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Conserved domains on  [gi|30697435|ref|NP_176869|]
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SHV3-like 2 [Arabidopsis thaliana]

Protein Classification

glycerophosphodiester phosphodiesterase family protein( domain architecture ID 10171244)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 50-349 0e+00

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: 543.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  50 PLVIARGGFSGLYPDSSIAAYQLATLTSVADVVLWCDLQLTKDGLGICFPDLNLANASTIDRVYPNREKSYSVNGVTTKG 129
Cdd:cd08603   1 PLVIARGGFSGLFPDSSLFAYQFAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPKRKKTYSVNGVSTKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 130 WFPNDFSLTELQNFLLIRGILSRTDRFDGNgYLISTIEDVVTTLNREGFWLNVQHDAFYEQQNLSMSSFLLSVSRTVSID 209
Cdd:cd08603  81 WFSVDFTLAELQQVTLIQGIFSRTPIFDGQ-YPISTVEDVVTLAKPEGLWLNVQHDAFYQQHNLSMSSYLLSLSKTVKVD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 210 FISSPEVNFFKKITGSFGRNGPTFVFQFLGKEDFEPTTNRTYGSILSNLTFVKTFASGILVPKSYILPLDDEQYLVPHTS 289
Cdd:cd08603 160 YISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSILKNLTFIKTFASGILVPKSYIWPVDSDQYLQPATS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 290 LVQDAHKAGLQVYVSGFANDVDIAYNYSSDPVSEYLSFVDNGDFSVDGVLSDFPITASAA 349
Cdd:cd08603 240 LVQDAHKAGLEVYASGFANDFDISYNYSYDPVAEYLSFVGNGNFSVDGVLSDFPITASEA 299
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 366-667 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: 531.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 366 FLVISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLRNSIAALQNTFSNRSTSVPEISSVPGIF 445
Cdd:cd08604   1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSKFSNRATTVPEIGSTSGIF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 446 TFSLTWPEIQSLTPAISNPFRVYRIFRNPREKNSGKLISLSQFLDLAKTYtSLSGVLISVENAAYLREKQGLDVVQAVLD 525
Cdd:cd08604  81 TFDLTWSEIQTLKPAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNK-SLSGVLINVENAAYLAEKKGLDVVDAVLD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 526 TLTEAGYSNGtTTTKVMIQSTNSSVLVDFKKQSKYETVYKIEETIGNIRDSAIEDIKKFANAVVINKDSVFPNSDSFLTG 605
Cdd:cd08604 160 ALTNAGYDNQ-TAQKVLIQSTDSSVLAAFKKQISYERVYVVDETIRDASDSSIEEIKKFADAVVIDRGSVFPVSTSFLTR 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30697435 606 QTNVVERLQKSQLPVYVELFRNEFVSQAYDFFSDATVEINAYIYGAGINGTITEFPFTAARY 667
Cdd:cd08604 239 QTNVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSYVQGAGVDGFITEFPATAARY 300
 
Name Accession Description Interval E-value
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 50-349 0e+00

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: 543.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  50 PLVIARGGFSGLYPDSSIAAYQLATLTSVADVVLWCDLQLTKDGLGICFPDLNLANASTIDRVYPNREKSYSVNGVTTKG 129
Cdd:cd08603   1 PLVIARGGFSGLFPDSSLFAYQFAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPKRKKTYSVNGVSTKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 130 WFPNDFSLTELQNFLLIRGILSRTDRFDGNgYLISTIEDVVTTLNREGFWLNVQHDAFYEQQNLSMSSFLLSVSRTVSID 209
Cdd:cd08603  81 WFSVDFTLAELQQVTLIQGIFSRTPIFDGQ-YPISTVEDVVTLAKPEGLWLNVQHDAFYQQHNLSMSSYLLSLSKTVKVD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 210 FISSPEVNFFKKITGSFGRNGPTFVFQFLGKEDFEPTTNRTYGSILSNLTFVKTFASGILVPKSYILPLDDEQYLVPHTS 289
Cdd:cd08603 160 YISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSILKNLTFIKTFASGILVPKSYIWPVDSDQYLQPATS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 290 LVQDAHKAGLQVYVSGFANDVDIAYNYSSDPVSEYLSFVDNGDFSVDGVLSDFPITASAA 349
Cdd:cd08603 240 LVQDAHKAGLEVYASGFANDFDISYNYSYDPVAEYLSFVGNGNFSVDGVLSDFPITASEA 299
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 366-667 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: 531.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 366 FLVISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLRNSIAALQNTFSNRSTSVPEISSVPGIF 445
Cdd:cd08604   1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSKFSNRATTVPEIGSTSGIF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 446 TFSLTWPEIQSLTPAISNPFRVYRIFRNPREKNSGKLISLSQFLDLAKTYtSLSGVLISVENAAYLREKQGLDVVQAVLD 525
Cdd:cd08604  81 TFDLTWSEIQTLKPAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNK-SLSGVLINVENAAYLAEKKGLDVVDAVLD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 526 TLTEAGYSNGtTTTKVMIQSTNSSVLVDFKKQSKYETVYKIEETIGNIRDSAIEDIKKFANAVVINKDSVFPNSDSFLTG 605
Cdd:cd08604 160 ALTNAGYDNQ-TAQKVLIQSTDSSVLAAFKKQISYERVYVVDETIRDASDSSIEEIKKFADAVVIDRGSVFPVSTSFLTR 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30697435 606 QTNVVERLQKSQLPVYVELFRNEFVSQAYDFFSDATVEINAYIYGAGINGTITEFPFTAARY 667
Cdd:cd08604 239 QTNVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSYVQGAGVDGFITEFPATAARY 300
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 373-661 1.67e-20

