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Conserved domains on  [gi|300579209|emb|CBV20687|]
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unnamed protein product [Pseudomonas aeruginosa PAO1]

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 ...
 55-373 0e+00

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: 516.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQHPEFADRKRTQKVDGVELTG 134
Cdd:cd08602    1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHPEFADRKTTKTVDGVNVTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 135 WFSEDFTLAELKTLRAIERIPTIRPGnarLDGTFEIPTLQEIIDLVKSLQISQQRTIGLYPEIKHGTHF-QRLGLAMERP 213
Cdd:cd08602   81 WFTEDFTLAELKTLRARQRLPYRDQS---YDGQFPIPTFEEIIALAKAASAATGRTVGIYPEIKHPTYFnAPLGLPMEDK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 214 LVKTLHRNGYLGPRAPVFIQSFEVNNLKELKRLTGIRLVQLYGS-GQPYDQQAAGGSLTYAEMATAKGLRQVARYAYGVG 292
Cdd:cd08602  158 LLETLKKYGYTGKKAPVFIQSFEVTNLKYLRNKTDLPLVQLIDDaTIPPQDTPEGDSRTYADLTTDAGLKEIATYADGIG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 293 PDKSYVIPRDANGNLGQPTRFVGDAHAAGLKVHPYTFRAENSFLPAEFrsadgnpqsRGDLAGEIRAYLDAGIDGLFSDQ 372
Cdd:cd08602  238 PWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNENTFLPPDF---------FGDPYAEYRAFLDAGVDGLFTDF 308


                 .
gi 300579209 373 P 373
Cdd:cd08602  309 P 309
 
Name Accession Description Interval E-value
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 55-373 0e+00

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: 516.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQHPEFADRKRTQKVDGVELTG 134
Cdd:cd08602    1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHPEFADRKTTKTVDGVNVTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 135 WFSEDFTLAELKTLRAIERIPTIRPGnarLDGTFEIPTLQEIIDLVKSLQISQQRTIGLYPEIKHGTHF-QRLGLAMERP 213
Cdd:cd08602   81 WFTEDFTLAELKTLRARQRLPYRDQS---YDGQFPIPTFEEIIALAKAASAATGRTVGIYPEIKHPTYFnAPLGLPMEDK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 214 LVKTLHRNGYLGPRAPVFIQSFEVNNLKELKRLTGIRLVQLYGS-GQPYDQQAAGGSLTYAEMATAKGLRQVARYAYGVG 292
Cdd:cd08602  158 LLETLKKYGYTGKKAPVFIQSFEVTNLKYLRNKTDLPLVQLIDDaTIPPQDTPEGDSRTYADLTTDAGLKEIATYADGIG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 293 PDKSYVIPRDANGNLGQPTRFVGDAHAAGLKVHPYTFRAENSFLPAEFrsadgnpqsRGDLAGEIRAYLDAGIDGLFSDQ 372
Cdd:cd08602  238 PWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNENTFLPPDF---------FGDPYAEYRAFLDAGVDGLFTDF 308


                 .
gi 300579209 373 P 373
Cdd:cd08602  309 P 309
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 43-377 4.86e-79

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 246.89  E-value: 4.86e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  43 ASVRHPASDERSPLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQhpEFADRK 122
Cdd:PRK11143  15 AGSAAAAADSAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAE--RFPDRA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 123 RTqkvDGveltGWFSEDFTLAELKTLRAIERIpTIRPGN------ARL---DGTFEIPTLQEIIDLVKSLQISQQRTIGL 193
Cdd:PRK11143  93 RK---DG----RYYAIDFTLDEIKSLKFTEGF-DIENGKkvqvypGRFpmgKSDFRVHTFEEEIEFIQGLNHSTGKNIGI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 194 YPEIKHGTHFQRLGLAMERPLVKTLHRNGYLGPRAPVFIQSFEVNNLKELKRL------TGIRLVQL-----YGSGQPYD 262
Cdd:PRK11143 165 YPEIKAPWFHHQEGKDIAAKVLEVLKKYGYTGKDDKVYLQCFDANELKRIKNElepkmgMDLKLVQLiaytdWNETQEKQ 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 263 QQAAGGSLTYAEMATAKGLRQVARYAYGVGPDKSYVIPRDA-NGNLgQPTRFVGDAHAAGLKVHPYTFRAENsfLPAEFR 341
Cdd:PRK11143 245 PDGKWVNYNYDWMFKPGAMKEVAKYADGIGPDYHMLVDETStPGNI-KLTGMVKEAHQAKLVVHPYTVRADQ--LPEYAT 321

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 300579209 342 SADgnpQSRGDLageiraYLDAGIDGLFSDQPDVAV 377
Cdd:PRK11143 322 DVN---QLYDIL------YNQAGVDGVFTDFPDKAV 348
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
53-382 3.92e-66

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 209.73  E-value: 3.92e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  53 RSPLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVaqhpefadrkrTQKVdgvel 132
Cdd:COG0584    1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNG-----------TGRV----- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 133 tgwfsEDFTLAELKTLRAieriptirpGNARLDGTFEIPTLQEIIDLVKslqisqqRTIGLYPEIKHGTHFQRlglAMER 212
Cdd:COG0584   65 -----ADLTLAELRQLDA---------GSGPDFAGERIPTLEEVLELVP-------GDVGLNIEIKSPPAAEP---DLAE 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 213 PLVKTLHRNGYLGpraPVFIQSFEVNNLKELKRLT-GIRLVQLYGSgqpydqqAAGGSLTYAEmatakglrqvARYAYGV 291
Cdd:COG0584  121 AVAALLKRYGLED---RVIVSSFDPEALRRLRELApDVPLGLLVEE-------LPADPLELAR----------ALGADGV 180

