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Conserved domains on  [gi|1262831582|gb|PFU42082.1|]
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glycerophosphodiester phosphodiesterase [Bacillus thuringiensis]

Protein Classification

glycerophosphodiester phosphodiesterase family protein( domain architecture ID 10171266)

glycerophosphodiester phosphodiesterase (GDPD) family protein similar to GDPD which degrades various glycerophosphodiesters to produce glycerol-3-phosphate and the corresponding alcohol moiety

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_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 16-323 0e+00

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of mammalian glycerophosphodiester phosphodiesterase GDE4; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial homologs of mammalian GDE4, a transmembrane protein whose cellular function has not been elucidated yet.


:

Pssm-ID: 176554 [Multi-domain]  Cd Length: 309  Bit Score: 546.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  16 ILILFVFVYVNNSSFFAERADRTPLLLAHRGLSQTFSMEGIEGDTCTAKRINKPEHSYLENTIPSMEAAFKAGADLVEFD 95
Cdd:cd08613     1 LLLAAAGVWLNNTSLLAPPPGGKPKLLAHRGLAQTFDREGVENDTCTAERIDPPTHDYLENTIASMQAAFDAGADVVELD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  96 VQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTKELQALDIGYGYTADGGKTFPFRGKGHNLMPTLDEVLTHFPDRSFLIH 175
Cdd:cd08613    81 VHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELKTLDIGYGYTADGGKTFPFRGKGVGMMPTLDEVFAAFPDRRFLIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 176 IKSDDENEGIQMATYLKKLPAKRLDQLTVYGGDKPIAAIKERIPSLRIMSKATMKKDLITYMALGWTGYIPSSLKHGELH 255
Cdd:cd08613   161 FKSDDAAEGELLAEKLATLPRKRLQVLTVYGGDKPIAALRELTPDLRTLSKASMKDCLIEYLALGWTGYVPDSCRNTTLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1262831582 256 IPDKVAPWLWGWPNRFLNRMDKADTRVIIVGGNGFGFSSG-FDSSEDIKRLPDDYTGGIWTNRIDKIAP 323
Cdd:cd08613   241 IPLNYAPWLWGWPNRFLARMEAAGTRVILVGPYTGGEFSEgFDTPEDLKRLPEGFTGYIWTNKIEALAP 309
 
Name Accession Description Interval E-value
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 16-323 0e+00

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of mammalian glycerophosphodiester phosphodiesterase GDE4; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial homologs of mammalian GDE4, a transmembrane protein whose cellular function has not been elucidated yet.


Pssm-ID: 176554 [Multi-domain]  Cd Length: 309  Bit Score: 546.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  16 ILILFVFVYVNNSSFFAERADRTPLLLAHRGLSQTFSMEGIEGDTCTAKRINKPEHSYLENTIPSMEAAFKAGADLVEFD 95
Cdd:cd08613     1 LLLAAAGVWLNNTSLLAPPPGGKPKLLAHRGLAQTFDREGVENDTCTAERIDPPTHDYLENTIASMQAAFDAGADVVELD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  96 VQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTKELQALDIGYGYTADGGKTFPFRGKGHNLMPTLDEVLTHFPDRSFLIH 175
Cdd:cd08613    81 VHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELKTLDIGYGYTADGGKTFPFRGKGVGMMPTLDEVFAAFPDRRFLIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 176 IKSDDENEGIQMATYLKKLPAKRLDQLTVYGGDKPIAAIKERIPSLRIMSKATMKKDLITYMALGWTGYIPSSLKHGELH 255
Cdd:cd08613   161 FKSDDAAEGELLAEKLATLPRKRLQVLTVYGGDKPIAALRELTPDLRTLSKASMKDCLIEYLALGWTGYVPDSCRNTTLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1262831582 256 IPDKVAPWLWGWPNRFLNRMDKADTRVIIVGGNGFGFSSG-FDSSEDIKRLPDDYTGGIWTNRIDKIAP 323
Cdd:cd08613   241 IPLNYAPWLWGWPNRFLARMEAAGTRVILVGPYTGGEFSEgFDTPEDLKRLPEGFTGYIWTNKIEALAP 309
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
37-327 2.75e-42

