NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489311540|ref|WP_003218946|]
View 

MULTISPECIES: glycerophosphodiester phosphodiesterase family protein [Pseudomonas]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
1-237 2.48e-79

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


:

Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 238.23  E-value: 2.48e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   1 MTLIYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDArkGG 80
Cdd:COG0584    2 RPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDA--GS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  81 PGWVNPCPIPRLEELFEQCDFD-HWQLEVKSASRTRAATtVLAIREMAQRFGLMDKVTVTSSSREVLKAALDLTPDLSRG 159
Cdd:COG0584   80 GPDFAGERIPTLEEVLELVPGDvGLNIEIKSPPAAEPDL-AEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489311540 160 LVAEYAWLDPLKVAANYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLITDFPGLATATL 237
Cdd:COG0584  159 LLVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRAVL 236
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
1-237 2.48e-79

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 238.23  E-value: 2.48e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   1 MTLIYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDArkGG 80
Cdd:COG0584    2 RPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDA--GS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  81 PGWVNPCPIPRLEELFEQCDFD-HWQLEVKSASRTRAATtVLAIREMAQRFGLMDKVTVTSSSREVLKAALDLTPDLSRG 159
Cdd:COG0584   80 GPDFAGERIPTLEEVLELVPGDvGLNIEIKSPPAAEPDL-AEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489311540 160 LVAEYAWLDPLKVAANYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLITDFPGLATATL 237
Cdd:COG0584  159 LLVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRAVL 236
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 4-230 1.27e-56

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: 180.11  E-value: 1.27e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   4 IYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDArkGgpGW 83
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDA--G--SW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  84 VNPC----PIPRLEELFEQC-DFDHW-QLEVKSASRTRAATTVLAIREMAQRFGLMDKVTVTSSSREVLKAALDLTPDLS 157
Cdd:cd08562   77 FSPEfagePIPTLADVLELArELGLGlNLEIKPDPGDEALTARVVAAALRELWPHASKLLLSSFSLEALRAARRAAPELP 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489311540 158 RGLVAEYAWLDPLKVAANYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLITDFP 230
Cdd:cd08562  157 LGLLFDTLPADWLELLAALGAVSIHLNYRGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 7-232 2.44e-41

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: 141.38  E-value: 2.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540    7 HRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDARKG--GPGWV 84
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGnsGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   85 NPCPIPRLEELFEQcDFDHW---QLEVKSASRTRAATTVLAIREMAQRF-------GLMDKVTVTSSSREVLKAALDLTP 154
Cdd:pfam03009  81 ERVPFPTLEEVLEF-DWDVGfniEIKIKPYVEAIAPEEGLIVKDLLLSVdeilakkADPRRVIFSSFNPDELKRLRELAP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  155 DLSRGLV---AEYAWLDPLKVAANY-GCEILALNWTLCT---PERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLIT 227
Cdd:pfam03009 160 KLPLVFLssgRAYAEADLLERAAAFaGAPALLGEVALVDealPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVIT 239


                  ....*
gi 489311540  228 DFPGL 232
Cdd:pfam03009 240 DRPDT 244
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 4-228 3.84e-35

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 125.44  E-value: 3.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   4 IYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDArkggPGW 83
Cdd:PRK09454  10 IVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDA----GSW 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  84 VNPC----PIPRLEELFEQCDFD--HWQLEVKSASRTRAAT---TVLAIREMAQrfGLMDKVTVTSSSREVLKAALDLTP 154
Cdd:PRK09454  86 FSAAfagePLPTLSQVAARCRAHgmAANIEIKPTTGREAETgrvVALAARALWA--GAAVPPLLSSFSEDALEAARQAAP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489311540 155 DLSRGLVAEYAWLDPLKVAANYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLITD 228
Cdd:PRK09454 164 ELPRGLLLDEWPDDWLELTRRLGCVSLHLNHKLLDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTD 237
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
1-237 2.48e-79

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 238.23  E-value: 2.48e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   1 MTLIYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDArkGG 80
Cdd:COG0584    2 RPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDA--GS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  81 PGWVNPCPIPRLEELFEQCDFD-HWQLEVKSASRTRAATtVLAIREMAQRFGLMDKVTVTSSSREVLKAALDLTPDLSRG 159
Cdd:COG0584   80 GPDFAGERIPTLEEVLELVPGDvGLNIEIKSPPAAEPDL-AEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489311540 160 LVAEYAWLDPLKVAANYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLITDFPGLATATL 237
Cdd:COG0584  159 LLVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRAVL 236
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 4-230 1.27e-56