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: 91.31  E-value: 1.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   373 GASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLrnsiaalqntfsNRSTSVPEissvpgiFTFSLTWP 452
Cdd:pfam03009   3 GASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNL------------DRTTDGAG-------YVRDLTLE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   453 EIQSLTPAIsnpfrvyRIFRNPREKNSgKLISLSQFLDLAKTYTSLSGVLISVENAAYLRE--KQGLDVVQAVLDTLTEA 530
Cdd:pfam03009  64 ELKRLDIGA-------GNSGPLSGERV-PFPTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEegLIVKDLLLSVDEILAKK 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   531 GysngtTTTKVMIQSTNSSVLVDFK-KQSKYETVykieeTIGNIRDSAiEDIKKFANAVVINKDSVFPNSDSFLTGQTNV 609
Cdd:pfam03009 136 A-----DPRRVIFSSFNPDELKRLReLAPKLPLV-----FLSSGRAYA-EADLLERAAAFAGAPALLGEVALVDEALPDL 204

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30697435   610 VERLQKSQLPVYVelfrnefvsqaYdffsdaTVEINAYIY---GAGINGTITEFP 661
Cdd:pfam03009 205 VKRAHARGLVVHV-----------W------TVNNEDEMKrllELGVDGVITDRP 242
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
373-669 1.15e-14

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 74.13  E-value: 1.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 373 GASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLrnsiaalqntfsNRSTSVP-EISsvpgiftfSLTW 451
Cdd:COG0584  10 GASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTL------------DRTTNGTgRVA--------DLTL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 452 PEIQSLTPAISNPFRVYRIfrnpreknsgklISLSQFLDLAKTytslsGVLISVE--NAAYLREkqglDVVQAVLDTLTE 529
Cdd:COG0584  70 AELRQLDAGSGPDFAGERI------------PTLEEVLELVPG-----DVGLNIEikSPPAAEP----DLAEAVAALLKR 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 530 AGYSNgttttKVMIQSTNSSVLVDFKKQ-SKYETVYkieeTIGNIRDSAIEDIKKF-ANAVVINKDSVFPnsdsfltgqt 607
Cdd:COG0584 129 YGLED-----RVIVSSFDPEALRRLRELaPDVPLGL----LVEELPADPLELARALgADGVGPDYDLLTP---------- 189

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30697435 608 NVVERLQKSQLPVYVelfrnefvsqaYdffsdaTV----EINAYIyGAGINGTITEFPFTAARYKR 669
Cdd:COG0584 190 ELVAAAHAAGLKVHV-----------W------TVndpeEMRRLL-DLGVDGIITDRPDLLRAVLR 237
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 57-345 1.66e-09

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: 58.95  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435    57 GFSGLYPDSSIAAYQLAtLTSVADVVLwCDLQLTKDGLGICFPDlnlanaSTIDRvypnreksysvngvTTKGW-FPNDF 135
Cdd:pfam03009   3 GASGSYPENTLASFRKA-AEAGADYIE-FDVQLTKDGVPVVLHD------FNLDR--------------TTDGAgYVRDL 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   136 SLTELQNfllIRGILSRTDRFDGNGYLISTIEDVVTtlNREGFWLNV------QHDAFYEQQNLSMSSFLLSVSRTVSID 209
Cdd:pfam03009  61 TLEELKR---LDIGAGNSGPLSGERVPFPTLEEVLE--FDWDVGFNIeikikpYVEAIAPEEGLIVKDLLLSVDEILAKK 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   210 ------FISSPEVNFFKKITgsfgRNGPTFVFQFLGKEdfepTTNRTYGSILSNLTFVKTFASGILVPKSYILPlddeqy 283
Cdd:pfam03009 136 adprrvIFSSFNPDELKRLR----ELAPKLPLVFLSSG----RAYAEADLLERAAAFAGAPALLGEVALVDEAL------ 201

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30697435   284 lvphTSLVQDAHKAGLQVYVSGFANDVDIAYnyssdpvseylsFVDNGdfsVDGVLSDFPIT 345
Cdd:pfam03009 202 ----PDLVKRAHARGLVVHVWTVNNEDEMKR------------LLELG---VDGVITDRPDT 244
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
48-352 7.50e-09

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 56.80  E-value: 7.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  48 DAPLVIARGGFSGLYPDSSIAAYQLAtLTSVADVVlWCDLQLTKDGLGICFPDlnlanaSTIDRvypnreksysvngVTT 127
Cdd:COG0584   1 PRPLIIAHRGASGLAPENTLAAFRAA-LELGADGI-ELDVQLTKDGVLVVFHD------PTLDR-------------TTN 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 128 KGWFPNDFSLTELQNFLLIRGIlsrtdrfDGNGYLISTIEDVVTTLNReGFWLNVQ--HDAFYEQQnlsmssFLLSVSRT 205
Cdd:COG0584  60 GTGRVADLTLAELRQLDAGSGP-------DFAGERIPTLEEVLELVPG-DVGLNIEikSPPAAEPD------LAEAVAAL 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 206 VSidfisspevnffkkitgSFGRNGPTFVFQF-------LGKEDFEPTTNRTYGSILSN-LTFVKTF-ASGILVPKSYIl 276
Cdd:COG0584 126 LK-----------------RYGLEDRVIVSSFdpealrrLRELAPDVPLGLLVEELPADpLELARALgADGVGPDYDLL- 187

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30697435 277 plddeqylvpHTSLVQDAHKAGLQVYVSGFaNDVDiaynyssdpvsEYLSFVDNGdfsVDGVLSDFPITASAAVDC 352
Cdd:COG0584 188 ----------TPELVAAAHAAGLKVHVWTV-NDPE-----------EMRRLLDLG---VDGIITDRPDLLRAVLRE 238
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 19-346 2.94e-06

