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Conserved domains on  [gi|18396047|ref|NP_566159|]
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senescence-related gene 3 [Arabidopsis thaliana]

Protein Classification

PI-PLC domain-containing protein( domain architecture ID 49489)

PI-PLC (phosphoinositide-specific phospholipase C) domain-containing protein may hydrolyze the membrane lipid phosphatidylinositol to produce phosphorylated myo-inositol and diacylglycerol

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_GDPD_SF super family cl14615
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 35-316 2.62e-140

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.


The actual alignment was detected with superfamily member cd08605:

Pssm-ID: 472694 [Multi-domain]  Cd Length: 282  Bit Score: 399.48  E-value: 2.62e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  35 VVVGHRGHGMNMSQSPDLRFSALKENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIYSEEQGVVYEKRVTEVCL 114
Cdd:cd08605   1 AVIGHRGLGMNRASHQPSVGPGIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVERGGEVESSRIRDLTL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 115 SEFMSYGPQRDTGKTGK-PLLRKSKEGKIHKWSVATDDSFCTLQEAFEKVEnPNLGFNIELKLDDNVFYSSDHLSRLLLP 193
Cdd:cd08605  81 AELKALGPQAESTKTSTvALYRKAKDPEPEPWIMDVEDSIPTLEEVFSEVP-PSLGFNIELKFGDDNKTEAEELVRELRA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 194 ILQVVSDIGNDRTIIFSSFHPDAALLVRKLQTTYPVFFLTNGGTEMYHDTRRNSLEEAIKVCLEGGLQGIVSEVKGVFRN 273
Cdd:cd08605 160 ILAVCKQHAPGRRIMFSSFDPDAAVLLRALQSLYPVMFLTDCGPYTHNDPRRNSIEAAIQVALEGGLQGIVSEVKVLLRN 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 18396047 274 PALVNKIKESKLSLMTYGKLNNVAEAVYMQHLMGIEGVIVDHV 316
Cdd:cd08605 240 PTAVSLVKASGLELGTYGKLNNDAEAVERQADLGVDGVIVDHV 282
 
Name Accession Description Interval E-value
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 35-316 2.62e-140

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: 399.48  E-value: 2.62e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  35 VVVGHRGHGMNMSQSPDLRFSALKENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIYSEEQGVVYEKRVTEVCL 114
Cdd:cd08605   1 AVIGHRGLGMNRASHQPSVGPGIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVERGGEVESSRIRDLTL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 115 SEFMSYGPQRDTGKTGK-PLLRKSKEGKIHKWSVATDDSFCTLQEAFEKVEnPNLGFNIELKLDDNVFYSSDHLSRLLLP 193
Cdd:cd08605  81 AELKALGPQAESTKTSTvALYRKAKDPEPEPWIMDVEDSIPTLEEVFSEVP-PSLGFNIELKFGDDNKTEAEELVRELRA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 194 ILQVVSDIGNDRTIIFSSFHPDAALLVRKLQTTYPVFFLTNGGTEMYHDTRRNSLEEAIKVCLEGGLQGIVSEVKGVFRN 273
Cdd:cd08605 160 ILAVCKQHAPGRRIMFSSFDPDAAVLLRALQSLYPVMFLTDCGPYTHNDPRRNSIEAAIQVALEGGLQGIVSEVKVLLRN 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 18396047 274 PALVNKIKESKLSLMTYGKLNNVAEAVYMQHLMGIEGVIVDHV 316
Cdd:cd08605 240 PTAVSLVKASGLELGTYGKLNNDAEAVERQADLGVDGVIVDHV 282
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 39-318 3.03e-56

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: 183.76  E-value: 3.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047    39 HRGHGMNMSqspdlrfsalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIYSEEQGVVYekrVTEVCLSEFM 118
Cdd:pfam03009   1 HRGASGSYP-----------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGY---VRDLTLEELK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047   119 SYgpqrdtgKTGKPLLRKSKEGKIHkwsvatddsFCTLQEAFEKveNPNLGFNIELKLDDNVFYSSDHLSRLLLPILQVV 198
Cdd:pfam03009  67 RL-------DIGAGNSGPLSGERVP---------FPTLEEVLEF--DWDVGFNIEIKIKPYVEAIAPEEGLIVKDLLLSV 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047   199 SDIG----NDRTIIFSSFHPDAALLVRKLQTTYPVFFLTNGGTEMYHDtrrnSLEEAIKVCLEGGLQGIVSEVkgVFRNP 274
Cdd:pfam03009 129 DEILakkaDPRRVIFSSFNPDELKRLRELAPKLPLVFLSSGRAYAEAD----LLERAAAFAGAPALLGEVALV--DEALP 202

