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Conserved domains on  [gi|491003178|ref|WP_004864899|]
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MULTISPECIES: glycerophosphodiester phosphodiesterase [Raoultella]

Protein Classification

glycerophosphoryl diester phosphodiesterase( domain architecture ID 11485225)

glycerophosphodiester phosphodiesterase catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols in a Ca2+-dependent manner

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 1-356 0e+00

glycerophosphodiester phosphodiesterase; Provisional


:

Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 706.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178   1 MKTVATTLMTAILLAGSTlSFSASAADKLVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLD 80
Cdd:PRK11143   1 LKNLSLALLLAALLAGSA-AAAADSAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  81 RVTDVAERFPQRARQDGRFYAIDFTLAEIKSLRFSEGFEPKDGKNIQTFPGRFPMGKSDFRIHTFEEEIEFVQGLNHSTG 160
Cdd:PRK11143  80 RVTDVAERFPDRARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKKVQVYPGRFPMGKSDFRVHTFEEEIEFIQGLNHSTG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 161 KNIGIYPEIKAPWFHHQEGKDIAVSVLQVLKKYGYTRKQDKIYLQCFDANELKRIKHELEPKMGMDLKLVQLIAYTDWNE 240
Cdd:PRK11143 160 KNIGIYPEIKAPWFHHQEGKDIAAKVLEVLKKYGYTGKDDKVYLQCFDANELKRIKNELEPKMGMDLKLVQLIAYTDWNE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 241 TRQRQADGKWVNYSYDWMFKPGAMTQIAQYADGIGPDYHMLVAANARPGQVALNEMVKEAHRQRLVVHPYTVRADQLPDY 320
Cdd:PRK11143 240 TQEKQPDGKWVNYNYDWMFKPGAMKEVAKYADGIGPDYHMLVDETSTPGNIKLTGMVKEAHQAKLVVHPYTVRADQLPEY 319

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 491003178 321 VTDVNQLFDLLYHQADVDGLFTDFPDKAVQFLKAKH 356
Cdd:PRK11143 320 ATDVNQLYDILYNQAGVDGVFTDFPDKAVKFLNKQK 355
 
Name Accession Description Interval E-value
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 1-356 0e+00

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 706.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178   1 MKTVATTLMTAILLAGSTlSFSASAADKLVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLD 80
Cdd:PRK11143   1 LKNLSLALLLAALLAGSA-AAAADSAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  81 RVTDVAERFPQRARQDGRFYAIDFTLAEIKSLRFSEGFEPKDGKNIQTFPGRFPMGKSDFRIHTFEEEIEFVQGLNHSTG 160
Cdd:PRK11143  80 RVTDVAERFPDRARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKKVQVYPGRFPMGKSDFRVHTFEEEIEFIQGLNHSTG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 161 KNIGIYPEIKAPWFHHQEGKDIAVSVLQVLKKYGYTRKQDKIYLQCFDANELKRIKHELEPKMGMDLKLVQLIAYTDWNE 240
Cdd:PRK11143 160 KNIGIYPEIKAPWFHHQEGKDIAAKVLEVLKKYGYTGKDDKVYLQCFDANELKRIKNELEPKMGMDLKLVQLIAYTDWNE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 241 TRQRQADGKWVNYSYDWMFKPGAMTQIAQYADGIGPDYHMLVAANARPGQVALNEMVKEAHRQRLVVHPYTVRADQLPDY 320
Cdd:PRK11143 240 TQEKQPDGKWVNYNYDWMFKPGAMKEVAKYADGIGPDYHMLVDETSTPGNIKLTGMVKEAHQAKLVVHPYTVRADQLPEY 319

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 491003178 321 VTDVNQLFDLLYHQADVDGLFTDFPDKAVQFLKAKH 356
Cdd:PRK11143 320 ATDVNQLYDILYNQAGVDGVFTDFPDKAVKFLNKQK 355
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 28-346 0e+00

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: 579.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  28 KLVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFPQRARQDGRFYAIDFTLA 107
Cdd:cd08600    1 KIIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKRKDGRYYVIDFTLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 108 EIKSLRFSEGFEPKDGKNIQTFPGRFPMGKSDFRIHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFHHQEGKDIAVSVL 187
Cdd:cd08600   81 ELKSLSVTERFDIENGKKVQVYPNRFPLWKSDFKIHTLEEEIELIQGLNKSTGKNVGIYPEIKAPWFHHQEGKDIAAATL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 188 QVLKKYGYTRKQDKIYLQCFDANELKRIKHELEPKMGMDLKLVQLIAYTDWNETRQRQaDGKWVNYSYDWMFKPGAMTQI 267
Cdd:cd08600  161 EVLKKYGYTSKNDKVYLQTFDPNELKRIKNELLPKMGMDLKLVQLIAYTDWGETQEKD-PGGWVNYDYDWMFTKGGLKEI 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003178 268 AQYADGIGPDYHMLVAANARPGQVALNEMVKEAHRQRLVVHPYTVRADQLPDYVTDVNQLFDLLYHQADVDGLFTDFPD 346
Cdd:cd08600  240 AKYADGVGPWYSMIIEEKSSKGNIVLTDLVKDAHEAGLEVHPYTVRKDALPEYAKDADQLLDALLNKAGVDGVFTDFPD 318
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
29-354 5.44e-66

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 208.57  E-value: 5.44e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERfpqrarqdgrfyAIDFTLAE 108
Cdd:COG0584    4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGR------------VADLTLAE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 109 IKSLRFsegfepkdgkniqtfpGRFPMGKSDfRIHTFEEEIEFVqglnhstGKNIGIYPEIKAPWFHHQegkDIAVSVLQ 188
Cdd:COG0584   72 LRQLDA----------------GSGPDFAGE-RIPTLEEVLELV-------PGDVGLNIEIKSPPAAEP---DLAEAVAA 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 189 VLKKYGYtrkQDKIYLQCFDANELKRIKhELEPkmgmDLKLVQLIAYTDWNETRQRQADGkwvnysydwmfkpgamtqia 268
Cdd:COG0584  125 LLKRYGL---EDRVIVSSFDPEALRRLR-ELAP----DVPLGLLVEELPADPLELARALG-------------------- 176