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 50.06  E-value: 2.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   19 LFCGVVLIHLFAAQidaqrstSRWQTLNGDaPLVIARGGFSGLYPDSSIAAYQLAtLTSVADVvLWCDLQLTKDGLGICF 98
Cdd:PRK11143   4 LSLALLLAALLAGS-------AAAAADSAE-KIVIAHRGASGYLPEHTLPAKAMA-YAQGADY-LEQDLVMTKDDQLVVL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   99 PDLNLANASTIDRVYPNREKS----YSVngvttkgwfpnDFSLTELQ------NFLLIRG--ILSRTDRFD--GNGYLIS 164
Cdd:PRK11143  74 HDHYLDRVTDVAERFPDRARKdgryYAI-----------DFTLDEIKslkfteGFDIENGkkVQVYPGRFPmgKSDFRVH 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  165 TIED---VVTTLNRE-----GFWLNVQHDAFYEQQNLSMSSFLLSVSRTVSID------FISSPEVNFFKKITGSF---- 226
Cdd:PRK11143 143 TFEEeieFIQGLNHStgkniGIYPEIKAPWFHHQEGKDIAAKVLEVLKKYGYTgkddkvYLQCFDANELKRIKNELepkm 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  227 GRNGPtfVFQFLGKEDFEPTTNRTYGSILSNLTF-----------VKTFASGIlVPKSYILpLDDEQYL--VPHTSLVQD 293
Cdd:PRK11143 223 GMDLK--LVQLIAYTDWNETQEKQPDGKWVNYNYdwmfkpgamkeVAKYADGI-GPDYHML-VDETSTPgnIKLTGMVKE 298

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30697435  294 AHKAGLQVYVsgfandvdiaYNYSSDPVSEYLSFVDN------GDFSVDGVLSDFPITA 346
Cdd:PRK11143 299 AHQAKLVVHP----------YTVRADQLPEYATDVNQlydilyNQAGVDGVFTDFPDKA 347
 
Name Accession Description Interval E-value
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 50-349 0e+00

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: 543.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  50 PLVIARGGFSGLYPDSSIAAYQLATLTSVADVVLWCDLQLTKDGLGICFPDLNLANASTIDRVYPNREKSYSVNGVTTKG 129
Cdd:cd08603   1 PLVIARGGFSGLFPDSSLFAYQFAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPKRKKTYSVNGVSTKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 130 WFPNDFSLTELQNFLLIRGILSRTDRFDGNgYLISTIEDVVTTLNREGFWLNVQHDAFYEQQNLSMSSFLLSVSRTVSID 209
Cdd:cd08603  81 WFSVDFTLAELQQVTLIQGIFSRTPIFDGQ-YPISTVEDVVTLAKPEGLWLNVQHDAFYQQHNLSMSSYLLSLSKTVKVD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 210 FISSPEVNFFKKITGSFGRNGPTFVFQFLGKEDFEPTTNRTYGSILSNLTFVKTFASGILVPKSYILPLDDEQYLVPHTS 289
Cdd:cd08603 160 YISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSILKNLTFIKTFASGILVPKSYIWPVDSDQYLQPATS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 290 LVQDAHKAGLQVYVSGFANDVDIAYNYSSDPVSEYLSFVDNGDFSVDGVLSDFPITASAA 349
Cdd:cd08603 240 LVQDAHKAGLEVYASGFANDFDISYNYSYDPVAEYLSFVGNGNFSVDGVLSDFPITASEA 299
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 366-667 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: 531.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 366 FLVISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLRNSIAALQNTFSNRSTSVPEISSVPGIF 445
Cdd:cd08604   1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSKFSNRATTVPEIGSTSGIF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 446 TFSLTWPEIQSLTPAISNPFRVYRIFRNPREKNSGKLISLSQFLDLAKTYtSLSGVLISVENAAYLREKQGLDVVQAVLD 525
Cdd:cd08604  81 TFDLTWSEIQTLKPAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNK-SLSGVLINVENAAYLAEKKGLDVVDAVLD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 526 TLTEAGYSNGtTTTKVMIQSTNSSVLVDFKKQSKYETVYKIEETIGNIRDSAIEDIKKFANAVVINKDSVFPNSDSFLTG 605
Cdd:cd08604 160 ALTNAGYDNQ-TAQKVLIQSTDSSVLAAFKKQISYERVYVVDETIRDASDSSIEEIKKFADAVVIDRGSVFPVSTSFLTR 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30697435 606 QTNVVERLQKSQLPVYVELFRNEFVSQAYDFFSDATVEINAYIYGAGINGTITEFPFTAARY 667
Cdd:cd08604 239 QTNVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSYVQGAGVDGFITEFPATAARY 300
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 366-667 4.12e-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: 427.09  E-value: 4.12e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 366 FLVISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLRNSIAALQNTFSNRSTSVPEISSVPGIF 445
Cdd:cd08571   1 PLVIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPKRKKTYVVEGQSTSGIF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 446 TFSLTWPEIQSLTPAISNPFRVyrIFRNPREKNSGKLISLSQFLDLAKTYTsLSGVLISVENAAYLREKQGLDVVQAVLD 525
Cdd:cd08571  81 SFDLTWAEIQTLKPIISNPFSV--LFRNPRNDNAGKILTLEDFLTLAKPKS-LSGVWINVENAAFLAEHKGLLSVDAVLT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 526 TLTEAGYSNgtTTTKVMIQSTNSSVLVDFKKQ---SKYETVYKIEETIGNIRDSAIEDIKKFANAVVINKDSVFP-NSDS 601
Cdd:cd08571 158 SLSKAGYDQ--TAKKVYISSPDSSVLKSFKKRvgtKLVFRVLDVDDTEPDTLLSNLTEIKKFASGVLVPKSYIWPvDSDS 235

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30697435 602 FLTGQTNVVERLQKSQLPVYVELFRNEFVSQAYDFFSDATVEINAYIYGA-GINGTITEFPFTAARY 667
Cdd:cd08571 236 FLTPQTSVVQDAHKAGLEVYVSGFANEFVSLAYDYSADPTLEILSFVGNGnSVDGVITDFPATAARA 302
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 50-349 1.81e-126

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: 379.32  E-value: 1.81e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  50 PLVIARGGFSGLYPDSSIAAYQLATLTSvaDVVLWCDLQLTKDGLGICFPDLNLANASTIDRVYPNREKSYSVNGVTTKG 129
Cdd:cd08571   1 PLVIARGGASGDYPDSTDLAYQKAISDG--ADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPKRKKTYVVEGQSTSG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 130 WFPNDFSLTELQNFLLIRGILSR---TDRFDGNGYLISTIEDVVTTLNR---EGFWLNVQHDAFYEQQ--NLSMSSFLLS 201
Cdd:cd08571  79 IFSFDLTWAEIQTLKPIISNPFSvlfRNPRNDNAGKILTLEDFLTLAKPkslSGVWINVENAAFLAEHkgLLSVDAVLTS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 202 VSR-----TVSIDFISSPEVNFFKKITgsfGRNGPTFVFQFLGKEDFEPTTnrtygsILSNLTFVKTFASGILVPKSYIL 276
Cdd:cd08571 159 LSKagydqTAKKVYISSPDSSVLKSFK---KRVGTKLVFRVLDVDDTEPDT------LLSNLTEIKKFASGVLVPKSYIW 229