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 18396047   275 ALVNKIKESKLSLMTYGKLNNvaEAVYMQHLMGIEGVIVDHVEE 318
Cdd:pfam03009 203 DLVKRAHARGLVVHVWTVNNE--DEMKRLLELGVDGVITDRPDT 244
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
32-325 3.82e-29

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 112.65  E-value: 3.82e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  32 NKFVVVGHRGhgmnmsqspdlrFSALK-ENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIyseeqgvvyeKRVT 110
Cdd:COG0584   1 PRPLIIAHRG------------ASGLApENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTL----------DRTT 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 111 EVclsefmsygpqrdTGKTGK-PL--LRKSKEGKIHKWsvaTDDSFCTLQEAFEKVEnPNLGFNIELKLDDnvfyssDHL 187
Cdd:COG0584  59 NG-------------TGRVADlTLaeLRQLDAGSGPDF---AGERIPTLEEVLELVP-GDVGLNIEIKSPP------AAE 115

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 188 SRLLLPILQVVSDIGNDRTIIFSSFHPDAALLVRKLQTTYPVFFLTnggtemyhdtrRNSLEEAIKVCLEGGLQGIVSEV 267
Cdd:COG0584 116 PDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLV-----------EELPADPLELARALGADGVGPDY 184

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 268 KGVfrNPALVNKIKESKLSLMTYGkLNNVAEavyMQHL--MGIEGVIVDHVEEITEAVRE 325
Cdd:COG0584 185 DLL--TPELVAAAHAAGLKVHVWT-VNDPEE---MRRLldLGVDGIITDRPDLLRAVLRE 238
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 36-94 1.57e-03

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 39.54  E-value: 1.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18396047   36 VVGHRGHGmnmSQSPdlrfsalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDD 94
Cdd:PRK09454  10 IVAHRGGG---KLAP--------ENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDD 57
 
Name Accession Description Interval E-value
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 35-316 2.62e-140

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: 399.48  E-value: 2.62e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  35 VVVGHRGHGMNMSQSPDLRFSALKENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIYSEEQGVVYEKRVTEVCL 114
Cdd:cd08605   1 AVIGHRGLGMNRASHQPSVGPGIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVERGGEVESSRIRDLTL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 115 SEFMSYGPQRDTGKTGK-PLLRKSKEGKIHKWSVATDDSFCTLQEAFEKVEnPNLGFNIELKLDDNVFYSSDHLSRLLLP 193
Cdd:cd08605  81 AELKALGPQAESTKTSTvALYRKAKDPEPEPWIMDVEDSIPTLEEVFSEVP-PSLGFNIELKFGDDNKTEAEELVRELRA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 194 ILQVVSDIGNDRTIIFSSFHPDAALLVRKLQTTYPVFFLTNGGTEMYHDTRRNSLEEAIKVCLEGGLQGIVSEVKGVFRN 273
Cdd:cd08605 160 ILAVCKQHAPGRRIMFSSFDPDAAVLLRALQSLYPVMFLTDCGPYTHNDPRRNSIEAAIQVALEGGLQGIVSEVKVLLRN 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 18396047 274 PALVNKIKESKLSLMTYGKLNNVAEAVYMQHLMGIEGVIVDHV 316
Cdd:cd08605 240 PTAVSLVKASGLELGTYGKLNNDAEAVERQADLGVDGVIVDHV 282
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 35-316 9.13e-101

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: 299.58  E-value: 9.13e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  35 VVVGHRGHGMNMSQSPDLrfsALKENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIYSEEQ-------GVVYEK 107
Cdd:cd08572   1 LVIGHRGLGKNYASGSLA---GIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKsktgsdeGELIEV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 108 RVTEVCLSEFMSYGPQRDTGKTGKPLLRKSKEGKIHKWSVATDDSFCTLQEAFEKVeNPNLGFNIELKLDDNVFYSSDHL 187
Cdd:cd08572  78 PIHDLTLEQLKELGLQHISALKRKALTRKAKGPKPNPWGMDEHDPFPTLQEVLEQV-PKDLGFNIEIKYPQLLEDGEGEL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 188 S------RLLLPILQVVSDIGNDRTIIFSSFHPDAALLVRKLQTTYPVFFLTNGGTEMYH--DTRRNSLEEAIKVCLEGG 259
Cdd:cd08572 157 TpyfernAFVDTILAVVFEHAGGRRIIFSSFDPDICIMLRLKQNKYPVLFLTNGGTNEVEhmDPRRRSLQAAVNFALAEG 236

