NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446701759|ref|WP_000779105|]
View 

MULTISPECIES: glycerophosphodiester phosphodiesterase [Enterobacteriaceae]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 5-358 0e+00

glycerophosphodiester phosphodiesterase; Provisional


:

Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 733.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759   5 LKNLSMAIMMSTIVMGSSAMAADSNEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDR 84
Cdd:PRK11143   1 LKNLSLALLLAALLAGSAAAAADSAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  85 VTDVADRFPDRARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKKVQTYPGRFPMGKSDFRVHTFEEEIEFVQGLNHSTGK 164
Cdd:PRK11143  81 VTDVAERFPDRARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKKVQVYPGRFPMGKSDFRVHTFEEEIEFIQGLNHSTGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 165 NIGIYPEIKAPWFHHQEGKDIAAKTLEVLKKYGYTGKDDKVYLQCFDADELKRIKNELEPKMGMELNLVQLIAYTDWNET 244
Cdd:PRK11143 161 NIGIYPEIKAPWFHHQEGKDIAAKVLEVLKKYGYTGKDDKVYLQCFDANELKRIKNELEPKMGMDLKLVQLIAYTDWNET 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 245 QQKQPDGSWVNYNYDWMFKPGAMKQVAEYADGIGPDYHMLIEETSQPGNIKLTGMVQDAQQNKLVVHPYTVRSDKLPEYT 324
Cdd:PRK11143 241 QEKQPDGKWVNYNYDWMFKPGAMKEVAKYADGIGPDYHMLVDETSTPGNIKLTGMVKEAHQAKLVVHPYTVRADQLPEYA 320

                        330       340       350
                 ....*....|....*....|....*....|....
gi 446701759 325 PDVNQLYDALYNKAGVNGLFTDFPDKAVKFLNKE 358
Cdd:PRK11143 321 TDVNQLYDILYNQAGVDGVFTDFPDKAVKFLNKQ 354
 
Name Accession Description Interval E-value
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 5-358 0e+00

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 733.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759   5 LKNLSMAIMMSTIVMGSSAMAADSNEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDR 84
Cdd:PRK11143   1 LKNLSLALLLAALLAGSAAAAADSAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  85 VTDVADRFPDRARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKKVQTYPGRFPMGKSDFRVHTFEEEIEFVQGLNHSTGK 164
Cdd:PRK11143  81 VTDVAERFPDRARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKKVQVYPGRFPMGKSDFRVHTFEEEIEFIQGLNHSTGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 165 NIGIYPEIKAPWFHHQEGKDIAAKTLEVLKKYGYTGKDDKVYLQCFDADELKRIKNELEPKMGMELNLVQLIAYTDWNET 244
Cdd:PRK11143 161 NIGIYPEIKAPWFHHQEGKDIAAKVLEVLKKYGYTGKDDKVYLQCFDANELKRIKNELEPKMGMDLKLVQLIAYTDWNET 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 245 QQKQPDGSWVNYNYDWMFKPGAMKQVAEYADGIGPDYHMLIEETSQPGNIKLTGMVQDAQQNKLVVHPYTVRSDKLPEYT 324
Cdd:PRK11143 241 QEKQPDGKWVNYNYDWMFKPGAMKEVAKYADGIGPDYHMLVDETSTPGNIKLTGMVKEAHQAKLVVHPYTVRADQLPEYA 320

                        330       340       350
                 ....*....|....*....|....*....|....
gi 446701759 325 PDVNQLYDALYNKAGVNGLFTDFPDKAVKFLNKE 358
Cdd:PRK11143 321 TDVNQLYDILYNQAGVDGVFTDFPDKAVKFLNKQ 354
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 31-349 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: 606.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  31 KIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPDRARKDGRYYAIDFTLD 110
Cdd:cd08600    1 KIIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKRKDGRYYVIDFTLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 111 EIKSLKFTEGFDIENGKKVQTYPGRFPMGKSDFRVHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFHHQEGKDIAAKTL 190
Cdd:cd08600   81 ELKSLSVTERFDIENGKKVQVYPNRFPLWKSDFKIHTLEEEIELIQGLNKSTGKNVGIYPEIKAPWFHHQEGKDIAAATL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 191 EVLKKYGYTGKDDKVYLQCFDADELKRIKNELEPKMGMELNLVQLIAYTDWNETQQKQPDGsWVNYNYDWMFKPGAMKQV 270
Cdd:cd08600  161 EVLKKYGYTSKNDKVYLQTFDPNELKRIKNELLPKMGMDLKLVQLIAYTDWGETQEKDPGG-WVNYDYDWMFTKGGLKEI 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446701759 271 AEYADGIGPDYHMLIEETSQPGNIKLTGMVQDAQQNKLVVHPYTVRSDKLPEYTPDVNQLYDALYNKAGVNGLFTDFPD 349
Cdd:cd08600  240 AKYADGVGPWYSMIIEEKSSKGNIVLTDLVKDAHEAGLEVHPYTVRKDALPEYAKDADQLLDALLNKAGVDGVFTDFPD 318
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 36-350 4.78e-70

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: 219.19  E-value: 4.78e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759   36 HRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADrfpdrarkdgryYAIDFTLDEIKSL 115
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG------------YVRDLTLEELKRL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  116 kftegfDIENGKKVQTYPGRFPmgksdfrVHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFhHQEGKDIAAKTLEVLKK 195
Cdd:pfam03009  69 ------DIGAGNSGPLSGERVP-------FPTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEE-GLIVKDLLLSVDEILAK 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  196 YgytGKDDKVYLQCFDADELKRIKNELepkmgMELNLVQLIAYTDWNETQqkqpdgsWVNYNYDWMFKPGAMKQVAEYAD 275
Cdd:pfam03009 135 K---ADPRRVIFSSFNPDELKRLRELA-----PKLPLVFLSSGRAYAEAD-------LLERAAAFAGAPALLGEVALVDE 199