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 146.17  E-value: 2.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  37 RTPLLLAHRGLSqtfsmegiegdtctakrinkpeHSYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRT 116
Cdd:COG0584     1 PRPLIIAHRGAS----------------------GLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTT 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 117 NGKGVTRDFTTKELQALDIGYGYTADGGKtfpfrgkghnlMPTLDEVLTHFPDR-SFLIHIKSDDENEGIQMATYLKKL- 194
Cdd:COG0584    59 NGTGRVADLTLAELRQLDAGSGPDFAGER-----------IPTLEEVLELVPGDvGLNIEIKSPPAAEPDLAEAVAALLk 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 195 PAKRLDQLTVYGGDKP-IAAIKERIPSLRImskatmkkdlitymALGWTGYIPSSLKHGELHIPDKVAPWLWGWPNRFLN 273
Cdd:COG0584   128 RYGLEDRVIVSSFDPEaLRRLRELAPDVPL--------------GLLVEELPADPLELARALGADGVGPDYDLLTPELVA 193

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1262831582 274 RMDKADTRVII--VggngfgfssgfDSSEDIKRLPDDYTGGIWTNRIDKIAPVFQK 327
Cdd:COG0584   194 AAHAAGLKVHVwtV-----------NDPEEMRRLLDLGVDGIITDRPDLLRAVLRE 238
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 71-187 4.15e-24

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: 98.63  E-value: 4.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  71 HSYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTKELQALDIGygytadGGKTFPFR 150
Cdd:pfam03009   6 GSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIG------AGNSGPLS 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1262831582 151 GKgHNLMPTLDEVLTHFPDRSFLIHIKSDDENEGIQM 187
Cdd:pfam03009  80 GE-RVPFPTLEEVLEFDWDVGFNIEIKIKPYVEAIAP 115
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 11-162 3.02e-13

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 69.70  E-value: 3.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  11 KTTLIILILFVFVYVNNSSFFAERADrtPLLLAHRGLSQTFsmegiegdtctakrinkPEHsylenTIPSMEAAFKAGAD 90
Cdd:PRK11143    1 LKNLSLALLLAALLAGSAAAAADSAE--KIVIAHRGASGYL-----------------PEH-----TLPAKAMAYAQGAD 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  91 LVEFDVQPTKDNNFVIFHDWTLD------------CRTNGKGVTRDFTTKELQALDIGYGYTADGGK---TFPFR---GK 152
Cdd:PRK11143   57 YLEQDLVMTKDDQLVVLHDHYLDrvtdvaerfpdrARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKkvqVYPGRfpmGK 136

                         170
                  ....*....|
gi 1262831582 153 GHNLMPTLDE 162
Cdd:PRK11143  137 SDFRVHTFEE 146
 
Name Accession Description Interval E-value
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 16-323 0e+00

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of mammalian glycerophosphodiester phosphodiesterase GDE4; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial homologs of mammalian GDE4, a transmembrane protein whose cellular function has not been elucidated yet.


Pssm-ID: 176554 [Multi-domain]  Cd Length: 309  Bit Score: 546.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  16 ILILFVFVYVNNSSFFAERADRTPLLLAHRGLSQTFSMEGIEGDTCTAKRINKPEHSYLENTIPSMEAAFKAGADLVEFD 95
Cdd:cd08613     1 LLLAAAGVWLNNTSLLAPPPGGKPKLLAHRGLAQTFDREGVENDTCTAERIDPPTHDYLENTIASMQAAFDAGADVVELD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  96 VQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTKELQALDIGYGYTADGGKTFPFRGKGHNLMPTLDEVLTHFPDRSFLIH 175
Cdd:cd08613    81 VHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELKTLDIGYGYTADGGKTFPFRGKGVGMMPTLDEVFAAFPDRRFLIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 176 IKSDDENEGIQMATYLKKLPAKRLDQLTVYGGDKPIAAIKERIPSLRIMSKATMKKDLITYMALGWTGYIPSSLKHGELH 255
Cdd:cd08613   161 FKSDDAAEGELLAEKLATLPRKRLQVLTVYGGDKPIAALRELTPDLRTLSKASMKDCLIEYLALGWTGYVPDSCRNTTLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1262831582 256 IPDKVAPWLWGWPNRFLNRMDKADTRVIIVGGNGFGFSSG-FDSSEDIKRLPDDYTGGIWTNRIDKIAP 323
Cdd:cd08613   241 IPLNYAPWLWGWPNRFLARMEAAGTRVILVGPYTGGEFSEgFDTPEDLKRLPEGFTGYIWTNKIEALAP 309
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 39-321 5.01e-89