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30697435 277 PLDDEQYLVPHTSLVQDAHKAGLQVYVSGFAND-VDIAYNYSSDPVSEYLSFVDNGdFSVDGVLSDFPITASAA 349
Cdd:cd08571 230 PVDSDSFLTPQTSVVQDAHKAGLEVYVSGFANEfVSLAYDYSADPTLEILSFVGNG-NSVDGVITDFPATAARA 302
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 50-343 2.26e-41

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: 153.61  E-value: 2.26e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  50 PLVIARGGFSGLYPDSSIAAYQLAtLTSVADVVlWCDLQLTKDGLGICFPDLNLANASTID--RVYPNREKSYSVNGVTT 127
Cdd:cd08602   1 PLVIAHRGASGYRPEHTLAAYQLA-IEQGADFI-EPDLVSTKDGVLICRHEPELSGTTDVAdhPEFADRKTTKTVDGVNV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 128 KGWFPNDFSLTELQNFLLIRGILSRTDRFDGNgYLISTIEDVV--------TTLNREGFWLNVQHDAFYEQQ-NLSMSSF 198
Cdd:cd08602  79 TGWFTEDFTLAELKTLRARQRLPYRDQSYDGQ-FPIPTFEEIIalakaasaATGRTVGIYPEIKHPTYFNAPlGLPMEDK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 199 LLSV-------SRTVSIdFISSPEVNFFKKITGsfgRNGPTFVfQFLGKE-----DFEPTTNRTYGSILSN--LTFVKTF 264
Cdd:cd08602 158 LLETlkkygytGKKAPV-FIQSFEVTNLKYLRN---KTDLPLV-QLIDDAtippqDTPEGDSRTYADLTTDagLKEIATY 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 265 ASGILVPKSYILPLDDEQYLVPHTSLVQDAHKAGLQVYVSGFAN-DVDIAYNYSSDPVSEYLSFVDNGdfsVDGVLSDFP 343
Cdd:cd08602 233 ADGIGPWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNeNTFLPPDFFGDPYAEYRAFLDAG---VDGLFTDFP 309
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 366-661 4.16e-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: 123.95  E-value: 4.16e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 366 FLVISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRS--IDLRNSIAALQNTFSNRSTSVPEISSVPG 443
Cdd:cd08602   1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEpeLSGTTDVADHPEFADRKTTKTVDGVNVTG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 444 IFTFSLTWPEIQSLTPAISNPFRvyrifrnpREKNSGK--LISLSQFLDLAKTYTSLS----GVLISVENAAYLREKQGL 517
Cdd:cd08602  81 WFTEDFTLAELKTLRARQRLPYR--------DQSYDGQfpIPTFEEIIALAKAASAATgrtvGIYPEIKHPTYFNAPLGL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 518 DVVQAVLDTLTEAGYsnGTTTTKVMIQS------------TNSS--VLVDFKKQSKYETVYKIEETIGN-IRDSAIEDIK 582
Cdd:cd08602 153 PMEDKLLETLKKYGY--TGKKAPVFIQSfevtnlkylrnkTDLPlvQLIDDATIPPQDTPEGDSRTYADlTTDAGLKEIA 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 583 KFANAVVINKDSVFP-NSDSFLTGQTNVVERLQKSQLPVYVELFRNEFVSQAYDFFSDATVEINAYiYGAGINGTITEFP 661
Cdd:cd08602 231 TYADGIGPWKDLIIPsDANGRLGTPTDLVEDAHAAGLQVHPYTFRNENTFLPPDFFGDPYAEYRAF-LDAGVDGLFTDFP 309
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 366-661 1.18e-30

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: 122.38  E-value: 1.18e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 366 FLVISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLrnsiaalqntfsNRSTSVPEIS-----S 440
Cdd:cd08559   1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTL------------DRTTNVAEHFpfrgrK 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 441 VPGIFTFSLTWPEIQSLTpAISNPFRVYrIFRNPREKNSGKLISLSQFLDLAKTYTSLSG--VLISVE-NAAYLREKQGL 517
Cdd:cd08559  69 DTGYFVIDFTLAELKTLR-AGSWFNQRY-PERAPSYYGGFKIPTLEEVIELAQGLNKSTGrnVGIYPEtKHPTFHKQEGP 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 518 DVVQAVLDTLTEAGYSNgtTTTKVMIQSTNSSVLVDFKKQSK-YETVYKIEETIGNIR-----------DSAIEDIKKFA 585
Cdd:cd08559 147 DIEEKLLEVLKKYGYTG--KNDPVFIQSFEPESLKRLRNETPdIPLVQLIDYGDWAETdkkytyawlttDAGLKEIAKYA 224

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30697435 586 NAVVINKDSVFPNSDSFLTGQTNVVERLQKSQLPVYVELFRNEFVSQAYDFFSDATVEINAyiygAGINGTITEFP 661
Cdd:cd08559 225 DGIGPWKSLIIPEDSNGLLVPTDLVKDAHKAGLLVHPYTFRNENLFLAPDFKQDMDALYNA----AGVDGVFTDFP 296
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 50-343 1.57e-30

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: 122.00  E-value: 1.57e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  50 PLVIARGGFSGLYPDSSIAAYQLAtLTSVADVvLWCDLQLTKDGLGICFPDLNLANASTIDRVYPNReksysvnGVTTKG 129
Cdd:cd08559   1 PLVIAHRGASGYAPEHTLAAYALA-IEMGADY-IEQDLVMTKDGVLVARHDPTLDRTTNVAEHFPFR-------GRKDTG 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 130 WFPNDFSLTELQNfllirgiLSRTDRF-----------DGNgYLISTIEDVV--------TTLNREGFWLNVQHDAFYEQ 190
Cdd:cd08559  72 YFVIDFTLAELKT-------LRAGSWFnqryperapsyYGG-FKIPTLEEVIelaqglnkSTGRNVGIYPETKHPTFHKQ 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 191 QNLSMSSFLLSV-------SRTVSIdFISSPEVNFFKKITGSFGrNGPTfvFQFLGKEDFEPT-TNRTYGSILSN--LTF 260
Cdd:cd08559 144 EGPDIEEKLLEVlkkygytGKNDPV-FIQSFEPESLKRLRNETP-DIPL--VQLIDYGDWAETdKKYTYAWLTTDagLKE 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 261 VKTFASGILVPKSYILPlDDEQYLVPHTSLVQDAHKAGLQVYVSGFAND-VDIAYNYSSDPVSEYLsfvdngDFSVDGVL 339
Cdd:cd08559 220 IAKYADGIGPWKSLIIP-EDSNGLLVPTDLVKDAHKAGLLVHPYTFRNEnLFLAPDFKQDMDALYN------AAGVDGVF 292


                ....
gi 30697435 340 SDFP 343
Cdd:cd08559 293 TDFP 296
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 50-346 8.30e-26

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: 108.19  E-value: 8.30e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  50 PLVIARGGFSGLYPDSSIAAYQLAtLTSVADVvLWCDLQLTKDGLGICFPDLNLANASTIDRV-YPNREKSYSVNGvTTK 128
Cdd:cd08604   1 PLIISHNGASGDYPGCTDLAYQKA-VKDGADV-IDCSVQMSKDGVPFCLDSINLINSTTVATSkFSNRATTVPEIG-STS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 129 GWFPNDFSLTELQNfllIRGILS---------RTDRFDGNGYLISTIE--DVVTTLNREGFWLNVQHDAF-YEQQNLSMS 196
Cdd:cd08604  78 GIFTFDLTWSEIQT---LKPAISnpysvtglfRNPANKNAGKFLTLSDflDLAKNKSLSGVLINVENAAYlAEKKGLDVV 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 197 SFLLSVSRTVSIDFISSPEV----------NFFKKITgSFGRngptfVFQflgkedfeptTNRTYGSIL-SNLTFVKTFA 265
Cdd:cd08604 155 DAVLDALTNAGYDNQTAQKVliqstdssvlAAFKKQI-SYER-----VYV----------VDETIRDASdSSIEEIKKFA 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 266 SGILVPKSYILPLDDeQYLVPHTSLVQDAHKAGLQVYVSGFAND-VDIAYNYSSDPVSEYLSFVdnGDFSVDGVLSDFPI 344
Cdd:cd08604 219 DAVVIDRGSVFPVST-SFLTRQTNVVEKLQSANLTVYVEVLRNEfVSLAFDFFADPTVEINSYV--QGAGVDGFITEFPA 295


                ..
gi 30697435 345 TA 346
Cdd:cd08604 296 TA 297
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 373-661 1.67e-20

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: 91.31  E-value: 1.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   373 GASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLrnsiaalqntfsNRSTSVPEissvpgiFTFSLTWP 452
Cdd:pfam03009   3 GASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNL------------DRTTDGAG-------YVRDLTLE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   453 EIQSLTPAIsnpfrvyRIFRNPREKNSgKLISLSQFLDLAKTYTSLSGVLISVENAAYLRE--KQGLDVVQAVLDTLTEA 530
Cdd:pfam03009  64 ELKRLDIGA-------GNSGPLSGERV-PFPTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEegLIVKDLLLSVDEILAKK 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   531 GysngtTTTKVMIQSTNSSVLVDFK-KQSKYETVykieeTIGNIRDSAiEDIKKFANAVVINKDSVFPNSDSFLTGQTNV 609
Cdd:pfam03009 136 A-----DPRRVIFSSFNPDELKRLReLAPKLPLV-----FLSSGRAYA-EADLLERAAAFAGAPALLGEVALVDEALPDL 204

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30697435   610 VERLQKSQLPVYVelfrnefvsqaYdffsdaTVEINAYIY---GAGINGTITEFP 661
Cdd:pfam03009 205 VKRAHARGLVVHV-----------W------TVNNEDEMKrllELGVDGVITDRP 242
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 367-666 6.43e-16

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: 78.97  E-value: 6.43e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 367 LVISKDGASGDYPGCTDLAYEKAIKDGAD--VIDCSVQMSSDGVPFCLRSIDLRNSiAALQNTFSNRSTS-VPEISSVPG 443
Cdd:cd08603   2 LVIARGGFSGLFPDSSLFAYQFAASSSSPdvALWCDLQLTKDGVGICLPDLNLDNS-TTIARVYPKRKKTySVNGVSTKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 444 IFTFSLTWPEIQSLTPAISNPFRVYRIFRNpreknsgklISLSQFLDLAKTYtSLSGVLISVENAAYLREkQGLDVVQAV 523
Cdd:cd08603  81 WFSVDFTLAELQQVTLIQGIFSRTPIFDGQ---------YPISTVEDVVTLA-KPEGLWLNVQHDAFYQQ-HNLSMSSYL 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 524 LDTL----------TEAGY------SNGTTTTKVMIQSTNSSVLVDFKKQskyetvykieeTIGNIRdSAIEDIKKFANA 587
Cdd:cd08603 150 LSLSktvkvdyissPEVGFlksiggRVGRNGTKLVFRFLDKDDVEPSTNQ-----------TYGSIL-KNLTFIKTFASG 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 588 VVINKDSVFP-NSDSFLTGQTNVVERLQKSQLPVYVELFRNEFVSqAYDFFSDATVEINAYIYGAG--INGTITEFPFTA 664
Cdd:cd08603 218 ILVPKSYIWPvDSDQYLQPATSLVQDAHKAGLEVYASGFANDFDI-SYNYSYDPVAEYLSFVGNGNfsVDGVLSDFPITA 296


                ..
gi 30697435 665 AR 666
Cdd:cd08603 297 SE 298
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
373-669 1.15e-14

