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Conserved domains on  [gi|1210155409|dbj|BAY74495|]
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glycerophosphoryl diester phosphodiesterase [Nostoc linckia NIES-25]

Protein Classification

glycerophosphodiester phosphodiesterase( domain architecture ID 10171238)

glycerophosphodiester phosphodiesterase domain (GDPD)-containing protein is part of 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 catalyze the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 10-320 3.69e-180

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: 500.67  E-value: 3.69e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARHTEFARRKTTKIIDGESKTG 89
Cdd:cd08602     1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHPEFADRKTTKTVDGVNVTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 WFTEDFTLGELKTLRAKERIPQLRPQnifYNGLFEIPTFQEIIDLVKKKSAEINRKIGIYPETKHPSYFKS-IGLPLEKP 168
Cdd:cd08602    81 WFTEDFTLAELKTLRARQRLPYRDQS---YDGQFPIPTFEEIIALAKAASAATGRTVGIYPEIKHPTYFNApLGLPMEDK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 169 LLTTLSANGYQGANAPVFIQSFEVSNLQDLSTKTDLPLVQLVNNTGKPYDFVVSSNGSTYTDLITTSGLEKIAKYAQAIG 248
Cdd:cd08602   158 LLETLKKYGYTGKKAPVFIQSFEVTNLKYLRNKTDLPLVQLIDDATIPPQDTPEGDSRTYADLTTDAGLKEIATYADGIG 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1210155409 249 IHKNLLVSRDSIGKLLSPTSLIINAHASGLLVHAWTFRNEDHFLPLDFQGNPQGEYELFFKLGIDGVFSDYP 320
Cdd:cd08602   238 PWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNENTFLPPDFFGDPYAEYRAFLDAGVDGLFTDFP 309
 
Name Accession Description Interval E-value
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 10-320 3.69e-180

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: 500.67  E-value: 3.69e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARHTEFARRKTTKIIDGESKTG 89
Cdd:cd08602     1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHPEFADRKTTKTVDGVNVTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 WFTEDFTLGELKTLRAKERIPQLRPQnifYNGLFEIPTFQEIIDLVKKKSAEINRKIGIYPETKHPSYFKS-IGLPLEKP 168
Cdd:cd08602    81 WFTEDFTLAELKTLRARQRLPYRDQS---YDGQFPIPTFEEIIALAKAASAATGRTVGIYPEIKHPTYFNApLGLPMEDK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 169 LLTTLSANGYQGANAPVFIQSFEVSNLQDLSTKTDLPLVQLVNNTGKPYDFVVSSNGSTYTDLITTSGLEKIAKYAQAIG 248
Cdd:cd08602   158 LLETLKKYGYTGKKAPVFIQSFEVTNLKYLRNKTDLPLVQLIDDATIPPQDTPEGDSRTYADLTTDAGLKEIATYADGIG 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1210155409 249 IHKNLLVSRDSIGKLLSPTSLIINAHASGLLVHAWTFRNEDHFLPLDFQGNPQGEYELFFKLGIDGVFSDYP 320
Cdd:cd08602   238 PWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNENTFLPPDFFGDPYAEYRAFLDAGVDGLFTDFP 309
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 10-323 3.59e-70

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 222.63  E-value: 3.59e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARhtEFARRKTTkiiDGEsktg 89
Cdd:PRK11143   27 KIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAE--RFPDRARK---DGR---- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 WFTEDFTLGELKTLRAKERIP-------QLRPQNI-FYNGLFEIPTFQEIIDLVKKKSAEINRKIGIYPETKHPSYFKSI 161
Cdd:PRK11143   98 YYAIDFTLDEIKSLKFTEGFDiengkkvQVYPGRFpMGKSDFRVHTFEEEIEFIQGLNHSTGKNIGIYPEIKAPWFHHQE 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 162 GLPLEKPLLTTLSANGYQGANAPVFIQSFEVSNLQDLST------KTDLPLVQLVNNTGKPYDFVVSSNGS----TYTDL 231
Cdd:PRK11143  178 GKDIAAKVLEVLKKYGYTGKDDKVYLQCFDANELKRIKNelepkmGMDLKLVQLIAYTDWNETQEKQPDGKwvnyNYDWM 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 232 ITTSGLEKIAKYAQAIGIHKNLLVSRDSIGKLLSPTSLIINAHASGLLVHAWTFRNEDhfLPlDFQGNPQGEYELFF-KL 310
Cdd:PRK11143  258 FKPGAMKEVAKYADGIGPDYHMLVDETSTPGNIKLTGMVKEAHQAKLVVHPYTVRADQ--LP-EYATDVNQLYDILYnQA 334

                         330
                  ....*....|...
gi 1210155409 311 GIDGVFSDYPDTA 323
Cdd:PRK11143  335 GVDGVFTDFPDKA 347
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
8-326 2.26e-66

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 208.95  E-value: 2.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409   8 KPPIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARHtefarrkttkiidgesk 87
Cdd:COG0584     1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGR----------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  88 tgwfTEDFTLGELKTLRAKeripqlrpQNIFYNGLfEIPTFQEIIDLVKkksaeinRKIGIYPETKHPSYFKSiglPLEK 167
Cdd:COG0584    64 ----VADLTLAELRQLDAG--------SGPDFAGE-RIPTLEEVLELVP-------GDVGLNIEIKSPPAAEP---DLAE 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 168 PLLTTLSANGYQGanaPVFIQSFEVSNLQDLSTKT-DLPLVQLVnntgkpydfvvssnGSTYTDLITTSGlekiAKYAQA 246
Cdd:COG0584   121 AVAALLKRYGLED---RVIVSSFDPEALRRLRELApDVPLGLLV--------------EELPADPLELAR----ALGADG 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 247 IGIHKNLLvsrdsigkllsPTSLIINAHASGLLVHAWTFRNEDhflpldfqgnpqgEYELFFKLGIDGVFSDYPDTAYAV 326
Cdd:COG0584   180 VGPDYDLL-----------TPELVAAAHAAGLKVHVWTVNDPE-------------EMRRLLDLGVDGIITDRPDLLRAV 235
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 15-322 5.73e-48

