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Conserved domains on  [gi|499595374|ref|WP_011276108|]
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MULTISPECIES: glycerophosphodiester phosphodiesterase [Staphylococcus]

Protein Classification

glycerophosphodiester phosphodiesterase( domain architecture ID 10171128)

glycerophosphodiester phosphodiesterase hydrolyzes deacylated phospholipids to glycerol 3-phosphate and the corresponding alcohols

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 48-302 1.84e-100

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: 294.94  E-value: 1.84e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGYHFKDI 127
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 128 NGQFPYRGHQKAKILTFDELLKMYPNMYINVDLKDAPDSYEGTVAptkmyeDIINN-QAQDRVLVTSFYKEQNVRFREIS 206
Cdd:cd08561   81 GGRTYPYRGQGIRIPTLEELFEAFPDVRLNIEIKDDGPAAAAALA------DLIERyGAQDRVLVASFSDRVLRRFRRLC 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 207 kGQVAIGASQKEVAEGFIKFNLGLGNKYQPIADTFQMPTQFKGIPLTSKRFIQWLNLLNIVPGFYGINSTDLMTDLYHKG 286
Cdd:cd08561  155 -PRVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLG 233

                        250
                 ....*....|....*.
gi 499595374 287 VHTLVTDRPDLGKQFK 302
Cdd:cd08561  234 VDGIITDRPDLLLEVL 249
 
Name Accession Description Interval E-value
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 48-302 1.84e-100

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: 294.94  E-value: 1.84e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGYHFKDI 127
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 128 NGQFPYRGHQKAKILTFDELLKMYPNMYINVDLKDAPDSYEGTVAptkmyeDIINN-QAQDRVLVTSFYKEQNVRFREIS 206
Cdd:cd08561   81 GGRTYPYRGQGIRIPTLEELFEAFPDVRLNIEIKDDGPAAAAALA------DLIERyGAQDRVLVASFSDRVLRRFRRLC 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 207 kGQVAIGASQKEVAEGFIKFNLGLGNKYQPIADTFQMPTQFKGIPLTSKRFIQWLNLLNIVPGFYGINSTDLMTDLYHKG 286
Cdd:cd08561  155 -PRVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLG 233

                        250
                 ....*....|....*.
gi 499595374 287 VHTLVTDRPDLGKQFK 302
Cdd:cd08561  234 VDGIITDRPDLLLEVL 249
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
44-301 8.25e-61

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 193.55  E-value: 8.25e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  44 KAPYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGYH 123
Cdd:COG0584    1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 124 fkdingqfpyRGHQKAKILTFDELLKMYP-NMYINVDLKDAPDSYEGTVAptKMYEDIINNQAQDRVLVTSFYKEQNVRF 202
Cdd:COG0584   81 ----------PDFAGERIPTLEEVLELVPgDVGLNIEIKSPPAAEPDLAE--AVAALLKRYGLEDRVIVSSFDPEALRRL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 203 REISKgQVAIGASQKEVAEGFIKFNLGLGnkyqpiADTFQMPtqfkgIPLTSKRFIQWLNLLNIVPGFYGINSTDLMTDL 282
Cdd:COG0584  149 RELAP-DVPLGLLVEELPADPLELARALG------ADGVGPD-----YDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRL 216

                        250
                 ....*....|....*....
gi 499595374 283 YHKGVHTLVTDRPDLGKQF 301
Cdd:COG0584  217 LDLGVDGIITDRPDLLRAV 235
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 51-194 3.29e-25

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: 100.94  E-value: 3.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374   51 HRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGyhfKDINGQ 130
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIG---AGNSGP 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499595374  131 FPyrgHQKAKILTFDELLKMYP----NMYINVDLKDAPDSYEGT--VAPTKMYEDII--NNQAQDRVLVTSF 194
Cdd:pfam03009  78 LS---GERVPFPTLEEVLEFDWdvgfNIEIKIKPYVEAIAPEEGliVKDLLLSVDEIlaKKADPRRVIFSSF 146
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 46-121 1.92e-19

