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Conserved domains on  [gi|15232292|ref|NP_188688|]
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SHV3-like 3 [Arabidopsis thaliana]

Protein Classification

glycerophosphodiester phosphodiesterase family protein( domain architecture ID 10171244)

glycerophosphodiester phosphodiesterase (GDPD) family protein similar to Arabidopsis thaliana glycerophosphoryl diester phosphodiesterase-like proteins that may play important roles in cell wall organization

EC:  3.1.4.-
Gene Ontology:  GO:0008081|GO:0006629

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 33-319 7.37e-176

Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 1 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play an important role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This family includes domain I, the first GDPD domain of SHV3 and SVLs.


:

Pssm-ID: 176545  Cd Length: 299  Bit Score: 504.61  E-value: 7.37e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292  33 PAVIARGGFSGMFPDSSIQAYQLVNITTSPDVMLWCDLQLTKDGVGICFPNLKLDNGSNVIRIDP-----------HYKE 101
Cdd:cd08603   1 PLVIARGGFSGLFPDSSLFAYQFAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPkrkktysvngvSTKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 102 RFSVDFTWKELSDVKLAQGVVSRPYIFDDVSSILAIEEVAKLTA-SGLWLNIQDSAFYAKHNLSMRNSVVSLSRRLKVNF 180
Cdd:cd08603  81 WFSVDFTLAELQQVTLIQGIFSRTPIFDGQYPISTVEDVVTLAKpEGLWLNVQHDAFYQQHNLSMSSYLLSLSKTVKVDY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 181 ISSPGISFLKSMKNSVKPTVTKLIFRFLKQEHIEPFTNQSYGSLAKNLSYIRTFSSGILVPKSYIWPVDSALYLQPHTSL 260
Cdd:cd08603 161 ISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSILKNLTFIKTFASGILVPKSYIWPVDSDQYLQPATSL 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15232292 261 VTDAHKEGLQVFASEFANDFVIAYNYSYDPTAEYLSFIDNGNFSVDGFLSDFPVTPYRA 319
Cdd:cd08603 241 VQDAHKAGLEVYASGFANDFDISYNYSYDPVAEYLSFVGNGNFSVDGVLSDFPITASEA 299
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 337-644 4.08e-161

Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 2 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play important an role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This CD includes domain II (the second GDPD domain of SHV3 and SVLs), which is necessary for SHV3 function.


:

Pssm-ID: 176546  Cd Length: 300  Bit Score: 466.81  E-value: 4.08e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 337 ITIISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNVIETSFRNLSSVVSEINPrRSGI 416
Cdd:cd08604   1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSKFSNRATTVPEIGS-TSGI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 417 YTFSLTMSQIQTLKPTISNLEKDSGLFRNPRNNKAGKFLTLSEFLFLPNRYsSLLGLLIEVENAAYLVEHQGISVVDAVL 496
Cdd:cd08604  80 FTFDLTWSEIQTLKPAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNK-SLSGVLINVENAAYLAEKKGLDVVDAVL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 497 DELKRATTQQNktSARTILIQSTDKSVLMKFKEKnkmNHDELVYRVDDNIRDVADSAIKDIKNFAGSIVISKKSVFPYKG 576
Cdd:cd08604 159 DALTNAGYDNQ--TAQKVLIQSTDSSVLAAFKKQ---ISYERVYVVDETIRDASDSSIEEIKKFADAVVIDRGSVFPVST 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232292 577 FIILEKeTNIASKLKSNGLRVYVERFSNECVTHAFDFYDDPTLEIDSFVRDVQIDGIITDFPATTARY 644
Cdd:cd08604 234 SFLTRQ-TNVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSYVQGAGVDGFITEFPATAARY 300
 
Name Accession Description Interval E-value
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 33-319 7.37e-176

Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 1 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play an important role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This family includes domain I, the first GDPD domain of SHV3 and SVLs.


Pssm-ID: 176545  Cd Length: 299  Bit Score: 504.61  E-value: 7.37e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292  33 PAVIARGGFSGMFPDSSIQAYQLVNITTSPDVMLWCDLQLTKDGVGICFPNLKLDNGSNVIRIDP-----------HYKE 101
Cdd:cd08603   1 PLVIARGGFSGLFPDSSLFAYQFAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPkrkktysvngvSTKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 102 RFSVDFTWKELSDVKLAQGVVSRPYIFDDVSSILAIEEVAKLTA-SGLWLNIQDSAFYAKHNLSMRNSVVSLSRRLKVNF 180
Cdd:cd08603  81 WFSVDFTLAELQQVTLIQGIFSRTPIFDGQYPISTVEDVVTLAKpEGLWLNVQHDAFYQQHNLSMSSYLLSLSKTVKVDY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 181 ISSPGISFLKSMKNSVKPTVTKLIFRFLKQEHIEPFTNQSYGSLAKNLSYIRTFSSGILVPKSYIWPVDSALYLQPHTSL 260
Cdd:cd08603 161 ISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSILKNLTFIKTFASGILVPKSYIWPVDSDQYLQPATSL 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15232292 261 VTDAHKEGLQVFASEFANDFVIAYNYSYDPTAEYLSFIDNGNFSVDGFLSDFPVTPYRA 319
Cdd:cd08603 241 VQDAHKAGLEVYASGFANDFDISYNYSYDPVAEYLSFVGNGNFSVDGVLSDFPITASEA 299
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 337-644 4.08e-161

Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 2 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play important an role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This CD includes domain II (the second GDPD domain of SHV3 and SVLs), which is necessary for SHV3 function.


