDLQQVKDrGPVVSLWPAPGKHSEIYNKLStvEHMTVYEKEAIpsrfyyKKGKFVSP----LTLVADE 325
Cdd:COG1524 248 PPDIDLNR-LRLAGLLAVRA-GESAHLYLKDGADAEVRALLG--LPARVLTREEL------AAGHFGPHrigdLVLVAKP 317
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23503267 326 GWfiTENREMlpfwmnstgrregwqRGWHGYDNELmDMRGIFLAFGPDFKSNFRAapirsVDVYNVMCNVVGI 398
Cdd:COG1524 318 GW--ALDAPL---------------KGSHGGLPDE-EMRVPLLASGPGFRPGVRN-----VDVAPTIARLLGL 367
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
26-247 4.77e-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: 71.30  E-value: 4.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267  26 LLVFLLDGFRSDYISD--EALESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPTTNKSF 103
Cdd:cd00016   3 VVLIVLDGLGADDLGKagNPAPTTPNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELPSRA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503267 104 DIgvnkdslmplWWNGSEPLWVTLTKAKRKVYMYYwpgceveilgvrptycleyknvptdinfanaVSDALDSFKSGRAD 183
Cdd:cd00016  83 AG----------KDEDGPTIPELLKQAGYRTGVIG-------------------------------LLKAIDETSKEKPF 121
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23503267 184 LAAIYHERIDVEGHHYGPASPQRKDALKAVDTVL-KYMTKwIQERGLQDRLNVIIFSDHGMTDIF 247
Cdd:cd00016 122 VLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIgKVLDA-LKKAGDADDTVIIVTADHGGIDKG 185
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
196-245 2.78e-06

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: 48.71  E-value: 2.78e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 23503267 196 GHHYGPASPQRKDALKAVDTVLKYMTKWIQERGLqdrlnVIIFSDHGMTD 245
Cdd:cd16023 174 GHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTL-----LLVFGDHGMTE 218
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
196-245 3.62e-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: 42.17  E-value: 3.62e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 23503267 196 GHHYGPASPQRKDALKAVDTVLKYMTKWIQERGLQDRLNVIIFSDHGMTD 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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