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: 180.11  E-value: 1.27e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   4 IYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDArkGgpGW 83
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDA--G--SW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  84 VNPC----PIPRLEELFEQC-DFDHW-QLEVKSASRTRAATTVLAIREMAQRFGLMDKVTVTSSSREVLKAALDLTPDLS 157
Cdd:cd08562   77 FSPEfagePIPTLADVLELArELGLGlNLEIKPDPGDEALTARVVAAALRELWPHASKLLLSSFSLEALRAARRAAPELP 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489311540 158 RGLVAEYAWLDPLKVAANYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLITDFP 230
Cdd:cd08562  157 LGLLFDTLPADWLELLAALGAVSIHLNYRGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 4-229 1.82e-56

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: 178.23  E-value: 1.82e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   4 IYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDptlkrttdrrgkvveysaadlvkmdarkggpgw 83
Cdd:cd08556    1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  84 vnpcpIPRLEELFEQC-DFDHWQLEVKSASRTRAAttVLAIREMAQRFGLMDKVTVTSSSREVLKAALDLTPDLSRGLVA 162
Cdd:cd08556   48 -----IPTLEEVLELVkGGVGLNIELKEPTRYPGL--EAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVPTGLLV 120

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489311540 163 EYAWLDPLK--VAANYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLITDF 229
Cdd:cd08556  121 DKPPLDPLLaeLARALGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITDD 189
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 2-230 5.61e-55

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: 175.82  E-value: 5.61e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   2 TLIYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDARKGGP 81
Cdd:cd08563    1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  82 GWVNPCPIPRLEELFEQC-DFDHW-QLEVKsasrtraaTTVLA-------IREMAQRFGLMDKVTVTSSSREVLKAALDL 152
Cdd:cd08563   81 EKFTGEKIPTLEEVLDLLkDKDLLlNIEIK--------TDVIHypgiekkVLELVKEYNLEDRVIFSSFNHESLKRLKKL 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489311540 153 TPDLSRGLVAEYAWLDPLKVAANYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLITDFP 230
Cdd:cd08563  153 DPKIKLALLYETGLQDPKDYAKKIGADSLHPDFKLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 4-233 6.51e-54

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: 173.60  E-value: 6.51e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   4 IYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDA---RKGG 80
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAgyhFTDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  81 PGWVNPC-----PIPRLEELFEQCDFDHWQLEVKSASRTRAATTVLAIRemaqRFGLMDKVTVTSSSREVLKAALDLTPD 155
Cdd:cd08561   81 GGRTYPYrgqgiRIPTLEELFEAFPDVRLNIEIKDDGPAAAAALADLIE----RYGAQDRVLVASFSDRVLRRFRRLCPR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 156 L----SRGLVAEYAWLDP--LKVAANYGCEILALNWT-----LCTPERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDS 224
Cdd:cd08561  157 VatsaGEGEVAAFVLASRlgLGSLYSPPYDALQIPVRyggvpLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLGVDG 236


                 ....*....
gi 489311540 225 LITDFPGLA 233
Cdd:cd08561  237 IITDRPDLL 245
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 4-232 2.09e-42

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: 144.76  E-value: 2.09e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   4 IYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTL--KRTTDRRGKVVEYSAADLVKMD------ 75
Cdd:cd08567    3 LQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLnpDITRDPDGAWLPYEGPALYELTlaeikq 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  76 ----ARKGGPGW---------VNPCPIPRLEELFEQCDFDHWQ-----LEVKSASRTRAATtvLAIREMAQ-------RF 130
Cdd:cd08567   83 ldvgEKRPGSDYaklfpeqipVPGTRIPTLEEVFALVEKYGNQkvrfnIETKSDPDRDILH--PPPEEFVDavlavirKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 131 GLMDKVTVTSSSREVLKAALDLTPDLSRG-LVAEYAWLDPLKVAANYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVN 209
Cdd:cd08567  161 GLEDRVVLQSFDWRTLQEVRRLAPDIPTVaLTEETTLGNLPRAAKKLGADIWSPYFTLVTKELVDEAHALGLKVVPWTVN 240

                        250       260
                 ....*....|....*....|...
gi 489311540 210 EPALMRRLADFGVDSLITDFPGL 232
Cdd:cd08567  241 DPEDMARLIDLGVDGIITDYPDL 263
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 7-232 2.44e-41

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: 141.38  E-value: 2.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540    7 HRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDARKG--GPGWV 84
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGnsGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   85 NPCPIPRLEELFEQcDFDHW---QLEVKSASRTRAATTVLAIREMAQRF-------GLMDKVTVTSSSREVLKAALDLTP 154
Cdd:pfam03009  81 ERVPFPTLEEVLEF-DWDVGfniEIKIKPYVEAIAPEEGLIVKDLLLSVdeilakkADPRRVIFSSFNPDELKRLRELAP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  155 DLSRGLV---AEYAWLDPLKVAANY-GCEILALNWTLCT---PERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLIT 227
Cdd:pfam03009 160 KLPLVFLssgRAYAEADLLERAAAFaGAPALLGEVALVDealPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVIT 239