Pssm-ID: 176546  Cd Length: 300  Bit Score: 466.81  E-value: 4.08e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 337 ITIISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNVIETSFRNLSSVVSEINPrRSGI 416
Cdd:cd08604   1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSKFSNRATTVPEIGS-TSGI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 417 YTFSLTMSQIQTLKPTISNLEKDSGLFRNPRNNKAGKFLTLSEFLFLPNRYsSLLGLLIEVENAAYLVEHQGISVVDAVL 496
Cdd:cd08604  80 FTFDLTWSEIQTLKPAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNK-SLSGVLINVENAAYLAEKKGLDVVDAVL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 497 DELKRATTQQNktSARTILIQSTDKSVLMKFKEKnkmNHDELVYRVDDNIRDVADSAIKDIKNFAGSIVISKKSVFPYKG 576
Cdd:cd08604 159 DALTNAGYDNQ--TAQKVLIQSTDSSVLAAFKKQ---ISYERVYVVDETIRDASDSSIEEIKKFADAVVIDRGSVFPVST 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232292 577 FIILEKeTNIASKLKSNGLRVYVERFSNECVTHAFDFYDDPTLEIDSFVRDVQIDGIITDFPATTARY 644
Cdd:cd08604 234 SFLTRQ-TNVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSYVQGAGVDGFITEFPATAARY 300
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 343-640 7.17e-17

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: 80.91  E-value: 7.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292   343 NGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNVIEtsfrnlssvvseinprrsgiYTFSLT 422
Cdd:pfam03009   2 RGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG--------------------YVRDLT 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292   423 MSQIQTLKPTISNLEKDSGlfrnprnnKAGKFLTLSEFL-FLPNrysslLGLLIEVE---NAAYLVEHQGISVVDAVLDE 498
Cdd:pfam03009  62 LEELKRLDIGAGNSGPLSG--------ERVPFPTLEEVLeFDWD-----VGFNIEIKikpYVEAIAPEEGLIVKDLLLSV 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292   499 LKRATtqqNKTSARTILIQSTDKSVLMKFKEKNKMnhdelvYRVDDNIRDVADSAIKDIKNFAGSIvisKKSVFPYKGFI 578
Cdd:pfam03009 129 DEILA---KKADPRRVIFSSFNPDELKRLRELAPK------LPLVFLSSGRAYAEADLLERAAAFA---GAPALLGEVAL 196

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232292   579 ILEKETNIASKLKSNGLRVYVERFSNEcvthafdfyddptlEIDSFVRDVQIDGIITDFPAT 640
Cdd:pfam03009 197 VDEALPDLVKRAHARGLVVHVWTVNNE--------------DEMKRLLELGVDGVITDRPDT 244
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
344-646 2.36e-16

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 79.14  E-value: 2.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 344 GASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNVietsfrnlSSVVSEinprrsgiytfsLTM 423
Cdd:COG0584  10 GASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNG--------TGRVAD------------LTL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 424 SQIQTLKptisnlekdsglFRNPRNNKAGKFLTLSEFL-FLPNRysslLGLLIEVENAAYLVEhqgiSVVDAVLDELKRA 502
Cdd:COG0584  70 AELRQLD------------AGSGPDFAGERIPTLEEVLeLVPGD----VGLNIEIKSPPAAEP----DLAEAVAALLKRY 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 503 TTqqnktsARTILIQSTDKSVLMKFKEKNKmnHDELVYRVDDNIRDVADsaikdiknFAGSIVISkkSVFPYKGFIilek 582
Cdd:COG0584 130 GL------EDRVIVSSFDPEALRRLRELAP--DVPLGLLVEELPADPLE--------LARALGAD--GVGPDYDLL---- 187

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232292 583 ETNIASKLKSNGLRVYVerfsnecvthafdfY--DDPTlEIDSFvRDVQIDGIITDFPATTARYRK 646
Cdd:COG0584 188 TPELVAAAHAAGLKVHV--------------WtvNDPE-EMRRL-LDLGVDGIITDRPDLLRAVLR 237
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
31-322 1.30e-08

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 56.03  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292  31 KPPAVIARGGFSGMFPDSSIQAYQL-----VNittspdvMLWCDLQLTKDGVGICF--PNLK-LDNGSNVIRidphyker 102
Cdd:COG0584   1 PRPLIIAHRGASGLAPENTLAAFRAalelgAD-------GIELDVQLTKDGVLVVFhdPTLDrTTNGTGRVA-------- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 103 fsvDFTWKELSDVKLAqgvvsRPYIFDDVsSILAIEEVAKLTASGLWLNI---QDSAFYAKhnlsMRNSVVSLSRRLKVN 179
Cdd:COG0584  66 ---DLTLAELRQLDAG-----SGPDFAGE-RIPTLEEVLELVPGDVGLNIeikSPPAAEPD----LAEAVAALLKRYGLE 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 180 ---FISSPGISFLKSMKNSVKPTVTKLIFRFLKQEHIEpftnqsygsLAKNLSYirtfsSGILVPKSYIwpvdsalylqp 256
Cdd:COG0584 133 drvIVSSFDPEALRRLRELAPDVPLGLLVEELPADPLE---------LARALGA-----DGVGPDYDLL----------- 187

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232292 257 HTSLVTDAHKEGLQVFAsefandfviaynYSYDPTAEYLSFIDNGnfsVDGFLSDFPVTPYRAINC 322
Cdd:COG0584 188 TPELVAAAHAAGLKVHV------------WTVNDPEEMRRLLDLG---VDGIITDRPDLLRAVLRE 238
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 40-315 1.93e-04