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446701759  276 GIgpdyhmlieetsqpgniklTGMVQDAQQNKLVVHPYTVRsdklpeytpdvNQLYDALYNKAGVNGLFTDFPDK 350
Cdd:pfam03009 200 AL-------------------PDLVKRAHARGLVVHVWTVN-----------NEDEMKRLLELGVDGVITDRPDT 244
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
32-357 2.39e-66

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 209.34  E-value: 2.39e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  32 IVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRfpdrarkdgryyAIDFTLDE 111
Cdd:COG0584    4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGR------------VADLTLAE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 112 IKSLKFTegfdiengkkvqtYPGRFpmgkSDFRVHTFEEEIEFVqglnhstGKNIGIYPEIKAPWFHHQegkDIAAKTLE 191
Cdd:COG0584   72 LRQLDAG-------------SGPDF----AGERIPTLEEVLELV-------PGDVGLNIEIKSPPAAEP---DLAEAVAA 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 192 VLKKYGYtgkDDKVYLQCFDADELKRIKnELEPkmgmELNLVQLIAYTDWNETQQKQpdgswvnynydwmfkpgamkqvA 271
Cdd:COG0584  125 LLKRYGL---EDRVIVSSFDPEALRRLR-ELAP----DVPLGLLVEELPADPLELAR----------------------A 174

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 272 EYADGIGPDYHMLIEEtsqpgnikltgMVQDAQQNKLVVHPYTVRSDKlpeytpDVNQLYDAlynkaGVNGLFTDFPDKA 351
Cdd:COG0584  175 LGADGVGPDYDLLTPE-----------LVAAAHAAGLKVHVWTVNDPE------EMRRLLDL-----GVDGIITDRPDLL 232


                 ....*.
gi 446701759 352 VKFLNK 357
Cdd:COG0584  233 RAVLRE 238
 
Name Accession Description Interval E-value
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 5-358 0e+00

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 733.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759   5 LKNLSMAIMMSTIVMGSSAMAADSNEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDR 84
Cdd:PRK11143   1 LKNLSLALLLAALLAGSAAAAADSAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  85 VTDVADRFPDRARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKKVQTYPGRFPMGKSDFRVHTFEEEIEFVQGLNHSTGK 164
Cdd:PRK11143  81 VTDVAERFPDRARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKKVQVYPGRFPMGKSDFRVHTFEEEIEFIQGLNHSTGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 165 NIGIYPEIKAPWFHHQEGKDIAAKTLEVLKKYGYTGKDDKVYLQCFDADELKRIKNELEPKMGMELNLVQLIAYTDWNET 244
Cdd:PRK11143 161 NIGIYPEIKAPWFHHQEGKDIAAKVLEVLKKYGYTGKDDKVYLQCFDANELKRIKNELEPKMGMDLKLVQLIAYTDWNET 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 245 QQKQPDGSWVNYNYDWMFKPGAMKQVAEYADGIGPDYHMLIEETSQPGNIKLTGMVQDAQQNKLVVHPYTVRSDKLPEYT 324
Cdd:PRK11143 241 QEKQPDGKWVNYNYDWMFKPGAMKEVAKYADGIGPDYHMLVDETSTPGNIKLTGMVKEAHQAKLVVHPYTVRADQLPEYA 320

                        330       340       350
                 ....*....|....*....|....*....|....
gi 446701759 325 PDVNQLYDALYNKAGVNGLFTDFPDKAVKFLNKE 358
Cdd:PRK11143 321 TDVNQLYDILYNQAGVDGVFTDFPDKAVKFLNKQ 354
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 31-349 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: 606.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  31 KIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPDRARKDGRYYAIDFTLD 110
Cdd:cd08600    1 KIIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKRKDGRYYVIDFTLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 111 EIKSLKFTEGFDIENGKKVQTYPGRFPMGKSDFRVHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFHHQEGKDIAAKTL 190
Cdd:cd08600   81 ELKSLSVTERFDIENGKKVQVYPNRFPLWKSDFKIHTLEEEIELIQGLNKSTGKNVGIYPEIKAPWFHHQEGKDIAAATL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 191 EVLKKYGYTGKDDKVYLQCFDADELKRIKNELEPKMGMELNLVQLIAYTDWNETQQKQPDGsWVNYNYDWMFKPGAMKQV 270
Cdd:cd08600  161 EVLKKYGYTSKNDKVYLQTFDPNELKRIKNELLPKMGMDLKLVQLIAYTDWGETQEKDPGG-WVNYDYDWMFTKGGLKEI 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446701759 271 AEYADGIGPDYHMLIEETSQPGNIKLTGMVQDAQQNKLVVHPYTVRSDKLPEYTPDVNQLYDALYNKAGVNGLFTDFPD 349
Cdd:cd08600  240 AKYADGVGPWYSMIIEEKSSKGNIVLTDLVKDAHEAGLEVHPYTVRKDALPEYAKDADQLLDALLNKAGVDGVFTDFPD 318
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 31-348 7.51e-161

