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Conserved domains on  [gi|1267979542|ref|WP_098626650|]
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MULTISPECIES: glycerophosphodiester phosphodiesterase family protein [Priestia]

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];
33-261 7.54e-95

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


:

Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 279.45  E-value: 7.54e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSwkGDSF 112
Cdd:COG0584     6 IAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGS--GPDF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 113 TNEKIPTLSQVLDEFQGKIGILIELKAPE-LYPGIEKKVAFEINKRQL-DHVIIQSFNVSSMKKMHELLPNVPIGILTSs 190
Cdd:COG0584    84 AGERIPTLEEVLELVPGDVGLNIEIKSPPaAEPDLAEAVAALLKRYGLeDRVIVSSFDPEALRRLRELAPDVPLGLLVE- 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267979542 191 qrDASPNSIQQFAAF-ATYFNPSYDILTPALIHQVHSAGMKISPWsgTKRLPASF--LWKTKSDGVITNYPDEV 261
Cdd:COG0584   163 --ELPADPLELARALgADGVGPDYDLLTPELVAAAHAAGLKVHVW--TVNDPEEMrrLLDLGVDGIITDRPDLL 232
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
33-261 7.54e-95

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 279.45  E-value: 7.54e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSwkGDSF 112
Cdd:COG0584     6 IAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGS--GPDF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 113 TNEKIPTLSQVLDEFQGKIGILIELKAPE-LYPGIEKKVAFEINKRQL-DHVIIQSFNVSSMKKMHELLPNVPIGILTSs 190
Cdd:COG0584    84 AGERIPTLEEVLELVPGDVGLNIEIKSPPaAEPDLAEAVAALLKRYGLeDRVIVSSFDPEALRRLRELAPDVPLGLLVE- 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267979542 191 qrDASPNSIQQFAAF-ATYFNPSYDILTPALIHQVHSAGMKISPWsgTKRLPASF--LWKTKSDGVITNYPDEV 261
Cdd:COG0584   163 --ELPADPLELARALgADGVGPDYDLLTPELVAAAHAAGLKVHVW--TVNDPEEMrrLLDLGVDGIITDRPDLL 232
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 32-258 2.68e-79

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: 239.77  E-value: 2.68e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  32 NIAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSWKGDS 111
Cdd:cd08563     3 IFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFDEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 112 FTNEKIPTLSQVLDEFQGKIGIL-IELKAPEL-YPGIEKKVAFEINKRQL-DHVIIQSFNVSSMKKMHELLPNVPIGILT 188
Cdd:cd08563    83 FTGEKIPTLEEVLDLLKDKDLLLnIEIKTDVIhYPGIEKKVLELVKEYNLeDRVIFSSFNHESLKRLKKLDPKIKLALLY 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 189 SSQRDASPNSIQQFAAFAtyFNPSYDILTPALIHQVHSAGMKISPWSGTKRLPASFLWKTKSDGVITNYP 258
Cdd:cd08563   163 ETGLQDPKDYAKKIGADS--LHPDFKLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 35-260 9.42e-62

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: 195.70  E-value: 9.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  35 HRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSWKGDSFTN 114
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 115 EK--IPTLSQVLDEFQGkIGILIELKaPELYPGIEKKVAFEINKRQLDH-------------VIIQSFNVSSMKKMHELL 179
Cdd:pfam03009  81 ERvpFPTLEEVLEFDWD-VGFNIEIK-IKPYVEAIAPEEGLIVKDLLLSvdeilakkadprrVIFSSFNPDELKRLRELA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 180 PNVPIGILTSSQRDASPNSIQQFAAFATYF-----NPSYDILTPALIHQVHSAGMKISPWsgTKRLPASFLWKTKS--DG 252
Cdd:pfam03009 159 PKLPLVFLSSGRAYAEADLLERAAAFAGAPallgeVALVDEALPDLVKRAHARGLVVHVW--TVNNEDEMKRLLELgvDG 236


                  ....*...
gi 1267979542 253 VITNYPDE 260
Cdd:pfam03009 237 VITDRPDT 244
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 33-261 2.47e-40

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 140.46  E-value: 2.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSWKGDSF 112
Cdd:PRK09454   11 VAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAAF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 113 TNEKIPTLSQVLDEFQgKIGIL--IELKaPElyPGIE----KKVAFEInkRQL-----DHVIIQSFNVSSMKKMHELLPN 181
Cdd:PRK09454   91 AGEPLPTLSQVAARCR-AHGMAanIEIK-PT--TGREaetgRVVALAA--RALwagaaVPPLLSSFSEDALEAARQAAPE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 182 VPIGILTSSQRDASPNSIQQFAAFATYFNPSYdiLTPALIHQVHSAGMKISPWSGTKRLPASFLWKTKSDGVITNYPDEV 261
Cdd:PRK09454  165 LPRGLLLDEWPDDWLELTRRLGCVSLHLNHKL--LDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTDRIDLI 242
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
33-261 7.54e-95