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 292 GPDKSYViprdangnlgqPTRFVGDAHAAGLKVHPYTFRAENsflpaefrsadgnpqsrgdlagEIRAYLDAGIDGLFSD 371
Cdd:COG0584  181 GPDYDLL-----------TPELVAAAHAAGLKVHVWTVNDPE----------------------EMRRLLDLGVDGIITD 227

                        330
                 ....*....|.
gi 300579209 372 QPDVAVRLREQ 382
Cdd:COG0584  228 RPDLLRAVLRE 238
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 60-375 3.91e-39

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: 139.84  E-value: 3.91e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209   60 HRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQhpefadrkrtqkvdgveltgwFSED 139
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG---------------------YVRD 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  140 FTLAELKTLRAIERIPTIRPGNArldgtFEIPTLQEIIDLVKSLQISQQRTIGLYPEIKHgthfqRLGLAMERPLVKTL- 218
Cdd:pfam03009  60 LTLEELKRLDIGAGNSGPLSGER-----VPFPTLEEVLEFDWDVGFNIEIKIKPYVEAIA-----PEEGLIVKDLLLSVd 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  219 -HRNGYLGPRaPVFIQSFEVNNLKELKRL-TGIRLVQLygsgqpydqqaaggsLTYAEMATAKGLRQVARYAYGVGpdks 296
Cdd:pfam03009 130 eILAKKADPR-RVIFSSFNPDELKRLRELaPKLPLVFL---------------SSGRAYAEADLLERAAAFAGAPA---- 189

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300579209  297 yVIPRDANGNLGQPtRFVGDAHAAGLKVHPYTFRAENsflpaefrsadgnpqsrgdlagEIRAYLDAGIDGLFSDQPDV 375
Cdd:pfam03009 190 -LLGEVALVDEALP-DLVKRAHARGLVVHVWTVNNED----------------------EMKRLLELGVDGVITDRPDT 244
 
Name Accession Description Interval E-value
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 55-373 0e+00

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: 516.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQHPEFADRKRTQKVDGVELTG 134
Cdd:cd08602    1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHPEFADRKTTKTVDGVNVTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 135 WFSEDFTLAELKTLRAIERIPTIRPGnarLDGTFEIPTLQEIIDLVKSLQISQQRTIGLYPEIKHGTHF-QRLGLAMERP 213
Cdd:cd08602   81 WFTEDFTLAELKTLRARQRLPYRDQS---YDGQFPIPTFEEIIALAKAASAATGRTVGIYPEIKHPTYFnAPLGLPMEDK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 214 LVKTLHRNGYLGPRAPVFIQSFEVNNLKELKRLTGIRLVQLYGS-GQPYDQQAAGGSLTYAEMATAKGLRQVARYAYGVG 292
Cdd:cd08602  158 LLETLKKYGYTGKKAPVFIQSFEVTNLKYLRNKTDLPLVQLIDDaTIPPQDTPEGDSRTYADLTTDAGLKEIATYADGIG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 293 PDKSYVIPRDANGNLGQPTRFVGDAHAAGLKVHPYTFRAENSFLPAEFrsadgnpqsRGDLAGEIRAYLDAGIDGLFSDQ 372
Cdd:cd08602  238 PWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNENTFLPPDF---------FGDPYAEYRAFLDAGVDGLFTDF 308


                 .
gi 300579209 373 P 373
Cdd:cd08602  309 P 309
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 55-373 4.78e-147

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: 418.22  E-value: 4.78e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQHPEFADRKRtqkvdgvelTG 134
Cdd:cd08559    1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVAEHFPFRGRKD---------TG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 135 WFSEDFTLAELKTLRAIERIPTIRPGNARL-DGTFEIPTLQEIIDLVKSLQISQQRTIGLYPEIKHGTHFQRLGLAMERP 213
Cdd:cd08559   72 YFVIDFTLAELKTLRAGSWFNQRYPERAPSyYGGFKIPTLEEVIELAQGLNKSTGRNVGIYPETKHPTFHKQEGPDIEEK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 214 LVKTLHRNGYLGPRAPVFIQSFEVNNLKELKRLT-GIRLVQLYGSGQPYDQQAAggsLTYAEMATAKGLRQVARYAYGVG 292
Cdd:cd08559  152 LLEVLKKYGYTGKNDPVFIQSFEPESLKRLRNETpDIPLVQLIDYGDWAETDKK---YTYAWLTTDAGLKEIAKYADGIG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 293 PDKSYVIPRDANGnLGQPTRFVGDAHAAGLKVHPYTFRAENSFLpaeFRSADGNPqsrgdlageIRAYLDAGIDGLFSDQ 372
Cdd:cd08559  229 PWKSLIIPEDSNG-LLVPTDLVKDAHKAGLLVHPYTFRNENLFL---APDFKQDM---------DALYNAAGVDGVFTDF 295


                 .
gi 300579209 373 P 373
Cdd:cd08559  296 P 296
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 55-374 4.68e-80

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: 248.46  E-value: 4.68e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQhpEFADRKRTqkvDGveltG 134
Cdd:cd08600    1 KIIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAE--KFPDRKRK---DG----R 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 135 WFSEDFTLAELKTLRAIERIPTIRPGNARL--------DGTFEIPTLQEIIDLVKSLQISQQRTIGLYPEIKHGTHFQRL 206
Cdd:cd08600   72 YYVIDFTLDELKSLSVTERFDIENGKKVQVypnrfplwKSDFKIHTLEEEIELIQGLNKSTGKNVGIYPEIKAPWFHHQE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 207 GLAMERPLVKTLHRNGYLGPRAPVFIQSFEVNNLKELKRLTG------IRLVQLYGSGQ----PYDQQAAGGSLTYAEMA 276
Cdd:cd08600  152 GKDIAAATLEVLKKYGYTSKNDKVYLQTFDPNELKRIKNELLpkmgmdLKLVQLIAYTDwgetQEKDPGGWVNYDYDWMF 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 277 TAKGLRQVARYAYGVGPDKSYVIPRDANGNLGQPTRFVGDAHAAGLKVHPYTFRAENsfLPAEFRSADgnpQSRGDLage 356
Cdd:cd08600  232 TKGGLKEIAKYADGVGPWYSMIIEEKSSKGNIVLTDLVKDAHEAGLEVHPYTVRKDA--LPEYAKDAD---QLLDAL--- 303