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: 452.11  E-value: 7.51e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  31 KIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPDRARKDGRYYAIDFTLD 110
Cdd:cd08559    1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVAEHFPFRGRKDTGYFVIDFTLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 111 EIKSLKFTEGFdiengkkVQTYPGRFPMGKSDFRVHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFHHQEGKDIAAKTL 190
Cdd:cd08559   81 ELKTLRAGSWF-------NQRYPERAPSYYGGFKIPTLEEVIELAQGLNKSTGRNVGIYPETKHPTFHKQEGPDIEEKLL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 191 EVLKKYGYTGKDDKVYLQCFDADELKRIKNELepkmgMELNLVQLIAYTDWNETQqkqpdgswVNYNYDWMFKPGAMKQV 270
Cdd:cd08559  154 EVLKKYGYTGKNDPVFIQSFEPESLKRLRNET-----PDIPLVQLIDYGDWAETD--------KKYTYAWLTTDAGLKEI 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446701759 271 AEYADGIGPDYHMLIEETSQpGNIKLTGMVQDAQQNKLVVHPYTVRSDKLPeYTPDVNQLYDALYNKAGVNGLFTDFP 348
Cdd:cd08559  221 AKYADGIGPWKSLIIPEDSN-GLLVPTDLVKDAHKAGLLVHPYTFRNENLF-LAPDFKQDMDALYNAAGVDGVFTDFP 296
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 32-348 1.46e-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: 261.08  E-value: 1.46e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  32 IVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADR--FPDRARK---DGR----Y 102
Cdd:cd08602    2 LVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHpeFADRKTTktvDGVnvtgW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 103 YAIDFTLDEIKSLKFTEGFDIENgkkvQTYPGRFPMGksdfrvhTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFHHQE- 181
Cdd:cd08602   82 FTEDFTLAELKTLRARQRLPYRD----QSYDGQFPIP-------TFEEIIALAKAASAATGRTVGIYPEIKHPTYFNAPl 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 182 GKDIAAKTLEVLKKYGYTGKDDKVYLQCFDADELKRIKNElepkmgMELNLVQLIAytdwNETQQKQPDGSWVNYNYDWM 261
Cdd:cd08602  151 GLPMEDKLLETLKKYGYTGKKAPVFIQSFEVTNLKYLRNK------TDLPLVQLID----DATIPPQDTPEGDSRTYADL 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 262 FKPGAMKQVAEYADGIGPDYHMLIEETSQPGNIKLTGMVQDAQQNKLVVHPYTVRSDK---LPEYTPDVNQLYDALYNkA 338
Cdd:cd08602  221 TTDAGLKEIATYADGIGPWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNENtflPPDFFGDPYAEYRAFLD-A 299

                        330
                 ....*....|
gi 446701759 339 GVNGLFTDFP 348
Cdd:cd08602  300 GVDGLFTDFP 309
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 36-350 4.78e-70

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: 219.19  E-value: 4.78e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759   36 HRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADrfpdrarkdgryYAIDFTLDEIKSL 115
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG------------YVRDLTLEELKRL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  116 kftegfDIENGKKVQTYPGRFPmgksdfrVHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFhHQEGKDIAAKTLEVLKK 195
Cdd:pfam03009  69 ------DIGAGNSGPLSGERVP-------FPTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEE-GLIVKDLLLSVDEILAK 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  196 YgytGKDDKVYLQCFDADELKRIKNELepkmgMELNLVQLIAYTDWNETQqkqpdgsWVNYNYDWMFKPGAMKQVAEYAD 275
Cdd:pfam03009 135 K---ADPRRVIFSSFNPDELKRLRELA-----PKLPLVFLSSGRAYAEAD-------LLERAAAFAGAPALLGEVALVDE 199

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446701759  276 GIgpdyhmlieetsqpgniklTGMVQDAQQNKLVVHPYTVRsdklpeytpdvNQLYDALYNKAGVNGLFTDFPDK 350
Cdd:pfam03009 200 AL-------------------PDLVKRAHARGLVVHVWTVN-----------NEDEMKRLLELGVDGVITDRPDT 244
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
32-357 2.39e-66

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 209.34  E-value: 2.39e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  32 IVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRfpdrarkdgryyAIDFTLDE 111
Cdd:COG0584    4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGR------------VADLTLAE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 112 IKSLKFTegfdiengkkvqtYPGRFpmgkSDFRVHTFEEEIEFVqglnhstGKNIGIYPEIKAPWFHHQegkDIAAKTLE 191
Cdd:COG0584   72 LRQLDAG-------------SGPDF----AGERIPTLEEVLELV-------PGDVGLNIEIKSPPAAEP---DLAEAVAA 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 192 VLKKYGYtgkDDKVYLQCFDADELKRIKnELEPkmgmELNLVQLIAYTDWNETQQKQpdgswvnynydwmfkpgamkqvA 271
Cdd:COG0584  125 LLKRYGL---EDRVIVSSFDPEALRRLR-ELAP----DVPLGLLVEELPADPLELAR----------------------A 174

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 272 EYADGIGPDYHMLIEEtsqpgnikltgMVQDAQQNKLVVHPYTVRSDKlpeytpDVNQLYDAlynkaGVNGLFTDFPDKA 351
Cdd:COG0584  175 LGADGVGPDYDLLTPE-----------LVAAAHAAGLKVHVWTVNDPE------EMRRLLDL-----GVDGIITDRPDLL 232


                 ....*.
gi 446701759 352 VKFLNK 357
Cdd:COG0584  233 RAVLRE 238
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 33-355 4.32e-51

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: 170.57  E-value: 4.32e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVAdrFPDRARkdgryyaiDFTLDEI 112
Cdd:cd08601    3 VIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIE--RPGPVK--------DYTLAEI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 113 KSLKFTEGFDiengkkvQTYPGRFPMGKSDFRVHTFEEEIEFVqglnhstGKNIGIYPEIKAPWFHhqegKDIAAKTLEV 192
Cdd:cd08601   73 KQLDAGSWFN-------KAYPEYARESYSGLKVPTLEEVIERY-------GGRANYYIETKSPDLY----PGMEEKLLAT 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 193 LKKYGYTGKD---DKVYLQCFDADELKRIkNELEPKMGMelnlVQLIAYTDWNETQQKqpdgswvnynydwmfkpgAMKQ 269
Cdd:cd08601  135 LDKYGLLTDNlknGQVIIQSFSKESLKKL-HQLNPNIPL----VQLLWYGEGAETYDK------------------WLDE 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 270 VAEYADGIGPDYHMLIEEtsqpgnikltgMVQDAQQNKLVVHPYTVrsdklpeytpDVNQLYDALYNkAGVNGLFTDFPD 349
Cdd:cd08601  192 IKEYAIGIGPSIADADPW-----------MVHLIHKKGLLVHPYTV----------NEKADMIRLIN-WGVDGMFTNYPD 249