                  ....*
gi 489311540  228 DFPGL 232
Cdd:pfam03009 240 DRPDT 244
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 7-232 1.77e-39

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: 136.29  E-value: 1.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   7 HRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDARKGGPGWVNP 86
Cdd:cd08582    4 HRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGSWKGESYKG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  87 CPIPRLEELFEQC-DFD-HWQLEVKSASRTRAATTVLaIREMAQRFGLMDKVTVTSSSREVLKAALDLTPDLSRGLVAEY 164
Cdd:cd08582   84 EKVPTLEEYLAIVpKYGkKLFIEIKHPRRGPEAEEEL-LKLLKESGLLPEQIVIISFDAEALKRVRELAPTLETLWLRNY 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489311540 165 A--WLDPLKVAANYGCEILALN-WTLCTPERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLITDFPGL 232
Cdd:cd08582  163 KspKEDPRPLAKSGGAAGLDLSyEKKLNPAFIKALRDAGLKLNVWTVDDAEDAKRLIELGVDSITTNRPGR 233
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 4-230 1.52e-36

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: 128.05  E-value: 1.52e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   4 IYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDARKGGPGw 83
Cdd:cd08579    1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIGENGHG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  84 vnpCPIPRLEELFEQCDFDHWQL--EVKSASRTRAattvlairEMAQRF-------GLMDKVTVTSSSREVLKAALDLTP 154
Cdd:cd08579   80 ---AKIPSLDEYLALAKGLKQKLliELKPHGHDSP--------DLVEKFvklykqnLIENQHQVHSLDYRVIEKVKKLDP 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489311540 155 DLSRGLVAEYAWLDPLKVAANYgceiLALNWTLCTPERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLITDFP 230
Cdd:cd08579  149 KIKTGYILPFNIGNLPKTNVDF----YSIEYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 4-228 3.84e-35

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 125.44  E-value: 3.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   4 IYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDArkggPGW 83
Cdd:PRK09454  10 IVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDA----GSW 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  84 VNPC----PIPRLEELFEQCDFD--HWQLEVKSASRTRAAT---TVLAIREMAQrfGLMDKVTVTSSSREVLKAALDLTP 154
Cdd:PRK09454  86 FSAAfagePLPTLSQVAARCRAHgmAANIEIKPTTGREAETgrvVALAARALWA--GAAVPPLLSSFSEDALEAARQAAP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489311540 155 DLSRGLVAEYAWLDPLKVAANYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLITD 228
Cdd:PRK09454 164 ELPRGLLLDEWPDDWLELTRRLGCVSLHLNHKLLDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTD 237
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 4-233 1.87e-33

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: 120.59  E-value: 1.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   4 IYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDARkggpGW 83
Cdd:cd08565    1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLR----DS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  84 VNPCpIPRLEELFE--QCDFDHWQLEVKS-ASRTRAATTVLAIREMAQRFGLMDKVTVTSSSREVLKAALDLTPDLSRGL 160
Cdd:cd08565   77 FGEK-IPTLEEVLAlfAPSGLELHVEIKTdADGTPYPGAAALAAATLRRHGLLERSVLTSFDPAVLTEVRKHPGVRTLGS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 161 VAE--YAWLDPLKVAANY----GCEI------LALNWTLCtperleKAQRQGLHVSVWTVNEPALMRRLADFGVDSLITD 228
Cdd:cd08565  156 VDEdmLERLGGELPFLTAtalkAHIVaveqslLAATWELV------RAAVPGLRLGVWTVNDDSLIRYWLACGVRQLTTD 229


                 ....*
gi 489311540 229 FPGLA 233
Cdd:cd08565  230 RPDLA 234
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 7-230 2.29e-30

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: 113.47  E-value: 2.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   7 HRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDAR--------K 78
Cdd:cd08575    6 HRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGygytfdggK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  79 GGPGWV-NPCPIPRLEELFEQcdFDHWQ--LEVKSASRTRAATTVLAIREmaqRFGLMDKVTVTSSSREVLKAALDLTP- 154
Cdd:cd08575   86 TGYPRGgGDGRIPTLEEVFKA--FPDTPinIDIKSPDAEELIAAVLDLLE---KYKREDRTVWGSTNPEYLRALHPENPn 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 155 -----DLSRGL----------------VAEYAWLDPLKVA----ANYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVN 209
Cdd:cd08575  161 lfesfSMTRCLllylalgytgllpfvpIKESFFEIPRPVIvletFTLGEGASIVAALLWWPNLFDHLRKRGIQVYLWVLN 240

