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Conserved domains on  [gi|15242971|ref|NP_200625|]
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SHV3-like 5 [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_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 355-653 0e+00

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: 528.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 355 ALVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFCHDAADLTASTTAMT-IFMSRATSVPEIQPTNGIF 433
Cdd:cd08604   1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATsKFSNRATTVPEIGSTSGIF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 434 SFDLTWAEIQSVKPQIENPFTATGFQRNPANKNAGKFITLADFLDFSKAKAVTGVMINIENAAYLASKKGLGVVDAVKSA 513
Cdd:cd08604  81 TFDLTWSEIQTLKPAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNKSLSGVLINVENAAYLAEKKGLDVVDAVLDA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 514 LAKSTLDKQSTQKVLIQSDDSSVLASFEAVPPYTRVLSIDKEIGGAPKPSVDEIKKYAEAVNLLRTSLVTVSQSFTTGKT 593
Cdd:cd08604 161 LTNAGYDNQTAQKVLIQSTDSSVLAAFKKQISYERVYVVDETIRDASDSSIEEIKKFADAVVIDRGSVFPVSTSFLTRQT 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 594 NVVEEMHKGNISVYVSVLRNEYISVAFDYFSDPTIELATFISGSGVDGVITEFPATATRY 653
Cdd:cd08604 241 NVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSYVQGAGVDGFITEFPATAARY 300
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 41-338 2.87e-178

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: 511.55  E-value: 2.87e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  41 PAVVARGGFSGLFPESSASANDLAIGTSSPGLTMLCNLQMTKDGVGLCLSDIILDNATTISSVFPKAQKTYKVNGQDLKG 120
Cdd:cd08603   1 PLVIARGGFSGLFPDSSLFAYQFAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPKRKKTYSVNGVSTKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 121 WFVLDYDADTIFNnVTLVQNIFSRPSIFDGQMSVSAVEDVLGTKPP-KFWLSVQYDAFYMEHKLSPAEYLRSLQFR-GIN 198
Cdd:cd08603  81 WFSVDFTLAELQQ-VTLIQGIFSRTPIFDGQYPISTVEDVVTLAKPeGLWLNVQHDAFYQQHNLSMSSYLLSLSKTvKVD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 199 VISSPEIGFLKSIGMDAGRAKTKLIFEFKDPEAVEPTTNKKYSEIQQNLAAIKAFASGVLVPKDYIWPIDSAKYLKPATT 278
Cdd:cd08603 160 YISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSILKNLTFIKTFASGILVPKSYIWPVDSDQYLQPATS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 279 FVADAHKAGLEVYASGFANDLRTSFNYSYDPSAEYLQFVDNGQFSVDGVITDFPPTASQS 338
Cdd:cd08603 240 LVQDAHKAGLEVYASGFANDFDISYNYSYDPVAEYLSFVGNGNFSVDGVLSDFPITASEA 299
 
Name Accession Description Interval E-value
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 355-653 0e+00

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: 528.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 355 ALVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFCHDAADLTASTTAMT-IFMSRATSVPEIQPTNGIF 433
Cdd:cd08604   1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATsKFSNRATTVPEIGSTSGIF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 434 SFDLTWAEIQSVKPQIENPFTATGFQRNPANKNAGKFITLADFLDFSKAKAVTGVMINIENAAYLASKKGLGVVDAVKSA 513
Cdd:cd08604  81 TFDLTWSEIQTLKPAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNKSLSGVLINVENAAYLAEKKGLDVVDAVLDA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 514 LAKSTLDKQSTQKVLIQSDDSSVLASFEAVPPYTRVLSIDKEIGGAPKPSVDEIKKYAEAVNLLRTSLVTVSQSFTTGKT 593
Cdd:cd08604 161 LTNAGYDNQTAQKVLIQSTDSSVLAAFKKQISYERVYVVDETIRDASDSSIEEIKKFADAVVIDRGSVFPVSTSFLTRQT 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 594 NVVEEMHKGNISVYVSVLRNEYISVAFDYFSDPTIELATFISGSGVDGVITEFPATATRY 653
Cdd:cd08604 241 NVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSYVQGAGVDGFITEFPATAARY 300
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 41-338 2.87e-178

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: 511.55  E-value: 2.87e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  41 PAVVARGGFSGLFPESSASANDLAIGTSSPGLTMLCNLQMTKDGVGLCLSDIILDNATTISSVFPKAQKTYKVNGQDLKG 120
Cdd:cd08603   1 PLVIARGGFSGLFPDSSLFAYQFAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPKRKKTYSVNGVSTKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 121 WFVLDYDADTIFNnVTLVQNIFSRPSIFDGQMSVSAVEDVLGTKPP-KFWLSVQYDAFYMEHKLSPAEYLRSLQFR-GIN 198
Cdd:cd08603  81 WFSVDFTLAELQQ-VTLIQGIFSRTPIFDGQYPISTVEDVVTLAKPeGLWLNVQHDAFYQQHNLSMSSYLLSLSKTvKVD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 199 VISSPEIGFLKSIGMDAGRAKTKLIFEFKDPEAVEPTTNKKYSEIQQNLAAIKAFASGVLVPKDYIWPIDSAKYLKPATT 278
Cdd:cd08603 160 YISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSILKNLTFIKTFASGILVPKSYIWPVDSDQYLQPATS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 279 FVADAHKAGLEVYASGFANDLRTSFNYSYDPSAEYLQFVDNGQFSVDGVITDFPPTASQS 338
Cdd:cd08603 240 LVQDAHKAGLEVYASGFANDFDISYNYSYDPVAEYLSFVGNGNFSVDGVLSDFPITASEA 299
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 360-649 1.68e-22

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: 97.09  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971   360 HNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFC-HDAadltasttamtiFMSRATSVPEiqptngiFSFDLT 438
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVlHDF------------NLDRTTDGAG-------YVRDLT 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971   439 WAEIQSVKPQIENPFTATGfqrnpankNAGKFITLADFLDFSKAkavTGVMINIENAAYLAS--KKGLGVVDAVKSALAK 516
Cdd:pfam03009  62 LEELKRLDIGAGNSGPLSG--------ERVPFPTLEEVLEFDWD---VGFNIEIKIKPYVEAiaPEEGLIVKDLLLSVDE 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971   517 STLDKQSTQKVLIQSDDSSVLASF-EAVPPYTRVLSIDkeiGGAPKPSVDEIKKYAEAVNllrTSLVTVSQSFTTGKTNV 595
Cdd:pfam03009 131 ILAKKADPRRVIFSSFNPDELKRLrELAPKLPLVFLSS---GRAYAEADLLERAAAFAGA---PALLGEVALVDEALPDL 204

