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Conserved domains on  [gi|219892334|emb|CAW78844|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

glycerophosphodiester phosphodiesterase family protein( domain architecture ID 10171244)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 360-660 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: 533.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 360 FLVITKDGASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLGNSTTVSLTAFRNRSTTVPELGSLGAIY 439
Cdd:cd08604    1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSKFSNRATTVPEIGSTSGIF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 440 TFSLTWAEIQTLTPAISNPYRVTSLFRNPKQKNAGKLFSLSDFLSLAKNStSLSGVLISVENAAYLREEQGLDVVKAVLD 519
Cdd:cd08604   81 TFDLTWSEIQTLKPAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNK-SLSGVLINVENAAYLAEKKGLDVVDAVLD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 520 TLTQTGYSNSTATKVMIQSTNSSVLVDFKKQSQYETVYKVEENIRDILDSAIEDIKKFADAVVIQKLSVFPVAQSFITTQ 599
Cdd:cd08604  160 ALTNAGYDNQTAQKVLIQSTDSSVLAAFKKQISYERVYVVDETIRDASDSSIEEIKKFADAVVIDRGSVFPVSTSFLTRQ 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219892334 600 TNVVEKLQKSQLPVYVELFQNEFLSQPYDFFADATVEINSYITGAGINGTITEFPFTAARY 660
Cdd:cd08604  240 TNVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSYVQGAGVDGFITEFPATAARY 300
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 44-343 9.63e-178

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


:

Pssm-ID: 176545  Cd Length: 299  Bit Score: 510.39  E-value: 9.63e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  44 PLVIARGGFSGLFPDSSYDAYNFAILTSVPDAVLWCDVQLTKDALGICFPDLTMRNSSSIEAVYPTRQKSYPVNGVPTSG 123
Cdd:cd08603    1 PLVIARGGFSGLFPDSSLFAYQFAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPKRKKTYSVNGVSTKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 124 WFTIDFSLKDLKDVNLIRGILSRSEKFDGNSnPIMTVQSVSTQMKPSFFWLNVQHDAFYAQHNLSMSSFLVAASKTVLID 203
Cdd:cd08603   81 WFSVDFTLAELQQVTLIQGIFSRTPIFDGQY-PISTVEDVVTLAKPEGLWLNVQHDAFYQQHNLSMSSYLLSLSKTVKVD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 204 FISSPEVNFFKKIAGRFGRNGPSLVFRFLGQDEFEPTTNRTYGSILSNLTFVKTFASGILVPKSYILPLDDQQYLLPHTS 283
Cdd:cd08603  160 YISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSILKNLTFIKTFASGILVPKSYIWPVDSDQYLQPATS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 284 LVQDAHKAGLEVFVSGFANDIDIAHDYSFDPVSEYLSFVDNGNFSVDGVLSDFPITASAS 343
Cdd:cd08603  240 LVQDAHKAGLEVYASGFANDFDISYNYSYDPVAEYLSFVGNGNFSVDGVLSDFPITASEA 299
 
Name Accession Description Interval E-value
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 360-660 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: 533.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 360 FLVITKDGASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLGNSTTVSLTAFRNRSTTVPELGSLGAIY 439
Cdd:cd08604    1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSKFSNRATTVPEIGSTSGIF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 440 TFSLTWAEIQTLTPAISNPYRVTSLFRNPKQKNAGKLFSLSDFLSLAKNStSLSGVLISVENAAYLREEQGLDVVKAVLD 519
Cdd:cd08604   81 TFDLTWSEIQTLKPAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNK-SLSGVLINVENAAYLAEKKGLDVVDAVLD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 520 TLTQTGYSNSTATKVMIQSTNSSVLVDFKKQSQYETVYKVEENIRDILDSAIEDIKKFADAVVIQKLSVFPVAQSFITTQ 599
Cdd:cd08604  160 ALTNAGYDNQTAQKVLIQSTDSSVLAAFKKQISYERVYVVDETIRDASDSSIEEIKKFADAVVIDRGSVFPVSTSFLTRQ 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219892334 600 TNVVEKLQKSQLPVYVELFQNEFLSQPYDFFADATVEINSYITGAGINGTITEFPFTAARY 660
Cdd:cd08604  240 TNVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSYVQGAGVDGFITEFPATAARY 300
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 44-343 9.63e-178

