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Conserved domains on  [gi|148235333|ref|NP_001090139|]
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glycerophosphodiester phosphodiesterase domain containing 1 L homeolog [Xenopus laevis]

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 3.82e-170

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: 474.78  E-value: 3.82e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  13 GGYAVTSYYLLKNPHILHKKKKLSFYCRHISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLR 92
Cdd:cd08612    1 GGYIATSYFLLRNPTLLHKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  93 QTGHDVSICDITYEELPLYREPLEVTFFPGHY--SSGSDRRIPQLEEVFQRFPHMPINVEIKEETPELVKQVSDLVKRYQ 170
Cdd:cd08612   81 SCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYcvPKGSDRRIPLLEEVFEAFPDTPINIDIKVENDELIKKVSDLVRKYK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 171 RSERTVWASVKDPIMKLCQEENPDMPIMFTARRGLILLLLYYTGLLPFVPLRESVLEMHMPSIINRTYFPPNQLMRNRFL 250
Cdd:cd08612  161 REDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYFPKSMSRLNRFV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 251 VFLQDKLMMRKSLFQHLQARGIQVYLWVLNEESDYQRGLECGADGIMTDYPSNLRSFLQR 310
Cdd:cd08612  241 LFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLREFLDK 300
 
Name Accession Description Interval E-value
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 13-310 3.82e-170

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: 474.78  E-value: 3.82e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  13 GGYAVTSYYLLKNPHILHKKKKLSFYCRHISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLR 92
Cdd:cd08612    1 GGYIATSYFLLRNPTLLHKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  93 QTGHDVSICDITYEELPLYREPLEVTFFPGHY--SSGSDRRIPQLEEVFQRFPHMPINVEIKEETPELVKQVSDLVKRYQ 170
Cdd:cd08612   81 SCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYcvPKGSDRRIPLLEEVFEAFPDTPINIDIKVENDELIKKVSDLVRKYK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 171 RSERTVWASVKDPIMKLCQEENPDMPIMFTARRGLILLLLYYTGLLPFVPLRESVLEMHMPSIINRTYFPPNQLMRNRFL 250
Cdd:cd08612  161 REDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYFPKSMSRLNRFV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 251 VFLQDKLMMRKSLFQHLQARGIQVYLWVLNEESDYQRGLECGADGIMTDYPSNLRSFLQR 310
Cdd:cd08612  241 LFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLREFLDK 300
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
42-310 4.54e-51

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 169.28  E-value: 4.54e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELplyrepleVTFFP 121
Cdd:COG0584    6 IAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAEL--------RQLDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 122 GHYSSGSDRRIPQLEEVFQRFPH-MPINVEIKEET---PELVKQVSDLVKRYQRSERTVWASVKDPIMKLCQEENPDMPI 197
Cdd:COG0584   78 GSGPDFAGERIPTLEEVLELVPGdVGLNIEIKSPPaaePDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 198 MFTARRGLILLLLYYTGLLP-FVPLRESVLEmhmpsiinrtyfppnqlmrnrflvflqdklmmrKSLFQHLQARGIQVYL 276
Cdd:COG0584  158 GLLVEELPADPLELARALGAdGVGPDYDLLT---------------------------------PELVAAAHAAGLKVHV 204

                        250       260       270
                 ....*....|....*....|....*....|....
gi 148235333 277 WVLNEESDYQRGLECGADGIMTDYPSNLRSFLQR 310
Cdd:COG0584  205 WTVNDPEEMRRLLDLGVDGIITDRPDLLRAVLRE 238
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 44-301 1.09e-35

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: 129.44  E-value: 1.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333   44 HRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELPLYREPLEVTFfpgh 123
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSG---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  124 YSSGSDRRIPQLEEVFQRFPHMPINVEIK-------------EETPELVKQVSDLVKRYQRsERTVWASVKDP-IMKLCQ 189
Cdd:pfam03009  77 PLSGERVPFPTLEEVLEFDWDVGFNIEIKikpyveaiapeegLIVKDLLLSVDEILAKKAD-PRRVIFSSFNPdELKRLR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  190 EENPDMPIMFtarrglillllyytgllpfvpLRESVLEMHMPSIiNRTY---FPPNQLMRNRFLVFLQDKLMMRkslfqh 266
Cdd:pfam03009 156 ELAPKLPLVF---------------------LSSGRAYAEADLL-ERAAafaGAPALLGEVALVDEALPDLVKR------ 207

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 148235333  267 LQARGIQVYLWVLNEESDYQRGLECGADGIMTDYP 301
Cdd:pfam03009 208 AHARGLVVHVWTVNNEDEMKRLLELGVDGVITDRP 242
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 38-159 4.05e-07