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15242971   596 VEEMHKGNISVYV-SVLRNEYISVAFDYfsdptielatfisgsGVDGVITEFPAT 649
Cdd:pfam03009 205 VKRAHARGLVVHVwTVNNEDEMKRLLEL---------------GVDGVITDRPDT 244
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
356-656 4.36e-21

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 93.01  E-value: 4.36e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 356 LVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFC-HDAadltasttamTIfmSRATSVpeiqptNGIFS 434
Cdd:COG0584   4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVfHDP----------TL--DRTTNG------TGRVA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 435 fDLTWAEIQSVKPqienpftatgfqRNPANKNAGKFITLADFLDFSKakavTGVMINIE--NAAYLASkkglGVVDAVKS 512
Cdd:COG0584  66 -DLTLAELRQLDA------------GSGPDFAGERIPTLEEVLELVP----GDVGLNIEikSPPAAEP----DLAEAVAA 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 513 ALAKSTLDKQstqkVLIQSDDSSVLASF-EAVPPYTRVLSIDKeiggAPKPSVDEIKK-YAEAVNlLRTSLVTvsqsftt 590
Cdd:COG0584 125 LLKRYGLEDR----VIVSSFDPEALRRLrELAPDVPLGLLVEE----LPADPLELARAlGADGVG-PDYDLLT------- 188

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242971 591 gkTNVVEEMHKGNISVYVSVLRNEYisvafdyfsdptiELATFISgSGVDGVITEFPATATRYLKS 656
Cdd:COG0584 189 --PELVAAAHAAGLKVHVWTVNDPE-------------EMRRLLD-LGVDGIITDRPDLLRAVLRE 238
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 356-657 3.82e-11

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 65.46  E-value: 3.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  356 LVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDG-IAFCHDaadltasttamtIFMSRATSVPEIQP----TN 430
Cdd:PRK11143  28 IVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDqLVVLHD------------HYLDRVTDVAERFPdrarKD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  431 GIF-SFDLTWAEIQSVK----PQIENPFTATGF-QRNPANKNAGKFITLADFLDF------SKAKAVtGVMINIEnAAYL 498
Cdd:PRK11143  96 GRYyAIDFTLDEIKSLKftegFDIENGKKVQVYpGRFPMGKSDFRVHTFEEEIEFiqglnhSTGKNI-GIYPEIK-APWF 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  499 ASKKGLGVVDAVKSALAKSTLDKQStQKVLIQSDDSSVLASF--EAVPPYTRVL-------------SIDKEIGGAPKP- 562
Cdd:PRK11143 174 HHQEGKDIAAKVLEVLKKYGYTGKD-DKVYLQCFDANELKRIknELEPKMGMDLklvqliaytdwneTQEKQPDGKWVNy 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  563 ---------SVDEIKKYAEAVNLLRTSLVT-VSQSFTTGKTNVVEEMHKGNISVYVSVLRNEYISvafDYFSDPTIELAT 632
Cdd:PRK11143 253 nydwmfkpgAMKEVAKYADGIGPDYHMLVDeTSTPGNIKLTGMVKEAHQAKLVVHPYTVRADQLP---EYATDVNQLYDI 329

                        330       340
                 ....*....|....*....|....*
gi 15242971  633 FISGSGVDGVITEFPATATRYLKSP 657
Cdd:PRK11143 330 LYNQAGVDGVFTDFPDKAVKFLNKQ 354
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
41-337 4.43e-08

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 54.49  E-value: 4.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  41 PAVVARGGFSGLFPESSASANDLAIGTsspGLTML-CNLQMTKDGVGLCLSDIILDNATTISSvfPKAQKTYKvngqDLK 119
Cdd:COG0584   3 PLIIAHRGASGLAPENTLAAFRAALEL---GADGIeLDVQLTKDGVLVVFHDPTLDRTTNGTG--RVADLTLA----ELR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 120 GwfvLDYDADTIFNNVTLvqnifsrPSIfdgqmsvsavEDVLGTKPPKFWL-----SVQYDAFYMEHKLspAEYLRSLQF 194
Cdd:COG0584  74 Q---LDAGSGPDFAGERI-------PTL----------EEVLELVPGDVGLnieikSPPAAEPDLAEAV--AALLKRYGL 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 195 RGINVISSPEIGFLKSIGMDAGRAKTKLIFEFKDPEAVEpttnkkyseiqqnlAAIKAFASGVLVPKDYIwpidsakylk 274
Cdd:COG0584 132 EDRVIVSSFDPEALRRLRELAPDVPLGLLVEELPADPLE--------------LARALGADGVGPDYDLL---------- 187

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242971 275 pATTFVADAHKAGLEVYAsgfandlrtsfnYSYDPSAEYLQFVDNGqfsVDGVITDFPPTASQ 337
Cdd:COG0584 188 -TPELVAAAHAAGLKVHV------------WTVNDPEEMRRLLDLG---VDGIITDRPDLLRA 234
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 48-332 1.04e-05

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: 47.39  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971    48 GFSGLFPESSASANDLAIgtsSPGLTML-CNLQMTKDGVGLCLSDIILDNATTISSV---FPKAQktykVNGQDLKGWFV 123
Cdd:pfam03009   3 GASGSYPENTLASFRKAA---EAGADYIeFDVQLTKDGVPVVLHDFNLDRTTDGAGYvrdLTLEE----LKRLDIGAGNS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971   124 LDYDADTIfnNVTLVQNIFSRPsifdgqmsvSAVEDVLGTKPPKFW--LSVQYDAFYMEHKLSPAEYLRSLQFRGINVIS 201
Cdd:pfam03009  76 GPLSGERV--PFPTLEEVLEFD---------WDVGFNIEIKIKPYVeaIAPEEGLIVKDLLLSVDEILAKKADPRRVIFS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971   202 SPEIGFLKSIgmdAGRAKT-KLIFEFKDPEAVEPTTNKKYSeiqqNLAAIKAFASGVLVPKDYIwpidsakylkpaTTFV 280
Cdd:pfam03009 145 SFNPDELKRL---RELAPKlPLVFLSSGRAYAEADLLERAA----AFAGAPALLGEVALVDEAL------------PDLV 205

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15242971   281 ADAHKAGLEVYAsgfandlrtsfnYSYDPSAEYLQFVDNGqfsVDGVITDFP 332
Cdd:pfam03009 206 KRAHARGLVVHV------------WTVNNEDEMKRLLELG---VDGVITDRP 242
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 39-105 1.96e-04

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 44.28  E-value: 1.96e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15242971   39 QEPAVVARGGFSGLFPESSASANDLAIGTSSPGLTMlcNLQMTKDGVGLCLSDIILDNATTISSVFP 105
Cdd:PRK11143  25 AEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQ--DLVMTKDDQLVVLHDHYLDRVTDVAERFP 89
 