                 ....*.
gi 446701759 350 KAVKFL 355
Cdd:cd08601  250 RLKEVL 255
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 33-347 7.60e-36

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: 128.71  E-value: 7.60e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDvadrfpdrarkdgryyaidftldei 112
Cdd:cd08555    1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTA------------------------- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 113 kslkftegfdiengkkvqtypgrfpmgksDFRVHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFhhqEGKDIAAKTLEV 192
Cdd:cd08555   56 -----------------------------GILPPTLEEVLELIADYLKNPDYTIILSLEIKQDSP---EYDEFLAKVLKE 103

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 193 LKKYGYTGKDDKVYLQCFDAdelkriknelepkmgmelnlvqliaytdwnetqqkqpdgswvnynydwmfkpgamkqvae 272
Cdd:cd08555  104 LRVYFDYDLRGKVVLSSFNA------------------------------------------------------------ 123

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446701759 273 yadgIGPDYHMLIeetsqPGNIKLTGMVQDAQQNKLVVHPYTVrsdklpeytPDVNQLYDALYNKaGVNGLFTDF 347
Cdd:cd08555  124 ----LGVDYYNFS-----SKLIKDTELIASANKLGLLSRIWTV---------NDNNEIINKFLNL-GVDGLITDF 179
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 33-347 1.37e-30

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: 115.05  E-value: 1.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDhyldrvtdvadrfpdrarkdgryyaidftldei 112
Cdd:cd08556    1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 113 kslkftegfdiengkkvqtypgrfpmgksdfrVHTFEEEIEFVQGlnhstgkNIGIYPEIKAPWFHHqegkDIAAKTLEV 192
Cdd:cd08556   48 --------------------------------IPTLEEVLELVKG-------GVGLNIELKEPTRYP----GLEAKVAEL 84

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 193 LKKYgytGKDDKVYLQCFDADELKRIKnelepKMGMELNLVQLIAYTDWNETQQkqpdgswvnynydwmfkpgaMKQVAE 272
Cdd:cd08556   85 LREY---GLEERVVVSSFDHEALRALK-----ELDPEVPTGLLVDKPPLDPLLA--------------------ELARAL 136

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446701759 273 YADGIGPDYHMLIEEtsqpgnikltgMVQDAQQNKLVVHPYTVRSDKLPEYtpdvnqlydalYNKAGVNGLFTDF 347
Cdd:cd08556  137 GADAVNPHYKLLTPE-----------LVRAAHAAGLKVYVWTVNDPEDARR-----------LLALGVDGIITDD 189
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 33-348 2.68e-29

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: 112.65  E-value: 2.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTdvadrfpdrarkDGRYYAIDFTLDEI 112
Cdd:cd08563    3 IFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTT------------NGKGYVKDLTLEEL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 113 KSLKFTEGFDIENGKKvqtypgrfpmgksdfRVHTFEEEIEFVQGlnhsTGKNIGIypEIKAPWFHHqegKDIAAKTLEV 192
Cdd:cd08563   71 KKLDAGSWFDEKFTGE---------------KIPTLEEVLDLLKD----KDLLLNI--EIKTDVIHY---PGIEKKVLEL 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 193 LKKYgytGKDDKVYLQCFDADELKRIKnELEPKMGmelnlvqlIAYTDWnetqqkqpdgswvnynyDWMFKPGAMKQVAE 272
Cdd:cd08563  127 VKEY---NLEDRVIFSSFNHESLKRLK-KLDPKIK--------LALLYE-----------------TGLQDPKDYAKKIG 177

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446701759 273 yADGIGPDYHMLIEEtsqpgnikltgMVQDAQQNKLVVHPYTVRSDKlpeytpDVNQLYDalynkAGVNGLFTDFP 348
Cdd:cd08563  178 -ADSLHPDFKLLTEE-----------VVEELKKRGIPVRLWTVNEEE------DMKRLKD-----LGVDGIITNYP 230
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 33-355 1.37e-28

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: 111.20  E-value: 1.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTdvadrfpdrarkDGRYYAIDFTLDEI 112
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTT------------DGTGPVADLTLAEL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 113 KSLKFTEGFDIENGkkvQTYPGRfpmgKSDFRVHTFEEEIEFVQGLNhstgKNIgiypEIKapwfhhQEGKDIAAKTLEV 192
Cdd:cd08561   69 RRLDAGYHFTDDGG---RTYPYR----GQGIRIPTLEELFEAFPDVR----LNI----EIK------DDGPAAAAALADL 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 193 LKKYGYTgkdDKVYLQCFDADELKRIKnELEPKM---GMELNLVQLIAytdwnetqqkqpdgsWVNYNYDWMFKPGAmkq 269
Cdd:cd08561  128 IERYGAQ---DRVLVASFSDRVLRRFR-RLCPRVatsAGEGEVAAFVL---------------ASRLGLGSLYSPPY--- 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 270 vaeyadgigpdYHMLIEETSQPGNIKLTGMVQDAQQNKLVVHPYTVRSDklpeytpdvnQLYDALYNKaGVNGLFTDFPD 349
Cdd:cd08561  186 -----------DALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDP----------AEMRRLLDL-GVDGIITDRPD 243


                 ....*.
gi 446701759 350 KAVKFL 355
Cdd:cd08561  244 LLLEVL 249
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 33-349 3.86e-28