                        250       260
                 ....*....|....*....|.
gi 489311540 210 EPALMRRLADFGVDSLITDFP 230
Cdd:cd08575  241 DEEDFEEAFDLGADGVMTDSP 261
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 3-230 4.24e-30

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: 112.01  E-value: 4.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   3 LIYGHRGAKGE-APENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDARKGGp 81
Cdd:cd08566    1 LVVAHRGGWGAgAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKDGD- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  82 GWVNPCPIPRLEELFEQC-DFDHWQLEVKSASRTRAAttvlairEMAQRFGLMDKVTVTSSSREVLKAALDLTP------ 154
Cdd:cd08566   80 GEVTDEKVPTLEEALAWAkGKILLNLDLKDADLDEVI-------ALVKKHGALDQVIFKSYSEEQAKELRALAPevmlmp 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 155 ------DLSRGLVAEYAWLDPLKVAANYGceilalnwTLCTPERLEKAQRQ-GLHVSV---WTVNEPALMR--------- 215
Cdd:cd08566  153 ivrdaeDLDEEEARAIDALNLLAFEITFD--------DLDLPPLFDELLRAlGIRVWVntlGDDDTAGLDRalsdprevw 224

                        250
                 ....*....|....*.
gi 489311540 216 -RLADFGVDSLITDFP 230
Cdd:cd08566  225 gELVDAGVDVIQTDRP 240
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 3-230 1.77e-28

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: 108.17  E-value: 1.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   3 LIYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTT--DRRGKVVEYSAADLVKMDARKgg 80
Cdd:cd08601    2 AVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTniERPGPVKDYTLAEIKQLDAGS-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  81 pgWVNPC-P-----------IPRLEELFEQCDFD-HWQLEVKSASRTRAATTVLaiREMAQRFGLM------DKVTVTSS 141
Cdd:cd08601   80 --WFNKAyPeyaresysglkVPTLEEVIERYGGRaNYYIETKSPDLYPGMEEKL--LATLDKYGLLtdnlknGQVIIQSF 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 142 SREVLKAALDLTPD------LSRGLVAEY--AWLDplkvAANYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVNEPAL 213
Cdd:cd08601  156 SKESLKKLHQLNPNiplvqlLWYGEGAETydKWLD----EIKEYAIGIGPSIADADPWMVHLIHKKGLLVHPYTVNEKAD 231

                        250
                 ....*....|....*..
gi 489311540 214 MRRLADFGVDSLITDFP 230
Cdd:cd08601  232 MIRLINWGVDGMFTNYP 248
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 4-230 5.36e-28

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: 106.54  E-value: 5.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   4 IYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDARKGGPgw 83
Cdd:cd08570    1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDSTWDELSHLRTIEEP-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  84 vnPCPIPRLEELFE-----QCDfDHW-QLEVKsasRTRAATTVL-AIREM----------AQR--FGLMDkVTVTSSSRE 144
Cdd:cd08570   79 --HQPMPTLKDVLEwlvehELP-DVKlMLDIK---RDNDPEILFkLIAEMlavkpdldfwRERiiLGLWH-LDFLKYGKE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 145 VLK----AALDLTPDLSRglvaEYAWLDPLKVAANYgceILALNWTLCTPERLEKAQRQGLHVSVWTVNEPALMRRLADF 220
Cdd:cd08570  152 VLPgfpvFHIGFSLDYAR----HFLNYSEKLVGISM---HFVSLWGPFGQAFLPELKKNGKKVFVWTVNTEEDMRYAIRL 224

                        250
                 ....*....|
gi 489311540 221 GVDSLITDFP 230
Cdd:cd08570  225 GVDGVITDDP 234
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 3-228 6.32e-27

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: 103.53  E-value: 6.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   3 LIYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDarkggpg 82
Cdd:cd08568    1 IILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLH------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  83 wVNPCPIPRLEELFEQCDFDH-WQLEVKSasrTRAATTVLairEMAQRFGLMDKVTVTSSSREVLKAALDLTPDLSRGLV 161
Cdd:cd08568   74 -PGGELIPTLEEVFRALPNDAiINVEIKD---IDAVEPVL---EIVEKFNALDRVIFSSFNHDALRELRKLDPDAKVGLL 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489311540 162 AEYAWLDPLKVAANYGCEILALNWTLCTP---------ERLEKAQRQGLHVSVWTVNEPALMRRLADFgVDSLITD 228
Cdd:cd08568  147 IGEEEEGFSIPELHEKLKLYSLHVPIDAIgyigfekfvELLRLLRKLGLKIVLWTVNDPELVPKLKGL-VDGVITD 221
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 4-228 1.11e-23