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18396047 260 LQGIVSEVKGVFRNPALVNKIKESKLSLMTYGKLNNVAEAVYMQHLMGIEGVIVDHV 316
Cdd:cd08572 237 LLGVVLHAEDLLKNPSLISLVKALGLVLFTYGDDNNDPENVKKQKELGVDGVIYDRV 293
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 39-318 3.03e-56

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: 183.76  E-value: 3.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047    39 HRGHGMNMSqspdlrfsalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIYSEEQGVVYekrVTEVCLSEFM 118
Cdd:pfam03009   1 HRGASGSYP-----------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGY---VRDLTLEELK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047   119 SYgpqrdtgKTGKPLLRKSKEGKIHkwsvatddsFCTLQEAFEKveNPNLGFNIELKLDDNVFYSSDHLSRLLLPILQVV 198
Cdd:pfam03009  67 RL-------DIGAGNSGPLSGERVP---------FPTLEEVLEF--DWDVGFNIEIKIKPYVEAIAPEEGLIVKDLLLSV 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047   199 SDIG----NDRTIIFSSFHPDAALLVRKLQTTYPVFFLTNGGTEMYHDtrrnSLEEAIKVCLEGGLQGIVSEVkgVFRNP 274
Cdd:pfam03009 129 DEILakkaDPRRVIFSSFNPDELKRLRELAPKLPLVFLSSGRAYAEAD----LLERAAAFAGAPALLGEVALV--DEALP 202

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 18396047   275 ALVNKIKESKLSLMTYGKLNNvaEAVYMQHLMGIEGVIVDHVEE 318
Cdd:pfam03009 203 DLVKRAHARGLVVHVWTVNNE--DEMKRLLELGVDGVITDRPDT 244
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 36-325 2.03e-55

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: 183.03  E-value: 2.03e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  36 VVGHRGHGMNMSQSPDLRfsaLKENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDdFIYSEeQGVvyEKRVTEVCLS 115
Cdd:cd08606   4 VIGHRGLGKNTAERKSLQ---LGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHD-FLVSE-TGT--DVPIHDLTLE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 116 EFMSYGPQRDTgktgKPLLRKSKEGKIHKWSVAtdDSFCTLQEAFEKVEnPNLGFNIELK----------------LDDN 179
Cdd:cd08606  77 QFLHLSRMKYT----VDFKKKGFKGNSRGHSIQ--APFTTLEELLKKLP-KSVGFNIELKypmlheaeeeevapvaIELN 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 180 VFYSSdhlsrlllpILQVVSDIGNDRTIIFSSFHPDAALLVRKLQTTYPVFFLTNGGTEMYHDTRRNSLEEAIKVCLEGG 259
Cdd:cd08606 150 AFVDT---------VLEKVFDYGAGRNIIFSSFTPDICILLSLKQPGYPVLFLTEAGKAPDMDVRAASLQEAIRFAKQWN 220

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18396047 260 LQGIVSEVKGVFRNPALVNKIKESKLSLMTYGKLNNVAEAVYMQHLMGIEGVIVDHVEEITEAVRE 325
Cdd:cd08606 221 LLGLVSAAEPLVMCPRLIQVVKRSGLVCVSYGVLNNDPENAKTQVKAGVDAVIVDSVLAIRRGLTE 286
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 37-316 4.30e-42

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: 148.21  E-value: 4.30e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  37 VGHRGHGMNMSQSPDlrfsALKENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIY--SEEQGVVYEKRVTEVCL 114
Cdd:cd08607   3 VGHRGAGNSYTAASA----VVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRvsLKSKGDSDRDDLLEVPV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 115 SEFmSYgpqrDTGKTGKPLLRKSKEGKIHKWSVATDDS-----FCTLQEAFEKVeNPNLGFNIELK----LDDNVFySSD 185
Cdd:cd08607  79 KDL-TY----EQLKLLKLFHISALKVKEYKSVEEDEDPpehqpFPTLSDVLESV-PEDVGFNIEIKwpqqQKDGSW-ESE 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 186 HLSRL-----LLPILQVVSDIGNDRTIIFSSFHPDAALLVRKLQTTYPVFFLTNGGTEMYH---DTRRNSLEEAIKVCLE 257
Cdd:cd08607 152 LFTYFdrnlfVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPefmDLRTRTFEIAVNFAQA 231