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: 110.48  E-value: 3.86e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDrvtdvadrfPDRAR-KDGRYYAI------ 105
Cdd:cd08567    3 LQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLN---------PDITRdPDGAWLPYegpaly 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 106 DFTLDEIKSLkftegfDIENGKKVQTYPGRFPMGKSDFRVH--TFEEEIEFVQglnHSTGKNIGIYPEIKAPWFH---HQ 180
Cdd:cd08567   74 ELTLAEIKQL------DVGEKRPGSDYAKLFPEQIPVPGTRipTLEEVFALVE---KYGNQKVRFNIETKSDPDRdilHP 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 181 EGKDIAAKTLEVLKKYGYTgkdDKVYLQCFDADELKRIKnELEPKmgmeLNLVQLIAYTDwnetqqkqpdgswvNYNYdw 260
Cdd:cd08567  145 PPEEFVDAVLAVIRKAGLE---DRVVLQSFDWRTLQEVR-RLAPD----IPTVALTEETT--------------LGNL-- 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 261 mfkPGAMKQVAeyADGIGPDYHMLIEEtsqpgnikltgMVQDAQQNKLVVHPYTVRSdklPEytpDVNQLYDalynkAGV 340
Cdd:cd08567  201 ---PRAAKKLG--ADIWSPYFTLVTKE-----------LVDEAHALGLKVVPWTVND---PE---DMARLID-----LGV 253


                 ....*....
gi 446701759 341 NGLFTDFPD 349
Cdd:cd08567  254 DGIITDYPD 262
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 33-349 2.24e-22

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity 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: 93.92  E-value: 2.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVadrfpDRARKdgryyaiDFTLDEI 112
Cdd:cd08582    1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGG-----DGAVS-------DLTLAEL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 113 KSLKFTEGFDIENGKKvqtypgrfpmgksdfRVHTFEEEIEFVqglnhsTGKNIGIYPEIKAPWFhhqeGKDIAAKTLEV 192
Cdd:cd08582   69 RKLDIGSWKGESYKGE---------------KVPTLEEYLAIV------PKYGKKLFIEIKHPRR----GPEAEEELLKL 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 193 LKKYGytGKDDKVYLQCFDADELKRIKnELEPkmgmELNLVQLiaytdwnetqqkqpdgswVNYNYDWMFKPGAMKQVae 272
Cdd:cd08582  124 LKESG--LLPEQIVIISFDAEALKRVR-ELAP----TLETLWL------------------RNYKSPKEDPRPLAKSG-- 176

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446701759 273 YADGIGPDYHMLIEETsqpgnikltgMVQDAQQNKLVVHPYTVRSDKlpeytpDVNQLYDalynkAGVNGLFTDFPD 349
Cdd:cd08582  177 GAAGLDLSYEKKLNPA----------FIKALRDAGLKLNVWTVDDAE------DAKRLIE-----LGVDSITTNRPG 232
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 32-348 2.02e-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: 84.26  E-value: 2.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  32 IVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPDRAR--------KDGrYY 103
Cdd:cd08571    2 LVIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPKRKKtyvvegqsTSG-IF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 104 AIDFTLDEIKSLKFTegfdIENgkkVQTYPGRFPMGKSDFRVHTFEeeiEFVQGLNHSTGknIGIYPEIK-APWFHHQEG 182
Cdd:cd08571   81 SFDLTWAEIQTLKPI----ISN---PFSVLFRNPRNDNAGKILTLE---DFLTLAKPKSL--SGVWINVEnAAFLAEHKG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 183 KDIAAKTLEVLKKYGYTGKDDKVYLQCFDADELKRIKNELEPKmgmelnLVQLIAYTDWNEtqqkqPDGSwvnynydwmf 262
Cdd:cd08571  149 LLSVDAVLTSLSKAGYDQTAKKVYISSPDSSVLKSFKKRVGTK------LVFRVLDVDDTE-----PDTL---------- 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 263 kPGAMKQVAEYADGIgpdyhmLIEETS----QPGN--IKLTGMVQDAQ-----------QNKLVVHPYTVRSDKLPEYtp 325
Cdd:cd08571  208 -LSNLTEIKKFASGV------LVPKSYiwpvDSDSflTPQTSVVQDAHkaglevyvsgfANEFVSLAYDYSADPTLEI-- 278

                        330       340
                 ....*....|....*....|...
gi 446701759 326 dvNQLYDalyNKAGVNGLFTDFP 348
Cdd:cd08571  279 --LSFVG---NGNSVDGVITDFP 296
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 33-226 3.06e-18

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


Pssm-ID: 176521 [Multi-domain]  Cd Length: 220  Bit Score: 82.21  E-value: 3.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVaDRFPDrarkdgryyaiDFTLDEI 112
Cdd:cd08579    1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGV-NKKVW-----------DLTLEEL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 113 KSLKFTEGFdiengkkvqtYPGRFPmgksdfrvhTFEEEIEFVQGLnhstgkNIGIYPEIKApwfHHQEGKDIAAKtleV 192
Cdd:cd08579   69 KKLTIGENG----------HGAKIP---------SLDEYLALAKGL------KQKLLIELKP---HGHDSPDLVEK---F 117

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446701759 193 LKKYGYTGKDDKVYLQCFDADELKRIKnELEPKM 226
Cdd:cd08579  118 VKLYKQNLIENQHQVHSLDYRVIEKVK-KLDPKI 150
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 34-197 5.16e-18

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: 82.65  E-value: 5.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  34 IAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADrfpdrarkdgryYAIDFTLDEIK 113
Cdd:cd08575    4 IAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSG------------LVSDLTYAELP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 114 SLKFTEGFDIENGKKVqtypgrFPMGKSDFRVHTFEEEI-EFvqglnhstgKNIGIYPEIKAPwfhhqEGKDIAAKTLEV 192
Cdd:cd08575   72 PLDAGYGYTFDGGKTG------YPRGGGDGRIPTLEEVFkAF---------PDTPINIDIKSP-----DAEELIAAVLDL 131