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: 267.16  E-value: 5.01e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  39 PLLLAHRGLSQTFsmegiegdtctakrinkpehsyLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNG 118
Cdd:cd08575     1 PLHIAHRGGAAEF----------------------PENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGG 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 119 KGVTRDFTTKELQALDIGYGYTADGGKTFPFRGKGHNLMPTLDEVLTHFPDRSFLIHIKSDDENEGIQMatYLKKLPAKR 198
Cdd:cd08575    59 SGLVSDLTYAELPPLDAGYGYTFDGGKTGYPRGGGDGRIPTLEEVFKAFPDTPINIDIKSPDAEELIAA--VLDLLEKYK 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 199 LDQLTVYGGDKPiAAIKERIPSLR-IMSKATMKKDLITYMALGWTGYIPSSLKHGE-LHIPDKVAP-------------- 262
Cdd:cd08575   137 REDRTVWGSTNP-EYLRALHPENPnLFESFSMTRCLLLYLALGYTGLLPFVPIKESfFEIPRPVIVletftlgegasiva 215

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 263 WLWGWPNRFLNRMD-KADTRVIIVggngfgfssgfDSSEDIKRLPDDYTGGIWTNRIDKI 321
Cdd:cd08575   216 ALLWWPNLFDHLRKrGIQVYLWVL-----------NDEEDFEEAFDLGADGVMTDSPTKL 264
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
37-327 2.75e-42

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 146.17  E-value: 2.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  37 RTPLLLAHRGLSqtfsmegiegdtctakrinkpeHSYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRT 116
Cdd:COG0584     1 PRPLIIAHRGAS----------------------GLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTT 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 117 NGKGVTRDFTTKELQALDIGYGYTADGGKtfpfrgkghnlMPTLDEVLTHFPDR-SFLIHIKSDDENEGIQMATYLKKL- 194
Cdd:COG0584    59 NGTGRVADLTLAELRQLDAGSGPDFAGER-----------IPTLEEVLELVPGDvGLNIEIKSPPAAEPDLAEAVAALLk 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 195 PAKRLDQLTVYGGDKP-IAAIKERIPSLRImskatmkkdlitymALGWTGYIPSSLKHGELHIPDKVAPWLWGWPNRFLN 273
Cdd:COG0584   128 RYGLEDRVIVSSFDPEaLRRLRELAPDVPL--------------GLLVEELPADPLELARALGADGVGPDYDLLTPELVA 193

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1262831582 274 RMDKADTRVII--VggngfgfssgfDSSEDIKRLPDDYTGGIWTNRIDKIAPVFQK 327
Cdd:COG0584   194 AAHAAGLKVHVwtV-----------NDPEEMRRLLDLGVDGIITDRPDLLRAVLRE 238
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 70-319 2.69e-33

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: 123.14  E-value: 2.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  70 EHSYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTKELQALDIGYGYTADGGKTFPF 149
Cdd:cd08561     8 AGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDDGGRTYPY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 150 RGKGHNLmPTLDEVLTHFPDRSFLIHIKSDDENEGIQMATYLKKlpAKRLDQLTVYG-GDKPIAAIKERIPslRIMSKAT 228
Cdd:cd08561    88 RGQGIRI-PTLEELFEAFPDVRLNIEIKDDGPAAAAALADLIER--YGAQDRVLVASfSDRVLRRFRRLCP--RVATSAG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 229 MkKDLITYMALGWTGYI-PSSLKHGELHIP------DKVAPwlwgwpnRFLNRMDKADTRV---IIvggngfgfssgfDS 298
Cdd:cd08561   163 E-GEVAAFVLASRLGLGsLYSPPYDALQIPvryggvPLVTP-------RFVRAAHAAGLEVhvwTV------------ND 222

