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Conserved domains on  [gi|42563134|ref|NP_177290|]
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PLC-like phosphodiesterases superfamily protein [Arabidopsis thaliana]

Protein Classification

glycerophosphodiester phosphodiesterase( domain architecture ID 11426576)

glycerophosphodiester phosphodiesterase catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols

CATH:  3.20.20.190
EC:  3.1.4.-
Gene Ontology:  GO:0008081|GO:0006629|GO:0046872
PubMed:  38491249

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
73-313 4.19e-50

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


:

Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 166.58  E-value: 4.19e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  73 PLVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDVSEiv 152
Cdd:COG0584   3 PLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTT-NGTGRVADLTLAELRQLDAGS-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 153 KGTLGSSRIPTLEEALALISNSVRkVILDAKvGPPMYEKGLAQDILSIIERAQC-NNCIVWAKSDTLARDIIRRAPDTMV 231
Cdd:COG0584  80 GPDFAGERIPTLEEVLELVPGDVG-LNIEIK-SPPAAEPDLAEAVAALLKRYGLeDRVIVSSFDPEALRRLRELAPDVPL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 232 GYIVMVDPLTGARnsLLRMKGARVVGVYHPLIDEELVRVVRRRNKEVYAWTVDDADPMKRMLHLGVDAVVTSDPSMFQGL 311
Cdd:COG0584 158 GLLVEELPADPLE--LARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRAV 235


                ..
gi 42563134 312 ME 313
Cdd:COG0584 236 LR 237
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
73-313 4.19e-50

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 166.58  E-value: 4.19e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  73 PLVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDVSEiv 152
Cdd:COG0584   3 PLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTT-NGTGRVADLTLAELRQLDAGS-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 153 KGTLGSSRIPTLEEALALISNSVRkVILDAKvGPPMYEKGLAQDILSIIERAQC-NNCIVWAKSDTLARDIIRRAPDTMV 231
Cdd:COG0584  80 GPDFAGERIPTLEEVLELVPGDVG-LNIEIK-SPPAAEPDLAEAVAALLKRYGLeDRVIVSSFDPEALRRLRELAPDVPL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 232 GYIVMVDPLTGARnsLLRMKGARVVGVYHPLIDEELVRVVRRRNKEVYAWTVDDADPMKRMLHLGVDAVVTSDPSMFQGL 311
Cdd:COG0584 158 GLLVEELPADPLE--LARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRAV 235


                ..
gi 42563134 312 ME 313
Cdd:COG0584 236 LR 237
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 75-304 1.09e-43

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: 148.57  E-value: 1.09e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  75 VCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNrdlqriarnssvqvgdlsmkqikeldvseivkg 154
Cdd:cd08556   1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 155 tlgssrIPTLEEALALISNSVrKVILDAKVGPPmyEKGLAQDILSIIERAQC-NNCIVWAKSDTLARDIIRRAPDTMVGY 233
Cdd:cd08556  48 ------IPTLEEVLELVKGGV-GLNIELKEPTR--YPGLEAKVAELLREYGLeERVVVSSFDHEALRALKELDPEVPTGL 118

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42563134 234 IVMVDPLTGARNSLLRMKGARVVGVYHPLIDEELVRVVRRRNKEVYAWTVDDADPMKRMLHLGVDAVVTSD 304
Cdd:cd08556 119 LVDKPPLDPLLAELARALGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITDD 189
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 78-305 6.69e-24

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: 97.86  E-value: 6.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134    78 HGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDV-SEIVKGTL 156
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTT-DGAGYVRDLTLEELKRLDIgAGNSGPLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134   157 GS-SRIPTLEEALALISNsvRKVILDAKVGPPM-----YEKGLAQDILSIIeraqcnncIVWAKSDTLARDIIRR--APD 228
Cdd:pfam03009  80 GErVPFPTLEEVLEFDWD--VGFNIEIKIKPYVeaiapEEGLIVKDLLLSV--------DEILAKKADPRRVIFSsfNPD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134   229 TM------------VGYIVMVDP-LTGARNSLLRMKGARVVGVYHPLIDE---ELVRVVRRRNKEVYAWTVDDADPMKRM 292
Cdd:pfam03009 150 ELkrlrelapklplVFLSSGRAYaEADLLERAAAFAGAPALLGEVALVDEalpDLVKRAHARGLVVHVWTVNNEDEMKRL 229