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: 161.80  E-value: 5.73e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  15 HRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARhtefarrkttkiidgesktgwFTED 94
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG---------------------YVRD 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  95 FTLGELKTLR-AKERIPQLRPQNifynglFEIPTFQEIIDLVKKKSAEINRKIGIYPETKHPsYFKSIGLPLekpLLTTL 173
Cdd:pfam03009  60 LTLEELKRLDiGAGNSGPLSGER------VPFPTLEEVLEFDWDVGFNIEIKIKPYVEAIAP-EEGLIVKDL---LLSVD 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 174 SANGYQGANAPVFIQSFEVSNLQDLSTK-TDLPLVQLvnntgkpydfvvssngSTYTDLITTSGLEKIAKYAQAIGIHKN 252
Cdd:pfam03009 130 EILAKKADPRRVIFSSFNPDELKRLRELaPKLPLVFL----------------SSGRAYAEADLLERAAAFAGAPALLGE 193

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 253 LLVSRDSIGKLLSPtsliinAHASGLLVHAWTFRNEDhflpldfqgnpqgEYELFFKLGIDGVFSDYPDT 322
Cdd:pfam03009 194 VALVDEALPDLVKR------AHARGLVVHVWTVNNED-------------EMKRLLELGVDGVITDRPDT 244
 
Name Accession Description Interval E-value
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 10-320 3.69e-180

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: 500.67  E-value: 3.69e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARHTEFARRKTTKIIDGESKTG 89
Cdd:cd08602     1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHPEFADRKTTKTVDGVNVTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 WFTEDFTLGELKTLRAKERIPQLRPQnifYNGLFEIPTFQEIIDLVKKKSAEINRKIGIYPETKHPSYFKS-IGLPLEKP 168
Cdd:cd08602    81 WFTEDFTLAELKTLRARQRLPYRDQS---YDGQFPIPTFEEIIALAKAASAATGRTVGIYPEIKHPTYFNApLGLPMEDK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 169 LLTTLSANGYQGANAPVFIQSFEVSNLQDLSTKTDLPLVQLVNNTGKPYDFVVSSNGSTYTDLITTSGLEKIAKYAQAIG 248
Cdd:cd08602   158 LLETLKKYGYTGKKAPVFIQSFEVTNLKYLRNKTDLPLVQLIDDATIPPQDTPEGDSRTYADLTTDAGLKEIATYADGIG 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1210155409 249 IHKNLLVSRDSIGKLLSPTSLIINAHASGLLVHAWTFRNEDHFLPLDFQGNPQGEYELFFKLGIDGVFSDYP 320
Cdd:cd08602   238 PWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNENTFLPPDFFGDPYAEYRAFLDAGVDGLFTDFP 309
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 10-320 3.29e-141

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: 401.65  E-value: 3.29e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARHTEFARRKTtkiidgeskTG 89
Cdd:cd08559     1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVAEHFPFRGRKD---------TG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 WFTEDFTLGELKTLRAK----ERIPQLRPQnifYNGLFEIPTFQEIIDLVKKKSAEINRKIGIYPETKHPSYFKSIGLPL 165
Cdd:cd08559    72 YFVIDFTLAELKTLRAGswfnQRYPERAPS---YYGGFKIPTLEEVIELAQGLNKSTGRNVGIYPETKHPTFHKQEGPDI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 166 EKPLLTTLSANGYQGANAPVFIQSFEVSNLQDLSTKT-DLPLVQLVNNTGKPYDFvvssNGSTYTDLITTSGLEKIAKYA 244
Cdd:cd08559   149 EEKLLEVLKKYGYTGKNDPVFIQSFEPESLKRLRNETpDIPLVQLIDYGDWAETD----KKYTYAWLTTDAGLKEIAKYA 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1210155409 245 QAIGIHKNLLVSRDSIGkLLSPTSLIINAHASGLLVHAWTFRNEDHFLPLDFQGNPQGEYElffKLGIDGVFSDYP 320
Cdd:cd08559   225 DGIGPWKSLIIPEDSNG-LLVPTDLVKDAHKAGLLVHPYTFRNENLFLAPDFKQDMDALYN---AAGVDGVFTDFP 296
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 10-321 1.64e-76

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: 237.67  E-value: 1.64e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARhtEFARRKTTkiiDGEsktg 89
Cdd:cd08600     1 KIIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAE--KFPDRKRK---DGR---- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 WFTEDFTLGELKTLRAKERI-------PQLRPQNiFYNGL--FEIPTFQEIIDLVKKKSAEINRKIGIYPETKHPSYFKS 160
Cdd:cd08600    72 YYVIDFTLDELKSLSVTERFdiengkkVQVYPNR-FPLWKsdFKIHTLEEEIELIQGLNKSTGKNVGIYPEIKAPWFHHQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 161 IGLPLEKPLLTTLSANGYQGANAPVFIQSFEVSNLQDLSTK------TDLPLVQLVNNTGKPYDFVVSSNGST---YTDL 231
Cdd:cd08600   151 EGKDIAAATLEVLKKYGYTSKNDKVYLQTFDPNELKRIKNEllpkmgMDLKLVQLIAYTDWGETQEKDPGGWVnydYDWM 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 232 ITTSGLEKIAKYAQAIGIHKNLLVSRDSIGKLLSPTSLIINAHASGLLVHAWTFRNEDhfLPLDFQGNPQGEYELFFKLG 311
Cdd:cd08600   231 FTKGGLKEIAKYADGVGPWYSMIIEEKSSKGNIVLTDLVKDAHEAGLEVHPYTVRKDA--LPEYAKDADQLLDALLNKAG 308

