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Conserved domains on  [gi|1281033169|ref|XP_023001046|]
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glycerophosphodiester phosphodiesterase GDPD6-like [Cucurbita maxima]

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 ...
 49-360 4.04e-168

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: 472.55  E-value: 4.04e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  49 PYNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYRKFANRKRTYEVQGVNITG 128
Cdd:cd08602     1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHPEFADRKTTKTVDGVNVTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 129 FFTVDFTLKELQSLRVKQRFPYRDQQYNGKFSIITFEDFIEIALQAP----RVVGIYPEIKNPVFINQRvkwgDGKRFED 204
Cdd:cd08602    81 WFTEDFTLAELKTLRARQRLPYRDQSYDGQFPIPTFEEIIALAKAASaatgRTVGIYPEIKHPTYFNAP----LGLPMED 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 205 KFVEILKKYGYQGSylsknwlKQPVFIQSFAPTSIIHISNLTDLPKILLIDDTTIPTQDT----NQTYWEITSDSYFEYI 280
Cdd:cd08602   157 KLLETLKKYGYTGK-------KAPVFIQSFEVTNLKYLRNKTDLPLVQLIDDATIPPQDTpegdSRTYADLTTDAGLKEI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 281 KNYVVGIGPWKDTVVPAV-NNYILTPTDLVTRAHAHNLQVHPYTYRNEYNFIHFNFHQDPYEEFDYWINtIGVDGLFTDF 359
Cdd:cd08602   230 ATYADGIGPWKDLIIPSDaNGRLGTPTDLVEDAHAAGLQVHPYTFRNENTFLPPDFFGDPYAEYRAFLD-AGVDGLFTDF 308


                  .
gi 1281033169 360 T 360
Cdd:cd08602   309 P 309
 
Name Accession Description Interval E-value
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 49-360 4.04e-168

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: 472.55  E-value: 4.04e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  49 PYNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYRKFANRKRTYEVQGVNITG 128
Cdd:cd08602     1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHPEFADRKTTKTVDGVNVTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 129 FFTVDFTLKELQSLRVKQRFPYRDQQYNGKFSIITFEDFIEIALQAP----RVVGIYPEIKNPVFINQRvkwgDGKRFED 204
Cdd:cd08602    81 WFTEDFTLAELKTLRARQRLPYRDQSYDGQFPIPTFEEIIALAKAASaatgRTVGIYPEIKHPTYFNAP----LGLPMED 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 205 KFVEILKKYGYQGSylsknwlKQPVFIQSFAPTSIIHISNLTDLPKILLIDDTTIPTQDT----NQTYWEITSDSYFEYI 280
Cdd:cd08602   157 KLLETLKKYGYTGK-------KAPVFIQSFEVTNLKYLRNKTDLPLVQLIDDATIPPQDTpegdSRTYADLTTDAGLKEI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 281 KNYVVGIGPWKDTVVPAV-NNYILTPTDLVTRAHAHNLQVHPYTYRNEYNFIHFNFHQDPYEEFDYWINtIGVDGLFTDF 359
Cdd:cd08602   230 ATYADGIGPWKDLIIPSDaNGRLGTPTDLVEDAHAAGLQVHPYTFRNENTFLPPDFFGDPYAEYRAFLD-AGVDGLFTDF 308


                  .
gi 1281033169 360 T 360
Cdd:cd08602   309 P 309
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 52-360 1.43e-57

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 191.81  E-value: 1.43e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKyrKFANRKRTyevqgvniTG-FF 130
Cdd:PRK11143   30 IAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAE--RFPDRARK--------DGrYY 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 131 TVDFTLKELQSLRVKQRF-----------PYRDQQYNGKFSIITFEDFIEIALQAPRV----VGIYPEIKNPVFINQrvk 195
Cdd:PRK11143  100 AIDFTLDEIKSLKFTEGFdiengkkvqvyPGRFPMGKSDFRVHTFEEEIEFIQGLNHStgknIGIYPEIKAPWFHHQ--- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 196 wgDGKRFEDKFVEILKKYGYQgsylSKNwlkQPVFIQSFAPTSIIHISNL------TDLPKILLIDDT---TIPTQDTNQ 266
Cdd:PRK11143  177 --EGKDIAAKVLEVLKKYGYT----GKD---DKVYLQCFDANELKRIKNElepkmgMDLKLVQLIAYTdwnETQEKQPDG 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 267 TYWEITSDSYF-----EYIKNYVVGIGPWKDTVVPAVN---NYILTPtdLVTRAHAHNLQVHPYTYRN----EYnFIHFN 334
Cdd:PRK11143  248 KWVNYNYDWMFkpgamKEVAKYADGIGPDYHMLVDETStpgNIKLTG--MVKEAHQAKLVVHPYTVRAdqlpEY-ATDVN 324

                         330       340
                  ....*....|....*....|....*.
gi 1281033169 335 fhqdpyEEFDYWINTIGVDGLFTDFT 360
Cdd:PRK11143  325 ------QLYDILYNQAGVDGVFTDFP 344
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
47-359 1.53e-56

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 185.46  E-value: 1.53e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  47 TRPYNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVgkyrkfanrkrtyevqgvni 126
Cdd:COG0584     1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNG-------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 127 TGfFTVDFTLKELQSLRVKQRFPYRDQQyngkfsIITFEDFIEIalqAPRVVGIYPEIKNPvfinqrvkWGDGKRFEDKF 206
Cdd:COG0584    61 TG-RVADLTLAELRQLDAGSGPDFAGER------IPTLEEVLEL---VPGDVGLNIEIKSP--------PAAEPDLAEAV 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 207 VEILKKYGYQGsylsknwlkqPVFIQSFAPTSIIHISNLT-DLPKILLIDDTTiptqdtnqtyweitsDSYFEYIKN-YV 284
Cdd:COG0584   123 AALLKRYGLED----------RVIVSSFDPEALRRLRELApDVPLGLLVEELP---------------ADPLELARAlGA 177