                         250
                  ....*....|...
gi 42563134   293 LHLGVDAVVTSDP 305
Cdd:pfam03009 230 LELGVDGVITDRP 242
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 72-302 2.44e-07

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 51.09  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134   72 PPLVcAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDVSEI 151
Cdd:PRK09454   8 PRIV-AHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTS-NGWGVAGELTWQDLAQLDAGSW 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  152 VKGTLGSSRIPTLEEALA------LISN------------SVRKVILDAKVgppMYEKGLAQDILSIIEraqcnncivwa 213
Cdd:PRK09454  86 FSAAFAGEPLPTLSQVAArcrahgMAANieikpttgreaeTGRVVALAARA---LWAGAAVPPLLSSFS----------- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  214 kSDTL--ARDIirrAPDTMVGyiVMVDPLTGARNSLLRMKGARVVGVYHPLIDEELVRVVRRRNKEVYAWTVDDADPMKR 291
Cdd:PRK09454 152 -EDALeaARQA---APELPRG--LLLDEWPDDWLELTRRLGCVSLHLNHKLLDEARVAALKAAGLRILVYTVNDPARARE 225

                        250
                 ....*....|.
gi 42563134  292 MLHLGVDAVVT 302
Cdd:PRK09454 226 LLRWGVDCICT 236
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
73-313 4.19e-50

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 166.58  E-value: 4.19e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  73 PLVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDVSEiv 152
Cdd:COG0584   3 PLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTT-NGTGRVADLTLAELRQLDAGS-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 153 KGTLGSSRIPTLEEALALISNSVRkVILDAKvGPPMYEKGLAQDILSIIERAQC-NNCIVWAKSDTLARDIIRRAPDTMV 231
Cdd:COG0584  80 GPDFAGERIPTLEEVLELVPGDVG-LNIEIK-SPPAAEPDLAEAVAALLKRYGLeDRVIVSSFDPEALRRLRELAPDVPL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 232 GYIVMVDPLTGARnsLLRMKGARVVGVYHPLIDEELVRVVRRRNKEVYAWTVDDADPMKRMLHLGVDAVVTSDPSMFQGL 311
Cdd:COG0584 158 GLLVEELPADPLE--LARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRAV 235


                ..
gi 42563134 312 ME 313
Cdd:COG0584 236 LR 237
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 75-304 1.09e-43

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: 148.57  E-value: 1.09e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  75 VCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNrdlqriarnssvqvgdlsmkqikeldvseivkg 154
Cdd:cd08556   1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 155 tlgssrIPTLEEALALISNSVrKVILDAKVGPPmyEKGLAQDILSIIERAQC-NNCIVWAKSDTLARDIIRRAPDTMVGY 233
Cdd:cd08556  48 ------IPTLEEVLELVKGGV-GLNIELKEPTR--YPGLEAKVAELLREYGLeERVVVSSFDHEALRALKELDPEVPTGL 118

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42563134 234 IVMVDPLTGARNSLLRMKGARVVGVYHPLIDEELVRVVRRRNKEVYAWTVDDADPMKRMLHLGVDAVVTSD 304
Cdd:cd08556 119 LVDKPPLDPLLAELARALGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITDD 189
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 77-305 1.76e-34

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: 125.35  E-value: 1.76e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  77 AHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIA-RNSSVQvgDLSMKQIKELDVSEIVKGT 155
Cdd:cd08579   3 AHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAgVNKKVW--DLTLEELKKLTIGENGHGA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 156 lgssRIPTLEEALALISNSVRKVILDAKVgPPMYEKGLAQDILSIIERAQC-NNCIVWAKSDTLARDIIRRAPDTMVGYI 234
Cdd:cd08579  81 ----KIPSLDEYLALAKGLKQKLLIELKP-HGHDSPDLVEKFVKLYKQNLIeNQHQVHSLDYRVIEKVKKLDPKIKTGYI 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42563134 235 VMVDpltgarNSLLRMKGARVVGVYHPLIDEELVRVVRRRNKEVYAWTVDDADPMKRMLHLGVDAVVTSDP 305
Cdd:cd08579 156 LPFN------IGNLPKTNVDFYSIEYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 75-306 6.38e-29