Name Accession Description Interval E-value
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 355-653 0e+00

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: 528.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 355 ALVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFCHDAADLTASTTAMT-IFMSRATSVPEIQPTNGIF 433
Cdd:cd08604   1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATsKFSNRATTVPEIGSTSGIF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 434 SFDLTWAEIQSVKPQIENPFTATGFQRNPANKNAGKFITLADFLDFSKAKAVTGVMINIENAAYLASKKGLGVVDAVKSA 513
Cdd:cd08604  81 TFDLTWSEIQTLKPAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNKSLSGVLINVENAAYLAEKKGLDVVDAVLDA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 514 LAKSTLDKQSTQKVLIQSDDSSVLASFEAVPPYTRVLSIDKEIGGAPKPSVDEIKKYAEAVNLLRTSLVTVSQSFTTGKT 593
Cdd:cd08604 161 LTNAGYDNQTAQKVLIQSTDSSVLAAFKKQISYERVYVVDETIRDASDSSIEEIKKFADAVVIDRGSVFPVSTSFLTRQT 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 594 NVVEEMHKGNISVYVSVLRNEYISVAFDYFSDPTIELATFISGSGVDGVITEFPATATRY 653
Cdd:cd08604 241 NVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSYVQGAGVDGFITEFPATAARY 300
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 41-338 2.87e-178

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: 511.55  E-value: 2.87e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  41 PAVVARGGFSGLFPESSASANDLAIGTSSPGLTMLCNLQMTKDGVGLCLSDIILDNATTISSVFPKAQKTYKVNGQDLKG 120
Cdd:cd08603   1 PLVIARGGFSGLFPDSSLFAYQFAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPKRKKTYSVNGVSTKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 121 WFVLDYDADTIFNnVTLVQNIFSRPSIFDGQMSVSAVEDVLGTKPP-KFWLSVQYDAFYMEHKLSPAEYLRSLQFR-GIN 198
Cdd:cd08603  81 WFSVDFTLAELQQ-VTLIQGIFSRTPIFDGQYPISTVEDVVTLAKPeGLWLNVQHDAFYQQHNLSMSSYLLSLSKTvKVD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 199 VISSPEIGFLKSIGMDAGRAKTKLIFEFKDPEAVEPTTNKKYSEIQQNLAAIKAFASGVLVPKDYIWPIDSAKYLKPATT 278
Cdd:cd08603 160 YISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSILKNLTFIKTFASGILVPKSYIWPVDSDQYLQPATS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 279 FVADAHKAGLEVYASGFANDLRTSFNYSYDPSAEYLQFVDNGQFSVDGVITDFPPTASQS 338
Cdd:cd08603 240 LVQDAHKAGLEVYASGFANDFDISYNYSYDPVAEYLSFVGNGNFSVDGVLSDFPITASEA 299
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 356-653 1.44e-145

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: 427.86  E-value: 1.44e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 356 LVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFCHDAADLTASTTAMTIFMSRATS-VPEIQPTNGIFS 434
Cdd:cd08571   2 LVIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPKRKKTyVVEGQSTSGIFS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 435 FDLTWAEIQSVKPQIENPFTAtgFQRNPANKNAGKFITLADFLDFSKAKAVTGVMINIENAAYLASKKGLGVVDAVKSAL 514
Cdd:cd08571  82 FDLTWAEIQTLKPIISNPFSV--LFRNPRNDNAGKILTLEDFLTLAKPKSLSGVWINVENAAFLAEHKGLLSVDAVLTSL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 515 AKSTLDkQSTQKVLIQSDDSSVLASFEAV---PPYTRVLSIDKEIGGAPKPSVDEIKKYAEAVNLLRTSLVTVS-QSFTT 590
Cdd:cd08571 160 SKAGYD-QTAKKVYISSPDSSVLKSFKKRvgtKLVFRVLDVDDTEPDTLLSNLTEIKKFASGVLVPKSYIWPVDsDSFLT 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242971 591 GKTNVVEEMHKGNISVYVSVLRNEYISVAFDYFSDPTIELATFISGS-GVDGVITEFPATATRY 653
Cdd:cd08571 239 PQTSVVQDAHKAGLEVYVSGFANEFVSLAYDYSADPTLEILSFVGNGnSVDGVITDFPATAARA 302
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 41-337 2.08e-118

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: 358.14  E-value: 2.08e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  41 PAVVARGGFSGLFPESSASANDLAIGTSspGLTMLCNLQMTKDGVGLCLSDIILDNATTISSVFPKAQKTYKVNGQDLKG 120
Cdd:cd08571   1 PLVIARGGASGDYPDSTDLAYQKAISDG--ADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPKRKKTYVVEGQSTSG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 121 WFVLDYDADTIFNNVTLVQNIFS---RPSIFDGQMSVSAVEDVLGTKPPK----FWLSVQYDAFYMEHK--LSPAEYLRS 191
Cdd:cd08571  79 IFSFDLTWAEIQTLKPIISNPFSvlfRNPRNDNAGKILTLEDFLTLAKPKslsgVWINVENAAFLAEHKglLSVDAVLTS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 192 LQFRG------INVISSPEIGFLKSIGmdaGRAKTKLIFEFKDPEAVEPTTnkkyseIQQNLAAIKAFASGVLVPKDYIW 265
Cdd:cd08571 159 LSKAGydqtakKVYISSPDSSVLKSFK---KRVGTKLVFRVLDVDDTEPDT------LLSNLTEIKKFASGVLVPKSYIW 229

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242971 266 PIDSAKYLKPATTFVADAHKAGLEVYASGFANDLRT-SFNYSYDPSAEYLQFVDNGqFSVDGVITDFPPTASQ 337
Cdd:cd08571 230 PVDSDSFLTPQTSVVQDAHKAGLEVYVSGFANEFVSlAYDYSADPTLEILSFVGNG-NSVDGVITDFPATAAR 301
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 41-332 6.14e-32

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: 126.26  E-value: 6.14e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  41 PAVVARGGFSGLFPESSASANDLAIGTsspGLTML-CNLQMTKDGVGLCLSDIILDNATTISSV--FPKAQKTYKVNGQD 117
Cdd:cd08602   1 PLVIAHRGASGYRPEHTLAAYQLAIEQ---GADFIePDLVSTKDGVLICRHEPELSGTTDVADHpeFADRKTTKTVDGVN 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 118 LKGWFVLDYDADTIfnnVTL--VQNI-FSRPSiFDGQMSVSAVEDVLG------------------TKPPKFWlsVQYDA 176
Cdd:cd08602  78 VTGWFTEDFTLAEL---KTLraRQRLpYRDQS-YDGQFPIPTFEEIIAlakaasaatgrtvgiypeIKHPTYF--NAPLG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 177 FYMEHKLspaeyLRSLQFRGINVISSP------EIGFLKSIgmdagRAKT--KLIFEFKDPEAVEPTT----NKKYSEI- 243
Cdd:cd08602 152 LPMEDKL-----LETLKKYGYTGKKAPvfiqsfEVTNLKYL-----RNKTdlPLVQLIDDATIPPQDTpegdSRTYADLt 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 244 -QQNLAAIKAFASGVLVPKDYIWPIDSAKYLKPATTFVADAHKAGLEVYASGFAN-DLRTSFNYSYDPSAEYLQFVDNGq 321
Cdd:cd08602 222 tDAGLKEIATYADGIGPWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNeNTFLPPDFFGDPYAEYRAFLDAG- 300