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: 95.40  E-value: 1.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   4 IYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDARKGGPGW 83
Cdd:cd08573    1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  84 --VNPCPIPRLEELFEQC-------DFDhwqleVKSASrTRAATtvlAIREMAQRF-GLMDKVTVTSSSREVLKAALDLT 153
Cdd:cd08573   81 srFPGEKIPTLEEAVKEClennlrmIFD-----VKSNS-SKLVD---ALKNLFKKYpGLYDKAIVCSFNPIVIYKVRKAD 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 154 PDLSRGLV---AEYA-------------WLDPLKVAANYGCEILALNWT--LC------------TPERLEKAQRQGLHV 203
Cdd:cd08573  152 PKILTGLTwrpWFLSytddeggprrksgWKHFLYSMLDVILEWSLHSWLpyFLgvsallihkddiSSAYVRYWRARGIRV 231

                        250       260
                 ....*....|....*....|....*.
gi 489311540 204 SVWTVNEPALMRRLAD-FGVdSLITD 228
Cdd:cd08573  232 IAWTVNTPTEKQYFAKtLNV-PYITD 256
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 6-230 1.19e-22

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


Pssm-ID: 176523 [Multi-domain]  Cd Length: 229  Bit Score: 92.01  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   6 GHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDARKggPGWVN 85
Cdd:cd08581    3 AHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVAE--PARFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  86 PC----PIPRLEELFEQCDfDHWQ----LEVKSASRTR-AATTVLA--IREMAQRFglmDKVTVTSSSREVLKAA----- 149
Cdd:cd08581   81 SRfagePLPSLAAVVQWLA-QHPQvtlfVEIKTESLDRfGLERVVDkvLRALPAVA---AQRVLISFDYDLLALAkqqgg 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 150 ------LDLTPDLSRGLVAEyawldplkvaanygceiLALNWTLCTPERL---EKAQRQGLHVSVWTVNEPALMRRLADF 220
Cdd:cd08581  157 prtgwvLPDWDDASLAEADE-----------------LQPDYLFCDKNLLpdtGDLWAGTWKWVIYEVNEPAEALALAAR 219

                        250
                 ....*....|
gi 489311540 221 GVDSLITDFP 230
Cdd:cd08581  220 GVALIETDNI 229
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 3-230 6.12e-18

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: 80.78  E-value: 6.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   3 LIYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTD------------RRGKVVEYSAAD 70
Cdd:cd08559    2 LVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNvaehfpfrgrkdTGYFVIDFTLAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  71 LVKMDARKGG--------PGWVNPCPIPRLEE---LFEQCDFDHWQ-----LEVKSASRTRAA--TTVLAIREMAQRFGL 132
Cdd:cd08559   82 LKTLRAGSWFnqryperaPSYYGGFKIPTLEEvieLAQGLNKSTGRnvgiyPETKHPTFHKQEgpDIEEKLLEVLKKYGY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 133 M---DKVTVTSSSREVLKAALDLTPDLSR-GLVAEYAWLDP--------------LKVAANYgCEILALNWTLCTPER-- 192
Cdd:cd08559  162 TgknDPVFIQSFEPESLKRLRNETPDIPLvQLIDYGDWAETdkkytyawlttdagLKEIAKY-ADGIGPWKSLIIPEDsn 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489311540 193 --------LEKAQRQGLHVSVWTVNEPAL---------MRRL-ADFGVDSLITDFP 230
Cdd:cd08559  241 gllvptdlVKDAHKAGLLVHPYTFRNENLflapdfkqdMDALyNAAGVDGVFTDFP 296
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 2-237 3.22e-17

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: 78.28  E-value: 3.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   2 TLIYGHRGA--KGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIH-------DPTLKRTTDRRGK-VVEYSAADL 71
Cdd:cd08564    4 PIIVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteddtnPDTSIQLDDSGFKnINDLSLDEI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  72 VKMDARKggPGWVNPCP--------IPRLEELFEQC-DFDHWQLEVKSasrtRAATTVLAIREMAQRFGLMDKVTVTS-S 141
Cdd:cd08564   84 TRLHFKQ--LFDEKPCGadeikgekIPTLEDVLVTFkDKLKYNIELKG----REVGLGERVLNLVEKYGMILQVHFSSfL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 142 SREVLKAALDLTPDLSRGLVAEYAW-------LDPLKVAANYGCEILALNWTLCTPERLEKAQRQGLHVSVW---TVNEP 211
Cdd:cd08564  158 HYDRLDLLKALRPNKLNVPIALLFNevkspspLDFLEQAKYYNATWVNFSYDFWTEEFVKKAHENGLKVMTYfdePVNDN 237