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


Pssm-ID: 176524 [Multi-domain]  Cd Length: 233  Bit Score: 111.25  E-value: 6.38e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  75 VCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDVSEIVKG 154
Cdd:cd08582   1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTS-GGDGAVSDLTLAELRKLDIGSWKGE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 155 TLGSSRIPTLEEALALISNSVRKVILDAKvgPPMYEKGLAQDILSIIERAQC--NNCIVWAKSDTLARDIIRRAPDTMVG 232
Cdd:cd08582  80 SYKGEKVPTLEEYLAIVPKYGKKLFIEIK--HPRRGPEAEEELLKLLKESGLlpEQIVIISFDAEALKRVRELAPTLETL 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42563134 233 YIVMVDPltGARNSLLRMKGARVVGV---YHPLIDEELVRVVRRRNKEVYAWTVDDADPMKRMLHLGVDAVVTSDPS 306
Cdd:cd08582 158 WLRNYKS--PKEDPRPLAKSGGAAGLdlsYEKKLNPAFIKALRDAGLKLNVWTVDDAEDAKRLIELGVDSITTNRPG 232
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 73-305 1.43e-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: 104.56  E-value: 1.43e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  73 PLVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDVSEIV 152
Cdd:cd08563   1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTT-NGKGYVKDLTLEELKKLDAGSWF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 153 KGTLGSSRIPTLEEALALISNSvrKVIL------DAKVgppmYEkGLAQDILSIIERAQC-NNCIVwakS----DTLARd 221
Cdd:cd08563  80 DEKFTGEKIPTLEEVLDLLKDK--DLLLnieiktDVIH----YP-GIEKKVLELVKEYNLeDRVIF---SsfnhESLKR- 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 222 IIRRAPDTMVGYIVMvDPLTGARNSLLRMKgarvVGVYHP---LIDEELVRVVRRRNKEVYAWTVDDADPMKRMLHLGVD 298
Cdd:cd08563 149 LKKLDPKIKLALLYE-TGLQDPKDYAKKIG----ADSLHPdfkLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVD 223


                ....*..
gi 42563134 299 AVVTSDP 305
Cdd:cd08563 224 GIITNYP 230
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 77-312 5.78e-26

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: 5.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  77 AHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDVSEIVKGTL 156
Cdd:cd08561   3 AHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTT-DGTGPVADLTLAELRRLDAGYHFTDDG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 157 GSS--------RIPTLEEALALISNsVRKVIlDAKVGPPmyekGLAQDILSIIERA-QCNNCIVWAKSDTLARDIIRRAP 227
Cdd:cd08561  82 GRTypyrgqgiRIPTLEELFEAFPD-VRLNI-EIKDDGP----AAAAALADLIERYgAQDRVLVASFSDRVLRRFRRLCP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 228 DTMV--GYIVMVDPLTGAR---NSLLRMKGA------RVVGVyhPLIDEELVRVVRRRNKEVYAWTVDDADPMKRMLHLG 296
Cdd:cd08561 156 RVATsaGEGEVAAFVLASRlglGSLYSPPYDalqipvRYGGV--PLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLG 233

                       250
                ....*....|....*.
gi 42563134 297 VDAVVTSDPSMFQGLM 312
Cdd:cd08561 234 VDGIITDRPDLLLEVL 249
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 78-305 6.69e-24

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: 97.86  E-value: 6.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134    78 HGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDV-SEIVKGTL 156
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTT-DGAGYVRDLTLEELKRLDIgAGNSGPLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134   157 GS-SRIPTLEEALALISNsvRKVILDAKVGPPM-----YEKGLAQDILSIIeraqcnncIVWAKSDTLARDIIRR--APD 228
Cdd:pfam03009  80 GErVPFPTLEEVLEFDWD--VGFNIEIKIKPYVeaiapEEGLIVKDLLLSV--------DEILAKKADPRRVIFSsfNPD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134   229 TM------------VGYIVMVDP-LTGARNSLLRMKGARVVGVYHPLIDE---ELVRVVRRRNKEVYAWTVDDADPMKRM 292
Cdd:pfam03009 150 ELkrlrelapklplVFLSSGRAYaEADLLERAAAFAGAPALLGEVALVDEalpDLVKRAHARGLVVHVWTVNNEDEMKRL 229