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 279.45  E-value: 7.54e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSwkGDSF 112
Cdd:COG0584     6 IAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGS--GPDF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 113 TNEKIPTLSQVLDEFQGKIGILIELKAPE-LYPGIEKKVAFEINKRQL-DHVIIQSFNVSSMKKMHELLPNVPIGILTSs 190
Cdd:COG0584    84 AGERIPTLEEVLELVPGDVGLNIEIKSPPaAEPDLAEAVAALLKRYGLeDRVIVSSFDPEALRRLRELAPDVPLGLLVE- 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267979542 191 qrDASPNSIQQFAAF-ATYFNPSYDILTPALIHQVHSAGMKISPWsgTKRLPASF--LWKTKSDGVITNYPDEV 261
Cdd:COG0584   163 --ELPADPLELARALgADGVGPDYDLLTPELVAAAHAAGLKVHVW--TVNDPEEMrrLLDLGVDGIITDRPDLL 232
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 32-258 2.68e-79

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: 239.77  E-value: 2.68e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  32 NIAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSWKGDS 111
Cdd:cd08563     3 IFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFDEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 112 FTNEKIPTLSQVLDEFQGKIGIL-IELKAPEL-YPGIEKKVAFEINKRQL-DHVIIQSFNVSSMKKMHELLPNVPIGILT 188
Cdd:cd08563    83 FTGEKIPTLEEVLDLLKDKDLLLnIEIKTDVIhYPGIEKKVLELVKEYNLeDRVIFSSFNHESLKRLKKLDPKIKLALLY 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 189 SSQRDASPNSIQQFAAFAtyFNPSYDILTPALIHQVHSAGMKISPWSGTKRLPASFLWKTKSDGVITNYP 258
Cdd:cd08563   163 ETGLQDPKDYAKKIGADS--LHPDFKLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 31-259 1.29e-77

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: 236.44  E-value: 1.29e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  31 TNIAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGH--IRELTYAELQRLDAGSW- 107
Cdd:cd08601     2 AVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIERPgpVKDYTLAEIKQLDAGSWf 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 108 -------KGDSFTNEKIPTLSQVLDEFQGKIGILIELKAPELYPGIEKKVAFEINKRQL-------DHVIIQSFNVSSMK 173
Cdd:cd08601    82 nkaypeyARESYSGLKVPTLEEVIERYGGRANYYIETKSPDLYPGMEEKLLATLDKYGLltdnlknGQVIIQSFSKESLK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 174 KMHELLPNVPIGILTS--SQRDASPNSIQQFAAFATYFNPSYDILTPALIHQVHSAGMKISPWSGTKRLPASFLWKTKSD 251
Cdd:cd08601   162 KLHQLNPNIPLVQLLWygEGAETYDKWLDEIKEYAIGIGPSIADADPWMVHLIHKKGLLVHPYTVNEKADMIRLINWGVD 241


                  ....*...
gi 1267979542 252 GVITNYPD 259
Cdd:cd08601   242 GMFTNYPD 249
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 33-257 4.08e-64

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: 199.80  E-value: 4.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDrtvdrttngsghireltyaelqrldagswkgdsf 112
Cdd:cd08556     2 IAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD---------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 113 tnekIPTLSQVLDEFQGKIGILIELKAPELYPGIEKKVAFEINKRQL-DHVIIQSFNVSSMKKMHELLPNVPIGILTSSQ 191
Cdd:cd08556    48 ----IPTLEEVLELVKGGVGLNIELKEPTRYPGLEAKVAELLREYGLeERVVVSSFDHEALRALKELDPEVPTGLLVDKP 123

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267979542 192 RDASPNSIQQFAAFATYFNPSYDILTPALIHQVHSAGMKISPWSGTKRLPASFLWKTKSDGVITNY 257
Cdd:cd08556   124 PLDPLLAELARALGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITDD 189
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 33-258 7.22e-64

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: 200.53  E-value: 7.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSWKGDSF 112
Cdd:cd08562     2 IAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFSPEF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 113 TNEKIPTLSQVLD---EFQgkIGILIELKApelYPGIEKKVAFEINK--RQLDH----VIIQSFNVSSMKKMHELLPNVP 183
Cdd:cd08562    82 AGEPIPTLADVLElarELG--LGLNLEIKP---DPGDEALTARVVAAalRELWPhaskLLLSSFSLEALRAARRAAPELP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267979542 184 IGILTSsqrDASPNSIQQFAAF-ATYFNPSYDILTPALIHQVHSAGMKISPWSGTKRLPASFLWKTKSDGVITNYP 258
Cdd:cd08562   157 LGLLFD---TLPADWLELLAALgAVSIHLNYRGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 35-260 9.42e-62

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: 195.70  E-value: 9.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  35 HRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSWKGDSFTN 114
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 115 EK--IPTLSQVLDEFQGkIGILIELKaPELYPGIEKKVAFEINKRQLDH-------------VIIQSFNVSSMKKMHELL 179
Cdd:pfam03009  81 ERvpFPTLEEVLEFDWD-VGFNIEIK-IKPYVEAIAPEEGLIVKDLLLSvdeilakkadprrVIFSSFNPDELKRLRELA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 180 PNVPIGILTSSQRDASPNSIQQFAAFATYF-----NPSYDILTPALIHQVHSAGMKISPWsgTKRLPASFLWKTKS--DG 252
Cdd:pfam03009 159 PKLPLVFLSSGRAYAEADLLERAAAFAGAPallgeVALVDEALPDLVKRAHARGLVVHVW--TVNNEDEMKRLLELgvDG 236