                       330
                ....*....|.
gi 15242971 322 fsVDGVITDFP 332
Cdd:cd08602 301 --VDGLFTDFP 309
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 356-647 1.57e-31

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: 125.10  E-value: 1.57e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 356 LVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFCHDAADLTASTTAMTI--FMSR-ATSVPEIQPTNGI 432
Cdd:cd08602   2 LVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHpeFADRkTTKTVDGVNVTGW 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 433 FSFDLTWAEIQSVKPQienpftatgfQRNPANKNA--GKF--ITLADFLDFSKAKAVT-----GVMINIENAAYLASKKG 503
Cdd:cd08602  82 FTEDFTLAELKTLRAR----------QRLPYRDQSydGQFpiPTFEEIIALAKAASAAtgrtvGIYPEIKHPTYFNAPLG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 504 LGVVDAVKSALAKSTLDKqSTQKVLIQSDDSS--------------VLASFEAVPPYTRVLSIDKEIGGAPKP-SVDEIK 568
Cdd:cd08602 152 LPMEDKLLETLKKYGYTG-KKAPVFIQSFEVTnlkylrnktdlplvQLIDDATIPPQDTPEGDSRTYADLTTDaGLKEIA 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 569 KYAEAVNLLRTSLV-TVSQSFTTGKTNVVEEMHKGNISVYVSVLRNEYISVAFDYFSDPTIELATFISgSGVDGVITEFP 647
Cdd:cd08602 231 TYADGIGPWKDLIIpSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNENTFLPPDFFGDPYAEYRAFLD-AGVDGLFTDFP 309
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 356-647 2.34e-31

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: 124.31  E-value: 2.34e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 356 LVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDG--IAFcHDAAdLTASTTAMTIFMSRATSVpeiqptNGIF 433
Cdd:cd08559   2 LVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGvlVAR-HDPT-LDRTTNVAEHFPFRGRKD------TGYF 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 434 SFDLTWAEIQSVKpqIENPFTATGFQRNPANKNAGKFITLADFLDFSKAK-AVTGVMINI--E-NAAYLASKKGLGVVDA 509
Cdd:cd08559  74 VIDFTLAELKTLR--AGSWFNQRYPERAPSYYGGFKIPTLEEVIELAQGLnKSTGRNVGIypEtKHPTFHKQEGPDIEEK 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 510 VKSALAKSTLDKQStQKVLIQSDDSSVL----ASFEAVPpytRVLSIDKEIGGAPKPSV-----------DEIKKYAEAV 574
Cdd:cd08559 152 LLEVLKKYGYTGKN-DPVFIQSFEPESLkrlrNETPDIP---LVQLIDYGDWAETDKKYtyawlttdaglKEIAKYADGI 227

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242971 575 NLLRTSLVTVSQSFTTGKTNVVEEMHKGNISVYVSVLRNEYISVAFDYFSDPTIELATfisgSGVDGVITEFP 647
Cdd:cd08559 228 GPWKSLIIPEDSNGLLVPTDLVKDAHKAGLLVHPYTFRNENLFLAPDFKQDMDALYNA----AGVDGVFTDFP 296
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 41-332 2.37e-26

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: 109.67  E-value: 2.37e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  41 PAVVARGGFSGLFPESSASANDLAIGTsspGLTML-CNLQMTKDGVGLCLSDIILDNATTISSVFPKAqktykvnGQDLK 119
Cdd:cd08559   1 PLVIAHRGASGYAPEHTLAAYALAIEM---GADYIeQDLVMTKDGVLVARHDPTLDRTTNVAEHFPFR-------GRKDT 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 120 GWFVLDY--------DADTIFNNVtlvqNIFSRPSiFDGQMSVSAVEDVL--------------G----TKPPKFWLSVQ 173
Cdd:cd08559  71 GYFVIDFtlaelktlRAGSWFNQR----YPERAPS-YYGGFKIPTLEEVIelaqglnkstgrnvGiypeTKHPTFHKQEG 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 174 YDafyMEHKLspaeyLRSLQFRGIN------VISSPEIGFLKSIgmdagRAKT---KLIFEFKDPEAVEPTTNKKYSEI- 243
Cdd:cd08559 146 PD---IEEKL-----LEVLKKYGYTgkndpvFIQSFEPESLKRL-----RNETpdiPLVQLIDYGDWAETDKKYTYAWLt 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 244 -QQNLAAIKAFASGVLVPKDYIWPIDSaKYLKPATTFVADAHKAGLEVYASGFAND-LRTSFNYSYDPSAEYLqfvdngQ 321
Cdd:cd08559 213 tDAGLKEIAKYADGIGPWKSLIIPEDS-NGLLVPTDLVKDAHKAGLLVHPYTFRNEnLFLAPDFKQDMDALYN------A 285

                       330
                ....*....|.
gi 15242971 322 FSVDGVITDFP 332
Cdd:cd08559 286 AGVDGVFTDFP 296
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 360-649 1.68e-22

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: 97.09  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971   360 HNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFC-HDAadltasttamtiFMSRATSVPEiqptngiFSFDLT 438
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVlHDF------------NLDRTTDGAG-------YVRDLT 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971   439 WAEIQSVKPQIENPFTATGfqrnpankNAGKFITLADFLDFSKAkavTGVMINIENAAYLAS--KKGLGVVDAVKSALAK 516
Cdd:pfam03009  62 LEELKRLDIGAGNSGPLSG--------ERVPFPTLEEVLEFDWD---VGFNIEIKIKPYVEAiaPEEGLIVKDLLLSVDE 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971   517 STLDKQSTQKVLIQSDDSSVLASF-EAVPPYTRVLSIDkeiGGAPKPSVDEIKKYAEAVNllrTSLVTVSQSFTTGKTNV 595
Cdd:pfam03009 131 ILAKKADPRRVIFSSFNPDELKRLrELAPKLPLVFLSS---GRAYAEADLLERAAAFAGA---PALLGEVALVDEALPDL 204