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 269 qyADGIGPDYHMLVAanarpgqvalnEMVKEAHRQRLVVHPYTVRADQlpdyvtDVNQLFDLlyhqaDVDGLFTDFPDKA 348
Cdd:COG0584  177 --ADGVGPDYDLLTP-----------ELVAAAHAAGLKVHVWTVNDPE------EMRRLLDL-----GVDGIITDRPDLL 232


                 ....*.
gi 491003178 349 VQFLKA 354
Cdd:COG0584  233 RAVLRE 238
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 33-347 2.07e-62

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: 199.55  E-value: 2.07e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178   33 HRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAErfpqrarqdgrfYAIDFTLAEIKSL 112
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG------------YVRDLTLEELKRL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  113 RfsegfePKDGKNIQTFPGRFPmgksdfrIHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFhHQEGKDIAVSVLQVLKK 192
Cdd:pfam03009  69 D------IGAGNSGPLSGERVP-------FPTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEE-GLIVKDLLLSVDEILAK 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  193 YGytrKQDKIYLQCFDANELKRIKhELEPKmgmdLKLVQLIAYTDWNETRqrqadgkWVNYSYDWMFKPGAMTQIAQYAD 272
Cdd:pfam03009 135 KA---DPRRVIFSSFNPDELKRLR-ELAPK----LPLVFLSSGRAYAEAD-------LLERAAAFAGAPALLGEVALVDE 199

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003178  273 GIgpdyhmlvaanarpgqvalNEMVKEAHRQRLVVHPYTVRadqlpdyvtdvNQLFDLLYHQADVDGLFTDFPDK 347
Cdd:pfam03009 200 AL-------------------PDLVKRAHARGLVVHVWTVN-----------NEDEMKRLLELGVDGVITDRPDT 244
 
Name Accession Description Interval E-value
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 1-356 0e+00

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 706.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178   1 MKTVATTLMTAILLAGSTlSFSASAADKLVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLD 80
Cdd:PRK11143   1 LKNLSLALLLAALLAGSA-AAAADSAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  81 RVTDVAERFPQRARQDGRFYAIDFTLAEIKSLRFSEGFEPKDGKNIQTFPGRFPMGKSDFRIHTFEEEIEFVQGLNHSTG 160
Cdd:PRK11143  80 RVTDVAERFPDRARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKKVQVYPGRFPMGKSDFRVHTFEEEIEFIQGLNHSTG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 161 KNIGIYPEIKAPWFHHQEGKDIAVSVLQVLKKYGYTRKQDKIYLQCFDANELKRIKHELEPKMGMDLKLVQLIAYTDWNE 240
Cdd:PRK11143 160 KNIGIYPEIKAPWFHHQEGKDIAAKVLEVLKKYGYTGKDDKVYLQCFDANELKRIKNELEPKMGMDLKLVQLIAYTDWNE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 241 TRQRQADGKWVNYSYDWMFKPGAMTQIAQYADGIGPDYHMLVAANARPGQVALNEMVKEAHRQRLVVHPYTVRADQLPDY 320
Cdd:PRK11143 240 TQEKQPDGKWVNYNYDWMFKPGAMKEVAKYADGIGPDYHMLVDETSTPGNIKLTGMVKEAHQAKLVVHPYTVRADQLPEY 319

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 491003178 321 VTDVNQLFDLLYHQADVDGLFTDFPDKAVQFLKAKH 356
Cdd:PRK11143 320 ATDVNQLYDILYNQAGVDGVFTDFPDKAVKFLNKQK 355
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 28-346 0e+00

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: 579.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  28 KLVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFPQRARQDGRFYAIDFTLA 107
Cdd:cd08600    1 KIIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKRKDGRYYVIDFTLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 108 EIKSLRFSEGFEPKDGKNIQTFPGRFPMGKSDFRIHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFHHQEGKDIAVSVL 187
Cdd:cd08600   81 ELKSLSVTERFDIENGKKVQVYPNRFPLWKSDFKIHTLEEEIELIQGLNKSTGKNVGIYPEIKAPWFHHQEGKDIAAATL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 188 QVLKKYGYTRKQDKIYLQCFDANELKRIKHELEPKMGMDLKLVQLIAYTDWNETRQRQaDGKWVNYSYDWMFKPGAMTQI 267
Cdd:cd08600  161 EVLKKYGYTSKNDKVYLQTFDPNELKRIKNELLPKMGMDLKLVQLIAYTDWGETQEKD-PGGWVNYDYDWMFTKGGLKEI 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003178 268 AQYADGIGPDYHMLVAANARPGQVALNEMVKEAHRQRLVVHPYTVRADQLPDYVTDVNQLFDLLYHQADVDGLFTDFPD 346
Cdd:cd08600  240 AKYADGVGPWYSMIIEEKSSKGNIVLTDLVKDAHEAGLEVHPYTVRKDALPEYAKDADQLLDALLNKAGVDGVFTDFPD 318
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 28-345 4.26e-152

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: 429.77  E-value: 4.26e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  28 KLVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFPQRARQDGRFYAIDFTLA 107
Cdd:cd08559    1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVAEHFPFRGRKDTGYFVIDFTLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 108 EIKSLRFSEGFEpkdgkniQTFPGRFPMGKSDFRIHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFHHQEGKDIAVSVL 187
Cdd:cd08559   81 ELKTLRAGSWFN-------QRYPERAPSYYGGFKIPTLEEVIELAQGLNKSTGRNVGIYPETKHPTFHKQEGPDIEEKLL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 188 QVLKKYGYTRKQDKIYLQCFDANELKRIKHELepkmgMDLKLVQLIAYTDWNETRqrqadgkwVNYSYDWMFKPGAMTQI 267
Cdd:cd08559  154 EVLKKYGYTGKNDPVFIQSFEPESLKRLRNET-----PDIPLVQLIDYGDWAETD--------KKYTYAWLTTDAGLKEI 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491003178 268 AQYADGIGPDYHMLVAANARpGQVALNEMVKEAHRQRLVVHPYTVRADQLPdYVTDVNQLFDLLYHQADVDGLFTDFP 345
Cdd:cd08559  221 AKYADGIGPWKSLIIPEDSN-GLLVPTDLVKDAHKAGLLVHPYTFRNENLF-LAPDFKQDMDALYNAAGVDGVFTDFP 296
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 29-345 9.83e-85

