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Conserved domains on  [gi|17556807|ref|NP_498106|]
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GP-PDE domain-containing protein [Caenorhabditis elegans]

Protein Classification

glycerophosphodiester phosphodiesterase family protein( domain architecture ID 10171153)

glycerophosphodiester phosphodiesterase (GDPD) family protein similar to Homo sapiens glycerophosphodiester phosphodiesterase 1 (GDE1) that hydrolyzes the phosphodiester bond of glycerophosphodiesters such as glycerophosphoinositol (GroPIns) and glycerophosphoethanolamine (GroPEth), to yield a glycerol phosphate and an alcohol

EC:  3.1.4.-
Gene Ontology:  GO:0008081|GO:0006629

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 120-370 3.59e-109

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE1 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE1 (also known as MIR16, membrane interacting protein of RGS16) and their metazoan homologs. GDE1 is widely expressed in mammalian tissues, including the heart, brain, liver, and kidney. It shows sequence homology to bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. GDE1 has been characterized as GPI-GDE (EC 3.1.4.44) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate glycerol phosphate and inositol. It functions as an integral membrane-bound glycoprotein interacting with regulator of G protein signaling protein RGS16, and is modulated by G protein-coupled receptor (GPCR) signaling. In addition, GDE1 may interact with PRA1 domain family, member 2 (PRAF2, also known as JM4), which is an interacting protein of the G protein-coupled chemokine receptor CCR5. The catalytic activity, which is dependent on the integrity of the GDPD domain, is required for GDE1 cellular function.


:

Pssm-ID: 176515 [Multi-domain]  Cd Length: 258  Bit Score: 319.97  E-value: 3.59e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 120 IGGHRGSAHDdIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLRFTGTNIS 199
Cdd:cd08573   1 IIGHRGAGHD-APENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 200 --------LPTFEEAVSYCVANDIMMIWDVKNVDENLLKQFVIQMKTHN-LYSKVLVSGFNPIDTYKVKMADPKILTGFT 270
Cdd:cd08573  80 ssrfpgekIPTLEEAVKECLENNLRMIFDVKSNSSKLVDALKNLFKKYPgLYDKAIVCSFNPIVIYKVRKADPKILTGLT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 271 WRNWELSTTDEAARIPRFTGALNAIASVLDVLV-FGLARSLimPKFLGSDVIFYHVNDISSFLKTDAAANNIYLAGWTSN 349
Cdd:cd08573 160 WRPWFLSYTDDEGGPRRKSGWKHFLYSMLDVILeWSLHSWL--PYFLGVSALLIHKDDISSAYVRYWRARGIRVIAWTVN 237

                       250       260
                ....*....|....*....|.
gi 17556807 350 NPTEQVWLRDYLNVPFLTDNV 370
Cdd:cd08573 238 TPTEKQYFAKTLNVPYITDSL 258
 
Name Accession Description Interval E-value
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 120-370 3.59e-109

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE1 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE1 (also known as MIR16, membrane interacting protein of RGS16) and their metazoan homologs. GDE1 is widely expressed in mammalian tissues, including the heart, brain, liver, and kidney. It shows sequence homology to bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. GDE1 has been characterized as GPI-GDE (EC 3.1.4.44) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate glycerol phosphate and inositol. It functions as an integral membrane-bound glycoprotein interacting with regulator of G protein signaling protein RGS16, and is modulated by G protein-coupled receptor (GPCR) signaling. In addition, GDE1 may interact with PRA1 domain family, member 2 (PRAF2, also known as JM4), which is an interacting protein of the G protein-coupled chemokine receptor CCR5. The catalytic activity, which is dependent on the integrity of the GDPD domain, is required for GDE1 cellular function.


Pssm-ID: 176515 [Multi-domain]  Cd Length: 258  Bit Score: 319.97  E-value: 3.59e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 120 IGGHRGSAHDdIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLRFTGTNIS 199
Cdd:cd08573   1 IIGHRGAGHD-APENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 200 --------LPTFEEAVSYCVANDIMMIWDVKNVDENLLKQFVIQMKTHN-LYSKVLVSGFNPIDTYKVKMADPKILTGFT 270
Cdd:cd08573  80 ssrfpgekIPTLEEAVKECLENNLRMIFDVKSNSSKLVDALKNLFKKYPgLYDKAIVCSFNPIVIYKVRKADPKILTGLT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 271 WRNWELSTTDEAARIPRFTGALNAIASVLDVLV-FGLARSLimPKFLGSDVIFYHVNDISSFLKTDAAANNIYLAGWTSN 349
Cdd:cd08573 160 WRPWFLSYTDDEGGPRRKSGWKHFLYSMLDVILeWSLHSWL--PYFLGVSALLIHKDDISSAYVRYWRARGIRVIAWTVN 237

                       250       260
                ....*....|....*....|.
gi 17556807 350 NPTEQVWLRDYLNVPFLTDNV 370
Cdd:cd08573 238 TPTEKQYFAKTLNVPYITDSL 258
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 123-372 1.56e-50

Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes of glycerophosphoryl diester phosphodiesterase (GDPD) - periplasmic and cytosolic. This family also includes agrocinopine synthase, the similarity to GDPD has been noted. This family appears to have weak but not significant matches to mammalian phospholipase C pfam00388, which suggests that this family may adopt a TIM barrel fold.