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281033169 285 VGIGPWKDTVvpavnnyiltPTDLVTRAHAHNLQVHPYTYRNEynfihfnfhqdpyEEFDYWINtIGVDGLFTDF 359
Cdd:COG0584   178 DGVGPDYDLL----------TPELVAAAHAAGLKVHVWTVNDP-------------EEMRRLLD-LGVDGIITDR 228
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 54-361 6.93e-54

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: 178.75  E-value: 6.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  54 HRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYrkfanrkrtyevqgvnitgffTVD 133
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGY---------------------VRD 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 134 FTLKELQSLRVKQRFPYrdQQYNGKFSIITFEDFIEialqAPRVVGIYPEIKNPVFINQRVKWGDGkrFEDKFVEILKKY 213
Cdd:pfam03009  60 LTLEELKRLDIGAGNSG--PLSGERVPFPTLEEVLE----FDWDVGFNIEIKIKPYVEAIAPEEGL--IVKDLLLSVDEI 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 214 GYqgsylsKNWLKQPVFIQSFAPTSIIHISNL-TDLPKILLIDDTTIPTQDT-NQTYWEITSDSYFEYIKNYVVGIgpwk 291
Cdd:pfam03009 132 LA------KKADPRRVIFSSFNPDELKRLRELaPKLPLVFLSSGRAYAEADLlERAAAFAGAPALLGEVALVDEAL---- 201

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 292 dtvvpavnnyiltpTDLVTRAHAHNLQVHPYTYRNEYNfihfnfhqdpyeefDYWINTIGVDGLFTDFTG 361
Cdd:pfam03009 202 --------------PDLVKRAHARGLVVHVWTVNNEDE--------------MKRLLELGVDGVITDRPD 243
 
Name Accession Description Interval E-value
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 49-360 4.04e-168

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: 472.55  E-value: 4.04e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  49 PYNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYRKFANRKRTYEVQGVNITG 128
Cdd:cd08602     1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHPEFADRKTTKTVDGVNVTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 129 FFTVDFTLKELQSLRVKQRFPYRDQQYNGKFSIITFEDFIEIALQAP----RVVGIYPEIKNPVFINQRvkwgDGKRFED 204
Cdd:cd08602    81 WFTEDFTLAELKTLRARQRLPYRDQSYDGQFPIPTFEEIIALAKAASaatgRTVGIYPEIKHPTYFNAP----LGLPMED 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 205 KFVEILKKYGYQGSylsknwlKQPVFIQSFAPTSIIHISNLTDLPKILLIDDTTIPTQDT----NQTYWEITSDSYFEYI 280
Cdd:cd08602   157 KLLETLKKYGYTGK-------KAPVFIQSFEVTNLKYLRNKTDLPLVQLIDDATIPPQDTpegdSRTYADLTTDAGLKEI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 281 KNYVVGIGPWKDTVVPAV-NNYILTPTDLVTRAHAHNLQVHPYTYRNEYNFIHFNFHQDPYEEFDYWINtIGVDGLFTDF 359
Cdd:cd08602   230 ATYADGIGPWKDLIIPSDaNGRLGTPTDLVEDAHAAGLQVHPYTFRNENTFLPPDFFGDPYAEYRAFLD-AGVDGLFTDF 308


                  .
gi 1281033169 360 T 360
Cdd:cd08602   309 P 309
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 49-360 3.54e-134

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: 386.24  E-value: 3.54e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  49 PYNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVgkyrkfANRkrtYEVQGVNITG 128
Cdd:cd08559     1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNV------AEH---FPFRGRKDTG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 129 FFTVDFTLKELQSLRVK----QRFPYRDQQYNGKFSIITFEDFIEIALQAP----RVVGIYPEIKNPVFINQrvkwgDGK 200
Cdd:cd08559    72 YFVIDFTLAELKTLRAGswfnQRYPERAPSYYGGFKIPTLEEVIELAQGLNkstgRNVGIYPETKHPTFHKQ-----EGP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 201 RFEDKFVEILKKYGYQGSylsknwlKQPVFIQSFAPTSIIHISNLT-DLPKILLIDDTTIPTQDTNQTYWEITSDSYFEY 279
Cdd:cd08559   147 DIEEKLLEVLKKYGYTGK-------NDPVFIQSFEPESLKRLRNETpDIPLVQLIDYGDWAETDKKYTYAWLTTDAGLKE 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 280 IKNYVVGIGPWKDTVVPAVNNYILTPTDLVTRAHAHNLQVHPYTYRNEYNFIHFNFHQDPYEEfdywINTIGVDGLFTDF 359
Cdd:cd08559   220 IAKYADGIGPWKSLIIPEDSNGLLVPTDLVKDAHKAGLLVHPYTFRNENLFLAPDFKQDMDAL----YNAAGVDGVFTDF 295


                  .
gi 1281033169 360 T 360
Cdd:cd08559   296 P 296
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 52-360 1.67e-60