                 ....*
gi 446701759 193 LKKYG 197
Cdd:cd08575  132 LEKYK 136
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 32-228 1.10e-17

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: 81.19  E-value: 1.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  32 IVIAHRGASGYL-PEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPdrarkdgryyaiDFTLD 110
Cdd:cd08566    1 LVVAHRGGWGAGaPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVS------------DLTLA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 111 EIKSLKFTEGFdiengkkvqtypGRFpmgkSDFRVHTFEEEIEFVQGlnhstgkNIGIYPEIKapwfhhqegKDIAAKTL 190
Cdd:cd08566   69 EIRKLRLKDGD------------GEV----TDEKVPTLEEALAWAKG-------KILLNLDLK---------DADLDEVI 116

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446701759 191 EVLKKYGYtgkDDKVYLQCFDADELKRIKNELEPKMGM 228
Cdd:cd08566  117 ALVKKHGA---LDQVIFKSYSEEQAKELRALAPEVMLM 151
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 33-257 1.96e-17

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: 80.07  E-value: 1.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPdrarkdgryyaiDFTLDEI 112
Cdd:cd08581    1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLH------------ELEDAEL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 113 KSLkftegfdiengkkVQTYPGRFPMGKSDFRVHTFEeeiEFVQGLNHSTGknIGIYPEIKAPWFHHQEGKDIAAKTLEV 192
Cdd:cd08581   69 DSL-------------RVAEPARFGSRFAGEPLPSLA---AVVQWLAQHPQ--VTLFVEIKTESLDRFGLERVVDKVLRA 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446701759 193 LkkygytgkdDKVYLQC----FDADELKRIKNELEPKMGMELNLVQLiayTDWNETQQKQPDGSWVNYN 257
Cdd:cd08581  131 L---------PAVAAQRvlisFDYDLLALAKQQGGPRTGWVLPDWDD---ASLAEADELQPDYLFCDKN 187
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 34-348 5.57e-16

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: 78.23  E-value: 5.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  34 IAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHY-LDRVTDVADRfPDRARKDGRYYAI------- 105
Cdd:cd08560   20 IGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSQCdLHTTTNILAI-PELAAKCTQPFTPanatkpa 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 106 -------DFTLDEIKSLKF-TEGFDiengkKVQTYPGRFPMGKSDFR---------VHTFEEEIEFVQGLnhstgkNIGI 168
Cdd:cd08560   99 saecctsDITLAEFKSLCGkMDASN-----PSATTPEEYQNGTPDWRtdlyatcgtLMTHKESIALFKSL------GVKM 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 169 YPEIKAPWF-------HHQEgkDIAAKTLEVLKKYGYTGkdDKVYLQCFD-ADELKRIKNelEPKMGMelnlvQLIAYTD 240
Cdd:cd08560  168 TPELKSPSVpmpfdgnYTQE--DYAQQMIDEYKEAGVPP--SRVWPQSFNlDDIFYWIKN--EPDFGR-----QAVYLDD 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 241 WNETQQKQPDGSwvnynydwmfkpGAMKQVaeYADG---IGPDYHMLIEETSQpGNIKLTGMVQDAQQNKLVVHPYTV-R 316
Cdd:cd08560  237 RDDTADFPATWS------------PSMDEL--KARGvniIAPPIWMLVDPDEN-GKIVPSEYAKAAKAAGLDIITWTLeR 301

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 446701759 317 SDKLPE--------------YTPDVNQLYDALYNKAGVNGLFTDFP 348
Cdd:cd08560  302 SGPLASgggwyyqtiedvinNDGDMYNVLDVLARDVGILGIFSDWP 347
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 33-348 1.15e-15

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


Pssm-ID: 176505 [Multi-domain]  Cd Length: 229  Bit Score: 75.34  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDvadrfpdrarKDGRYYaiDFTLDEI 112
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTN----------GSGAVT--ELTWAEL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 113 KSLKFTEGFDIEngkkvqtypgrFpmgkSDFRVHTFEEEIEFvqgLNHStgkNIGIYPEIKApwfHHQEGKDIAAKTLEV 192
Cdd:cd08562   69 AQLDAGSWFSPE-----------F----AGEPIPTLADVLEL---AREL---GLGLNLEIKP---DPGDEALTARVVAAA 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 193 LKKYGYTGkdDKVYLQCFDADELKRIKnELEPkmgmELNLVQLiaYTDWNEtqqkqpdgswvnynyDWmfkpgamkqvAE 272
Cdd:cd08562  125 LRELWPHA--SKLLLSSFSLEALRAAR-RAAP----ELPLGLL--FDTLPA---------------DW----------LE 170

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 273 YADGIG-----PDYHMLIEETsqpgnIKltgMVQDAqqnKLVVHPYTVRSDKLpeytpdVNQLYDalynkAGVNGLFTDF 347
Cdd:cd08562  171 LLAALGavsihLNYRGLTEEQ-----VK---ALKDA---GYKLLVYTVNDPAR------AAELLE-----WGVDAIFTDR 228


                 .
gi 446701759 348 P 348
Cdd:cd08562  229 P 229
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 33-120 2.54e-15

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


Pssm-ID: 176512 [Multi-domain]  Cd Length: 234  Bit Score: 74.18  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPDrarkdgryyaiDFTLDEI 112
Cdd:cd08570    1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIID-----------DSTWDEL 69


                 ....*...
gi 446701759 113 KSLKFTEG 120
Cdd:cd08570   70 SHLRTIEE 77
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 33-87 4.98e-14