                  ....*...
gi 1267979542 253 VITNYPDE 260
Cdd:pfam03009 237 VITDRPDT 244
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 31-258 2.50e-61

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: 196.34  E-value: 2.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  31 TNIAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGH------------IRELTYAE 98
Cdd:cd08559     2 LVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVAEHfpfrgrkdtgyfVIDFTLAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  99 LQRLDAGSWK--------GDSFTNEKIPTLSQVLDEFQG-------KIGILIELKAPE----LYPGIEKKVAFEINKRQL 159
Cdd:cd08559    82 LKTLRAGSWFnqryperaPSYYGGFKIPTLEEVIELAQGlnkstgrNVGIYPETKHPTfhkqEGPDIEEKLLEVLKKYGY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 160 ----DHVIIQSFNVSSMKKMHELLPNVP----IGILTSSQRD--------ASPNSIQQFAAFATYFNPSYDILT------ 217
Cdd:cd08559   162 tgknDPVFIQSFEPESLKRLRNETPDIPlvqlIDYGDWAETDkkytyawlTTDAGLKEIAKYADGIGPWKSLIIpedsng 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1267979542 218 ----PALIHQVHSAGMKISPWsgTKRLPASFLWKTKS------------DGVITNYP 258
Cdd:cd08559   242 llvpTDLVKDAHKAGLLVHPY--TFRNENLFLAPDFKqdmdalynaagvDGVFTDFP 296
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 32-259 7.17e-59

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: 188.24  E-value: 7.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  32 NIAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSW---- 107
Cdd:cd08561     1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHftdd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 108 KGDSF----TNEKIPTLSQVLDEFQGkIGILIELKAPElyPGIEKKVAFEINK-RQLDHVIIQSFNVSSMKKMHELLPNV 182
Cdd:cd08561    81 GGRTYpyrgQGIRIPTLEELFEAFPD-VRLNIEIKDDG--PAAAAALADLIERyGAQDRVLVASFSDRVLRRFRRLCPRV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 183 PIGiltssqrdASPNSIQQFAAFA-----TYFNPSYDIL------------TPALIHQVHSAGMKISPWsgT-------K 238
Cdd:cd08561   158 ATS--------AGEGEVAAFVLASrlglgSLYSPPYDALqipvryggvplvTPRFVRAAHAAGLEVHVW--TvndpaemR 227

                         250       260
                  ....*....|....*....|.
gi 1267979542 239 RLPAsflwkTKSDGVITNYPD 259
Cdd:cd08561   228 RLLD-----LGVDGIITDRPD 243
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 33-259 7.38e-58

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: 185.21  E-value: 7.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSWKGDSF 112
Cdd:cd08582     2 IAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGSWKGESY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 113 TNEKIPTLSQVLDEF-QGKIGILIELKAPELYPGIEKKVAFEINKRQLDH---VIIqSFNVSSMKKMHELLPNVPIGILT 188
Cdd:cd08582    82 KGEKVPTLEEYLAIVpKYGKKLFIEIKHPRRGPEAEEELLKLLKESGLLPeqiVII-SFDAEALKRVRELAPTLETLWLR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267979542 189 SSQRDASPNSIQQFAAFATYFNPSYD-ILTPALIHQVHSAGMKISPWsgTKRLPASFLW--KTKSDGVITNYPD 259
Cdd:cd08582   161 NYKSPKEDPRPLAKSGGAAGLDLSYEkKLNPAFIKALRDAGLKLNVW--TVDDAEDAKRliELGVDSITTNRPG 232
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 33-237 5.87e-54

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: 175.57  E-value: 5.87e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAY-APENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSWKGDs 111
Cdd:cd08566     3 VAHRGGWGAgAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKDGDGE- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 112 FTNEKIPTLSQVLDEFQGKIGILIELKapelyPGIEKKVAFEINKRQ-LDHVIIQSFNVSSMKKMHELLPNVPIG-ILTS 189
Cdd:cd08566    82 VTDEKVPTLEEALAWAKGKILLNLDLK-----DADLDEVIALVKKHGaLDQVIFKSYSEEQAKELRALAPEVMLMpIVRD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1267979542 190 SQRDASPNSIQQFAAFATYFNPSY-DILTPALIHQV-HSAGMKIspWSGT 237
Cdd:cd08566   157 AEDLDEEEARAIDALNLLAFEITFdDLDLPPLFDELlRALGIRV--WVNT 204
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 33-259 4.04e-49