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: 198.38  E-value: 1.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKyrKFANRKRTyevQGvnitGFFT 131
Cdd:cd08600     4 IAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAE--KFPDRKRK---DG----RYYV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 132 VDFTLKELQSLRVKQRFP---------YRDQQYNGK--FSIITFEDFIEIALQAPRV----VGIYPEIKNPVFINQrvkw 196
Cdd:cd08600    75 IDFTLDELKSLSVTERFDiengkkvqvYPNRFPLWKsdFKIHTLEEEIELIQGLNKStgknVGIYPEIKAPWFHHQ---- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 197 gDGKRFEDKFVEILKKYGYQgsylSKNwlkQPVFIQSFAPTSIIHISN------LTDLPKILLIDDTTI-PTQDTNQTYW 269
Cdd:cd08600   151 -EGKDIAAATLEVLKKYGYT----SKN---DKVYLQTFDPNELKRIKNellpkmGMDLKLVQLIAYTDWgETQEKDPGGW 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 270 EITSDSYF------EYIKNYVVGIGPWKDTVVPAVNNY-ILTPTDLVTRAHAHNLQVHPYTYRNEYNFIhfnFHQDPYEE 342
Cdd:cd08600   223 VNYDYDWMftkgglKEIAKYADGVGPWYSMIIEEKSSKgNIVLTDLVKDAHEAGLEVHPYTVRKDALPE---YAKDADQL 299

                         330
                  ....*....|....*...
gi 1281033169 343 FDYWINTIGVDGLFTDFT 360
Cdd:cd08600   300 LDALLNKAGVDGVFTDFP 317
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 52-360 1.43e-57

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 191.81  E-value: 1.43e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKyrKFANRKRTyevqgvniTG-FF 130
Cdd:PRK11143   30 IAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAE--RFPDRARK--------DGrYY 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 131 TVDFTLKELQSLRVKQRF-----------PYRDQQYNGKFSIITFEDFIEIALQAPRV----VGIYPEIKNPVFINQrvk 195
Cdd:PRK11143  100 AIDFTLDEIKSLKFTEGFdiengkkvqvyPGRFPMGKSDFRVHTFEEEIEFIQGLNHStgknIGIYPEIKAPWFHHQ--- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 196 wgDGKRFEDKFVEILKKYGYQgsylSKNwlkQPVFIQSFAPTSIIHISNL------TDLPKILLIDDT---TIPTQDTNQ 266
Cdd:PRK11143  177 --EGKDIAAKVLEVLKKYGYT----GKD---DKVYLQCFDANELKRIKNElepkmgMDLKLVQLIAYTdwnETQEKQPDG 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 267 TYWEITSDSYF-----EYIKNYVVGIGPWKDTVVPAVN---NYILTPtdLVTRAHAHNLQVHPYTYRN----EYnFIHFN 334
Cdd:PRK11143  248 KWVNYNYDWMFkpgamKEVAKYADGIGPDYHMLVDETStpgNIKLTG--MVKEAHQAKLVVHPYTVRAdqlpEY-ATDVN 324

                         330       340
                  ....*....|....*....|....*.
gi 1281033169 335 fhqdpyEEFDYWINTIGVDGLFTDFT 360
Cdd:PRK11143  325 ------QLYDILYNQAGVDGVFTDFP 344
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
47-359 1.53e-56

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 185.46  E-value: 1.53e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  47 TRPYNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVgkyrkfanrkrtyevqgvni 126
Cdd:COG0584     1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNG-------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 127 TGfFTVDFTLKELQSLRVKQRFPYRDQQyngkfsIITFEDFIEIalqAPRVVGIYPEIKNPvfinqrvkWGDGKRFEDKF 206
Cdd:COG0584    61 TG-RVADLTLAELRQLDAGSGPDFAGER------IPTLEEVLEL---VPGDVGLNIEIKSP--------PAAEPDLAEAV 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 207 VEILKKYGYQGsylsknwlkqPVFIQSFAPTSIIHISNLT-DLPKILLIDDTTiptqdtnqtyweitsDSYFEYIKN-YV 284
Cdd:COG0584   123 AALLKRYGLED----------RVIVSSFDPEALRRLRELApDVPLGLLVEELP---------------ADPLELARAlGA 177

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281033169 285 VGIGPWKDTVvpavnnyiltPTDLVTRAHAHNLQVHPYTYRNEynfihfnfhqdpyEEFDYWINtIGVDGLFTDF 359
Cdd:COG0584   178 DGVGPDYDLL----------TPELVAAAHAAGLKVHVWTVNDP-------------EEMRRLLD-LGVDGIITDR 228
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 54-361 6.93e-54

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: 178.75  E-value: 6.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  54 HRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYrkfanrkrtyevqgvnitgffTVD 133
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGY---------------------VRD 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 134 FTLKELQSLRVKQRFPYrdQQYNGKFSIITFEDFIEialqAPRVVGIYPEIKNPVFINQRVKWGDGkrFEDKFVEILKKY 213
Cdd:pfam03009  60 LTLEELKRLDIGAGNSG--PLSGERVPFPTLEEVLE----FDWDVGFNIEIKIKPYVEAIAPEEGL--IVKDLLLSVDEI 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 214 GYqgsylsKNWLKQPVFIQSFAPTSIIHISNL-TDLPKILLIDDTTIPTQDT-NQTYWEITSDSYFEYIKNYVVGIgpwk 291
Cdd:pfam03009 132 LA------KKADPRRVIFSSFNPDELKRLRELaPKLPLVFLSSGRAYAEADLlERAAAFAGAPALLGEVALVDEAL---- 201

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 292 dtvvpavnnyiltpTDLVTRAHAHNLQVHPYTYRNEYNfihfnfhqdpyeefDYWINTIGVDGLFTDFTG 361
Cdd:pfam03009 202 --------------PDLVKRAHARGLVVHVWTVNNEDE--------------MKRLLELGVDGVITDRPD 243
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 52-359 2.27e-52