                        330
                 ....*....|....*...
gi 300579209 357 iraYLDAGIDGLFSDQPD 374
Cdd:cd08600  304 ---LNKAGVDGVFTDFPD 318
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 43-377 4.86e-79

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 246.89  E-value: 4.86e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  43 ASVRHPASDERSPLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQhpEFADRK 122
Cdd:PRK11143  15 AGSAAAAADSAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAE--RFPDRA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 123 RTqkvDGveltGWFSEDFTLAELKTLRAIERIpTIRPGN------ARL---DGTFEIPTLQEIIDLVKSLQISQQRTIGL 193
Cdd:PRK11143  93 RK---DG----RYYAIDFTLDEIKSLKFTEGF-DIENGKkvqvypGRFpmgKSDFRVHTFEEEIEFIQGLNHSTGKNIGI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 194 YPEIKHGTHFQRLGLAMERPLVKTLHRNGYLGPRAPVFIQSFEVNNLKELKRL------TGIRLVQL-----YGSGQPYD 262
Cdd:PRK11143 165 YPEIKAPWFHHQEGKDIAAKVLEVLKKYGYTGKDDKVYLQCFDANELKRIKNElepkmgMDLKLVQLiaytdWNETQEKQ 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 263 QQAAGGSLTYAEMATAKGLRQVARYAYGVGPDKSYVIPRDA-NGNLgQPTRFVGDAHAAGLKVHPYTFRAENsfLPAEFR 341
Cdd:PRK11143 245 PDGKWVNYNYDWMFKPGAMKEVAKYADGIGPDYHMLVDETStPGNI-KLTGMVKEAHQAKLVVHPYTVRADQ--LPEYAT 321

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 300579209 342 SADgnpQSRGDLageiraYLDAGIDGLFSDQPDVAV 377
Cdd:PRK11143 322 DVN---QLYDIL------YNQAGVDGVFTDFPDKAV 348
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
53-382 3.92e-66

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 209.73  E-value: 3.92e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  53 RSPLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVaqhpefadrkrTQKVdgvel 132
Cdd:COG0584    1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNG-----------TGRV----- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 133 tgwfsEDFTLAELKTLRAieriptirpGNARLDGTFEIPTLQEIIDLVKslqisqqRTIGLYPEIKHGTHFQRlglAMER 212
Cdd:COG0584   65 -----ADLTLAELRQLDA---------GSGPDFAGERIPTLEEVLELVP-------GDVGLNIEIKSPPAAEP---DLAE 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 213 PLVKTLHRNGYLGpraPVFIQSFEVNNLKELKRLT-GIRLVQLYGSgqpydqqAAGGSLTYAEmatakglrqvARYAYGV 291
Cdd:COG0584  121 AVAALLKRYGLED---RVIVSSFDPEALRRLRELApDVPLGLLVEE-------LPADPLELAR----------ALGADGV 180

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 292 GPDKSYViprdangnlgqPTRFVGDAHAAGLKVHPYTFRAENsflpaefrsadgnpqsrgdlagEIRAYLDAGIDGLFSD 371
Cdd:COG0584  181 GPDYDLL-----------TPELVAAAHAAGLKVHVWTVNDPE----------------------EMRRLLDLGVDGIITD 227

                        330
                 ....*....|.
gi 300579209 372 QPDVAVRLREQ 382
Cdd:COG0584  228 RPDLLRAVLRE 238
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 55-380 6.49e-54

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: 178.66  E-value: 6.49e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQHpefadrkrtqkvdgveltg 134
Cdd:cd08601    1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIERP------------------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 135 WFSEDFTLAELKTLRA--------IERiptIRPGNARLDgtfeIPTLQEIIDLVKslqisqqRTIGLYPEIKHGTHFQrl 206
Cdd:cd08601   62 GPVKDYTLAEIKQLDAgswfnkayPEY---ARESYSGLK----VPTLEEVIERYG-------GRANYYIETKSPDLYP-- 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 207 glAMERPLVKTLHRNGYLGPRAP---VFIQSFEVNNLKELKRLT-GIRLVQLYGSGQPYDqqaaggsltyaemATAKGLR 282
Cdd:cd08601  126 --GMEEKLLATLDKYGLLTDNLKngqVIIQSFSKESLKKLHQLNpNIPLVQLLWYGEGAE-------------TYDKWLD 190

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 283 QVARYAYGVGPDKSYVIPrdangnlgqptRFVGDAHAAGLKVHPYTFraensflpaefrsadgnpqsrgDLAGEIRAYLD 362
Cdd:cd08601  191 EIKEYAIGIGPSIADADP-----------WMVHLIHKKGLLVHPYTV----------------------NEKADMIRLIN 237

                        330
                 ....*....|....*...
gi 300579209 363 AGIDGLFSDQPDVAVRLR 380
Cdd:cd08601  238 WGVDGMFTNYPDRLKEVL 255
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 55-378 4.07e-50