                         330
                  ....*....|
gi 1210155409 312 IDGVFSDYPD 321
Cdd:cd08600   309 VDGVFTDFPD 318
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 10-323 3.59e-70

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 222.63  E-value: 3.59e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARhtEFARRKTTkiiDGEsktg 89
Cdd:PRK11143   27 KIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAE--RFPDRARK---DGR---- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 WFTEDFTLGELKTLRAKERIP-------QLRPQNI-FYNGLFEIPTFQEIIDLVKKKSAEINRKIGIYPETKHPSYFKSI 161
Cdd:PRK11143   98 YYAIDFTLDEIKSLKFTEGFDiengkkvQVYPGRFpMGKSDFRVHTFEEEIEFIQGLNHSTGKNIGIYPEIKAPWFHHQE 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 162 GLPLEKPLLTTLSANGYQGANAPVFIQSFEVSNLQDLST------KTDLPLVQLVNNTGKPYDFVVSSNGS----TYTDL 231
Cdd:PRK11143  178 GKDIAAKVLEVLKKYGYTGKDDKVYLQCFDANELKRIKNelepkmGMDLKLVQLIAYTDWNETQEKQPDGKwvnyNYDWM 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 232 ITTSGLEKIAKYAQAIGIHKNLLVSRDSIGKLLSPTSLIINAHASGLLVHAWTFRNEDhfLPlDFQGNPQGEYELFF-KL 310
Cdd:PRK11143  258 FKPGAMKEVAKYADGIGPDYHMLVDETSTPGNIKLTGMVKEAHQAKLVVHPYTVRADQ--LP-EYATDVNQLYDILYnQA 334

                         330
                  ....*....|...
gi 1210155409 311 GIDGVFSDYPDTA 323
Cdd:PRK11143  335 GVDGVFTDFPDKA 347
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
8-326 2.26e-66

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 208.95  E-value: 2.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409   8 KPPIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARHtefarrkttkiidgesk 87
Cdd:COG0584     1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGR----------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  88 tgwfTEDFTLGELKTLRAKeripqlrpQNIFYNGLfEIPTFQEIIDLVKkksaeinRKIGIYPETKHPSYFKSiglPLEK 167
Cdd:COG0584    64 ----VADLTLAELRQLDAG--------SGPDFAGE-RIPTLEEVLELVP-------GDVGLNIEIKSPPAAEP---DLAE 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 168 PLLTTLSANGYQGanaPVFIQSFEVSNLQDLSTKT-DLPLVQLVnntgkpydfvvssnGSTYTDLITTSGlekiAKYAQA 246
Cdd:COG0584   121 AVAALLKRYGLED---RVIVSSFDPEALRRLRELApDVPLGLLV--------------EELPADPLELAR----ALGADG 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 247 IGIHKNLLvsrdsigkllsPTSLIINAHASGLLVHAWTFRNEDhflpldfqgnpqgEYELFFKLGIDGVFSDYPDTAYAV 326
Cdd:COG0584   180 VGPDYDLL-----------TPELVAAAHAAGLKVHVWTVNDPE-------------EMRRLLDLGVDGIITDRPDLLRAV 235
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 10-325 2.95e-51

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: 172.09  E-value: 2.95e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVArhTEFARRKTTKIIDGESKTG 89
Cdd:cd08571     1 PLVIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTIA--SVFPKRKKTYVVEGQSTSG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 WFTEDFTLGELKTLRAK-ERIPQLRPQNIFYNGLFEIPTFQEIIDLVKKKSAEinrkiGIYPETKHPSYF-KSIGLPLEK 167
Cdd:cd08571    79 IFSFDLTWAEIQTLKPIiSNPFSVLFRNPRNDNAGKILTLEDFLTLAKPKSLS-----GVWINVENAAFLaEHKGLLSVD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 168 PLLTTLSANGYQGANAPVFIQSFEVSNLQDLSTKTDLPLVQLVNNTGKPYDFVVSSNgstytdlittsgLEKIAKYAQAI 247
Cdd:cd08571   154 AVLTSLSKAGYDQTAKKVYISSPDSSVLKSFKKRVGTKLVFRVLDVDDTEPDTLLSN------------LTEIKKFASGV 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 248 GIHKNLLVSRDSIGKLLSPTSLIINAHASGLLVHAWTFRNEDHFLPLDFQGNPQGEYELFFKLG--IDGVFSDYPDTAYA 325
Cdd:cd08571   222 LVPKSYIWPVDSDSFLTPQTSVVQDAHKAGLEVYVSGFANEFVSLAYDYSADPTLEILSFVGNGnsVDGVITDFPATAAR 301
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 10-328 4.95e-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: 170.19  E-value: 4.95e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARHtefarrkttkiidgesktg 89
Cdd:cd08601     1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIERP------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 WFTEDFTLGELKTLRA----KERIPQL-RPQnifYNGLfEIPTFQEIIDLVKKKSaeinrkiGIYPETKHPSYFKSIglp 164
Cdd:cd08601    62 GPVKDYTLAEIKQLDAgswfNKAYPEYaRES---YSGL-KVPTLEEVIERYGGRA-------NYYIETKSPDLYPGM--- 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 165 lEKPLLTTLSANGYQG---ANAPVFIQSFEVSNLQDL-STKTDLPLVQLVNNTgkpydfvvssNGSTYTDlittSGLEKI 240
Cdd:cd08601   128 -EEKLLATLDKYGLLTdnlKNGQVIIQSFSKESLKKLhQLNPNIPLVQLLWYG----------EGAETYD----KWLDEI 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 241 AKYAQAIGIHKNLLvsrdsigkllsPTSLIINAHASGLLVHAWTFrnedhflpldfqgNPQGEYELFFKLGIDGVFSDYP 320
Cdd:cd08601   193 KEYAIGIGPSIADA-----------DPWMVHLIHKKGLLVHPYTV-------------NEKADMIRLINWGVDGMFTNYP 248