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: 176.71  E-value: 2.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYrkFANRKRTYEVQGVNITGFFT 131
Cdd:cd08571     4 IARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTIASV--FPKRKKTYVVEGQSTSGIFS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 132 VDFTLKELQSLRVKQRFPY----RDQQYNGKFSIITFEDFIEIAlQAPRVVGIYPEIKNPVFINQRvkwgDGKRFEDKFV 207
Cdd:cd08571    82 FDLTWAEIQTLKPIISNPFsvlfRNPRNDNAGKILTLEDFLTLA-KPKSLSGVWINVENAAFLAEH----KGLLSVDAVL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 208 EILKKYGYQGSYlsknwlkQPVFIQSFAPTSIIHISNLTDLPKILL---IDDtTIPTqdtnqtyweiTSDSYFEYIKNYV 284
Cdd:cd08571   157 TSLSKAGYDQTA-------KKVYISSPDSSVLKSFKKRVGTKLVFRvldVDD-TEPD----------TLLSNLTEIKKFA 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1281033169 285 VGIGPWKDTVVPAV-NNYILTPTDLVTRAHAHNLQVHPYTYRNEYNFIHFNFHQDPYEEFDYWI-NTIGVDGLFTDF 359
Cdd:cd08571   219 SGVLVPKSYIWPVDsDSFLTPQTSVVQDAHKAGLEVYVSGFANEFVSLAYDYSADPTLEILSFVgNGNSVDGVITDF 295
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 51-364 6.09e-49

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: 166.34  E-value: 6.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  51 NIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTdvgkyrkfaNRKRTYEVQgvnitgff 130
Cdd:cd08601     3 VIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTT---------NIERPGPVK-------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 131 tvDFTLKELQSLRV----KQRFP-YRDQQYNGKfSIITFEDFIEIALQAPrvvGIYPEIKNP-VFinqrvkwgdgKRFED 204
Cdd:cd08601    66 --DYTLAEIKQLDAgswfNKAYPeYARESYSGL-KVPTLEEVIERYGGRA---NYYIETKSPdLY----------PGMEE 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 205 KFVEILKKYGYQGSYLsKNWlkqPVFIQSFAPTSIIHISNLT-DLPKILLIDDTTIPtqdtnqtyweITSDSYFEYIKNY 283
Cdd:cd08601   130 KLLATLDKYGLLTDNL-KNG---QVIIQSFSKESLKKLHQLNpNIPLVQLLWYGEGA----------ETYDKWLDEIKEY 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 284 VVGIGPwkdtvvpavnNYILTPTDLVTRAHAHNLQVHPYTYRNEynfihfnfhqdpyEEFDYWINTiGVDGLFTDFTGSL 363
Cdd:cd08601   196 AIGIGP----------SIADADPWMVHLIHKKGLLVHPYTVNEK-------------ADMIRLINW-GVDGMFTNYPDRL 251


                  .
gi 1281033169 364 H 364
Cdd:cd08601   252 K 252
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 52-359 7.52e-40

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: 143.63  E-value: 7.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKyRKFANRKRTY-EVQGVNitGFF 130
Cdd:cd08604     4 ISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVAT-SKFSNRATTVpEIGSTS--GIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 131 TVDFTLKELQSLRVKQRFPY------RDQQYNGKFSIITFEDFIEIAlQAPRVVGIYPEIKNPVFInqRVKWGDGkrFED 204
Cdd:cd08604    81 TFDLTWSEIQTLKPAISNPYsvtglfRNPANKNAGKFLTLSDFLDLA-KNKSLSGVLINVENAAYL--AEKKGLD--VVD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 205 KFVEILKKYGYQgsylskNWLKQPVFIQSFAPTSIIHISNLTDLPKILLIDDTTiptqdtnqtywEITSDSYFEYIKNYV 284
Cdd:cd08604   156 AVLDALTNAGYD------NQTAQKVLIQSTDSSVLAAFKKQISYERVYVVDETI-----------RDASDSSIEEIKKFA 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281033169 285 VGIGPWKDTVVPAVNNYILTPTDLVTRAHAHNLQVHPYTYRNEYNFIHFNFHQDPYEEFDYWINTIGVDGLFTDF 359
Cdd:cd08604   219 DAVVIDRGSVFPVSTSFLTRQTNVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSYVQGAGVDGFITEF 293
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 49-359 2.42e-35

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: 131.74  E-value: 2.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  49 PYNIAHRGSNGEFPEETLPAYKRAIEEGA-DF-IETDILSSKDGVLICFHDVTLDETTDVGKYrkFANRKRTYEVQGVNI 126
Cdd:cd08603     1 PLVIARGGFSGLFPDSSLFAYQFAASSSSpDVaLWCDLQLTKDGVGICLPDLNLDNSTTIARV--YPKRKKTYSVNGVST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 127 TGFFTVDFTLKELQSLRVKQRFPYRDQQYNGKFSIITFEDFIEIAlqAPrvVGIYPEIKNPVFINQRvkwgdGKRFEDKF 206
Cdd:cd08603    79 KGWFSVDFTLAELQQVTLIQGIFSRTPIFDGQYPISTVEDVVTLA--KP--EGLWLNVQHDAFYQQH-----NLSMSSYL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 207 VEILKKYGYQgsYLSKNWLKqpvFIQSFAPTSiihISNLTDLPKILLIDDTTIPTqdTNQTYWEITSDsyFEYIKNYVVG 286
Cdd:cd08603   150 LSLSKTVKVD--YISSPEVG---FLKSIGGRV---GRNGTKLVFRFLDKDDVEPS--TNQTYGSILKN--LTFIKTFASG 217

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1281033169 287 IGPWKDTVVPAV-NNYILTPTDLVTRAHAHNLQVHPYTYRNEYNfIHFNFHQDPYEEFdywINTIG-----VDGLFTDF 359
Cdd:cd08603   218 ILVPKSYIWPVDsDQYLQPATSLVQDAHKAGLEVYASGFANDFD-ISYNYSYDPVAEY---LSFVGngnfsVDGVLSDF 292
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 52-359 4.55e-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: 108.89  E-value: 4.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDvtldettdvgkyrkfanrkrtyevqgvnitgfft 131
Cdd:cd08556     2 IAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD---------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 132 vdftlkelqslrvkqrfpyrdqqyngkfsIITFEDFIEIalqAPRVVGIYPEIKNPvfinqrvkwGDGKRFEDKFVEILK 211
Cdd:cd08556    48 -----------------------------IPTLEEVLEL---VKGGVGLNIELKEP---------TRYPGLEAKVAELLR 86