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15242971   596 VEEMHKGNISVYV-SVLRNEYISVAFDYfsdptielatfisgsGVDGVITEFPAT 649
Cdd:pfam03009 205 VKRAHARGLVVHVwTVNNEDEMKRLLEL---------------GVDGVITDRPDT 244
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
356-656 4.36e-21

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 93.01  E-value: 4.36e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 356 LVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFC-HDAadltasttamTIfmSRATSVpeiqptNGIFS 434
Cdd:COG0584   4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVfHDP----------TL--DRTTNG------TGRVA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 435 fDLTWAEIQSVKPqienpftatgfqRNPANKNAGKFITLADFLDFSKakavTGVMINIE--NAAYLASkkglGVVDAVKS 512
Cdd:COG0584  66 -DLTLAELRQLDA------------GSGPDFAGERIPTLEEVLELVP----GDVGLNIEikSPPAAEP----DLAEAVAA 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 513 ALAKSTLDKQstqkVLIQSDDSSVLASF-EAVPPYTRVLSIDKeiggAPKPSVDEIKK-YAEAVNlLRTSLVTvsqsftt 590
Cdd:COG0584 125 LLKRYGLEDR----VIVSSFDPEALRRLrELAPDVPLGLLVEE----LPADPLELARAlGADGVG-PDYDLLT------- 188

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242971 591 gkTNVVEEMHKGNISVYVSVLRNEYisvafdyfsdptiELATFISgSGVDGVITEFPATATRYLKS 656
Cdd:COG0584 189 --PELVAAAHAAGLKVHVWTVNDPE-------------EMRRLLD-LGVDGIITDRPDLLRAVLRE 238
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 356-652 3.12e-19

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: 88.98  E-value: 3.12e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 356 LVITHNGASGDYPGCTDLAYQKAVDDGAD--VIDCSVQMSKDGIAFCHDAADLTASTTAMTIFMSRATS-VPEIQPTNGI 432
Cdd:cd08603   2 LVIARGGFSGLFPDSSLFAYQFAASSSSPdvALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPKRKKTySVNGVSTKGW 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 433 FSFDLTWAEIQSVKpqienpFTATGFQRNPANKNAGKFITLAdflDFSKAKAVTGVMINIENAAYLASKkglgvvdavKS 512
Cdd:cd08603  82 FSVDFTLAELQQVT------LIQGIFSRTPIFDGQYPISTVE---DVVTLAKPEGLWLNVQHDAFYQQH---------NL 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 513 ALAKSTLDKQSTQKV-LIQSDDSSVLASF--EAVPPYTR-VLS-IDKEiggAPKPSVDeiKKYAE-AVNL--LRT--SLV 582
Cdd:cd08603 144 SMSSYLLSLSKTVKVdYISSPEVGFLKSIggRVGRNGTKlVFRfLDKD---DVEPSTN--QTYGSiLKNLtfIKTfaSGI 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 583 TVSQSF----TTGK-----TNVVEEMHKGNISVYVSVLRNEyISVAFDYFSDPTIELATFISGSG--VDGVITEFPATAT 651
Cdd:cd08603 219 LVPKSYiwpvDSDQylqpaTSLVQDAHKAGLEVYASGFAND-FDISYNYSYDPVAEYLSFVGNGNfsVDGVLSDFPITAS 297


                .
gi 15242971 652 R 652
Cdd:cd08603 298 E 298
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 41-335 1.93e-16

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: 80.84  E-value: 1.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  41 PAVVARGGFSGLFPESSASANDLAIGTSSPGLTmlCNLQMTKDGVGLCLSDIILDNATTI-SSVFPKAQKTYKvNGQDLK 119
Cdd:cd08604   1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVID--CSVQMSKDGVPFCLDSINLINSTTVaTSKFSNRATTVP-EIGSTS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 120 GWFVLDYDADTIFNNVTLVQNIFSRPSIF-----DGQMSVSAVEDVLGTKPPKFWLSVQYDafyMEHklspAEYLRSLQf 194
Cdd:cd08604  78 GIFTFDLTWSEIQTLKPAISNPYSVTGLFrnpanKNAGKFLTLSDFLDLAKNKSLSGVLIN---VEN----AAYLAEKK- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 195 rGINVISSPeIGFLKSIGMDAGRAKTKLI--------FEFKDPEAVE-----PTTNKKYSEIqqNLAAIKAFASGVLVPK 261
Cdd:cd08604 150 -GLDVVDAV-LDALTNAGYDNQTAQKVLIqstdssvlAAFKKQISYErvyvvDETIRDASDS--SIEEIKKFADAVVIDR 225

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242971 262 DYIWPIDSAkYLKPATTFVADAHKAGLEVYASGFAND-LRTSFNYSYDPSAEYLQFVdnGQFSVDGVITDFPPTA 335
Cdd:cd08604 226 GSVFPVSTS-FLTRQTNVVEKLQSANLTVYVEVLRNEfVSLAFDFFADPTVEINSYV--QGAGVDGFITEFPATA 297
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 355-648 3.12e-13

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: 71.27  E-value: 3.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 355 ALVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFC-HDAAdLTASTTAMTIFmsratsvPEIQPTNGIF 433
Cdd:cd08600   1 KIIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVViHDHY-LDNVTNVAEKF-------PDRKRKDGRY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 434 -SFDLTWAEIQSVKpQIENPFTATGF------QRNPANKNAGKFITLADFLDF------SKAKAVtGVMINIEnAAYLAS 500
Cdd:cd08600  73 yVIDFTLDELKSLS-VTERFDIENGKkvqvypNRFPLWKSDFKIHTLEEEIELiqglnkSTGKNV-GIYPEIK-APWFHH 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 501 KKGLGVVDAVKSALAKSTLDKQSTqKVLIQSDDSSVLASF--EAVPPYTRVLSI-------------DKEIGGAPKPSVD 565
Cdd:cd08600 150 QEGKDIAAATLEVLKKYGYTSKND-KVYLQTFDPNELKRIknELLPKMGMDLKLvqliaytdwgetqEKDPGGWVNYDYD 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 566 ---------EIKKYAEAVNLLRTSLVT-VSQSFTTGKTNVVEEMHKGNISVYVSVLRNEYISvafDYFSDPTIELATFIS 635
Cdd:cd08600 229 wmftkgglkEIAKYADGVGPWYSMIIEeKSSKGNIVLTDLVKDAHEAGLEVHPYTVRKDALP---EYAKDADQLLDALLN 305

                       330
                ....*....|...
gi 15242971 636 GSGVDGVITEFPA 648
Cdd:cd08600 306 KAGVDGVFTDFPD 318
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 357-646 5.91e-12