                         250       260
                  ....*....|....*....|.
gi 1262831582 299 SEDIKRLPDDYTGGIWTNRID 319
Cdd:cd08561   223 PAEMRRLLDLGVDGIITDRPD 243
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 39-179 1.55e-26

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: 104.56  E-value: 1.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  39 PLLLAHRGLSQTfsmegiegdtctakrinkpehsYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNG 118
Cdd:cd08563     1 TLIFAHRGYSGT----------------------APENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNG 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1262831582 119 KGVTRDFTTKELQALDIGYGYtadggktfpFRGKGHNLMPTLDEVLTHFPDRSFL--IHIKSD 179
Cdd:cd08563    59 KGYVKDLTLEELKKLDAGSWF---------DEKFTGEKIPTLEEVLDLLKDKDLLlnIEIKTD 112
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 40-224 4.04e-26

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: 103.92  E-value: 4.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  40 LLLAHRGLsqtfsmegiegdtctakrinkPEHSYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGK 119
Cdd:cd08566     1 LVVAHRGG---------------------WGAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGK 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 120 GVTRDFTTKELQALDIGygyTADGGKTfpfrgkGHNlMPTLDEVLTHFPDRSFL-IHIKSDDENEGIQMatyLKKLPAkr 198
Cdd:cd08566    60 GKVSDLTLAEIRKLRLK---DGDGEVT------DEK-VPTLEEALAWAKGKILLnLDLKDADLDEVIAL---VKKHGA-- 124

                         170       180
                  ....*....|....*....|....*..
gi 1262831582 199 LDQLTVYGGDKPIAA-IKERIPSLRIM 224
Cdd:cd08566   125 LDQVIFKSYSEEQAKeLRALAPEVMLM 151
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 71-187 4.15e-24

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: 98.63  E-value: 4.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  71 HSYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTKELQALDIGygytadGGKTFPFR 150
Cdd:pfam03009   6 GSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIG------AGNSGPLS 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1262831582 151 GKgHNLMPTLDEVLTHFPDRSFLIHIKSDDENEGIQM 187
Cdd:pfam03009  80 GE-RVPFPTLEEVLEFDWDVGFNIEIKIKPYVEAIAP 115
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 39-209 5.54e-24

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: 98.55  E-value: 5.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  39 PLLLAHRGlsqtfsmegieGdtcTAkriNKPEhsyleNTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNG 118
Cdd:cd08580     1 PLIVAHRG-----------G---TA---DAPE-----NTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNG 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 119 KGVTRDFTTKELQALDIGYGYTADGGKtfPFRGKGHNLmPTLDEVLTHFPDRSFLIHIKSDDENEGIQ-MATYLKKLpaK 197
Cdd:cd08580    59 SGAVSAYTAAQLATLNAGYNFKPEGGY--PYRGKPVGI-PTLEQVLRAFPDTPFILDMKSLPADPQAKaVARVLERE--N 133

                         170
                  ....*....|..
gi 1262831582 198 RLDQLTVYGGDK 209
Cdd:cd08580   134 AWSRVRIYSTNA 145
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 40-183 4.12e-22

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: 94.27  E-value: 4.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  40 LLLAHRGLSQTfsmegiegdtctakRINKPEHSYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGK 119
Cdd:cd08572     1 LVIGHRGLGKN--------------YASGSLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 120 GVT----------RDFTTKELQALDIgYGYTADGGKTFPFRGKG----------HNLMPTLDEVLTHFP-DRSFLIHIKS 178
Cdd:cd08572    67 TGSdegelievpiHDLTLEQLKELGL-QHISALKRKALTRKAKGpkpnpwgmdeHDPFPTLQEVLEQVPkDLGFNIEIKY 145


                  ....*
gi 1262831582 179 DDENE 183
Cdd:cd08572   146 PQLLE 150
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 41-227 2.18e-20

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: 88.14  E-value: 2.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  41 LLAHRGLSQTfsmegiegdtctakrinkpehsYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGKG 120
Cdd:cd08582     1 VIAHRGASAE----------------------APENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDG 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 121 VTRDFTTKELQALDIGYGYTADGGKTfpfrgkghnLMPTLDEVLTHFPDRSFLIHIKsddenegIQMATYLKKLPAKRLD 200
Cdd:cd08582    59 AVSDLTLAELRKLDIGSWKGESYKGE---------KVPTLEEYLAIVPKYGKKLFIE-------IKHPRRGPEAEEELLK 122