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: 163.64  E-value: 4.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVD-RTTNGSGH---------IRELTYAELQRL 102
Cdd:cd08567     4 QGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNpDITRDPDGawlpyegpaLYELTLAEIKQL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 103 DAGSWKGDS-----------FTNEKIPTLSQVLDEFQG----KIGILIELK----APELYPGIE---KKVAFEINK-RQL 159
Cdd:cd08567    84 DVGEKRPGSdyaklfpeqipVPGTRIPTLEEVFALVEKygnqKVRFNIETKsdpdRDILHPPPEefvDAVLAVIRKaGLE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 160 DHVIIQSFNVSSMKKMHELLPNVPIGILTSSQRDASPNSIQQfAAFATYFNPSYDILTPALIHQVHSAGMKISPWsgTKR 239
Cdd:cd08567   164 DRVVLQSFDWRTLQEVRRLAPDIPTVALTEETTLGNLPRAAK-KLGADIWSPYFTLVTKELVDEAHALGLKVVPW--TVN 240

                         250       260
                  ....*....|....*....|..
gi 1267979542 240 LPASFLW--KTKSDGVITNYPD 259
Cdd:cd08567   241 DPEDMARliDLGVDGIITDYPD 262
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 33-258 5.66e-49

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: 161.94  E-value: 5.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSWkgdsF 112
Cdd:cd08579     2 IAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIGEN----G 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 113 TNEKIPTLSQVLDEFQG-KIGILIELK-APELYPGIEKKVAFEINKRQL-DHVIIQSFNVSSMKKMHELLPNVPIGILTS 189
Cdd:cd08579    78 HGAKIPSLDEYLALAKGlKQKLLIELKpHGHDSPDLVEKFVKLYKQNLIeNQHQVHSLDYRVIEKVKKLDPKIKTGYILP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267979542 190 SQRDASPNSiqqfaaFATYFNPSYDILTPALIHQVHSAGMKISPWSGTKRLPASFLWKTKSDGVITNYP 258
Cdd:cd08579   158 FNIGNLPKT------NVDFYSIEYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 33-184 1.92e-45

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: 154.30  E-value: 1.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAG------- 105
Cdd:cd08575     4 IAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGygytfdg 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 106 SWKGDSFTNE--KIPTLSQVLDEFQGKIgILIELKAPELYPGIEKKVAFEINKRQLDHVIIQSFNVSSMKKMHELLPNVP 183
Cdd:cd08575    84 GKTGYPRGGGdgRIPTLEEVFKAFPDTP-INIDIKSPDAEELIAAVLDLLEKYKREDRTVWGSTNPEYLRALHPENPNLF 162


                  .
gi 1267979542 184 I 184
Cdd:cd08575   163 E 163
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 33-261 2.47e-40

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 140.46  E-value: 2.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSWKGDSF 112
Cdd:PRK09454   11 VAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAAF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 113 TNEKIPTLSQVLDEFQgKIGIL--IELKaPElyPGIE----KKVAFEInkRQL-----DHVIIQSFNVSSMKKMHELLPN 181
Cdd:PRK09454   91 AGEPLPTLSQVAARCR-AHGMAanIEIK-PT--TGREaetgRVVALAA--RALwagaaVPPLLSSFSEDALEAARQAAPE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 182 VPIGILTSSQRDASPNSIQQFAAFATYFNPSYdiLTPALIHQVHSAGMKISPWSGTKRLPASFLWKTKSDGVITNYPDEV 261
Cdd:PRK09454  165 LPRGLLLDEWPDDWLELTRRLGCVSLHLNHKL--LDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTDRIDLI 242
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 33-178 1.32e-38

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: 135.61  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSWKGdsf 112
Cdd:cd08565     2 AGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLRDSFG--- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267979542 113 tnEKIPTLSQVLDEFQ-GKIGILIELK---APELYPGIEKKVAFEINKRQLDHV-IIQSFNVSSMKKMHEL 178
Cdd:cd08565    79 --EKIPTLEEVLALFApSGLELHVEIKtdaDGTPYPGAAALAAATLRRHGLLERsVLTSFDPAVLTEVRKH 147
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 33-186 2.54e-34

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: 125.06  E-value: 2.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSWKGDS- 111
Cdd:cd08573     2 IGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRLSs 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267979542 112 -FTNEKIPTLSQVLDE-FQGKIGILIELKAPELypGIEKKVAFEINKR-QL-DHVIIQSFNVSSMKKMHELLPNVPIGI 186
Cdd:cd08573    82 rFPGEKIPTLEEAVKEcLENNLRMIFDVKSNSS--KLVDALKNLFKKYpGLyDKAIVCSFNPIVIYKVRKADPKILTGL 158
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 33-221 1.12e-33

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: 122.44  E-value: 1.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDA--GSWKGD 110
Cdd:cd08581     2 VAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVaePARFGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 111 SFTNEKIPTLSQVLDEFQGK--IGILIELKAPEL-YPGIEKKVA--FEINKRQLDHVIIQSFNVSSMKKMHELLpNVPIG 185
Cdd:cd08581    82 RFAGEPLPSLAAVVQWLAQHpqVTLFVEIKTESLdRFGLERVVDkvLRALPAVAAQRVLISFDYDLLALAKQQG-GPRTG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1267979542 186 ILTSSQRDASPNSIQQfaafatyFNPSYDILTPALI 221
Cdd:cd08581   161 WVLPDWDDASLAEADE-------LQPDYLFCDKNLL 189
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 35-258 1.90e-33