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: 43.54  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292    40 GFSGMFPDSSIQAYQLVnITTSPDvMLWCDLQLTKDGVGICFPNLKLDNGSNVIridphykeRFSVDFTWKELSdvKLAQ 119
Cdd:pfam03009   3 GASGSYPENTLASFRKA-AEAGAD-YIEFDVQLTKDGVPVVLHDFNLDRTTDGA--------GYVRDLTLEELK--RLDI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292   120 GVVSRPYIFDDVSSILAIEEVAKLTAsGLWLNI------QDSAFYAKHNLSMRNSVVSLSRRLKV------NFISSPGIS 187
Cdd:pfam03009  71 GAGNSGPLSGERVPFPTLEEVLEFDW-DVGFNIeikikpYVEAIAPEEGLIVKDLLLSVDEILAKkadprrVIFSSFNPD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292   188 FLKSMKNSvkptVTKLIFRFLkqehIEPFTNQSYGSLAKNLSYIRTFSSGILVPksyiwpvdsaLYLQPHTSLVTDAHKE 267
Cdd:pfam03009 150 ELKRLREL----APKLPLVFL----SSGRAYAEADLLERAAAFAGAPALLGEVA----------LVDEALPDLVKRAHAR 211

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 15232292   268 GLQVFAsefandfviaynYSYDPTAEYLSFIDNGnfsVDGFLSDFPVT 315
Cdd:pfam03009 212 GLVVHV------------WTVNNEDEMKRLLELG---VDGVITDRPDT 244
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 10-120 2.08e-03

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 41.20  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292   10 ILITFFILQTAFSSSWQTLSGKP-PAVIARGGFSGMFPDSSIQAYQLVnITTSPDvMLWCDLQLTKDGVGICFPNLKLDN 88
Cdd:PRK11143   3 NLSLALLLAALLAGSAAAAADSAeKIVIAHRGASGYLPEHTLPAKAMA-YAQGAD-YLEQDLVMTKDDQLVVLHDHYLDR 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15232292   89 GSNVI-------RIDPHYkerFSVDFTWKELSDVKLAQG 120
Cdd:PRK11143  81 VTDVAerfpdraRKDGRY---YAIDFTLDEIKSLKFTEG 116
 
Name Accession Description Interval E-value
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 33-319 7.37e-176

Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 1 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play an important role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This family includes domain I, the first GDPD domain of SHV3 and SVLs.


Pssm-ID: 176545  Cd Length: 299  Bit Score: 504.61  E-value: 7.37e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292  33 PAVIARGGFSGMFPDSSIQAYQLVNITTSPDVMLWCDLQLTKDGVGICFPNLKLDNGSNVIRIDP-----------HYKE 101
Cdd:cd08603   1 PLVIARGGFSGLFPDSSLFAYQFAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPkrkktysvngvSTKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 102 RFSVDFTWKELSDVKLAQGVVSRPYIFDDVSSILAIEEVAKLTA-SGLWLNIQDSAFYAKHNLSMRNSVVSLSRRLKVNF 180
Cdd:cd08603  81 WFSVDFTLAELQQVTLIQGIFSRTPIFDGQYPISTVEDVVTLAKpEGLWLNVQHDAFYQQHNLSMSSYLLSLSKTVKVDY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 181 ISSPGISFLKSMKNSVKPTVTKLIFRFLKQEHIEPFTNQSYGSLAKNLSYIRTFSSGILVPKSYIWPVDSALYLQPHTSL 260
Cdd:cd08603 161 ISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSILKNLTFIKTFASGILVPKSYIWPVDSDQYLQPATSL 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15232292 261 VTDAHKEGLQVFASEFANDFVIAYNYSYDPTAEYLSFIDNGNFSVDGFLSDFPVTPYRA 319
Cdd:cd08603 241 VQDAHKAGLEVYASGFANDFDISYNYSYDPVAEYLSFVGNGNFSVDGVLSDFPITASEA 299
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 337-644 4.08e-161

Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 2 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play important an role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This CD includes domain II (the second GDPD domain of SHV3 and SVLs), which is necessary for SHV3 function.


Pssm-ID: 176546  Cd Length: 300  Bit Score: 466.81  E-value: 4.08e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 337 ITIISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNVIETSFRNLSSVVSEINPrRSGI 416
Cdd:cd08604   1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSKFSNRATTVPEIGS-TSGI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 417 YTFSLTMSQIQTLKPTISNLEKDSGLFRNPRNNKAGKFLTLSEFLFLPNRYsSLLGLLIEVENAAYLVEHQGISVVDAVL 496
Cdd:cd08604  80 FTFDLTWSEIQTLKPAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNK-SLSGVLINVENAAYLAEKKGLDVVDAVL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 497 DELKRATTQQNktSARTILIQSTDKSVLMKFKEKnkmNHDELVYRVDDNIRDVADSAIKDIKNFAGSIVISKKSVFPYKG 576
Cdd:cd08604 159 DALTNAGYDNQ--TAQKVLIQSTDSSVLAAFKKQ---ISYERVYVVDETIRDASDSSIEEIKKFADAVVIDRGSVFPVST 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232292 577 FIILEKeTNIASKLKSNGLRVYVERFSNECVTHAFDFYDDPTLEIDSFVRDVQIDGIITDFPATTARY 644
Cdd:cd08604 234 SFLTRQ-TNVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSYVQGAGVDGFITEFPATAARY 300
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 337-644 4.89e-135

Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase (GDPD) domain present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play an important role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens.