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


Pssm-ID: 176545  Cd Length: 299  Bit Score: 510.39  E-value: 9.63e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  44 PLVIARGGFSGLFPDSSYDAYNFAILTSVPDAVLWCDVQLTKDALGICFPDLTMRNSSSIEAVYPTRQKSYPVNGVPTSG 123
Cdd:cd08603    1 PLVIARGGFSGLFPDSSLFAYQFAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPKRKKTYSVNGVSTKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 124 WFTIDFSLKDLKDVNLIRGILSRSEKFDGNSnPIMTVQSVSTQMKPSFFWLNVQHDAFYAQHNLSMSSFLVAASKTVLID 203
Cdd:cd08603   81 WFSVDFTLAELQQVTLIQGIFSRTPIFDGQY-PISTVEDVVTLAKPEGLWLNVQHDAFYQQHNLSMSSYLLSLSKTVKVD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 204 FISSPEVNFFKKIAGRFGRNGPSLVFRFLGQDEFEPTTNRTYGSILSNLTFVKTFASGILVPKSYILPLDDQQYLLPHTS 283
Cdd:cd08603  160 YISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSILKNLTFIKTFASGILVPKSYIWPVDSDQYLQPATS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 284 LVQDAHKAGLEVFVSGFANDIDIAHDYSFDPVSEYLSFVDNGNFSVDGVLSDFPITASAS 343
Cdd:cd08603  240 LVQDAHKAGLEVYASGFANDFDISYNYSYDPVAEYLSFVGNGNFSVDGVLSDFPITASEA 299
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 367-654 1.58e-19

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: 88.61  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  367 GASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLgnsttvsltafrNRSTTVpelgslgAIYTFSLTWA 446
Cdd:pfam03009   3 GASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNL------------DRTTDG-------AGYVRDLTLE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  447 EIQTLTPAISNPYrvtslfrnPKQKNAGKLFSLSDFLSLAKNSTSLSGVLISVENAAYLREEqgLDVVKAVLDTLTQTGY 526
Cdd:pfam03009  64 ELKRLDIGAGNSG--------PLSGERVPFPTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEE--GLIVKDLLLSVDEILA 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  527 SNSTATKVMIQSTNSSVLVDFkkqSQYETVYKVEENIRDILDSaiEDIKKFADAVVIQKLSVFPVAQSFITTQTNVVEKL 606
Cdd:pfam03009 134 KKADPRRVIFSSFNPDELKRL---RELAPKLPLVFLSSGRAYA--EADLLERAAAFAGAPALLGEVALVDEALPDLVKRA 208

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 219892334  607 QKSQLPVYVelfqneflsqpYdffadaTVEINSYIT---GAGINGTITEFP 654
Cdd:pfam03009 209 HARGLVVHV-----------W------TVNNEDEMKrllELGVDGVITDRP 242
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
367-662 1.51e-15

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 76.83  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 367 GASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLgnsttvsltafrNRSTTVPelgslGAIYTFslTWA 446
Cdd:COG0584   10 GASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTL------------DRTTNGT-----GRVADL--TLA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 447 EIQTLTpaisnpyrvtslFRNPKQKNAGKLFSLSDFLSLAKNstslsGVLISVE--NAAYLREeqglDVVKAVLDTLTQT 524
Cdd:COG0584   71 ELRQLD------------AGSGPDFAGERIPTLEEVLELVPG-----DVGLNIEikSPPAAEP----DLAEAVAALLKRY 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 525 GYSNstatKVMIQSTNSSVLVDFKKQ-SQYETVYKVEENIRDILDSAIEDikkFADAVviqklsvfPVAQSFITTQtnVV 603
Cdd:COG0584  130 GLED----RVIVSSFDPEALRRLRELaPDVPLGLLVEELPADPLELARAL---GADGV--------GPDYDLLTPE--LV 192

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 219892334 604 EKLQKSQLPVYVelfqneflsqpydFFADATVEINSYItGAGINGTITEFPFTAARYKR 662
Cdd:COG0584  193 AAAHAAGLKVHV-------------WTVNDPEEMRRLL-DLGVDGIITDRPDLLRAVLR 237
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 338-660 2.90e-06