Pssm-ID: 397241 [Multi-domain]  Cd Length: 244  Bit Score: 169.50  E-value: 1.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807   123 HRGSAHDdIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLRfTGTNISLPT 202
Cdd:pfam03009   1 HRGASGS-YPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLD-IGAGNSGPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807   203 FEEAVSY-CVANDIMMIWDVKNVDENLLKQFVIQMKTHN-LYSKVLVSGFNPIDTYKvkmADPKILTGFTWRNWELSTTD 280
Cdd:pfam03009  79 SGERVPFpTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEEgLIVKDLLLSVDEILAKK---ADPRRVIFSSFNPDELKRLR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807   281 EAARIPRFTGALNAIASVLDVLVFGLARSLIMPKFLGSDVIFYHVndISSFLKtDAAANNIYLAGWTSNNPTEQVWLRDY 360
Cdd:pfam03009 156 ELAPKLPLVFLSSGRAYAEADLLERAAAFAGAPALLGEVALVDEA--LPDLVK-RAHARGLVVHVWTVNNEDEMKRLLEL 232

                         250
                  ....*....|..
gi 17556807   361 LNVPFLTDNVGT 372
Cdd:pfam03009 233 GVDGVITDRPDT 244
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
122-360 5.94e-28

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 109.57  E-value: 5.94e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 122 GHRGsAHDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLR------FTG 195
Cdd:COG0584   7 AHRG-ASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDagsgpdFAG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 196 TNIslPTFEEAVSYCvANDIMMIWDVKN---VDENLLKQFVIQMKTHNLYSKVLVSGFNPIDTYKVKMADPKILTGFTWR 272
Cdd:COG0584  86 ERI--PTLEEVLELV-PGDVGLNIEIKSppaAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLVE 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 273 NWELSTTDEAARiprftgalnaiasvldvlvfglarslimpkfLGSDVIFYHVNDISSFLKTDAAANNIYLAGWTSNNPT 352
Cdd:COG0584 163 ELPADPLELARA-------------------------------LGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPE 211


                ....*...
gi 17556807 353 EQVWLRDY 360
Cdd:COG0584 212 EMRRLLDL 219
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 123-216 6.33e-07

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 49.94  E-value: 6.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807  123 HRGSAHDdIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVT---GVDKDistMNITEFRKL-------- 191
Cdd:PRK09454  13 HRGGGKL-APENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSngwGVAGE---LTWQDLAQLdagswfsa 88

                         90       100
                 ....*....|....*....|....*
gi 17556807  192 RFTGTniSLPTFEEAVSYCVANDIM 216
Cdd:PRK09454  89 AFAGE--PLPTLSQVAARCRAHGMA 111
 
Name Accession Description Interval E-value
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 120-370 3.59e-109

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE1 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE1 (also known as MIR16, membrane interacting protein of RGS16) and their metazoan homologs. GDE1 is widely expressed in mammalian tissues, including the heart, brain, liver, and kidney. It shows sequence homology to bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. GDE1 has been characterized as GPI-GDE (EC 3.1.4.44) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate glycerol phosphate and inositol. It functions as an integral membrane-bound glycoprotein interacting with regulator of G protein signaling protein RGS16, and is modulated by G protein-coupled receptor (GPCR) signaling. In addition, GDE1 may interact with PRA1 domain family, member 2 (PRAF2, also known as JM4), which is an interacting protein of the G protein-coupled chemokine receptor CCR5. The catalytic activity, which is dependent on the integrity of the GDPD domain, is required for GDE1 cellular function.


Pssm-ID: 176515 [Multi-domain]  Cd Length: 258  Bit Score: 319.97  E-value: 3.59e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 120 IGGHRGSAHDdIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLRFTGTNIS 199
Cdd:cd08573   1 IIGHRGAGHD-APENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 200 --------LPTFEEAVSYCVANDIMMIWDVKNVDENLLKQFVIQMKTHN-LYSKVLVSGFNPIDTYKVKMADPKILTGFT 270
Cdd:cd08573  80 ssrfpgekIPTLEEAVKECLENNLRMIFDVKSNSSKLVDALKNLFKKYPgLYDKAIVCSFNPIVIYKVRKADPKILTGLT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 271 WRNWELSTTDEAARIPRFTGALNAIASVLDVLV-FGLARSLimPKFLGSDVIFYHVNDISSFLKTDAAANNIYLAGWTSN 349
Cdd:cd08573 160 WRPWFLSYTDDEGGPRRKSGWKHFLYSMLDVILeWSLHSWL--PYFLGVSALLIHKDDISSAYVRYWRARGIRVIAWTVN 237

                       250       260
                ....*....|....*....|.
gi 17556807 350 NPTEQVWLRDYLNVPFLTDNV 370
Cdd:cd08573 238 TPTEKQYFAKTLNVPYITDSL 258
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 123-372 1.56e-50

Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes of glycerophosphoryl diester phosphodiesterase (GDPD) - periplasmic and cytosolic. This family also includes agrocinopine synthase, the similarity to GDPD has been noted. This family appears to have weak but not significant matches to mammalian phospholipase C pfam00388, which suggests that this family may adopt a TIM barrel fold.