Pssm-ID: 176513  Cd Length: 302  Bit Score: 400.12  E-value: 4.89e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 337 ITIISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNVIETSFRNLSSVVSEInPRRSGI 416
Cdd:cd08571   1 PLVIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPKRKKTYVVEG-QSTSGI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 417 YTFSLTMSQIQTLKPTISNLEKDsgLFRNPRNNKAGKFLTLSEFLFLPNRYSsLLGLLIEVENAAYLVEHQGISVVDAVL 496
Cdd:cd08571  80 FSFDLTWAEIQTLKPIISNPFSV--LFRNPRNDNAGKILTLEDFLTLAKPKS-LSGVWINVENAAFLAEHKGLLSVDAVL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 497 DELKRATTQQnktSARTILIQSTDKSVLMKFKEKNKMNHDELVYRVDDNIRDVADSAIKDIKNFAGSIVISKKSVFPYKG 576
Cdd:cd08571 157 TSLSKAGYDQ---TAKKVYISSPDSSVLKSFKKRVGTKLVFRVLDVDDTEPDTLLSNLTEIKKFASGVLVPKSYIWPVDS 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232292 577 FIILEKETNIASKLKSNGLRVYVERFSNECVTHAFDFYDDPTLEIDSFVRDVQ-IDGIITDFPATTARY 644
Cdd:cd08571 234 DSFLTPQTSVVQDAHKAGLEVYVSGFANEFVSLAYDYSADPTLEILSFVGNGNsVDGVITDFPATAARA 302
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 33-319 4.58e-116

Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase (GDPD) domain present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play an important role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens.


Pssm-ID: 176513  Cd Length: 302  Bit Score: 351.59  E-value: 4.58e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292  33 PAVIARGGFSGMFPDSSIQAYQLVNITTspDVMLWCDLQLTKDGVGICFPNLKLDNGSNVIRIDP-----------HYKE 101
Cdd:cd08571   1 PLVIARGGASGDYPDSTDLAYQKAISDG--ADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPkrkktyvvegqSTSG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 102 RFSVDFTWKELSDVKLAQG----VVSRPYIFDDVSSILAIEEVAKLTA----SGLWLNIQDSAFYAKH--NLSMRNSVVS 171
Cdd:cd08571  79 IFSFDLTWAEIQTLKPIISnpfsVLFRNPRNDNAGKILTLEDFLTLAKpkslSGVWINVENAAFLAEHkgLLSVDAVLTS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 172 LSRR-----LKVNFISSPGISFLKSMKNSVKptvTKLIFRFLKQEHIEPFTnqsygsLAKNLSYIRTFSSGILVPKSYIW 246
Cdd:cd08571 159 LSKAgydqtAKKVYISSPDSSVLKSFKKRVG---TKLVFRVLDVDDTEPDT------LLSNLTEIKKFASGVLVPKSYIW 229

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232292 247 PVDSALYLQPHTSLVTDAHKEGLQVFASEFANDFV-IAYNYSYDPTAEYLSFIDNGNfSVDGFLSDFPVTPYRA 319
Cdd:cd08571 230 PVDSDSFLTPQTSVVQDAHKAGLEVYVSGFANEFVsLAYDYSADPTLEILSFVGNGN-SVDGVITDFPATAARA 302
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 33-313 4.38e-30

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: 120.87  E-value: 4.38e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292  33 PAVIARGGFSGMFPDSSIQAYQLVnITTSPDVmLWCDLQLTKDGVGICFPNLKLDNGSNVIRIdPHYKER---------- 102
Cdd:cd08602   1 PLVIAHRGASGYRPEHTLAAYQLA-IEQGADF-IEPDLVSTKDGVLICRHEPELSGTTDVADH-PEFADRkttktvdgvn 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 103 ----FSVDFTWKELSDVKLAQgvvSRPYI---FDDVSSILAIEEVAKLTAS---------GLWLNIQDSAFYAKH-NLSM 165
Cdd:cd08602  78 vtgwFTEDFTLAELKTLRARQ---RLPYRdqsYDGQFPIPTFEEIIALAKAasaatgrtvGIYPEIKHPTYFNAPlGLPM 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 166 RNSVVSLSRRLKVNFISSPGI--SF----LKSMKNSVKPTVTKLIFRFLK-QEHIEPFTNQSYGSLA--KNLSYIRTFSS 236
Cdd:cd08602 155 EDKLLETLKKYGYTGKKAPVFiqSFevtnLKYLRNKTDLPLVQLIDDATIpPQDTPEGDSRTYADLTtdAGLKEIATYAD 234

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232292 237 GILVPKSYIWPVDSALYLQPHTSLVTDAHKEGLQVFASEFAN-DFVIAYNYSYDPTAEYLSFIDNGnfsVDGFLSDFP 313
Cdd:cd08602 235 GIGPWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNeNTFLPPDFFGDPYAEYRAFLDAG---VDGLFTDFP 309
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 337-638 2.10e-22