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 212 KYGyqgsylsknwLKQPVFIQSFAPTSIIHISNLTDLPKILLIDDttiptqdtnqtYWEITSDSYFEYIKNYVVGIGPWK 291
Cdd:cd08556    87 EYG----------LEERVVVSSFDHEALRALKELDPEVPTGLLVD-----------KPPLDPLLAELARALGADAVNPHY 145

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281033169 292 DTVVPAvnnyiltptdLVTRAHAHNLQVHPYTYRNEynfihfnfhqdpyEEFDYWINtIGVDGLFTDF 359
Cdd:cd08556   146 KLLTPE----------LVRAAHAAGLKVYVWTVNDP-------------EDARRLLA-LGVDGIITDD 189
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 49-359 2.39e-26

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: 105.33  E-value: 2.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  49 PYNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYRKfanrkrtyevqgvnitg 128
Cdd:cd08563     1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVK----------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 129 fftvDFTLKELQSLRVKQRFP--YRDQQyngkfsIITFEDFIEIALQAPRVVGIypEIKNPVFinqrvkwgDGKRFEDKF 206
Cdd:cd08563    64 ----DLTLEELKKLDAGSWFDekFTGEK------IPTLEEVLDLLKDKDLLLNI--EIKTDVI--------HYPGIEKKV 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 207 VEILKKYGYQGSylsknwlkqpVFIQSFAPTSIIHISNLTDLPKILLIddttiptqdtnqtyWEITSDSYFEYIKNYVV- 285
Cdd:cd08563   124 LELVKEYNLEDR----------VIFSSFNHESLKRLKKLDPKIKLALL--------------YETGLQDPKDYAKKIGAd 179

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1281033169 286 GIGPWKDTVVPAVnnyiltptdlVTRAHAHNLQVHPYTYRNEynfihfnfhqdpyEEFDYWINtIGVDGLFTDF 359
Cdd:cd08563   180 SLHPDFKLLTEEV----------VEELKKRGIPVRLWTVNEE-------------EDMKRLKD-LGVDGIITNY 229
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 52-358 2.70e-26

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: 105.47  E-value: 2.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTdvGKYRKFAnrkrtyevqgvnitgfft 131
Cdd:cd08582     2 IAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTS--GGDGAVS------------------ 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 132 vDFTLKELQSLRVKQRfpyRDQQYNGKfSIITFEDFIEIALQAPRVVGIypEIKNPVFinqrvkwgdGKRFEDKFVEILK 211
Cdd:cd08582    62 -DLTLAELRKLDIGSW---KGESYKGE-KVPTLEEYLAIVPKYGKKLFI--EIKHPRR---------GPEAEEELLKLLK 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 212 KYGYQGsylsknwlKQPVFIqSFAPTSIIHISNLtdlpkilliddttIPTQDtnqTYWEITSDSYFEYIKNYVVGIGPWK 291
Cdd:cd08582   126 ESGLLP--------EQIVII-SFDAEALKRVREL-------------APTLE---TLWLRNYKSPKEDPRPLAKSGGAAG 180

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1281033169 292 dtvvPAVNNYILTPTDLVTRAHAHNLQVHPYTYrneynfihfnfhqDPYEEFDYWINtIGVDGLFTD 358
Cdd:cd08582   181 ----LDLSYEKKLNPAFIKALRDAGLKLNVWTV-------------DDAEDAKRLIE-LGVDSITTN 229
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 51-359 2.00e-25

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: 103.49  E-value: 2.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  51 NIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDvGKYRkfanrkrtyevqgVNitgff 130
Cdd:cd08561     1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTD-GTGP-------------VA----- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 131 tvDFTLKELQSLRVKQRF--------PYRDQqyngKFSIITFEDFIEiALQAPRVVgIypEIKnpvfinqrvkwGDGKRF 202
Cdd:cd08561    62 --DLTLAELRRLDAGYHFtddggrtyPYRGQ----GIRIPTLEELFE-AFPDVRLN-I--EIK-----------DDGPAA 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 203 EDKFVEILKKYGYQGSylsknwlkqpVFIQSFaptsiiHISNLTDLPKILliddttiPTQDTNQTYWEITsdsyfEYIKN 282
Cdd:cd08561   121 AAALADLIERYGAQDR----------VLVASF------SDRVLRRFRRLC-------PRVATSAGEGEVA-----AFVLA 172

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 283 YVVGIGPWKDTVVPAVN---NY----ILTPtDLVTRAHAHNLQVHPYTyrneynfihFNfhqDPyEEFDYWINTiGVDGL 355
Cdd:cd08561   173 SRLGLGSLYSPPYDALQipvRYggvpLVTP-RFVRAAHAAGLEVHVWT---------VN---DP-AEMRRLLDL-GVDGI 237


                  ....
gi 1281033169 356 FTDF 359
Cdd:cd08561   238 ITDR 241
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 52-358 1.52e-23

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: 98.14  E-value: 1.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGE-FPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTdvgkyrkfanrkrtyevqgvNITGFF 130
Cdd:cd08566     3 VAHRGGWGAgAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTT--------------------NGKGKV 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 131 TvDFTLKELQSLRVKQRFPYRDQQyngkfSIITFEDFIEIAlqaprvvgiypeiKNPVFINQRVKWGDgkrfEDKFVEIL 210
Cdd:cd08566    63 S-DLTLAEIRKLRLKDGDGEVTDE-----KVPTLEEALAWA-------------KGKILLNLDLKDAD----LDEVIALV 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 211 KKYGYQGSylsknwlkqpVFIQSFAPTSIIHISNLtdLPKILLiddttIPTQDTNQTYWEITSDsyfEYIKNYVVGIGPW 290
Cdd:cd08566   120 KKHGALDQ----------VIFKSYSEEQAKELRAL--APEVML-----MPIVRDAEDLDEEEAR---AIDALNLLAFEIT 179