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: 122.97  E-value: 1.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  35 HRGA--SAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMH---DRTVDRTT-----NGSGHIRELTYAELQRL-- 102
Cdd:cd08564     9 HRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteDDTNPDTSiqlddSGFKNINDLSLDEITRLhf 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 103 ----DAGSWKGDSFTNEKIPTLSQVLDEFQGKIGILIELKAPELYPGIEKKVAFEINKRQLDhVIIQSFN-VSSMKKMHE 177
Cdd:cd08564    89 kqlfDEKPCGADEIKGEKIPTLEDVLVTFKDKLKYNIELKGREVGLGERVLNLVEKYGMILQ-VHFSSFLhYDRLDLLKA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 178 LLPN---VPIGILTSSQRDASPNSIQQFAA--FATYFNPSYDILTPALIHQVHSAGMKISPWSGTKRLPASFLWK----T 248
Cdd:cd08564   168 LRPNklnVPIALLFNEVKSPSPLDFLEQAKyyNATWVNFSYDFWTEEFVKKAHENGLKVMTYFDEPVNDNEEDYKvyleL 247

                         250
                  ....*....|
gi 1267979542 249 KSDGVITNYP 258
Cdd:cd08564   248 GVDCICPNDP 257
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 33-194 1.13e-32

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: 120.12  E-value: 1.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRG---ASAYAPENTMAAFHQALEmnADY-IELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGSwk 108
Cdd:cd08585     7 IAHRGlhdRDAGIPENSLSAFRAAAE--AGYgIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRLLG-- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 109 gdsfTNEKIPTLSQVLDEFQGKIGILIELKAPELYPG-IEKKVAfEINKRQLDHVIIQSFNVSSMKKMHELLPNVPIGIL 187
Cdd:cd08585    83 ----TDEHIPTLDEVLELVAGRVPLLIELKSCGGGDGgLERRVL-AALKDYKGPAAIMSFDPRVVRWFRKLAPGIPRGQL 157


                  ....*..
gi 1267979542 188 TSSQRDA 194
Cdd:cd08585   158 SEGSNDE 164
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 33-259 3.82e-32

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: 120.96  E-value: 3.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTN------------GSGHIRELTYAELQ 100
Cdd:cd08600     4 IAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNvaekfpdrkrkdGRYYVIDFTLDELK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 101 RLDAGS-----WK------GDSF----TNEKIPTLSQVLDEFQG-------KIGILIELKAPELYPGIEK---KVAFEIN 155
Cdd:cd08600    84 SLSVTErfdieNGkkvqvyPNRFplwkSDFKIHTLEEEIELIQGlnkstgkNVGIYPEIKAPWFHHQEGKdiaAATLEVL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 156 KR-----QLDHVIIQSFNVSSMKKM-HELLP----NVPIG--ILTSSQRDA-----------------SPNSIQQFAAFA 206
Cdd:cd08600   164 KKygytsKNDKVYLQTFDPNELKRIkNELLPkmgmDLKLVqlIAYTDWGETqekdpggwvnydydwmfTKGGLKEIAKYA 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267979542 207 TYFNPSY-----------DILTPALIHQVHSAGMKISPWSGTK-RLPA----------SFLWKTKSDGVITNYPD 259
Cdd:cd08600   244 DGVGPWYsmiieeksskgNIVLTDLVKDAHEAGLEVHPYTVRKdALPEyakdadqlldALLNKAGVDGVFTDFPD 318
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 25-186 1.81e-31

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: 118.47  E-value: 1.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  25 RTEEKLTNIAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAEL----Q 100
Cdd:cd08612    22 KSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLppylE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 101 RLDAGSWKGD----SFTNEKIPTLSQVLDEFQGkIGILIELKAPElyPGIEKKVAFEINKRQLDHVII-QSFNVSSMKKM 175
Cdd:cd08612   102 KLEVTFSPGDycvpKGSDRRIPLLEEVFEAFPD-TPINIDIKVEN--DELIKKVSDLVRKYKREDITVwGSFNDEIVKKC 178

                         170
                  ....*....|.
gi 1267979542 176 HELLPNVPIGI 186
Cdd:cd08612   179 HKENPNIPLFF 189
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 33-258 2.57e-30

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: 113.55  E-value: 2.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGswkgdsf 112
Cdd:cd08568     3 LGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHPG------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 113 tNEKIPTLSQVLDEFQGKIGILIELKAPElypGIEKKVAFEINKRQLDHVIIQSFNVSSMKKMHELLPNVPIGILTSSQR 192
Cdd:cd08568    76 -GELIPTLEEVFRALPNDAIINVEIKDID---AVEPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPDAKVGLLIGEEE 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267979542 193 DAsPNSIQQFAAFATY-FNPSYDILTP-------ALIHQVHSAGMKISPWsgTKRLPaSFLWKTKS--DGVITNYP 258
Cdd:cd08568   152 EG-FSIPELHEKLKLYsLHVPIDAIGYigfekfvELLRLLRKLGLKIVLW--TVNDP-ELVPKLKGlvDGVITDDV 223
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 31-258 2.87e-30