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: 98.11  E-value: 2.10e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 337 ITIISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNVietsfrnlSSVVSEINPRRSGI 416
Cdd:cd08559   1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNV--------AEHFPFRGRKDTGY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 417 YTFSLTMSQIQTLKPTISNLEKDSGLFrnpRNNKAG-KFLTLSEFLFLPNRYSSLL----GLLIEVENAAYlVEHQGISV 491
Cdd:cd08559  73 FVIDFTLAELKTLRAGSWFNQRYPERA---PSYYGGfKIPTLEEVIELAQGLNKSTgrnvGIYPETKHPTF-HKQEGPDI 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 492 VDAVLDELKRAttQQNKTSARTIlIQSTDKSVLMKFkeKNKMNHDELVYRVD-------DNIRDVA----DSAIKDIKNF 560
Cdd:cd08559 149 EEKLLEVLKKY--GYTGKNDPVF-IQSFEPESLKRL--RNETPDIPLVQLIDygdwaetDKKYTYAwlttDAGLKEIAKY 223

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232292 561 AGSIVISKKSVFPYKGFIILEKeTNIASKLKSNGLRVYVERFSNECVTHAFDFYDDPTLEIdsfvRDVQIDGIITDFP 638
Cdd:cd08559 224 ADGIGPWKSLIIPEDSNGLLVP-TDLVKDAHKAGLLVHPYTFRNENLFLAPDFKQDMDALY----NAAGVDGVFTDFP 296
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 33-313 2.76e-22

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: 97.73  E-value: 2.76e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292  33 PAVIARGGFSGMFPDSSIQAYQLVnITTSPDVmLWCDLQLTKDGVGICFPNLKLDNGSNViriDPHYKER-------FSV 105
Cdd:cd08559   1 PLVIAHRGASGYAPEHTLAAYALA-IEMGADY-IEQDLVMTKDGVLVARHDPTLDRTTNV---AEHFPFRgrkdtgyFVI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 106 DFTWKELSDVKLAQGVVSR-PYIF---DDVSSILAIEEV----AKLTAS-----GLWLNIQDSAFYAKHNLSMRNSVVSL 172
Cdd:cd08559  76 DFTLAELKTLRAGSWFNQRyPERApsyYGGFKIPTLEEVielaQGLNKStgrnvGIYPETKHPTFHKQEGPDIEEKLLEV 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 173 SRRLKVNFISSPGI--SF----LKSMKNSVKPtvTKLIFRFLKQEHIEPFTNQSYGSL--AKNLSYIRTFSSGILVPKSY 244
Cdd:cd08559 156 LKKYGYTGKNDPVFiqSFepesLKRLRNETPD--IPLVQLIDYGDWAETDKKYTYAWLttDAGLKEIAKYADGIGPWKSL 233

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 245 IWPVDSALYLQPhTSLVTDAHKEGLQVFASEFANDFV-IAYNYSYDPTAEYLsfiDNGnfsVDGFLSDFP 313
Cdd:cd08559 234 IIPEDSNGLLVP-TDLVKDAHKAGLLVHPYTFRNENLfLAPDFKQDMDALYN---AAG---VDGVFTDFP 296
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 338-638 6.37e-21

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: 94.29  E-value: 6.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 338 TIISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNV---IETSFRNLSSVVSEINprRS 414
Cdd:cd08602   2 LVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVadhPEFADRKTTKTVDGVN--VT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 415 GIYTFSLTMSQIQTLKpTISNLEkdsglFRNPRNNkaGKF--LTLSEFLFLPNRYSSLLGLLI----EVENAAYLVEHQG 488
Cdd:cd08602  80 GWFTEDFTLAELKTLR-ARQRLP-----YRDQSYD--GQFpiPTFEEIIALAKAASAATGRTVgiypEIKHPTYFNAPLG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 489 ISVVDAVLDELKRAttqqNKTSART-ILIQSTDKSVLMKFKEKNKMNHDELVYRVDDNIRDVA------------DSAIK 555
Cdd:cd08602 152 LPMEDKLLETLKKY----GYTGKKApVFIQSFEVTNLKYLRNKTDLPLVQLIDDATIPPQDTPegdsrtyadlttDAGLK 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 556 DIKNFAGSIVISKKSVFPYKGFIILEKETNIASKLKSNGLRVYVERFSNECVTHAFDFYDDPTLEIDSFVrDVQIDGIIT 635
Cdd:cd08602 228 EIATYADGIGPWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNENTFLPPDFFGDPYAEYRAFL-DAGVDGLFT 306


                ...
gi 15232292 636 DFP 638
Cdd:cd08602 307 DFP 309
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 33-318 9.36e-21

Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 2 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play important an role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This CD includes domain II (the second GDPD domain of SHV3 and SVLs), which is necessary for SHV3 function.


Pssm-ID: 176546  Cd Length: 300  Bit Score: 93.56  E-value: 9.36e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292  33 PAVIARGGFSGMFPDSSIQAYQLVnITTSPDVmLWCDLQLTKDGVGICFPNLKLDNGSNVIRID--------PHYKER-- 102
Cdd:cd08604   1 PLIISHNGASGDYPGCTDLAYQKA-VKDGADV-IDCSVQMSKDGVPFCLDSINLINSTTVATSKfsnrattvPEIGSTsg 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 103 -FSVDFTWKELSDVKlaqGVVSRPY----IFDDVS-----SILAIEE---VAKLTA-SGLWLNIQDSAFYAKH-NLSMRN 167
Cdd:cd08604  79 iFTFDLTWSEIQTLK---PAISNPYsvtgLFRNPAnknagKFLTLSDfldLAKNKSlSGVLINVENAAYLAEKkGLDVVD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 168 SVVS-LSR-------RLKVnFISSPGISFLKSMKnsvKPTVTKLIFRflkqehiepfTNQSYGSLAKN-LSYIRTFSSGI 238
Cdd:cd08604 156 AVLDaLTNagydnqtAQKV-LIQSTDSSVLAAFK---KQISYERVYV----------VDETIRDASDSsIEEIKKFADAV 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 239 LVPKSYIWPVDSAlYLQPHTSLVTDAHKEGLQVFASEFANDFV-IAYNYSYDPTAEYLSFIdnGNFSVDGFLSDFPVTPY 317
Cdd:cd08604 222 VIDRGSVFPVSTS-FLTRQTNVVEKLQSANLTVYVEVLRNEFVsLAFDFFADPTVEINSYV--QGAGVDGFITEFPATAA 298


                .
gi 15232292 318 R 318
Cdd:cd08604 299 R 299
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 339-643 2.72e-20

Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 1 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play an important role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This family includes domain I, the first GDPD domain of SHV3 and SVLs.


Pssm-ID: 176545  Cd Length: 299  Bit Score: 92.06  E-value: 2.72e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 339 IISKNGASGDFPGCTDLAYQRAASDGAD--ILDCNVQMSKDKIPFCMSSFDLINSTNVIETsFRNLSSVVSEINPRRSGI 416
Cdd:cd08603   3 VIARGGFSGLFPDSSLFAYQFAASSSSPdvALWCDLQLTKDGVGICLPDLNLDNSTTIARV-YPKRKKTYSVNGVSTKGW 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 417 YTFSLTMSQIQTLKPTISNLEkdsglfRNPRNNKAGKFLTLSEFLFLPNRysslLGLLIEVENAAYLVEHqGISVVDAVL 496
Cdd:cd08603  82 FSVDFTLAELQQVTLIQGIFS------RTPIFDGQYPISTVEDVVTLAKP----EGLWLNVQHDAFYQQH-NLSMSSYLL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 497 DELKRATTQqnktsartiLIQSTDKSVLMKFKEKNKMNHDELVYRVDDniRDVAD-----------SAIKDIKNFAGSIV 565
Cdd:cd08603 151 SLSKTVKVD---------YISSPEVGFLKSIGGRVGRNGTKLVFRFLD--KDDVEpstnqtygsilKNLTFIKTFASGIL 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 566 ISKKSVFPYKGFIILEKETNIASKLKSNGLRVYVERFSNECVThAFDFYDDPTLEIDSFVRDVQ--IDGIITDFPATTAR 643
Cdd:cd08603 220 VPKSYIWPVDSDQYLQPATSLVQDAHKAGLEVYASGFANDFDI-SYNYSYDPVAEYLSFVGNGNfsVDGVLSDFPITASE 298
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 343-640 7.17e-17

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: 80.91  E-value: 7.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292   343 NGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNVIEtsfrnlssvvseinprrsgiYTFSLT 422
Cdd:pfam03009   2 RGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAG--------------------YVRDLT 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292   423 MSQIQTLKPTISNLEKDSGlfrnprnnKAGKFLTLSEFL-FLPNrysslLGLLIEVE---NAAYLVEHQGISVVDAVLDE 498
Cdd:pfam03009  62 LEELKRLDIGAGNSGPLSG--------ERVPFPTLEEVLeFDWD-----VGFNIEIKikpYVEAIAPEEGLIVKDLLLSV 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292   499 LKRATtqqNKTSARTILIQSTDKSVLMKFKEKNKMnhdelvYRVDDNIRDVADSAIKDIKNFAGSIvisKKSVFPYKGFI 578
Cdd:pfam03009 129 DEILA---KKADPRRVIFSSFNPDELKRLRELAPK------LPLVFLSSGRAYAEADLLERAAAFA---GAPALLGEVAL 196

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232292   579 ILEKETNIASKLKSNGLRVYVERFSNEcvthafdfyddptlEIDSFVRDVQIDGIITDFPAT 640
Cdd:pfam03009 197 VDEALPDLVKRAHARGLVVHVWTVNNE--------------DEMKRLLELGVDGVITDRPDT 244
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
344-646 2.36e-16

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 79.14  E-value: 2.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 344 GASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNVietsfrnlSSVVSEinprrsgiytfsLTM 423
Cdd:COG0584  10 GASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNG--------TGRVAD------------LTL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 424 SQIQTLKptisnlekdsglFRNPRNNKAGKFLTLSEFL-FLPNRysslLGLLIEVENAAYLVEhqgiSVVDAVLDELKRA 502
Cdd:COG0584  70 AELRQLD------------AGSGPDFAGERIPTLEEVLeLVPGD----VGLNIEIKSPPAAEP----DLAEAVAALLKRY 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 503 TTqqnktsARTILIQSTDKSVLMKFKEKNKmnHDELVYRVDDNIRDVADsaikdiknFAGSIVISkkSVFPYKGFIilek 582
Cdd:COG0584 130 GL------EDRVIVSSFDPEALRRLRELAP--DVPLGLLVEELPADPLE--------LARALGAD--GVGPDYDLL---- 187

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232292 583 ETNIASKLKSNGLRVYVerfsnecvthafdfY--DDPTlEIDSFvRDVQIDGIITDFPATTARYRK 646
Cdd:COG0584 188 TPELVAAAHAAGLKVHV--------------WtvNDPE-EMRRL-LDLGVDGIITDRPDLLRAVLR 237
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 338-639 1.23e-11