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281033169 291 KDTvvpavnnyILTPTDLVTRAHAHNLQVHPYTYRNEYNFIHFNFHQDPYEEFDYWINtIGVDGLFTD 358
Cdd:cd08566   180 FDD--------LDLPPLFDELLRALGIRVWVNTLGDDDTAGLDRALSDPREVWGELVD-AGVDVIQTD 238
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 52-358 6.29e-22

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: 92.99  E-value: 6.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTdvGKYRKFAnrkrtyevqgvnitgfft 131
Cdd:cd08579     2 IAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLA--GVNKKVW------------------ 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 132 vDFTLKELQSLRVKQRFpyrdqqYNGKfsIITFEDFIEIA--LQAPRVVgiypEIK-NPvfinqrvkwGDGKRFEDKFVE 208
Cdd:cd08579    62 -DLTLEELKKLTIGENG------HGAK--IPSLDEYLALAkgLKQKLLI----ELKpHG---------HDSPDLVEKFVK 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 209 ILKKYGyqgsylsknwLKQPVFIQSFAPTSIIHISNLtdLPKIL--LIddttIPTQDTNqtYWEITSDSYfeyiknyvvg 286
Cdd:cd08579   120 LYKQNL----------IENQHQVHSLDYRVIEKVKKL--DPKIKtgYI----LPFNIGN--LPKTNVDFY---------- 171

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1281033169 287 igpwkdtvvpAVNNYILTPtDLVTRAHAHNLQVHPYTYRNEYNFIHFNFHqdpyeefdywintiGVDGLFTD 358
Cdd:cd08579   172 ----------SIEYSTLNK-EFIRQAHQNGKKVYVWTVNDPDDMQRYLAM--------------GVDGIITD 218
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 52-359 7.30e-21

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: 91.22  E-value: 7.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYRKFANRKRTYevqgvnitgffT 131
Cdd:cd08567     4 QGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDITRDPDGAWLPYEGPA-----------L 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 132 VDFTLKELQSLRVKQRFP-------YRDQQYNGKFSIITFEDFIEIA----LQAPRVVGiypEIKNPVFINQRVkwGDGK 200
Cdd:cd08567    73 YELTLAEIKQLDVGEKRPgsdyaklFPEQIPVPGTRIPTLEEVFALVekygNQKVRFNI---ETKSDPDRDILH--PPPE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 201 RFEDKFVEILKKYGYQGSylsknwlkqpVFIQSFAPTSIIHISNLT-DLPKILLIDDTTIPT-----QDTNQTYWEitsd 274
Cdd:cd08567   148 EFVDAVLAVIRKAGLEDR----------VVLQSFDWRTLQEVRRLApDIPTVALTEETTLGNlpraaKKLGADIWS---- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 275 syfeyiknyvvgigPWKDTVVPavnnyiltptDLVTRAHAHNLQVHPYTYRNeynfihfnfhqdpYEEFDYWInTIGVDG 354
Cdd:cd08567   214 --------------PYFTLVTK----------ELVDEAHALGLKVVPWTVND-------------PEDMARLI-DLGVDG 255


                  ....*
gi 1281033169 355 LFTDF 359
Cdd:cd08567   256 IITDY 260
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 52-187 4.28e-18

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: 82.77  E-value: 4.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYrkfanrkrtyevqgvnitgffT 131
Cdd:cd08581     2 VAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGL---------------------L 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1281033169 132 VDFTLKELQSLRVkqrfpYRDQQYNGKFS---IITFEDFIEIALQAPRvVGIYPEIKNP 187
Cdd:cd08581    61 HELEDAELDSLRV-----AEPARFGSRFAgepLPSLAAVVQWLAQHPQ-VTLFVEIKTE 113
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 52-252 1.19e-17

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: 81.92  E-value: 1.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYRKfanrkrtyevqgvnitgfft 131
Cdd:cd08573     2 IGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVA-------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 132 vDFTLKELQSLRVKQRFPYRDQQYNGKfsIITFEDFIEIALQaprvvgiypeiknpvfINQRVKWgDGKRFEDKFVEILK 211
Cdd:cd08573    62 -ELTWEELRKLNAAAKHRLSSRFPGEK--IPTLEEAVKECLE----------------NNLRMIF-DVKSNSSKLVDALK 121

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1281033169 212 KYgyqgsYLSKNWLKQPVFIQSFAPTSIIHISNlTDlPKIL 252
Cdd:cd08573   122 NL-----FKKYPGLYDKAIVCSFNPIVIYKVRK-AD-PKIL 155
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 51-185 1.44e-17

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: 81.11  E-value: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  51 NIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLdettdvgkyrkfanrKRTYevqgvNITGFF 130
Cdd:cd08570     1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNL---------------KRCF-----GKDGLI 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1281033169 131 TVDFTLKELQSLRVKQrfpyrdqqyNGKFSIITFEDFIEIALQAprvvgIYPEIK 185
Cdd:cd08570    61 IDDSTWDELSHLRTIE---------EPHQPMPTLKDVLEWLVEH-----ELPDVK 101
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 49-214 6.95e-17