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 50.32  E-value: 4.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  38 YCRHISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQT-GHDVsICDITYEELplyreple 116
Cdd:PRK09454   7 YPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSnGWGV-AGELTWQDL-------- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148235333 117 VTFFPGHYSSG--SDRRIPQLEEVFQRFPH--MPINVEIK------EETPELV 159
Cdd:PRK09454  78 AQLDAGSWFSAafAGEPLPTLSQVAARCRAhgMAANIEIKpttgreAETGRVV 130
 
Name Accession Description Interval E-value
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 13-310 3.82e-170

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: 474.78  E-value: 3.82e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  13 GGYAVTSYYLLKNPHILHKKKKLSFYCRHISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLR 92
Cdd:cd08612    1 GGYIATSYFLLRNPTLLHKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  93 QTGHDVSICDITYEELPLYREPLEVTFFPGHY--SSGSDRRIPQLEEVFQRFPHMPINVEIKEETPELVKQVSDLVKRYQ 170
Cdd:cd08612   81 SCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYcvPKGSDRRIPLLEEVFEAFPDTPINIDIKVENDELIKKVSDLVRKYK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 171 RSERTVWASVKDPIMKLCQEENPDMPIMFTARRGLILLLLYYTGLLPFVPLRESVLEMHMPSIINRTYFPPNQLMRNRFL 250
Cdd:cd08612  161 REDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYFPKSMSRLNRFV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 251 VFLQDKLMMRKSLFQHLQARGIQVYLWVLNEESDYQRGLECGADGIMTDYPSNLRSFLQR 310
Cdd:cd08612  241 LFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLREFLDK 300
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 39-304 3.95e-121

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: 349.21  E-value: 3.95e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  39 CRHISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELPLYREPLEVT 118
Cdd:cd08575    1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGYT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 119 FFPG---HYSSGSDRRIPQLEEVFQRFPHMPINVEIKEETP-ELVKQVSDLVKRYQRSERTVWASVKDPIMKLCQEENPD 194
Cdd:cd08575   81 FDGGktgYPRGGGDGRIPTLEEVFKAFPDTPINIDIKSPDAeELIAAVLDLLEKYKREDRTVWGSTNPEYLRALHPENPN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 195 MPIMFTARRGLILLLLYYTG-LLPFVPLRESVLEMHMPSIINRTYFPPNQlmrnrflVFLQDKLMMRKSLFQHLQARGIQ 273
Cdd:cd08575  161 LFESFSMTRCLLLYLALGYTgLLPFVPIKESFFEIPRPVIVLETFTLGEG-------ASIVAALLWWPNLFDHLRKRGIQ 233

                        250       260       270
                 ....*....|....*....|....*....|.
gi 148235333 274 VYLWVLNEESDYQRGLECGADGIMTDYPSNL 304
Cdd:cd08575  234 VYLWVLNDEEDFEEAFDLGADGVMTDSPTKL 264
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 41-308 2.22e-52

Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic phosphodiesterases UgpQ2 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized cytoplasmic phosphodiesterases which predominantly exist in bacteria. The prototype of this family is a putative cytoplasmic phosphodiesterase encoded by gene ulpQ2 (SCO1419) in the Streptomyces coelicolor genome. It is distantly related to the Escherichia coli cytoplasmic phosphodiesterases UgpQ that catalyzes the hydrolysis of glycerophosphodiesters at the inner side of the cytoplasmic membrane to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176504 [Multi-domain]  Cd Length: 249  Bit Score: 173.21  E-value: 2.22e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  41 HISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELPLYR-----EPL 115
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDagyhfTDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 116 EVTFFPghySSGSDRRIPQLEEVFQRFPHMPINVEIKEETPELVKQVSDLVKRYQRSERTVWASVKDPIMKLCQEENPDM 195
Cdd:cd08561   81 GGRTYP---YRGQGIRIPTLEELFEAFPDVRLNIEIKDDGPAAAAALADLIERYGAQDRVLVASFSDRVLRRFRRLCPRV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 196 PIMFTARRGLILLLLYYTGLLPFVPLRESVLEMhmpsiinrtyfpPNQLMRNRFLVflqdklmmrKSLFQHLQARGIQVY 275
Cdd:cd08561  158 ATSAGEGEVAAFVLASRLGLGSLYSPPYDALQI------------PVRYGGVPLVT---------PRFVRAAHAAGLEVH 216

                        250       260       270
                 ....*....|....*....|....*....|...
gi 148235333 276 LWVLNEESDYQRGLECGADGIMTDYPSNLRSFL 308
Cdd:cd08561  217 VWTVNDPAEMRRLLDLGVDGIITDRPDLLLEVL 249
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
42-310 4.54e-51