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: 170.54  E-value: 4.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQhpEFADRKRTQKVDGVELTG 134
Cdd:cd08571    1 PLVIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTIAS--VFPKRKKTYVVEGQSTSG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 135 WFSEDFTLAELKTLR-AIERIPTIRPGNARLDGTFEIPTLQEIIDLVKSLQISqqrtiGLYPEIKHGTHF-QRLGLAMER 212
Cdd:cd08571   79 IFSFDLTWAEIQTLKpIISNPFSVLFRNPRNDNAGKILTLEDFLTLAKPKSLS-----GVWINVENAAFLaEHKGLLSVD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 213 PLVKTLHRNGYLGPRAPVFIQSFEVNNLKELKRLTGIRLVQLYgsgqpYDQQAAGGSltyaemATAKGLRQVARYAYGVG 292
Cdd:cd08571  154 AVLTSLSKAGYDQTAKKVYISSPDSSVLKSFKKRVGTKLVFRV-----LDVDDTEPD------TLLSNLTEIKKFASGVL 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 293 PDKSYVIPRDANGNLGQPTRFVGDAHAAGLKVHPYTFRAENSFLPAEFRSadgnpqsrgDLAGEIRAYLD--AGIDGLFS 370
Cdd:cd08571  223 VPKSYIWPVDSDSFLTPQTSVVQDAHKAGLEVYVSGFANEFVSLAYDYSA---------DPTLEILSFVGngNSVDGVIT 293


                 ....*...
gi 300579209 371 DQPDVAVR 378
Cdd:cd08571  294 DFPATAAR 301
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 60-375 3.91e-39

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: 139.84  E-value: 3.91e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209   60 HRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQhpefadrkrtqkvdgveltgwFSED 139
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG---------------------YVRD 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  140 FTLAELKTLRAIERIPTIRPGNArldgtFEIPTLQEIIDLVKSLQISQQRTIGLYPEIKHgthfqRLGLAMERPLVKTL- 218
Cdd:pfam03009  60 LTLEELKRLDIGAGNSGPLSGER-----VPFPTLEEVLEFDWDVGFNIEIKIKPYVEAIA-----PEEGLIVKDLLLSVd 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  219 -HRNGYLGPRaPVFIQSFEVNNLKELKRL-TGIRLVQLygsgqpydqqaaggsLTYAEMATAKGLRQVARYAYGVGpdks 296
Cdd:pfam03009 130 eILAKKADPR-RVIFSSFNPDELKRLRELaPKLPLVFL---------------SSGRAYAEADLLERAAAFAGAPA---- 189

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300579209  297 yVIPRDANGNLGQPtRFVGDAHAAGLKVHPYTFRAENsflpaefrsadgnpqsrgdlagEIRAYLDAGIDGLFSDQPDV 375
Cdd:pfam03009 190 -LLGEVALVDEALP-DLVKRAHARGLVVHVWTVNNED----------------------EMKRLLELGVDGVITDRPDT 244
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 55-376 8.17e-37

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: 135.21  E-value: 8.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGAdyvePDLVM------TRDGKLVARHDNELGLTTDVAQHpeFADRKRTQKVD 128
Cdd:cd08603    1 PLVIARGGFSGLFPDSSLFAYQFAASSSS----PDVALwcdlqlTKDGVGICLPDLNLDNSTTIARV--YPKRKKTYSVN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 129 GVELTGWFSEDFTLAELKTLRAIERIPTiRPgnARLDGTFEIPTLQEIIDLVKSLqisqqrtiGLYPEIKHGTHFQRLGL 208
Cdd:cd08603   75 GVSTKGWFSVDFTLAELQQVTLIQGIFS-RT--PIFDGQYPISTVEDVVTLAKPE--------GLWLNVQHDAFYQQHNL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 209 AMERPLVKTLHRNGylgpraPVFIQSFEVNNLKELKRLTGIRLVQLYGSGQPYDQQAAGGSLTYAEMAtaKGLRQVARYA 288
Cdd:cd08603  144 SMSSYLLSLSKTVK------VDYISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSIL--KNLTFIKTFA 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 289 YGVGPDKSYVIPRDANGNLGQPTRFVGDAHAAGLKVHPYTFraENSFLPAEFRSADgnPQSrgdlagEIRAYLDAG---I 365
Cdd:cd08603  216 SGILVPKSYIWPVDSDQYLQPATSLVQDAHKAGLEVYASGF--ANDFDISYNYSYD--PVA------EYLSFVGNGnfsV 285

                        330
                 ....*....|.
gi 300579209 366 DGLFSDQPDVA 376
Cdd:cd08603  286 DGVLSDFPITA 296
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 57-336 1.38e-29

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: 113.95  E-value: 1.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  57 VIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELglttdvaqhpefadrKRTQKVDGVeltgwf 136
Cdd:cd08582    1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTL---------------KRTSGGDGA------ 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 137 SEDFTLAELKTLRAIERIPTIRPGNArldgtfeIPTLQEIIDLVKslqisqQRTIGLYPEIKHGThfqRLGLAMERpLVK 216
Cdd:cd08582   60 VSDLTLAELRKLDIGSWKGESYKGEK-------VPTLEEYLAIVP------KYGKKLFIEIKHPR---RGPEAEEE-LLK 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 217 TLHRNGYLGPRaPVFIqSFEVNNLKELKRLT-GIRLVQLYGSGQPydqqaaggsltyaematAKGLRQVARYAYGVGPDK 295
Cdd:cd08582  123 LLKESGLLPEQ-IVII-SFDAEALKRVRELApTLETLWLRNYKSP-----------------KEDPRPLAKSGGAAGLDL 183

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 300579209 296 SYVIPRDANgnlgqptrFVGDAHAAGLKVHPYTFRAENSFL 336
Cdd:cd08582  184 SYEKKLNPA--------FIKALRDAGLKLNVWTVDDAEDAK 216
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 57-371 5.22e-28

Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and similar proteins; The typical glycerophosphodiester phosphodiesterase domain (GDPD) consists of a TIM barrel and a small insertion domain named the GDPD-insertion (GDPD-I) domain, which is specific for GDPD proteins. This family corresponds to both typical GDPD domain and GDPD-like domain which lacks the GDPD-I region. Members in this family mainly consist of a large family of prokaryotic and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), and a number of uncharacterized homologs. Sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria are also included in this family. GDPD plays an essential role in glycerol metabolism and catalyzes the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols are major sources of carbon and phosphate. Its catalytic mechanism is based on the metal ion-dependent acid-base reaction, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). Both, GDPD related proteins and PI-PLCs, belong to the superfamily of PI-PLC-like phosphodiesterases.