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: 79.95  E-value: 6.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  49 PYNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYrkfanrkrtyevqgvnitg 128
Cdd:cd08575     1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGL------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 129 ffTVDFTLKELQSLR--------VKQRFPYRDQQyNGKfsIITFEDfieiALQAprvvgiYPEIknPVFINqrVKWGDGK 200
Cdd:cd08575    62 --VSDLTYAELPPLDagygytfdGGKTGYPRGGG-DGR--IPTLEE----VFKA------FPDT--PINID--IKSPDAE 122

                         170
                  ....*....|....
gi 1281033169 201 RFEDKFVEILKKYG 214
Cdd:cd08575   123 ELIAAVLDLLEKYK 136
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 52-216 3.33e-14

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: 71.67  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDvgkyrkfanrkRTYEVqgvnitgfft 131
Cdd:cd08565     2 AGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTH-----------GTGAV---------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 132 VDFTLKELQSLRVKQRFpyrdqqyngKFSIITFEDFIEIaLQAPRVVgIYPEIKnpvfinQRVKWGDGKRFEDKFVEILK 211
Cdd:cd08565    61 RDLTLAERKALRLRDSF---------GEKIPTLEEVLAL-FAPSGLE-LHVEIK------TDADGTPYPGAAALAAATLR 123


                  ....*
gi 1281033169 212 KYGYQ 216
Cdd:cd08565   124 RHGLL 128
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 52-105 3.29e-13

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: 68.40  E-value: 3.29e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTD 105
Cdd:cd08562     2 IAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTN 55
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 23-368 1.26e-12

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: 68.60  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  23 GCAARPFYplHSRFlegtrqplqttrpyNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHD-VTLD 101
Cdd:cd08560     7 SCAEKPFR--KTDF--------------SIGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSqCDLH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 102 ETTDVGKYRKFANRKRTYEVQGVNITGF----FTVDFTLKELQSLRVKQRF----------------PYRDQQYNGKFSI 161
Cdd:cd08560    71 TTTNILAIPELAAKCTQPFTPANATKPAsaecCTSDITLAEFKSLCGKMDAsnpsattpeeyqngtpDWRTDLYATCGTL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 162 ITFEDFIEIALQAPrvVGIYPEIKNPVfinqrvkwgdgkrfedkfVEIlkkyGYQGSYLSKNWLKQ-------------P 228
Cdd:cd08560   151 MTHKESIALFKSLG--VKMTPELKSPS------------------VPM----PFDGNYTQEDYAQQmideykeagvppsR 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 229 VFIQSFAPTSIIH-ISNLTDLPK--ILLIDDTTIPTQDTNqtyWEITSDSYFEYIKNYvvgIGPWKDTVVPAVNNYILTP 305
Cdd:cd08560   207 VWPQSFNLDDIFYwIKNEPDFGRqaVYLDDRDDTADFPAT---WSPSMDELKARGVNI---IAPPIWMLVDPDENGKIVP 280

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281033169 306 TDLVTRAHAHNLQVHPYTY--------RNEYNFI----HFNFHQDPYEEFDYWINTIGVDGLFTDFTGSLHHFKN 368
Cdd:cd08560   281 SEYAKAAKAAGLDIITWTLersgplasGGGWYYQtiedVINNDGDMYNVLDVLARDVGILGIFSDWPATVTYYAN 355
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 48-171 1.63e-12

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: 66.95  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  48 RPYNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGkyRKFANRKRTYevqgvnit 127
Cdd:cd08574     1 KPALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVA--DVFPERAHER-------- 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1281033169 128 gffTVDFTLKELQSLRVKQRF------------PYRDQQYNGKFSIITFEDFIEIA 171
Cdd:cd08574    71 ---ASMFTWTDLQQLNAGQWFlkddpfwtasslSESDREEAGNQSIPSLAELLRLA 123
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 52-236 2.15e-11

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: 63.50  E-value: 2.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRG---SNGEFPEETLPAYKRAIEegADF-IETDILSSKDGVLICFHDVTLDETTDVgkyrkfanrkrtyevqgvniT 127
Cdd:cd08585     7 IAHRGlhdRDAGIPENSLSAFRAAAE--AGYgIELDVQLTADGEVVVFHDDNLKRLTGV--------------------E 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 128 GFFTvDFTLKELQSLRVKqrfpyrdqqyNGKFSIITFEDFIE-IALQAPRVVgiypEIKNPvfinqrvkWGDGKRFEDKF 206
Cdd:cd08585    65 GRVE-ELTAAELRALRLL----------GTDEHIPTLDEVLElVAGRVPLLI----ELKSC--------GGGDGGLERRV 121

                         170       180       190
                  ....*....|....*....|....*....|
gi 1281033169 207 VEILKKYgyqgsylsknwlKQPVFIQSFAP 236
Cdd:cd08585   122 LAALKDY------------KGPAAIMSFDP 139
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 52-255 2.67e-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: 62.70  E-value: 2.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYRKfanrkrtyevqgvnitgfft 131
Cdd:cd08568     3 LGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVK-------------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 132 vDFTLKELQSLRvkqrfpyrdqqYNGKFsIITFEDFIEIalqAPRVVGIYPEIKNPvfinQRVKwgdgkrfedKFVEILK 211
Cdd:cd08568    63 -ELTYKELKKLH-----------PGGEL-IPTLEEVFRA---LPNDAIINVEIKDI----DAVE---------PVLEIVE 113

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1281033169 212 KYgyqgsylskNWLKQPVFiQSFAPTSIIHISNLTDLPKI-LLID 255
Cdd:cd08568   114 KF---------NALDRVIF-SSFNHDALRELRKLDPDAKVgLLIG 148
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 46-267 4.26e-11