                         170       180
                  ....*....|....*....|....*...
gi 1262831582 201 QLTVYGG-DKPIAAIKERIPSLRIMSKA 227
Cdd:cd08582   123 LLKESGLlPEQIVIISFDAEALKRVREL 150
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 39-326 1.64e-19

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: 86.22  E-value: 1.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  39 PLLLAHRGLSQtfsmegiegdtctakriNKPEHsylenTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNG 118
Cdd:cd08601     1 NAVIAHRGASG-----------------YAPEH-----TFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNI 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 119 --KGVTRDFTTKELQALDIGYGYTadggKTFPFRGK---GHNLMPTLDEVLTHF-PDRSFLIHIKSDDENEGIQmatylK 192
Cdd:cd08601    59 erPGPVKDYTLAEIKQLDAGSWFN----KAYPEYAResySGLKVPTLEEVIERYgGRANYYIETKSPDLYPGME-----E 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 193 KLPAKrLDQLTVYGGD----------------KPIAAIKERIPSLRIMSK---ATMKKDLITYMALGWTGYIPSSlkhge 253
Cdd:cd08601   130 KLLAT-LDKYGLLTDNlkngqviiqsfskeslKKLHQLNPNIPLVQLLWYgegAETYDKWLDEIKEYAIGIGPSI----- 203

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1262831582 254 lhipDKVAPWLwgwpnrflnrMDKADTRVIIVggngfgFSSGFDSSEDIKRLPDDYTGGIWTNRIDKIAPVFQ 326
Cdd:cd08601   204 ----ADADPWM----------VHLIHKKGLLV------HPYTVNEKADMIRLINWGVDGMFTNYPDRLKEVLK 256
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 41-224 4.01e-18

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: 80.77  E-value: 4.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  41 LLAHRGLSQTfsmegiegdtctakrinkpehsYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDwtldcrtngkg 120
Cdd:cd08556     1 IIAHRGASGE----------------------APENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD----------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 121 vtrdfttkelqaldigygytadggktfpfrgkghnlMPTLDEVLTHFPDRSFL-IHIKSDDENEGI--QMATYLKKLPAK 197
Cdd:cd08556    48 ------------------------------------IPTLEEVLELVKGGVGLnIELKEPTRYPGLeaKVAELLREYGLE 91

                         170       180
                  ....*....|....*....|....*...
gi 1262831582 198 rlDQLTVYGGD-KPIAAIKERIPSLRIM 224
Cdd:cd08556    92 --ERVVVSSFDhEALRALKELDPEVPTG 117
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 75-224 4.41e-18

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: 81.44  E-value: 4.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  75 ENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTKELQALDIGygytaDGGKTFPFrgkgh 154
Cdd:cd08579    13 ENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIG-----ENGHGAKI----- 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1262831582 155 nlmPTLDEVLT--HFPDRSFLIHIKSDDENEGIQMATYLKKLPAKRLDQLTV-----YggdKPIAAIKERIPSLRIM 224
Cdd:cd08579    83 ---PSLDEYLAlaKGLKQKLLIELKPHGHDSPDLVEKFVKLYKQNLIENQHQvhsldY---RVIEKVKKLDPKIKTG 153
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 75-194 1.28e-17

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: 80.77  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  75 ENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTKELQALDIgygytadgGKTFPFRGKGH 154
Cdd:cd08573    13 ENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNA--------AAKHRLSSRFP 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1262831582 155 NL-MPTLDEVLTHFPDR--SFLIHIKSDDEnegiQMATYLKKL 194
Cdd:cd08573    85 GEkIPTLEEAVKECLENnlRMIFDVKSNSS----KLVDALKNL 123
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 71-179 7.26e-17

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: 78.21  E-value: 7.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  71 HSYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTKELQALDIGYGytaDGGKtfpfr 150
Cdd:cd08565     9 NLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLRDS---FGEK----- 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1262831582 151 gkghnlMPTLDEVLTHFPDRSFLIH--IKSD 179
Cdd:cd08565    81 ------IPTLEEVLALFAPSGLELHveIKTD 105
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 44-193 7.67e-17