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 85.38  E-value: 1.92e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595374  46 PYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAG 121
Cdd:PRK09454   8 PRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAG 83
 
Name Accession Description Interval E-value
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 48-302 1.84e-100

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: 294.94  E-value: 1.84e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGYHFKDI 127
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 128 NGQFPYRGHQKAKILTFDELLKMYPNMYINVDLKDAPDSYEGTVAptkmyeDIINN-QAQDRVLVTSFYKEQNVRFREIS 206
Cdd:cd08561   81 GGRTYPYRGQGIRIPTLEELFEAFPDVRLNIEIKDDGPAAAAALA------DLIERyGAQDRVLVASFSDRVLRRFRRLC 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 207 kGQVAIGASQKEVAEGFIKFNLGLGNKYQPIADTFQMPTQFKGIPLTSKRFIQWLNLLNIVPGFYGINSTDLMTDLYHKG 286
Cdd:cd08561  155 -PRVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLG 233

                        250
                 ....*....|....*.
gi 499595374 287 VHTLVTDRPDLGKQFK 302
Cdd:cd08561  234 VDGIITDRPDLLLEVL 249
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
44-301 8.25e-61

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 193.55  E-value: 8.25e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  44 KAPYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGYH 123
Cdd:COG0584    1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 124 fkdingqfpyRGHQKAKILTFDELLKMYP-NMYINVDLKDAPDSYEGTVAptKMYEDIINNQAQDRVLVTSFYKEQNVRF 202
Cdd:COG0584   81 ----------PDFAGERIPTLEEVLELVPgDVGLNIEIKSPPAAEPDLAE--AVAALLKRYGLEDRVIVSSFDPEALRRL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 203 REISKgQVAIGASQKEVAEGFIKFNLGLGnkyqpiADTFQMPtqfkgIPLTSKRFIQWLNLLNIVPGFYGINSTDLMTDL 282
Cdd:COG0584  149 RELAP-DVPLGLLVEELPADPLELARALG------ADGVGPD-----YDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRL 216

                        250
                 ....*....|....*....
gi 499595374 283 YHKGVHTLVTDRPDLGKQF 301
Cdd:COG0584  217 LDLGVDGIITDRPDLLRAV 235
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 46-295 8.20e-43

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: 146.93  E-value: 8.20e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  46 PYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGYHFK 125
Cdd:cd08563    1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 126 dingqfpyRGHQKAKILTFDELLKMYP--NMYINVDLKDAPDSYEGTVAptKMYEDIINNQAQDRVLVTSFYKEQNVRFR 203
Cdd:cd08563   81 --------EKFTGEKIPTLEEVLDLLKdkDLLLNIEIKTDVIHYPGIEK--KVLELVKEYNLEDRVIFSSFNHESLKRLK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 204 EISKgQVAIGAsqkevaegfikfnLGLGNKYQPIADTFQMPtqFKGI----PLTSKRFIQWLNLLNIVPGFYGINSTDLM 279
Cdd:cd08563  151 KLDP-KIKLAL-------------LYETGLQDPKDYAKKIG--ADSLhpdfKLLTEEVVEELKKRGIPVRLWTVNEEEDM 214

                        250
                 ....*....|....*.
gi 499595374 280 TDLYHKGVHTLVTDRP 295
Cdd:cd08563  215 KRLKDLGVDGIITNYP 230
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 46-291 7.93e-41

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: 142.74  E-value: 7.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  46 PYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGYHFK 125
Cdd:cd08575    1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGYT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 126 DINGQ-FPYRGHQKAKILTFDELLKMYPNMYINVDLKdAPDSYEGTvapTKMYEDIINNQAQDRVLVTSF-YKEQNVRFR 203
Cdd:cd08575   81 FDGGKtGYPRGGGDGRIPTLEEVFKAFPDTPINIDIK-SPDAEELI---AAVLDLLEKYKREDRTVWGSTnPEYLRALHP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 204 EISkgQVAIGASQKEVaegfIKFNLGLGnkYQPIADTFQMPTQFKGIPLTSKRFIQWLNLLNIVPGFYGINSTDLMTDLY 283
Cdd:cd08575  157 ENP--NLFESFSMTRC----LLLYLALG--YTGLLPFVPIKESFFEIPRPVIVLETFTLGEGASIVAALLWWPNLFDHLR 228