                         250
                  ....*....|...
gi 42563134   293 LHLGVDAVVTSDP 305
Cdd:pfam03009 230 LELGVDGVITDRP 242
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 73-305 1.39e-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: 91.99  E-value: 1.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  73 PLVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQ-RIARNSS--------VQVGDLSMKQI 143
Cdd:cd08567   1 FDLQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNpDITRDPDgawlpyegPALYELTLAEI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 144 KELDVSEIVKGTLGSS-----------RIPTLEEALALISNSVRKVIL--------DAKVGPPMYEKGLAQDILSIIERA 204
Cdd:cd08567  81 KQLDVGEKRPGSDYAKlfpeqipvpgtRIPTLEEVFALVEKYGNQKVRfnietksdPDRDILHPPPEEFVDAVLAVIRKA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 205 Q-CNNCIVWAKSDTLARDIIRRAPDTMVGYIVMvdpLTGARNSLLRMK--GARVVGVYHPLIDEELVRVVRRRNKEVYAW 281
Cdd:cd08567 161 GlEDRVVLQSFDWRTLQEVRRLAPDIPTVALTE---ETTLGNLPRAAKklGADIWSPYFTLVTKELVDEAHALGLKVVPW 237

                       250       260
                ....*....|....*....|....
gi 42563134 282 TVDDADPMKRMLHLGVDAVVTSDP 305
Cdd:cd08567 238 TVNDPEDMARLIDLGVDGIITDYP 261
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 74-305 1.62e-21

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: 91.21  E-value: 1.62e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  74 LVCAHGGDSTLAFP-NTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNrdlQRIARNSSVQ--VGDLSMKQIKELDVSe 150
Cdd:cd08566   1 LVVAHRGGWGAGAPeNSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHD---DTLDRTTNGKgkVSDLTLAEIRKLRLK- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 151 IVKGTLGSSRIPTLEEALALISNSVrKVILDAKvgppmyeKGLAQDILSIIERAQC-NNCIVWAKSDTLARDIIRRAPDT 229
Cdd:cd08566  77 DGDGEVTDEKVPTLEEALAWAKGKI-LLNLDLK-------DADLDEVIALVKKHGAlDQVIFKSYSEEQAKELRALAPEV 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 230 MvgYIVMVDPLTG-ARNSLLRMKGARVVGVY----HPLIDEELVRVVRRRNKEVYAWTVDDADPMK-------------R 291
Cdd:cd08566 149 M--LMPIVRDAEDlDEEEARAIDALNLLAFEitfdDLDLPPLFDELLRALGIRVWVNTLGDDDTAGldralsdprevwgE 226

                       250
                ....*....|....
gi 42563134 292 MLHLGVDAVVTSDP 305
Cdd:cd08566 227 LVDAGVDVIQTDRP 240
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 73-305 2.89e-19

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE4 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1)) and similar proteins. Mammalian GDE4 is a transmembrane protein whose cellular function is not elucidated. It is expressed widely, including in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. It is also expressed in the growth cones in neuroblastoma Neuro2a cells, which suggests mammalian GDE4 may play some distinct role from other members of mammalian GDEs family. Also included in this subfamily are uncharacterized mammalian glycerophosphodiester phosphodiesterase domain-containing protein 3 (GDPD3) and similar proteins which display very high sequence homology to mammalian GDE4.


Pssm-ID: 176517 [Multi-domain]  Cd Length: 264  Bit Score: 85.73  E-value: 2.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  73 PLVCAH-GGdsTLAFP-NTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDVSE 150
Cdd:cd08575   1 PLHIAHrGG--AAEFPeNTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLT-GGSGLVSDLTYAELPPLDAGY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 151 IVKGTLGSS---------RIPTLEEALALISNsvRKVILDAKVgPPMYEkgLAQDILSIIERAQCNNCIVW-----AKSD 216
Cdd:cd08575  78 GYTFDGGKTgyprgggdgRIPTLEEVFKAFPD--TPINIDIKS-PDAEE--LIAAVLDLLEKYKREDRTVWgstnpEYLR 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 217 TLARD-----IIRRAPDTMVGYIVM-----VDPLTGARNSL-LRMKGARV------VGVYHP---LIDEELVRVVRRRNK 276
Cdd:cd08575 153 ALHPEnpnlfESFSMTRCLLLYLALgytglLPFVPIKESFFeIPRPVIVLetftlgEGASIVaalLWWPNLFDHLRKRGI 232

                       250       260
                ....*....|....*....|....*....
gi 42563134 277 EVYAWTVDDADPMKRMLHLGVDAVVTSDP 305
Cdd:cd08575 233 QVYLWVLNDEEDFEEAFDLGADGVMTDSP 261
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 77-305 3.93e-19