Pssm-ID: 397241 [Multi-domain]  Cd Length: 244  Bit Score: 169.50  E-value: 1.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807   123 HRGSAHDdIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLRfTGTNISLPT 202
Cdd:pfam03009   1 HRGASGS-YPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLD-IGAGNSGPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807   203 FEEAVSY-CVANDIMMIWDVKNVDENLLKQFVIQMKTHN-LYSKVLVSGFNPIDTYKvkmADPKILTGFTWRNWELSTTD 280
Cdd:pfam03009  79 SGERVPFpTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEEgLIVKDLLLSVDEILAKK---ADPRRVIFSSFNPDELKRLR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807   281 EAARIPRFTGALNAIASVLDVLVFGLARSLIMPKFLGSDVIFYHVndISSFLKtDAAANNIYLAGWTSNNPTEQVWLRDY 360
Cdd:pfam03009 156 ELAPKLPLVFLSSGRAYAEADLLERAAAFAGAPALLGEVALVDEA--LPDLVK-RAHARGLVVHVWTVNNEDEMKRLLEL 232

                         250
                  ....*....|..
gi 17556807   361 LNVPFLTDNVGT 372
Cdd:pfam03009 233 GVDGVITDRPDT 244
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
122-360 5.94e-28

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 109.57  E-value: 5.94e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 122 GHRGsAHDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLR------FTG 195
Cdd:COG0584   7 AHRG-ASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDagsgpdFAG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 196 TNIslPTFEEAVSYCvANDIMMIWDVKN---VDENLLKQFVIQMKTHNLYSKVLVSGFNPIDTYKVKMADPKILTGFTWR 272
Cdd:COG0584  86 ERI--PTLEEVLELV-PGDVGLNIEIKSppaAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLVE 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 273 NWELSTTDEAARiprftgalnaiasvldvlvfglarslimpkfLGSDVIFYHVNDISSFLKTDAAANNIYLAGWTSNNPT 352
Cdd:COG0584 163 ELPADPLELARA-------------------------------LGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPE 211


                ....*...
gi 17556807 353 EQVWLRDY 360
Cdd:COG0584 212 EMRRLLDL 219
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 120-266 4.28e-23

Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (AtGDE, EC 3.1.4.46) and its uncharacterized eukaryotic homolgoues. Members in this family shows high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. AtGDE exists as a hexamer that is a trimer of dimers, which is unique among current known GDPD family members. However, it remains unclear if the hexamer plays a physiological role in AtGDE enzymatic function.


Pssm-ID: 176509 [Multi-domain]  Cd Length: 240  Bit Score: 96.60  E-value: 4.28e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 120 IGGHRGSAHDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLRF-----T 194
Cdd:cd08566   2 VVAHRGGWGAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLkdgdgE 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17556807 195 GTNISLPTFEEAVSYCvANDIMMIWDVKNVDenlLKQFVIQMKTHNLYSKVLVSGFNPIDTYKVKMADPKIL 266
Cdd:cd08566  82 VTDEKVPTLEEALAWA-KGKILLNLDLKDAD---LDEVIALVKKHGALDQVIFKSYSEEQAKELRALAPEVM 149
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 123-354 2.63e-22

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity with Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176527 [Multi-domain]  Cd Length: 237  Bit Score: 94.31  E-value: 2.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 123 HRG--SAHDDIPENSLEAFSAVKrEGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLRFTGTNISL 200
Cdd:cd08585   9 HRGlhDRDAGIPENSLSAFRAAA-EAGYGIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRLLGTDEHI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 201 PTFEEAVSYcVANDIMMIWDVKNVDENL--LKQFVIQM-KTHNlySKVLVSGFNPIDTYKVKMADPKILTGFTWRNWELS 277
Cdd:cd08585  88 PTLDEVLEL-VAGRVPLLIELKSCGGGDggLERRVLAAlKDYK--GPAAIMSFDPRVVRWFRKLAPGIPRGQLSEGSNDE 164

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17556807 278 TTDEAARIPRFTGALNAIASvldvlvfglarslimpkflGSDVIFYHVNDI-SSFLKTDAAANNIYLAGWTSNNPTEQ 354
Cdd:cd08585 165 ADPAFWNEALLSALFSNLLT-------------------RPDFIAYHLDDLpNPFVTLARALLGMPVIVWTVRTEEDI 223
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 119-286 3.90e-21

Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermoanaerobacter tengcongensis glycerophosphodiester phosphodiesterase (TtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Despite the fact that most of GDPD family members exist as the monomer, TtGDE can function as a dimeric unit. Its catalytic mechanism is based on the general base-acid catalysis, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). A divalent metal cation is required for the enzyme activity of TtGDE.