                  ....*...
gi 1210155409 321 DTAYAVNQ 328
Cdd:cd08601   249 DRLKEVLK 256
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 15-322 5.73e-48

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: 161.80  E-value: 5.73e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  15 HRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARhtefarrkttkiidgesktgwFTED 94
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG---------------------YVRD 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  95 FTLGELKTLR-AKERIPQLRPQNifynglFEIPTFQEIIDLVKKKSAEINRKIGIYPETKHPsYFKSIGLPLekpLLTTL 173
Cdd:pfam03009  60 LTLEELKRLDiGAGNSGPLSGER------VPFPTLEEVLEFDWDVGFNIEIKIKPYVEAIAP-EEGLIVKDL---LLSVD 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 174 SANGYQGANAPVFIQSFEVSNLQDLSTK-TDLPLVQLvnntgkpydfvvssngSTYTDLITTSGLEKIAKYAQAIGIHKN 252
Cdd:pfam03009 130 EILAKKADPRRVIFSSFNPDELKRLRELaPKLPLVFL----------------SSGRAYAEADLLERAAAFAGAPALLGE 193

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 253 LLVSRDSIGKLLSPtsliinAHASGLLVHAWTFRNEDhflpldfqgnpqgEYELFFKLGIDGVFSDYPDT 322
Cdd:pfam03009 194 VALVDEALPDLVKR------AHARGLVVHVWTVNNED-------------EMKRLLELGVDGVITDRPDT 244
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 10-324 1.11e-35

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: 131.31  E-value: 1.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARhTEFARRKTTkIIDGESKTG 89
Cdd:cd08604     1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVAT-SKFSNRATT-VPEIGSTSG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 WFTEDFTLGELKTLRakeriPQL-RPQNIFynGLFEIP---------TFQEIIDLVKKKSAeinrkIGIYPETKHPSYF- 158
Cdd:cd08604    79 IFTFDLTWSEIQTLK-----PAIsNPYSVT--GLFRNPanknagkflTLSDFLDLAKNKSL-----SGVLINVENAAYLa 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 159 KSIGLPLEKPLLTTLSANGYQGANAP-VFIQSFEVSNLQDLSTKTDLPLVQLVNNTGKPydfvvssngstytdlITTSGL 237
Cdd:cd08604   147 EKKGLDVVDAVLDALTNAGYDNQTAQkVLIQSTDSSVLAAFKKQISYERVYVVDETIRD---------------ASDSSI 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 238 EKIAKYAQAIGIHKNLLVSRDSiGKLLSPTSLIINAHASGLLVHAWTFRNEDHFLPLDFQGNPQGE-YELFFKLGIDGVF 316
Cdd:cd08604   212 EEIKKFADAVVIDRGSVFPVST-SFLTRQTNVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEiNSYVQGAGVDGFI 290


                  ....*...
gi 1210155409 317 SDYPDTAY 324
Cdd:cd08604   291 TEFPATAA 298
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 10-325 5.85e-31

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: 118.64  E-value: 5.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGAdyiePDLVS------TKDGVLIARHENEISETTDVARHteFARRKTTKIID 83
Cdd:cd08603     1 PLVIARGGFSGLFPDSSLFAYQFAASSSS----PDVALwcdlqlTKDGVGICLPDLNLDNSTTIARV--YPKRKKTYSVN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  84 GESKTGWFTEDFTLGELKTLRAKeripqlrpQNIF-----YNGLFEIPTFQEIIDLVKKKSAEINrkigiypeTKHPSYF 158
Cdd:cd08603    75 GVSTKGWFSVDFTLAELQQVTLI--------QGIFsrtpiFDGQYPISTVEDVVTLAKPEGLWLN--------VQHDAFY 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 159 KSIGLPLEKPLLTTLSANGYQganapvFIQSFEVSNLQDLSTKTDLPLVQLVNNTGKPYDFVVSSNgSTYTDLIttSGLE 238
Cdd:cd08603   139 QQHNLSMSSYLLSLSKTVKVD------YISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTN-QTYGSIL--KNLT 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 239 KIAKYAQAIGIHKNLLVSRDSIGKLLSPTSLIINAHASGLLVHAWTFRNeDHFLPLDFQGNPQGEYELFFKLG---IDGV 315
Cdd:cd08603   210 FIKTFASGILVPKSYIWPVDSDQYLQPATSLVQDAHKAGLEVYASGFAN-DFDISYNYSYDPVAEYLSFVGNGnfsVDGV 288

                         330
                  ....*....|
gi 1210155409 316 FSDYPDTAYA 325
Cdd:cd08603   289 LSDFPITASE 298
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 12-319 2.64e-26

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: 103.11  E-value: 2.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  12 IIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHeneisettdvarhtefarrkttkiidgesktgwf 91
Cdd:cd08556     1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIH---------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  92 tedftlgelktlrakeripqlrpqnifynglfEIPTFQEIIDLVKKksaeinrKIGIYPETKHPsyfkSIGLPLEKPLLT 171
Cdd:cd08556    47 --------------------------------DIPTLEEVLELVKG-------GVGLNIELKEP----TRYPGLEAKVAE 83

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 172 TLSANgyqGANAPVFIQSFEVSNLQDL-STKTDLPLVQLVnntgkpydfvvssngsTYTDLITTSGLEKIAKYAQAIGIH 250
Cdd:cd08556    84 LLREY---GLEERVVVSSFDHEALRALkELDPEVPTGLLV----------------DKPPLDPLLAELARALGADAVNPH 144