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 169.28  E-value: 4.54e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELplyrepleVTFFP 121
Cdd:COG0584    6 IAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAEL--------RQLDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 122 GHYSSGSDRRIPQLEEVFQRFPH-MPINVEIKEET---PELVKQVSDLVKRYQRSERTVWASVKDPIMKLCQEENPDMPI 197
Cdd:COG0584   78 GSGPDFAGERIPTLEEVLELVPGdVGLNIEIKSPPaaePDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 198 MFTARRGLILLLLYYTGLLP-FVPLRESVLEmhmpsiinrtyfppnqlmrnrflvflqdklmmrKSLFQHLQARGIQVYL 276
Cdd:COG0584  158 GLLVEELPADPLELARALGAdGVGPDYDLLT---------------------------------PELVAAAHAAGLKVHV 204

                        250       260       270
                 ....*....|....*....|....*....|....
gi 148235333 277 WVLNEESDYQRGLECGADGIMTDYPSNLRSFLQR 310
Cdd:COG0584  205 WTVNDPEEMRRLLDLGVDGIITDRPDLLRAVLRE 238
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 42-300 1.39e-36

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: 130.08  E-value: 1.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDlnllrqtghdvsicdityeelplyreplevtffp 121
Cdd:cd08556    2 IAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD---------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 122 ghyssgsdrrIPQLEEVFQRFP-HMPINVEIKEET--PELVKQVSDLVKRYQRSERTVWASVKDPIMKLCQEENPDMPIM 198
Cdd:cd08556   48 ----------IPTLEEVLELVKgGVGLNIELKEPTryPGLEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVPTG 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 199 FTARRGlillllyytgllPFVPLRESVLEMHMPSIINRTYfppnqlmrnrflvflqdkLMMRKSLFQHLQARGIQVYLWV 278
Cdd:cd08556  118 LLVDKP------------PLDPLLAELARALGADAVNPHY------------------KLLTPELVRAAHAAGLKVYVWT 167

                        250       260
                 ....*....|....*....|..
gi 148235333 279 LNEESDYQRGLECGADGIMTDY 300
Cdd:cd08556  168 VNDPEDARRLLALGVDGIITDD 189
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 44-301 1.09e-35

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: 129.44  E-value: 1.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333   44 HRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELPLYREPLEVTFfpgh 123
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSG---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  124 YSSGSDRRIPQLEEVFQRFPHMPINVEIK-------------EETPELVKQVSDLVKRYQRsERTVWASVKDP-IMKLCQ 189
Cdd:pfam03009  77 PLSGERVPFPTLEEVLEFDWDVGFNIEIKikpyveaiapeegLIVKDLLLSVDEILAKKAD-PRRVIFSSFNPdELKRLR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  190 EENPDMPIMFtarrglillllyytgllpfvpLRESVLEMHMPSIiNRTY---FPPNQLMRNRFLVFLQDKLMMRkslfqh 266
Cdd:pfam03009 156 ELAPKLPLVF---------------------LSSGRAYAEADLL-ERAAafaGAPALLGEVALVDEALPDLVKR------ 207

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 148235333  267 LQARGIQVYLWVLNEESDYQRGLECGADGIMTDYP 301
Cdd:pfam03009 208 AHARGLVVHVWTVNNEDEMKRLLELGVDGVITDRP 242
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 42-301 3.34e-34

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: 124.97  E-value: 3.34e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELplyrEPLEVTffp 121
Cdd:cd08579    2 IAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEEL----KKLTIG--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 122 ghySSGSDRRIPQLEEVFQRF--PHMPINVEIK---EETPELVKQVSDLVKRYQRSERTVWASVKDPIMKLCQEENPDMP 196
Cdd:cd08579   75 ---ENGHGAKIPSLDEYLALAkgLKQKLLIELKphgHDSPDLVEKFVKLYKQNLIENQHQVHSLDYRVIEKVKKLDPKIK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 197 IMFtarrglillllyytgllpFVPLresvlemhmpsiiNRTYFPpnqLMRNRFLVfLQDkLMMRKSLFQHLQARGIQVYL 276
Cdd:cd08579  152 TGY------------------ILPF-------------NIGNLP---KTNVDFYS-IEY-STLNKEFIRQAHQNGKKVYV 195

                        250       260
                 ....*....|....*....|....*
gi 148235333 277 WVLNEESDYQRGLECGADGIMTDYP 301
Cdd:cd08579  196 WTVNDPDDMQRYLAMGVDGIITDYP 220
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 42-301 2.37e-30

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: 114.96  E-value: 2.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELPLYREPLevtFFP 121
Cdd:cd08563    4 FAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGS---WFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 122 GHYssgSDRRIPQLEEVFQRFPH--MPINVEIKE---ETPELVKQVSDLVKRYQRSERTVWASVKDPIMKLCQEENPDMP 196
Cdd:cd08563   81 EKF---TGEKIPTLEEVLDLLKDkdLLLNIEIKTdviHYPGIEKKVLELVKEYNLEDRVIFSSFNHESLKRLKKLDPKIK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 197 IMFtarrglillllyytgllpfvpLRESVLEMH---MPSIINRTYFPPNQlmrnrflvFLQDKLMmrkslfQHLQARGIQ 273
Cdd:cd08563  158 LAL---------------------LYETGLQDPkdyAKKIGADSLHPDFK--------LLTEEVV------EELKKRGIP 202