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: 115.47  E-value: 2.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  31 TNIAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIR------------------ 92
Cdd:cd08602     2 LVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHPEfadrkttktvdgvnvtgw 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  93 ---ELTYAELQRLDA--------GSWKGdSFTnekIPTLSQVLD-------EFQGKIGILIELKAP-----ELYPGIEKK 149
Cdd:cd08602    82 fteDFTLAELKTLRArqrlpyrdQSYDG-QFP---IPTFEEIIAlakaasaATGRTVGIYPEIKHPtyfnaPLGLPMEDK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 150 VAFEINKRQLDH----VIIQSFNVSSMKKMHEL---------------LPNVPIGILTSSQRDASPNSIQQFAAFATYFN 210
Cdd:cd08602   158 LLETLKKYGYTGkkapVFIQSFEVTNLKYLRNKtdlplvqliddatipPQDTPEGDSRTYADLTTDAGLKEIATYADGIG 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267979542 211 PSYDILTPA-----------LIHQVHSAGMKISPWsgTKRLPASFL-WKTKS--------------DGVITNYP 258
Cdd:cd08602   238 PWKDLIIPSdangrlgtptdLVEDAHAAGLQVHPY--TFRNENTFLpPDFFGdpyaeyrafldagvDGLFTDFP 309
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 1-259 1.17e-29

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 115.16  E-value: 1.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542   1 MKKYLAGLSAVALLCCSiaSSAFARTEEKLTnIAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRT 80
Cdd:PRK11143    1 LKNLSLALLLAALLAGS--AAAAADSAEKIV-IAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  81 VDRTTN------------GSGHIRELTYAELQRL--------DAGS-----------WKGDsFTnekIPTLSQVLDEFQG 129
Cdd:PRK11143   78 LDRVTDvaerfpdrarkdGRYYAIDFTLDEIKSLkftegfdiENGKkvqvypgrfpmGKSD-FR---VHTFEEEIEFIQG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 130 -------KIGILIELKAPELY----PGIEKKVaFEINKR-----QLDHVIIQSFNVSSMKKM-HELLPNV---------- 182
Cdd:PRK11143  154 lnhstgkNIGIYPEIKAPWFHhqegKDIAAKV-LEVLKKygytgKDDKVYLQCFDANELKRIkNELEPKMgmdlklvqli 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 183 ------------PIGILTSSQRDA--SPNSIQQFAAFATYFNPSYD------------ILTPaLIHQVHSAGMKISPWSG 236
Cdd:PRK11143  233 aytdwnetqekqPDGKWVNYNYDWmfKPGAMKEVAKYADGIGPDYHmlvdetstpgniKLTG-MVKEAHQAKLVVHPYTV 311

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1267979542 237 TK-RLPA----------SFLWKTKSDGVITNYPD 259
Cdd:PRK11143  312 RAdQLPEyatdvnqlydILYNQAGVDGVFTDFPD 345
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 32-258 3.72e-29

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: 110.77  E-value: 3.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  32 NIAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIREL-TYAELQRL---DAGSw 107
Cdd:cd08570     1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDsTWDELSHLrtiEEPH- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 108 kgdsftnEKIPTLSQVLD---EFQGK-IGILIELKA---PELypgIEKKVA--FEIN---KRQLDHVIIQSFNVSSMKKM 175
Cdd:cd08570    80 -------QPMPTLKDVLEwlvEHELPdVKLMLDIKRdndPEI---LFKLIAemLAVKpdlDFWRERIILGLWHLDFLKYG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 176 HELLPNVPIGILTSSQRDASP--NSIQQFAAFATYFNPSYDILTPALIHQVHSAGMKISPWSGTKRLPASFLWKTKSDGV 253
Cdd:cd08570   150 KEVLPGFPVFHIGFSLDYARHflNYSEKLVGISMHFVSLWGPFGQAFLPELKKNGKKVFVWTVNTEEDMRYAIRLGVDGV 229


                  ....*
gi 1267979542 254 ITNYP 258
Cdd:cd08570   230 ITDDP 234
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 33-168 2.46e-26

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: 103.94  E-value: 2.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAGsW----K 108
Cdd:cd08580     4 VAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAG-YnfkpE 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267979542 109 GDSF---TNEKIPTLSQVLDEFQgKIGILIELKAPELYPGIeKKVAFEINKRQ-LDHVIIQSFN 168
Cdd:cd08580    83 GGYPyrgKPVGIPTLEQVLRAFP-DTPFILDMKSLPADPQA-KAVARVLERENaWSRVRIYSTN 144
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 33-234 2.65e-25

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: 101.97  E-value: 2.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGA------SAYA--PENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTV-----DRTTNGSGH-----IREL 94
Cdd:cd08572     3 IGHRGLgknyasGSLAgiRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTIsvsekSKTGSDEGElievpIHDL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  95 TYAELQRL----------DAGSWKGDSFTNEK--------IPTLSQVLDEFQGKIGILIELKAPEL--YPGIEKKVAFEI 154
Cdd:cd08572    83 TLEQLKELglqhisalkrKALTRKAKGPKPNPwgmdehdpFPTLQEVLEQVPKDLGFNIEIKYPQLleDGEGELTPYFER 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 155 N-------KRQLDH-----VIIQSFN--VSSM--KKMHELlpnvPIGILTSSQRDASP------NSIQQFAAFATYFN-- 210
Cdd:cd08572   163 NafvdtilAVVFEHaggrrIIFSSFDpdICIMlrLKQNKY----PVLFLTNGGTNEVEhmdprrRSLQAAVNFALAEGll 238