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1210155409 251 KNLLVsrdsigkllspTSLIINAHASGLLVHAWTFRNEDHFLPLdfqgnpqgeyelfFKLGIDGVFSDY 319
Cdd:cd08556   145 YKLLT-----------PELVRAAHAAGLKVYVWTVNDPEDARRL-------------LALGVDGIITDD 189
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 12-326 3.13e-24

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: 99.25  E-value: 3.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  12 IIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDvarhtefarrkTTKIIdgesktgwf 91
Cdd:cd08561     1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTD-----------GTGPV--------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  92 tEDFTLGELKTLRAKERIPQLRPQNIFYNGLFE-IPTFQEI----------IDLvkkksaeinrkigiypetkhpsyfKS 160
Cdd:cd08561    61 -ADLTLAELRRLDAGYHFTDDGGRTYPYRGQGIrIPTLEELfeafpdvrlnIEI------------------------KD 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 161 IGLPLEKPLLTTLSANGYQGAnapVFIQSFEVSNLQDLSTKTdlPLVQLVNNTGKPYDFVVSSNGstytdlittsGLEKI 240
Cdd:cd08561   116 DGPAAAAALADLIERYGAQDR---VLVASFSDRVLRRFRRLC--PRVATSAGEGEVAAFVLASRL----------GLGSL 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 241 AKY-AQAIGI---HKNL-LVSRDSIGKllsptsliinAHASGLLVHAWTFrnedhflpldfqgNPQGEYELFFKLGIDGV 315
Cdd:cd08561   181 YSPpYDALQIpvrYGGVpLVTPRFVRA----------AHAAGLEVHVWTV-------------NDPAEMRRLLDLGVDGI 237

                         330
                  ....*....|.
gi 1210155409 316 FSDYPDTAYAV 326
Cdd:cd08561   238 ITDRPDLLLEV 248
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 12-322 7.62e-24

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


Pssm-ID: 176524 [Multi-domain]  Cd Length: 233  Bit Score: 97.77  E-value: 7.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  12 IIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARHtefarrkttkiidgesktgwf 91
Cdd:cd08582     1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGA--------------------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  92 TEDFTLGELKTLRAKeripqlrpqnIFYNGLFE---IPTFQEIIDLVKKKSaeinrkIGIYPETKHPSYfksiGLPLEKP 168
Cdd:cd08582    60 VSDLTLAELRKLDIG----------SWKGESYKgekVPTLEEYLAIVPKYG------KKLFIEIKHPRR----GPEAEEE 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 169 LLTTLSANGYQGANaPVFIqSFevsnlqdlstktDLPLVQLVnntgKPYDFVVssngSTYTDLITTSGLEKIAKYAQAIG 248
Cdd:cd08582   120 LLKLLKESGLLPEQ-IVII-SF------------DAEALKRV----RELAPTL----ETLWLRNYKSPKEDPRPLAKSGG 177

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1210155409 249 IhknllvsrDSI----GKLLSPTsLIINAHASGLLVHAWTFRNEDhflpldfqgnpqgEYELFFKLGIDGVFSDYPDT 322
Cdd:cd08582   178 A--------AGLdlsyEKKLNPA-FIKALRDAGLKLNVWTVDDAE-------------DAKRLIELGVDSITTNRPGR 233
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 10-320 3.83e-23

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: 95.70  E-value: 3.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVarhtefarrkttkiidgeskTG 89
Cdd:cd08563     1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNG--------------------KG 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 WfTEDFTLGELKTLRAkeripqlrpqNIFYNGLF---EIPTFQEIIDLVKKKSAEINrkIgiypETKHpSYFKSIGlpLE 166
Cdd:cd08563    61 Y-VKDLTLEELKKLDA----------GSWFDEKFtgeKIPTLEEVLDLLKDKDLLLN--I----EIKT-DVIHYPG--IE 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 167 KPLLTTLsaNGYQGANApVFIQSFevsNLQDLSTKTDLplvqlvnntgkpydfvvssNGSTYTDLITTSGLEKIAKYAQA 246
Cdd:cd08563   121 KKVLELV--KEYNLEDR-VIFSSF---NHESLKRLKKL-------------------DPKIKLALLYETGLQDPKDYAKK 175

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1210155409 247 IGIhknllvsrDSI---GKLLSPtSLIINAHASGLLVHAWTFRNEDhflpldfqgnpqgEYELFFKLGIDGVFSDYP 320
Cdd:cd08563   176 IGA--------DSLhpdFKLLTE-EVVEELKKRGIPVRLWTVNEEE-------------DMKRLKDLGVDGIITNYP 230
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 12-321 9.59e-23

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: 95.46  E-value: 9.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  12 IIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEIS-ETTDVARHTEFARRKTTkiidgesktgw 90
Cdd:cd08567     3 LQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNpDITRDPDGAWLPYEGPA----------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  91 fTEDFTLGELKTLRAKERIPQLRPQNIFYNGLF----EIPTFQEIIDLVKKKSAEiNRKIGIypETKHPSYFKSIGLPLE 166
Cdd:cd08567    72 -LYELTLAEIKQLDVGEKRPGSDYAKLFPEQIPvpgtRIPTLEEVFALVEKYGNQ-KVRFNI--ETKSDPDRDILHPPPE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 167 KPLLTTLSANGYQGANAPVFIQSFEVSNLQDLSTKT-DLPLVQLvnntgkpydfvvssngstyTDLITTSGLEKIAKyaq 245
Cdd:cd08567   148 EFVDAVLAVIRKAGLEDRVVLQSFDWRTLQEVRRLApDIPTVAL-------------------TEETTLGNLPRAAK--- 205