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: 259.15  E-value: 9.83e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAER--FPQRARQ---DGR----F 99
Cdd:cd08602    2 LVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHpeFADRKTTktvDGVnvtgW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 100 YAIDFTLAEIKSLRFSEGFEPKDgkniQTFPGRFPmgksdfrIHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFHHQE- 178
Cdd:cd08602   82 FTEDFTLAELKTLRARQRLPYRD----QSYDGQFP-------IPTFEEIIALAKAASAATGRTVGIYPEIKHPTYFNAPl 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 179 GKDIAVSVLQVLKKYGYTRKQDKIYLQCFDANELKRIKHElepkmgMDLKLVQLIAytdwNETRQRQADGKWVNYSYDWM 258
Cdd:cd08602  151 GLPMEDKLLETLKKYGYTGKKAPVFIQSFEVTNLKYLRNK------TDLPLVQLID----DATIPPQDTPEGDSRTYADL 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 259 FKPGAMTQIAQYADGIGPDYHMLVAANARPGQVALNEMVKEAHRQRLVVHPYTVRADQ---LPDYVTDVNQLFDLLYHqA 335
Cdd:cd08602  221 TTDAGLKEIATYADGIGPWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNENtflPPDFFGDPYAEYRAFLD-A 299

                        330
                 ....*....|
gi 491003178 336 DVDGLFTDFP 345
Cdd:cd08602  300 GVDGLFTDFP 309
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
29-354 5.44e-66

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 208.57  E-value: 5.44e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERfpqrarqdgrfyAIDFTLAE 108
Cdd:COG0584    4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGR------------VADLTLAE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 109 IKSLRFsegfepkdgkniqtfpGRFPMGKSDfRIHTFEEEIEFVqglnhstGKNIGIYPEIKAPWFHHQegkDIAVSVLQ 188
Cdd:COG0584   72 LRQLDA----------------GSGPDFAGE-RIPTLEEVLELV-------PGDVGLNIEIKSPPAAEP---DLAEAVAA 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 189 VLKKYGYtrkQDKIYLQCFDANELKRIKhELEPkmgmDLKLVQLIAYTDWNETRQRQADGkwvnysydwmfkpgamtqia 268
Cdd:COG0584  125 LLKRYGL---EDRVIVSSFDPEALRRLR-ELAP----DVPLGLLVEELPADPLELARALG-------------------- 176

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 269 qyADGIGPDYHMLVAanarpgqvalnEMVKEAHRQRLVVHPYTVRADQlpdyvtDVNQLFDLlyhqaDVDGLFTDFPDKA 348
Cdd:COG0584  177 --ADGVGPDYDLLTP-----------ELVAAAHAAGLKVHVWTVNDPE------EMRRLLDL-----GVDGIITDRPDLL 232


                 ....*.
gi 491003178 349 VQFLKA 354
Cdd:COG0584  233 RAVLRE 238
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 33-347 2.07e-62

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: 199.55  E-value: 2.07e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178   33 HRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAErfpqrarqdgrfYAIDFTLAEIKSL 112
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG------------YVRDLTLEELKRL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  113 RfsegfePKDGKNIQTFPGRFPmgksdfrIHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFhHQEGKDIAVSVLQVLKK 192
Cdd:pfam03009  69 D------IGAGNSGPLSGERVP-------FPTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEE-GLIVKDLLLSVDEILAK 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  193 YGytrKQDKIYLQCFDANELKRIKhELEPKmgmdLKLVQLIAYTDWNETRqrqadgkWVNYSYDWMFKPGAMTQIAQYAD 272
Cdd:pfam03009 135 KA---DPRRVIFSSFNPDELKRLR-ELAPK----LPLVFLSSGRAYAEAD-------LLERAAAFAGAPALLGEVALVDE 199

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003178  273 GIgpdyhmlvaanarpgqvalNEMVKEAHRQRLVVHPYTVRadqlpdyvtdvNQLFDLLYHQADVDGLFTDFPDK 347
Cdd:pfam03009 200 AL-------------------PDLVKRAHARGLVVHVWTVN-----------NEDEMKRLLELGVDGVITDRPDT 244
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 29-353 1.05e-48

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: 164.41  E-value: 1.05e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFPQRarqdgrfyaiDFTLAE 108
Cdd:cd08601    2 AVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIERPGPVK----------DYTLAE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 109 IKSLRFSEGFEpkdgkniQTFPGRFPMGKSDFRIHTFEEEIEFVqglnhstGKNIGIYPEIKAPWFHhqegKDIAVSVLQ 188
Cdd:cd08601   72 IKQLDAGSWFN-------KAYPEYARESYSGLKVPTLEEVIERY-------GGRANYYIETKSPDLY----PGMEEKLLA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 189 VLKKYGYTR---KQDKIYLQCFDANELKRIkHELEPkmgmDLKLVQLIAYTDWNETRQrqadgKWVNysydwmfkpgamt 265
Cdd:cd08601  134 TLDKYGLLTdnlKNGQVIIQSFSKESLKKL-HQLNP----NIPLVQLLWYGEGAETYD-----KWLD------------- 190

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 266 QIAQYADGIGPDYHMLVAanarpgqvalnEMVKEAHRQRLVVHPYTVradqlpdyvtDVNQLFDLLYhQADVDGLFTDFP 345
Cdd:cd08601  191 EIKEYAIGIGPSIADADP-----------WMVHLIHKKGLLVHPYTV----------NEKADMIRLI-NWGVDGMFTNYP 248