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: 79.26  E-value: 7.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  44 HRGLSQTFSmegiegdtctakrinKPEHSYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGKGVT- 122
Cdd:cd08607     5 HRGAGNSYT---------------AASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSd 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 123 ---------RDFTTKELQALDIgYGYTADGGKTFPFRGKG-----HNLMPTLDEVLTHFP-DRSFLIHIK-----SDDEN 182
Cdd:cd08607    70 rddllevpvKDLTYEQLKLLKL-FHISALKVKEYKSVEEDedppeHQPFPTLSDVLESVPeDVGFNIEIKwpqqqKDGSW 148

                         170
                  ....*....|.
gi 1262831582 183 EGiQMATYLKK 193
Cdd:cd08607   149 ES-ELFTYFDR 158
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 39-165 1.97e-16

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: 78.08  E-value: 1.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  39 PLLLAHRGLSQTFsmegiegdtctakrinkPEHsylenTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTN- 117
Cdd:cd08559     1 PLVIAHRGASGYA-----------------PEH-----TLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNv 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1262831582 118 -----------GKGVTRDFTTKELQALDIGYGYTadggKTFPFR---GKGHNLMPTLDEVLT 165
Cdd:cd08559    59 aehfpfrgrkdTGYFVIDFTLAELKTLRAGSWFN----QRYPERapsYYGGFKIPTLEEVIE 116
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 75-183 7.90e-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: 75.34  E-value: 7.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  75 ENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTKELQALDIGYGYTADggktfpFRGKGh 154
Cdd:cd08562    13 ENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFSPE------FAGEP- 85

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1262831582 155 nlMPTLDEVLThFPDRSFL---IHIKSDDENE 183
Cdd:cd08562    86 --IPTLADVLE-LARELGLglnLEIKPDPGDE 114
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 72-182 1.71e-14

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: 72.44  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  72 SYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGKGVT---RDFTTKELQALDIGYGYTADGGKTFP 148
Cdd:cd08605    22 GIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVERGGEVESsriRDLTLAELKALGPQAESTKTSTVALY 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1262831582 149 FRGKG----------HNLMPTLDEVLTHFPDR-SFLIHIKSDDEN 182
Cdd:cd08605   102 RKAKDpepepwimdvEDSIPTLEEVFSEVPPSlGFNIELKFGDDN 146
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 73-177 1.11e-13

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: 69.25  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  73 YLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTKELQALDIgygytadGGKtfpfrgk 152
Cdd:cd08568    12 YPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHP-------GGE------- 77

                          90       100
                  ....*....|....*....|....*.
gi 1262831582 153 ghnLMPTLDEVLTHFPDRSFL-IHIK 177
Cdd:cd08568    78 ---LIPTLEEVFRALPNDAIInVEIK 100
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 11-162 3.02e-13

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 69.70  E-value: 3.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  11 KTTLIILILFVFVYVNNSSFFAERADrtPLLLAHRGLSQTFsmegiegdtctakrinkPEHsylenTIPSMEAAFKAGAD 90
Cdd:PRK11143    1 LKNLSLALLLAALLAGSAAAAADSAE--KIVIAHRGASGYL-----------------PEH-----TLPAKAMAYAQGAD 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  91 LVEFDVQPTKDNNFVIFHDWTLD------------CRTNGKGVTRDFTTKELQALDIGYGYTADGGK---TFPFR---GK 152
Cdd:PRK11143   57 YLEQDLVMTKDDQLVVLHDHYLDrvtdvaerfpdrARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKkvqVYPGRfpmGK 136

                         170
                  ....*....|
gi 1262831582 153 GHNLMPTLDE 162
Cdd:PRK11143  137 SDFRVHTFEE 146
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 75-185 5.69e-13

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: 67.35  E-value: 5.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  75 ENTIPSMEAAFKAGADlVEFDVQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTKELQALDIGygytaDGGKTfpfrgkgh 154
Cdd:cd08585    21 ENSLSAFRAAAEAGYG-IELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRLL-----GTDEH-------- 86