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1210155409 246 AIGIHknlLVSRDSigKLLSPtSLIINAHASGLLVHAWTFrnedhflpldfqgNPQGEYELFFKLGIDGVFSDYPD 321
Cdd:cd08567   206 KLGAD---IWSPYF--TLVTK-ELVDEAHALGLKVVPWTV-------------NDPEDMARLIDLGVDGIITDYPD 262
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 13-325 1.21e-19

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: 88.63  E-value: 1.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  13 IAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARH-ENEISETTDVARHTEFARRKTTKIIDGESKTG-- 89
Cdd:cd08560    20 IGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHsQCDLHTTTNILAIPELAAKCTQPFTPANATKPas 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 --WFTEDFTLGELKTLRAKERI--PQLRPQNIFYNG-------LF----EIPTFQEIIDLVKkksaeinrKIGIY--PET 152
Cdd:cd08560   100 aeCCTSDITLAEFKSLCGKMDAsnPSATTPEEYQNGtpdwrtdLYatcgTLMTHKESIALFK--------SLGVKmtPEL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 153 KHPsyfkSIGLPLEKPLLTTLSA----NGYQGANAP---VFIQSFevsNLQDlstktdlpLVQLVNNTGkpyDF----VV 221
Cdd:cd08560   172 KSP----SVPMPFDGNYTQEDYAqqmiDEYKEAGVPpsrVWPQSF---NLDD--------IFYWIKNEP---DFgrqaVY 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 222 SSNGSTYTDLITT--SGLEKI-AKYAQAIGIHKNLLVSRDSIGKLLsPTSLIINAHASGLLVHAWTF--------RNEDH 290
Cdd:cd08560   234 LDDRDDTADFPATwsPSMDELkARGVNIIAPPIWMLVDPDENGKIV-PSEYAKAAKAAGLDIITWTLersgplasGGGWY 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1210155409 291 FLPLDFQGNPQGEYE-----LFFKLGIDGVFSDYPDTA--YA 325
Cdd:cd08560   313 YQTIEDVINNDGDMYnvldvLARDVGILGIFSDWPATVtyYA 354
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 11-138 1.11e-18

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


Pssm-ID: 176509 [Multi-domain]  Cd Length: 240  Bit Score: 83.89  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  11 IIIAHRGASGYR-PEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVarhtefarrkTTKIidgesktg 89
Cdd:cd08566     1 LVVAHRGGWGAGaPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNG----------KGKV-------- 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1210155409  90 wftEDFTLGELKTLRAKERIPQLRPQNifynglfeIPTFQEIIDLVKKK 138
Cdd:cd08566    63 ---SDLTLAEIRKLRLKDGDGEVTDEK--------VPTLEEALAWAKGK 100
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 10-323 1.18e-16

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: 78.41  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARHtefarrkttkiidgesktg 89
Cdd:cd08575     1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGL------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 wfTEDFTLGELKTLRAKERIPQLRPQNIFY--NGLFEIPTFQE----------IID--------LVKKKSAEINRK---- 145
Cdd:cd08575    62 --VSDLTYAELPPLDAGYGYTFDGGKTGYPrgGGDGRIPTLEEvfkafpdtpiNIDikspdaeeLIAAVLDLLEKYkred 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 146 IGIYPETKHPSYfksiglplekpllTTLSANgyqgaNAPVFIqSFevsnlqdlSTKTDLPLVQLVNNTGK-PYdfvvssn 224
Cdd:cd08575   140 RTVWGSTNPEYL-------------RALHPE-----NPNLFE-SF--------SMTRCLLLYLALGYTGLlPF------- 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 225 gstytDLITTSGLEKIAKYaqAIGIHKNLLVSRDSIGKLLSPTSLIINAHASGLLVHAWTFrnedhflpldfqgNPQGEY 304
Cdd:cd08575   186 -----VPIKESFFEIPRPV--IVLETFTLGEGASIVAALLWWPNLFDHLRKRGIQVYLWVL-------------NDEEDF 245

                         330
                  ....*....|....*....
gi 1210155409 305 ELFFKLGIDGVFSDYPDTA 323
Cdd:cd08575   246 EEAFDLGADGVMTDSPTKL 264
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 12-320 4.25e-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: 73.41  E-value: 4.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  12 IIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTD----VARHTeFARRKTtkiIDGESk 87
Cdd:cd08562     1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNgsgaVTELT-WAELAQ---LDAGS- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  88 tgWFTEDFtlgelktlrAKERipqlrpqnifynglfeIPTFQEIIDLVkkKSAEINRKIGIYPETKHPSYfksiglpLEK 167
Cdd:cd08562    76 --WFSPEF---------AGEP----------------IPTLADVLELA--RELGLGLNLEIKPDPGDEAL-------TAR 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 168 PLLTTLSAngYQGANAPVFIQSFEVSNLQDL-STKTDLPLVQLVNNTgkPYDFvvssngstytdlittsglEKIAKYAQA 246
Cdd:cd08562   120 VVAAALRE--LWPHASKLLLSSFSLEALRAArRAAPELPLGLLFDTL--PADW------------------LELLAALGA 177

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1210155409 247 IGIHKNLlvsrdsigKLLSPTsLIINAHASGLLVHAWTFRNEDHFLPLdfqgnpqgeyelfFKLGIDGVFSDYP 320
Cdd:cd08562   178 VSIHLNY--------RGLTEE-QVKALKDAGYKLLVYTVNDPARAAEL-------------LEWGVDAIFTDRP 229
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 12-137 1.01e-14

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


Pssm-ID: 176512 [Multi-domain]  Cd Length: 234  Bit Score: 72.64  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  12 IIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDvarhtefarrKTTKIIDgesktgwf 91
Cdd:cd08570     1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFG----------KDGLIID-------- 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1210155409  92 teDFTLGELKTLRAKERiPQLRpqnifynglfeIPTFQEIIDLVKK 137
Cdd:cd08570    63 --DSTWDELSHLRTIEE-PHQP-----------MPTLKDVLEWLVE 94
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 12-137 3.20e-14