                         250       260
                  ....*....|....*....|....*....
gi 1267979542 211 ----PSYDIL-TPALIHQVHSAGMKISPW 234
Cdd:cd08572   239 gvvlHAEDLLkNPSLISLVKALGLVLFTY 267
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 33-125 2.91e-25

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: 100.84  E-value: 2.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTN------GSGHIRE--LTYAELQRLDA 104
Cdd:cd08574     5 IGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNvadvfpERAHERAsmFTWTDLQQLNA 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1267979542 105 GSW--KGDSF--------------TNEKIPTLSQVLD 125
Cdd:cd08574    85 GQWflKDDPFwtasslsesdreeaGNQSIPSLAELLR 121
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 32-140 1.45e-21

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: 91.59  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  32 NIAHRG-------ASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRT----VDRTTNGSGH------IREL 94
Cdd:cd08607     2 DVGHRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTlrvsLKSKGDSDRDdllevpVKDL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1267979542  95 TYAELQRLD-------AGSWKGDSFTNEKI------PTLSQVLDEFQGKIGILIELKAP 140
Cdd:cd08607    82 TYEQLKLLKlfhisalKVKEYKSVEEDEDPpehqpfPTLSDVLESVPEDVGFNIEIKWP 140
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 32-257 2.12e-20

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: 85.95  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  32 NIAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGsghIRELTYAELQRLDAGSWKGDS 111
Cdd:cd08555     1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAG---ILPPTLEEVLELIADYLKNPD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 112 FTnekiptlsqvldefqgkIGILIELKAPEL-YPGIEKKVAFEINKRQ----LDHVIIQSFNVSSmkkmhellpnvpigi 186
Cdd:cd08555    78 YT-----------------IILSLEIKQDSPeYDEFLAKVLKELRVYFdydlRGKVVLSSFNALG--------------- 125

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267979542 187 ltssqrdaspnsiqqfaafATYFNPSYD-ILTPALIHQVHSAGMKISPW-SGTKRLPASFLWKTKSDGVITNY 257
Cdd:cd08555   126 -------------------VDYYNFSSKlIKDTELIASANKLGLLSRIWtVNDNNEIINKFLNLGVDGLITDF 179
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 33-140 3.06e-20

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: 88.44  E-value: 3.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTN--------GSGHIRELTYAELQRLDA 104
Cdd:cd08609    30 VGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNvkdvfpgrDAAGSNNFTWTELKTLNA 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1267979542 105 GSW--KGDSF--------------TNEKIPTLSQVLDEFQG-KIGILIELKAP 140
Cdd:cd08609   110 GSWflERRPFwtlsslseedrreaDNQTVPSLSELLDLAKKhNVSIMFDLRNE 162
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 44-146 1.59e-18

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: 83.56  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  44 ENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTYAELQRLDAG----SWKGDSFTNE---- 115
Cdd:cd08613    60 ENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELKTLDIGygytADGGKTFPFRgkgv 139

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1267979542 116 -KIPTLSQVLDEFQGKiGILIELKAPELYPGI 146
Cdd:cd08613   140 gMMPTLDEVFAAFPDR-RFLINFKSDDAAEGE 170
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 33-112 6.47e-17

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: 79.50  E-value: 6.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRELTY--------AELQRLDA 104
Cdd:cd08608     5 IGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYedasmfnwTDLERLNA 84

                          90
                  ....*....|
gi 1267979542 105 GSW--KGDSF 112
Cdd:cd08608    85 GQWflKDDPF 94
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 29-210 4.77e-16

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: 76.84  E-value: 4.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  29 KLTNIAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNgsghIREL------------TY 96
Cdd:cd08610    22 KPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTN----IGEVqpesacenpaffNW 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  97 AELQRLDAGSW--KGDSFT--------------NEKIPTLSQVLD--EFQGKIGILIELKAPELYP-------------- 144
Cdd:cd08610    98 DFLSTLNAGKWfvKPRPFYnmkplseadkerarNQSIPKLSNFLRlaEKENKLVIFDLYRPPPKHPyrhtwirrvlevil 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267979542 145 ---GIEKKVAF--EINKRQLDHVIIQSFN--VSSMKKMHELLPNvPIGILTSSQRDASPNSIQQFAAFATYFN 210
Cdd:cd08610   178 nevGIEQHLVLwlPAHDRQYVQSVAPGFKqhVGRKVPIETLLKN-NISILNLAYKKLFSNDIRDYKAANIHTN 249
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 33-200 7.67e-14