Pssm-ID: 176506 [Multi-domain]  Cd Length: 230  Bit Score: 90.69  E-value: 3.90e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 119 KIGGHRGSAhDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKL------- 191
Cdd:cd08563   2 LIFAHRGYS-GTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLdagswfd 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 192 -RFTGTNIslPTFEEAVSYCVANDIMMIWDVKN---VDENLLKQFVIQMKTHNLYSKVLVSGFNPIDTYKVKMADPKILT 267
Cdd:cd08563  81 eKFTGEKI--PTLEEVLDLLKDKDLLLNIEIKTdviHYPGIEKKVLELVKEYNLEDRVIFSSFNHESLKRLKKLDPKIKL 158

                       170
                ....*....|....*....
gi 17556807 268 GFTWRNWELSTTDEAARIP 286
Cdd:cd08563 159 ALLYETGLQDPKDYAKKIG 177
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 120-269 9.05e-21

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial glycerophosphodiester phosphodiesterases. In addition to a C-terminal GDPD domain, most members in this family have an N-terminus that functions as a membrane anchor.


Pssm-ID: 176521 [Multi-domain]  Cd Length: 220  Bit Score: 89.53  E-value: 9.05e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 120 IGGHRGSAhDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLR----FTG 195
Cdd:cd08579   1 IIAHRGVS-SNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTigenGHG 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17556807 196 TNIslPTFEEAVSYCVANDIMMIWDVK---NVDENLLKQFVIQMKTHNLYSKVLVSGFNPIDTYKVKMADPKILTGF 269
Cdd:cd08579  80 AKI--PSLDEYLALAKGLKQKLLIELKphgHDSPDLVEKFVKLYKQNLIENQHQVHSLDYRVIEKVKKLDPKIKTGY 154
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 123-291 1.02e-18

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity to Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176524 [Multi-domain]  Cd Length: 233  Bit Score: 84.29  E-value: 1.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 123 HRGSAHDdIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLRFTG------T 196
Cdd:cd08582   4 HRGASAE-APENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGSwkgesyK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 197 NISLPTFEEAVSYCVANDI-------MMIWDVKNVDE--NLLKQFviQMKTHNLyskVLVSgFNPIDTYKVKMADPKILT 267
Cdd:cd08582  83 GEKVPTLEEYLAIVPKYGKklfieikHPRRGPEAEEEllKLLKES--GLLPEQI---VIIS-FDAEALKRVRELAPTLET 156

                       170       180
                ....*....|....*....|....*
gi 17556807 268 GFTWRNW-ELSTTDEAARIPRFTGA 291
Cdd:cd08582 157 LWLRNYKsPKEDPRPLAKSGGAAGL 181
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 120-333 4.60e-16

Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and similar proteins; The typical glycerophosphodiester phosphodiesterase domain (GDPD) consists of a TIM barrel and a small insertion domain named the GDPD-insertion (GDPD-I) domain, which is specific for GDPD proteins. This family corresponds to both typical GDPD domain and GDPD-like domain which lacks the GDPD-I region. Members in this family mainly consist of a large family of prokaryotic and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), and a number of uncharacterized homologs. Sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria are also included in this family. GDPD plays an essential role in glycerol metabolism and catalyzes the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols are major sources of carbon and phosphate. Its catalytic mechanism is based on the metal ion-dependent acid-base reaction, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). Both, GDPD related proteins and PI-PLCs, belong to the superfamily of PI-PLC-like phosphodiesterases.


Pssm-ID: 176499 [Multi-domain]  Cd Length: 189  Bit Score: 75.76  E-value: 4.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 120 IGGHRGSAHDDiPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDantvrvtgvdkdistmnitefrklrftgtnis 199
Cdd:cd08556   1 IIAHRGASGEA-PENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD-------------------------------- 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 200 LPTFEEAVSYCVANDIMMIwDVK--NVDENLLKQFVIQMKTHNLYSKVLVSGFNPIDTYKVKMADPKILTGFTWRNWELS 277
Cdd:cd08556  48 IPTLEEVLELVKGGVGLNI-ELKepTRYPGLEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVPTGLLVDKPPLD 126

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17556807 278 TTDEAAriprftgALNAIASVLDVLVFGLARSLIMP-KFLGSDVIFYHVNDISSFLK 333
Cdd:cd08556 127 PLLAEL-------ARALGADAVNPHYKLLTPELVRAaHAAGLKVYVWTVNDPEDARR 176
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 122-271 4.79e-16

Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic glycerophosphodiester phosphodiesterase UgpQ and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Escherichia coli cytosolic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46), UgpQ, and similar proteins. GP-GDE plays an essential role in the metabolic pathway of E. coli. It catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. E. coli possesses two major G3P uptake systems: Glp and Ugp, which contain genes coding for two distinct GP-GDEs. UgpQ gene from the E. coli ugp operon codes for a cytosolic phosphodiesterase GlpQ, which is the prototype of this family. Various glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), can only be hydrolyzed by UgpQ during transport at the inner side of the cytoplasmic membrane to alcohols and G3P, which is a source of phosphate. In contrast to Ca2+-dependent periplasmic phosphodiesterase GlpQ, cytosolic phosphodiesterase UgpQ requires divalent cations, such as Mg2+, Co2+, or Mn2+, for its enzyme activity.