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: 84.58  E-value: 3.93e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  77 AHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDV----SEIV 152
Cdd:cd08562   3 AHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTT-NGSGAVTELTWAELAQLDAgswfSPEF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 153 KGTlgssRIPTLEEALALISNSVRKVILDAKVGpPMYEKGLAQDILSIIERAQCNNCIVWAKS-DTLARDIIRR-APDTM 230
Cdd:cd08562  82 AGE----PIPTLADVLELARELGLGLNLEIKPD-PGDEALTARVVAAALRELWPHASKLLLSSfSLEALRAARRaAPELP 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42563134 231 VGYIVMV---DPLTgarnsLLRMKGARVVGVYHPLIDEELVRVVRRRNKEVYAWTVDDADPMKRMLHLGVDAVVTSDP 305
Cdd:cd08562 157 LGLLFDTlpaDWLE-----LLAALGAVSIHLNYRGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 74-305 8.04e-19

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: 83.50  E-value: 8.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  74 LVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRiarnssvqVGDLSMKqIKELDVSEIVK 153
Cdd:cd08568   1 IILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKR--------VGGVDLK-VKELTYKELKK 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 154 GTLGSSRIPTLEEALALISNsvRKVI-LDAKvgppmyEKGLAQDILSIIERAQC-NNCIVWAKSDTLARDIIRRAPDTMV 231
Cdd:cd08568  72 LHPGGELIPTLEEVFRALPN--DAIInVEIK------DIDAVEPVLEIVEKFNAlDRVIFSSFNHDALRELRKLDPDAKV 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 232 GYivMVDPLTGAR--NSLLRMKGARVVGVYHPLIDE-------ELVRVVRRRNKEVYAWTVDDADPMKRMLHLgVDAVVT 302
Cdd:cd08568 144 GL--LIGEEEEGFsiPELHEKLKLYSLHVPIDAIGYigfekfvELLRLLRKLGLKIVLWTVNDPELVPKLKGL-VDGVIT 220


                ...
gi 42563134 303 SDP 305
Cdd:cd08568 221 DDV 223
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 73-308 4.36e-15

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: 73.89  E-value: 4.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  73 PLVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIAR-NSSVQVGDLSMKQIKELDVS-- 149
Cdd:cd08601   1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNiERPGPVKDYTLAEIKQLDAGsw 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 150 ------EIVKGTLGSSRIPTLEEALALISNSVrKVILDAKVgpPMYEKGLAQDILSIIERAQCNNcivwaKSDTLARDII 223
Cdd:cd08601  81 fnkaypEYARESYSGLKVPTLEEVIERYGGRA-NYYIETKS--PDLYPGMEEKLLATLDKYGLLT-----DNLKNGQVII 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 224 R----------RAPDTMVGYIVMVDPLTGARNSLLRMK----GARVVGVYHPLIDEELVRVVRRRNKEVYAWTVDDADPM 289
Cdd:cd08601 153 QsfskeslkklHQLNPNIPLVQLLWYGEGAETYDKWLDeikeYAIGIGPSIADADPWMVHLIHKKGLLVHPYTVNEKADM 232

                       250
                ....*....|....*....
gi 42563134 290 KRMLHLGVDAVVTSDPSMF 308
Cdd:cd08601 233 IRLINWGVDGMFTNYPDRL 251
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 75-305 2.38e-14

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


Pssm-ID: 176512 [Multi-domain]  Cd Length: 234  Bit Score: 71.10  E-value: 2.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  75 VCAHGGDStLAFP-NTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRiarnssvqVGDLSMKQIKELDVSEIvk 153
Cdd:cd08570   1 VIGHRGYK-AKYPeNTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKR--------CFGKDGLIIDDSTWDEL-- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 154 GTL-----GSSRIPTLEEALALISNSVR---KVILDAKV-GPPMYEKGLAQDILSIieraqcNNCIvwaksDTLARDII- 223
Cdd:cd08570  70 SHLrtieePHQPMPTLKDVLEWLVEHELpdvKLMLDIKRdNDPEILFKLIAEMLAV------KPDL-----DFWRERIIl 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 224 ------------RRAPDTMVGYIVMvdpltgarnSLLRMK-----GARVVGV-------YHPLIDeELVRVVRRRNKEVY 279
Cdd:cd08570 139 glwhldflkygkEVLPGFPVFHIGF---------SLDYARhflnySEKLVGIsmhfvslWGPFGQ-AFLPELKKNGKKVF 208

                       250       260
                ....*....|....*....|....*.
gi 42563134 280 AWTVDDADPMKRMLHLGVDAVVTSDP 305
Cdd:cd08570 209 VWTVNTEEDMRYAIRLGVDGVITDDP 234
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 75-305 9.23e-13

