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Conserved domains on  [gi|146198640|ref|NP_077283|]
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lysophospholipase D GDPD3 [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 ...
 13-310 8.36e-163

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: 455.52  E-value: 8.36e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  13 GSYAMLSIFFLRRPHLLHTPRAPTFRIRLGAHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCR 92
Cdd:cd08612    1 GGYIATSYFLLRNPTLLHKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  93 QSGLNRDVGSLDFEDLPLYKEKLEVYFSPGHF--AHGSDRRMVRLEDLFQRFPRTPMSVEIKGKNEELIREIAGLVRRYD 170
Cdd:cd08612   81 SCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYcvPKGSDRRIPLLEEVFEAFPDTPINIDIKVENDELIKKVSDLVRKYK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 171 RNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVLLSYYLGLLPFIPIPEKFFFCFLPNIINRTYFPFSCSCLNQLL 250
Cdd:cd08612  161 REDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYFPKSMSRLNRFV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 251 AVVSKWLIMRKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGATGVITDYPTALRHYLDN 310
Cdd:cd08612  241 LFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLREFLDK 300
 
Name Accession Description Interval E-value
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 13-310 8.36e-163

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: 455.52  E-value: 8.36e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  13 GSYAMLSIFFLRRPHLLHTPRAPTFRIRLGAHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCR 92
Cdd:cd08612    1 GGYIATSYFLLRNPTLLHKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  93 QSGLNRDVGSLDFEDLPLYKEKLEVYFSPGHF--AHGSDRRMVRLEDLFQRFPRTPMSVEIKGKNEELIREIAGLVRRYD 170
Cdd:cd08612   81 SCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYcvPKGSDRRIPLLEEVFEAFPDTPINIDIKVENDELIKKVSDLVRKYK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 171 RNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVLLSYYLGLLPFIPIPEKFFFCFLPNIINRTYFPFSCSCLNQLL 250
Cdd:cd08612  161 REDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYFPKSMSRLNRFV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 251 AVVSKWLIMRKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGATGVITDYPTALRHYLDN 310
Cdd:cd08612  241 LFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLREFLDK 300
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
43-309 4.11e-43

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 148.09  E-value: 4.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLplykEKLEVyfspG 122
Cdd:COG0584    7 AHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAEL----RQLDA----G 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 123 HFAHGSDRRMVRLEDLFQRFP-RTPMSVEIK---GKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLS 198
Cdd:COG0584   79 SGPDFAGERIPTLEEVLELVPgDVGLNIEIKsppAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 199 FTISRGFWVLLSYYLGLLP-FIPIPekfffcflpniinrtyfpfscsclnqllavvskWLIMRKSLIRHLEERGVQVVFW 277
Cdd:COG0584  159 LLVEELPADPLELARALGAdGVGPD---------------------------------YDLLTPELVAAAHAAGLKVHVW 205

                        250       260       270
                 ....*....|....*....|....*....|..
gi 146198640 278 CLNEESDFEAAFSVGATGVITDYPTALRHYLD 309
Cdd:COG0584  206 TVNDPEEMRRLLDLGVDGIITDRPDLLRAVLR 237
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 44-301 3.82e-28

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: 109.03  E-value: 3.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640   44 HRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLE--VYFSP 121
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGnsGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  122 GHFahgsdrRMVRLEDLFQRFPRTPMSVEIKGK---------NEELIREIAGLVRRYD----RNEITIWASEKSSVMKKC 188
Cdd:pfam03009  81 ERV------PFPTLEEVLEFDWDVGFNIEIKIKpyveaiapeEGLIVKDLLLSVDEILakkaDPRRVIFSSFNPDELKRL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  189 KAANPEMPLSFTISRGFWVLLSYYLGLLPFIPIPEkfffcFLPNIinrtyfpfscsclnQLLAVVSKWLIMRkslirhLE 268
Cdd:pfam03009 155 RELAPKLPLVFLSSGRAYAEADLLERAAAFAGAPA-----LLGEV--------------ALVDEALPDLVKR------AH 209

                         250       260       270
                  ....*....|....*....|....*....|...
gi 146198640  269 ERGVQVVFWCLNEESDFEAAFSVGATGVITDYP 301
Cdd:pfam03009 210 ARGLVVHVWTVNNEDEMKRLLELGVDGVITDRP 242
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 43-92 2.24e-08

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 54.68  E-value: 2.24e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCR 92
Cdd:PRK11143  31 AHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDR 80
 
Name Accession Description Interval E-value
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 13-310 8.36e-163

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: 455.52  E-value: 8.36e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  13 GSYAMLSIFFLRRPHLLHTPRAPTFRIRLGAHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCR 92
Cdd:cd08612    1 GGYIATSYFLLRNPTLLHKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  93 QSGLNRDVGSLDFEDLPLYKEKLEVYFSPGHF--AHGSDRRMVRLEDLFQRFPRTPMSVEIKGKNEELIREIAGLVRRYD 170
Cdd:cd08612   81 SCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYcvPKGSDRRIPLLEEVFEAFPDTPINIDIKVENDELIKKVSDLVRKYK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 171 RNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVLLSYYLGLLPFIPIPEKFFFCFLPNIINRTYFPFSCSCLNQLL 250
Cdd:cd08612  161 REDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYFPKSMSRLNRFV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 251 AVVSKWLIMRKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGATGVITDYPTALRHYLDN 310
Cdd:cd08612  241 LFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLREFLDK 300
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 39-304 1.75e-111

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: 323.79  E-value: 1.75e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  39 IRLGAHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLEVY 118
Cdd:cd08575    1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGYT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 119 FSPG---HFAHGSDRRMVRLEDLFQRFPRTPMSVEIKGKN-EELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPE 194
Cdd:cd08575   81 FDGGktgYPRGGGDGRIPTLEEVFKAFPDTPINIDIKSPDaEELIAAVLDLLEKYKREDRTVWGSTNPEYLRALHPENPN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 195 MPLSFTISRGFWVLLS-YYLGLLPFIPIPEKFFFCFLPNIINRTYFPFSCsclnqllAVVSKWLIMRKSLIRHLEERGVQ 273
Cdd:cd08575  161 LFESFSMTRCLLLYLAlGYTGLLPFVPIKESFFEIPRPVIVLETFTLGEG-------ASIVAALLWWPNLFDHLRKRGIQ 233

                        250       260       270
                 ....*....|....*....|....*....|.
gi 146198640 274 VVFWCLNEESDFEAAFSVGATGVITDYPTAL 304
Cdd:cd08575  234 VYLWVLNDEEDFEEAFDLGADGVMTDSPTKL 264
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
43-309 4.11e-43

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 148.09  E-value: 4.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLplykEKLEVyfspG 122
Cdd:COG0584    7 AHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAEL----RQLDA----G 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 123 HFAHGSDRRMVRLEDLFQRFP-RTPMSVEIK---GKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLS 198
Cdd:COG0584   79 SGPDFAGERIPTLEEVLELVPgDVGLNIEIKsppAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 199 FTISRGFWVLLSYYLGLLP-FIPIPekfffcflpniinrtyfpfscsclnqllavvskWLIMRKSLIRHLEERGVQVVFW 277
Cdd:COG0584  159 LLVEELPADPLELARALGAdGVGPD---------------------------------YDLLTPELVAAAHAAGLKVHVW 205

                        250       260       270
                 ....*....|....*....|....*....|..
gi 146198640 278 CLNEESDFEAAFSVGATGVITDYPTALRHYLD 309
Cdd:COG0584  206 TVNDPEEMRRLLDLGVDGIITDRPDLLRAVLR 237
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 43-305 2.66e-40

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: 141.24  E-value: 2.66e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLplykEKLEV--YFS 120
Cdd:cd08561    3 AHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAEL----RRLDAgyHFT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 121 P--GHFA--HGSDRRMVRLEDLFQRFPRTPMSVEIKGKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMP 196
Cdd:cd08561   79 DdgGRTYpyRGQGIRIPTLEELFEAFPDVRLNIEIKDDGPAAAAALADLIERYGAQDRVLVASFSDRVLRRFRRLCPRVA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 197 LSFTISRGFWVLLSYYLGLLPFIPIPEKFFfcflpniinrtYFPFSCSCLNqllaVVSkwlimrKSLIRHLEERGVQVVF 276
Cdd:cd08561  159 TSAGEGEVAAFVLASRLGLGSLYSPPYDAL-----------QIPVRYGGVP----LVT------PRFVRAAHAAGLEVHV 217

                        250       260
                 ....*....|....*....|....*....
gi 146198640 277 WCLNEESDFEAAFSVGATGVITDYPTALR 305
Cdd:cd08561  218 WTVNDPAEMRRLLDLGVDGIITDRPDLLL 246
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 44-301 3.82e-28

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: 109.03  E-value: 3.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640   44 HRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLE--VYFSP 121
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGnsGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  122 GHFahgsdrRMVRLEDLFQRFPRTPMSVEIKGK---------NEELIREIAGLVRRYD----RNEITIWASEKSSVMKKC 188
Cdd:pfam03009  81 ERV------PFPTLEEVLEFDWDVGFNIEIKIKpyveaiapeEGLIVKDLLLSVDEILakkaDPRRVIFSSFNPDELKRL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  189 KAANPEMPLSFTISRGFWVLLSYYLGLLPFIPIPEkfffcFLPNIinrtyfpfscsclnQLLAVVSKWLIMRkslirhLE 268
Cdd:pfam03009 155 RELAPKLPLVFLSSGRAYAEADLLERAAAFAGAPA-----LLGEV--------------ALVDEALPDLVKR------AH 209

                         250       260       270
                  ....*....|....*....|....*....|...
gi 146198640  269 ERGVQVVFWCLNEESDFEAAFSVGATGVITDYP 301
Cdd:pfam03009 210 ARGLVVHVWTVNNEDEMKRLLELGVDGVITDRP 242
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 43-300 3.34e-27

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: 105.04  E-value: 3.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHdenlcrqsglnrdvgsldfeDLPlykeklevyfspg 122
Cdd:cd08556    3 AHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIH--------------------DIP------------- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 123 hfahgsdrrmvRLEDLFQRFP-RTPMSVEIKG--KNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLsf 199
Cdd:cd08556   50 -----------TLEEVLELVKgGVGLNIELKEptRYPGLEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVPT-- 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 200 tisrgfwVLLSYYLGLLPFIPIPEKFFFCFlpniinrtyfpfscsclnqllAVVSKWLIMRKSLIRHLEERGVQVVFWCL 279
Cdd:cd08556  117 -------GLLVDKPPLDPLLAELARALGAD---------------------AVNPHYKLLTPELVRAAHAAGLKVYVWTV 168

                        250       260
                 ....*....|....*....|.
gi 146198640 280 NEESDFEAAFSVGATGVITDY 300
Cdd:cd08556  169 NDPEDARRLLALGVDGIITDD 189
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 43-301 1.92e-26

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: 103.78  E-value: 1.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLplykEKLEVyfspg 122
Cdd:cd08579    3 AHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEEL----KKLTI----- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 123 hFAHGSDRRMVRLEDLFQRF--PRTPMSVEIK---GKNEELIREiagLVRRYDRNEIT---IWASEKSSVMKKCKAANPE 194
Cdd:cd08579   74 -GENGHGAKIPSLDEYLALAkgLKQKLLIELKphgHDSPDLVEK---FVKLYKQNLIEnqhQVHSLDYRVIEKVKKLDPK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 195 MPLSFtisrgfwvLLSYYLGLLP-----FIPIPEkfffcflpniinrtyfpfscSCLNqllavvskwlimrKSLIRHLEE 269
Cdd:cd08579  150 IKTGY--------ILPFNIGNLPktnvdFYSIEY--------------------STLN-------------KEFIRQAHQ 188

                        250       260       270
                 ....*....|....*....|....*....|..
gi 146198640 270 RGVQVVFWCLNEESDFEAAFSVGATGVITDYP 301
Cdd:cd08579  189 NGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 43-301 6.90e-22

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: 91.85  E-value: 6.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKeklevyFSPG 122
Cdd:cd08563    5 AHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLD------AGSW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 123 HFAHGSDRRMVRLEDLFQRFPRTPM--SVEIK---GKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPempl 197
Cdd:cd08563   79 FDEKFTGEKIPTLEEVLDLLKDKDLllNIEIKtdvIHYPGIEKKVLELVKEYNLEDRVIFSSFNHESLKRLKKLDP---- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 198 sftisrgfwvllSYYLGLLpfipipekfFFCFLPNIINrtYFPFscsclNQLLAVVSKWLIMRKSLIRHLEERGVQVVFW 277
Cdd:cd08563  155 ------------KIKLALL---------YETGLQDPKD--YAKK-----IGADSLHPDFKLLTEEVVEELKKRGIPVRLW 206

                        250       260
                 ....*....|....*....|....
gi 146198640 278 CLNEESDFEAAFSVGATGVITDYP 301
Cdd:cd08563  207 TVNEEEDMKRLKDLGVDGIITNYP 230
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 43-301 2.36e-21

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: 90.74  E-value: 2.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDlplYKEKLEVYFSPg 122
Cdd:cd08570    3 GHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDSTWD---ELSHLRTIEEP- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 123 hfahgsDRRMVRLEDLFQRF-----PRTPMSVEIKGKN--EELIREIAGLVRRYdrNEITIWASEkssvmkkckaanpem 195
Cdd:cd08570   79 ------HQPMPTLKDVLEWLvehelPDVKLMLDIKRDNdpEILFKLIAEMLAVK--PDLDFWRER--------------- 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 196 plsftISRGFWVL--LSYYLGLLPFIPIpekffFCFLPNI-INRTYFPFSCSCLNQLLAVVSKWLIMRKSLIRHLEERGV 272
Cdd:cd08570  136 -----IILGLWHLdfLKYGKEVLPGFPV-----FHIGFSLdYARHFLNYSEKLVGISMHFVSLWGPFGQAFLPELKKNGK 205

                        250       260
                 ....*....|....*....|....*....
gi 146198640 273 QVVFWCLNEESDFEAAFSVGATGVITDYP 301
Cdd:cd08570  206 KVFVWTVNTEEDMRYAIRLGVDGVITDDP 234
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 43-303 4.32e-20

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: 86.98  E-value: 4.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKeklevyFSPG 122
Cdd:cd08582    3 AHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLD------IGSW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 123 HFAHGSDRRMVRLEDLFQRFPRTPMS--VEIKGK--NEELIREIAGLVRRY--DRNEITIwASEKSSVMKKCKAANPEMP 196
Cdd:cd08582   77 KGESYKGEKVPTLEEYLAIVPKYGKKlfIEIKHPrrGPEAEEELLKLLKESglLPEQIVI-ISFDAEALKRVRELAPTLE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 197 LsftisrgfwvllsYYLGllPFIPIPEkfffcfLPNIINRTYFP--FSCSCLNQLlavvskwlimRKSLIRHLEERGVQV 274
Cdd:cd08582  156 T-------------LWLR--NYKSPKE------DPRPLAKSGGAagLDLSYEKKL----------NPAFIKALRDAGLKL 204

                        250       260
                 ....*....|....*....|....*....
gi 146198640 275 VFWCLNEESDFEAAFSVGATGVITDYPTA 303
Cdd:cd08582  205 NVWTVDDAEDAKRLIELGVDSITTNRPGR 233
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 39-301 8.53e-20

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: 86.98  E-value: 8.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  39 IRLGAHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENL----CRQSGLNR---------------- 98
Cdd:cd08567    1 FDLQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLnpdiTRDPDGAWlpyegpalyeltlaei 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  99 ---DVGSLDFED--LPLYKEKLEVyfsPGhfahgsdRRMVRLEDLF-----QRFPRTPMSVEIK---------GKNEELI 159
Cdd:cd08567   81 kqlDVGEKRPGSdyAKLFPEQIPV---PG-------TRIPTLEEVFalvekYGNQKVRFNIETKsdpdrdilhPPPEEFV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 160 REIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLsftisrgfwVLLSYYLGLLPFIPIPEKFFFcflpniinRTYF 239
Cdd:cd08567  151 DAVLAVIRKAGLEDRVVLQSFDWRTLQEVRRLAPDIPT---------VALTEETTLGNLPRAAKKLGA--------DIWS 213

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 146198640 240 PFscsclnqlLAVVSkwlimrKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGATGVITDYP 301
Cdd:cd08567  214 PY--------FTLVT------KELVDEAHALGLKVVPWTVNDPEDMARLIDLGVDGIITDYP 261
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 39-301 3.64e-18

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: 81.58  E-value: 3.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  39 IRLGaHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYkeklevy 118
Cdd:cd08568    1 IILG-HRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKL------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 119 fspghfaHGSDRRMVRLEDLFQRFPRTP-MSVEIKGKneELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPL 197
Cdd:cd08568   73 -------HPGGELIPTLEEVFRALPNDAiINVEIKDI--DAVEPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPDAKV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 198 SFTISrgfwvllSYYLGllpfipipekfffcFLPNIINRTYFPFSCSCLNQLLAVVSKWLImrKSLIRHLEERGVQVVFW 277
Cdd:cd08568  144 GLLIG-------EEEEG--------------FSIPELHEKLKLYSLHVPIDAIGYIGFEKF--VELLRLLRKLGLKIVLW 200

                        250       260
                 ....*....|....*....|....
gi 146198640 278 CLNEESDFEaAFSVGATGVITDYP 301
Cdd:cd08568  201 TVNDPELVP-KLKGLVDGVITDDV 223
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 43-198 1.40e-14

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: 71.95  E-value: 1.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELL-ENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLplykEKLEvYFSP 121
Cdd:cd08566    4 AHRGGWGAGApENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEI----RKLR-LKDG 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 146198640 122 ghFAHGSDRRMVRLEDLFQRFP-RTPMSVEIKgknEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLS 198
Cdd:cd08566   79 --DGEVTDEKVPTLEEALAWAKgKILLNLDLK---DADLDEVIALVKKHGALDQVIFKSYSEEQAKELRALAPEVMLM 151
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 43-309 1.34e-13

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: 69.27  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRD--VGSLDFEDLplykEKLEV--Y 118
Cdd:cd08601    5 AHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIERPgpVKDYTLAEI----KQLDAgsW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 119 FSPGH-------FAHgsdRRMVRLEDLFQRF-PRTPMSVEIK------GKNEELIREIA--GLVRRYDRNEITIWAS-EK 181
Cdd:cd08601   81 FNKAYpeyaresYSG---LKVPTLEEVIERYgGRANYYIETKspdlypGMEEKLLATLDkyGLLTDNLKNGQVIIQSfSK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 182 SSvMKKCKAANPEMPLSFTISRGfwVLLSYYLGLLPFIpipEKFFFCFLPNIinrtyfpfscsclnqllAVVSKWlimrk 261
Cdd:cd08601  158 ES-LKKLHQLNPNIPLVQLLWYG--EGAETYDKWLDEI---KEYAIGIGPSI-----------------ADADPW----- 209

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 146198640 262 sLIRHLEERGVQVVFWCLNEESDFEAAFSVGATGVITDYPTALRHYLD 309
Cdd:cd08601  210 -MVHLIHKKGLLVHPYTVNEKADMIRLINWGVDGMFTNYPDRLKEVLK 256
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 43-301 1.58e-12

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: 65.71  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPlykeKLEV--YFS 120
Cdd:cd08562    3 AHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELA----QLDAgsWFS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 121 PgHFAhgsDRRMVRLEDLFQRFPRTPM--SVEIK---GKNEELIREIAGLVRRYD--RNEITIwasekSS----VMKKCK 189
Cdd:cd08562   79 P-EFA---GEPIPTLADVLELARELGLglNLEIKpdpGDEALTARVVAAALRELWphASKLLL-----SSfsleALRAAR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 190 AANPEMPlsftisrgfwvllsyyLGLLpfipipekfFFCFLPNI--INRTYFPFSCSCLNQLLAvvskwlimrKSLIRHL 267
Cdd:cd08562  150 RAAPELP----------------LGLL---------FDTLPADWleLLAALGAVSIHLNYRGLT---------EEQVKAL 195

                        250       260       270
                 ....*....|....*....|....*....|....
gi 146198640 268 EERGVQVVFWCLNEESDFEAAFSVGATGVITDYP 301
Cdd:cd08562  196 KDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 41-301 1.20e-11

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: 63.82  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  41 LGAHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDL------------ 108
Cdd:cd08573    1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELrklnaaakhrls 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 109 --------PLYKE--------KLEVYFS-PGHfahgSDRRMVRLEDLFQRFPRTPMSVEIKGKNEELIreiaGLVRRYDR 171
Cdd:cd08573   81 srfpgekiPTLEEavkeclenNLRMIFDvKSN----SSKLVDALKNLFKKYPGLYDKAIVCSFNPIVI----YKVRKADP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 172 NEIT--IWAS-EKSSVMKKCKAANPEMPLSFTIS-------RGFWVLLSYYLGLlpfipipEKFFFCFlpNIINRTYfpf 241
Cdd:cd08573  153 KILTglTWRPwFLSYTDDEGGPRRKSGWKHFLYSmldvileWSLHSWLPYFLGV-------SALLIHK--DDISSAY--- 220

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146198640 242 scsclnqllavvskwlimrkslIRHLEERGVQVVFWCLNEESD---FEAAFSVgatGVITDYP 301
Cdd:cd08573  221 ----------------------VRYWRARGIRVIAWTVNTPTEkqyFAKTLNV---PYITDSL 258
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 43-170 5.42e-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 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: 61.57  E-value: 5.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGgsgeLLENTMEAMENSM-----AQRSDL-LELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKle 116
Cdd:cd08585    8 AHRG----LHDRDAGIPENSLsafraAAEAGYgIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRLL-- 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 146198640 117 vyfspghfahGSDRRMVRLEDLFQRFP-RTPMSVEIK---GKNEELIREIAGLVRRYD 170
Cdd:cd08585   82 ----------GTDEHIPTLDEVLELVAgRVPLLIELKscgGGDGGLERRVLAALKDYK 129
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 43-168 6.01e-11

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


Pssm-ID: 176522 [Multi-domain]  Cd Length: 263  Bit Score: 61.96  E-value: 6.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENL---CRQSGLnrdVGSLDFEDLPL------YKE 113
Cdd:cd08580    5 AHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLkslTNGSGA---VSAYTAAQLATlnagynFKP 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 146198640 114 KLEVYFspghfaHGSDRRMVRLEDLFQRFPRTPMSVEIKGKN-EELIREIAGLVRR 168
Cdd:cd08580   82 EGGYPY------RGKPVGIPTLEQVLRAFPDTPFILDMKSLPaDPQAKAVARVLER 131
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 42-119 3.51e-10

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: 58.22  E-value: 3.51e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 146198640  42 GAHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDvgsldfedlPLYKEKLEVYF 119
Cdd:cd08555    2 LSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGILP---------PTLEEVLELIA 70
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 43-90 3.97e-10

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: 59.59  E-value: 3.97e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENL 90
Cdd:cd08559    5 AHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTL 52
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 43-90 2.67e-09

Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Escherichia coli periplasmic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46), GlpQ, and similar proteins. GP-GDE plays an essential role in the metabolic pathway of E. coli. It catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. E. coli possesses two major G3P uptake systems: Glp and Ugp, which contain genes coding for two different GP-GDEs. GlpQ gene from the E. coli glp operon codes for a periplasmic phosphodiesterase GlpQ, which is the prototype of this family. GlpQ is a dimeric enzyme that hydrolyzes periplasmic glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), to the corresponding alcohols and G3P, which is subsequently transported into the cell through the GlpT transport system. Ca2+ is required for the enzymatic activity of GlpQ. This family also includes a surface-exposed lipoprotein, protein D (HPD), from Haemophilus influenza Type b and nontypeable strains, which shows very high sequence similarity with E. coli GlpQ. HPD has been characterized as a human immunoglobulin D-binding protein with glycerophosphodiester phosphodiesterase activity. It can hydrolyze phosphatidylcholine from host membranes to produce free choline on the lipopolysaccharides on the surface of pathogenic bacteria.


Pssm-ID: 176542 [Multi-domain]  Cd Length: 318  Bit Score: 57.40  E-value: 2.67e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENL 90
Cdd:cd08600    5 AHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYL 52
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 43-152 8.43e-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: 55.03  E-value: 8.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLEVYFSPG 122
Cdd:cd08581    3 AHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVAEPARFGSR 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 146198640 123 hFAhgsDRRMVRLEDLFQ---RFPRTPMSVEIK 152
Cdd:cd08581   83 -FA---GEPLPSLAAVVQwlaQHPQVTLFVEIK 111
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 44-169 1.98e-08

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: 54.40  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  44 HRGG--SGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSH--DENLCRQSGL-NRDVGSLDFEDLPlYKEKLEVY 118
Cdd:cd08564    9 HRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgtEDDTNPDTSIqLDDSGFKNINDLS-LDEITRLH 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 146198640 119 FSP-----GHFAHGSDRRMV-RLEDLFQRF-PRTPMSVEIKGKNEELIREIAGLVRRY 169
Cdd:cd08564   88 FKQlfdekPCGADEIKGEKIpTLEDVLVTFkDKLKYNIELKGREVGLGERVLNLVEKY 145
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 43-92 2.24e-08

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 54.68  E-value: 2.24e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCR 92
Cdd:PRK11143  31 AHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDR 80
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 43-302 4.39e-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: 53.18  E-value: 4.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQ---SGLNRD----------VGSLDFEDLP 109
Cdd:cd08565    3 GHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTthgTGAVRDltlaerkalrLRDSFGEKIP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 110 LYKEKLEVYFSPGHFAHgsdrrmvrledlfqrfprtpmsVEIKGKN-----EELIREIAGLVRRYDRNEITIWASEKSSV 184
Cdd:cd08565   83 TLEEVLALFAPSGLELH----------------------VEIKTDAdgtpyPGAAALAAATLRRHGLLERSVLTSFDPAV 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 185 MKKCKAANPEMPLSFTISRgfwvLLSYYLGLLPFIPIpekfffcflpniinrtyfpfsCSCLNQLLAVVSKWLIMRKSLI 264
Cdd:cd08565  141 LTEVRKHPGVRTLGSVDED----MLERLGGELPFLTA---------------------TALKAHIVAVEQSLLAATWELV 195

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 146198640 265 RHLEERGVQVVfWCLNEESDFEAAFSVGATGVITDYPT 302
Cdd:cd08565  196 RAAVPGLRLGV-WTVNDDSLIRYWLACGVRQLTTDRPD 232
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 44-110 1.37e-06

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: 48.83  E-value: 1.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 146198640  44 HRG-------GSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPL 110
Cdd:cd08607    5 HRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSDRDDLLEVPV 78
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 51-178 2.74e-06

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: 48.13  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  51 LLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENL-CRQ--SGLNRDvgsLDFEDLplykEKLEVYFspGHFAHG 127
Cdd:cd08613   58 YLENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLdCRTdgSGVTRD---HTMAEL----KTLDIGY--GYTADG 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640 128 SDR---------RMVRLEDLFQRFPRTPMSVEIKGKNEELIREIAGLVRRYDRNEITIWA 178
Cdd:cd08613  129 GKTfpfrgkgvgMMPTLDEVFAAFPDRRFLINFKSDDAAEGELLAEKLATLPRKRLQVLT 188
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 44-87 4.11e-06

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: 47.66  E-value: 4.11e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 146198640  44 HRG--------GSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHD 87
Cdd:cd08572    5 HRGlgknyasgSLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHD 56
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 43-107 1.88e-05

Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of putative bacterial and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ, as well as plant glycerophosphodiester phosphodiesterases (GP-PDEs), all of which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. The prototypes of this family include putative secreted phosphodiesterase encoded by gene glpQ1 (SCO1565) from the pho regulon in Streptomyces coelicolor genome, and in plants, two distinct Arabidopsis thaliana genes, AT5G08030 and AT1G74210, coding putative GP-PDEs from the cell walls and vacuoles, respectively.


Pssm-ID: 176544 [Multi-domain]  Cd Length: 309  Bit Score: 45.75  E-value: 1.88e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 146198640  43 AHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLcrqsGLNRDVGSL-DFED 107
Cdd:cd08602    5 AHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPEL----SGTTDVADHpEFAD 66
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 39-152 5.02e-05

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: 44.36  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  39 IRLGAHRG--------GSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDeNLCRQSGLNRDVGSLDFED-LP 109
Cdd:cd08606    2 VQVIGHRGlgkntaerKSLQLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHD-FLVSETGTDVPIHDLTLEQfLH 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 146198640 110 LYKEKLEVYFSP--------GHFAHGSdrrMVRLEDLFQRFPRT-PMSVEIK 152
Cdd:cd08606   81 LSRMKYTVDFKKkgfkgnsrGHSIQAP---FTTLEELLKKLPKSvGFNIELK 129
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 43-96 7.32e-04

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


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 40.36  E-value: 7.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 146198640  43 AHRGG--SGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSH--DENLCRQSGL 96
Cdd:cd08583    3 AHAMGgiDGKTYTNSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHswDESLLKQLGL 60
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 40-169 5.08e-03

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 38.00  E-value: 5.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146198640  40 RLGAHRGGsGELL-ENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLplykEKLEV- 117
Cdd:PRK09454   9 RIVAHRGG-GKLApENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDL----AQLDAg 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 146198640 118 -YFSPGhFAhgsDRRMVRLEDLFQRFPRTPMS--VEIK---GKNEELIREIAGLVRRY 169
Cdd:PRK09454  84 sWFSAA-FA---GEPLPTLSQVAARCRAHGMAanIEIKpttGREAETGRVVALAARAL 137
 
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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