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: 71.14  E-value: 4.98e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTD 87
Cdd:cd08573    1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTD 55
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 32-213 1.32e-12

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: 67.30  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  32 IVIAHRGA------SGY--LPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLdRVTDvaDRFPDRARKDGRYY 103
Cdd:cd08572    1 LVIGHRGLgknyasGSLagIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTI-SVSE--KSKTGSDEGELIEV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 104 AI-DFTLDEIKSLKftegFDIENGKKVQTYPGRFPMGKSDFRVHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPwFHHQEG 182
Cdd:cd08572   78 PIhDLTLEQLKELG----LQHISALKRKALTRKAKGPKPNPWGMDEHDPFPTLQEVLEQVPKDLGFNIEIKYP-QLLEDG 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446701759 183 KDIAA----------KTLEVLKKYgytGKDDKVYLQCFDAD 213
Cdd:cd08572  153 EGELTpyfernafvdTILAVVFEH---AGGRRIIFSSFDPD 190
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 34-210 1.94e-12

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: 66.85  E-value: 1.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  34 IAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVAdrfpdrarkdgrYYAIDFTLDEIk 113
Cdd:cd08612   30 ISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVD------------KLVSDLNYADL- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 114 sLKFTEGFDIENGKKVQTYPGRfpmgkSDFRVHTFEEEIE-FvqglnhstgKNIGIYPEIKAPwfhhqeGKDIAAKTLEV 192
Cdd:cd08612   97 -PPYLEKLEVTFSPGDYCVPKG-----SDRRIPLLEEVFEaF---------PDTPINIDIKVE------NDELIKKVSDL 155

                        170       180
                 ....*....|....*....|....
gi 446701759 193 LKKYGYTGK------DDKVYLQCF 210
Cdd:cd08612  156 VRKYKREDItvwgsfNDEIVKKCH 179
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 33-218 6.06e-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: 64.73  E-value: 6.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTdvadrfpdrarkDGRYYAIDFTLDEI 112
Cdd:cd08565    1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTT------------HGTGAVRDLTLAER 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 113 KSLKFTEGFDIengkkvqtypgrfpmgksdfRVHTFEEEIEFVQglnhstGKNIGIYPEIKaPWFHHQEGKDIAAKTLEV 192
Cdd:cd08565   69 KALRLRDSFGE--------------------KIPTLEEVLALFA------PSGLELHVEIK-TDADGTPYPGAAALAAAT 121

                        170       180
                 ....*....|....*....|....*.
gi 446701759 193 LKKYGYtgkDDKVYLQCFDADELKRI 218
Cdd:cd08565  122 LRRHGL---LERSVLTSFDPAVLTEV 144
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 32-354 6.31e-11

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: 62.36  E-value: 6.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  32 IVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKD------------DNLVVLHDHYLDRVTDVadrfPDRARKD 99
Cdd:cd08604    2 LIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDgvpfcldsinliNSTTVATSKFSNRATTV----PEIGSTS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 100 GrYYAIDFTLDEIKSLKftegFDIENGKKVQTYpGRFPMGKSDFRVHTFEEEIEFVQGLNHStgkniGIYPEIK-APWFH 178
Cdd:cd08604   78 G-IFTFDLTWSEIQTLK----PAISNPYSVTGL-FRNPANKNAGKFLTLSDFLDLAKNKSLS-----GVLINVEnAAYLA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 179 HQEGKDIAAKTLEVLKKYGYT-GKDDKVYLQCFDADELKRIKnelepkmgmelnlvQLIAYTDWNETQQKQPDGSwvnyn 257
Cdd:cd08604  147 EKKGLDVVDAVLDALTNAGYDnQTAQKVLIQSTDSSVLAAFK--------------KQISYERVYVVDETIRDAS----- 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 258 ydwmfkPGAMKQVAEYADGIGPDYHMLIEEtSQPGNIKLTGMVQDAQQNKLVVHPYTVRSdklpEYtpdVNQLYD----- 332
Cdd:cd08604  208 ------DSSIEEIKKFADAVVIDRGSVFPV-STSFLTRQTNVVEKLQSANLTVYVEVLRN----EF---VSLAFDffadp 273

                        330       340
                 ....*....|....*....|....*..
gi 446701759 333 -----ALYNKAGVNGLFTDFPDKAVKF 354
Cdd:cd08604  274 tveinSYVQGAGVDGFITEFPATAARY 300
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 33-115 1.09e-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: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPDRARKDgryyAIDFTLDEI 112
Cdd:cd08574    4 LIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVADVFPERAHER----ASMFTWTDL 79


                 ...
gi 446701759 113 KSL 115
Cdd:cd08574   80 QQL 82
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 32-131 9.26e-10

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: 58.08  E-value: 9.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  32 IVIAHRGASGYLPEHTLPA--KAMAYaqGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVadrfpdrarkdgRYYAIDFTL 109
Cdd:cd08568    1 IILGHRGYRAKYPENTLEAfkKAIEY--GADGVELDVWLTKDGKLVVLHDENLKRVGGV------------DLKVKELTY 66

                         90       100
                 ....*....|....*....|..
gi 446701759 110 DEIKSLKFtegfdieNGKKVQT 131
Cdd:cd08568   67 KELKKLHP-------GGELIPT 81
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 33-197 1.24e-09

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


Pssm-ID: 176551 [Multi-domain]  Cd Length: 315  Bit Score: 58.78  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPDRARKDgryyAIDFTLDEI 112
Cdd:cd08609   29 LVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKDVFPGRDAAG----SNNFTWTEL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 113 KSLKFTEGFdiengKKVQTYPGRFPMGKSDFRVHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFHHQEGKDIAAKTLEV 192
Cdd:cd08609  105 KTLNAGSWF-----LERRPFWTLSSLSEEDRREADNQTVPSLSELLDLAKKHNVSIMFDLRNENNSHVFYSSFVFYTLET 179