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


Pssm-ID: 176508 [Multi-domain]  Cd Length: 235  Bit Score: 66.66  E-value: 9.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  75 VCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDvseiVKG 154
Cdd:cd08565   1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTT-HGTGAVRDLTLAERKALR----LRD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 155 TLGSSrIPTLEEALALISNSVRKVILDAKVGPP-MYEKGLAQDILSIIERAQCNNCIVWAKSDTLARDIIRRAPDTMVgy 233
Cdd:cd08565  76 SFGEK-IPTLEEVLALFAPSGLELHVEIKTDADgTPYPGAAALAAATLRRHGLLERSVLTSFDPAVLTEVRKHPGVRT-- 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42563134 234 IVMVDP----LTGARNSLLRMK--GARVVGVYHPLIDEELVRVVR-RRNKEVYAWTVDDADPMKRMLHLGVDAVVTSDP 305
Cdd:cd08565 153 LGSVDEdmleRLGGELPFLTATalKAHIVAVEQSLLAATWELVRAaVPGLRLGVWTVNDDSLIRYWLACGVRQLTTDRP 231
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 77-294 3.74e-12

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE1 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE1 (also known as MIR16, membrane interacting protein of RGS16) and their metazoan homologs. GDE1 is widely expressed in mammalian tissues, including the heart, brain, liver, and kidney. It shows sequence homology to bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. GDE1 has been characterized as GPI-GDE (EC 3.1.4.44) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate glycerol phosphate and inositol. It functions as an integral membrane-bound glycoprotein interacting with regulator of G protein signaling protein RGS16, and is modulated by G protein-coupled receptor (GPCR) signaling. In addition, GDE1 may interact with PRA1 domain family, member 2 (PRAF2, also known as JM4), which is an interacting protein of the G protein-coupled chemokine receptor CCR5. The catalytic activity, which is dependent on the integrity of the GDPD domain, is required for GDE1 cellular function.


Pssm-ID: 176515 [Multi-domain]  Cd Length: 258  Bit Score: 65.36  E-value: 3.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  77 AHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDVS--EIVKG 154
Cdd:cd08573   3 GHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTT-DGTGLVAELTWEELRKLNAAakHRLSS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 155 TLGSSRIPTLEEALALISNSVRKVILDAKVG---------------PPMYEKGL-----AQDILSIieRAQCNNCIV--- 211
Cdd:cd08573  82 RFPGEKIPTLEEAVKECLENNLRMIFDVKSNssklvdalknlfkkyPGLYDKAIvcsfnPIVIYKV--RKADPKILTglt 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 212 ---WAKSDTLARDIIRRAPDTMVGYIVMVDPLT--GARNSLLRMKGARVVGVYHPLIDEELVRVVRRRNKEVYAWTVDDA 286
Cdd:cd08573 160 wrpWFLSYTDDEGGPRRKSGWKHFLYSMLDVILewSLHSWLPYFLGVSALLIHKDDISSAYVRYWRARGIRVIAWTVNTP 239


                ....*...
gi 42563134 287 DPMKRMLH 294
Cdd:cd08573 240 TEKQYFAK 247
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 72-305 1.60e-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: 63.65  E-value: 1.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  72 PPLVCAH--GGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRD-------LQRIARNSSVQVGDLSMKQ 142
Cdd:cd08564   3 RPIIVGHrgAGCSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHGTEddtnpdtSIQLDDSGFKNINDLSLDE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 143 IKELDVSEIV------KGTLGSSRIPTLEEALALISNSVrKVILDAKvGPpmyEKGLAQDILSIIERAQCNNCIV----- 211
Cdd:cd08564  83 ITRLHFKQLFdekpcgADEIKGEKIPTLEDVLVTFKDKL-KYNIELK-GR---EVGLGERVLNLVEKYGMILQVHfssfl 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 212 WAKSDTLARDIIRRAPDTMVGYIVMVDPLTGARNSLLRMK--GARVVGVYHPLIDEELVRVVRRRNKEVYAW----TVDD 285
Cdd:cd08564 158 HYDRLDLLKALRPNKLNVPIALLFNEVKSPSPLDFLEQAKyyNATWVNFSYDFWTEEFVKKAHENGLKVMTYfdepVNDN 237

                       250       260
                ....*....|....*....|
gi 42563134 286 ADPMKRMLHLGVDAVVTSDP 305
Cdd:cd08564 238 EEDYKVYLELGVDCICPNDP 257
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 73-305 1.03e-09