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: 64.98  E-value: 5.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 357 VITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFC-HDaadltasttamtifmsratsVPeiqptngifsf 435
Cdd:cd08556   1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVViHD--------------------IP----------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 436 dltwaeiqsvkpqienpftatgfqrnpanknagkfiTLADFLDFskakAVTGVMINIENAAYlasKKGLGVVDAVKSALA 515
Cdd:cd08556  50 ------------------------------------TLEEVLEL----VKGGVGLNIELKEP---TRYPGLEAKVAELLR 86

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 516 KSTLDKQstqkVLIQSDDSSVLASF-EAVPPYTRVLSIDKEIGGAPKPSVDeIKKYAEAVNlLRTSLVTvsqsfttgkTN 594
Cdd:cd08556  87 EYGLEER----VVVSSFDHEALRALkELDPEVPTGLLVDKPPLDPLLAELA-RALGADAVN-PHYKLLT---------PE 151

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15242971 595 VVEEMHKGNISVYVSVLRNEyisvafdyfsdptiELATFISGSGVDGVITEF 646
Cdd:cd08556 152 LVRAAHAAGLKVYVWTVNDP--------------EDARRLLALGVDGIITDD 189
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 356-657 3.82e-11

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 65.46  E-value: 3.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  356 LVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDG-IAFCHDaadltasttamtIFMSRATSVPEIQP----TN 430
Cdd:PRK11143  28 IVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDqLVVLHD------------HYLDRVTDVAERFPdrarKD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  431 GIF-SFDLTWAEIQSVK----PQIENPFTATGF-QRNPANKNAGKFITLADFLDF------SKAKAVtGVMINIEnAAYL 498
Cdd:PRK11143  96 GRYyAIDFTLDEIKSLKftegFDIENGKKVQVYpGRFPMGKSDFRVHTFEEEIEFiqglnhSTGKNI-GIYPEIK-APWF 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  499 ASKKGLGVVDAVKSALAKSTLDKQStQKVLIQSDDSSVLASF--EAVPPYTRVL-------------SIDKEIGGAPKP- 562
Cdd:PRK11143 174 HHQEGKDIAAKVLEVLKKYGYTGKD-DKVYLQCFDANELKRIknELEPKMGMDLklvqliaytdwneTQEKQPDGKWVNy 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  563 ---------SVDEIKKYAEAVNLLRTSLVT-VSQSFTTGKTNVVEEMHKGNISVYVSVLRNEYISvafDYFSDPTIELAT 632
Cdd:PRK11143 253 nydwmfkpgAMKEVAKYADGIGPDYHMLVDeTSTPGNIKLTGMVKEAHQAKLVVHPYTVRADQLP---EYATDVNQLYDI 329

                        330       340
                 ....*....|....*....|....*
gi 15242971  633 FISGSGVDGVITEFPATATRYLKSP 657
Cdd:PRK11143 330 LYNQAGVDGVFTDFPDKAVKFLNKQ 354
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 357-570 1.21e-09

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity to Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176524 [Multi-domain]  Cd Length: 233  Bit Score: 59.25  E-value: 1.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 357 VITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDG-IAFCHDAadltasTTAMTIFMSRATSvpeiqptngifsf 435
Cdd:cd08582   1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGeLVCVHDP------TLKRTSGGDGAVS------------- 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 436 DLTWAEIQSVKPqienpftatGFQRNPANKNAgKFITLADFLDFSKAKAVtGVMINIENAAYlaskkGLGVVDAVKSALA 515
Cdd:cd08582  62 DLTLAELRKLDI---------GSWKGESYKGE-KVPTLEEYLAIVPKYGK-KLFIEIKHPRR-----GPEAEEELLKLLK 125

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15242971 516 KSTLDKQstQKVLIqSDDSSVLASFEAVPPYTRV--LSIDKEIGGAPKPSVDEIKKY 570
Cdd:cd08582 126 ESGLLPE--QIVII-SFDAEALKRVRELAPTLETlwLRNYKSPKEDPRPLAKSGGAA 179
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 357-403 4.98e-09

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: 57.23  E-value: 4.98e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15242971 357 VITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDG-IAFCHDA 403
Cdd:cd08570   1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGvVVISHDP 48
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 356-442 1.40e-08

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


Pssm-ID: 176543 [Multi-domain]  Cd Length: 256  Bit Score: 56.56  E-value: 1.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 356 LVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDG--IAFcHDAA-DLTASTTAMTIFMsratsvpeiqptngi 432
Cdd:cd08601   2 AVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGvlVAM-HDETlDRTTNIERPGPVK--------------- 65

                        90
                ....*....|
gi 15242971 433 fsfDLTWAEI 442
Cdd:cd08601  66 ---DYTLAEI 72
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 356-502 2.16e-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: 56.07  E-value: 2.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 356 LVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDG-IAFCHDaADLtasttamtifmSRATSVpeiqptNGIFS 434
Cdd:cd08575   2 LHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGqVVVFHD-WDL-----------DRLTGG------SGLVS 63

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242971 435 fDLTWAEIQSVKPQIenPFTATGFQRN-PANKNAGKFITLADFLD-FSKakavTGVMINI--ENAAYLASKK 502
Cdd:cd08575  64 -DLTYAELPPLDAGY--GYTFDGGKTGyPRGGGDGRIPTLEEVFKaFPD----TPINIDIksPDAEELIAAV 128
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 356-402 2.38e-08

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: 55.26  E-value: 2.38e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15242971 356 LVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDG-IAFCHD 402
Cdd:cd08563   2 LIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGqLVVIHD 49
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
41-337 4.43e-08

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 54.49  E-value: 4.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  41 PAVVARGGFSGLFPESSASANDLAIGTsspGLTML-CNLQMTKDGVGLCLSDIILDNATTISSvfPKAQKTYKvngqDLK 119
Cdd:COG0584   3 PLIIAHRGASGLAPENTLAAFRAALEL---GADGIeLDVQLTKDGVLVVFHDPTLDRTTNGTG--RVADLTLA----ELR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 120 GwfvLDYDADTIFNNVTLvqnifsrPSIfdgqmsvsavEDVLGTKPPKFWL-----SVQYDAFYMEHKLspAEYLRSLQF 194
Cdd:COG0584  74 Q---LDAGSGPDFAGERI-------PTL----------EEVLELVPGDVGLnieikSPPAAEPDLAEAV--AALLKRYGL 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 195 RGINVISSPEIGFLKSIGMDAGRAKTKLIFEFKDPEAVEpttnkkyseiqqnlAAIKAFASGVLVPKDYIwpidsakylk 274
Cdd:COG0584 132 EDRVIVSSFDPEALRRLRELAPDVPLGLLVEELPADPLE--------------LARALGADGVGPDYDLL---------- 187

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242971 275 pATTFVADAHKAGLEVYAsgfandlrtsfnYSYDPSAEYLQFVDNGqfsVDGVITDFPPTASQ 337
Cdd:COG0584 188 -TPELVAAAHAAGLKVHV------------WTVNDPEEMRRLLDLG---VDGIITDRPDLLRA 234
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 43-332 2.02e-07