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: 66.26  E-value: 1.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 338 TIISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNvietsfrnlssvVSEINPRRS--- 414
Cdd:cd08600   2 IIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTN------------VAEKFPDRKrkd 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 415 -GIYTFSLTMSQIQTLKPTIS-NLEKDSGLFRNPR---NNKAG-KFLTLSEFLFLPNRYSSL----LGLLIEVEnAAYLV 484
Cdd:cd08600  70 gRYYVIDFTLDELKSLSVTERfDIENGKKVQVYPNrfpLWKSDfKIHTLEEEIELIQGLNKStgknVGIYPEIK-APWFH 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 485 EHQGISVVDAVLDELKRA--TTQQNKtsartILIQSTDKSVLMKFKE--KNKMNHD-ELVYRVDDNirDVADSAIKD--- 556
Cdd:cd08600 149 HQEGKDIAAATLEVLKKYgyTSKNDK-----VYLQTFDPNELKRIKNelLPKMGMDlKLVQLIAYT--DWGETQEKDpgg 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 557 --------IKNFAGSIVISK--KSVFPYKGFIILEKE-------TNIASKLKSNGLRVYVERFSNECV-THAFDFYDDpt 618
Cdd:cd08600 222 wvnydydwMFTKGGLKEIAKyaDGVGPWYSMIIEEKSskgnivlTDLVKDAHEAGLEVHPYTVRKDALpEYAKDADQL-- 299

                       330       340
                ....*....|....*....|.
gi 15232292 619 leIDSFVRDVQIDGIITDFPA 639
Cdd:cd08600 300 --LDALLNKAGVDGVFTDFPD 318
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 35-313 2.01e-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: 59.71  E-value: 2.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292  35 VIARGGFSGMFPDSSIQAYQLVNITTSPdvMLWCDLQLTKDGVGICFPNLKLDNGSNVIRIDPHYKER----FSVDFTWK 110
Cdd:cd08600   3 IIAHRGASGYLPEHTLEAKALAYAQGAD--YLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKRKdgryYVIDFTLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 111 ELSDVKLAQGVVS-----------RPYIFDDVSSILAIEEVAKL---------TASGLWLNIQDSAFY------------ 158
Cdd:cd08600  81 ELKSLSVTERFDIengkkvqvypnRFPLWKSDFKIHTLEEEIELiqglnkstgKNVGIYPEIKAPWFHhqegkdiaaatl 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 159 ---AKHNLSMRNSVVslsrrlkvnFISSPGISFLKSMKNSVKPTVT---KLIFRFLKQEHIEPFTNQSYGSLAKNLSY-- 230
Cdd:cd08600 161 evlKKYGYTSKNDKV---------YLQTFDPNELKRIKNELLPKMGmdlKLVQLIAYTDWGETQEKDPGGWVNYDYDWmf 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 231 -------IRTFSSGILVPKSYIWPVDSALYLQPHTSLVTDAHKEGLQVFASEFANDFVIAYNYSYDPTAEYLsFIDNGnf 303
Cdd:cd08600 232 tkgglkeIAKYADGVGPWYSMIIEEKSSKGNIVLTDLVKDAHEAGLEVHPYTVRKDALPEYAKDADQLLDAL-LNKAG-- 308

                       330
                ....*....|
gi 15232292 304 sVDGFLSDFP 313
Cdd:cd08600 309 -VDGVFTDFP 317
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
31-322 1.30e-08

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 56.03  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292  31 KPPAVIARGGFSGMFPDSSIQAYQL-----VNittspdvMLWCDLQLTKDGVGICF--PNLK-LDNGSNVIRidphyker 102
Cdd:COG0584   1 PRPLIIAHRGASGLAPENTLAAFRAalelgAD-------GIELDVQLTKDGVLVVFhdPTLDrTTNGTGRVA-------- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 103 fsvDFTWKELSDVKLAqgvvsRPYIFDDVsSILAIEEVAKLTASGLWLNI---QDSAFYAKhnlsMRNSVVSLSRRLKVN 179
Cdd:COG0584  66 ---DLTLAELRQLDAG-----SGPDFAGE-RIPTLEEVLELVPGDVGLNIeikSPPAAEPD----LAEAVAALLKRYGLE 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 180 ---FISSPGISFLKSMKNSVKPTVTKLIFRFLKQEHIEpftnqsygsLAKNLSYirtfsSGILVPKSYIwpvdsalylqp 256
Cdd:COG0584 133 drvIVSSFDPEALRRLRELAPDVPLGLLVEELPADPLE---------LARALGA-----DGVGPDYDLL----------- 187

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232292 257 HTSLVTDAHKEGLQVFAsefandfviaynYSYDPTAEYLSFIDNGnfsVDGFLSDFPVTPYRAINC 322
Cdd:COG0584 188 TPELVAAAHAAGLKVHV------------WTVNDPEEMRRLLDLG---VDGIITDRPDLLRAVLRE 238
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 337-532 1.31e-08

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: 56.46  E-value: 1.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 337 ITIISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNVietsfrnlSSVVSEinprrsgi 416
Cdd:cd08575   1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGG--------SGLVSD-------- 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 417 ytfsLTMSQIQTLKPTIsNLEKDSGLFRNPRNNKAGKFLTLSE-FLFLPNRyssLLGLLIEVENAAYLVEhqgisvvdAV 495
Cdd:cd08575  65 ----LTYAELPPLDAGY-GYTFDGGKTGYPRGGGDGRIPTLEEvFKAFPDT---PINIDIKSPDAEELIA--------AV 128

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15232292 496 LDELKRaTTQQNKTsartiLIQSTDKSVLMKFKEKNK 532
Cdd:cd08575 129 LDLLEK-YKREDRT-----VWGSTNPEYLRALHPENP 159
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 339-383 5.53e-07