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 74.13  E-value: 1.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 373 GASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLrnsiaalqntfsNRSTSVP-EISsvpgiftfSLTW 451
Cdd:COG0584  10 GASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTL------------DRTTNGTgRVA--------DLTL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 452 PEIQSLTPAISNPFRVYRIfrnpreknsgklISLSQFLDLAKTytslsGVLISVE--NAAYLREkqglDVVQAVLDTLTE 529
Cdd:COG0584  70 AELRQLDAGSGPDFAGERI------------PTLEEVLELVPG-----DVGLNIEikSPPAAEP----DLAEAVAALLKR 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 530 AGYSNgttttKVMIQSTNSSVLVDFKKQ-SKYETVYkieeTIGNIRDSAIEDIKKF-ANAVVINKDSVFPnsdsfltgqt 607
Cdd:COG0584 129 YGLED-----RVIVSSFDPEALRRLRELaPDVPLGL----LVEELPADPLELARALgADGVGPDYDLLTP---------- 189

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30697435 608 NVVERLQKSQLPVYVelfrnefvsqaYdffsdaTV----EINAYIyGAGINGTITEFPFTAARYKR 669
Cdd:COG0584 190 ELVAAAHAAGLKVHV-----------W------TVndpeEMRRLL-DLGVDGIITDRPDLLRAVLR 237
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 368-660 4.13e-14

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: 71.53  E-value: 4.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 368 VISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFClrsidlrnsiaalqntfsnrstsvpeISSVPgiftf 447
Cdd:cd08556   1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVV--------------------------IHDIP----- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 448 sltwpeiqsltpaisnpfrvyrifrnpreknsgkliSLSQFLDLAKTytslsGVLISVENAAYlreKQGLDVVQAVLDTL 527
Cdd:cd08556  50 ------------------------------------TLEEVLELVKG-----GVGLNIELKEP---TRYPGLEAKVAELL 85

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 528 TEAGysngtTTTKVMIQSTNSSVLVDFKKQSKYETVYKIEETIGNIRDSAIEDIKKFANAVVINKDSVFPnsdsfltgqt 607
Cdd:cd08556  86 REYG-----LEERVVVSSFDHEALRALKELDPEVPTGLLVDKPPLDPLLAELARALGADAVNPHYKLLTP---------- 150

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 30697435 608 NVVERLQKSQLPVYVELFRNEfvsqaydffsdatvEINAYIYGAGINGTITEF 660
Cdd:cd08556 151 ELVRAAHAAGLKVYVWTVNDP--------------EDARRLLALGVDGIITDD 189
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 50-343 4.63e-12

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: 67.80  E-value: 4.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  50 PLVIARGGFSGLYPDSSIAAYQLATLTSvADVvLWCDLQLTKDGLGICFPDLNLANASTIDRVYPNREK---SYSVngvt 126
Cdd:cd08600   1 KIIIAHRGASGYLPEHTLEAKALAYAQG-ADY-LEQDVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKRkdgRYYV---- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 127 tkgwfpNDFSLTELQNfllirgiLSRTDRFD----------GN-------GYLISTIEDVV--------TTLNREGFWLN 181
Cdd:cd08600  75 ------IDFTLDELKS-------LSVTERFDiengkkvqvyPNrfplwksDFKIHTLEEEIeliqglnkSTGKNVGIYPE 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 182 VQHDAFYEQQNLSMSSFLLSVSRTVSID------FISSPEVNFFKKITGSFG--RNGPTFVFQFLGKEDFEPT------- 246
Cdd:cd08600 142 IKAPWFHHQEGKDIAAATLEVLKKYGYTskndkvYLQTFDPNELKRIKNELLpkMGMDLKLVQLIAYTDWGETqekdpgg 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 247 -TNRTYGSILS--NLTFVKTFASGILVPKSYILPLDDEQYLVPHTSLVQDAHKAGLQVYVsgfandvdiaYNYSSDPVSE 323
Cdd:cd08600 222 wVNYDYDWMFTkgGLKEIAKYADGVGPWYSMIIEEKSSKGNIVLTDLVKDAHEAGLEVHP----------YTVRKDALPE 291

                       330       340
                ....*....|....*....|....*.
gi 30697435 324 YLSFVDN------GDFSVDGVLSDFP 343
Cdd:cd08600 292 YAKDADQlldallNKAGVDGVFTDFP 317
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 366-661 7.86e-12

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: 67.03  E-value: 7.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 366 FLVISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLrnsiaalqNTFSNRSTSVPEISSVPGIF 445
Cdd:cd08600   1 KIIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYL--------DNVTNVAEKFPDRKRKDGRY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 446 -TFSLTWPEIQSLTpaISNPFRVYRIF-------RNPREKNSGKLISLSQFLDLAKTYTSLSG--VLISVE-NAAYLREK 514
Cdd:cd08600  73 yVIDFTLDELKSLS--VTERFDIENGKkvqvypnRFPLWKSDFKIHTLEEEIELIQGLNKSTGknVGIYPEiKAPWFHHQ 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 515 QGLDVVQAVLDTLTEAGYSNgtTTTKVMIQSTNSSVLVDFKKQ--SKYETVYKIEETIG--------NIRDS-------- 576
Cdd:cd08600 151 EGKDIAAATLEVLKKYGYTS--KNDKVYLQTFDPNELKRIKNEllPKMGMDLKLVQLIAytdwgetqEKDPGgwvnydyd 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 577 ------AIEDIKKFANAV-----VINKDSVFPNSDSFltgqTNVVERLQKSQLPVYVELFRNEFVSQaydFFSDATVEIN 645
Cdd:cd08600 229 wmftkgGLKEIAKYADGVgpwysMIIEEKSSKGNIVL----TDLVKDAHEAGLEVHPYTVRKDALPE---YAKDADQLLD 301

                       330
                ....*....|....*.
gi 30697435 646 AYIYGAGINGTITEFP 661
Cdd:cd08600 302 ALLNKAGVDGVFTDFP 317
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 57-345 1.66e-09

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: 58.95  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435    57 GFSGLYPDSSIAAYQLAtLTSVADVVLwCDLQLTKDGLGICFPDlnlanaSTIDRvypnreksysvngvTTKGW-FPNDF 135
Cdd:pfam03009   3 GASGSYPENTLASFRKA-AEAGADYIE-FDVQLTKDGVPVVLHD------FNLDR--------------TTDGAgYVRDL 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   136 SLTELQNfllIRGILSRTDRFDGNGYLISTIEDVVTtlNREGFWLNV------QHDAFYEQQNLSMSSFLLSVSRTVSID 209
Cdd:pfam03009  61 TLEELKR---LDIGAGNSGPLSGERVPFPTLEEVLE--FDWDVGFNIeikikpYVEAIAPEEGLIVKDLLLSVDEILAKK 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   210 ------FISSPEVNFFKKITgsfgRNGPTFVFQFLGKEdfepTTNRTYGSILSNLTFVKTFASGILVPKSYILPlddeqy 283
Cdd:pfam03009 136 adprrvIFSSFNPDELKRLR----ELAPKLPLVFLSSG----RAYAEADLLERAAAFAGAPALLGEVALVDEAL------ 201

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30697435   284 lvphTSLVQDAHKAGLQVYVSGFANDVDIAYnyssdpvseylsFVDNGdfsVDGVLSDFPIT 345
Cdd:pfam03009 202 ----PDLVKRAHARGLVVHVWTVNNEDEMKR------------LLELG---VDGVITDRPDT 244
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
48-352 7.50e-09

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 56.80  E-value: 7.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  48 DAPLVIARGGFSGLYPDSSIAAYQLAtLTSVADVVlWCDLQLTKDGLGICFPDlnlanaSTIDRvypnreksysvngVTT 127
Cdd:COG0584   1 PRPLIIAHRGASGLAPENTLAAFRAA-LELGADGI-ELDVQLTKDGVLVVFHD------PTLDR-------------TTN 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 128 KGWFPNDFSLTELQNFLLIRGIlsrtdrfDGNGYLISTIEDVVTTLNReGFWLNVQ--HDAFYEQQnlsmssFLLSVSRT 205
Cdd:COG0584  60 GTGRVADLTLAELRQLDAGSGP-------DFAGERIPTLEEVLELVPG-DVGLNIEikSPPAAEPD------LAEAVAAL 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 206 VSidfisspevnffkkitgSFGRNGPTFVFQF-------LGKEDFEPTTNRTYGSILSN-LTFVKTF-ASGILVPKSYIl 276
Cdd:COG0584 126 LK-----------------RYGLEDRVIVSSFdpealrrLRELAPDVPLGLLVEELPADpLELARALgADGVGPDYDLL- 187

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30697435 277 plddeqylvpHTSLVQDAHKAGLQVYVSGFaNDVDiaynyssdpvsEYLSFVDNGdfsVDGVLSDFPITASAAVDC 352
Cdd:COG0584 188 ----------TPELVAAAHAAGLKVHVWTV-NDPE-----------EMRRLLDLG---VDGIITDRPDLLRAVLRE 238
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 367-674 1.20e-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: 53.87  E-value: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 367 LVISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLrnsiaalqNTFSNRSTSVPeissvpgift 446
Cdd:cd08580   2 LIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDL--------KSLTNGSGAVS---------- 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 447 fSLTWPEIQSLTPAIsnpfrvyrifrNPREKNSGKlislsqFLDLAKTYTSLSGVLISV-ENAAYLREKQgLD---VVQA 522
Cdd:cd08580  64 -AYTAAQLATLNAGY-----------NFKPEGGYP------YRGKPVGIPTLEQVLRAFpDTPFILDMKS-LPadpQAKA 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 523 VLDTLTEAGYSNgttttKVMIQSTNSSVLVDFKKQSKYETVYKIEETigniRdsaiediKKFANAVVINKDSVFPNSDSF 602
Cdd:cd08580 125 VARVLERENAWS-----RVRIYSTNADYQDALAPYPQARLFESRDVT----R-------TRLANVAMAHQCDLPPDSGAW 188

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30697435 603 ----LTGQTNVVER--LQKSQLPVYVELFRnefvSQAYDFFSDATveiNAYIYGAGINgtitefpfTAARYKRNRCLG 674
Cdd:cd08580 189 agfeLRRKVTVVETftLGEGRSPVQATLWT----PAAVDCFRRNS---KVKIVLFGIN--------TADDYRLAKCLG 251
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 368-408 4.11e-07

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: 51.84  E-value: 4.11e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 30697435 368 VISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGV 408
Cdd:cd08570   1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGV 41
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 366-588 2.82e-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: 49.62  E-value: 2.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 366 FLVISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVpfclrsidlrnsIAALQNTFSNRSTSVpeisSVPGIF 445
Cdd:cd08601   1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGV------------LVAMHDETLDRTTNI----ERPGPV 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 446 TfSLTWPEIQSLTpAIS-----NPfrvyrifRNPREKNSG-KLISLSQFLDLAKtytslsgvlisvENAAYLREKQGLDV 519
Cdd:cd08601  65 K-DYTLAEIKQLD-AGSwfnkaYP-------EYARESYSGlKVPTLEEVIERYG------------GRANYYIETKSPDL 123

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30697435 520 VQA----VLDTLTEAGYSNGTTTT-KVMIQSTNSSVLVDFKKQSK-YETVYKIEETIG-NIRDSAIEDIKKFANAV 588
Cdd:cd08601 124 YPGmeekLLATLDKYGLLTDNLKNgQVIIQSFSKESLKKLHQLNPnIPLVQLLWYGEGaETYDKWLDEIKEYAIGI 199
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 19-346 2.94e-06