Pssm-ID: 176499 [Multi-domain]  Cd Length: 189  Bit Score: 108.50  E-value: 5.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  57 VIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDnelglttdvaqhpefadrkrtqkvdgveltgwf 136
Cdd:cd08556    1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 137 sedftlaelktlraieriptirpgnarldgtfeIPTLQEIIDLVKslqisqqRTIGLYPEIKHGTHFQRLglamERPLVK 216
Cdd:cd08556   48 ---------------------------------IPTLEEVLELVK-------GGVGLNIELKEPTRYPGL----EAKVAE 83

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 217 TLHRngyLGPRAPVFIQSFEVNNLKELKRL-TGIRLVQLYgsgqpydqqaAGGSLTYAEMATAKGLRqvaryAYGVGPDK 295
Cdd:cd08556   84 LLRE---YGLEERVVVSSFDHEALRALKELdPEVPTGLLV----------DKPPLDPLLAELARALG-----ADAVNPHY 145

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300579209 296 SYVIPrdangnlgqptRFVGDAHAAGLKVHPYTFraensflpaefrsadgnpqsrgDLAGEIRAYLDAGIDGLFSD 371
Cdd:cd08556  146 KLLTP-----------ELVRAAHAAGLKVYVWTV----------------------NDPEDARRLLALGVDGIITD 188
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 55-375 1.06e-26

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: 107.01  E-value: 1.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELG-LTTDVAQHPEFADRKRTQKvdgvelt 133
Cdd:cd08567    1 FDLQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNpDITRDPDGAWLPYEGPALY------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 134 gwfseDFTLAELKTLRAIERIPTIR-----PGNARLDGTfEIPTLQEIIDLVKSLQISQQRtigLYPEIK---HGTHFQR 205
Cdd:cd08567   74 -----ELTLAEIKQLDVGEKRPGSDyaklfPEQIPVPGT-RIPTLEEVFALVEKYGNQKVR---FNIETKsdpDRDILHP 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 206 LGLAMERPLVKTLHRNGYLgPRapVFIQSFEVNNLKELKRLT-GIRLVQLygsgqpYDQQAAGGsltYAEMATAKGlrqv 284
Cdd:cd08567  145 PPEEFVDAVLAVIRKAGLE-DR--VVLQSFDWRTLQEVRRLApDIPTVAL------TEETTLGN---LPRAAKKLG---- 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 285 aryAYGVGPDKSYVIPRDangnlgqptrfVGDAHAAGLKVHPYT-FRAEnsflpaefrsadgnpqsrgdlagEIRAYLDA 363
Cdd:cd08567  209 ---ADIWSPYFTLVTKEL-----------VDEAHALGLKVVPWTvNDPE-----------------------DMARLIDL 251

                        330
                 ....*....|..
gi 300579209 364 GIDGLFSDQPDV 375
Cdd:cd08567  252 GVDGIITDYPDL 263
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 55-378 4.23e-25

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: 103.57  E-value: 4.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQHPeFADRKRT----QKVDGV 130
Cdd:cd08604    1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSK-FSNRATTvpeiGSTSGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 131 eltgwFSEDFTLAELKTLRAIERIPTIRPG---NARLDGTFEIPTLQEIIDLVKSLQISqqrtiGLYPEIKHGTHFQR-L 206
Cdd:cd08604   80 -----FTFDLTWSEIQTLKPAISNPYSVTGlfrNPANKNAGKFLTLSDFLDLAKNKSLS-----GVLINVENAAYLAEkK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 207 GLAMERPLVKTLHRNGYLGPRAP-VFIQSFEVNNLKELKRLTGIRLVqlYgsgqpydqqaaggSLTYAEMATAK-GLRQV 284
Cdd:cd08604  150 GLDVVDAVLDALTNAGYDNQTAQkVLIQSTDSSVLAAFKKQISYERV--Y-------------VVDETIRDASDsSIEEI 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 285 ARYAYGVGPDKSYVIPRDANGNLGQpTRFVGDAHAAGLKVHPYTFRAENSFLPAEFRSadgnpqsrgDLAGEIRAYL-DA 363
Cdd:cd08604  215 KKFADAVVIDRGSVFPVSTSFLTRQ-TNVVEKLQSANLTVYVEVLRNEFVSLAFDFFA---------DPTVEINSYVqGA 284

                        330
                 ....*....|....*
gi 300579209 364 GIDGLFSDQPDVAVR 378
Cdd:cd08604  285 GVDGFITEFPATAAR 299
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 55-373 6.03e-25

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: 101.48  E-value: 6.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVaqhpefadrkrtqkvdgvelTG 134
Cdd:cd08563    1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNG--------------------KG 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 135 WFSeDFTLAELKTLRAieriptirpgNARLDGTF---EIPTLQEIIDLVKSLQIsqqrTIGLypEIKHGthfQRLGLAME 211
Cdd:cd08563   61 YVK-DLTLEELKKLDA----------GSWFDEKFtgeKIPTLEEVLDLLKDKDL----LLNI--EIKTD---VIHYPGIE 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 212 RPLVKTLHRNGyLGPRapVFIQSFEVNNLKELKRLtgirlvqlygsgqpyDQQAAGGSLTYAEMATAKGLRQVARyAYGV 291
Cdd:cd08563  121 KKVLELVKEYN-LEDR--VIFSSFNHESLKRLKKL---------------DPKIKLALLYETGLQDPKDYAKKIG-ADSL 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 292 GPDKSYVIPrdangnlgqptRFVGDAHAAGLKVHPYTFRAENsflpaefrsadgnpqsrgdlagEIRAYLDAGIDGLFSD 371
Cdd:cd08563  182 HPDFKLLTE-----------EVVEELKKRGIPVRLWTVNEEE----------------------DMKRLKDLGVDGIITN 228