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


Pssm-ID: 176507 [Multi-domain]  Cd Length: 265  Bit Score: 62.88  E-value: 4.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  46 TTRPYNIAHRG--SNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYRKFANRKRtyevqg 123
Cdd:cd08564     1 MVRPIIVGHRGagCSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHGTEDDTNPDTSIQLDDSGFKN------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169 124 vnitgffTVDFTLKELQSLRVKQRFpyrDQQYNGKFSIitfeDFIEIalqaPRVVGIYPEIKNPVFINQRVKwGDGKRFE 203
Cdd:cd08564    75 -------INDLSLDEITRLHFKQLF---DEKPCGADEI----KGEKI----PTLEDVLVTFKDKLKYNIELK-GREVGLG 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281033169 204 DKFVEILKKYG--YQGSYLSKNWLKQPVFIQSFaptsiihISNLTDLPKILLIDDTTIPTQDTNQT 267
Cdd:cd08564   136 ERVLNLVEKYGmiLQVHFSSFLHYDRLDLLKAL-------RPNKLNVPIALLFNEVKSPSPLDFLE 194
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 49-187 3.83e-10

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: 60.03  E-value: 3.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  49 PYNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDvgKYRKFAnrkrtyevqgvnitg 128
Cdd:cd08580     1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTN--GSGAVS--------------- 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281033169 129 fftvDFTLKELQSL------RVKQRFPYRDQQYngkfSIITFEDfieiALQAPRVVGIYPEIKNP 187
Cdd:cd08580    64 ----AYTAAQLATLnagynfKPEGGYPYRGKPV----GIPTLEQ----VLRAFPDTPFILDMKSL 116
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 51-197 4.38e-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: 58.60  E-value: 4.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  51 NIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKYRKFANRKRTYEVQGVNITGFF 130
Cdd:cd08555     1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGILPPTLEEVLELIADYLKNPDYTI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1281033169 131 TVDFTLK----ELQSLRVKQRFPYRDQQYNGKFSIITFEDFIEIAlqAPRVVGIYPEIKNPVFINQRVKWG 197
Cdd:cd08555    81 ILSLEIKqdspEYDEFLAKVLKELRVYFDYDLRGKVVLSSFNALG--VDYYNFSSKLIKDTELIASANKLG 149
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 51-109 4.75e-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: 60.31  E-value: 4.75e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1281033169  51 NIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKY 109
Cdd:cd08612    29 HISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKL 87
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 48-152 5.54e-09

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


Pssm-ID: 176551 [Multi-domain]  Cd Length: 315  Bit Score: 57.24  E-value: 5.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  48 RPYNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGKyrKFANRKRTYevqgvnit 127
Cdd:cd08609    26 KPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKD--VFPGRDAAG-------- 95

                          90       100
                  ....*....|....*....|....*
gi 1281033169 128 gffTVDFTLKELQSLRVKQRFPYRD 152
Cdd:cd08609    96 ---SNNFTWTELKTLNAGSWFLERR 117
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 48-108 1.36e-08

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: 56.04  E-value: 1.36e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1281033169  48 RPYNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGK 108
Cdd:cd08610    22 KPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNIGE 82
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 48-178 6.00e-08

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


Pssm-ID: 176550  Cd Length: 351  Bit Score: 54.08  E-value: 6.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  48 RPYNIAHRGSNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTDVGkyRKFANRKRTY-------E 120
Cdd:cd08608     1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVD--RVFPERQYEDasmfnwtD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1281033169 121 VQGVNITGFFTVDFTLKELQSLRVKQRFPYRDQqyngkfSIITFEDFIEIALQAPRVV 178
Cdd:cd08608    79 LERLNAGQWFLKDDPFWTAQSLSPSDRKEAGNQ------SVCSLAELLELAKRYNASV 130
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 48-142 1.34e-07

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: 52.75  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  48 RPYNIAHRGSNGEFPEE----------------------TLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTD 105
Cdd:cd08613    23 KPKLLAHRGLAQTFDREgvendtctaeridppthdylenTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTD 102

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1281033169 106 vgkyrkfanrkrtyeVQGVnitgffTVDFTLKELQSL 142
Cdd:cd08613   103 ---------------GSGV------TRDHTMAELKTL 118
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 52-144 2.30e-07

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: 51.90  E-value: 2.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  52 IAHRG--------SNGEFPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTdvgKYRKFANRKRTYEVqG 123
Cdd:cd08572     3 IGHRGlgknyasgSLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSE---KSKTGSDEGELIEV-P 78

                          90       100
                  ....*....|....*....|.
gi 1281033169 124 VNitgfftvDFTLKELQSLRV 144
Cdd:cd08572    79 IH-------DLTLEQLKELGL 92
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 51-147 3.46e-07

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: 51.53  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281033169  51 NIAHRGSNGEF-------PEETLPAYKRAIEEGADFIETDILSSKDGVLICFHDVTLDETTdvgkyrkfanrKRTYEVQG 123
Cdd:cd08607     2 DVGHRGAGNSYtaasavvRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSL-----------KSKGDSDR 70

                          90       100
                  ....*....|....*....|....
gi 1281033169 124 VNITGFFTVDFTLKELQSLRVKQR 147
Cdd:cd08607    71 DDLLEVPVKDLTYEQLKLLKLFHI 94
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 49-105 5.21e-06

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 47.24  E-value: 5.21e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1281033169  49 PYNIAHRGSNGEFPEETLPAykraIEEGADF----IETDILSSKDGVLICFHDVTLDETTD 105
Cdd:PRK09454    8 PRIVAHRGGGKLAPENTLAA----IDVGARYghrmIEFDAKLSADGEIFLLHDDTLERTSN 64
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 52-97 2.55e-03

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


Pssm-ID: 176547 [Multi-domain]  Cd Length: 282  Bit Score: 39.32  E-value: 2.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1281033169  52 IAHRGsNGE------------FPEETLPAYKRAIEEGADFIETDILSSKDGVLICFHD 97
Cdd:cd08605     3 IGHRG-LGMnrashqpsvgpgIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHD 59
 
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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