                        250       260
                 ....*....|....*....|....*..
gi 489311540 212 A-LMRRLADFGVDSLITDFPGLATATL 237
Cdd:cd08564  238 EeDYKVYLELGVDCICPNDPVLLVNFL 264
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 7-230 5.26e-17

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: 78.03  E-value: 5.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   7 HRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADL------VKMDARKGG 80
Cdd:cd08612   32 HRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLppylekLEVTFSPGD 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  81 PGWV--NPCPIPRLEELFEQCDFDHWQLEVKSASRtraattvLAIREMAQ---RFGLMDKVTVTSSSREVLKAALDLTPD 155
Cdd:cd08612  112 YCVPkgSDRRIPLLEEVFEAFPDTPINIDIKVEND-------ELIKKVSDlvrKYKREDITVWGSFNDEIVKKCHKENPN 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 156 LSRG---------LVAEYAWL-----------------------DPLKVAANYGCEILALNWTLCTPERLEKAQRQGLHV 203
Cdd:cd08612  185 IPLFfslkrvlllLLLYYTGLlpfipikesfleipmpsiflktyFPKSMSRLNRFVLFLIDWLLMRPSLFRHLQKRGIQV 264

                        250       260
                 ....*....|....*....|....*..
gi 489311540 204 SVWTVNEPALMRRLADFGVDSLITDFP 230
Cdd:cd08612  265 YGWVLNDEEEFERAFELGADGVMTDYP 291
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 5-217 2.34e-16

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: 75.44  E-value: 2.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   5 YGHRG---AKGEAPENTLTSFQECLKHGVRrCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMdARKGGP 81
Cdd:cd08585    7 IAHRGlhdRDAGIPENSLSAFRAAAEAGYG-IELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRAL-RLLGTD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  82 GwvnpcPIPRLEELFEQCDFDHWQL-EVKS-ASRTRA-ATTVLAIremaqrfgLMD---KVTVTSSSREVLKAALDLTPD 155
Cdd:cd08585   85 E-----HIPTLDEVLELVAGRVPLLiELKScGGGDGGlERRVLAA--------LKDykgPAAIMSFDPRVVRWFRKLAPG 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489311540 156 LSRGLVAE------YAWLDPLKVAANYGCEILA-----------LNWTLCTPERlekaQRQGLHVSVWTVNEPALMRRL 217
Cdd:cd08585  152 IPRGQLSEgsndeaDPAFWNEALLSALFSNLLTrpdfiayhlddLPNPFVTLAR----ALLGMPVIVWTVRTEEDIARL 226
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 3-58 5.58e-16

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: 74.65  E-value: 5.58e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489311540   3 LIYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTD 58
Cdd:cd08574    3 ALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTN 58
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 3-148 1.48e-15

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: 73.51  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   3 LIYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDA-----R 77
Cdd:cd08580    2 LIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAgynfkP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489311540  78 KGGPGWVN-PCPIPRLEELFEQCDFDHWQLEVKSasrTRAATTVLAIREMAQRFGLMDKVTVTSSSREVLKA 148
Cdd:cd08580   82 EGGYPYRGkPVGIPTLEQVLRAFPDTPFILDMKS---LPADPQAKAVARVLERENAWSRVRIYSTNADYQDA 150
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 6-229 3.80e-14

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: 70.00  E-value: 3.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   6 GHRG-----AKGEAP---ENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTL-----KRTTDRRGKVVEY------ 66
Cdd:cd08572    4 GHRGlgknyASGSLAgirENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTIsvsekSKTGSDEGELIEVpihdlt 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  67 -----------SAADLVKMDARKGGPGWVNPC------PIPRLEELFEQCD----FDhwqLEVK----SASRTRAATTVL 121
Cdd:cd08572   84 leqlkelglqhISALKRKALTRKAKGPKPNPWgmdehdPFPTLQEVLEQVPkdlgFN---IEIKypqlLEDGEGELTPYF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 122 AIREMAQRfgLMDKVTVTSSSREVLKAALDltPD----------------LSRGLVAEYAWLDP----LKVAAN--YGCE 179
Cdd:cd08572  161 ERNAFVDT--ILAVVFEHAGGRRIIFSSFD--PDicimlrlkqnkypvlfLTNGGTNEVEHMDPrrrsLQAAVNfaLAEG 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489311540 180 ILAL----NWTLCTPERLEKAQRQGLHVSVW--TVNEPALMRRLADFGVDSLITDF 229
Cdd:cd08572  237 LLGVvlhaEDLLKNPSLISLVKALGLVLFTYgdDNNDPENVKKQKELGVDGVIYDR 292
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 4-230 8.68e-14