                 ....*...
gi 491003178 346 DKAVQFLK 353
Cdd:cd08601  249 DRLKEVLK 256
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 30-352 4.00e-29

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: 112.74  E-value: 4.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFpqrarqdgrfyaIDFTLAEI 109
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPV------------ADLTLAEL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 110 KSLRFSEGFEPKDGkniQTFPGRfpmgKSDFRIHTFEEEIEFVQGLNhstgKNIgiypEIKapwfhhQEGKDIAVSVLQV 189
Cdd:cd08561   69 RRLDAGYHFTDDGG---RTYPYR----GQGIRIPTLEELFEAFPDVR----LNI----EIK------DDGPAAAAALADL 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 190 LKKYGytrKQDKIYLQCFDANELKRIkHELEPK----MGMDlKLVQLIAytdwnetrqrqadgkWVNYSYDWMFKPGAMT 265
Cdd:cd08561  128 IERYG---AQDRVLVASFSDRVLRRF-RRLCPRvatsAGEG-EVAAFVL---------------ASRLGLGSLYSPPYDA 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 266 -QIaqyadgigPDYHMLVaanarpgQVALNEMVKEAHRQRLVVHPYTVradqlpDYVTDVNQLFDLlyhqaDVDGLFTDF 344
Cdd:cd08561  188 lQI--------PVRYGGV-------PLVTPRFVRAAHAAGLEVHVWTV------NDPAEMRRLLDL-----GVDGIITDR 241


                 ....*...
gi 491003178 345 PDKAVQFL 352
Cdd:cd08561  242 PDLLLEVL 249
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 29-345 1.58e-28

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: 110.72  E-value: 1.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTdvaerfpqrarqDGRFYAIDFTLAE 108
Cdd:cd08563    2 LIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTT------------NGKGYVKDLTLEE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 109 IKSLRFSEGFEPKDGKNiqtfpgrfpmgksdfRIHTFEEEIEFVQGlnhsTGKNIGIypEIKAPWFHHqegKDIAVSVLQ 188
Cdd:cd08563   70 LKKLDAGSWFDEKFTGE---------------KIPTLEEVLDLLKD----KDLLLNI--EIKTDVIHY---PGIEKKVLE 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 189 VLKKYGytrKQDKIYLQCFDANELKRIKhELEPKmgmdLKlvqlIAYTDWnetrqrqadgkwvnysyDWMFKPGAMTQIA 268
Cdd:cd08563  126 LVKEYN---LEDRVIFSSFNHESLKRLK-KLDPK----IK----LALLYE-----------------TGLQDPKDYAKKI 176

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491003178 269 QyADGIGPDYHMLVAanarpgqvalnEMVKEAHRQRLVVHPYTVRADqlpdyvTDVNQLFDLlyhqaDVDGLFTDFP 345
Cdd:cd08563  177 G-ADSLHPDFKLLTE-----------EVVEELKKRGIPVRLWTVNEE------EDMKRLKDL-----GVDGIITNYP 230
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 30-344 1.83e-28

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: 109.28  E-value: 1.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDhyldrvtdvaerfpqrarqdgrfyaidftlaei 109
Cdd:cd08556    1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 110 kslrfsegfepkdgkniqtfpgrfpmgksdfrIHTFEEEIEFVQGlnhstgkNIGIYPEIKAPWFHHqegkDIAVSVLQV 189
Cdd:cd08556   48 --------------------------------IPTLEEVLELVKG-------GVGLNIELKEPTRYP----GLEAKVAEL 84

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 190 LKKYGytrKQDKIYLQCFDANELKRIKhelepKMGMDLKLVQLIAYTDWNETRQRQAdgkwvnysydwmfkpgamtqIAQ 269
Cdd:cd08556   85 LREYG---LEERVVVSSFDHEALRALK-----ELDPEVPTGLLVDKPPLDPLLAELA--------------------RAL 136

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003178 270 YADGIGPDYHMLVAanarpgqvalnEMVKEAHRQRLVVHPYTVRadqlpdyvtDVNQLFDLLyhQADVDGLFTDF 344
Cdd:cd08556  137 GADAVNPHYKLLTP-----------ELVRAAHAAGLKVYVWTVN---------DPEDARRLL--ALGVDGIITDD 189
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 30-344 7.22e-28

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: 107.52  E-value: 7.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDvaerfpqrarqdgrfyaidftlaei 109
Cdd:cd08555    1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTA------------------------- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 110 kslrfsegfepkdgkniqtfpgrfpmgksDFRIHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFhhqEGKDIAVSVLQV 189
Cdd:cd08555   56 -----------------------------GILPPTLEEVLELIADYLKNPDYTIILSLEIKQDSP---EYDEFLAKVLKE 103

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 190 LKKYGYTRKQDKIYLQCFDAnelkrikhelepkmgmdlklvqliaytdwnetrqrqadgkwvnysydwmfkpgamtqiaq 269
Cdd:cd08555  104 LRVYFDYDLRGKVVLSSFNA------------------------------------------------------------ 123

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003178 270 yadgIGPDYHmlvaaNARPGQVALNEMVKEAHRQRLVVHPYTVRadqlpdyvtDVNQLFDLLYhQADVDGLFTDF 344
Cdd:cd08555  124 ----LGVDYY-----NFSSKLIKDTELIASANKLGLLSRIWTVN---------DNNEIINKFL-NLGVDGLITDF 179
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 30-346 1.08e-27