Pssm-ID: 176505 [Multi-domain]  Cd Length: 229  Bit Score: 76.49  E-value: 4.79e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 122 GHRGsAHDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKL--------RF 193
Cdd:cd08562   3 AHRG-ASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLdagswfspEF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 194 TGTNIslPTFEEAVSYCVANDIMMIWDVK--NVDENLLKQFVIQM-KTHNLY-SKVLVSGFNPIDTYKVKMADPKILTGF 269
Cdd:cd08562  82 AGEPI--PTLADVLELARELGLGLNLEIKpdPGDEALTARVVAAAlRELWPHaSKLLLSSFSLEALRAARRAAPELPLGL 159


                ..
gi 17556807 270 TW 271
Cdd:cd08562 160 LF 161
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 93-270 1.44e-15

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE4 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1)) and similar proteins. Mammalian GDE4 is a transmembrane protein whose cellular function has not yet been elucidated. It is expressed widely, including in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. It is also expressed in the growth cones in neuroblastoma Neuro2a cells, which suggests GDE4 may play some distinct role from other members of the GDE family.


Pssm-ID: 176553 [Multi-domain]  Cd Length: 300  Bit Score: 76.48  E-value: 1.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807  93 LMIAFFIFRIPQLTNEPhKSQFFSAWKIGgHRGSAHDDiPENSLEAFS-AVKrEGGQLAEMDIQITLDGVPVICHDANTV 171
Cdd:cd08612   4 IATSYFLLRNPTLLHKK-KKSPFPCRHIS-HRGGSGEN-LENTMEAFEhAVK-VGTDMLELDVHLTKDGQVVVSHDENLL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 172 RVTGVDKDISTMNITEF----RKLRFT----------GTNISLPTFEEaVSYCVANDIMMIwDVKNVDENLLKQFVIQMK 237
Cdd:cd08612  80 RSCGVDKLVSDLNYADLppylEKLEVTfspgdycvpkGSDRRIPLLEE-VFEAFPDTPINI-DIKVENDELIKKVSDLVR 157

                       170       180       190
                ....*....|....*....|....*....|...
gi 17556807 238 THNLYSKVLVSGFNPIDTYKVKMADPKILTGFT 270
Cdd:cd08612 158 KYKREDITVWGSFNDEIVKKCHKENPNIPLFFS 190
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 120-357 2.69e-15

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL206cp and uncharacterized hypothetical homologs existing in fungi. The product of S. cerevisiae ORF YPL206c (PGC1), YPL206cp (Pgc1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL206cp is an integral membrane protein with a single GDPD domain following by a short hydrophobic C-terminal tail that may function as a membrane anchor. This protein plays an essential role in the regulation of the cardiolipin (CL) biosynthetic pathway in yeast by removing the excess phosphatidylglycerol (PG) content of membranes via a phospholipase C-type degradation mechanism. YPL206cp has been characterized as a PG-specific phospholipase C that selectively catalyzes the cleavage of PG, not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate. Members in this family are distantly related to S. cerevisiae YPL110cp, which selectively hydrolyzes glycerophosphocholine (GPC), not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate, and has been characterized as a cytoplasmic GPC-specific phosphodiesterase.


Pssm-ID: 176512 [Multi-domain]  Cd Length: 234  Bit Score: 74.56  E-value: 2.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 120 IGGHRG-SAHddIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVD-KDISTMNITEFRKLRFT-GT 196
Cdd:cd08570   1 VIGHRGyKAK--YPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDgLIIDDSTWDELSHLRTIeEP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 197 NISLPTFEEAVSYCVANDIMMIW---DVKNVDENLLKQFVIQMkthnlyskvLVSGFNPIDTYKvkmadPKILTGFtwrn 273
Cdd:cd08570  79 HQPMPTLKDVLEWLVEHELPDVKlmlDIKRDNDPEILFKLIAE---------MLAVKPDLDFWR-----ERIILGL---- 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 274 WElsttdeaariPRFTGALNAIASVLDVLVFGL----ARSLIMPKFLGSDVIFYHVNDISSFLKT---DAAANNIYLAGW 346
Cdd:cd08570 141 WH----------LDFLKYGKEVLPGFPVFHIGFsldyARHFLNYSEKLVGISMHFVSLWGPFGQAflpELKKNGKKVFVW 210

                       250
                ....*....|.
gi 17556807 347 TSNNPTEQVWL 357
Cdd:cd08570 211 TVNTEEDMRYA 221
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 119-269 6.66e-15

Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermotoga maritime glycerophosphodiester phosphodiesterase (TmGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. TmGDE exists as a monomer that might be the biologically relevant form.