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18396047 258 GGLQGIVSEVKGVFRNPALVNKIKESKLSLMTYGKLNNVAEAVYMQHLMGIEGVIVDHV 316
Cdd:cd08607 232 EELLGVNLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDRI 290
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
32-325 3.82e-29

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 112.65  E-value: 3.82e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  32 NKFVVVGHRGhgmnmsqspdlrFSALK-ENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIyseeqgvvyeKRVT 110
Cdd:COG0584   1 PRPLIIAHRG------------ASGLApENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTL----------DRTT 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 111 EVclsefmsygpqrdTGKTGK-PL--LRKSKEGKIHKWsvaTDDSFCTLQEAFEKVEnPNLGFNIELKLDDnvfyssDHL 187
Cdd:COG0584  59 NG-------------TGRVADlTLaeLRQLDAGSGPDF---AGERIPTLEEVLELVP-GDVGLNIEIKSPP------AAE 115

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 188 SRLLLPILQVVSDIGNDRTIIFSSFHPDAALLVRKLQTTYPVFFLTnggtemyhdtrRNSLEEAIKVCLEGGLQGIVSEV 267
Cdd:COG0584 116 PDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLV-----------EELPADPLELARALGADGVGPDY 184

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 268 KGVfrNPALVNKIKESKLSLMTYGkLNNVAEavyMQHL--MGIEGVIVDHVEEITEAVRE 325
Cdd:COG0584 185 DLL--TPELVAAAHAAGLKVHVWT-VNDPEE---MRRLldLGVDGIITDRPDLLRAVLRE 238
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 36-315 1.14e-23

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: 96.56  E-value: 1.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  36 VVGHRGHGMnmsQSPdlrfsalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDdfiyseeqgvvyekrvtevcls 115
Cdd:cd08556   1 IIAHRGASG---EAP--------ENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD---------------------- 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 116 efmsygpqrdtgktgkpllrkskegkihkwsvatddsFCTLQEAFEKVENpNLGFNIELKlddnvfySSDHLSRLLLPIL 195
Cdd:cd08556  48 -------------------------------------IPTLEEVLELVKG-GVGLNIELK-------EPTRYPGLEAKVA 82

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 196 QVVSDIGNDRTIIFSSFHPDAALLVRKLQTTYPVFFLTnggtemyhdTRRNSLEEAIKVCLEGGLQGIVSEVKGVfrNPA 275
Cdd:cd08556  83 ELLREYGLEERVVVSSFDHEALRALKELDPEVPTGLLV---------DKPPLDPLLAELARALGADAVNPHYKLL--TPE 151

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 18396047 276 LVNKIKESKLSLMTYGkLNNVAEAVYMQHlMGIEGVIVDH 315
Cdd:cd08556 152 LVRAAHAAGLKVYVWT-VNDPEDARRLLA-LGVDGIITDD 189
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 36-314 1.51e-17

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: 80.68  E-value: 1.51e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  36 VVGHRGhgmNMSQSPdlrfsalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIY--SEEQGVVYEKRVTEvc 113
Cdd:cd08563   3 IFAHRG---YSGTAP--------ENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDrtTNGKGYVKDLTLEE-- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 114 lsefmsygpqrdtgktgkplLRKSKEGKIHKWSVaTDDSFCTLQEAFEKVENPNLGFNIELKldDNVFyssdHLSRLLLP 193
Cdd:cd08563  70 --------------------LKKLDAGSWFDEKF-TGEKIPTLEEVLDLLKDKDLLLNIEIK--TDVI----HYPGIEKK 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 194 ILQVVSDIGNDRTIIFSSFHPDAALLVRKLQTTYPVFFLTNGGTEmyhdtrrNSLEEAIKVCLEgglqGIVSEVKgvFRN 273
Cdd:cd08563 123 VLELVKEYNLEDRVIFSSFNHESLKRLKKLDPKIKLALLYETGLQ-------DPKDYAKKIGAD----SLHPDFK--LLT 189

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 18396047 274 PALVNKIKESKLSLMTYgklnNVAEAVYMQHLM--GIEGVIVD 314
Cdd:cd08563 190 EEVVEELKKRGIPVRLW----TVNEEEDMKRLKdlGVDGIITN 228
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 36-314 1.80e-14