                        250       260
                 ....*....|....*....|....*...
gi 148235333 274 VYLWVLNEESDYQRGLECGADGIMTDYP 301
Cdd:cd08563  203 VRLWTVNEEEDMKRLKDLGVDGIITNYP 230
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 42-302 7.91e-30

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: 113.56  E-value: 7.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELPLYReplevtFFP 121
Cdd:cd08582    2 IAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLD------IGS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 122 GHYSSGSDRRIPQLEEVFQRFPHMP--INVEIKEET--PELVKQVSDLVKRYQ-RSERTVWASVKDPIMKLCQEENPDMP 196
Cdd:cd08582   76 WKGESYKGEKVPTLEEYLAIVPKYGkkLFIEIKHPRrgPEAEEELLKLLKESGlLPEQIVIISFDAEALKRVRELAPTLE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 197 IMFtarrglillllyytgllpfvpLRESVLEMHMPSIINRTYfPPNQLMRNrfLVFLQDKLMMRKslfqhLQARGIQVYL 276
Cdd:cd08582  156 TLW---------------------LRNYKSPKEDPRPLAKSG-GAAGLDLS--YEKKLNPAFIKA-----LRDAGLKLNV 206

                        250       260
                 ....*....|....*....|....*.
gi 148235333 277 WVLNEESDYQRGLECGADGIMTDYPS 302
Cdd:cd08582  207 WTVDDAEDAKRLIELGVDSITTNRPG 232
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 42-301 5.96e-29

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: 111.24  E-value: 5.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELPLYREplevtffp 121
Cdd:cd08568    3 LGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHP-------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 122 ghyssgSDRRIPQLEEVFQRFPHMPI-NVEIKEetPELVKQVSDLVKRYQRSERTVWASVKDPIMKLCQEENPDMPI--M 198
Cdd:cd08568   75 ------GGELIPTLEEVFRALPNDAIiNVEIKD--IDAVEPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPDAKVglL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 199 FTARRGlillllyytgllpfVPLRESVLEMHMPSIINrtyfPPNQLmrnrflvFLQDKLMMRKSLFQHLQARGIQVYLWV 278
Cdd:cd08568  147 IGEEEE--------------GFSIPELHEKLKLYSLH----VPIDA-------IGYIGFEKFVELLRLLRKLGLKIVLWT 201

                        250       260
                 ....*....|....*....|...
gi 148235333 279 LNEESDYQRgLECGADGIMTDYP 301
Cdd:cd08568  202 VNDPELVPK-LKGLVDGVITDDV 223
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 44-301 8.66e-28

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: 108.94  E-value: 8.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  44 HRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELPLYREPLEV--TFFP 121
Cdd:cd08567    6 HRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDITRDPDGAWLPYEGPALYELTLAEikQLDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 122 GHYSSGSDR-------------RIPQLEEVFQRFPH-----MPINVEIK------EETP---ELVKQVSDLVKRYQRSER 174
Cdd:cd08567   86 GEKRPGSDYaklfpeqipvpgtRIPTLEEVFALVEKygnqkVRFNIETKsdpdrdILHPppeEFVDAVLAVIRKAGLEDR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 175 TVWASVKDPIMKLCQEENPDMPIMF-TARRglillllyytgllpfvplresvlemhmpsiinRTYFPPNQLMRNRFLVFL 253
Cdd:cd08567  166 VVLQSFDWRTLQEVRRLAPDIPTVAlTEET--------------------------------TLGNLPRAAKKLGADIWS 213

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 148235333 254 QDKLMMRKSLFQHLQARGIQVYLWVLNEESDYQRGLECGADGIMTDYP 301
Cdd:cd08567  214 PYFTLVTKELVDEAHALGLKVVPWTVNDPEDMARLIDLGVDGIITDYP 261
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 42-301 5.52e-23

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: 95.37  E-value: 5.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSIC-DITYEELPLYR---EPLEv 117
Cdd:cd08570    2 IGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIdDSTWDELSHLRtieEPHQ- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 118 tffpghyssgsdrRIPQLEEVFQRF-----PHMPINVEIKEETP---------ELVKQVSDLVKRYQRSERTVWASvkdP 183
Cdd:cd08570   81 -------------PMPTLKDVLEWLvehelPDVKLMLDIKRDNDpeilfkliaEMLAVKPDLDFWRERIILGLWHL---D 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 184 IMKLCQEENPDMP---IMFT---ARRglillllyytgllpFV--PLRESVLEMHMPSIInrTYFppnqlmRNRFLvflqd 255
Cdd:cd08570  145 FLKYGKEVLPGFPvfhIGFSldyARH--------------FLnySEKLVGISMHFVSLW--GPF------GQAFL----- 197

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148235333 256 klmmrkslfQHLQARGIQVYLWVLNEESDYQRGLECGADGIMTDYP 301
Cdd:cd08570  198 ---------PELKKNGKKVFVWTVNTEEDMRYAIRLGVDGVITDDP 234
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 42-309 3.65e-20

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: 88.14  E-value: 3.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTG--HDVSICDITYEELplyrEPLEV-T 118
Cdd:cd08601    4 IAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNieRPGPVKDYTLAEI----KQLDAgS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 119 FFPGHY-----SSGSDRRIPQLEEVFQRF-PHMPINVEIKEET--PELVKQVSDLVKRY------QRSERTVWASVKDPI 184
Cdd:cd08601   80 WFNKAYpeyarESYSGLKVPTLEEVIERYgGRANYYIETKSPDlyPGMEEKLLATLDKYglltdnLKNGQVIIQSFSKES 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 185 MKLCQEENPDMPIMFTARRGLILLLlyytgllpfvpLRESVLEMHMPSII---NRTYFPPnqlmrnrflvflqdklmmrk 261
Cdd:cd08601  160 LKKLHQLNPNIPLVQLLWYGEGAET-----------YDKWLDEIKEYAIGigpSIADADP-------------------- 208

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 148235333 262 SLFQHLQARGIQVYLWVLNEESDYQRGLECGADGIMTDYPSNLRSFLQ 309
Cdd:cd08601  209 WMVHLIHKKGLLVHPYTVNEKADMIRLINWGVDGMFTNYPDRLKEVLK 256
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 42-301 5.20e-18

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: 81.68  E-value: 5.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELPLYREPlevtffp 121
Cdd:cd08565    2 AGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLR------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 122 ghYSSGSdrRIPQLEEVFQRF--PHMPINVEIKEE-----TPELVKQVSDLVKRYQRSERTVWASVKDPIMKLCQEenpd 194
Cdd:cd08565   75 --DSFGE--KIPTLEEVLALFapSGLELHVEIKTDadgtpYPGAAALAAATLRRHGLLERSVLTSFDPAVLTEVRK---- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 195 mpiMFTARRGLILLLLYYTGLLPFVPLRESV--------LEMHMPSIIN--RTYFPPNQlmrnRFLVflqdklmmrkslf 264
Cdd:cd08565  147 ---HPGVRTLGSVDEDMLERLGGELPFLTATalkahivaVEQSLLAATWelVRAAVPGL----RLGV------------- 206

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148235333 265 qhlqargiqvylWVLNEESDYQRGLECGADGIMTDYP 301
Cdd:cd08565  207 ------------WTVNDDSLIRYWLACGVRQLTTDRP 231
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 42-301 5.87e-18

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: 81.92  E-value: 5.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELplyrEPLEVTFFP 121
Cdd:cd08573    2 IGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEEL----RKLNAAAKH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 122 GHYSSGSDRRIPQLEEVFQRFPH--MPINVEIKEETPELVKQVSDLVKRYQRSERTVWASVKDPIM--KLCQeENPDMPI 197
Cdd:cd08573   78 RLSSRFPGEKIPTLEEAVKECLEnnLRMIFDVKSNSSKLVDALKNLFKKYPGLYDKAIVCSFNPIViyKVRK-ADPKILT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 198 MFTARRGLILLLLYYTGLLPFVPLRESVLEM----HMPSIINRTYfppnqlmrnRFL---VFLQDKLMMRKSLFQHLQAR 270
Cdd:cd08573  157 GLTWRPWFLSYTDDEGGPRRKSGWKHFLYSMldviLEWSLHSWLP---------YFLgvsALLIHKDDISSAYVRYWRAR 227

                        250       260       270
                 ....*....|....*....|....*....|....
gi 148235333 271 GIQVYLWVLNEESD---YQRGLECgadGIMTDYP 301
Cdd:cd08573  228 GIRVIAWTVNTPTEkqyFAKTLNV---PYITDSL 258
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 42-301 1.30e-17

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: 80.81  E-value: 1.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERI-ESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEE---LPLYREPLEV 117
Cdd:cd08566    3 VAHRGGWGAGApENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEirkLRLKDGDGEV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 118 TffpghyssgsDRRIPQLEEVFQRFP-HMPINVEIKEETPElvkQVSDLVKRYQRSERTVwasVKDPIMKLCQE---ENP 193
Cdd:cd08566   83 T----------DEKVPTLEEALAWAKgKILLNLDLKDADLD---EVIALVKKHGALDQVI---FKSYSEEQAKElraLAP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 194 DMPIMftarrglillllyytgllPFVPLRESVLEMHMPSI--INRTYFPPNqlmrnrFLVFLQDKLMmrKSLFQHLQARG 271
Cdd:cd08566  147 EVMLM------------------PIVRDAEDLDEEEARAIdaLNLLAFEIT------FDDLDLPPLF--DELLRALGIRV 200

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 148235333 272 IQVYLWVLNE----------ESDYQRGLECGADGIMTDYP 301
Cdd:cd08566  201 WVNTLGDDDTagldralsdpREVWGELVDAGVDVIQTDRP 240
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 42-301 3.67e-16

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: 76.98  E-value: 3.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSH--DLNLLrqTGHDVSICDITYEELPL------YRE 113
Cdd:cd08580    4 VAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRpsDLKSL--TNGSGAVSAYTAAQLATlnagynFKP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 114 PlevtffPGHYSSGSDRRIPQLEEVFQRFPHMPINVEIKEETPE-LVKQVSDLVKRYQRSERTVWASVK-------DPIM 185
Cdd:cd08580   82 E------GGYPYRGKPVGIPTLEQVLRAFPDTPFILDMKSLPADpQAKAVARVLERENAWSRVRIYSTNadyqdalAPYP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 186 KLCQEENPDmpimfTARRGLILLLLYYTGLLPFVPLRESVLEMHMPSIINRTY------FPPNQLMRNRFLV--Flqdkl 257
Cdd:cd08580  156 QARLFESRD-----VTRTRLANVAMAHQCDLPPDSGAWAGFELRRKVTVVETFtlgegrSPVQATLWTPAAVdcF----- 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 148235333 258 mmRKSLFQHLQARGIqvylwvlNEESDYQRGLECGADGIMTDYP 301
Cdd:cd08580  226 --RRNSKVKIVLFGI-------NTADDYRLAKCLGADAVMVDSP 260
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 40-169 1.59e-14

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: 71.97  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  40 RHISHRG---GAGERIESTLEAFDNAVSNHTDLlELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELPLYReple 116
Cdd:cd08585    5 RPIAHRGlhdRDAGIPENSLSAFRAAAEAGYGI-ELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALR---- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148235333 117 vtffpghySSGSDRRIPQLEEVFQRFPH-MPINVEIK---EETPELVKQVSDLVKRY 169
Cdd:cd08585   80 --------LLGTDEHIPTLDEVLELVAGrVPLLIELKscgGGDGGLERRVLAALKDY 128
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 41-199 1.04e-13

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins. GDE5 is widely expressed in mammalian tissues, with highest expression in spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176514 [Multi-domain]  Cd Length: 293  Bit Score: 70.39  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  41 HISHRG---------GAGERiESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLL----------RQTGHDVSIC 101
Cdd:cd08572    2 VIGHRGlgknyasgsLAGIR-ENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISvseksktgsdEGELIEVPIH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 102 DITYEELPLYREPLEVTFFPGHYSSGS------------DRRIPQLEEVFQRFP-HMPINVEIKeeTPELVKQVSDlvKR 168
Cdd:cd08572   81 DLTLEQLKELGLQHISALKRKALTRKAkgpkpnpwgmdeHDPFPTLQEVLEQVPkDLGFNIEIK--YPQLLEDGEG--EL 156

                        170       180       190
                 ....*....|....*....|....*....|.
gi 148235333 169 YQRSERTVWAsvkDPIMKLCQEENPDMPIMF 199
Cdd:cd08572  157 TPYFERNAFV---DTILAVVFEHAGGRRIIF 184
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 41-152 2.44e-13

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: 69.25  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  41 HISHRG--------GAGERiESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNL-------LRQTGHD---VSICD 102
Cdd:cd08607    2 DVGHRGagnsytaaSAVVR-ENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLrvslkskGDSDRDDlleVPVKD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148235333 103 ITYEELPLYRePLEVTFFPG-HYSSGSD-------RRIPQLEEVFQRFP-HMPINVEIK 152
Cdd:cd08607   81 LTYEQLKLLK-LFHISALKVkEYKSVEEdedppehQPFPTLSDVLESVPeDVGFNIEIK 138
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 42-192 4.85e-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: 176523 [Multi-domain]  Cd Length: 229  Bit Score: 64.66  E-value: 4.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELPLYREPLEVTF-- 119
Cdd:cd08581    2 VAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVAEPARFgs 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 120 -FPGHyssgsdrRIPQLEEVFQ---RFPHMPINVEIKEETPEL--VKQVSDLVKR--YQRSERTVWASVKDPIMKLCQEE 191
Cdd:cd08581   82 rFAGE-------PLPSLAAVVQwlaQHPQVTLFVEIKTESLDRfgLERVVDKVLRalPAVAAQRVLISFDYDLLALAKQQ 154


                 .
gi 148235333 192 N 192
Cdd:cd08581  155 G 155
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 42-161 6.63e-12

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: 64.99  E-value: 6.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTghDVS--------------ICDITYEE 107
Cdd:cd08559    4 IAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTT--NVAehfpfrgrkdtgyfVIDFTLAE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148235333 108 L-------------PLYREPLEVTFfpghyssgsdrRIPQLEEVFQRFPHMP--------INVEIKEetPELVKQ 161
Cdd:cd08559   82 LktlragswfnqryPERAPSYYGGF-----------KIPTLEEVIELAQGLNkstgrnvgIYPETKH--PTFHKQ 143
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 44-309 5.04e-11

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: 62.10  E-value: 5.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  44 HRGG--AGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSH-------DLNLLRQTGHDVS-ICDITYEELPLYRE 113
Cdd:cd08564    9 HRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteddtnPDTSIQLDDSGFKnINDLSLDEITRLHF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 114 PLEVTFFPGHYSSGSDRRIPQLEEVFQRF-PHMPINVEIKEETPELVKQVSDLVKRYQRSERTVWASV--KDPImKLCQE 190
Cdd:cd08564   89 KQLFDEKPCGADEIKGEKIPTLEDVLVTFkDKLKYNIELKGREVGLGERVLNLVEKYGMILQVHFSSFlhYDRL-DLLKA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 191 ENPDmpimftarrglillllyyTGLLPFVPLRESVLEMHMPSIIN--RTYFPPNQLMRNRFLVflqdklmmrKSLFQHLQ 268
Cdd:cd08564  168 LRPN------------------KLNVPIALLFNEVKSPSPLDFLEqaKYYNATWVNFSYDFWT---------EEFVKKAH 220

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 148235333 269 ARGIQVYLW----VLNEESDYQRGLECGADGIMTDYPSNLRSFLQ 309
Cdd:cd08564  221 ENGLKVMTYfdepVNDNEEDYKVYLELGVDCICPNDPVLLVNFLK 265
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 42-301 5.49e-11

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: 61.47  E-value: 5.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVSICDITYEELPLyrepLEVtffp 121
Cdd:cd08562    2 IAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQ----LDA---- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 122 GHYSSGS--DRRIPQLEEV--FQRFPHMPINVEIK---EETPELVKQVSDLVKRY-QRSERTVWASVKDPIMKLCQEENP 193
Cdd:cd08562   74 GSWFSPEfaGEPIPTLADVleLARELGLGLNLEIKpdpGDEALTARVVAAALRELwPHASKLLLSSFSLEALRAARRAAP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 194 DMPIMFTARRGLILLllyytgllpfvplRESVLEMHMPSIInrtyfpPNQlmrnRFLVFLQDKLMMRKslfqhlqarGIQ 273
Cdd:cd08562  154 ELPLGLLFDTLPADW-------------LELLAALGAVSIH------LNY----RGLTEEQVKALKDA---------GYK 201

                        250       260
                 ....*....|....*....|....*...
gi 148235333 274 VYLWVLNEESDYQRGLECGADGIMTDYP 301
Cdd:cd08562  202 LLVYTVNDPARAAELLEWGVDAIFTDRP 229
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 42-169 4.92e-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: 57.83  E-value: 4.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGhdvSICDITYEE-LPLYREPLevtff 120
Cdd:cd08555    2 LSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTA---GILPPTLEEvLELIADYL----- 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148235333 121 pghyssgsdrripqleevFQRFPHMPINVEIKE---ETPELVKQVSDLVKRY 169
Cdd:cd08555   74 ------------------KNPDYTIILSLEIKQdspEYDEFLAKVLKELRVY 107
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 42-140 6.62e-10

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: 59.33  E-value: 6.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNL-------------LRQTGHDVSIcDITYEEL 108
Cdd:cd08600    4 IAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLdnvtnvaekfpdrKRKDGRYYVI-DFTLDEL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 148235333 109 PLyrepLEVT------------FFPGHYSSG-SDRRIPQLEEVFQ 140
Cdd:cd08600   83 KS----LSVTerfdiengkkvqVYPNRFPLWkSDFKIHTLEEEIE 123
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 42-178 4.63e-09

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: 56.60  E-value: 4.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGA--------------GERI--------ESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDVS 99
Cdd:cd08613   27 LAHRGLAqtfdregvendtctAERIdppthdylENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSGV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 100 ICDITYEELplyrEPLEVTFfpGHYSSGSDR---------RIPQLEEVFQRFPHMPINVEIKEETPELVKQVSDLVKRYQ 170
Cdd:cd08613  107 TRDHTMAEL----KTLDIGY--GYTADGGKTfpfrgkgvgMMPTLDEVFAAFPDRRFLINFKSDDAAEGELLAEKLATLP 180


                 ....*...
gi 148235333 171 RSERTVWA 178
Cdd:cd08613  181 RKRLQVLT 188
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 53-199 4.48e-08

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: 53.60  E-value: 4.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  53 ESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLnLLRQTGHDVSICDITYEE-LPLYREPLEVTFFPGHY---SSGS 128
Cdd:cd08606   24 ENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDF-LVSETGTDVPIHDLTLEQfLHLSRMKYTVDFKKKGFkgnSRGH 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 129 DRRIP--QLEEVFQRFP-HMPINVEIK---------EETPEL-------VKQVSDLVKRYQRSERTVWASVKDPIMKLCQ 189
Cdd:cd08606  103 SIQAPftTLEELLKKLPkSVGFNIELKypmlheaeeEEVAPVaielnafVDTVLEKVFDYGAGRNIIFSSFTPDICILLS 182

                        170
                 ....*....|
gi 148235333 190 EENPDMPIMF 199
Cdd:cd08606  183 LKQPGYPVLF 192
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 38-159 4.05e-07

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 50.32  E-value: 4.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  38 YCRHISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQT-GHDVsICDITYEELplyreple 116
Cdd:PRK09454   7 YPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSnGWGV-AGELTWQDL-------- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148235333 117 VTFFPGHYSSG--SDRRIPQLEEVFQRFPH--MPINVEIK------EETPELV 159
Cdd:PRK09454  78 AQLDAGSWFSAafAGEPLPTLSQVAARCRAhgMAANIEIKpttgreAETGRVV 130
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 42-200 4.37e-07

Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester phosphodiesterase-like proteins similar to mammalian GDE5; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized plant glycerophosphodiester phosphodiesterase (GP-PDE)-like proteins. Members in this family show very high sequence homology to mammalian glycerophosphodiester phosphodiesterase GDE5 and are distantly related to plant GP-PDEs.


Pssm-ID: 176547 [Multi-domain]  Cd Length: 282  Bit Score: 50.49  E-value: 4.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRG------------GAGERiESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTGHDV---SICDITYE 106
Cdd:cd08605    3 IGHRGlgmnrashqpsvGPGIR-ENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVERGGEVessRIRDLTLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333 107 ELPLYREPLEVTFFP--GHYSSGSDRR-----------IPQLEEVFQRFP-HMPINVEIKEETPELVKqvsdlvkryqrS 172
Cdd:cd08605   82 ELKALGPQAESTKTStvALYRKAKDPEpepwimdvedsIPTLEEVFSEVPpSLGFNIELKFGDDNKTE-----------A 150

                        170       180
                 ....*....|....*....|....*...
gi 148235333 173 ERTVwaSVKDPIMKLCQEENPDMPIMFT 200
Cdd:cd08605  151 EELV--RELRAILAVCKQHAPGRRIMFS 176
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 42-90 7.91e-07

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: 49.99  E-value: 7.91e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNL 90
Cdd:cd08602    4 IAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPEL 52
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 42-137 1.09e-06

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 49.67  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235333  42 ISHRGGAGERIESTLEAFDNAVSNHTDLLELDCHITKDGKVVVSHDLNLLRQTghDVS--------------ICDITYEE 107
Cdd:PRK11143  30 IAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVT--DVAerfpdrarkdgryyAIDFTLDE 107

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 148235333 108 LPLYR--EPLE------VTFFPGHYSSG-SDRRIPQLEE 137
Cdd:PRK11143 108 IKSLKftEGFDiengkkVQVYPGRFPMGkSDFRVHTFEE 146
GDPD_2 pfam13653
Glycerophosphoryl diester phosphodiesterase family; This family also includes ...
 273-301 1.55e-03

Glycerophosphoryl diester phosphodiesterase family; This family also includes glycerophosphoryl diester phosphodiesterases as well as agrocinopine synthase, the similarity to GDPD has been noted. This family appears to have weak but not significant matches to mammalian phospholipase C pfam00388, which suggests that this family may adopt a TIM barrel fold.


Pssm-ID: 433380 [Multi-domain]  Cd Length: 30  Bit Score: 35.55  E-value: 1.55e-03
                          10        20
                  ....*....|....*....|....*....
gi 148235333  273 QVYLWVLNEESDYQRGLECGADGIMTDYP 301
Cdd:pfam13653   1 KVRFWTIDNKAAWKELMRLGVDGLNTDDP 29
COG4885 COG4885
Uncharacterized conserved protein [Function unknown];
41-98 6.13e-03

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443913  Cd Length: 335  Bit Score: 38.07  E-value: 6.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148235333  41 HISHRGGAGERIESTLEAFDnavsNHTDLLELDCH-----ITKDGKVVVSHDLNLLRQTGHDV 98
Cdd:COG4885   66 RLEHRGGPTENVTVLVRAVD----AESGLLETTTTtdvgtVEGGGEVSVTTNLTVPREGGYRI 124
 
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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