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Conserved domains on  [gi|33988692|gb|AAH02714|]
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Glycerophosphodiester phosphodiesterase domain containing 3 [Homo sapiens]

Protein Classification

glycerophosphodiester phosphodiesterase family protein( domain architecture ID 10171264)

glycerophosphodiester phosphodiesterase (GDPD) family protein similar to Homo sapiens lysophospholipase D GDPD1/GDE4 and GDPD3/GDE7, which hydrolyze lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines glycerophosphodiester phosphodiesterase 1

CATH:  3.20.20.190
EC:  3.1.4.-
Gene Ontology:  GO:0008081|GO:0006629|GO:0046872|GO:0004622
SCOP:  4000418

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 1-252 8.70e-135

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: 381.95  E-value: 8.70e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   1 MENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLEVYFSPGHF--AHGSDRRMVRLE 78
Cdd:cd08612  47 FEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYcvPKGSDRRIPLLE 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  79 DLFQRFPRTPMSVEIKGKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVLLSYYLGLL 158
Cdd:cd08612 127 EVFEAFPDTPINIDIKVENDELIKKVSDLVRKYKREDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLL 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 159 PFIPIPEKFFFCFLPNIINRTYFPFSCSCLNQLLAVVSKWLIMRKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGATGV 238
Cdd:cd08612 207 PFIPIKESFLEIPMPSIFLKTYFPKSMSRLNRFVLFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGV 286

                       250
                ....*....|....
gi 33988692 239 ITDYPTALRHYLDN 252
Cdd:cd08612 287 MTDYPTKLREFLDK 300
 
Name Accession Description Interval E-value
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 1-252 8.70e-135

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: 381.95  E-value: 8.70e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   1 MENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLEVYFSPGHF--AHGSDRRMVRLE 78
Cdd:cd08612  47 FEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYcvPKGSDRRIPLLE 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  79 DLFQRFPRTPMSVEIKGKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVLLSYYLGLL 158
Cdd:cd08612 127 EVFEAFPDTPINIDIKVENDELIKKVSDLVRKYKREDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLL 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 159 PFIPIPEKFFFCFLPNIINRTYFPFSCSCLNQLLAVVSKWLIMRKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGATGV 238
Cdd:cd08612 207 PFIPIKESFLEIPMPSIFLKTYFPKSMSRLNRFVLFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGV 286

                       250
                ....*....|....
gi 33988692 239 ITDYPTALRHYLDN 252
Cdd:cd08612 287 MTDYPTKLREFLDK 300
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
2-251 1.45e-31

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 116.51  E-value: 1.45e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   2 ENSMA-------QRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLplykEKLEVyfspGHFAHGSDRRM 74
Cdd:COG0584  17 ENTLAafraaleLGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAEL----RQLDA----GSGPDFAGERI 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  75 VRLEDLFQRFP-RTPMSVEIK---GKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVL 150
Cdd:COG0584  89 PTLEEVLELVPgDVGLNIEIKsppAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLVEELPADP 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 151 LSYYLGLLP-FIPIPekfffcflpniinrtyfpfscsclnqllavvskWLIMRKSLIRHLEERGVQVVFWCLNEESDFEA 229
Cdd:COG0584 169 LELARALGAdGVGPD---------------------------------YDLLTPELVAAAHAAGLKVHVWTVNDPEEMRR 215

                       250       260
                ....*....|....*....|..
gi 33988692 230 AFSVGATGVITDYPTALRHYLD 251
Cdd:COG0584 216 LLDLGVDGIITDRPDLLRAVLR 237
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 2-243 4.16e-19

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: 83.60  E-value: 4.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692     2 ENSMA-------QRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLE--VYFSPGHFahgsdr 72
Cdd:pfam03009  10 ENTLAsfrkaaeAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGnsGPLSGERV------ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692    73 RMVRLEDLFQRFPRTPMSVEIKGK---------NEELIREIAGLVRRYD----RNEITIWASEKSSVMKKCKAANPEMPL 139
Cdd:pfam03009  84 PFPTLEEVLEFDWDVGFNIEIKIKpyveaiapeEGLIVKDLLLSVDEILakkaDPRRVIFSSFNPDELKRLRELAPKLPL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   140 SFTISRGFWVLLSYYLGLLPFIPIPEkfffcflpniinrtyfpfscsclnqLLAVVSKWLIMRKSLIRHLEERGVQVVFW 219
Cdd:pfam03009 164 VFLSSGRAYAEADLLERAAAFAGAPA-------------------------LLGEVALVDEALPDLVKRAHARGLVVHVW 218

                         250       260
                  ....*....|....*....|....
gi 33988692   220 CLNEESDFEAAFSVGATGVITDYP 243
Cdd:pfam03009 219 TVNNEDEMKRLLELGVDGVITDRP 242
 
Name Accession Description Interval E-value
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 1-252 8.70e-135

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: 381.95  E-value: 8.70e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   1 MENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLEVYFSPGHF--AHGSDRRMVRLE 78
Cdd:cd08612  47 FEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYcvPKGSDRRIPLLE 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  79 DLFQRFPRTPMSVEIKGKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVLLSYYLGLL 158
Cdd:cd08612 127 EVFEAFPDTPINIDIKVENDELIKKVSDLVRKYKREDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLL 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 159 PFIPIPEKFFFCFLPNIINRTYFPFSCSCLNQLLAVVSKWLIMRKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGATGV 238
Cdd:cd08612 207 PFIPIKESFLEIPMPSIFLKTYFPKSMSRLNRFVLFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGV 286

                       250
                ....*....|....
gi 33988692 239 ITDYPTALRHYLDN 252
Cdd:cd08612 287 MTDYPTKLREFLDK 300
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 1-246 1.00e-97

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: 286.81  E-value: 1.00e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   1 MENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLEVYFSPG---HFAHGSDRRMVRL 77
Cdd:cd08575  21 FRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGYTFDGGktgYPRGGGDGRIPTL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  78 EDLFQRFPRTPMSVEIKGKN-EELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVLLS-YYL 155
Cdd:cd08575 101 EEVFKAFPDTPINIDIKSPDaEELIAAVLDLLEKYKREDRTVWGSTNPEYLRALHPENPNLFESFSMTRCLLLYLAlGYT 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 156 GLLPFIPIPEKFFFCFLPNIINRTYFPFSCsclnqllAVVSKWLIMRKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGA 235
Cdd:cd08575 181 GLLPFVPIKESFFEIPRPVIVLETFTLGEG-------ASIVAALLWWPNLFDHLRKRGIQVYLWVLNDEEDFEEAFDLGA 253

                       250
                ....*....|.
gi 33988692 236 TGVITDYPTAL 246
Cdd:cd08575 254 DGVMTDSPTKL 264
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
2-251 1.45e-31

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 116.51  E-value: 1.45e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   2 ENSMA-------QRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLplykEKLEVyfspGHFAHGSDRRM 74
Cdd:COG0584  17 ENTLAafraaleLGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAEL----RQLDA----GSGPDFAGERI 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  75 VRLEDLFQRFP-RTPMSVEIK---GKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVL 150
Cdd:COG0584  89 PTLEEVLELVPgDVGLNIEIKsppAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLVEELPADP 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 151 LSYYLGLLP-FIPIPekfffcflpniinrtyfpfscsclnqllavvskWLIMRKSLIRHLEERGVQVVFWCLNEESDFEA 229
Cdd:COG0584 169 LELARALGAdGVGPD---------------------------------YDLLTPELVAAAHAAGLKVHVWTVNDPEEMRR 215

                       250       260
                ....*....|....*....|..
gi 33988692 230 AFSVGATGVITDYPTALRHYLD 251
Cdd:COG0584 216 LLDLGVDGIITDRPDLLRAVLR 237
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 2-247 8.98e-31

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: 114.66  E-value: 8.98e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   2 ENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLplykEKLEV--YFSP--GHFA--HGSDRRMV 75
Cdd:cd08561  20 EDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAEL----RRLDAgyHFTDdgGRTYpyRGQGIRIP 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  76 RLEDLFQRFPRTPMSVEIKGKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVLLSYYL 155
Cdd:cd08561  96 TLEELFEAFPDVRLNIEIKDDGPAAAAALADLIERYGAQDRVLVASFSDRVLRRFRRLCPRVATSAGEGEVAAFVLASRL 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 156 GLLPFIPIPEKFFfcflpniinrtYFPFSCSCLNqllaVVSkwlimrKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGA 235
Cdd:cd08561 176 GLGSLYSPPYDAL-----------QIPVRYGGVP----LVT------PRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLGV 234

                       250
                ....*....|..
gi 33988692 236 TGVITDYPTALR 247
Cdd:cd08561 235 DGIITDRPDLLL 246
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 2-243 4.16e-19

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: 83.60  E-value: 4.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692     2 ENSMA-------QRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLE--VYFSPGHFahgsdr 72
Cdd:pfam03009  10 ENTLAsfrkaaeAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGnsGPLSGERV------ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692    73 RMVRLEDLFQRFPRTPMSVEIKGK---------NEELIREIAGLVRRYD----RNEITIWASEKSSVMKKCKAANPEMPL 139
Cdd:pfam03009  84 PFPTLEEVLEFDWDVGFNIEIKIKpyveaiapeEGLIVKDLLLSVDEILakkaDPRRVIFSSFNPDELKRLRELAPKLPL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   140 SFTISRGFWVLLSYYLGLLPFIPIPEkfffcflpniinrtyfpfscsclnqLLAVVSKWLIMRKSLIRHLEERGVQVVFW 219
Cdd:pfam03009 164 VFLSSGRAYAEADLLERAAAFAGAPA-------------------------LLGEVALVDEALPDLVKRAHARGLVVHVW 218

                         250       260
                  ....*....|....*....|....
gi 33988692   220 CLNEESDFEAAFSVGATGVITDYP 243
Cdd:pfam03009 219 TVNNEDEMKRLLELGVDGVITDRP 242
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 1-243 1.76e-18

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: 81.05  E-value: 1.76e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   1 MENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLplykEKLEVyfspghFAHGSDRRMVRLEDL 80
Cdd:cd08579  19 LEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEEL----KKLTI------GENGHGAKIPSLDEY 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  81 FQRF--PRTPMSVEIK---GKNEELIREiagLVRRYDRNEIT---IWASEKSSVMKKCKAANPEMPLSFtisrgfwvLLS 152
Cdd:cd08579  89 LALAkgLKQKLLIELKphgHDSPDLVEK---FVKLYKQNLIEnqhQVHSLDYRVIEKVKKLDPKIKTGY--------ILP 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 153 YYLGLLP-----FIPIPEkfffcflpniinrtyfpfscSCLNqllavvskwlimrKSLIRHLEERGVQVVFWCLNEESDF 227
Cdd:cd08579 158 FNIGNLPktnvdFYSIEY--------------------STLN-------------KEFIRQAHQNGKKVYVWTVNDPDDM 204

                       250
                ....*....|....*.
gi 33988692 228 EAAFSVGATGVITDYP 243
Cdd:cd08579 205 QRYLAMGVDGIITDYP 220
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 2-242 4.23e-17

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: 76.92  E-value: 4.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   2 ENSMA-------QRSDLLELDCQLTRDRVVVVSHDenlcrqsglnrdvgsldfedLPlykeklevyfspghfahgsdrrm 74
Cdd:cd08556  13 ENTLAafrkaleAGADGVELDVQLTKDGVLVVIHD--------------------IP----------------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  75 vRLEDLFQRFP-RTPMSVEIKG--KNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLsftisrgfwVLL 151
Cdd:cd08556  50 -TLEEVLELVKgGVGLNIELKEptRYPGLEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVPT---------GLL 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 152 SYYLGLLPFIPIPEKFFFCFlpniinrtyfpfscsclnqllAVVSKWLIMRKSLIRHLEERGVQVVFWCLNEESDFEAAF 231
Cdd:cd08556 120 VDKPPLDPLLAELARALGAD---------------------AVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLL 178

                       250
                ....*....|.
gi 33988692 232 SVGATGVITDY 242
Cdd:cd08556 179 ALGVDGIITDD 189
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 2-243 1.52e-14

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


Pssm-ID: 176512 [Multi-domain]  Cd Length: 234  Bit Score: 70.71  E-value: 1.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   2 ENSMA-------QRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDlplYKEKLEVYFSPghfahgsDRRM 74
Cdd:cd08570  13 ENTLLafekaveAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDSTWD---ELSHLRTIEEP-------HQPM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  75 VRLEDLFQRF-----PRTPMSVEIKGKN--EELIREIAGLVRRYdrNEITIWASEkssvmkkckaanpemplsftISRGF 147
Cdd:cd08570  83 PTLKDVLEWLvehelPDVKLMLDIKRDNdpEILFKLIAEMLAVK--PDLDFWRER--------------------IILGL 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 148 WVL--LSYYLGLLPFIPIpekffFCFLPNI-INRTYFPFSCSCLNQLLAVVSKWLIMRKSLIRHLEERGVQVVFWCLNEE 224
Cdd:cd08570 141 WHLdfLKYGKEVLPGFPV-----FHIGFSLdYARHFLNYSEKLVGISMHFVSLWGPFGQAFLPELKKNGKKVFVWTVNTE 215

                       250
                ....*....|....*....
gi 33988692 225 SDFEAAFSVGATGVITDYP 243
Cdd:cd08570 216 EDMRYAIRLGVDGVITDDP 234
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 2-243 1.69e-13

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: 67.58  E-value: 1.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   2 ENSMA-------QRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKeklevyFSPGHFAHGSDRRM 74
Cdd:cd08563  15 ENTLLafkkaieAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLD------AGSWFDEKFTGEKI 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  75 VRLEDLFQRFPRTPM--SVEIK---GKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPemplsftisrgfwv 149
Cdd:cd08563  89 PTLEEVLDLLKDKDLllNIEIKtdvIHYPGIEKKVLELVKEYNLEDRVIFSSFNHESLKRLKKLDP-------------- 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 150 llSYYLGLLpfipipekfFFCFLPNIINrtYFPFscsclNQLLAVVSKWLIMRKSLIRHLEERGVQVVFWCLNEESDFEA 229
Cdd:cd08563 155 --KIKLALL---------YETGLQDPKD--YAKK-----IGADSLHPDFKLLTEEVVEELKKRGIPVRLWTVNEEEDMKR 216

                       250
                ....*....|....
gi 33988692 230 AFSVGATGVITDYP 243
Cdd:cd08563 217 LKDLGVDGIITNYP 230
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 10-243 1.66e-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: 65.01  E-value: 1.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  10 DLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYkeklevyfspghfaHGSDRRMVRLEDLFQRFPRTP- 88
Cdd:cd08568  29 DGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKL--------------HPGGELIPTLEEVFRALPNDAi 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  89 MSVEIKGKneELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLSFTISrgfwvllSYYLGllpfipipekff 168
Cdd:cd08568  95 INVEIKDI--DAVEPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPDAKVGLLIG-------EEEEG------------ 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33988692 169 fcFLPNIINRTYFPFSCSCLNQLLAVVSKWLImrKSLIRHLEERGVQVVFWCLNEESDFEaAFSVGATGVITDYP 243
Cdd:cd08568 154 --FSIPELHEKLKLYSLHVPIDAIGYIGFEKF--VELLRLLRKLGLKIVLWTVNDPELVP-KLKGLVDGVITDDV 223
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 1-245 8.51e-12

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: 63.10  E-value: 8.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   1 MENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKeklevyFSPGHFAHGSDRRMVRLEDL 80
Cdd:cd08582  19 FELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLD------IGSWKGESYKGEKVPTLEEY 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  81 FQRFPRTPMS--VEIKGK--NEELIREIAGLVRRY--DRNEITIwASEKSSVMKKCKAANPEMPLsftisrgfwvllsYY 154
Cdd:cd08582  93 LAIVPKYGKKlfIEIKHPrrGPEAEEELLKLLKESglLPEQIVI-ISFDAEALKRVRELAPTLET-------------LW 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 155 LGllPFIPIPEkfffcfLPNIINRTYFP--FSCSCLNQLlavvskwlimRKSLIRHLEERGVQVVFWCLNEESDFEAAFS 232
Cdd:cd08582 159 LR--NYKSPKE------DPRPLAKSGGAagLDLSYEKKL----------NPAFIKALRDAGLKLNVWTVDDAEDAKRLIE 220

                       250
                ....*....|...
gi 33988692 233 VGATGVITDYPTA 245
Cdd:cd08582 221 LGVDSITTNRPGR 233
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 1-243 7.64e-11

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: 60.79  E-value: 7.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   1 MENSMAQRSDLLELDCQLTRDRVVVVSHDENL----CRQSGLNR-------------------DVGSLDFED--LPLYKE 55
Cdd:cd08567  21 FAKALDLGVDTLELDLVLTKDGVIVVSHDPKLnpdiTRDPDGAWlpyegpalyeltlaeikqlDVGEKRPGSdyAKLFPE 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  56 KLEVyfsPGhfahgsdRRMVRLEDLF-----QRFPRTPMSVEIK---------GKNEELIREIAGLVRRYDRNEITIWAS 121
Cdd:cd08567 101 QIPV---PG-------TRIPTLEEVFalvekYGNQKVRFNIETKsdpdrdilhPPPEEFVDAVLAVIRKAGLEDRVVLQS 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 122 EKSSVMKKCKAANPEMPLsftisrgfwVLLSYYLGLLPFIPIPEKFFFcflpniinRTYFPFscsclnqlLAVVSkwlim 201
Cdd:cd08567 171 FDWRTLQEVRRLAPDIPT---------VALTEETTLGNLPRAAKKLGA--------DIWSPY--------FTLVT----- 220

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 33988692 202 rKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGATGVITDYP 243
Cdd:cd08567 221 -KELVDEAHALGLKVVPWTVNDPEDMARLIDLGVDGIITDYP 261
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 2-112 2.11e-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 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: 56.18  E-value: 2.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   2 ENSM-----AQRSDL-LELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKlevyfspghfahGSDRRMV 75
Cdd:cd08585  21 ENSLsafraAAEAGYgIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRLL------------GTDEHIP 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 33988692  76 RLEDLFQRFP-RTPMSVEIK---GKNEELIREIAGLVRRYD 112
Cdd:cd08585  89 TLDEVLELVAgRVPLLIELKscgGGDGGLERRVLAALKDYK 129
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 10-251 1.17e-08

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: 54.24  E-value: 1.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  10 DLLELDCQLTRDRVVVVSHDENLCRQSGLNRD--VGSLDFEDLplykEKLEV--YFSPGH-------FAHgsdRRMVRLE 78
Cdd:cd08601  30 DYIELDLQMTKDGVLVAMHDETLDRTTNIERPgpVKDYTLAEI----KQLDAgsWFNKAYpeyaresYSG---LKVPTLE 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  79 DLFQRF-PRTPMSVEIK------GKNEELIREIA--GLVRRYDRNEITIWAS-EKSSvMKKCKAANPEMPLSFTISRGfw 148
Cdd:cd08601 103 EVIERYgGRANYYIETKspdlypGMEEKLLATLDkyGLLTDNLKNGQVIIQSfSKES-LKKLHQLNPNIPLVQLLWYG-- 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 149 VLLSYYLGLLPFIpipEKFFFCFLPNIinrtyfpfscsclnqllAVVSKWlimrksLIRHLEERGVQVVFWCLNEESDFE 228
Cdd:cd08601 180 EGAETYDKWLDEI---KEYAIGIGPSI-----------------ADADPW------MVHLIHKKGLLVHPYTVNEKADMI 233

                       250       260
                ....*....|....*....|...
gi 33988692 229 AAFSVGATGVITDYPTALRHYLD 251
Cdd:cd08601 234 RLINWGVDGMFTNYPDRLKEVLK 256
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 2-140 6.28e-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: 51.92  E-value: 6.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   2 ENSMA--QRS-----DLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLplykEKLEvYFSPghFAHGSDRRM 74
Cdd:cd08566  15 ENSLAaiEAAidlgaDIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEI----RKLR-LKDG--DGEVTDEKV 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33988692  75 VRLEDLFQRFP-RTPMSVEIKgknEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLS 140
Cdd:cd08566  88 PTLEEALAWAKgKILLNLDLK---DADLDEVIALVKKHGALDQVIFKSYSEEQAKELRALAPEVMLM 151
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 12-243 2.58e-07

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: 49.91  E-value: 2.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  12 LELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPlykeKLEV--YFSPgHFAhgsDRRMVRLEDLFQRFPRTPM 89
Cdd:cd08562  30 VEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELA----QLDAgsWFSP-EFA---GEPIPTLADVLELARELGL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  90 --SVEIK---GKNEELIREIAGLVRRYD--RNEITIwasekSS----VMKKCKAANPEMPlsftisrgfwvllsyyLGLL 158
Cdd:cd08562 102 glNLEIKpdpGDEALTARVVAAALRELWphASKLLL-----SSfsleALRAARRAAPELP----------------LGLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 159 pfipipekfFFCFLPNI--INRTYFPFSCSCLNQLLAvvskwlimrKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGAT 236
Cdd:cd08562 161 ---------FDTLPADWleLLAALGAVSIHLNYRGLT---------EEQVKALKDAGYKLLVYTVNDPARAAELLEWGVD 222


                ....*..
gi 33988692 237 GVITDYP 243
Cdd:cd08562 223 AIFTDRP 229
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 2-243 2.79e-05

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: 44.17  E-value: 2.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   2 ENSMA-------QRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDL--------------------PLYK 54
Cdd:cd08573  13 ENTLAafrqakkNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELrklnaaakhrlssrfpgekiPTLE 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  55 E--------KLEVYFS-PGHfahgSDRRMVRLEDLFQRFPRTPMSVEIKGKNEELIreiaGLVRRYDRNEIT--IWAS-E 122
Cdd:cd08573  93 EavkeclenNLRMIFDvKSN----SSKLVDALKNLFKKYPGLYDKAIVCSFNPIVI----YKVRKADPKILTglTWRPwF 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692 123 KSSVMKKCKAANPEMPLSFTIS-------RGFWVLLSYYLGLlpfipipEKFFFCFlpNIINRTYfpfscsclnqllavv 195
Cdd:cd08573 165 LSYTDDEGGPRRKSGWKHFLYSmldvileWSLHSWLPYFLGV-------SALLIHK--DDISSAY--------------- 220

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 33988692 196 skwlimrkslIRHLEERGVQVVFWCLNEESD---FEAAFSVgatGVITDYP 243
Cdd:cd08573 221 ----------VRYWRARGIRVIAWTVNTPTEkqyFAKTLNV---PYITDSL 258
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 13-94 2.10e-04

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: 41.55  E-value: 2.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692  13 ELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLEVYFSPGhFAhgsDRRMVRLEDLFQ---RFPRTPM 89
Cdd:cd08581  31 EFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVAEPARFGSR-FA---GEPLPSLAAVVQwlaQHPQVTL 106


                ....*
gi 33988692  90 SVEIK 94
Cdd:cd08581 107 FVEIK 111
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 8-52 1.95e-03

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: 38.81  E-value: 1.95e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 33988692   8 RSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPL 52
Cdd:cd08607  34 GADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSDRDDLLEVPV 78
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 4-61 3.47e-03

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: 37.42  E-value: 3.47e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 33988692   4 SMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDvgsldfedlPLYKEKLEVYF 61
Cdd:cd08555  22 ALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGILP---------PTLEEVLELIA 70
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 1-120 3.53e-03

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: 38.11  E-value: 3.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33988692   1 MENSMAQRSDLLELDCQLTRDRVVVVSHDENL-CRQ--SGLNRDvgsLDFEDLplykEKLEVYFspGHFAHGSDR----- 72
Cdd:cd08613  66 MQAAFDAGADVVELDVHPTKDGEFAVFHDWTLdCRTdgSGVTRD---HTMAEL----KTLDIGY--GYTADGGKTfpfrg 136

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 33988692  73 ----RMVRLEDLFQRFPRTPMSVEIKGKNEELIREIAGLVRRYDRNEITIWA 120
Cdd:cd08613 137 kgvgMMPTLDEVFAAFPDRRFLINFKSDDAAEGELLAEKLATLPRKRLQVLT 188
 
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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