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: 50.34  E-value: 5.53e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15232292 339 IISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCM 383
Cdd:cd08556   1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVI 45
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 337-638 7.12e-06

Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46) from Staphylococcus aureus, Bacillus subtilis and similar proteins. Members in this family show very high sequence similarity to Escherichia coli periplasmic phosphodiesterase GlpQ, which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176543 [Multi-domain]  Cd Length: 256  Bit Score: 48.08  E-value: 7.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 337 ITIISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNVIETSfrnlssvvseinprrsgi 416
Cdd:cd08601   1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIERPG------------------ 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 417 YTFSLTMSQIQTLkptisnlekDSGLFRN---PRNNKAG----KFLTLSEFLflpNRYSSLLGLLIEVENAAYlveHQGI 489
Cdd:cd08601  63 PVKDYTLAEIKQL---------DAGSWFNkayPEYARESysglKVPTLEEVI---ERYGGRANYYIETKSPDL---YPGM 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292 490 SvvDAVLDEL-KRATTQQNKTSARTIlIQSTDKSVLMKFKEKNKmnHDELVYRVD-DNIRDVADSAIKDIKNFAGSIVIS 567
Cdd:cd08601 128 E--EKLLATLdKYGLLTDNLKNGQVI-IQSFSKESLKKLHQLNP--NIPLVQLLWyGEGAETYDKWLDEIKEYAIGIGPS 202

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232292 568 KKSVFPYkgfiileketnIASKLKSNGLRVyverfsnecvtHAFDFYDDPTLEIdsfVRDVQIDGIITDFP 638
Cdd:cd08601 203 IADADPW-----------MVHLIHKKGLLV-----------HPYTVNEKADMIR---LINWGVDGMFTNYP 248
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 33-112 4.12e-05

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: 45.77  E-value: 4.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292  33 PAVIARGGFSGMFPDSSIQAYQLVnITTSPDvMLWCDLQLTKDGVGICFPNLKLDNGSNvirIDPHYKERfsvDFTWKEL 112
Cdd:cd08601   1 NAVIAHRGASGYAPEHTFAAYDLA-REMGAD-YIELDLQMTKDGVLVAMHDETLDRTTN---IERPGPVK---DYTLAEI 72
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 336-396 8.39e-05

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: 45.25  E-value: 8.39e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232292 336 KITIISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNVIE 396
Cdd:cd08610  22 KPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNIGE 82
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 40-315 1.93e-04

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: 43.54  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292    40 GFSGMFPDSSIQAYQLVnITTSPDvMLWCDLQLTKDGVGICFPNLKLDNGSNVIridphykeRFSVDFTWKELSdvKLAQ 119
Cdd:pfam03009   3 GASGSYPENTLASFRKA-AEAGAD-YIEFDVQLTKDGVPVVLHDFNLDRTTDGA--------GYVRDLTLEELK--RLDI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292   120 GVVSRPYIFDDVSSILAIEEVAKLTAsGLWLNI------QDSAFYAKHNLSMRNSVVSLSRRLKV------NFISSPGIS 187
Cdd:pfam03009  71 GAGNSGPLSGERVPFPTLEEVLEFDW-DVGFNIeikikpYVEAIAPEEGLIVKDLLLSVDEILAKkadprrVIFSSFNPD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292   188 FLKSMKNSvkptVTKLIFRFLkqehIEPFTNQSYGSLAKNLSYIRTFSSGILVPksyiwpvdsaLYLQPHTSLVTDAHKE 267
Cdd:pfam03009 150 ELKRLREL----APKLPLVFL----SSGRAYAEADLLERAAAFAGAPALLGEVA----------LVDEALPDLVKRAHAR 211

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 15232292   268 GLQVFAsefandfviaynYSYDPTAEYLSFIDNGnfsVDGFLSDFPVT 315
Cdd:pfam03009 212 GLVVHV------------WTVNNEDEMKRLLELG---VDGVITDRPDT 244
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 340-397 5.67e-04

Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic phosphodiesterase (GlpQ) include uncharacterized proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and their hypothetical homologs. Members in this subfamily show 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: 176503  Cd Length: 356  Bit Score: 42.79  E-value: 5.67e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15232292 340 ISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCM-SSFDLINSTNVIET 397
Cdd:cd08560  20 IGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRhSQCDLHTTTNILAI 78
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 10-120 2.08e-03

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 41.20  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232292   10 ILITFFILQTAFSSSWQTLSGKP-PAVIARGGFSGMFPDSSIQAYQLVnITTSPDvMLWCDLQLTKDGVGICFPNLKLDN 88
Cdd:PRK11143   3 NLSLALLLAALLAGSAAAAADSAeKIVIAHRGASGYLPEHTLPAKAMA-YAQGAD-YLEQDLVMTKDDQLVVLHDHYLDR 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15232292   89 GSNVI-------RIDPHYkerFSVDFTWKELSDVKLAQG 120
Cdd:PRK11143  81 VTDVAerfpdraRKDGRY---YAIDFTLDEIKSLKFTEG 116
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 339-377 4.03e-03

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: 39.51  E-value: 4.03e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 15232292 339 IISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKD 377
Cdd:cd08570   1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKD 39
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 339-393 4.86e-03

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: 39.62  E-value: 4.86e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15232292 339 IISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTN 393
Cdd:cd08580   3 IVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTN 57
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 336-394 8.82e-03

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: 38.44  E-value: 8.82e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15232292 336 KITIISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNV 394
Cdd:cd08574   1 KPALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNV 59
 
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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