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: 69.49  E-value: 8.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   4 IYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADlvkmdarkggPGW 83
Cdd:cd08608    4 IIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYED----------ASM 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  84 VNPCPIPRLE--ELFEQCDfDHWQLEVKSAS-RTRAAT-TVLAIREMAqRFGLMDKVTVTSSSRE--------------V 145
Cdd:cd08608   74 FNWTDLERLNagQWFLKDD-PFWTAQSLSPSdRKEAGNqSVCSLAELL-ELAKRYNASVLLNLRRpppnhpyhqswinlT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 146 LKAALD---------LTPDLSRGLVAEYAWL----DPLKVAANY----GCEILALNWTLCTPERLEKAQRQGLHVSVWTV 208
Cdd:cd08608  152 LKTILAsgipqeqvmWTPDWQRKLVRKVAPGfqqtSGEKLPVASlrerGITRLNLRYTQASAQEIRDYSASNLSVNLYTV 231

                        250       260
                 ....*....|....*....|..
gi 489311540 209 NEPALMRRLADFGVDSLITDFP 230
Cdd:cd08608  232 NEPWLYSLLWCSGVPSVTSDAS 253
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 6-229 2.50e-13

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: 65.92  E-value: 2.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   6 GHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRgkvveysaadlvkmdarkggpgwvn 85
Cdd:cd08555    3 SHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGI------------------------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  86 pcPIPRLEELFEQC-DFDHWQ-------LEVK--SASRTRAATTVLAIREMAQRFGLMDKVTVtsSSREVLKAALDLTPD 155
Cdd:cd08555   58 --LPPTLEEVLELIaDYLKNPdytiilsLEIKqdSPEYDEFLAKVLKELRVYFDYDLRGKVVL--SSFNALGVDYYNFSS 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489311540 156 LSRGLvaeyawldplkvaanygceilalnwtlctPERLEKAQRQGLHVSVWTVN-EPALMRRLADFGVDSLITDF 229
Cdd:cd08555  134 KLIKD-----------------------------TELIASANKLGLLSRIWTVNdNNEIINKFLNLGVDGLITDF 179
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 4-228 3.24e-13

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: 67.59  E-value: 3.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   4 IYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDrRGKVVEYSAAD---LVKMDARK-- 78
Cdd:cd08610   25 IIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTN-IGEVQPESACEnpaFFNWDFLStl 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  79 -GGPGWVNPCPIPRLEELFEQcDfdhwQLEVKSASRTRAAtTVLAIREMAQRFGLMD----------KVTVTSSSREVLK 147
Cdd:cd08610  104 nAGKWFVKPRPFYNMKPLSEA-D----KERARNQSIPKLS-NFLRLAEKENKLVIFDlyrpppkhpyRHTWIRRVLEVIL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 148 AALDLTPDL-------SRGLVAEYA--------WLDPLKVAANYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVNEPA 212
Cdd:cd08610  178 NEVGIEQHLvlwlpahDRQYVQSVApgfkqhvgRKVPIETLLKNNISILNLAYKKLFSNDIRDYKAANIHTNVYVINEPW 257

                        250
                 ....*....|....*.
gi 489311540 213 LMRRLADFGVDSLITD 228
Cdd:cd08610  258 LFSLAWCSGIHSVTTN 273
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 16-76 6.21e-10

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: 58.14  E-value: 6.21e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489311540  16 ENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRGKVVEYSAADLVKMDA 76
Cdd:cd08613   60 ENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELKTLDI 120
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 6-58 4.00e-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: 55.70  E-value: 4.00e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489311540   6 GHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTD 58
Cdd:cd08609   31 GHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTN 83
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 3-58 8.22e-09

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: 54.70  E-value: 8.22e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489311540   3 LIYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTD 58
Cdd:cd08600    2 IIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTN 57
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 3-78 1.08e-08

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: 54.61  E-value: 1.08e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489311540   3 LIYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDrrgkvveysAADLVKMDARK 78
Cdd:cd08602    2 LVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTD---------VADHPEFADRK 68
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 6-228 3.08e-08

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: 53.07  E-value: 3.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   6 GHRGA-----KGEA--PENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTDRRG------------KVVEY 66
Cdd:cd08607    4 GHRGAgnsytAASAvvRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGdsdrddllevpvKDLTY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  67 SAADLVKMDARKGGPGWVNPC-----------PIPRLEELFEQCDFD-------HWQLEVKSAS----------RTRAAT 118
Cdd:cd08607   84 EQLKLLKLFHISALKVKEYKSveededppehqPFPTLSDVLESVPEDvgfnieiKWPQQQKDGSweselftyfdRNLFVD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540 119 TVLAIremaqrfglmdkVTVTSSSREVLKAALDltPD----------------LSRGLVAEYA-WLDP----LKVAAN-- 175
Cdd:cd08607  164 IILKI------------VLEHAGKRRIIFSSFD--ADictmlrfkqnkypvlfLTQGKTQRYPeFMDLrtrtFEIAVNfa 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489311540 176 YGCEILALN----WTLCTPERLEKAQRQGLHVSVW--TVNEPALMRRLADFGVDSLITD 228
Cdd:cd08607  230 QAEELLGVNlhseDLLKDPSQIELAKSLGLVVFCWgdDLNDPENRKKLKELGVDGLIYD 288
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 3-58 4.29e-06

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 46.97  E-value: 4.29e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489311540   3 LIYGHRGAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLKRTTD 58
Cdd:PRK11143  28 IVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTD 83
GDPD_2 pfam13653
Glycerophosphoryl diester phosphodiesterase family; This family also includes ...
 202-230 5.65e-04

Glycerophosphoryl diester phosphodiesterase family; This family also includes glycerophosphoryl diester phosphodiesterases as well as 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: 433380 [Multi-domain]  Cd Length: 30  Bit Score: 36.32  E-value: 5.65e-04
                          10        20
                  ....*....|....*....|....*....
gi 489311540  202 HVSVWTVNEPALMRRLADFGVDSLITDFP 230
Cdd:pfam13653   1 KVRFWTIDNKAAWKELMRLGVDGLNTDDP 29
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 9-229 5.69e-04

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


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 39.98  E-value: 5.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   9 GAKGEAPENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHD---PTLKRT---TDRRGKVVEYsaadlvkmDARKGGP- 81
Cdd:cd08583    8 GIDGKTYTNSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHSwdeSLLKQLglpTSKNTKPLSY--------EEFKSKKi 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540  82 -GWVNPCPIPRLEELFEQCDFDHWQLEVKSASRTRAATTVLAIREMAQRFG--LMDKVTVTSSSREVLkAALDLTPDLSR 158
Cdd:cd08583   80 yGKYTPMDFKDVIDLLKKYPDVYIVTDTKQDDDNDIKKLYEYIVKEAKEVDpdLLDRVIPQIYNEEMY-EAIMSIYPFKS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489311540 159 GLVAEYA--WLDPLKVAA---NYGCEILALNWTLCTPERLEKAQRQGLHVSVWTVNEPALMRRLADFGVDSLITDF 229
Cdd:cd08583  159 VIYTLYRqdSIRLDEIIAfcyENGIKAVTISKNYVNDKLIEKLNKAGIYVYVYTINDLKDAQEYKKLGVYGIYTDF 234
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 6-100 5.43e-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: 37.39  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489311540   6 GHRG--------AKGEAP---ENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHDPTLkrtTDRRGKVVEYSA------ 68
Cdd:cd08605    4 GHRGlgmnrashQPSVGPgirENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFI---VVERGGEVESSRirdltl 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489311540  69 ADLVKMDA-------------RKGGPGWVNPC------PIPRLEELFEQCD 100
Cdd:cd08605   81 AELKALGPqaestktstvalyRKAKDPEPEPWimdvedSIPTLEEVFSEVP 131
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 2-50 9.40e-03

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL110cp and other uncharacterized fungal homologs. The product of S. cerevisiae ORF YPL110c (GDE1), YPL110cp (Gde1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL110cp has been characterized as a cytoplasmic glycerophosphocholine (GPC)-specific phosphodiesterase that selectively hydrolyzes GPC, not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate. YPL110cp has multi-domain architecture, including not only C-terminal GDPD, but also an SPX N-terminal domain along with several ankyrin repeats, which implies that YPL110cp may mediate protein-protein interactions in a variety of proteins and play a role in maintaining cellular phosphate levels. Members in this family are distantly related to S. cerevisiae YPL206cp, which selectively catalyzes the cleavage of phosphatidylglycerol (PG), not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate, and has been characterized as a PG-specific phospholipase C.


Pssm-ID: 176548 [Multi-domain]  Cd Length: 286  Bit Score: 36.65  E-value: 9.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489311540   2 TLIYGHRG-AKGEAP-------ENTLTSFQECLKHGVRRCELDLHLSMDGELMVIHD 50
Cdd:cd08606    2 VQVIGHRGlGKNTAErkslqlgENTVESFILAASLGASYVEVDVQLTKDLVPVIYHD 58
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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