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: 109.32  E-value: 1.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDrvtdvaerfPQRAR-QDGRFYAI------ 102
Cdd:cd08567    3 LQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLN---------PDITRdPDGAWLPYegpaly 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 103 DFTLAEIKSL-----RFSEGFEPKdgkniqtFPGRFPMgkSDFRIHTFEEEIEFVQglnHSTGKNIGIYPEIKAPWFH-- 175
Cdd:cd08567   74 ELTLAEIKQLdvgekRPGSDYAKL-------FPEQIPV--PGTRIPTLEEVFALVE---KYGNQKVRFNIETKSDPDRdi 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 176 -HQEGKDIAVSVLQVLKKYGytrKQDKIYLQCFDANELKRIKhELEPkmgmDLKLVQLIaytdwnetrqrqADGKWVNYs 254
Cdd:cd08567  142 lHPPPEEFVDAVLAVIRKAG---LEDRVVLQSFDWRTLQEVR-RLAP----DIPTVALT------------EETTLGNL- 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 255 ydwmfkPGAMTQIAqyADGIGPDYHMLVAanarpgqvalnEMVKEAHRQRLVVHPYTVRADQLPDYVTDvnqlfdllyhq 334
Cdd:cd08567  201 ------PRAAKKLG--ADIWSPYFTLVTK-----------ELVDEAHALGLKVVPWTVNDPEDMARLID----------- 250

                        330
                 ....*....|..
gi 491003178 335 ADVDGLFTDFPD 346
Cdd:cd08567  251 LGVDGIITDYPD 262
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 30-346 4.85e-25

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: 101.24  E-value: 4.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVaerfpqrarqDGRFYaiDFTLAEI 109
Cdd:cd08582    1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGG----------DGAVS--DLTLAEL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 110 KSLRFSEGFEPKDGKNiqtfpgrfpmgksdfRIHTFEEEIEFVqglnhsTGKNIGIYPEIKAPWFhhqeGKDIAVSVLQV 189
Cdd:cd08582   69 RKLDIGSWKGESYKGE---------------KVPTLEEYLAIV------PKYGKKLFIEIKHPRR----GPEAEEELLKL 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 190 LKKYGYTRKQdkIYLQCFDANELKRIKhELEPkmgmDLKLVQLiaytdwnetrqrqadgkwVNYSYDWMFKPGamtqIAQ 269
Cdd:cd08582  124 LKESGLLPEQ--IVIISFDAEALKRVR-ELAP----TLETLWL------------------RNYKSPKEDPRP----LAK 174

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491003178 270 YADGIGPDYHMLVAANArpgqvalnEMVKEAHRQRLVVHPYTVradqlpDYVTDVNQLFDLlyhqaDVDGLFTDFPD 346
Cdd:cd08582  175 SGGAAGLDLSYEKKLNP--------AFIKALRDAGLKLNVWTV------DDAEDAKRLIEL-----GVDSITTNRPG 232
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 29-194 6.99e-19

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: 84.96  E-value: 6.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVaerfpqrarqDGrfYAIDFTLAE 108
Cdd:cd08575    2 LHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGG----------SG--LVSDLTYAE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 109 IKSLRFSEGFEPKDGKniqtfpGRFPMGKSDFRIHTFEEEI-EFvqglnhstgKNIGIYPEIKAPwfhhqEGKDIAVSVL 187
Cdd:cd08575   70 LPPLDAGYGYTFDGGK------TGYPRGGGDGRIPTLEEVFkAF---------PDTPINIDIKSP-----DAEELIAAVL 129


                 ....*..
gi 491003178 188 QVLKKYG 194
Cdd:cd08575  130 DLLEKYK 136
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 29-345 1.50e-18

Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase (GDPD) domain present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play an important role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens.


Pssm-ID: 176513  Cd Length: 302  Bit Score: 84.64  E-value: 1.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFPQRAR--------QDGRFy 100
Cdd:cd08571    2 LVIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPKRKKtyvvegqsTSGIF- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 101 AIDFTLAEIKSLRfsegfePKDGkNIQTFPGRFPMGKSDFRIHTFEeeiEFVQGLNHSTGknIGIYPEIK-APWFHHQEG 179
Cdd:cd08571   81 SFDLTWAEIQTLK------PIIS-NPFSVLFRNPRNDNAGKILTLE---DFLTLAKPKSL--SGVWINVEnAAFLAEHKG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 180 KDIAVSVLQVLKKYGYTRKQDKIYLQCFDANELKRIKHELEPkmgmdlKLVQLIAYTDWNETrqrqadgkwvnysyDWMF 259
Cdd:cd08571  149 LLSVDAVLTSLSKAGYDQTAKKVYISSPDSSVLKSFKKRVGT------KLVFRVLDVDDTEP--------------DTLL 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 260 KpgAMTQIAQYADGI----------GPDYHMLVAANArpgqvalnemVKEAHRQRLVVHPYTVRADQLP---DYVTD-VN 325
Cdd:cd08571  209 S--NLTEIKKFASGVlvpksyiwpvDSDSFLTPQTSV----------VQDAHKAGLEVYVSGFANEFVSlayDYSADpTL 276

                        330       340
                 ....*....|....*....|
gi 491003178 326 QLFDLLYHQADVDGLFTDFP 345
Cdd:cd08571  277 EILSFVGNGNSVDGVITDFP 296
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 29-239 2.11e-18

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: 83.12  E-value: 2.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGASGYL-PEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTdvaerfpqrarqDGRFYAIDFTLA 107
Cdd:cd08566    1 LVVAHRGGWGAGaPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTT------------NGKGKVSDLTLA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 108 EIKSLRFSEGFEPkdgkniqtfpgrfpmgKSDFRIHTFEEEIEFVQGlnhstgkNIGIYPEIKapWFHHQEgkdiavsVL 187
Cdd:cd08566   69 EIRKLRLKDGDGE----------------VTDEKVPTLEEALAWAKG-------KILLNLDLK--DADLDE-------VI 116

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 188 QVLKKYGYtrkQDKIYLQCFDANELKRIkHELEPKM--------GMDLKLVQLIAYTDWN 239
Cdd:cd08566  117 ALVKKHGA---LDQVIFKSYSEEQAKEL-RALAPEVmlmpivrdAEDLDEEEARAIDALN 172
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 30-345 5.86e-18