Pssm-ID: 176511 [Multi-domain]  Cd Length: 226  Bit Score: 73.10  E-value: 6.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 119 KIGGHRGSAhDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLRFTGTNI 198
Cdd:cd08568   1 IILGHRGYR-AKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHPGGELI 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17556807 199 slPTFEEAVSYCVANDIMMIwDVKNVD--ENLLKqfviQMKTHNLYSKVLVSGFNPIDTYKVKMADPKILTGF 269
Cdd:cd08568  80 --PTLEEVFRALPNDAIINV-EIKDIDavEPVLE----IVEKFNALDRVIFSSFNHDALRELRKLDPDAKVGL 145
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 122-251 2.40e-13

Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic phosphodiesterases UgpQ2 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized cytoplasmic phosphodiesterases which predominantly exist in bacteria. The prototype of this family is a putative cytoplasmic phosphodiesterase encoded by gene ulpQ2 (SCO1419) in the Streptomyces coelicolor genome. It is distantly related to the Escherichia coli cytoplasmic phosphodiesterases UgpQ that catalyzes the hydrolysis of glycerophosphodiesters at the inner side of the cytoplasmic membrane to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176504 [Multi-domain]  Cd Length: 249  Bit Score: 69.21  E-value: 2.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 122 GHRGSAHDDiPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLRFT------- 194
Cdd:cd08561   3 AHRGGAGLA-PENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGyhftddg 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17556807 195 -------GTNISLPTFEE---AVSycvanDIMMIWDVKNVDENLLKQFVIQMKTHNLYSKVLVSGFN 251
Cdd:cd08561  82 grtypyrGQGIRIPTLEElfeAFP-----DVRLNIEIKDDGPAAAAALADLIERYGAQDRVLVASFS 143
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 123-240 5.42e-13

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE4 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1)) and similar proteins. Mammalian GDE4 is a transmembrane protein whose cellular function is not elucidated. It is expressed widely, including in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. It is also expressed in the growth cones in neuroblastoma Neuro2a cells, which suggests mammalian GDE4 may play some distinct role from other members of mammalian GDEs family. Also included in this subfamily are uncharacterized mammalian glycerophosphodiester phosphodiesterase domain-containing protein 3 (GDPD3) and similar proteins which display very high sequence homology to mammalian GDE4.


Pssm-ID: 176517 [Multi-domain]  Cd Length: 264  Bit Score: 68.40  E-value: 5.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 123 HRGSAHDdIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLrftgtNISLP- 201
Cdd:cd08575   6 HRGGAAE-FPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPL-----DAGYGy 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 17556807 202 TFEEAVSYCVAND-IMMIWDVKNVdenlLKQF-----VIQMKTHN 240
Cdd:cd08575  80 TFDGGKTGYPRGGgDGRIPTLEEV----FKAFpdtpiNIDIKSPD 120
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 122-176 2.71e-11

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity to Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176523 [Multi-domain]  Cd Length: 229  Bit Score: 62.73  E-value: 2.71e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17556807 122 GHRGSAhDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGV 176
Cdd:cd08581   3 AHRGYP-ARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGV 56
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 120-205 2.62e-08

Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (pAtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176508 [Multi-domain]  Cd Length: 235  Bit Score: 53.95  E-value: 2.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 120 IGGHRGSAHDdIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKLRF-TGTNI 198
Cdd:cd08565   1 IAGHRGGRNL-WPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLrDSFGE 79


                ....*..
gi 17556807 199 SLPTFEE 205
Cdd:cd08565  80 KIPTLEE 86
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 122-205 3.01e-08

Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and similar proteins. The prototype of this CD is a putative GP-GDE from Silicibacter pomeroyi (SpGDE). It shows high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176510 [Multi-domain]  Cd Length: 263  Bit Score: 54.24  E-value: 3.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 122 GHRGsAHDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHD----------ANTVRVTGVDKDISTMNITEFRKL 191
Cdd:cd08567   5 GHRG-ARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDpklnpditrdPDGAWLPYEGPALYELTLAEIKQL 83

                        90       100       110
                ....*....|....*....|....*....|...
gi 17556807 192 R-------------------FTGTNIslPTFEE 205
Cdd:cd08567  84 DvgekrpgsdyaklfpeqipVPGTRI--PTLEE 114
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 122-218 7.16e-08

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins. GDE5 is widely expressed in mammalian tissues, with highest expression in spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176514 [Multi-domain]  Cd Length: 293  Bit Score: 53.44  E-value: 7.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 122 GHRGS-------AHDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDaNTVRVTGVDKDIST-----------M 183
Cdd:cd08572   4 GHRGLgknyasgSLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHD-FTISVSEKSKTGSDegelievpihdL 82

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 17556807 184 NITEFRKLRFTGTNISLPTFEE--AVSYCVANDIMMI 218
Cdd:cd08572  83 TLEQLKELGLQHISALKRKALTrkAKGPKPNPWGMDE 119
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 122-167 7.99e-08

Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester phosphodiesterase GDE5 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative mammalian GDE5 and similar proteins. Mammalian GDE5 is widely expressed in mammalian tissues, with highest expression in the spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. In addition to C-terminal GDPD domain, all members in this subfamily have a starch binding domain (CBM20) in the N-terminus, which suggests these proteins may play a distinct role in glycerol metabolism.