                 ..
gi 300579209 372 QP 373
Cdd:cd08563  229 YP 230
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 57-379 5.81e-22

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: 93.86  E-value: 5.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  57 VIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDvaqhpefadrkRTQKVdgveltgwf 136
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTD-----------GTGPV--------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 137 sEDFTLAELKTLRAIERIPTI--RPGNARLDGtFEIPTLQEIIDlvkslqisqqrtigLYP------EIKhgthfQRlGL 208
Cdd:cd08561   61 -ADLTLAELRRLDAGYHFTDDggRTYPYRGQG-IRIPTLEELFE--------------AFPdvrlniEIK-----DD-GP 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 209 AMERPLVKTLHRNGYLGpRapVFIQSFEVNNLKELKRLtgirlvqlygsgqpydqqaAGGSLTYAEMATAKGLRQVARYA 288
Cdd:cd08561  119 AAAAALADLIERYGAQD-R--VLVASFSDRVLRRFRRL-------------------CPRVATSAGEGEVAAFVLASRLG 176

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 289 YGVGPDKSYV---IPRDANG-NLGQPtRFVGDAHAAGLKVHPYTFraensflpaefrsadgnpqsrgDLAGEIRAYLDAG 364
Cdd:cd08561  177 LGSLYSPPYDalqIPVRYGGvPLVTP-RFVRAAHAAGLEVHVWTV----------------------NDPAEMRRLLDLG 233

                        330
                 ....*....|....*
gi 300579209 365 IDGLFSDQPDVAVRL 379
Cdd:cd08561  234 VDGIITDRPDLLLEV 248
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 52-373 3.32e-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: 87.86  E-value: 3.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  52 ERSPLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHD-NELGLTTDVAQHPEFADRKRTQKVDGV 130
Cdd:cd08560   14 RKTDFSIGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSqCDLHTTTNILAIPELAAKCTQPFTPAN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 131 ELTGWFSE----DFTLAELKTLRAIERI--PTIRPGNARLDGT-----------FEIPTLQEIIDLVKSLqisqqrTIGL 193
Cdd:cd08560   94 ATKPASAEcctsDITLAEFKSLCGKMDAsnPSATTPEEYQNGTpdwrtdlyatcGTLMTHKESIALFKSL------GVKM 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 194 YPEIK--------HGTHFQRLglaMERPLVKTLHRNGYlgPRAPVFIQSFEVNN----LKELKRLtGIRLVQLygsgQPY 261
Cdd:cd08560  168 TPELKspsvpmpfDGNYTQED---YAQQMIDEYKEAGV--PPSRVWPQSFNLDDifywIKNEPDF-GRQAVYL----DDR 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 262 DQQAAGGSLTYAEMA--TAKGLRQVAryaygvgPDKSYVIPRDANGNLgQPTRFVGDAHAAGLKVHPYTFRaensflpae 339
Cdd:cd08560  238 DDTADFPATWSPSMDelKARGVNIIA-------PPIWMLVDPDENGKI-VPSEYAKAAKAAGLDIITWTLE--------- 300

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 300579209 340 fRSadGNPQSRGDL-----------AGEIRAYLDA-----GIDGLFSDQP 373
Cdd:cd08560  301 -RS--GPLASGGGWyyqtiedvinnDGDMYNVLDVlardvGILGIFSDWP 347
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 56-181 4.33e-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: 82.73  E-value: 4.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  56 LVIAHRGASGYV-PEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVaqhpefadrkrTQKVdgveltg 134
Cdd:cd08566    1 LVVAHRGGWGAGaPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNG-----------KGKV------- 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 300579209 135 wfsEDFTLAELKTLRAieRIPTIRPGNARldgtfeIPTLQEIIDLVK 181
Cdd:cd08566   63 ---SDLTLAEIRKLRL--KDGDGEVTDEK------VPTLEEALAWAK 98
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 57-373 2.00e-16

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


Pssm-ID: 176505 [Multi-domain]  Cd Length: 229  Bit Score: 77.65  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  57 VIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDvaqHPEFADRKRTQKVDGVELTGWF 136
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTN---GSGAVTELTWAELAQLDAGSWF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 137 SEDFtlaelktlrAIERiptirpgnarldgtfeIPTLQEIIDLVKSLQisqqrtIGLYPEIKHGTHFQrlglAMERPLVK 216
Cdd:cd08562   78 SPEF---------AGEP----------------IPTLADVLELARELG------LGLNLEIKPDPGDE----ALTARVVA 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 217 TLHRNGYLGPRAPVfIQSFEVNNLKELKRL-TGIRLVQLYgsgqpydqqaaggsltyaEMATAKGLRQVARY-AYGVGPD 294
Cdd:cd08562  123 AALRELWPHASKLL-LSSFSLEALRAARRAaPELPLGLLF------------------DTLPADWLELLAALgAVSIHLN 183

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300579209 295 KSYVIPRDangnlgqptrfVGDAHAAGLKVHPYTFraeNSflPAEFRSadgnpqsrgdlageiraYLDAGIDGLFSDQP 373
Cdd:cd08562  184 YRGLTEEQ-----------VKALKDAGYKLLVYTV---ND--PARAAE-----------------LLEWGVDAIFTDRP 229
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 57-246 5.40e-16

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: 76.05  E-value: 5.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  57 VIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELglttdvaqhpefadrKRTQKVDGVeltgwf 136
Cdd:cd08579    1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANL---------------KRLAGVNKK------ 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 137 SEDFTLAELKTLRAIERIPTIRpgnarldgtfeIPTLQEIIDLVKSLQisqqrtIGLYPEIK-HGTHFQRLglaMERpLV 215
Cdd:cd08579   60 VWDLTLEELKKLTIGENGHGAK-----------IPSLDEYLALAKGLK------QKLLIELKpHGHDSPDL---VEK-FV 118