                 ....*
gi 446701759 193 LKKYG 197
Cdd:cd08609  180 ILKLG 184
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 34-226 4.84e-09

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: 56.18  E-value: 4.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  34 IAHRG---ASGYLPEHTLPAKAMAYAqgADY-LEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPdrarkdgryyaiDFTL 109
Cdd:cd08585    7 IAHRGlhdRDAGIPENSLSAFRAAAE--AGYgIELDVQLTADGEVVVFHDDNLKRLTGVEGRVE------------ELTA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 110 DEIKSLKFtegfdiengkkvqtypgrfpmGKSDFRVHTFEEEIEFVQGlnhstgkNIGIYPEIKApwfHHQEGKDIAAKT 189
Cdd:cd08585   73 AELRALRL---------------------LGTDEHIPTLDEVLELVAG-------RVPLLIELKS---CGGGDGGLERRV 121

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446701759 190 LEVLKkyGYTGkddKVYLQCFDADELKRIKnELEPKM 226
Cdd:cd08585  122 LAALK--DYKG---PAAIMSFDPRVVRWFR-KLAPGI 152
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 28-264 8.04e-09

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: 55.94  E-value: 8.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  28 SNEKIVIAHRGA--SGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFpdraRKDGRYYAI 105
Cdd:cd08564    1 MVRPIIVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHGTEDDTNPDTSIQL----DDSGFKNIN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 106 DFTLDEIKSLKFTEGFDIENGKKVQTYPGRFPMGKSDFRvhTFEEEIEFvqglnhstgkNIgiypEIKAPwfhhqeGKDI 185
Cdd:cd08564   77 DLSLDEITRLHFKQLFDEKPCGADEIKGEKIPTLEDVLV--TFKDKLKY----------NI----ELKGR------EVGL 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 186 AAKTLEVLKKYGYTGkddKVYLQCFD-ADELKRIKnELEPKmgmelNLVQLIAYTDWNETQQKQPD---------GSWVN 255
Cdd:cd08564  135 GERVLNLVEKYGMIL---QVHFSSFLhYDRLDLLK-ALRPN-----KLNVPIALLFNEVKSPSPLDfleqakyynATWVN 205


                 ....*....
gi 446701759 256 YNYDWMFKP 264
Cdd:cd08564  206 FSYDFWTEE 214
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 27-135 7.06e-08

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: 53.52  E-value: 7.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  27 DSNEKIVIAHRGASG-----------------YLPEH-----TLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDr 84
Cdd:cd08613   20 PGGKPKLLAHRGLAQtfdregvendtctaeriDPPTHdylenTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLD- 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446701759  85 vtdvadrfpdrARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKkvqTYPGR 135
Cdd:cd08613   99 -----------CRTDGSGVTRDHTMAELKTLDIGYGYTADGGK---TFPFR 135
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 33-99 3.04e-07

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: 51.77  E-value: 3.04e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPDRARKD 99
Cdd:cd08608    4 IIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYED 70
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 34-117 1.01e-05

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


Pssm-ID: 176549 [Multi-domain]  Cd Length: 290  Bit Score: 46.52  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  34 IAHRG-------ASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLdrVTDVADRFpDRARKDGRYYAI- 105
Cdd:cd08607    3 VGHRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTL--RVSLKSKG-DSDRDDLLEVPVk 79

                         90
                 ....*....|..
gi 446701759 106 DFTLDEIKSLKF 117
Cdd:cd08607   80 DLTYEQLKLLKL 91
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 32-120 2.02e-05

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: 45.84  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  32 IVIAHRGASGYLPEHTLPAK--AMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPDRARK---DGR----Y 102
Cdd:cd08603    2 LVIARGGFSGLFPDSSLFAYqfAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPKRKKTysvNGVstkgW 81

                         90
                 ....*....|....*...
gi 446701759 103 YAIDFTLDEIKSLKFTEG 120
Cdd:cd08603   82 FSVDFTLAELQQVTLIQG 99
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 33-139 3.50e-05

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


Pssm-ID: 176522 [Multi-domain]  Cd Length: 263  Bit Score: 44.62  E-value: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDvadrfpdrarKDGRyyAIDFTLDEI 112
Cdd:cd08580    3 IVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTN----------GSGA--VSAYTAAQL 70

                         90       100
                 ....*....|....*....|....*..
gi 446701759 113 KSLKFTEGFDIENGKKvqtYPGRfPMG 139
Cdd:cd08580   71 ATLNAGYNFKPEGGYP---YRGK-PVG 93
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 33-107 9.55e-05

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: 43.71  E-value: 9.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPDRARKDGRYYAIDF 107
Cdd:cd08610   25 IIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNIGEVQPESACENPAFFNWDF 99
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 33-87 1.23e-04

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 43.00  E-value: 1.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446701759  33 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTD 87
Cdd:PRK09454  10 IVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSN 64
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 33-197 5.91e-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: 38.20  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759  33 VIAHRG--------ASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRV-TDVADRfpdrarkdgryy 103
Cdd:cd08606    4 VIGHRGlgkntaerKSLQLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETgTDVPIH------------ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446701759 104 aiDFTLDEIKSLKFTEgfdiengkkvqtYPGRFPMG--KSDFRVHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFHHQE 181
Cdd:cd08606   72 --DLTLEQFLHLSRMK------------YTVDFKKKgfKGNSRGHSIQAPFTTLEELLKKLPKSVGFNIELKYPMLHEAE 137

                        170       180
                 ....*....|....*....|....*.
gi 446701759 182 GKDIAA----------KTLEVLKKYG 197
Cdd:cd08606  138 EEEVAPvaielnafvdTVLEKVFDYG 163
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH