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Conserved domains on  [gi|57524501|ref|NP_001004118|]
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lysophospholipase D GDPD1 [Danio rerio]

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 ...
 12-310 0e+00

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: 522.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  12 TGYVLTSAFLLKCPSLLHRRKREAFRSRHISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKR 91
Cdd:cd08612   1 GGYIATSYFLLRNPTLLHKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  92 STGINAYVADVAYADLPPYLCKLGVSFKRDCYC-EGGEDKRIPLLRDVFEAFPSTPVNIDIKVNNDTLIKKVSELVIQYK 170
Cdd:cd08612  81 SCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYCvPKGSDRRIPLLEEVFEAFPDTPINIDIKVENDELIKKVSDLVRKYK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 171 RQDLTVWGNSSNEIVKKCHKENPQIPILFSLPRVLLLLGLFYTGLLPFVPIKEQFLEIPMPSIVSKLKDPQRQTRSQRFI 250
Cdd:cd08612 161 REDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYFPKSMSRLNRFV 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 251 TWLADKVLMRKSLFDHLTGRGIQVYIWVLNDEEDFQRAFDLGATGVMTDYPTKLKEFMEK 310
Cdd:cd08612 241 LFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLREFLDK 300
 
Name Accession Description Interval E-value
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 12-310 0e+00

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: 522.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  12 TGYVLTSAFLLKCPSLLHRRKREAFRSRHISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKR 91
Cdd:cd08612   1 GGYIATSYFLLRNPTLLHKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  92 STGINAYVADVAYADLPPYLCKLGVSFKRDCYC-EGGEDKRIPLLRDVFEAFPSTPVNIDIKVNNDTLIKKVSELVIQYK 170
Cdd:cd08612  81 SCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYCvPKGSDRRIPLLEEVFEAFPDTPINIDIKVENDELIKKVSDLVRKYK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 171 RQDLTVWGNSSNEIVKKCHKENPQIPILFSLPRVLLLLGLFYTGLLPFVPIKEQFLEIPMPSIVSKLKDPQRQTRSQRFI 250
Cdd:cd08612 161 REDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYFPKSMSRLNRFV 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 251 TWLADKVLMRKSLFDHLTGRGIQVYIWVLNDEEDFQRAFDLGATGVMTDYPTKLKEFMEK 310
Cdd:cd08612 241 LFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLREFLDK 300
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
41-310 1.69e-51

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 170.05  E-value: 1.69e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLppylCKLGVSFKR 120
Cdd:COG0584   6 IAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAEL----RQLDAGSGP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 121 DcycEGGEdkRIPLLRDVFEAFPS-TPVNIDIKVNNDT---LIKKVSELVIQYKRQDLTVWGNSSNEIVKKCHKENPQIP 196
Cdd:COG0584  82 D---FAGE--RIPTLEEVLELVPGdVGLNIEIKSPPAAepdLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVP 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 197 ILFSLPRVLLLLGLFYTGLLP-FVPIKEQFLEipmPSIVSKLKDpqrqtrsqrfitwladkvlmrkslfdhltgRGIQVY 275
Cdd:COG0584 157 LGLLVEELPADPLELARALGAdGVGPDYDLLT---PELVAAAHA------------------------------AGLKVH 203

                       250       260       270
                ....*....|....*....|....*....|....*
gi 57524501 276 IWVLNDEEDFQRAFDLGATGVMTDYPTKLKEFMEK 310
Cdd:COG0584 204 VWTVNDPEEMRRLLDLGVDGIITDRPDLLRAVLRE 238
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 43-301 4.12e-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: 127.52  E-value: 4.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501    43 HRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLP--PYLCKLGVSFKr 120
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKrlDIGAGNSGPLS- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501   121 dcycegGEDKRIPLLRDVFEAFPSTPVNIDIKV-------------NNDTLIKKVSELVIQYKRQDLTVWGNSSNEIVKK 187
Cdd:pfam03009  80 ------GERVPFPTLEEVLEFDWDVGFNIEIKIkpyveaiapeeglIVKDLLLSVDEILAKKADPRRVIFSSFNPDELKR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501   188 CHKENPQIPILFslprvllllglfytgllpfvpikeqfleipmpsiVSKLKDPQRQTRSQRFITWL-ADKVLMRKSLFDH 266
Cdd:pfam03009 154 LRELAPKLPLVF----------------------------------LSSGRAYAEADLLERAAAFAgAPALLGEVALVDE 199

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 57524501   267 LTG--------RGIQVYIWVLNDEEDFQRAFDLGATGVMTDYP 301
Cdd:pfam03009 200 ALPdlvkrahaRGLVVHVWTVNNEDEMKRLLELGVDGVITDRP 242
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 39-107 2.55e-11

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 62.65  E-value: 2.55e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57524501   39 RHISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADL 107
Cdd:PRK09454   9 RIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDL 77
 
Name Accession Description Interval E-value
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 12-310 0e+00

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: 522.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  12 TGYVLTSAFLLKCPSLLHRRKREAFRSRHISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKR 91
Cdd:cd08612   1 GGYIATSYFLLRNPTLLHKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  92 STGINAYVADVAYADLPPYLCKLGVSFKRDCYC-EGGEDKRIPLLRDVFEAFPSTPVNIDIKVNNDTLIKKVSELVIQYK 170
Cdd:cd08612  81 SCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYCvPKGSDRRIPLLEEVFEAFPDTPINIDIKVENDELIKKVSDLVRKYK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 171 RQDLTVWGNSSNEIVKKCHKENPQIPILFSLPRVLLLLGLFYTGLLPFVPIKEQFLEIPMPSIVSKLKDPQRQTRSQRFI 250
Cdd:cd08612 161 REDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYFPKSMSRLNRFV 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 251 TWLADKVLMRKSLFDHLTGRGIQVYIWVLNDEEDFQRAFDLGATGVMTDYPTKLKEFMEK 310
Cdd:cd08612 241 LFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLREFLDK 300
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 39-304 2.29e-139

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: 394.66  E-value: 2.29e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  39 RHISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLPPYLCKLGVSF 118
Cdd:cd08575   2 LHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGYTF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 119 K--RDCYCEGGEDKRIPLLRDVFEAFPSTPVNIDIKVNN-DTLIKKVSELVIQYKRQDLTVWGNSSNEIVKKCHKENPQI 195
Cdd:cd08575  82 DggKTGYPRGGGDGRIPTLEEVFKAFPDTPINIDIKSPDaEELIAAVLDLLEKYKREDRTVWGSTNPEYLRALHPENPNL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 196 PILFSLPRVLLLLGL-FYTGLLPFVPIKEQFLEIPMPSIVSKLKDPQRQtrsqrfiTWLADKVLMRKSLFDHLTGRGIQV 274
Cdd:cd08575 162 FESFSMTRCLLLYLAlGYTGLLPFVPIKESFFEIPRPVIVLETFTLGEG-------ASIVAALLWWPNLFDHLRKRGIQV 234

                       250       260       270
                ....*....|....*....|....*....|
gi 57524501 275 YIWVLNDEEDFQRAFDLGATGVMTDYPTKL 304
Cdd:cd08575 235 YLWVLNDEEDFEEAFDLGADGVMTDSPTKL 264
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 40-308 4.52e-57

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: 184.77  E-value: 4.52e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  40 HISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLPPYlcKLGVSFK 119
Cdd:cd08561   1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRL--DAGYHFT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 120 RD---CYCEGGEDKRIPLLRDVFEAFPSTPVNIDIKVNNDTLIKKVSELVIQYKRQDLTVWGNSSNEIVKKCHKENPQIP 196
Cdd:cd08561  79 DDggrTYPYRGQGIRIPTLEELFEAFPDVRLNIEIKDDGPAAAAALADLIERYGAQDRVLVASFSDRVLRRFRRLCPRVA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 197 ILFSLPRVLLLLGLFYTGLLPFVPIKEQFLEIPMPSIVSKLKDPqrqtrsqRFITWLadkvlmrkslfdHLtgRGIQVYI 276
Cdd:cd08561 159 TSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTP-------RFVRAA------------HA--AGLEVHV 217

                       250       260       270
                ....*....|....*....|....*....|..
gi 57524501 277 WVLNDEEDFQRAFDLGATGVMTDYPTKLKEFM 308
Cdd:cd08561 218 WTVNDPAEMRRLLDLGVDGIITDRPDLLLEVL 249
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
41-310 1.69e-51

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 170.05  E-value: 1.69e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLppylCKLGVSFKR 120
Cdd:COG0584   6 IAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAEL----RQLDAGSGP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 121 DcycEGGEdkRIPLLRDVFEAFPS-TPVNIDIKVNNDT---LIKKVSELVIQYKRQDLTVWGNSSNEIVKKCHKENPQIP 196
Cdd:COG0584  82 D---FAGE--RIPTLEEVLELVPGdVGLNIEIKSPPAAepdLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVP 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 197 ILFSLPRVLLLLGLFYTGLLP-FVPIKEQFLEipmPSIVSKLKDpqrqtrsqrfitwladkvlmrkslfdhltgRGIQVY 275
Cdd:COG0584 157 LGLLVEELPADPLELARALGAdGVGPDYDLLT---PELVAAAHA------------------------------AGLKVH 203

                       250       260       270
                ....*....|....*....|....*....|....*
gi 57524501 276 IWVLNDEEDFQRAFDLGATGVMTDYPTKLKEFMEK 310
Cdd:COG0584 204 VWTVNDPEEMRRLLDLGVDGIITDRPDLLRAVLRE 238
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 41-301 1.07e-38

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: 136.53  E-value: 1.07e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADlppyLCKL--GVSF 118
Cdd:cd08563   4 FAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEE----LKKLdaGSWF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 119 KRDCYCEggedkRIPLLRDVFEAFPSTPVNIDIKVNNDT-----LIKKVSELVIQYKRQDLTVWGNSSNEIVKKCHKENP 193
Cdd:cd08563  80 DEKFTGE-----KIPTLEEVLDLLKDKDLLLNIEIKTDVihypgIEKKVLELVKEYNLEDRVIFSSFNHESLKRLKKLDP 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 194 QIpilfslprvllllglfYTGLL---PFVPIKEQFLEIPMPSIvsklkdpqrqtRSQRFITWLADKVLMRKslfdhltgR 270
Cdd:cd08563 155 KI----------------KLALLyetGLQDPKDYAKKIGADSL-----------HPDFKLLTEEVVEELKK--------R 199

                       250       260       270
                ....*....|....*....|....*....|.
gi 57524501 271 GIQVYIWVLNDEEDFQRAFDLGATGVMTDYP 301
Cdd:cd08563 200 GIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 41-300 9.73e-38

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: 132.77  E-value: 9.73e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDsslkrstginayvadvayadlppylcklgvsfkr 120
Cdd:cd08556   2 IAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD---------------------------------- 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 121 dcyceggedkrIPLLRDVFEAFPS-TPVNIDIKVNN--DTLIKKVSELVIQYKRQDLTVWGNSSNEIVKKCHKENPQIPi 197
Cdd:cd08556  48 -----------IPTLEEVLELVKGgVGLNIELKEPTryPGLEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVP- 115

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 198 lfslprvllllglfyTGLLpFVPIKEQFLEipmpsivsklkdpQRQTRSQRFITWLADKVLMRKSLFDHLTGRGIQVYIW 277
Cdd:cd08556 116 ---------------TGLL-VDKPPLDPLL-------------AELARALGADAVNPHYKLLTPELVRAAHAAGLKVYVW 166

                       250       260
                ....*....|....*....|...
gi 57524501 278 VLNDEEDFQRAFDLGATGVMTDY 300
Cdd:cd08556 167 TVNDPEDARRLLALGVDGIITDD 189
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 43-301 4.12e-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: 127.52  E-value: 4.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501    43 HRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLP--PYLCKLGVSFKr 120
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKrlDIGAGNSGPLS- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501   121 dcycegGEDKRIPLLRDVFEAFPSTPVNIDIKV-------------NNDTLIKKVSELVIQYKRQDLTVWGNSSNEIVKK 187
Cdd:pfam03009  80 ------GERVPFPTLEEVLEFDWDVGFNIEIKIkpyveaiapeeglIVKDLLLSVDEILAKKADPRRVIFSSFNPDELKR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501   188 CHKENPQIPILFslprvllllglfytgllpfvpikeqfleipmpsiVSKLKDPQRQTRSQRFITWL-ADKVLMRKSLFDH 266
Cdd:pfam03009 154 LRELAPKLPLVF----------------------------------LSSGRAYAEADLLERAAAFAgAPALLGEVALVDE 199

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 57524501   267 LTG--------RGIQVYIWVLNDEEDFQRAFDLGATGVMTDYP 301
Cdd:pfam03009 200 ALPdlvkrahaRGLVVHVWTVNNEDEMKRLLELGVDGVITDRP 242
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 41-301 1.09e-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: 125.74  E-value: 1.09e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLPpylcKLGVSfkr 120
Cdd:cd08579   2 IAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELK----KLTIG--- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 121 dcycEGGEDKRIPLLRDVFEAF--PSTPVNIDIKV---NNDTLIKKVSELVIQYKRQDLTVWGNSSNEIVKKCHKENPQI 195
Cdd:cd08579  75 ----ENGHGAKIPSLDEYLALAkgLKQKLLIELKPhghDSPDLVEKFVKLYKQNLIENQHQVHSLDYRVIEKVKKLDPKI 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 196 PILFSLPrvllllglFYTGLLPFVPIkeQFLEIPMPSIvsklkdpqrqtrSQRFItwlaDKVlmrkslfdHLTGRgiQVY 275
Cdd:cd08579 151 KTGYILP--------FNIGNLPKTNV--DFYSIEYSTL------------NKEFI----RQA--------HQNGK--KVY 194

                       250       260
                ....*....|....*....|....*.
gi 57524501 276 IWVLNDEEDFQRAFDLGATGVMTDYP 301
Cdd:cd08579 195 VWTVNDPDDMQRYLAMGVDGIITDYP 220
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 41-301 6.03e-29

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


Pssm-ID: 176512 [Multi-domain]  Cd Length: 234  Bit Score: 111.16  E-value: 6.03e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYadlPPYLCKLgvsfkr 120
Cdd:cd08570   2 IGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDST---WDELSHL------ 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 121 dcYCEGGEDKRIPLLRDVFEAF-----PSTPVNIDIKVNNDT--LIKKVSELV-----IQYKRQDLtVWGNSSNEIVKKC 188
Cdd:cd08570  73 --RTIEEPHQPMPTLKDVLEWLvehelPDVKLMLDIKRDNDPeiLFKLIAEMLavkpdLDFWRERI-ILGLWHLDFLKYG 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 189 HKENPQIPIlfslprvllllglFYTGLlpFVPIKEQFleipmpsivskLKDPQRQTR-SQRFI-TWLADKVLMRKSLFDH 266
Cdd:cd08570 150 KEVLPGFPV-------------FHIGF--SLDYARHF-----------LNYSEKLVGiSMHFVsLWGPFGQAFLPELKKN 203

                       250       260       270
                ....*....|....*....|....*....|....*
gi 57524501 267 ltgrGIQVYIWVLNDEEDFQRAFDLGATGVMTDYP 301
Cdd:cd08570 204 ----GKKVFVWTVNTEEDMRYAIRLGVDGVITDDP 234
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 41-304 3.12e-28

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: 108.92  E-value: 3.12e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLPpylcKLGVsfkr 120
Cdd:cd08568   3 LGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELK----KLHP---- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 121 dcyceggEDKRIPLLRDVFEAFPSTP-VNIDIK-VNNdtlIKKVSELVIQYKRQDLTVWGNSSNEIVKKCHKENP--QIP 196
Cdd:cd08568  75 -------GGELIPTLEEVFRALPNDAiINVEIKdIDA---VEPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPdaKVG 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 197 ILFSLPRVLLLLGLFYTGLLPF---VPIK-------EQFLEipmpsivsklkdpqrqtrsqrFITWLadkvlmRKslfdh 266
Cdd:cd08568 145 LLIGEEEEGFSIPELHEKLKLYslhVPIDaigyigfEKFVE---------------------LLRLL------RK----- 192

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 57524501 267 ltgRGIQVYIWVLNDEEDFQRAFDLgATGVMTDYPTKL 304
Cdd:cd08568 193 ---LGLKIVLWTVNDPELVPKLKGL-VDGVITDDVEKI 226
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 41-302 6.69e-27

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: 105.47  E-value: 6.69e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLPpylcKLGVSFKR 120
Cdd:cd08582   2 IAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELR----KLDIGSWK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 121 DcycEGGEDKRIPLLRDVFEAFPSTPVNIDIKVNNDTLIKKVSELVIQykrqdltvwgnssneIVKKCHKENPQIPIL-F 199
Cdd:cd08582  78 G---ESYKGEKVPTLEEYLAIVPKYGKKLFIEIKHPRRGPEAEEELLK---------------LLKESGLLPEQIVIIsF 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 200 SLPRVLLllglfytgllpfvpIKEQFLEIPMPSIvsklkdpqRQTRSQRFITWLADK------------VLMRKSLFDHL 267
Cdd:cd08582 140 DAEALKR--------------VRELAPTLETLWL--------RNYKSPKEDPRPLAKsggaagldlsyeKKLNPAFIKAL 197

                       250       260       270
                ....*....|....*....|....*....|....*
gi 57524501 268 TGRGIQVYIWVLNDEEDFQRAFDLGATGVMTDYPT 302
Cdd:cd08582 198 RDAGLKLNVWTVDDAEDAKRLIELGVDSITTNRPG 232
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 41-301 1.21e-26

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: 105.47  E-value: 1.21e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSL----------KRSTGINAYVADVAYADLPPY 110
Cdd:cd08567   4 QGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLnpditrdpdgAWLPYEGPALYELTLAEIKQL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 111 LCklGVSFKRDCYCEGGEDK------RIPLLRDVFEAFPS---TPV--NIDIKVNNDTLI---------KKVSELVIQYK 170
Cdd:cd08567  84 DV--GEKRPGSDYAKLFPEQipvpgtRIPTLEEVFALVEKygnQKVrfNIETKSDPDRDIlhpppeefvDAVLAVIRKAG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 171 RQDLTV-----WgnssnEIVKKCHKENPQIPI--LFSLPRvllllglfytgllpfvpikeqfleipmpsivskLKDPQRQ 243
Cdd:cd08567 162 LEDRVVlqsfdW-----RTLQEVRRLAPDIPTvaLTEETT---------------------------------LGNLPRA 203

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 57524501 244 TRSQRFITWLADKVLMRKSLFDHLTGRGIQVYIWVLNDEEDFQRAFDLGATGVMTDYP 301
Cdd:cd08567 204 AKKLGADIWSPYFTLVTKELVDEAHALGLKVVPWTVNDPEDMARLIDLGVDGIITDYP 261
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 41-306 2.04e-24

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: 99.31  E-value: 2.04e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINA--YVADVAYADLPpylcKLGV-S 117
Cdd:cd08601   4 IAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIERpgPVKDYTLAEIK----QLDAgS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 118 FKRDCYCEGGEDK----RIPLLRDVFEAF-PSTPVNIDIKVNN------DTLIKKVSE--LVIQYKRQDLTVWGNSSNEI 184
Cdd:cd08601  80 WFNKAYPEYARESysglKVPTLEEVIERYgGRANYYIETKSPDlypgmeEKLLATLDKygLLTDNLKNGQVIIQSFSKES 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 185 VKKCHKENPQIPILFSLPrvLLLLGLFYTGLLPFvpIKEqFLEIPMPSIvsKLKDPqrqtrsqrfitWLADkvLMRKslf 264
Cdd:cd08601 160 LKKLHQLNPNIPLVQLLW--YGEGAETYDKWLDE--IKE-YAIGIGPSI--ADADP-----------WMVH--LIHK--- 216

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 57524501 265 dhltgRGIQVYIWVLNDEEDFQRAFDLGATGVMTDYPTKLKE 306
Cdd:cd08601 217 -----KGLLVHPYTVNEKADMIRLINWGVDGMFTNYPDRLKE 253
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 41-301 4.43e-23

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: 95.45  E-value: 4.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENL-ENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLppylcklgvsfk 119
Cdd:cd08566   3 VAHRGGWGAGApENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEI------------ 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 120 RDCYCEGGEDK----RIPLLRDVFEAFPS-TPVNIDIKvnnDTLIKKVSELVIQYKRQDLTVWGNSSNEIVKKCHKENPQ 194
Cdd:cd08566  71 RKLRLKDGDGEvtdeKVPTLEEALAWAKGkILLNLDLK---DADLDEVIALVKKHGALDQVIFKSYSEEQAKELRALAPE 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 195 IPIlfsLPRVLLLLGLFYTGLLPFVPIKeqfleiPMPSIVSKLKDPQRQtrsqrfitwLADKVLMR---KSLFDHLTGRG 271
Cdd:cd08566 148 VML---MPIVRDAEDLDEEEARAIDALN------LLAFEITFDDLDLPP---------LFDELLRAlgiRVWVNTLGDDD 209

                       250       260       270
                ....*....|....*....|....*....|.
gi 57524501 272 IQVYIWVLND-EEDFQRAFDLGATGVMTDYP 301
Cdd:cd08566 210 TAGLDRALSDpREVWGELVDAGVDVIQTDRP 240
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 35-170 3.84e-21

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: 90.07  E-value: 3.84e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  35 AFRSRHISHRGGAGENL---ENTMAAFKHAVKLGTDmLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLPpyL 111
Cdd:cd08585   1 WLKDRPIAHRGLHDRDAgipENSLSAFRAAAEAGYG-IELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELR--A 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57524501 112 CKLgvsfkrdcyceGGEDKRIPLLRDVFEAFP-STPVNIDIKV---NNDTLIKKVSELVIQYK 170
Cdd:cd08585  78 LRL-----------LGTDEHIPTLDEVLELVAgRVPLLIELKScggGDGGLERRVLAALKDYK 129
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 41-302 4.54e-21

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: 89.77  E-value: 4.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLPPYlcKLGVSFkr 120
Cdd:cd08565   2 AGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKAL--RLRDSF-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 121 dcyceggeDKRIPLLRDVFEAFPSTPV--NIDIKVNNDT-----LIKKVSELVIQYKRQDLTVWGNSSNEIVKKCHKeNP 193
Cdd:cd08565  78 --------GEKIPTLEEVLALFAPSGLelHVEIKTDADGtpypgAAALAAATLRRHGLLERSVLTSFDPAVLTEVRK-HP 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 194 QIPILFSLPRvllLLGLFYTGLLPFVPIKEQFLEipmpsIVSKLKDPQRQTRSQRFITWLADKVLmrkslfdhltgrgiq 273
Cdd:cd08565 149 GVRTLGSVDE---DMLERLGGELPFLTATALKAH-----IVAVEQSLLAATWELVRAAVPGLRLG--------------- 205

                       250       260
                ....*....|....*....|....*....
gi 57524501 274 vyIWVLNDEEDFQRAFDLGATGVMTDYPT 302
Cdd:cd08565 206 --VWTVNDDSLIRYWLACGVRQLTTDRPD 232
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 41-301 2.57e-20

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: 87.66  E-value: 2.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLPpylcKL------ 114
Cdd:cd08562   2 IAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELA----QLdagswf 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 115 GVSFKrdcycegGEdkRIPLLRDVFEAFPSTP--VNIDIKVNNDTLiKKVSELVIQYKRQdlTVWGNS-------SNEIV 185
Cdd:cd08562  78 SPEFA-------GE--PIPTLADVLELARELGlgLNLEIKPDPGDE-ALTARVVAAALRE--LWPHASklllssfSLEAL 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 186 KKCHKENPQIPIlfslprvllllglfytGLLpfvpikeqFLEIPmpsivsklKDPQRQTRS---------QRFITwlADK 256
Cdd:cd08562 146 RAARRAAPELPL----------------GLL--------FDTLP--------ADWLELLAAlgavsihlnYRGLT--EEQ 191

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 57524501 257 VLMrkslfdhLTGRGIQVYIWVLNDEEDFQRAFDLGATGVMTDYP 301
Cdd:cd08562 192 VKA-------LKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 41-166 6.56e-17

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: 78.91  E-value: 6.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLPpylcKL--GVSF 118
Cdd:cd08580   4 VAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLA----TLnaGYNF 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 57524501 119 KRDC-YCEGGEDKRIPLLRDVFEAFPSTPVNIDIK-VNNDTLIKKVSELV 166
Cdd:cd08580  80 KPEGgYPYRGKPVGIPTLEQVLRAFPDTPFILDMKsLPADPQAKAVARVL 129
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 43-307 4.58e-15

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: 73.66  E-value: 4.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  43 HRGGAGENL--ENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLH--------DSSLKRSTGINAYVADVAYADLPPYLC 112
Cdd:cd08564   9 HRGAGCSTLypENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteddtnpDTSIQLDDSGFKNINDLSLDEITRLHF 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 113 KLGVSFKRdCYCEGGEDKRIPLLRDVFEAF-PSTPVNIDIKVNNDTLIKKVSELVIQYKRQdLTVWGNSSNeivkkcHKE 191
Cdd:cd08564  89 KQLFDEKP-CGADEIKGEKIPTLEDVLVTFkDKLKYNIELKGREVGLGERVLNLVEKYGMI-LQVHFSSFL------HYD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 192 npqiPILFSLPRVLLLLGlfytgllpfVPIKEQFLEIPMPS---IVSKLKDPQRQTRSQRFITWLADKVlmrKSLFDHlt 268
Cdd:cd08564 161 ----RLDLLKALRPNKLN---------VPIALLFNEVKSPSpldFLEQAKYYNATWVNFSYDFWTEEFV---KKAHEN-- 222

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 57524501 269 grGIQVYIW----VLNDEEDFQRAFDLGATGVMTDYPTKLKEF 307
Cdd:cd08564 223 --GLKVMTYfdepVNDNEEDYKVYLELGVDCICPNDPVLLVNF 263
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 41-155 9.94e-15

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: 71.98  E-value: 9.94e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLPPYLCKLGVSFkR 120
Cdd:cd08581   2 VAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVAEPARF-G 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 57524501 121 DCYceggEDKRIPLLRDVFEA---FPSTPVNIDIKVNN 155
Cdd:cd08581  81 SRF----AGEPLPSLAAVVQWlaqHPQVTLFVEIKTES 114
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 41-169 1.85e-14

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: 71.91  E-value: 1.85e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADlppyLCKLGVSFKR 120
Cdd:cd08573   2 IGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEE----LRKLNAAAKH 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 57524501 121 DcYCEGGEDKRIPLLRD-VFEAFPS-TPVNIDIKVNNDTLIKKVSELVIQY 169
Cdd:cd08573  78 R-LSSRFPGEKIPTLEEaVKECLENnLRMIFDVKSNSSKLVDALKNLFKKY 127
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 40-152 2.19e-14

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: 72.31  E-value: 2.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  40 HISHRGgAGEN---------LENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHD----------SSLKRSTGINAYVA 100
Cdd:cd08572   2 VIGHRG-LGKNyasgslagiRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDftisvsekskTGSDEGELIEVPIH 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57524501 101 DVAYADL-------------PPYLCKLGVSFKRDCYCEggEDKRIPLLRDVFEAFP-STPVNIDIK 152
Cdd:cd08572  81 DLTLEQLkelglqhisalkrKALTRKAKGPKPNPWGMD--EHDPFPTLQEVLEQVPkDLGFNIEIK 144
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 51-178 4.28e-13

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: 68.54  E-value: 4.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  51 LENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADLPPYlcKLGVSFKRDcyceGGED- 129
Cdd:cd08613  59 LENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELKTL--DIGYGYTAD----GGKTf 132

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 130 -------KRIPLLRDVFEAFPSTPVNIDIKVNN----DTLIKKVSELViQYKRQDLTVWG 178
Cdd:cd08613 133 pfrgkgvGMMPTLDEVFAAFPDRRFLINFKSDDaaegELLAEKLATLP-RKRLQVLTVYG 191
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 40-152 1.37e-11

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: 63.85  E-value: 1.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  40 HISHRGgAGENL--------ENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHD----SSLKRSTG------INAYVAD 101
Cdd:cd08607   2 DVGHRG-AGNSYtaasavvrENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDftlrVSLKSKGDsdrddlLEVPVKD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57524501 102 VAYADLPpyLCKL----------GVSFKRDCYCEggEDKRIPLLRDVFEAFP-STPVNIDIK 152
Cdd:cd08607  81 LTYEQLK--LLKLfhisalkvkeYKSVEEDEDPP--EHQPFPTLSDVLESVPeDVGFNIEIK 138
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 39-107 2.55e-11

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 62.65  E-value: 2.55e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57524501   39 RHISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGINAYVADVAYADL 107
Cdd:PRK09454   9 RIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDL 77
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 41-95 3.62e-11

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: 62.68  E-value: 3.62e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGI 95
Cdd:cd08559   4 IAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNV 58
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 41-94 5.42e-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: 5.42e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTG 94
Cdd:cd08555   2 LSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTA 55
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 41-93 6.61e-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: 56.25  E-value: 6.61e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRST 93
Cdd:cd08600   4 IAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVT 56
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 41-103 6.00e-08

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 53.52  E-value: 6.00e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57524501   41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRstginayVADVA 103
Cdd:PRK11143  30 IAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDR-------VTDVA 85
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 41-103 5.70e-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: 50.37  E-value: 5.70e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTginayvaDVA 103
Cdd:cd08602   4 IAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTT-------DVA 59
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 41-95 6.27e-07

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE6 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE6 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 4 (GDPD4)) and their metazoan homologs. Mammalian GDE6 is a transmembrane protein predominantly expressed in the spermatocytes of testis. Although the specific physiological function of mammalian GDE6 has not been elucidated, its different pattern of tissue distribution suggests it might play a critical role in the completion of meiosis during male germ cell differentiation.


Pssm-ID: 176552 [Multi-domain]  Cd Length: 316  Bit Score: 50.26  E-value: 6.27e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGI 95
Cdd:cd08610  26 IGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNI 80
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 41-303 3.81e-06

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: 47.29  E-value: 3.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGGA--GENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLH--DSSLKRSTGinayvadvayadLPPYLCKLGV 116
Cdd:cd08583   2 IAHAMGGidGKTYTNSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHswDESLLKQLG------------LPTSKNTKPL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 117 SFKrdcyceggEDKRIPLLRDVfeafpsTPVNID-----IKVNNDTLIkkvselVIQYKRQDLTVWGNSSNEIVKKCHKE 191
Cdd:cd08583  70 SYE--------EFKSKKIYGKY------TPMDFKdvidlLKKYPDVYI------VTDTKQDDDNDIKKLYEYIVKEAKEV 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501 192 NPQIpilfsLPRVllllglfytglLPFVPIKEQFLEI----PMPSIVSKL--KDPQRQTRSQRFIT-----------WLA 254
Cdd:cd08583 130 DPDL-----LDRV-----------IPQIYNEEMYEAImsiyPFKSVIYTLyrQDSIRLDEIIAFCYengikavtiskNYV 193

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 57524501 255 DKVLMRKslfdhLTGRGIQVYIWVLNDEEDFQRAFDLGATGVMTDYPTK 303
Cdd:cd08583 194 NDKLIEK-----LNKAGIYVYVYTINDLKDAQEYKKLGVYGIYTDFLTE 237
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 41-152 1.31e-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: 45.90  E-value: 1.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGgAGENL---------ENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRsTGINAYVADVAyadLPPYL 111
Cdd:cd08606   5 IGHRG-LGKNTaerkslqlgENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSE-TGTDVPIHDLT---LEQFL 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 57524501 112 ----CKLGVSFKRDCYCEGGEDKRI----PLLRDVFEAFP-STPVNIDIK 152
Cdd:cd08606  80 hlsrMKYTVDFKKKGFKGNSRGHSIqapfTTLEELLKKLPkSVGFNIELK 129
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 41-102 3.99e-05

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2, GDE3, GDE6-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase domain-containing protein subtype 5 (GDE2), subtype 2 (GDE3), subtype 1 (GDE6), and their eukaryotic homologs. Mammalian GDE2, GDE3, and GDE6 show very high sequence similarity to each other and have been classified into the same family. Although they are all transmembrane proteins, based on different pattern of tissue distribution, these enzymes might display diverse cellular functions. Mammalian GDE2 is primarily expressed in mature neurons. It selectively hydrolyzes glycerophosphocholine (GPC) and mainly functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE3 is specifically expressed in bone tissues and spleen. It selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate inositol 1-phosphate (Ins1P) and glycerol and functions as an inducer of osteoblast differentiation. Mammalian GDE6 is predominantly expressed in the spermatocytes of testis, and its specific physiological function has not been elucidated yet.


Pssm-ID: 176516 [Multi-domain]  Cd Length: 252  Bit Score: 44.22  E-value: 3.99e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGinayVADV 102
Cdd:cd08574   5 IGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTN----VADV 62
GDPD_2 pfam13653
Glycerophosphoryl diester phosphodiesterase family; This family also includes ...
 273-302 1.12e-04

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: 38.63  E-value: 1.12e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 57524501   273 QVYIWVLNDEEDFQRAFDLGATGVMTDYPT 302
Cdd:pfam13653   1 KVRFWTIDNKAAWKELMRLGVDGLNTDDPE 30
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 41-157 5.59e-04

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: 40.86  E-value: 5.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524501  41 ISHRGgAGENL------------ENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDS--SLKRSTGINAY-VADVAYA 105
Cdd:cd08605   3 IGHRG-LGMNRashqpsvgpgirENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDfiVVERGGEVESSrIRDLTLA 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57524501 106 DLPPYLCKLGVSF--KRDCYCEGGE----------DKRIPLLRDVFEAFP-STPVNIDIKVNNDT 157
Cdd:cd08605  82 ELKALGPQAESTKtsTVALYRKAKDpepepwimdvEDSIPTLEEVFSEVPpSLGFNIELKFGDDN 146
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 41-95 1.57e-03

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE3 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE3 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 2 (GDPD2), Osteoblast differentiation promoting factor) and their metazoan homologs. Mammalian GDE3 is a transmembrane protein specifically expressed in bone tissues and spleen. It is a mammalian homolog of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Mammalian GDE3 has been characterized as glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate inositol 1-phosphate (Ins1P) and glycerol. Mammalian GDE3 functions as an inducer of osteoblast differentiation. It also plays a critical role for actin cytoskeletal modulation. The catalytic activity of GDPD domain is essential for mammalian GDE3 cellular function.


Pssm-ID: 176551 [Multi-domain]  Cd Length: 315  Bit Score: 39.52  E-value: 1.57e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 57524501  41 ISHRGGAGENLENTMAAFKHAVKLGTDMLELDCHLTKDEQVVVLHDSSLKRSTGI 95
Cdd:cd08609  30 VGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNV 84
 
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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