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


Pssm-ID: 176522 [Multi-domain]  Cd Length: 263  Bit Score: 58.11  E-value: 1.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  73 PLVCAH-GGdsTLAFP-NTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDVS- 149
Cdd:cd08580   1 PLIVAHrGG--TADAPeNTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLT-NGSGAVSAYTAAQLATLNAGy 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 150 ----EIVKGTLGSS-RIPTLEEALALISNSVrkVILDAKVGPPmyeKGLAQDILSIIERAQC-NNCIVWAKS----DTLA 219
Cdd:cd08580  78 nfkpEGGYPYRGKPvGIPTLEQVLRAFPDTP--FILDMKSLPA---DPQAKAVARVLERENAwSRVRIYSTNadyqDALA 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 220 ----------RDIIRRapdTMVGyIVM-----VDPLTGARNSL-LRMK---------GARVVGVYHPLIDEELVRVVRRR 274
Cdd:cd08580 153 pypqarlfesRDVTRT---RLAN-VAMahqcdLPPDSGAWAGFeLRRKvtvvetftlGEGRSPVQATLWTPAAVDCFRRN 228

                       250       260       270
                ....*....|....*....|....*....|..
gi 42563134 275 NK-EVYAWTVDDADPMKRMLHLGVDAVVTSDP 305
Cdd:cd08580 229 SKvKIVLFGINTADDYRLAKCLGADAVMVDSP 260
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 73-171 3.49e-08

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: 53.82  E-value: 3.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  73 PLVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIARNSSVQ-----------VGDLSMK 141
Cdd:cd08559   1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVAEHFpfrgrkdtgyfVIDFTLA 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 42563134 142 QIKELDVSEIVKGTL--------GSSRIPTLEEALALI 171
Cdd:cd08559  81 ELKTLRAGSWFNQRYperapsyyGGFKIPTLEEVIELA 118
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 68-203 8.16e-08

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


Pssm-ID: 176527 [Multi-domain]  Cd Length: 237  Bit Score: 52.32  E-value: 8.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  68 WLHHPPLvcAHGG--DSTLAFP-NTMDAYSFAIRSRVDcIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIK 144
Cdd:cd08585   1 WLKDRPI--AHRGlhDRDAGIPeNSLSAFRAAAEAGYG-IELDVQLTADGEVVVFHDDNLKRLT-GVEGRVEELTAAELR 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42563134 145 ELDvseiVKGTlgSSRIPTLEEALALISNSVrKVILDAKvGPPMYEKGLAQDILSIIER 203
Cdd:cd08585  77 ALR----LLGT--DEHIPTLDEVLELVAGRV-PLLIELK-SCGGGDGGLERRVLAALKD 127
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 77-173 2.08e-07

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: 51.18  E-value: 2.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  77 AHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIARNSSVqVGDLSMKQIKELDVSEivKGTL 156
Cdd:cd08581   3 AHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGL-LHELEDAELDSLRVAE--PARF 79

                        90       100
                ....*....|....*....|.
gi 42563134 157 GSS----RIPTLEEALALISN 173
Cdd:cd08581  80 GSRfagePLPSLAAVVQWLAQ 100
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 72-302 2.44e-07

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 51.09  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134   72 PPLVcAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIArNSSVQVGDLSMKQIKELDVSEI 151
Cdd:PRK09454   8 PRIV-AHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTS-NGWGVAGELTWQDLAQLDAGSW 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  152 VKGTLGSSRIPTLEEALA------LISN------------SVRKVILDAKVgppMYEKGLAQDILSIIEraqcnncivwa 213
Cdd:PRK09454  86 FSAAFAGEPLPTLSQVAArcrahgMAANieikpttgreaeTGRVVALAARA---LWAGAAVPPLLSSFS----------- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  214 kSDTL--ARDIirrAPDTMVGyiVMVDPLTGARNSLLRMKGARVVGVYHPLIDEELVRVVRRRNKEVYAWTVDDADPMKR 291
Cdd:PRK09454 152 -EDALeaARQA---APELPRG--LLLDEWPDDWLELTRRLGCVSLHLNHKLLDEARVAALKAAGLRILVYTVNDPARARE 225

                        250
                 ....*....|.
gi 42563134  292 MLHLGVDAVVT 302
Cdd:PRK09454 226 LLRWGVDCICT 236
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 73-285 3.57e-07