Pssm-ID: 176549 [Multi-domain]  Cd Length: 290  Bit Score: 53.07  E-value: 7.99e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 17556807 122 GHRGS------AHDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHD 167
Cdd:cd08607   4 GHRGAgnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHD 55
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 123-216 6.33e-07

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 49.94  E-value: 6.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807  123 HRGSAHDdIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVT---GVDKDistMNITEFRKL-------- 191
Cdd:PRK09454  13 HRGGGKL-APENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSngwGVAGE---LTWQDLAQLdagswfsa 88

                         90       100
                 ....*....|....*....|....*
gi 17556807  192 RFTGTniSLPTFEEAVSYCVANDIM 216
Cdd:PRK09454  89 AFAGE--PLPTLSQVAARCRAHGMA 111
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 122-191 6.90e-07

Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46) from Staphylococcus aureus, Bacillus subtilis and similar proteins. Members in this family show very high sequence similarity to Escherichia coli periplasmic phosphodiesterase GlpQ, which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176543 [Multi-domain]  Cd Length: 256  Bit Score: 50.01  E-value: 6.90e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17556807 122 GHRGsAHDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKD--ISTMNITEFRKL 191
Cdd:cd08601   5 AHRG-ASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIERPgpVKDYTLAEIKQL 75
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 122-195 7.94e-07

Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in bacterial and eukaryotic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ. GP-GDEs are involved in glycerol metabolism and catalyze the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. In E. coli, there are two major G3P uptake systems: Glp and Ugp, which contain genes coding for two different GP-GDEs. GlpQ gene from the glp operon codes for a periplasmic phosphodiesterase GlpQ. GlpQ is a dimeric enzyme that hydrolyzes periplasmic glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), to the corresponding alcohols and G3P, which is subsequently transported into the cell through the GlpT transport system. Ca2+ is required for GlpQ enzymatic activity. This subfamily also includes some GP-GDEs in higher plants and their eukaryotic homologs, which show very high sequence similarities with bacterial periplasmic GP-GDEs.


Pssm-ID: 176502 [Multi-domain]  Cd Length: 296  Bit Score: 49.96  E-value: 7.94e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17556807 122 GHRGSAHDdIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDkdistmNITEFRKLRFTG 195
Cdd:cd08559   5 AHRGASGY-APEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVA------EHFPFRGRKDTG 71
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 120-167 1.80e-06

Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester phosphodiesterase-like proteins similar to mammalian GDE5; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized plant glycerophosphodiester phosphodiesterase (GP-PDE)-like proteins. Members in this family show very high sequence homology to mammalian glycerophosphodiester phosphodiesterase GDE5 and are distantly related to plant GP-PDEs.


Pssm-ID: 176547 [Multi-domain]  Cd Length: 282  Bit Score: 48.95  E-value: 1.80e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17556807 120 IGGHRG-----SAHDD-----IPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHD 167
Cdd:cd08605   2 VIGHRGlgmnrASHQPsvgpgIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHD 59
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 122-188 2.10e-06

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL110cp and other uncharacterized fungal homologs. The product of S. cerevisiae ORF YPL110c (GDE1), YPL110cp (Gde1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL110cp has been characterized as a cytoplasmic glycerophosphocholine (GPC)-specific phosphodiesterase that selectively hydrolyzes GPC, not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate. YPL110cp has multi-domain architecture, including not only C-terminal GDPD, but also an SPX N-terminal domain along with several ankyrin repeats, which implies that YPL110cp may mediate protein-protein interactions in a variety of proteins and play a role in maintaining cellular phosphate levels. Members in this family are distantly related to S. cerevisiae YPL206cp, which selectively catalyzes the cleavage of phosphatidylglycerol (PG), not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate, and has been characterized as a PG-specific phospholipase C.


Pssm-ID: 176548 [Multi-domain]  Cd Length: 286  Bit Score: 48.98  E-value: 2.10e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17556807 122 GHRGSAHD-------DIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDAnTVRVTGVDKDISTMNITEF 188
Cdd:cd08606   6 GHRGLGKNtaerkslQLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDF-LVSETGTDVPIHDLTLEQF 78
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 123-205 7.26e-06

Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Escherichia coli periplasmic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46), GlpQ, and similar proteins. GP-GDE plays an essential role in the metabolic pathway of E. coli. It catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. E. coli possesses two major G3P uptake systems: Glp and Ugp, which contain genes coding for two different GP-GDEs. GlpQ gene from the E. coli glp operon codes for a periplasmic phosphodiesterase GlpQ, which is the prototype of this family. GlpQ is a dimeric enzyme that hydrolyzes periplasmic glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), to the corresponding alcohols and G3P, which is subsequently transported into the cell through the GlpT transport system. Ca2+ is required for the enzymatic activity of GlpQ. This family also includes a surface-exposed lipoprotein, protein D (HPD), from Haemophilus influenza Type b and nontypeable strains, which shows very high sequence similarity with E. coli GlpQ. HPD has been characterized as a human immunoglobulin D-binding protein with glycerophosphodiester phosphodiesterase activity. It can hydrolyze phosphatidylcholine from host membranes to produce free choline on the lipopolysaccharides on the surface of pathogenic bacteria.