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: 53.55  E-value: 2.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  43 VVARGGFSGLFPESSASANDLAIGTSSPGLTMlcNLQMTKDGVGLCLSDIILDNATTISSVFPKAQKTykvNGQdlkgWF 122
Cdd:cd08600   3 IIAHRGASGYLPEHTLEAKALAYAQGADYLEQ--DVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKRK---DGR----YY 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 123 VLDYDADTI--------FN--NVTLVQNIFSRPSIFDGQMSVSAVEDVLG------------------TKPPKFWLSVQY 174
Cdd:cd08600  74 VIDFTLDELkslsvterFDieNGKKVQVYPNRFPLWKSDFKIHTLEEEIEliqglnkstgknvgiypeIKAPWFHHQEGK 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 175 D--AFYME--------HKLSPAeYLRSLQF---RGINVISSPEIGF-LKSIGMDAGRaKTKLIFEFKDPEAVEptTNKKY 240
Cdd:cd08600 154 DiaAATLEvlkkygytSKNDKV-YLQTFDPnelKRIKNELLPKMGMdLKLVQLIAYT-DWGETQEKDPGGWVN--YDYDW 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 241 SEIQQNLAAIKAFASGVLVPKDYIWPIDSAKYLKPATTFVADAHKAGLEVYASGFANDLRTSFNYSYDPSAEYLQFvdng 320
Cdd:cd08600 230 MFTKGGLKEIAKYADGVGPWYSMIIEEKSSKGNIVLTDLVKDAHEAGLEVHPYTVRKDALPEYAKDADQLLDALLN---- 305

                       330
                ....*....|..
gi 15242971 321 QFSVDGVITDFP 332
Cdd:cd08600 306 KAGVDGVFTDFP 317
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 356-410 2.89e-07

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: 52.71  E-value: 2.89e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15242971 356 LVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFCHDAADLTAST 410
Cdd:cd08580   2 LIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLT 56
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 357-403 3.67e-06

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: 49.18  E-value: 3.67e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15242971 357 VITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFC-HDA 403
Cdd:cd08561   1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVViHDE 48
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 357-647 4.21e-06

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: 48.85  E-value: 4.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 357 VITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDG-IAFCHD---AADLTASTTamtifmsratsvPEIQPTNGI 432
Cdd:cd08567   3 LQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGvIVVSHDpklNPDITRDPD------------GAWLPYEGP 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 433 FSFDLTWAEIQSV-----KPqieNPFTATGF--QRNPANKnagKFITLADFLDFSKAKAVTGVMINIE------NAAYLA 499
Cdd:cd08567  71 ALYELTLAEIKQLdvgekRP---GSDYAKLFpeQIPVPGT---RIPTLEEVFALVEKYGNQKVRFNIEtksdpdRDILHP 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 500 SKKGLgvVDAVKSALAKSTLDKqstqKVLIQSDDSSVLASFEAVPPYTRV--LSIDKEIGGAPKpsvdeikkyaeavNLL 577
Cdd:cd08567 145 PPEEF--VDAVLAVIRKAGLED----RVVLQSFDWRTLQEVRRLAPDIPTvaLTEETTLGNLPR-------------AAK 205

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242971 578 RTSLVTVSQSFTTGKTNVVEEMHKGNISVYV-SVLRNEyisvafdyfsdptiELATFISgSGVDGVITEFP 647
Cdd:cd08567 206 KLGADIWSPYFTLVTKELVDEAHALGLKVVPwTVNDPE--------------DMARLID-LGVDGIITDYP 261
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 357-402 6.61e-06

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: 48.10  E-value: 6.61e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 15242971 357 VITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAF-CHD 402
Cdd:cd08581   1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVvFHD 47
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 41-332 9.94e-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: 47.70  E-value: 9.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971  41 PAVVARGGFSGLFPESSASANDLAIgtsSPGLTML-CNLQMTKDGVGLCLSDIILDNATTISSVFPKAQKTYKVNGQ-DL 118
Cdd:cd08601   1 NAVIAHRGASGYAPEHTFAAYDLAR---EMGADYIeLDLQMTKDGVLVAMHDETLDRTTNIERPGPVKDYTLAEIKQlDA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 119 KGWFvldydadtifnNVTLVQNifSRPSiFDGQmSVSAVEDVL---GTKPpkfwlsvqydAFYMEHKlSPAEY------- 188
Cdd:cd08601  78 GSWF-----------NKAYPEY--ARES-YSGL-KVPTLEEVIeryGGRA----------NYYIETK-SPDLYpgmeekl 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 189 LRSLQFRGIN---------VISSPEIGFLKsigmdagraktKLIFEFKDPEAVEPT-TNKKYSEIQQNLAAIKAFASGvl 258
Cdd:cd08601 132 LATLDKYGLLtdnlkngqvIIQSFSKESLK-----------KLHQLNPNIPLVQLLwYGEGAETYDKWLDEIKEYAIG-- 198

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242971 259 vpkdyIWPidSAKYLKPAttFVADAHKAGLEVYAsgfandlrtsfnYSYDPSAEYLQFVDNGqfsVDGVITDFP 332
Cdd:cd08601 199 -----IGP--SIADADPW--MVHLIHKKGLLVHP------------YTVNEKADMIRLINWG---VDGMFTNYP 248
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 48-332 1.04e-05

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: 47.39  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971    48 GFSGLFPESSASANDLAIgtsSPGLTML-CNLQMTKDGVGLCLSDIILDNATTISSV---FPKAQktykVNGQDLKGWFV 123
Cdd:pfam03009   3 GASGSYPENTLASFRKAA---EAGADYIeFDVQLTKDGVPVVLHDFNLDRTTDGAGYvrdLTLEE----LKRLDIGAGNS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971   124 LDYDADTIfnNVTLVQNIFSRPsifdgqmsvSAVEDVLGTKPPKFW--LSVQYDAFYMEHKLSPAEYLRSLQFRGINVIS 201
Cdd:pfam03009  76 GPLSGERV--PFPTLEEVLEFD---------WDVGFNIEIKIKPYVeaIAPEEGLIVKDLLLSVDEILAKKADPRRVIFS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971   202 SPEIGFLKSIgmdAGRAKT-KLIFEFKDPEAVEPTTNKKYSeiqqNLAAIKAFASGVLVPKDYIwpidsakylkpaTTFV 280
Cdd:pfam03009 145 SFNPDELKRL---RELAPKlPLVFLSSGRAYAEADLLERAA----AFAGAPALLGEVALVDEAL------------PDLV 205