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: 71.87  E-value: 1.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  36 VVGHRGHGmnmSQSPdlrfsalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFI--YSEEQGVVYEKRVTEVC 113
Cdd:cd08562   1 IIAHRGAS---SLAP--------ENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLdrTTNGSGAVTELTWAELA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 114 LSEFMS-YGPQRdtgkTGKPLLrkskegkihkwsvatddsfcTLQEAFEKVENPNLGFNIELKLDdnvfysSDHLSRLLL 192
Cdd:cd08562  70 QLDAGSwFSPEF----AGEPIP--------------------TLADVLELARELGLGLNLEIKPD------PGDEALTAR 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 193 PILQVVSDIGNDRT-IIFSSFHPDAALLVRKLQTTYPVFFLtnggtemYHDTRRNSLEEAIKVclegGLQGIVSEVKGVf 271
Cdd:cd08562 120 VVAAALRELWPHASkLLLSSFSLEALRAARRAAPELPLGLL-------FDTLPADWLELLAAL----GAVSIHLNYRGL- 187

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 18396047 272 rNPALVNKIKESKLSLMTYgKLNNVAEAVYMQHlMGIEGVIVD 314
Cdd:cd08562 188 -TEEQVKALKDAGYKLLVY-TVNDPARAAELLE-WGVDAIFTD 227
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 35-319 1.40e-12

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: 66.55  E-value: 1.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  35 VVVGHRGhgmnmsqspdlrFSAL-KENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIySEEQGVVYekRVTEVC 113
Cdd:cd08568   1 IILGHRG------------YRAKyPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENL-KRVGGVDL--KVKELT 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 114 LSEFMSYGPQrdtgktGKPLlrkskegkihkwsvatddsfCTLQEAFEKVENPNLgFNIELKLDDNVfyssdhlsrllLP 193
Cdd:cd08568  66 YKELKKLHPG------GELI--------------------PTLEEVFRALPNDAI-INVEIKDIDAV-----------EP 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 194 ILQVVSDIGNDRTIIFSSFHPDAALLVRKLQTTYPVFFLTNGGTEMYHDTRRNSLEEAIKVCLEGGLQGIVSEVKGVfrn 273
Cdd:cd08568 108 VLEIVEKFNALDRVIFSSFNHDALRELRKLDPDAKVGLLIGEEEEGFSIPELHEKLKLYSLHVPIDAIGYIGFEKFV--- 184

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 18396047 274 pALVNKIKES--KLSLMTYGKLNNVAEavymqhLMG-IEGVIVDHVEEI 319
Cdd:cd08568 185 -ELLRLLRKLglKIVLWTVNDPELVPK------LKGlVDGVITDDVEKI 226
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 59-213 7.56e-12

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: 64.93  E-value: 7.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  59 ENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIYS--EEQGVVYEKRVTEvcLSEFM-SYGPQRDTGKTGKPllR 135
Cdd:cd08575  15 ENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRltGGSGLVSDLTYAE--LPPLDaGYGYTFDGGKTGYP--R 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18396047 136 KSKEGKIhkwsvatddsfCTLQEAFEKVenPNLGFNIELKlddnvfysSDHLSRLLLPILQVVSDIG-NDRTIIFSSFH 213
Cdd:cd08575  91 GGGDGRI-----------PTLEEVFKAF--PDTPINIDIK--------SPDAEELIAAVLDLLEKYKrEDRTVWGSTNP 148
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 36-302 1.55e-11

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity 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: 63.49  E-value: 1.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  36 VVGHRGhgmNMSQSPdlrfsalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIYSEEQGvvyEKRVTEVCLS 115
Cdd:cd08582   1 VIAHRG---ASAEAP--------ENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGG---DGAVSDLTLA 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 116 EfmsygpqrdtgktgkplLRKSKEGKIHKWSVAtDDSFCTLQEAFEKVENPNLGFNIELKLDDNVfyssdhlSRLLLPIL 195
Cdd:cd08582  67 E-----------------LRKLDIGSWKGESYK-GEKVPTLEEYLAIVPKYGKKLFIEIKHPRRG-------PEAEEELL 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 196 QVVSDIGNDR---TIIfsSFHPDAALLVRKLQTTYPVFFLTNG--GTEMYHDTRRNSLEEAIKVCLEGGLqgivsevkgv 270
Cdd:cd08582 122 KLLKESGLLPeqiVII--SFDAEALKRVRELAPTLETLWLRNYksPKEDPRPLAKSGGAAGLDLSYEKKL---------- 189