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: 81.50  E-value: 5.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDvaerfpqrarQDGRFYaiDFTLAEI 109
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTN----------GSGAVT--ELTWAEL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 110 KSLRFSEGFEPKdgkniqtFPGRfpmgksdfRIHTFEEEIEFvqgLNHStgkNIGIYPEIKApwfHHQEGKDIAVSVLQV 189
Cdd:cd08562   69 AQLDAGSWFSPE-------FAGE--------PIPTLADVLEL---AREL---GLGLNLEIKP---DPGDEALTARVVAAA 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 190 LKKYGYTrkQDKIYLQCFDANELKRIkHELEPkmgmDLKLVQLiaYTDWNEtrqrqadgkwvnysyDWmfkpgaMTQIAQ 269
Cdd:cd08562  125 LRELWPH--ASKLLLSSFSLEALRAA-RRAAP----ELPLGLL--FDTLPA---------------DW------LELLAA 174

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491003178 270 Y-ADGIGPDYHMLVAANARpgqvalneMVKEAHRQRLVvhpYTVRADQLpdyvtdVNQLFDllyhqADVDGLFTDFP 345
Cdd:cd08562  175 LgAVSIHLNYRGLTEEQVK--------ALKDAGYKLLV---YTVNDPAR------AAELLE-----WGVDAIFTDRP 229
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 30-223 1.39e-17

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: 80.28  E-value: 1.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVaerfpqrarqDGRFYaiDFTLAEI 109
Cdd:cd08579    1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGV----------NKKVW--DLTLEEL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 110 KSLRFSEGFepkdgkniqtFPGRFPmgksdfrihTFEEEIEFVQGLnhstgkNIGIYPEIKApwfHHQEGKDIavsVLQV 189
Cdd:cd08579   69 KKLTIGENG----------HGAKIP---------SLDEYLALAKGL------KQKLLIELKP---HGHDSPDL---VEKF 117

                        170       180       190
                 ....*....|....*....|....*....|....
gi 491003178 190 LKKYGYTRKQDKIYLQCFDANELKRIKhELEPKM 223
Cdd:cd08579  118 VKLYKQNLIENQHQVHSLDYRVIEKVK-KLDPKI 150
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 30-151 2.44e-15

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: 74.99  E-value: 2.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVaerfpqrarqDGRFYaiDFTLAEI 109
Cdd:cd08573    1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDG----------TGLVA--ELTWEEL 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491003178 110 KSLRFSegfepkdGKNIqtFPGRFPMGKsdfrIHTFEEEIEF 151
Cdd:cd08573   69 RKLNAA-------AKHR--LSSRFPGEK----IPTLEEAVKE 97
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 30-224 4.25e-15

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: 73.52  E-value: 4.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFPqrarqdgrfyaiDFTLAEI 109
Cdd:cd08581    1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLH------------ELEDAEL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 110 KSLRFSEGfepkdgkniQTFPGRFPmgksDFRIHTFEeeiEFVQGLNHSTGknIGIYPEIKAPWFHHQeGKDIAVS-VLQ 188
Cdd:cd08581   69 DSLRVAEP---------ARFGSRFA----GEPLPSLA---AVVQWLAQHPQ--VTLFVEIKTESLDRF-GLERVVDkVLR 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 491003178 189 VLkkygytrkqDKIYLQC----FDANELKRIKHELEPKMG 224
Cdd:cd08581  130 AL---------PAVAAQRvlisFDYDLLALAKQQGGPRTG 160
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 30-113 2.55e-14

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: 71.48  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFPqrarqdgrfyaIDFTLAEI 109
Cdd:cd08570    1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLII-----------DDSTWDEL 69


                 ....
gi 491003178 110 KSLR 113
Cdd:cd08570   70 SHLR 73
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 31-86 5.89e-13

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: 68.40  E-value: 5.89e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491003178  31 IAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVA 86
Cdd:cd08612   30 ISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVD 85
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 30-349 3.29e-12

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: 65.50  E-value: 3.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTdvaerfpqrarqDGRFYAIDFTLAEI 109
Cdd:cd08565    1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTT------------HGTGAVRDLTLAER 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 110 KSLRFSEGFEPKdgkniqtfpgrfpmgksdfrIHTFEEEIEFVQglnhstGKNIGIYPEIKaPWFHHQEGKDIAVSVLQV 189
Cdd:cd08565   69 KALRLRDSFGEK--------------------IPTLEEVLALFA------PSGLELHVEIK-TDADGTPYPGAAALAAAT 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 190 LKKYGYtrkQDKIYLQCFDANELKRIKHELEPKmgmdlklvqliaytdwnetRQRQADGKWVNYSydwmfkpGAMTQIAQ 269
Cdd:cd08565  122 LRRHGL---LERSVLTSFDPAVLTEVRKHPGVR-------------------TLGSVDEDMLERL-------GGELPFLT 172

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 270 Y----ADGIGPDyHMLVAANarpgqvalNEMVKEA-HRQRLVVhpYTVRADqlpdyvTDVNQLFDLlyhqaDVDGLFTDF 344
Cdd:cd08565  173 AtalkAHIVAVE-QSLLAAT--------WELVRAAvPGLRLGV--WTVNDD------SLIRYWLAC-----GVRQLTTDR 230


                 ....*
gi 491003178 345 PDKAV 349
Cdd:cd08565  231 PDLAL 235
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 31-345 2.06e-11

Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic phosphodiesterase (GlpQ) include uncharacterized proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and their hypothetical homologs. Members in this subfamily show 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: 176503  Cd Length: 356  Bit Score: 64.36  E-value: 2.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  31 IAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHY-LDRVTDVAERfPQRARQ-------------- 95
Cdd:cd08560   20 IGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSQCdLHTTTNILAI-PELAAKctqpftpanatkpa 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  96 DGRFYAIDFTLAEIKSLRFS-EGFEPKdgkniQTFPGRFPMGKSDFR---------IHTFEEEIEFVQGLnhstgkNIGI 165
Cdd:cd08560   99 SAECCTSDITLAEFKSLCGKmDASNPS-----ATTPEEYQNGTPDWRtdlyatcgtLMTHKESIALFKSL------GVKM 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 166 YPEIKAPWF-------HHQEgkDIAVSVLQVLKKYGYTrkQDKIYLQCFDANELKR-IKHelEPKMGMdlklvQLIAYTD 237
Cdd:cd08560  168 TPELKSPSVpmpfdgnYTQE--DYAQQMIDEYKEAGVP--PSRVWPQSFNLDDIFYwIKN--EPDFGR-----QAVYLDD 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 238 WNETRQRQADGKwvnysydwmfkpGAMTQIaqYADG---IGPDYHMLVAANARpGQVALNEMVKEAHRQRLVVHPYTV-R 313
Cdd:cd08560  237 RDDTADFPATWS------------PSMDEL--KARGvniIAPPIWMLVDPDEN-GKIVPSEYAKAAKAAGLDIITWTLeR 301

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 491003178 314 ADQLPD----YVT----------DVNQLFDLLYHQADVDGLFTDFP 345
Cdd:cd08560  302 SGPLASgggwYYQtiedvinndgDMYNVLDVLARDVGILGIFSDWP 347
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 29-210 9.34e-11

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: 61.91  E-value: 9.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGA------SGY--LPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLdRVTDvaERFPQRARQDGRFY 100
Cdd:cd08572    1 LVIGHRGLgknyasGSLagIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTI-SVSE--KSKTGSDEGELIEV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 101 AI-DFTLAEIKSLrfseGFEPKDGKNIQTFPGRFPMGKSDFRIHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPwFHHQEG 179
Cdd:cd08572   78 PIhDLTLEQLKEL----GLQHISALKRKALTRKAKGPKPNPWGMDEHDPFPTLQEVLEQVPKDLGFNIEIKYP-QLLEDG 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 491003178 180 KDIAVS----------VLQVLKKYGYTRkqdKIYLQCFDAN 210
Cdd:cd08572  153 EGELTPyfernafvdtILAVVFEHAGGR---RIIFSSFDPD 190
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 29-139 1.07e-10

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: 61.17  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFPQRARQDgrfyAIDFTLAE 108
Cdd:cd08574    3 ALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVADVFPERAHER----ASMFTWTD 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491003178 109 IKSLRFSEGFEPKDgkniqTFPGRFPMGKSD 139
Cdd:cd08574   79 LQQLNAGQWFLKDD-----PFWTASSLSESD 104
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 29-351 3.76e-10

Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 2 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play important an role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This CD includes domain II (the second GDPD domain of SHV3 and SVLs), which is necessary for SHV3 function.


Pssm-ID: 176546  Cd Length: 300  Bit Score: 60.04  E-value: 3.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAER-FPQRA------RQDGRFYA 101
Cdd:cd08604    2 LIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSkFSNRAttvpeiGSTSGIFT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 102 IDFTLAEIKSLRfsegfEPKDGKNIQTFPGRFPMGKSDFRIHTFEEEIEFVQGLNHStgkniGIYPEIK-APWFHHQEGK 180
Cdd:cd08604   82 FDLTWSEIQTLK-----PAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNKSLS-----GVLINVEnAAYLAEKKGL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 181 DIAVSVLQVLKKYGYTR-KQDKIYLQCFDANELKRIKHELEpkmgmdLKLVQLIAYTDWNETRQrqadgkwvnysydwmf 259
Cdd:cd08604  152 DVVDAVLDALTNAGYDNqTAQKVLIQSTDSSVLAAFKKQIS------YERVYVVDETIRDASDS---------------- 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 260 kpgAMTQIAQYADGIGPDYHMLVAANarpgQVALNEM---VKEAHRQRLVV-----------HPYTVRAD---QLPDYVT 322
Cdd:cd08604  210 ---SIEEIKKFADAVVIDRGSVFPVS----TSFLTRQtnvVEKLQSANLTVyvevlrnefvsLAFDFFADptvEINSYVQ 282

                        330       340
                 ....*....|....*....|....*....
gi 491003178 323 DVNqlfdllyhqadVDGLFTDFPDKAVQF 351
Cdd:cd08604  283 GAG-----------VDGFITEFPATAARY 300
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 30-203 8.59e-10

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: 59.17  E-value: 8.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFPQRARQDgrfyAIDFTLAEI 109
Cdd:cd08609   29 LVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKDVFPGRDAAG----SNNFTWTEL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 110 KSLRFSEGFEPKDgkniqTFPGRFPMGKSDFRIHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFHHQEGKDIAVSVLQV 189
Cdd:cd08609  105 KTLNAGSWFLERR-----PFWTLSSLSEEDRREADNQTVPSLSELLDLAKKHNVSIMFDLRNENNSHVFYSSFVFYTLET 179

                        170
                 ....*....|....
gi 491003178 190 LKKYGYTrkQDKIY 203
Cdd:cd08609  180 ILKLGIP--PDKVW 191
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 29-120 1.60e-09

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: 57.31  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGASGYLPEHTLPA--KAMAYaqGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVaerfpqrarqdgRFYAIDFTL 106
Cdd:cd08568    1 IILGHRGYRAKYPENTLEAfkKAIEY--GADGVELDVWLTKDGKLVVLHDENLKRVGGV------------DLKVKELTY 66

                         90
                 ....*....|....
gi 491003178 107 AEIKSLRFSEGFEP 120
Cdd:cd08568   67 KELKKLHPGGELIP 80
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 17-132 6.62e-09