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 50.06  E-value: 2.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   19 LFCGVVLIHLFAAQidaqrstSRWQTLNGDaPLVIARGGFSGLYPDSSIAAYQLAtLTSVADVvLWCDLQLTKDGLGICF 98
Cdd:PRK11143   4 LSLALLLAALLAGS-------AAAAADSAE-KIVIAHRGASGYLPEHTLPAKAMA-YAQGADY-LEQDLVMTKDDQLVVL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435   99 PDLNLANASTIDRVYPNREKS----YSVngvttkgwfpnDFSLTELQ------NFLLIRG--ILSRTDRFD--GNGYLIS 164
Cdd:PRK11143  74 HDHYLDRVTDVAERFPDRARKdgryYAI-----------DFTLDEIKslkfteGFDIENGkkVQVYPGRFPmgKSDFRVH 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  165 TIED---VVTTLNRE-----GFWLNVQHDAFYEQQNLSMSSFLLSVSRTVSID------FISSPEVNFFKKITGSF---- 226
Cdd:PRK11143 143 TFEEeieFIQGLNHStgkniGIYPEIKAPWFHHQEGKDIAAKVLEVLKKYGYTgkddkvYLQCFDANELKRIKNELepkm 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435  227 GRNGPtfVFQFLGKEDFEPTTNRTYGSILSNLTF-----------VKTFASGIlVPKSYILpLDDEQYL--VPHTSLVQD 293
Cdd:PRK11143 223 GMDLK--LVQLIAYTDWNETQEKQPDGKWVNYNYdwmfkpgamkeVAKYADGI-GPDYHML-VDETSTPgnIKLTGMVKE 298

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30697435  294 AHKAGLQVYVsgfandvdiaYNYSSDPVSEYLSFVDN------GDFSVDGVLSDFPITA 346
Cdd:PRK11143 299 AHQAKLVVHP----------YTVRADQLPEYATDVNQlydilyNQAGVDGVFTDFPDKA 347
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 50-121 9.36e-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: 9.36e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30697435  50 PLVIARGGFSGLYPDSSIAAYQLAtLTSVADVvLWCDLQLTKDGLGICFPDLNLANASTIDRVYPNREKSYS 121
Cdd:cd08601   1 NAVIAHRGASGYAPEHTFAAYDLA-REMGADY-IELDLQMTKDGVLVAMHDETLDRTTNIERPGPVKDYTLA 70
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 382-498 2.04e-04

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: 43.83  E-value: 2.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 382 TDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLRnsiaalqntfsnRSTSV----PEISSVPGIFtfsLTWPEIQSL 457
Cdd:cd08574  18 TLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLR------------RTTNVadvfPERAHERASM---FTWTDLQQL 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 30697435 458 TPAI----SNPFrvYRIFR-NPREKNSG---KLISLSQFLDLAKTYTSL 498
Cdd:cd08574  83 NAGQwflkDDPF--WTASSlSESDREEAgnqSIPSLAELLRLAKKHNKS 129
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 367-417 3.34e-04

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: 42.97  E-value: 3.34e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 30697435 367 LVISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDL 417
Cdd:cd08575   2 LHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDL 52
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 368-559 7.92e-04

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: 41.86  E-value: 7.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 368 VISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCL------RSIDLRNSIAAlqntfsnrstsvpeissv 441
Cdd:cd08561   1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIhdetldRTTDGTGPVAD------------------ 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 442 pgiftfsLTWPEIQSLT-----PAISNPFRVYRifrnpreknsGKLISLSQFLDLaktYTSLSGVLISVEnaayLREKqG 516
Cdd:cd08561  63 -------LTLAELRRLDagyhfTDDGGRTYPYR----------GQGIRIPTLEEL---FEAFPDVRLNIE----IKDD-G 117

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 30697435 517 LDVVQAVLDTLTEAGYSNgttttKVMIQSTNSSVLVDFKKQSK 559
Cdd:cd08561 118 PAAAAALADLIERYGAQD-----RVLVASFSDRVLRRFRRLCP 155
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 52-101 1.19e-03

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: 40.71  E-value: 1.19e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 30697435  52 VIARGGFSGLYPDSSIAAYQLAtLTSVADVVlWCDLQLTKDGLGICFPDL 101
Cdd:cd08556   1 IIAHRGASGEAPENTLAAFRKA-LEAGADGV-ELDVQLTKDGVLVVIHDI 48
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 373-418 1.43e-03

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: 40.78  E-value: 1.43e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 30697435 373 GASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLR 418
Cdd:cd08581   6 GYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLL 51
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 368-493 2.97e-03

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


Pssm-ID: 176551 [Multi-domain]  Cd Length: 315  Bit Score: 40.68  E-value: 2.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 368 VISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLRNSiAALQNTFSNRSTsvpeissvpgIFTF 447
Cdd:cd08609  29 LVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRT-TNVKDVFPGRDA----------AGSN 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 30697435 448 SLTWPEIQSLTPAI----SNPFRVYRIFRNP--REKNSGKLISLSQFLDLAK 493
Cdd:cd08609  98 NFTWTELKTLNAGSwfleRRPFWTLSSLSEEdrREADNQTVPSLSELLDLAK 149
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 368-438 3.14e-03

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: 40.24  E-value: 3.14e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30697435 368 VISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLRnsiaalqntfsnRSTSVPEI 438
Cdd:cd08610  25 IIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLK------------RTTNIGEV 83
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 368-497 6.93e-03

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE2 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 5 (GDPD5)) and their metazoan homologs. Mammalian GDE2 is transmembrane protein primarily expressed in mature neurons. It is a mammalian homolog of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Mammalian GDE2 selectively hydrolyzes glycerophosphocholine (GPC) and has been characterized as GPC-GDE (EC 3.1.4.2) that contributes to osmotic regulation of cellular GPC. Mammalian GDE2 functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE2 also plays a critical role for retinoid-induced neuronal outgrowth. The catalytic activity of GDPD domain is essential for mammalian GDE2 cellular function.


Pssm-ID: 176550  Cd Length: 351  Bit Score: 39.44  E-value: 6.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 368 VISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLRnsiaalqntfsnRSTSV----PEISSVPG 443
Cdd:cd08608   4 IIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLR------------RTTNVdrvfPERQYEDA 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697435 444 IFtfsLTWPEIQSLTPAI----SNPFRV--YRIFRNPREKNSGKLISLSQFLDLAKTYTS 497
Cdd:cd08608  72 SM---FNWTDLERLNAGQwflkDDPFWTaqSLSPSDRKEAGNQSVCSLAELLELAKRYNA 128
 
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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