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


Pssm-ID: 176521 [Multi-domain]  Cd Length: 220  Bit Score: 70.65  E-value: 3.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  12 IIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENeisettdvarhtefarrkTTKIIDGESKTGWf 91
Cdd:cd08579     1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDA------------------NLKRLAGVNKKVW- 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1210155409  92 teDFTLGELKTLRAKERIPQLRpqnifynglfeIPTFQEIIDLVKK 137
Cdd:cd08579    62 --DLTLEELKKLTIGENGHGAK-----------IPSLDEYLALAKG 94
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 12-109 1.48e-11

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: 63.58  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  12 IIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVA---RHTEFARRKTTKIidgeskT 88
Cdd:cd08565     1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTgavRDLTLAERKALRL------R 74

                          90       100
                  ....*....|....*....|..
gi 1210155409  89 GWFTEDF-TLGELKTLRAKERI 109
Cdd:cd08565    75 DSFGEKIpTLEEVLALFAPSGL 96
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 12-113 7.23e-11

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: 61.89  E-value: 7.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  12 IIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDvarhtefarrkTTKIIDgesktgwf 91
Cdd:cd08573     1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTD-----------GTGLVA-------- 61

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1210155409  92 teDFTLGELKTLRA-----------KERIPQLR 113
Cdd:cd08573    62 --ELTWEELRKLNAaakhrlssrfpGEKIPTLE 92
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 10-105 1.02e-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: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARhtEFARRKTTKiidgesktg 89
Cdd:cd08574     2 PALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVAD--VFPERAHER--------- 70

                          90
                  ....*....|....*.
gi 1210155409  90 wfTEDFTLGELKTLRA 105
Cdd:cd08574    71 --ASMFTWTDLQQLNA 84
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 13-71 1.27e-10

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


Pssm-ID: 176553 [Multi-domain]  Cd Length: 300  Bit Score: 61.46  E-value: 1.27e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1210155409  13 IAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARHT 71
Cdd:cd08612    30 ISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLV 88
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 12-94 6.90e-10

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: 57.45  E-value: 6.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  12 IIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARH-ENEISETTDVARHT-----EFAR-----RKTTK 80
Cdd:cd08555     1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHgPTLDRTTAGILPPTleevlELIAdylknPDYTI 80

                          90
                  ....*....|....
gi 1210155409  81 IIDGESKTGWFTED 94
Cdd:cd08555    81 ILSLEIKQDSPEYD 94
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 10-160 9.44e-10

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


Pssm-ID: 176551 [Multi-domain]  Cd Length: 315  Bit Score: 59.17  E-value: 9.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVArhTEFARRKTTKiidgesktg 89
Cdd:cd08609    27 PALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVK--DVFPGRDAAG--------- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  90 wfTEDFTLGELKTLRAKERIPQLRP----QNIFYNGLFE-----IPTFQEIIDLVKKKSAEInrKIGIYPETKHPSYFKS 160
Cdd:cd08609    96 --SNNFTWTELKTLNAGSWFLERRPfwtlSSLSEEDRREadnqtVPSLSELLDLAKKHNVSI--MFDLRNENNSHVFYSS 171
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 12-131 1.25e-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 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: 57.73  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  12 IIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVARHT---EFARRKTTKIIDGEskt 88
Cdd:cd08581     1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLhelEDAELDSLRVAEPA--- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1210155409  89 gWFTEDFTLGELKTLRAKERIPQLRPQnifynglfeIPTFQEI 131
Cdd:cd08581    78 -RFGSRFAGEPLPSLAAVVQWLAQHPQ---------VTLFVEI 110
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 9-326 1.39e-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: 57.87  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409   9 PPIIIAHRGA--SGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEisetTDVARHTEFARRkttkiiDGES 86
Cdd:cd08564     3 RPIIVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHGTE----DDTNPDTSIQLD------DSGF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  87 KTgwfTEDFTLGELKTLRAKEripqlrPQNIFYNGLFE-----IPTFQEIIDLVKKKsaeINRKIgiypETKHPSyfksi 161
Cdd:cd08564    73 KN---INDLSLDEITRLHFKQ------LFDEKPCGADEikgekIPTLEDVLVTFKDK---LKYNI----ELKGRE----- 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 162 gLPLEKPLLTTLSANGYQGAnapVFIQSFEVSNLQDL-----STKTDLPLVQLVNNTGKPydfvvssngsTYTDLITTsg 236
Cdd:cd08564   132 -VGLGERVLNLVEKYGMILQ---VHFSSFLHYDRLDLlkalrPNKLNVPIALLFNEVKSP----------SPLDFLEQ-- 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 237 lekiAKYAQAIGIHknllVSRDSIGKllsptSLIINAHASGLLVHAW--TFRNEDhflpldfqgnpQGEYELFFKLGIDG 314
Cdd:cd08564   196 ----AKYYNATWVN----FSYDFWTE-----EFVKKAHENGLKVMTYfdEPVNDN-----------EEDYKVYLELGVDC 251

                         330
                  ....*....|..
gi 1210155409 315 VFSDYPDTAYAV 326
Cdd:cd08564   252 ICPNDPVLLVNF 263
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 10-132 1.43e-09

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: 58.11  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTdvarhtefarrkttkiiDGESKtg 89
Cdd:cd08580     1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLT-----------------NGSGA-- 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1210155409  90 wfTEDFTLGELKTLRAKEripQLRPQN-IFYNGL-FEIPTFQEII 132
Cdd:cd08580    62 --VSAYTAAQLATLNAGY---NFKPEGgYPYRGKpVGIPTLEQVL 101
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 11-153 1.01e-08