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1262831582 155 nlMPTLDEVLTHFPDRS-FLIHIKSDDENEGI 185
Cdd:cd08585    87 --IPTLDEVLELVAGRVpLLIELKSCGGGDGG 116
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 72-181 9.12e-13

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: 66.86  E-value: 9.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  72 SYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTK-ELQALdigygytadggKTfpfR 150
Cdd:cd08570    10 KYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDSTWdELSHL-----------RT---I 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1262831582 151 GKGHNLMPTLDEVLTHF-----PDRSFLIHIKSDDE 181
Cdd:cd08570    76 EEPHQPMPTLKDVLEWLvehelPDVKLMLDIKRDND 111
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 73-179 9.84e-13

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: 66.59  E-value: 9.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  73 YLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDcRTNG-KGVTRDFTTKELQALDIGYGYTAdgGKTFPfrg 151
Cdd:cd08581    11 YPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLL-RLTGvEGLLHELEDAELDSLRVAEPARF--GSRFA--- 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1262831582 152 kgHNLMPTLDEV---LTHFPDRSFLIHIKSD 179
Cdd:cd08581    85 --GEPLPSLAAVvqwLAQHPQVTLFVEIKTE 113
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 75-181 2.51e-12

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: 65.80  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  75 ENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLD---CR-TNGKGVT------RDFTTKELQALDIGY-GYTADG 143
Cdd:cd08567    15 ENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNpdiTRdPDGAWLPyegpalYELTLAEIKQLDVGEkRPGSDY 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1262831582 144 GKTFPFRgkgHNL----MPTLDEVLTHFPDRS-----FLIHIKSDDE 181
Cdd:cd08567    95 AKLFPEQ---IPVpgtrIPTLEEVFALVEKYGnqkvrFNIETKSDPD 138
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 39-211 8.47e-12

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: 64.77  E-value: 8.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  39 PLLLAHRGLSQtfsmegiegdtctakriNKPEHSYL---ENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLdcr 115
Cdd:cd08606     2 VQVIGHRGLGK-----------------NTAERKSLqlgENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLV--- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 116 tNGKGVtrDFTTKEL---QALDIGY-GYTAD-GGKTFPFRGKGHNL---MPTLDEVLTHFP-DRSFLIHIKSD--DENEG 184
Cdd:cd08606    62 -SETGT--DVPIHDLtleQFLHLSRmKYTVDfKKKGFKGNSRGHSIqapFTTLEELLKKLPkSVGFNIELKYPmlHEAEE 138

                         170       180       190
                  ....*....|....*....|....*....|
gi 1262831582 185 IQMATYLKKLPA---KRLDQLTVYGGDKPI 211
Cdd:cd08606   139 EEVAPVAIELNAfvdTVLEKVFDYGAGRNI 168
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 39-164 6.32e-11

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: 62.41  E-value: 6.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  39 PLLLAHRGLSqtfsmegiegdtctakrinkpehSYL-ENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTN 117
Cdd:cd08600     1 KIIIAHRGAS-----------------------GYLpEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTN 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1262831582 118 ------------GKGVTRDFTTKELQALDIGYGYTADGGK---TFPFR---GKGHNLMPTLDEVL 164
Cdd:cd08600    58 vaekfpdrkrkdGRYYVIDFTLDELKSLSVTERFDIENGKkvqVYPNRfplWKSDFKIHTLEEEI 122
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 75-163 1.34e-10

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 60.72  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  75 ENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNGKGVTRDFTTKELQALDIGYGYTADggktfpFRGKGh 154
Cdd:PRK09454   22 ENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAA------FAGEP- 94


                  ....*....
gi 1262831582 155 nlMPTLDEV 163
Cdd:PRK09454   95 --LPTLSQV 101
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 74-246 3.48e-10

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: 59.92  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  74 LENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLdCRTNGKGVT-RDFTTKEL----QALDI----GYGYTADGG 144
Cdd:cd08612    40 LENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENL-LRSCGVDKLvSDLNYADLppylEKLEVtfspGDYCVPKGS 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582 145 KTFpfrgkghnlMPTLDEVLTHFPDRSFLIHIKSDDENEGIQMATYLKKLpaKRLDqLTVYGG--DKPIAAIKERIPSLR 222
Cdd:cd08612   119 DRR---------IPLLEEVFEAFPDTPINIDIKVENDELIKKVSDLVRKY--KRED-ITVWGSfnDEIVKKCHKENPNIP 186

                         170       180
                  ....*....|....*....|....
gi 1262831582 223 IMskATMKKDLITYMALgWTGYIP 246
Cdd:cd08612   187 LF--FSLKRVLLLLLLY-YTGLLP 207
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 70-169 1.43e-08

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: 54.79  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  70 EHSYLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFH--------DWTLDCRTNGKGVTRDFTTKELQALDIGYGYta 141
Cdd:cd08564    15 STLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteddtnpDTSIQLDDSGFKNINDLSLDEITRLHFKQLF-- 92

                          90       100
                  ....*....|....*....|....*...
gi 1262831582 142 DGGKTFPFRGKGHNLmPTLDEVLTHFPD 169
Cdd:cd08564    93 DEKPCGADEIKGEKI-PTLEDVLVTFKD 119
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 73-150 2.62e-07

Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases superfamily; The PI-PLC-like phosphodiesterases superfamily represents the catalytic domains of bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11), glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), 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, as well as their uncharacterized homologs found in organisms ranging from bacteria and archaea to metazoans, plants, and fungi. PI-PLCs are ubiquitous enzymes hydrolyzing the membrane lipid phosphoinositides to yield two important second messengers, inositol phosphates and diacylglycerol (DAG). GP-GDEs play essential roles in glycerol metabolism and catalyze the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols that are major sources of carbon and phosphate. Both, PI-PLCs and GP-GDEs, can hydrolyze the 3'-5' phosphodiester bonds in different substrates, and utilize a similar mechanism of general base and acid catalysis with conserved histidine residues, which consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81, glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs). The residues essential for enzyme activities and metal binding are not conserved in these sequence homologs, which might suggest that the function of catalytic domains in these proteins might be distinct from those in typical PLC-like phosphodiesterases.


Pssm-ID: 176498 [Multi-domain]  Cd Length: 179  Bit Score: 50.13  E-value: 2.62e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1262831582  73 YLENTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDcrtNGKGVTRDFTTKELqaLDIGYGYTADGGKTFPFR 150
Cdd:cd08555    11 GQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLD---RTTAGILPPTLEEV--LELIADYLKNPDYTIILS 83
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 39-164 3.28e-06

Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of putative bacterial and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ, as well as plant glycerophosphodiester phosphodiesterases (GP-PDEs), all of which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. The prototypes of this family include putative secreted phosphodiesterase encoded by gene glpQ1 (SCO1565) from the pho regulon in Streptomyces coelicolor genome, and in plants, two distinct Arabidopsis thaliana genes, AT5G08030 and AT1G74210, coding putative GP-PDEs from the cell walls and vacuoles, respectively.


Pssm-ID: 176544 [Multi-domain]  Cd Length: 309  Bit Score: 48.06  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  39 PLLLAHRGLSQTFsmegiegdtctakrinkPEHsylenTIPSMEAAFKAGADLVEFDVQPTKDNNFVIFHDWTLDCRTNg 118
Cdd:cd08602     1 PLVIAHRGASGYR-----------------PEH-----TLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTD- 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1262831582 119 kgVT--RDF----TTKELQALDI-GY---GYTADGGKT------FPFRGKGHNLM---PTLDEVL 164
Cdd:cd08602    58 --VAdhPEFadrkTTKTVDGVNVtGWfteDFTLAELKTlrarqrLPYRDQSYDGQfpiPTFEEII 120
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 39-136 1.05e-03

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: 39.98  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262831582  39 PLLLAHRGlsqtFSMEGiegdtctakrinkPEhsyleNTIPSMEAAFKAGADLVEFDVQPTKDNnfVIF--HDWTLDCRT 116
Cdd:cd08574     2 PALIGHRG----APMLA-------------PE-----NTLMSFEKALEHGVYGLETDVTISYDG--VPFlmHDRTLRRTT 57

                          90       100
                  ....*....|....*....|....*...
gi 1262831582 117 NGKGV--TRD------FTTKELQALDIG 136
Cdd:cd08574    58 NVADVfpERAherasmFTWTDLQQLNAG 85
 
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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