                        170       180       190
                 ....*....|....*....|....*....|.
gi 300579209 216 KTLHRNgylGPRAPVFIQSFEVNNLKELKRL 246
Cdd:cd08579  119 KLYKQN---LIENQHQVHSLDYRVIEKVKKL 146
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 55-178 6.62e-13

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: 68.01  E-value: 6.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQHpefadrkrtqkvdgveltg 134
Cdd:cd08575    1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGL------------------- 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 300579209 135 wfSEDFTLAELKTLRAieRIPTIRPGNA----RLDGTFEIPTLQEIID 178
Cdd:cd08575   62 --VSDLTYAELPPLDA--GYGYTFDGGKtgypRGGGDGRIPTLEEVFK 105
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 57-156 9.70e-13

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


Pssm-ID: 176512 [Multi-domain]  Cd Length: 234  Bit Score: 67.25  E-value: 9.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  57 VIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVaqhpefADRKRtqkvdgveltgwf 136
Cdd:cd08570    1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGK------DGLII------------- 61

                         90       100
                 ....*....|....*....|....
gi 300579209 137 sEDFTLAELKTLRAIE----RIPT 156
Cdd:cd08570   62 -DDSTWDELSHLRTIEephqPMPT 84
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 57-377 1.52e-12

Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (pAtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176508 [Multi-domain]  Cd Length: 235  Bit Score: 66.66  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  57 VIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTdvaqHPEFADRkrtqkvdgveltgwf 136
Cdd:cd08565    1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTT----HGTGAVR--------------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 137 seDFTLAELKTLRAieriptirPGNARLdgtfEIPTLQEIIDLVKS------LQISQQRTIGLYPEIkhgthfqrLGLAM 210
Cdd:cd08565   62 --DLTLAERKALRL--------RDSFGE----KIPTLEEVLALFAPsglelhVEIKTDADGTPYPGA--------AALAA 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 211 ErplvkTLHRNGYLgPRApVFiQSFEVNNLKELKRLTGIRLVQLYGSgqpyDQQAAGGSLTYAEMATAKGlrqvaryAYG 290
Cdd:cd08565  120 A-----TLRRHGLL-ERS-VL-TSFDPAVLTEVRKHPGVRTLGSVDE----DMLERLGGELPFLTATALK-------AHI 180

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 291 VGPDKSYVIprdangnlGQPTRFVGDAHAAGLKVHPYtfraensflpaefrsadgNPQSrgdlagEIRAYLDAGIDGLFS 370
Cdd:cd08565  181 VAVEQSLLA--------ATWELVRAAVPGLRLGVWTV------------------NDDS------LIRYWLACGVRQLTT 228


                 ....*..
gi 300579209 371 DQPDVAV 377
Cdd:cd08565  229 DRPDLAL 235
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 57-151 6.88e-12

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: 64.66  E-value: 6.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  57 VIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQHpeFADRKRTQ-KVDGVELTGW 135
Cdd:cd08581    1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGL--LHELEDAElDSLRVAEPAR 78

                         90
                 ....*....|....*.
gi 300579209 136 FSEDFTLAELKTLRAI 151
Cdd:cd08581   79 FGSRFAGEPLPSLAAV 94
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 57-178 9.52e-12

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: 64.59  E-value: 9.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  57 VIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVaqhpefadrkrTQKVDgveltgwf 136
Cdd:cd08573    1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDG-----------TGLVA-------- 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 300579209 137 seDFTLAELKTLRAieriptirPGNARLDGTFE---IPTLQEIID 178
Cdd:cd08573   62 --ELTWEELRKLNA--------AAKHRLSSRFPgekIPTLEEAVK 96
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 55-186 1.52e-11

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: 64.56  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQhpEFADRKRTQkvdgveltg 134
Cdd:cd08609   27 PALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKD--VFPGRDAAG--------- 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300579209 135 wfSEDFTLAELKTLRA----IERIP--TIRP--GNARLDGTFE-IPTLQEIIDLVKSLQIS 186
Cdd:cd08609   96 --SNNFTWTELKTLNAgswfLERRPfwTLSSlsEEDRREADNQtVPSLSELLDLAKKHNVS 154
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 56-191 6.48e-11

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: 61.55  E-value: 6.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  56 LVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELglttdvaqhpefadrkrtQKVDGVELTgw 135
Cdd:cd08568    1 IILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENL------------------KRVGGVDLK-- 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300579209 136 fSEDFTLAELKTLRAI-ERIPTIR------PGNARLDgtFEIP---TLQEIIDLVKSLQIsQQRTI 191
Cdd:cd08568   61 -VKELTYKELKKLHPGgELIPTLEevfralPNDAIIN--VEIKdidAVEPVLEIVEKFNA-LDRVI 122
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 55-186 1.63e-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: 60.78  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQhpEFADRKRTQkvdgveltg 134
Cdd:cd08574    2 PALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVAD--VFPERAHER--------- 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300579209 135 wfSEDFTLAELKTLRA----IERIP-----TIRPGNARLDGTFEIPTLQEIIDLVKSLQIS 186
Cdd:cd08574   71 --ASMFTWTDLQQLNAgqwfLKDDPfwtasSLSESDREEAGNQSIPSLAELLRLAKKHNKS 129
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 58-115 4.91e-10

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


Pssm-ID: 176553 [Multi-domain]  Cd Length: 300  Bit Score: 59.92  E-value: 4.91e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 300579209  58 IAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQH 115
Cdd:cd08612   30 ISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKL 87
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 57-147 5.42e-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: 58.22  E-value: 5.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  57 VIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQHPEFADRKRTQKvdgvELTGWF 136
Cdd:cd08555    1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGILPPTLEEVLELIA----DYLKNP 76