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15242971   281 ADAHKAGLEVYAsgfandlrtsfnYSYDPSAEYLQFVDNGqfsVDGVITDFP 332
Cdd:pfam03009 206 KRAHARGLVVHV------------WTVNNEDEMKRLLELG---VDGVITDRP 242
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 345-477 8.17e-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: 8.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 345 QNGNL-PKAGhalVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFC-HDAAdltasttamtifMSRATS 422
Cdd:cd08610  15 EKETLgPKPT---IIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLmHDFT------------LKRTTN 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242971 423 VPEIQPTN-----GIFSFDlTWAEIQS----VKPQienPFTATG-FQRNPANKNAGKFI-TLADFL 477
Cdd:cd08610  80 IGEVQPESacenpAFFNWD-FLSTLNAgkwfVKPR---PFYNMKpLSEADKERARNQSIpKLSNFL 141
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 341-445 1.11e-04

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: 44.91  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 341 CFSHQNGNLPKAGhalVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFCHDAADLTASTTAMTIFMSRA 420
Cdd:cd08609  16 CIMEENNLPPKPA---LVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKDVFPGRD 92

                        90       100
                ....*....|....*....|....*
gi 15242971 421 TsvpeiqptngIFSFDLTWAEIQSV 445
Cdd:cd08609  93 A----------AGSNNFTWTELKTL 107
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 39-105 1.96e-04

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 44.28  E-value: 1.96e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15242971   39 QEPAVVARGGFSGLFPESSASANDLAIGTSSPGLTMlcNLQMTKDGVGLCLSDIILDNATTISSVFP 105
Cdd:PRK11143  25 AEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQ--DLVMTKDDQLVVLHDHYLDRVTDVAERFP 89
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 357-554 1.96e-04

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: 43.37  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 357 VITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAF-CHDAadltasttamTIfmSRATSvpeiqpTNGIFSf 435
Cdd:cd08562   1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVlIHDD----------TL--DRTTN------GSGAVT- 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 436 DLTWAEIQsvkpQIE--NPFtatgfqrNPANKNAgKFITLADFLDFSKAkavTGVMINIENAAYLASKKGLG-VVDAVKS 512
Cdd:cd08562  62 ELTWAELA----QLDagSWF-------SPEFAGE-PIPTLADVLELARE---LGLGLNLEIKPDPGDEALTArVVAAALR 126

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15242971 513 ALAkstldkQSTQKVLIQSDDSSVLASF-EAVPPYTRVLSIDK 554
Cdd:cd08562 127 ELW------PHASKLLLSSFSLEALRAArRAAPELPLGLLFDT 163
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 357-454 2.71e-04

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: 43.40  E-value: 2.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 357 VITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIA-FCHDaaDLTASTTAMTIFMSratsvpeiqptngifsf 435
Cdd:cd08573   1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPvLMHD--DTVDRTTDGTGLVA----------------- 61

                        90
                ....*....|....*....
gi 15242971 436 DLTWAEIQSVKPQIENPFT 454
Cdd:cd08573  62 ELTWEELRKLNAAAKHRLS 80
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 350-482 6.81e-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: 6.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 350 PKAGHALVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFC-HDAADLTASTTAMTI-FMSRATSVPeIQ 427
Cdd:cd08560  12 PFRKTDFSIGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCrHSQCDLHTTTNILAIpELAAKCTQP-FT 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242971 428 PTNGIF-------SFDLTWAEIQSVKPQIE--NP--FTATGFQ------RNPANKNAGKFITLADFLDFSKA 482
Cdd:cd08560  91 PANATKpasaeccTSDITLAEFKSLCGKMDasNPsaTTPEEYQngtpdwRTDLYATCGTLMTHKESIALFKS 162
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 358-402 3.11e-03

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: 40.28  E-value: 3.11e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15242971 358 ITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDG-IAFCHD 402
Cdd:cd08612  30 ISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGqVVVSHD 75
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 356-444 3.90e-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: 39.60  E-value: 3.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 356 LVITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFC-HDaadltaSTtamtifMSRATSVPEIQPTNGIF- 433
Cdd:cd08574   3 ALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLmHD------RT------LRRTTNVADVFPERAHEr 70

                        90
                ....*....|.
gi 15242971 434 SFDLTWAEIQS 444
Cdd:cd08574  71 ASMFTWTDLQQ 81
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 357-647 3.95e-03

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: 39.45  E-value: 3.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 357 VITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDGIAFC-HDaADLTasttamtifmsRATSVP-EIQptngifs 434
Cdd:cd08579   1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVmHD-ANLK-----------RLAGVNkKVW------- 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 435 fDLTWAEIQSVKpqienpftatgfqrNPANKNAGKFITLADFLDfsKAKAVtGVMINIE------NAAYLASKkglgVVD 508
Cdd:cd08579  62 -DLTLEELKKLT--------------IGENGHGAKIPSLDEYLA--LAKGL-KQKLLIElkphghDSPDLVEK----FVK 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 509 AVKSALAKstldkqstQKVLIQSDDSSVLASFEAVPPYTRV-LSIDKEIGGAPKPSVDeikkyaeavnllrtsLVTVSQS 587
Cdd:cd08579 120 LYKQNLIE--------NQHQVHSLDYRVIEKVKKLDPKIKTgYILPFNIGNLPKTNVD---------------FYSIEYS 176

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242971 588 FTTgkTNVVEEMHKGNISVYVSVLRNEYisvafdyfsdptiELATFISgSGVDGVITEFP 647
Cdd:cd08579 177 TLN--KEFIRQAHQNGKKVYVWTVNDPD-------------DMQRYLA-MGVDGIITDYP 220
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 357-396 5.84e-03

Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases superfamily; The PI-PLC-like phosphodiesterases superfamily represents the catalytic domains of bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11), glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria, as well as their uncharacterized homologs found in organisms ranging from bacteria and archaea to metazoans, plants, and fungi. PI-PLCs are ubiquitous enzymes hydrolyzing the membrane lipid phosphoinositides to yield two important second messengers, inositol phosphates and diacylglycerol (DAG). GP-GDEs play essential roles in glycerol metabolism and catalyze the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols that are major sources of carbon and phosphate. Both, PI-PLCs and GP-GDEs, can hydrolyze the 3'-5' phosphodiester bonds in different substrates, and utilize a similar mechanism of general base and acid catalysis with conserved histidine residues, which consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81, glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs). The residues essential for enzyme activities and metal binding are not conserved in these sequence homologs, which might suggest that the function of catalytic domains in these proteins might be distinct from those in typical PLC-like phosphodiesterases.


Pssm-ID: 176498 [Multi-domain]  Cd Length: 179  Bit Score: 38.57  E-value: 5.84e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 15242971 357 VITHNGASGDYPGCTDLAYQKAVDDGADVIDCSVQMSKDG 396
Cdd:cd08555   1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDG 40
 
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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