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: 56.60  E-value: 6.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  17 STLSFSASAADKLvIAHRGASG-----------------YLPEH-----TLPAKAMAYAQGADYLEQDLVMTKDDRLVVL 74
Cdd:cd08613   14 SLLAPPPGGKPKL-LAHRGLAQtfdregvendtctaeriDPPTHdylenTIASMQAAFDAGADVVELDVHPTKDGEFAVF 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491003178  75 HDHYLDrvtdvaerfpqrARQDGRFYAIDFTLAEIKSLRFSEGFEPKDGKniqTFPGR 132
Cdd:cd08613   93 HDWTLD------------CRTDGSGVTRDHTMAELKTLDIGYGYTADGGK---TFPFR 135
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 30-118 1.75e-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: 55.24  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFPQRARQDGRFyaidFTLAEI 109
Cdd:cd08608    4 IIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYEDASM----FNWTDL 79


                 ....*....
gi 491003178 110 KSLRFSEGF 118
Cdd:cd08608   80 ERLNAGQWF 88
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 31-193 2.25e-08

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: 54.25  E-value: 2.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  31 IAHRG---ASGYLPEHTLPAKAMAYAqgADY-LEQDLVMTKDDRLVVLHDHYLDRVTDVAERFPqrarqdgrfyaiDFTL 106
Cdd:cd08585    7 IAHRGlhdRDAGIPENSLSAFRAAAE--AGYgIELDVQLTADGEVVVFHDDNLKRLTGVEGRVE------------ELTA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 107 AEIKSLRFsegfepkdgkniqtfpgrfpmGKSDFRIHTFEEEIEFVQGlnhstgkNIGIYPEIKApwfHHQEGKDIAVSV 186
Cdd:cd08585   73 AELRALRL---------------------LGTDEHIPTLDEVLELVAG-------RVPLLIELKS---CGGGDGGLERRV 121


                 ....*..
gi 491003178 187 LQVLKKY 193
Cdd:cd08585  122 LAALKDY 128
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 29-348 2.90e-08

Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 1 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play an important role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This family includes domain I, the first GDPD domain of SHV3 and SVLs.


Pssm-ID: 176545  Cd Length: 299  Bit Score: 54.31  E-value: 2.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGASGYLPEHTLPAK--AMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFPQRAR--------QDGR 98
Cdd:cd08603    2 LVIARGGFSGLFPDSSLFAYqfAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPKRKKtysvngvsTKGW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  99 FyAIDFTLAEIKSLrfsegfepkdgKNIQTFPGRFPMGKSDFRIHTFEEeiefVQGLNhstgKNIGIYPEIKAPWFHHQE 178
Cdd:cd08603   82 F-SVDFTLAELQQV-----------TLIQGIFSRTPIFDGQYPISTVED----VVTLA----KPEGLWLNVQHDAFYQQH 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 179 GKDIAVSVLQVLKKYGYTrkqdkiYLQCFDANELKRIKHELEPKmgmDLKLV-QLIAYTDWNETrqrqadgkwVNYSYDW 257
Cdd:cd08603  142 NLSMSSYLLSLSKTVKVD------YISSPEVGFLKSIGGRVGRN---GTKLVfRFLDKDDVEPS---------TNQTYGS 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178 258 MFKpgAMTQIAQYADGI----------GPDYHMLVAANArpgqvalnemVKEAHRQRLVVH----------PYTVRADQL 317
Cdd:cd08603  204 ILK--NLTFIKTFASGIlvpksyiwpvDSDQYLQPATSL----------VQDAHKAGLEVYasgfandfdiSYNYSYDPV 271

                        330       340       350
                 ....*....|....*....|....*....|..
gi 491003178 318 PDYVTDV-NQLFDllyhqadVDGLFTDFPDKA 348
Cdd:cd08603  272 AEYLSFVgNGNFS-------VDGVLSDFPITA 296
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 29-121 1.95e-07

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: 51.70  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGA--SGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFpqraRQDGRFYAIDFTL 106
Cdd:cd08564    5 IIVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHGTEDDTNPDTSIQL----DDSGFKNINDLSL 80

                         90
                 ....*....|....*
gi 491003178 107 AEIKSLRFSEGFEPK 121
Cdd:cd08564   81 DEITRLHFKQLFDEK 95
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 29-124 7.56e-07

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: 50.02  E-value: 7.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDvaerfpqrarQDGRFYaiDFTLAE 108
Cdd:cd08580    2 LIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTN----------GSGAVS--AYTAAQ 69

                         90
                 ....*....|....*.
gi 491003178 109 IKSLRFSEGFEPKDGK 124
Cdd:cd08580   70 LATLNAGYNFKPEGGY 85
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 30-104 2.04e-06

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: 48.72  E-value: 2.04e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTDVAERFPQRARQDGRFYAIDF 104
Cdd:cd08610   25 IIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNIGEVQPESACENPAFFNWDF 99
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 30-84 1.64e-04

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 42.62  E-value: 1.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491003178  30 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRVTD 84
Cdd:PRK09454  10 IVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSN 64
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 29-114 7.83e-04

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: 40.74  E-value: 7.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  29 LVIAHRG-------ASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLdrVTDVAERFPQRaRQDGRFYA 101
Cdd:cd08607    1 LDVGHRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTL--RVSLKSKGDSD-RDDLLEVP 77

                         90
                 ....*....|....
gi 491003178 102 I-DFTLAEIKSLRF 114
Cdd:cd08607   78 VkDLTYEQLKLLKL 91
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 30-198 2.31e-03

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: 39.35  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  30 VIAHRG--------ASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDRLVVLHDHYLDRV-TDVA------ERFPQRAR 94
Cdd:cd08606    4 VIGHRGlgkntaerKSLQLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETgTDVPihdltlEQFLHLSR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003178  95 QDgrfYAIDFTlaeikslrfSEGFEPKD-GKNIQtfpgrfpmgkSDFRihTFEeeiEFVQGLNHSTGKNIgiypEIKAPW 173
Cdd:cd08606   84 MK---YTVDFK---------KKGFKGNSrGHSIQ----------APFT--TLE---ELLKKLPKSVGFNI----ELKYPM 132

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 491003178 174 FHHQEGKDIAV----------SVLQVLKKYGYTRK 198
Cdd:cd08606  133 LHEAEEEEVAPvaielnafvdTVLEKVFDYGAGRN 167
 
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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