                         90
                 ....*....|..
gi 300579209 137 SEDFTLA-ELKT 147
Cdd:cd08555   77 DYTIILSlEIKQ 88
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 58-280 1.95e-08

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


Pssm-ID: 176527 [Multi-domain]  Cd Length: 237  Bit Score: 54.64  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  58 IAHRG---ASGYVPEHTLGAYALAVmmGADY-VEPDLVMTRDGKLVARHDNELglttdvaqhpefadrKRTQKVDGvelt 133
Cdd:cd08585    7 IAHRGlhdRDAGIPENSLSAFRAAA--EAGYgIELDVQLTADGEVVVFHDDNL---------------KRLTGVEG---- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209 134 gwFSEDFTLAELKTLraieriptirpgnaRLDGTFE-IPTLQEIIDLVkslqisQQRTiGLYPEIKhgTHFQRLGlAMER 212
Cdd:cd08585   66 --RVEELTAAELRAL--------------RLLGTDEhIPTLDEVLELV------AGRV-PLLIELK--SCGGGDG-GLER 119

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300579209 213 PLVKTLhrNGYLGPRApvfIQSFEVNNLKELKRLT-GIRLVQLYGSgqpYDQQAAGGSLTYAEMATAKG 280
Cdd:cd08585  120 RVLAAL--KDYKGPAA---IMSFDPRVVRWFRKLApGIPRGQLSEG---SNDEADPAFWNEALLSALFS 180
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 54-182 2.12e-08

Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative Galdieria sulphuraria glycerophosphodiester phosphodiesterase (GsGDE, EC 3.1.4.46) and its uncharacterized eukaryotic homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176507 [Multi-domain]  Cd Length: 265  Bit Score: 54.79  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  54 SPLVIAHRGA--SGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHdnelGLTTDVAQHPEFadrkrtQKVDGVe 131
Cdd:cd08564    3 RPIIVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFH----GTEDDTNPDTSI------QLDDSG- 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 300579209 132 ltGWFSEDFTLAELKTLRAIEriPTIRPGNARLDGTFE-IPTLQEIIDLVKS 182
Cdd:cd08564   72 --FKNINDLSLDEITRLHFKQ--LFDEKPCGADEIKGEkIPTLEDVLVTFKD 119
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 55-177 5.64e-06

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: 47.32  E-value: 5.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDvaqhpefadrkRTQKVdgveltg 134
Cdd:cd08580    1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTN-----------GSGAV------- 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 300579209 135 wfsEDFTLAELKTLRAIERIPTirPGNARLDGT-FEIPTLQEII 177
Cdd:cd08580   63 ---SAYTAAQLATLNAGYNFKP--EGGYPYRGKpVGIPTLEQVL 101
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 56-176 7.44e-06

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: 47.27  E-value: 7.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  56 LVIAHRGA------SGY--VPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTdvaqhpefaDRKRTQKV 127
Cdd:cd08572    1 LVIGHRGLgknyasGSLagIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSE---------KSKTGSDE 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300579209 128 DGVELTGWfsEDFTLAELKTL----------RAIERIPTIRPGNARlDGTFE--IPTLQEI 176
Cdd:cd08572   72 GELIEVPI--HDLTLEQLKELglqhisalkrKALTRKAKGPKPNPW-GMDEHdpFPTLQEV 129
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 55-156 9.77e-06

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 46.47  E-value: 9.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQHpefADRKRTQKVDGVELTG 134
Cdd:PRK09454   8 PRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGV---AGELTWQDLAQLDAGS 84

                         90       100
                 ....*....|....*....|..
gi 300579209 135 WFSEDFtlaelktlrAIERIPT 156
Cdd:PRK09454  85 WFSAAF---------AGEPLPT 97
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 56-149 1.26e-05

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


Pssm-ID: 176549 [Multi-domain]  Cd Length: 290  Bit Score: 46.52  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  56 LVIAHRG-------ASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDnelgLTTDVAQhpefadrKRTQKVD 128
Cdd:cd08607    1 LDVGHRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHD----FTLRVSL-------KSKGDSD 69

                         90       100
                 ....*....|....*....|.
gi 300579209 129 GVELTGWFSEDFTLAELKTLR 149
Cdd:cd08607   70 RDDLLEVPVKDLTYEQLKLLK 90
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 53-150 1.89e-05

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


Pssm-ID: 176552 [Multi-domain]  Cd Length: 316  Bit Score: 46.02  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  53 RSPLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVaqhpefadrKRTQKVDGVEL 132
Cdd:cd08610   21 PKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNI---------GEVQPESACEN 91

                         90
                 ....*....|....*...
gi 300579209 133 TGWFSEDFtlaeLKTLRA 150
Cdd:cd08610   92 PAFFNWDF----LSTLNA 105
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 55-121 2.59e-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: 45.61  E-value: 2.59e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300579209  55 PLVIAHRGASGYVPEHTLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTDVAQ-HPEFADR 121
Cdd:cd08608    2 PAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRvFPERQYE 69
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 54-148 1.62e-04

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: 43.12  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300579209  54 SPLVIAHRGASG-----------------YVPEH-----TLGAYALAVMMGADYVEPDLVMTRDGKLVARHDNELGLTTD 111
Cdd:cd08613   23 KPKLLAHRGLAQtfdregvendtctaeriDPPTHdylenTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTD 102

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 300579209 112 VAqhpefadrkrtqkvdGVeltgwfSEDFTLAELKTL 148
Cdd:cd08613  103 GS---------------GV------TRDHTMAELKTL 118
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 54-115 5.40e-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: 41.28  E-value: 5.40e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300579209  54 SPLVIAHRGASGYVPEH--------TLGAYALAVMMGADYVEPDLVMTRDGKLVARHD---NELGltTDVAQH 115
Cdd:cd08606    1 SVQVIGHRGLGKNTAERkslqlgenTVESFILAASLGASYVEVDVQLTKDLVPVIYHDflvSETG--TDVPIH 71
 
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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