                 ....*...
gi 499595374 284 HKGVHTLV 291
Cdd:cd08575  229 KRGIQVYL 236
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 48-295 5.54e-32

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: 118.94  E-value: 5.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGG-MAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLdagyHFKD 126
Cdd:cd08566    2 VVAHRGGwGAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKL----RLKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 127 INGQFpyRGHqkaKILTFDELLKMYP-NMYINVDLKDAPdsyegtvaPTKMYEDIINNQAQDRVLVTSFYKEQNVRFREI 205
Cdd:cd08566   78 GDGEV--TDE---KVPTLEEALAWAKgKILLNLDLKDAD--------LDEVIALVKKHGALDQVIFKSYSEEQAKELRAL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 206 SKGqVAIGASQKEVAEGFIKFNLGLGNKYQPIAD-TFQMPTQFKGIPLTSKRF--IQWLNLLNIV-PGFYGINSTDLMTD 281
Cdd:cd08566  145 APE-VMLMPIVRDAEDLDEEEARAIDALNLLAFEiTFDDLDLPPLFDELLRALgiRVWVNTLGDDdTAGLDRALSDPREV 223

                        250
                 ....*....|....*..
gi 499595374 282 ---LYHKGVHTLVTDRP 295
Cdd:cd08566  224 wgeLVDAGVDVIQTDRP 240
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 46-193 5.79e-32

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: 119.35  E-value: 5.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  46 PYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGYHFK 125
Cdd:cd08580    1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAGYNFK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499595374 126 DiNGQFPYRGHQkAKILTFDELLKMYPNMYINVDLKdAPDSYEGTVAPTKMyedIINNQAQDRVLVTS 193
Cdd:cd08580   81 P-EGGYPYRGKP-VGIPTLEQVLRAFPDTPFILDMK-SLPADPQAKAVARV---LERENAWSRVRIYS 142
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 48-194 4.02e-31

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: 116.55  E-value: 4.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGYHFKDi 127
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFSP- 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 128 ngQFpyrghQKAKILTFDELLK--MYPNMYINVDLKDAPDSYEGTVAptKMYEDIIN-NQAQDRVLVTSF 194
Cdd:cd08562   80 --EF-----AGEPIPTLADVLElaRELGLGLNLEIKPDPGDEALTAR--VVAAALRElWPHASKLLLSSF 140
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 48-297 5.33e-28

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: 108.26  E-value: 5.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGYHFKDi 127
Cdd:cd08565    1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLRDSFGE- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 128 ngqfpyrghqkaKILTFDELLKMY--PNMYINVDLKDAPDS--YEGTVAPTKmyeDIINNQA-QDRVLVTSFYKEQNVRF 202
Cdd:cd08565   80 ------------KIPTLEEVLALFapSGLELHVEIKTDADGtpYPGAAALAA---ATLRRHGlLERSVLTSFDPAVLTEV 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 203 REISKG--QVAIGASQKEVAEGFIKFNLGLGNKYQPIADTFQMPTqfkGIPLTSKRFIQWLNLlnivpGFYGINSTDLMT 280
Cdd:cd08565  145 RKHPGVrtLGSVDEDMLERLGGELPFLTATALKAHIVAVEQSLLA---ATWELVRAAVPGLRL-----GVWTVNDDSLIR 216

                        250
                 ....*....|....*..
gi 499595374 281 DLYHKGVHTLVTDRPDL 297
Cdd:cd08565  217 YWLACGVRQLTTDRPDL 233
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 48-195 6.29e-27

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: 106.19  E-value: 6.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAgyhfkdi 127
Cdd:cd08573    1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNA------- 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499595374 128 NGQFPYRGH-QKAKILTFDELLK--MYPNMYINVDLKDapDSYEGTVAPTKMYEDiiNNQAQDRVLVTSFY 195
Cdd:cd08573   74 AAKHRLSSRfPGEKIPTLEEAVKecLENNLRMIFDVKS--NSSKLVDALKNLFKK--YPGLYDKAIVCSFN 140
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 51-194 3.29e-25

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: 100.94  E-value: 3.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374   51 HRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGyhfKDINGQ 130
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIG---AGNSGP 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499595374  131 FPyrgHQKAKILTFDELLKMYP----NMYINVDLKDAPDSYEGT--VAPTKMYEDII--NNQAQDRVLVTSF 194
Cdd:pfam03009  78 LS---GERVPFPTLEEVLEFDWdvgfNIEIKIKPYVEAIAPEEGliVKDLLLSVDEIlaKKADPRRVIFSSF 146
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 48-297 5.39e-25

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: 100.85  E-value: 5.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGS--GKVSDHRVSELKRLDAGYHFk 125
Cdd:cd08601    3 VIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIErpGPVKDYTLAEIKQLDAGSWF- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 126 diNGQFPYRGHQ---KAKILTFDELLKMY---PNMYINVDLKDA-PDSYEGTVAPTKMYEDIINNQAQDRVLVTSFYKEQ 198
Cdd:cd08601   82 --NKAYPEYAREsysGLKVPTLEEVIERYggrANYYIETKSPDLyPGMEEKLLATLDKYGLLTDNLKNGQVIIQSFSKES 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 199 NVRFRE----------ISKGQVAIGASQ--KEVAEGFIkfnlGLGNKYQPIADTFQMPTQFKGipltskrfiqwlnlLNI 266
Cdd:cd08601  160 LKKLHQlnpniplvqlLWYGEGAETYDKwlDEIKEYAI----GIGPSIADADPWMVHLIHKKG--------------LLV 221

                        250       260       270
                 ....*....|....*....|....*....|.
gi 499595374 267 VPgfYGINSTDLMTDLYHKGVHTLVTDRPDL 297
Cdd:cd08601  222 HP--YTVNEKADMIRLINWGVDGMFTNYPDR 250
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 48-294 9.66e-25

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: 98.49  E-value: 9.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDatvdrttngsgkvsdhrvselkrldagyhfkdi 127
Cdd:cd08556    1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 128 ngqfpyrghqkakILTFDELLKMYPN-MYINVDLKDaPDSYEGTVAptKMYEDIINNQAQDRVLVTSFYKEQNVRFRE-- 204
Cdd:cd08556   48 -------------IPTLEEVLELVKGgVGLNIELKE-PTRYPGLEA--KVAELLREYGLEERVVVSSFDHEALRALKEld 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 205 --ISKGQVAIGASQKEVAEGFIKFNLglgnkyqpiADTFQMPtqfkgIPLTSKRFIQWLNLLNIVPGFYGINSTDLMTDL 282
Cdd:cd08556  112 peVPTGLLVDKPPLDPLLAELARALG---------ADAVNPH-----YKLLTPELVRAAHAAGLKVYVWTVNDPEDARRL 177

                        250
                 ....*....|..
gi 499595374 283 YHKGVHTLVTDR 294
Cdd:cd08556  178 LALGVDGIITDD 189
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 48-153 2.68e-24

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: 98.16  E-value: 2.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGYhFKDi 127
Cdd:cd08582    1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGS-WKG- 78

                         90       100
                 ....*....|....*....|....*.
gi 499595374 128 ngqfpyRGHQKAKILTFDELLKMYPN 153
Cdd:cd08582   79 ------ESYKGEKVPTLEEYLAIVPK 98
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 48-208 5.45e-23

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: 94.67  E-value: 5.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLdagyhfkDI 127
Cdd:cd08568    2 ILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKL-------HP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 128 NGQfpyrghqkaKILTFDELLKMYPNMYI-NVDLKDaPDSYEgtvaptKMYEDIINNQAQDRVLVTSFYKEQNVRFREIS 206
Cdd:cd08568   75 GGE---------LIPTLEEVFRALPNDAIiNVEIKD-IDAVE------PVLEIVEKFNALDRVIFSSFNHDALRELRKLD 138


                 ..
gi 499595374 207 KG 208
Cdd:cd08568  139 PD 140
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 50-162 6.45e-22

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: 93.43  E-value: 6.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  50 AHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSEL----KRLDAgyHFK 125
Cdd:cd08612   31 SHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLppylEKLEV--TFS 108

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499595374 126 diNGQFPYRGHQKAKILTFDELLKMYPNMYINVDLKD 162
Cdd:cd08612  109 --PGDYCVPKGSDRRIPLLEEVFEAFPDTPINIDIKV 143
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 46-151 4.26e-21

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: 90.80  E-value: 4.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  46 PYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTN------------GSGKVSDHRVS 113
Cdd:cd08559    1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNvaehfpfrgrkdTGYFVIDFTLA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499595374 114 ELKRLDAGYHFkdiNGQFPYRGHQ---KAKILTFDELLKMY 151
Cdd:cd08559   81 ELKTLRAGSWF---NQRYPERAPSyygGFKIPTLEEVIELA 118
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 46-121 1.92e-19

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 85.38  E-value: 1.92e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595374  46 PYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAG 121
Cdd:PRK09454   8 PRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAG 83
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 48-161 7.44e-19

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: 83.42  E-value: 7.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDhrvselkrldagYHFKDI 127
Cdd:cd08570    1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIID------------DSTWDE 68

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499595374 128 NGQFPYRGHQKAKILTFDELLK-----MYPNMYINVDLK 161
Cdd:cd08570   69 LSHLRTIEEPHQPMPTLKDVLEwlvehELPDVKLMLDIK 107
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 43-195 1.04e-18

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: 84.72  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  43 GKAPYIFAHRGgMAVRPEQTQLAFDNAVA------------NNLDGF-----------ETDVRLTKDEKLIVFHDATVDR 99
Cdd:cd08613   21 GGKPKLLAHRG-LAQTFDREGVENDTCTAeridppthdyleNTIASMqaafdagadvvELDVHPTKDGEFAVFHDWTLDC 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 100 TTNGSGKVSDHRVSELKRLDAGYHFKDINGQ-FPYRGHQKAKILTFDELLKMYPNMYINVDLKDApDSYEGtvaptKMYE 178
Cdd:cd08613  100 RTDGSGVTRDHTMAELKTLDIGYGYTADGGKtFPFRGKGVGMMPTLDEVFAAFPDRRFLINFKSD-DAAEG-----ELLA 173

                        170
                 ....*....|....*..
gi 499595374 179 DIINNQAQDRVLVTSFY 195
Cdd:cd08613  174 EKLATLPRKRLQVLTVY 190
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 48-297 2.15e-15

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: 74.66  E-value: 2.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATV--DRTTNGSGK--------VSDHRVSELKR 117
Cdd:cd08567    3 LQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLnpDITRDPDGAwlpyegpaLYELTLAEIKQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 118 LDAGY---------HFKDingQFPYRGhqkAKILTFDELLKM-----YPNMYINVDLKDAPDSYEGTVAP----TKMYED 179
Cdd:cd08567   83 LDVGEkrpgsdyakLFPE---QIPVPG---TRIPTLEEVFALvekygNQKVRFNIETKSDPDRDILHPPPeefvDAVLAV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 180 IINNQAQDRVLVTSFykeqNVRFREISKGQ---VAIGA-SQKEVAEGFIKF--NLGlGNKYQPiadtfqmptQFKgipLT 253
Cdd:cd08567  157 IRKAGLEDRVVLQSF----DWRTLQEVRRLapdIPTVAlTEETTLGNLPRAakKLG-ADIWSP---------YFT---LV 219

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 499595374 254 SKRFIQWLNLLNI--VPgfYGINSTDLMTDLYHKGVHTLVTDRPDL 297
Cdd:cd08567  220 TKELVDEAHALGLkvVP--WTVNDPEDMARLIDLGVDGIITDYPDL 263
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 49-152 2.55e-14

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: 70.81  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  49 FAHRG--GMAVR-PEQTQLAFDNAVANNLdGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLdagyHFK 125
Cdd:cd08585    7 IAHRGlhDRDAGiPENSLSAFRAAAEAGY-GIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRAL----RLL 81

                         90       100
                 ....*....|....*....|....*..
gi 499595374 126 DINGQFPyrghqkakilTFDELLKMYP 152
Cdd:cd08585   82 GTDEHIP----------TLDEVLELVA 98
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 45-164 3.71e-14

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: 70.80  E-value: 3.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  45 APYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKV---SDHRVS-----ELK 116
Cdd:cd08574    1 KPALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVADVFperAHERASmftwtDLQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499595374 117 RLDAGYHF--KD---INGQFPYRGHQKA---KILTFDELL---KMYpNMYINVDLKDAP 164
Cdd:cd08574   81 QLNAGQWFlkDDpfwTASSLSESDREEAgnqSIPSLAELLrlaKKH-NKSVIFDLRRPP 138
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 48-149 5.17e-14

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: 69.88  E-value: 5.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGYHFkdi 127
Cdd:cd08579    1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIGENG--- 77

                         90       100
                 ....*....|....*....|..
gi 499595374 128 ngqfpyrghQKAKILTFDELLK 149
Cdd:cd08579   78 ---------HGAKIPSLDEYLA 90
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 48-194 5.55e-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: 66.97  E-value: 5.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKVSDHRVSELKRLDAGYhfkdi 127
Cdd:cd08581    1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVAE----- 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499595374 128 NGQFPYRGHQkAKILTFDEL---LKMYPNMYINVDLK-DAPDSYEGTVAPTKMYEDiINNQAQDRVLVtSF 194
Cdd:cd08581   76 PARFGSRFAG-EPLPSLAAVvqwLAQHPQVTLFVEIKtESLDRFGLERVVDKVLRA-LPAVAAQRVLI-SF 143
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 48-148 4.02e-12

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: 65.88  E-value: 4.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  48 IFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTN------------GSGKVSDHRVSEL 115
Cdd:cd08600    3 IIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNvaekfpdrkrkdGRYYVIDFTLDEL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 499595374 116 KRLDAGYHFKDING----QFPYR---GHQKAKILTFDELL 148
Cdd:cd08600   83 KSLSVTERFDIENGkkvqVYPNRfplWKSDFKIHTLEEEI 122
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 46-149 2.20e-11

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: 63.47  E-value: 2.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  46 PYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNgsgkVSDHR-------------- 111
Cdd:cd08602    1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTD----VADHPefadrkttktvdgv 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499595374 112 -----------VSELKRLDAGYHFKDI----NGQFPyrghqkakILTFDELLK 149
Cdd:cd08602   77 nvtgwftedftLAELKTLRARQRLPYRdqsyDGQFP--------IPTFEEIIA 121
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 46-161 4.04e-11

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: 62.10  E-value: 4.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  46 PYIFAHRG-GMAVR-PEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFH---DATVDRTT-----NGSGKVSDHRVSEL 115
Cdd:cd08564    4 PIIVGHRGaGCSTLyPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteDDTNPDTSiqlddSGFKNINDLSLDEI 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499595374 116 KRLDAGYHF-KDINGQFPYRGHqkaKILTFDELLKMY-PNMYINVDLK 161
Cdd:cd08564   84 TRLHFKQLFdEKPCGADEIKGE---KIPTLEDVLVTFkDKLKYNIELK 128
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 43-102 3.99e-10

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: 59.89  E-value: 3.99e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  43 GKAPYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTN 102
Cdd:cd08610   20 GPKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTN 79
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 50-195 5.34e-09

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: 54.75  E-value: 5.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  50 AHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSgkvSDHRVSELKRLDAGYHFkding 129
Cdd:cd08555    3 SHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGI---LPPTLEEVLELIADYLK----- 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499595374 130 qfpYRGhqkakiltfdellkmyPNMYINVDLKDAPDSYEGTVAPT-KMYEDIINNQAQDRVLVTSFY 195
Cdd:cd08555   75 ---NPD----------------YTIILSLEIKQDSPEYDEFLAKVlKELRVYFDYDLRGKVVLSSFN 122
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 46-124 7.79e-09

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: 55.70  E-value: 7.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  46 PYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGKV--------SDHRVSELKR 117
Cdd:cd08609   27 PALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKDVFpgrdaagsNNFTWTELKT 106


                 ....*..
gi 499595374 118 LDAGYHF 124
Cdd:cd08609  107 LNAGSWF 113
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 46-150 1.58e-08

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 55.06  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  46 PYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSGK------------VSDHRVS 113
Cdd:PRK11143  27 KIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAERfpdrarkdgryyAIDFTLD 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499595374 114 ELKRLDAGYHFKDINGQ----FPYR---GHQKAKILTFDELLKM 150
Cdd:PRK11143 107 EIKSLKFTEGFDIENGKkvqvYPGRfpmGKSDFRVHTFEEEIEF 150
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 45-124 3.61e-08

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE2 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 5 (GDPD5)) and their metazoan homologs. Mammalian GDE2 is transmembrane protein primarily expressed in mature neurons. It is a mammalian homolog of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Mammalian GDE2 selectively hydrolyzes glycerophosphocholine (GPC) and has been characterized as GPC-GDE (EC 3.1.4.2) that contributes to osmotic regulation of cellular GPC. Mammalian GDE2 functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE2 also plays a critical role for retinoid-induced neuronal outgrowth. The catalytic activity of GDPD domain is essential for mammalian GDE2 cellular function.


Pssm-ID: 176550  Cd Length: 351  Bit Score: 54.08  E-value: 3.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  45 APYIFAHRGGMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTTNGSG---KVSDHRVS-----ELK 116
Cdd:cd08608    1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRvfpERQYEDASmfnwtDLE 80


                 ....*...
gi 499595374 117 RLDAGYHF 124
Cdd:cd08608   81 RLNAGQWF 88
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 51-130 6.60e-05

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: 43.82  E-value: 6.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  51 HRG-------GMAVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATV---DRTTNGSGKVSDHRV-------S 113
Cdd:cd08607    5 HRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLrvsLKSKGDSDRDDLLEVpvkdltyE 84

                         90
                 ....*....|....*..
gi 499595374 114 ELKRLDAgYHFKDINGQ 130
Cdd:cd08607   85 QLKLLKL-FHISALKVK 100
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 51-190 1.26e-04

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: 43.04  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  51 HRG-GM-------AVRPEQTQLAFDNAVANNLDGFETDVRLTKDEKLIVFHDATV-----DRTTNGSGKVSDHRV----- 112
Cdd:cd08572    5 HRGlGKnyasgslAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTIsvsekSKTGSDEGELIEVPIhdltl 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 113 SELKRLDaGYHFKDINGQFPYRGHQKAKIL-----------TFDELL-KMYPNMYINVDLK-DAPDSYEGTVAPTkmYED 179
Cdd:cd08572   85 EQLKELG-LQHISALKRKALTRKAKGPKPNpwgmdehdpfpTLQEVLeQVPKDLGFNIEIKyPQLLEDGEGELTP--YFE 161

                        170
                 ....*....|.
gi 499595374 180 IinNQAQDRVL 190
Cdd:cd08572  162 R--NAFVDTIL 170
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 65-197 6.15e-04

Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases; This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues.


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 40.36  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374  65 AFDNAVANNLDGFETDVRLTKDEKLIVFHDATVDRTtngsgkvsDHRVSELKRLDAGYHFKDINGQFPYRGHQKAKILTF 144
Cdd:cd08583   20 AFEHNYKKGYRVFEVDLSLTSDGVLVARHSWDESLL--------KQLGLPTSKNTKPLSYEEFKSKKIYGKYTPMDFKDV 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595374 145 DELLKMYPNMYINVDLKDAPDsyegtVAPTKMYEDIInNQAQ-------DRVLVTSFYKE 197
Cdd:cd08583   92 IDLLKKYPDVYIVTDTKQDDD-----NDIKKLYEYIV-KEAKevdpdllDRVIPQIYNEE 145
 
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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