Pssm-ID: 176542 [Multi-domain]  Cd Length: 318  Bit Score: 47.39  E-value: 7.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 123 HRGsAHDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDK--------------------DIST 182
Cdd:cd08600   6 HRG-ASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAEkfpdrkrkdgryyvidftldELKS 84

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 17556807 183 MNITEFRKL-----------RF--TGTNISLPTFEE 205
Cdd:cd08600  85 LSVTERFDIengkkvqvypnRFplWKSDFKIHTLEE 120
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 123-247 2.17e-05

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial protein Rv2277c and similar proteins. Members in this subfamily are bacterial homologous of mammalian GDE4, a transmembrane protein whose cellular function has not yet been elucidated.


Pssm-ID: 176522 [Multi-domain]  Cd Length: 263  Bit Score: 45.39  E-value: 2.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 123 HRGSAhDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDKDISTMNITEFRKL----------- 191
Cdd:cd08580   6 HRGGT-ADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLnagynfkpegg 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17556807 192 -RFTGTNISLPTFEEAVSYCVANDImmIWDVKNVDENLLKQFVIQMKT-HNLYSKVLV 247
Cdd:cd08580  85 yPYRGKPVGIPTLEQVLRAFPDTPF--ILDMKSLPADPQAKAVARVLErENAWSRVRI 140
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 122-235 4.21e-05

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE3 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE3 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 2 (GDPD2), Osteoblast differentiation promoting factor) and their metazoan homologs. Mammalian GDE3 is a transmembrane protein specifically expressed in bone tissues and spleen. It is a mammalian homolog of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Mammalian GDE3 has been characterized as glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate inositol 1-phosphate (Ins1P) and glycerol. Mammalian GDE3 functions as an inducer of osteoblast differentiation. It also plays a critical role for actin cytoskeletal modulation. The catalytic activity of GDPD domain is essential for mammalian GDE3 cellular function.


Pssm-ID: 176551 [Multi-domain]  Cd Length: 315  Bit Score: 44.91  E-value: 4.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 122 GHRGsAHDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVdKDI---------STMNITEFRKL- 191
Cdd:cd08609  31 GHRG-APMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNV-KDVfpgrdaagsNNFTWTELKTLn 108

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17556807 192 ---------------------RFTGTNISLPTFEEAVSYCVANDIMMIWDVKNVDENLLKQ--FVIQ 235
Cdd:cd08609 109 agswflerrpfwtlsslseedRREADNQTVPSLSELLDLAKKHNVSIMFDLRNENNSHVFYssFVFY 175
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 119-209 4.44e-05

Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative Galdieria sulphuraria glycerophosphodiester phosphodiesterase (GsGDE, EC 3.1.4.46) and its uncharacterized eukaryotic homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176507 [Multi-domain]  Cd Length: 265  Bit Score: 44.77  E-value: 4.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 119 KIGGHRGSA-HDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICH--------DANTVRVTGVDKDISTMNITEFR 189
Cdd:cd08564   5 IIVGHRGAGcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteddtnpDTSIQLDDSGFKNINDLSLDEIT 84

                        90       100
                ....*....|....*....|
gi 17556807 190 KLRFTGTNISLPTFEEAVSY 209
Cdd:cd08564  85 RLHFKQLFDEKPCGADEIKG 104
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 119-191 9.09e-05

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2, GDE3, GDE6-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase domain-containing protein subtype 5 (GDE2), subtype 2 (GDE3), subtype 1 (GDE6), and their eukaryotic homologs. Mammalian GDE2, GDE3, and GDE6 show very high sequence similarity to each other and have been classified into the same family. Although they are all transmembrane proteins, based on different pattern of tissue distribution, these enzymes might display diverse cellular functions. Mammalian GDE2 is primarily expressed in mature neurons. It selectively hydrolyzes glycerophosphocholine (GPC) and mainly functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE3 is specifically expressed in bone tissues and spleen. It selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate inositol 1-phosphate (Ins1P) and glycerol and functions as an inducer of osteoblast differentiation. Mammalian GDE6 is predominantly expressed in the spermatocytes of testis, and its specific physiological function has not been elucidated yet.


Pssm-ID: 176516 [Multi-domain]  Cd Length: 252  Bit Score: 43.45  E-value: 9.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556807 119 KIGGHRGsAHDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGVDK--------DISTMNITEFRK 190
Cdd:cd08574   3 ALIGHRG-APMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVADvfperaheRASMFTWTDLQQ 81


                .
gi 17556807 191 L 191
Cdd:cd08574  82 L 82
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 122-176 5.70e-03

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE6 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE6 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 4 (GDPD4)) and their metazoan homologs. Mammalian GDE6 is a transmembrane protein predominantly expressed in the spermatocytes of testis. Although the specific physiological function of mammalian GDE6 has not been elucidated, its different pattern of tissue distribution suggests it might play a critical role in the completion of meiosis during male germ cell differentiation.


Pssm-ID: 176552 [Multi-domain]  Cd Length: 316  Bit Score: 38.32  E-value: 5.70e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17556807 122 GHRGsAHDDIPENSLEAFSAVKREGGQLAEMDIQITLDGVPVICHDANTVRVTGV 176
Cdd:cd08610  27 GHRG-APMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNI 80
 
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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