                       250       260       270
                ....*....|....*....|....*....|..
gi 18396047 271 frNPALVNKIKESKLSLMTYgKLNNVAEAVYM 302
Cdd:cd08582 190 --NPAFIKALRDAGLKLNVW-TVDDAEDAKRL 218
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 36-229 1.41e-09

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: 57.73  E-value: 1.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  36 VVGHRGhgmNMSQSPdlrfsalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFI--YSEEQGVVYEkrVTEVC 113
Cdd:cd08581   1 LVAHRG---YPARYP--------ENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLlrLTGVEGLLHE--LEDAE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 114 LSEFMSYGPQRdTGKtgkpllrkskegKIHKWSVATDDSFCTLQEafekvENPNLGFNIELKLDdnvfySSDH--LSRLL 191
Cdd:cd08581  68 LDSLRVAEPAR-FGS------------RFAGEPLPSLAAVVQWLA-----QHPQVTLFVEIKTE-----SLDRfgLERVV 124

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 18396047 192 LPILQVVSDIGNDRTIIfsSFHPDAALLVRKlQTTYPV 229
Cdd:cd08581 125 DKVLRALPAVAAQRVLI--SFDYDLLALAKQ-QGGPRT 159
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 32-290 3.21e-09

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: 57.10  E-value: 3.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  32 NKFVVVGHRGHGMnmsqspDLRFSalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFH--------DDFIYSEEQGV 103
Cdd:cd08564   2 VRPIIVGHRGAGC------STLYP---ENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteddtnpDTSIQLDDSGF 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 104 vyeKRVTEVCLSEFMSYgpqrdtgKTGKPLLRKSKEGKIHKWSVATddsfcTLQEAFEKVEnPNLGFNIELKLDDNvfys 183
Cdd:cd08564  73 ---KNINDLSLDEITRL-------HFKQLFDEKPCGADEIKGEKIP-----TLEDVLVTFK-DKLKYNIELKGREV---- 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 184 sdhlsRLLLPILQVVSDIGNDRTIIFSSF-HPDAALLVRKL---QTTYPVFFLTNGGTEMyhdtrrnSLEEAIKVCLEGG 259
Cdd:cd08564 133 -----GLGERVLNLVEKYGMILQVHFSSFlHYDRLDLLKALrpnKLNVPIALLFNEVKSP-------SPLDFLEQAKYYN 200

                       250       260       270
                ....*....|....*....|....*....|.
gi 18396047 260 LQGIVseVKGVFRNPALVNKIKESKLSLMTY 290
Cdd:cd08564 201 ATWVN--FSYDFWTEEFVKKAHENGLKVMTY 229
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 36-94 8.38e-09

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: 55.73  E-value: 8.38e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18396047  36 VVGHRGHGMnmsQSPdlrfsalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDD 94
Cdd:cd08573   1 IIGHRGAGH---DAP--------ENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDD 48
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 36-223 1.56e-08

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: 54.72  E-value: 1.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  36 VVGHRGHGmnmsqspdlrfSALKENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIyseeqgvvyeKRVTEvcls 115
Cdd:cd08565   1 IAGHRGGR-----------NLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTL----------DRTTH---- 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 116 efmSYGPQRDTGktgkplLRKSKEGKIHKWsvaTDDSFCTLQEAFEKVENPNLGFNIELKLDDNVFYSSDHLSRlllpIL 195
Cdd:cd08565  56 ---GTGAVRDLT------LAERKALRLRDS---FGEKIPTLEEVLALFAPSGLELHVEIKTDADGTPYPGAAAL----AA 119

                       170       180
                ....*....|....*....|....*...
gi 18396047 196 QVVSDIGNDRTIIFSSFHPDAALLVRKL 223
Cdd:cd08565 120 ATLRRHGLLERSVLTSFDPAVLTEVRKH 147
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 35-94 6.51e-08

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: 52.69  E-value: 6.51e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18396047  35 VVVGHRG-HGMNMsqsPdlrfsalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDD 94
Cdd:cd08566   1 LVVAHRGgWGAGA---P--------ENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDD 50
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 59-179 1.89e-07

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: 51.01  E-value: 1.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  59 ENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIySEEQGVvyEKRVTEVCLSEFMSYgpqrdtgktgkpllrksk 138
Cdd:cd08579  13 ENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANL-KRLAGV--NKKVWDLTLEELKKL------------------ 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 18396047 139 egKIHKWSVATddSFCTLQEAFEKVENPNLGFNIELKLDDN 179
Cdd:cd08579  72 --TIGENGHGA--KIPSLDEYLALAKGLKQKLLIELKPHGH 108
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 59-248 2.11e-07

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of mammalian glycerophosphodiester phosphodiesterase GDE4; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial homologs of mammalian GDE4, a transmembrane protein whose cellular function has not been elucidated yet.


Pssm-ID: 176554 [Multi-domain]  Cd Length: 309  Bit Score: 51.98  E-value: 2.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  59 ENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHD---DFiYSEEQGVVYEKRVTEvcLSEF-MSYGPQRDTGKTgKPlL 134
Cdd:cd08613  60 ENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDwtlDC-RTDGSGVTRDHTMAE--LKTLdIGYGYTADGGKT-FP-F 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 135 RKSKEGKIHkwsvatddsfcTLQEAFEkvENPNLGFNIELKLDDNVFYS--SDHLSRLLLPILQVVSDIGNDRTI-IFSS 211
Cdd:cd08613 135 RGKGVGMMP-----------TLDEVFA--AFPDRRFLINFKSDDAAEGEllAEKLATLPRKRLQVLTVYGGDKPIaALRE 201

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 18396047 212 FHPDAALLVRKLQTTYPVFFLTNGGTEMYHDTRRNSL 248
Cdd:cd08613 202 LTPDLRTLSKASMKDCLIEYLALGWTGYVPDSCRNTT 238
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 37-94 4.06e-07

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity 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: 50.40  E-value: 4.06e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  37 VGHRG-HGMNmsqspdlrfSALKENSILSFNAASKfpLDF-IEFDVQVTRDGCPIIFHDD 94
Cdd:cd08585   7 IAHRGlHDRD---------AGIPENSLSAFRAAAE--AGYgIELDVQLTADGEVVVFHDD 55
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 36-93 4.53e-07

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: 50.30  E-value: 4.53e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18396047  36 VVGHRGhgmnmsqspdlrFSA-LKENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHD 93
Cdd:cd08570   1 VIGHRG------------YKAkYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHD 47
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 34-315 3.05e-06

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: 48.08  E-value: 3.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  34 FVVVGHRGhgmnmsqspdlrFSALK-ENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFI------------YSEE 100
Cdd:cd08567   1 FDLQGHRG------------ARGLLpENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLnpditrdpdgawLPYE 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 101 QGVVYEKRVTEVclsefmsygPQRDTGKTgKPLLRKSKEGKIHKwsVATDDSFCTLQEAFEKVE---NPNLGFNIELKLD 177
Cdd:cd08567  69 GPALYELTLAEI---------KQLDVGEK-RPGSDYAKLFPEQI--PVPGTRIPTLEEVFALVEkygNQKVRFNIETKSD 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 178 DNVFYSSDHLSRLLLPILQVVSDIG-NDRTIIFsSFHPDAALLVRKLQTTYPVFFLTNggtemyhDTRRNSLEEAIKvcl 256
Cdd:cd08567 137 PDRDILHPPPEEFVDAVLAVIRKAGlEDRVVLQ-SFDWRTLQEVRRLAPDIPTVALTE-------ETTLGNLPRAAK--- 205

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18396047 257 EGGLQGIVSEVKGVfrNPALVNKIKESKLSLMTYGkLNNVAEAVYMQHlMGIEGVIVDH 315
Cdd:cd08567 206 KLGADIWSPYFTLV--TKELVDEAHALGLKVVPWT-VNDPEDMARLID-LGVDGIITDY 260
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 59-223 6.18e-06

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: 46.87  E-value: 6.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  59 ENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFI--YSEEQGvvyekRVTEVCLSEFMSYgpqrDTGKTGKPLLRK 136
Cdd:cd08561  13 ENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLdrTTDGTG-----PVADLTLAELRRL----DAGYHFTDDGGR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 137 SKEGKIHKWSVAtddsfcTLQEAFEKVenPNLGFNIELKldDNVFYSSDhlsrlllPILQVVSDIG-NDRtIIFSSFHPD 215
Cdd:cd08561  84 TYPYRGQGIRIP------TLEELFEAF--PDVRLNIEIK--DDGPAAAA-------ALADLIERYGaQDR-VLVASFSDR 145


                ....*...
gi 18396047 216 AALLVRKL 223
Cdd:cd08561 146 VLRRFRRL 153
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 34-311 9.10e-06

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: 46.54  E-value: 9.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  34 FVVVGHRGHGMNmsqSPdlrfsalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIySEEQGVVYEKRVTEVC 113
Cdd:cd08601   1 NAVIAHRGASGY---AP--------EHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETL-DRTTNIERPGPVKDYT 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 114 LSEFMsygpQRDTG----KTGKPLLRKSKEG-KIHkwsvatddsfcTLQEAFEKVEnPNLGFNIELKLDDnvFYSSdhLS 188
Cdd:cd08601  69 LAEIK----QLDAGswfnKAYPEYARESYSGlKVP-----------TLEEVIERYG-GRANYYIETKSPD--LYPG--ME 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 189 RLLLPILQ----VVSDIGNDRTIIfSSFHPDAALLVRKLQTTYPVFFLTNGGT--EMYHDtrrnSLEEAIKVCLegglqG 262
Cdd:cd08601 129 EKLLATLDkyglLTDNLKNGQVII-QSFSKESLKKLHQLNPNIPLVQLLWYGEgaETYDK----WLDEIKEYAI-----G 198

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 18396047 263 IVSEVKGVfrNPALVNKIKESKLSLMTYgKLNNVAEavyMQHLM--GIEGV 311
Cdd:cd08601 199 IGPSIADA--DPWMVHLIHKKGLLVHPY-TVNEKAD---MIRLInwGVDGM 243
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 34-285 9.39e-06

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: 46.88  E-value: 9.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  34 FVVVGHRG-HGMnmsqspdlrfsaLKENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIySEEQGV--VYEKRVT 110
Cdd:cd08559   1 PLVIAHRGaSGY------------APEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTL-DRTTNVaeHFPFRGR 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 111 EVC--------LSEFM-----SYGPQRdtgktgKPLLRKSKEGkihKWSVATDDSFCTLQEAFEKVENPNLGFNIELKld 177
Cdd:cd08559  68 KDTgyfvidftLAELKtlragSWFNQR------YPERAPSYYG---GFKIPTLEEVIELAQGLNKSTGRNVGIYPETK-- 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 178 dnvfySSDHLSRLLLPILQVVSDI-------GNDRTIIFSSFHPDAALLVRKLQTTYPVFFLTNGGTEMYHDTRRNSLEE 250
Cdd:cd08559 137 -----HPTFHKQEGPDIEEKLLEVlkkygytGKNDPVFIQSFEPESLKRLRNETPDIPLVQLIDYGDWAETDKKYTYAWL 211

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 18396047 251 AIkvclEGGLQGIVSEVKGV---------------FRNPALVNKIKESKL 285
Cdd:cd08559 212 TT----DAGLKEIAKYADGIgpwksliipedsnglLVPTDLVKDAHKAGL 257
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 34-96 3.97e-05

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: 45.07  E-value: 3.97e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18396047  34 FVVVGHRGHgmnmsqspdlrfSA-LKENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFI 96
Cdd:cd08600   1 KIIIAHRGA------------SGyLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYL 52
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 33-94 5.24e-05

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: 44.22  E-value: 5.24e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18396047  33 KFVVVGHRGhgmnmsqSPDLRfsalKENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDD 94
Cdd:cd08574   1 KPALIGHRG-------APMLA----PENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDR 51
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 24-185 4.86e-04

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: 41.45  E-value: 4.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047  24 ICSSRKANNKFVVVGHRGHGMnmsQSPdlrfsalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDfiyseeqgv 103
Cdd:cd08609  17 IMEENNLPPKPALVGHRGAPM---LAP--------ENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDE--------- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396047 104 vYEKRVTEVclsefMSYGPQRDTGKTGKPLLRKSKEGKIHKWSV------------------ATDDSFCTLQEAFEKVEN 165
Cdd:cd08609  77 -GLLRTTNV-----KDVFPGRDAAGSNNFTWTELKTLNAGSWFLerrpfwtlsslseedrreADNQTVPSLSELLDLAKK 150

                       170       180
                ....*....|....*....|..
gi 18396047 166 PNLGFNIELKLDDN--VFYSSD 185
Cdd:cd08609 151 HNVSIMFDLRNENNshVFYSSF 172
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 36-94 1.57e-03

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 39.54  E-value: 1.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18396047   36 VVGHRGHGmnmSQSPdlrfsalkENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDD 94
Cdd:PRK09454  10 IVAHRGGG---KLAP--------ENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDD 57
 
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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