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: 55.00  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  11 IIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVarhtefarrkttkiiDGESKtgw 90
Cdd:cd08568     1 IILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGV---------------DLKVK--- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  91 fteDFTLGELKTLRAK-ERIPQLR------PQN-IFYNGLFEIPTFQEIIDLVKKKSAE------------INRKIGIYP 150
Cdd:cd08568    63 ---ELTYKELKKLHPGgELIPTLEevfralPNDaIINVEIKDIDAVEPVLEIVEKFNALdrvifssfnhdaLRELRKLDP 139


                  ...
gi 1210155409 151 ETK 153
Cdd:cd08568   140 DAK 142
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 7-67 1.80e-06

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


Pssm-ID: 176552 [Multi-domain]  Cd Length: 316  Bit Score: 49.10  E-value: 1.80e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1210155409   7 GKPPIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDV 67
Cdd:cd08610    20 GPKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNI 80
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 2-103 1.81e-05

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: 45.81  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409   2 TKTFTGKP---PIIIAHRGASG-----------------YRPEH-----TLAAYELAIALGADYIEPDLVSTKDGVLIAR 56
Cdd:cd08613    13 TSLLAPPPggkPKLLAHRGLAQtfdregvendtctaeriDPPTHdylenTIASMQAAFDAGADVVELDVHPTKDGEFAVF 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1210155409  57 HENEISETTDvarhtefarrkttkiIDGEsktgwfTEDFTLGELKTL 103
Cdd:cd08613    93 HDWTLDCRTD---------------GSGV------TRDHTMAELKTL 118
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 10-66 1.99e-05

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 45.32  E-value: 1.99e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTD 66
Cdd:PRK09454    8 PRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSN 64
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 10-69 3.64e-05

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: 45.22  E-value: 3.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  10 PIIIAHRGASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETTDVAR 69
Cdd:cd08608     2 PAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDR 61
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 11-319 2.00e-04

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


Pssm-ID: 176514 [Multi-domain]  Cd Length: 293  Bit Score: 42.65  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  11 IIIAHRGA---------SGYRpEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISETtdvarhtefarRKTTKI 81
Cdd:cd08572     1 LVIGHRGLgknyasgslAGIR-ENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVS-----------EKSKTG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  82 IDGESKTGWFTEDFTLGELKTL----------RAKERIPQLRPQN---IFYNGLFeiPTFQEIIDlvkkksaEINRKIGI 148
Cdd:cd08572    69 SDEGELIEVPIHDLTLEQLKELglqhisalkrKALTRKAKGPKPNpwgMDEHDPF--PTLQEVLE-------QVPKDLGF 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 149 YPETKHPSYFKSIGLPLEkpllTTLSANGY----------QGANAPVFIQSFEVSNLQDLSTKTDL-PLVQLVNntgkpy 217
Cdd:cd08572   140 NIEIKYPQLLEDGEGELT----PYFERNAFvdtilavvfeHAGGRRIIFSSFDPDICIMLRLKQNKyPVLFLTN------ 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409 218 dfvVSSNGSTYTDLITTSgLEKIAKYAQAIGIhknLLVSRDSiGKLLSPTSLIINAHASGLLVHAWTFRNEDHflpldfq 297
Cdd:cd08572   210 ---GGTNEVEHMDPRRRS-LQAAVNFALAEGL---LGVVLHA-EDLLKNPSLISLVKALGLVLFTYGDDNNDP------- 274

                         330       340
                  ....*....|....*....|..
gi 1210155409 298 gnpqGEYELFFKLGIDGVFSDY 319
Cdd:cd08572   275 ----ENVKKQKELGVDGVIYDR 292
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 11-62 2.23e-04

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


Pssm-ID: 176547 [Multi-domain]  Cd Length: 282  Bit Score: 42.40  E-value: 2.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1210155409  11 IIIAHRG------------ASGYRpEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEIS 62
Cdd:cd08605     1 AVIGHRGlgmnrashqpsvGPGIR-ENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIV 63
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 10-71 6.27e-04

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: 40.89  E-value: 6.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1210155409  10 PIIIAHRGASGYRPEH--------TLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISET-TDVARHT 71
Cdd:cd08606     2 VQVIGHRGLGKNTAERkslqlgenTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETgTDVPIHD 72
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 13-90 1.25e-03

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


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 39.98  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  13 IAHR--GASGYRPEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHE----------NEISETTDVARHTEFarrKTTK 80
Cdd:cd08583     2 IAHAmgGIDGKTYTNSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHSwdesllkqlgLPTSKNTKPLSYEEF---KSKK 78

                          90
                  ....*....|
gi 1210155409  81 IIDGESKTGW 90
Cdd:cd08583    79 IYGKYTPMDF 88
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 13-178 1.73e-03

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: 39.58  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  13 IAHRGA-SGYR------PEHTLAAYELAIALGADYIEPDLVSTKDGVLIARHENEISetTDVARHTEFARRKTTKIIdge 85
Cdd:cd08607     3 VGHRGAgNSYTaasavvRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLR--VSLKSKGDSDRDDLLEVP--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210155409  86 sktgwfTEDFTLGELKTLRAKERIpqlRPQNIFYNGLFE---------IPTFQEIIDlvkkksaEINRKIGIYPETKHPS 156
Cdd:cd08607    78 ------VKDLTYEQLKLLKLFHIS---ALKVKEYKSVEEdedppehqpFPTLSDVLE-------SVPEDVGFNIEIKWPQ 141

                         170       180
                  ....*....|....*....|..
gi 1210155409 157 YFKSiGLPlEKPLLTTLSANGY 178
Cdd:cd08607   142 QQKD-GSW-ESELFTYFDRNLF 161
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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