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: 70.13  E-value: 7.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRG------------ASAYApENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNG---SGHIRELTYA 97
Cdd:cd08605     3 IGHRGlgmnrashqpsvGPGIR-ENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVERGGeveSSRIRDLTLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  98 ELQRL--DAGS-------------------WKGDsfTNEKIPTLSQVLDEFQGKIGILIELK------------APELYP 144
Cdd:cd08605    82 ELKALgpQAEStktstvalyrkakdpepepWIMD--VEDSIPTLEEVFSEVPPSLGFNIELKfgddnkteaeelVRELRA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 145 GIEkkVAFEINKRQldHVIIQSFNVSSMKKMHELLPNVPIGILT----SSQRDASPNSIQ 200
Cdd:cd08605   160 ILA--VCKQHAPGR--RIMFSSFDPDAAVLLRALQSLYPVMFLTdcgpYTHNDPRRNSIE 215
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 33-229 2.45e-11

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: 62.85  E-value: 2.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAP--------ENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRT-TNGSGHirELTyaELQRLD 103
Cdd:cd08606     5 IGHRGLGKNTAerkslqlgENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETgTDVPIH--DLT--LEQFLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 104 AG-----------SWKGDS---FTNEKIPTLSQVLDEFQGKIGILIELKAPELYPGIEKK---VAFEIN----------- 155
Cdd:cd08606    81 LSrmkytvdfkkkGFKGNSrghSIQAPFTTLEELLKKLPKSVGFNIELKYPMLHEAEEEEvapVAIELNafvdtvlekvf 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 156 ----KRQldhVIIQSFN-----VSSMKKmhellPNVPIGILTSS----QRDASPNSIQQFAAFATYFN-------PSYDI 215
Cdd:cd08606   161 dygaGRN---IIFSSFTpdiciLLSLKQ-----PGYPVLFLTEAgkapDMDVRAASLQEAIRFAKQWNllglvsaAEPLV 232

                         250
                  ....*....|....
gi 1267979542 216 LTPALIHQVHSAGM 229
Cdd:cd08606   233 MCPRLIQVVKRSGL 246
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 33-175 5.19e-08

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: 53.06  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTN------------------GSGHIR-E 93
Cdd:cd08571     4 IARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTiasvfpkrkktyvvegqsTSGIFSfD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  94 LTYAELQ--RLDAGSWKGDSFTN------EKIPTLSQVLDefQGKI----GILIELKAPELY-----PGIEKKVAFEINK 156
Cdd:cd08571    84 LTWAEIQtlKPIISNPFSVLFRNprndnaGKILTLEDFLT--LAKPkslsGVWINVENAAFLaehkgLLSVDAVLTSLSK 161

                         170       180
                  ....*....|....*....|...
gi 1267979542 157 RQLDH----VIIQSFNVSSMKKM 175
Cdd:cd08571   162 AGYDQtakkVYISSPDSSVLKSF 184
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 33-207 1.11e-07

Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 2 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play important an role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This CD includes domain II (the second GDPD domain of SHV3 and SVLs), which is necessary for SHV3 function.


Pssm-ID: 176546  Cd Length: 300  Bit Score: 51.95  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRTTNGSGHIRE------------------- 93
Cdd:cd08604     4 ISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSKFSnrattvpeigstsgiftfd 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  94 LTYAELQRL---------DAGSWKGDSFTN-EKIPTLSQVLDEFQGK--IGILIELK-APELYP----GIEKKVAFEINK 156
Cdd:cd08604    84 LTWSEIQTLkpaisnpysVTGLFRNPANKNaGKFLTLSDFLDLAKNKslSGVLINVEnAAYLAEkkglDVVDAVLDALTN 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1267979542 157 RQLDH-----VIIQSFNVSSMKKMHELLPNVPIGILTSSQRDASPNSIQQFAAFAT 207
Cdd:cd08604   164 AGYDNqtaqkVLIQSTDSSVLAAFKKQISYERVYVVDETIRDASDSSIEEIKKFAD 219
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 33-86 1.48e-05

Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic phosphodiesterase (GlpQ) include uncharacterized proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and their hypothetical homologs. Members in this subfamily show high sequence similarity to Escherichia coli periplasmic phosphodiesterase GlpQ, which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176503  Cd Length: 356  Bit Score: 45.88  E-value: 1.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1267979542  33 IAHRGASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRT-VDRTTN 86
Cdd:cd08560    20 IGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSQCdLHTTTN 74
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 33-228 1.96e-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: 41.90  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542  33 IAHR--GASAYAPENTMAAFHQALEMNADYIELDVQQSKDGVLVIMHDRTVDRT-TNGSGHIReltyaelqrlDAGSWKG 109
Cdd:cd08583     2 IAHAmgGIDGKTYTNSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHSWDESLLkQLGLPTSK----------NTKPLSY 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267979542 110 DSFTNEKI----PTLSqvldefqgkIGILIEL--KAPELYPGIEKK----------------VAFEINKRQLDHVIIQSF 167
Cdd:cd08583    72 EEFKSKKIygkyTPMD---------FKDVIDLlkKYPDVYIVTDTKqdddndikklyeyivkEAKEVDPDLLDRVIPQIY 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267979542 168 NvssmKKMHELLPNV---PIGILTSSQRDasPNSIQQFAAFA-----TYFNPSYDILTPALIHQVHSAG 228
Cdd:cd08583   143 N----EEMYEAIMSIypfKSVIYTLYRQD--SIRLDEIIAFCyengiKAVTISKNYVNDKLIEKLNKAG 205
 
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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