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: 50.38  E-value: 3.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  73 PLVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQR-----------IARNSSvqvgDLSMK 141
Cdd:cd08574   2 PALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRttnvadvfperAHERAS----MFTWT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 142 QIKELD----------------VSEIVKGTLGSSRIPTLEEALALISNSVRKVILDAKvGPPM---YEKGLAQDILSIIE 202
Cdd:cd08574  78 DLQQLNagqwflkddpfwtassLSESDREEAGNQSIPSLAELLRLAKKHNKSVIFDLR-RPPPnhpYYQSYVNITLDTIL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 203 RAQCNNCIVWAKSDTLARDIIRRAPDtmvgyivmVDPLTGAR--NSLLRMKGARVVGVYHPLIDEELVRVVRRRNKEVYA 280
Cdd:cd08574 157 ASGIPQHQVFWLPDEYRALVRKVAPG--------FQQVSGRKlpVESLRENGISRLNLEYSQLSAQEIREYSKANISVNL 228


                ....*
gi 42563134 281 WTVDD 285
Cdd:cd08574 229 YVVNE 233
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 73-309 1.90e-06

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: 48.77  E-value: 1.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  73 PLVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDL-----------QRIARNSSvqvgDLSMK 141
Cdd:cd08609  27 PALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLlrttnvkdvfpGRDAAGSN----NFTWT 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 142 QIKELD----------------VSEIVKGTLGSSRIPTLEEALALISNSVRKVILDAKVGPP--MYEKGLAQDILSIIER 203
Cdd:cd08609 103 ELKTLNagswflerrpfwtlssLSEEDRREADNQTVPSLSELLDLAKKHNVSIMFDLRNENNshVFYSSFVFYTLETILK 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 204 AQCNNCIVWAKSDTLARDIIRRAPDTMVGYivmvdpltgARNSLLRMKGARVVGVYHPLIDEELVRVVRRRNKEVYAWTV 283
Cdd:cd08609 183 LGIPPDKVWWLPDEYRHDVMKMEPGFKQVY---------GRQKEMLMDGGNFMNLPYQDLSALEIKELRKDNVSVNLWVV 253

                       250       260
                ....*....|....*....|....*.
gi 42563134 284 DDADPMKRMLHLGVDAVVTSDPSMFQ 309
Cdd:cd08609 254 NEPWLFSLLWCSGVSSVTTNACQLLK 279
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 75-302 2.90e-06

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: 47.05  E-value: 2.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  75 VCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNrdlqriarnssvqvgdlsmkqikeldvsEIVKG 154
Cdd:cd08555   1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHG----------------------------PTLDR 52

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134 155 TLGSSRIPTLEEALALIS----NSVRKVI--LDAKVGPPMYEKGLAQdilsiieraqcnncivwaksdtLARDIIRRAPD 228
Cdd:cd08555  53 TTAGILPPTLEEVLELIAdylkNPDYTIIlsLEIKQDSPEYDEFLAK----------------------VLKELRVYFDY 110

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42563134 229 TMVGYIVmvdpltgarnslLRMKGARVVGVY--HPL--IDEELVRVVRRRNKEVYAWTVDDADPM-KRMLHLGVDAVVT 302
Cdd:cd08555 111 DLRGKVV------------LSSFNALGVDYYnfSSKliKDTELIASANKLGLLSRIWTVNDNNEIiNKFLNLGVDGLIT 177
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 73-124 3.40e-05

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: 44.97  E-value: 3.40e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 42563134  73 PLVCAHGGDSTLaFP-NTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDL 124
Cdd:cd08571   1 PLVIARGGASGD-YPdSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINL 52
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 73-170 4.03e-04

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: 41.52  E-value: 4.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563134  73 PLVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHN---------------RDLQRIARNSSVQVG- 136
Cdd:cd08602   1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEpelsgttdvadhpefADRKTTKTVDGVNVTg 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 42563134 137 ----DLSMKQIKELDVSE----IVKGTLGSSRIPTLEEALAL 170
Cdd:cd08602  81 wfteDFTLAELKTLRARQrlpyRDQSYDGQFPIPTFEEIIAL 122
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 73-126 7.06e-04

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: 40.98  E-value: 7.06e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 42563134  73 PLVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQR 126
Cdd:cd08608   2 PAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRR 55
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 73-134 8.04e-04

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: 40.63  E-value: 8.04e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42563134  73 PLVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIARNSSVQ 134
Cdd:cd08610  23 PTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNIGEVQ 84
 
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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