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 50.06  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 338 ITASASLDCFSHvgrNATKQVDFLVITKDGASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLGNSTTV 417
Cdd:PRK11143   8 LLLAALLAGSAA---AAADSAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 418 SlTAFRNRSTTVpelgslGAIYTFSLTWAEIQTLtpaisnpyRVTSLF--RNPKQ-KNAGKLFSL--SDF---------- 482
Cdd:PRK11143  85 A-ERFPDRARKD------GRYYAIDFTLDEIKSL--------KFTEGFdiENGKKvQVYPGRFPMgkSDFrvhtfeeeie 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 483 ------LSLAKNstslSGVLISVEnAAYLREEQGLDVVKAVLDTLTQTGYSNSTAtKVMIQSTNSSVL------------ 544
Cdd:PRK11143 150 fiqglnHSTGKN----IGIYPEIK-APWFHHQEGKDIAAKVLEVLKKYGYTGKDD-KVYLQCFDANELkriknelepkmg 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 545 VDFK------KQSQYET-VYKVEENIRDI------LDSAIEDIKKFADAV------VIQKLSvfpvaQSFITTQTNVVEK 605
Cdd:PRK11143 224 MDLKlvqliaYTDWNETqEKQPDGKWVNYnydwmfKPGAMKEVAKYADGIgpdyhmLVDETS-----TPGNIKLTGMVKE 298

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219892334 606 LQKSQLPVYvelfqneflsqPYDFFADAtveINSYITG-----------AGINGTITEFPFTAARY 660
Cdd:PRK11143 299 AHQAKLVVH-----------PYTVRADQ---LPEYATDvnqlydilynqAGVDGVFTDFPDKAVKF 350
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
281-346 3.00e-03

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 39.85  E-value: 3.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219892334 281 HTSLVQDAHKAGLEVFVsgfandidiahdYSFDPVSEYLSFVDNGnfsVDGVLSDFPITASASLDC 346
Cdd:COG0584  188 TPELVAAAHAAGLKVHV------------WTVNDPEEMRRLLDLG---VDGIITDRPDLLRAVLRE 238
 
Name Accession Description Interval E-value
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 360-660 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: 533.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 360 FLVITKDGASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLGNSTTVSLTAFRNRSTTVPELGSLGAIY 439
Cdd:cd08604    1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVATSKFSNRATTVPEIGSTSGIF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 440 TFSLTWAEIQTLTPAISNPYRVTSLFRNPKQKNAGKLFSLSDFLSLAKNStSLSGVLISVENAAYLREEQGLDVVKAVLD 519
Cdd:cd08604   81 TFDLTWSEIQTLKPAISNPYSVTGLFRNPANKNAGKFLTLSDFLDLAKNK-SLSGVLINVENAAYLAEKKGLDVVDAVLD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 520 TLTQTGYSNSTATKVMIQSTNSSVLVDFKKQSQYETVYKVEENIRDILDSAIEDIKKFADAVVIQKLSVFPVAQSFITTQ 599
Cdd:cd08604  160 ALTNAGYDNQTAQKVLIQSTDSSVLAAFKKQISYERVYVVDETIRDASDSSIEEIKKFADAVVIDRGSVFPVSTSFLTRQ 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219892334 600 TNVVEKLQKSQLPVYVELFQNEFLSQPYDFFADATVEINSYITGAGINGTITEFPFTAARY 660
Cdd:cd08604  240 TNVVEKLQSANLTVYVEVLRNEFVSLAFDFFADPTVEINSYVQGAGVDGFITEFPATAARY 300
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 44-343 9.63e-178

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


Pssm-ID: 176545  Cd Length: 299  Bit Score: 510.39  E-value: 9.63e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  44 PLVIARGGFSGLFPDSSYDAYNFAILTSVPDAVLWCDVQLTKDALGICFPDLTMRNSSSIEAVYPTRQKSYPVNGVPTSG 123
Cdd:cd08603    1 PLVIARGGFSGLFPDSSLFAYQFAASSSSPDVALWCDLQLTKDGVGICLPDLNLDNSTTIARVYPKRKKTYSVNGVSTKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 124 WFTIDFSLKDLKDVNLIRGILSRSEKFDGNSnPIMTVQSVSTQMKPSFFWLNVQHDAFYAQHNLSMSSFLVAASKTVLID 203
Cdd:cd08603   81 WFSVDFTLAELQQVTLIQGIFSRTPIFDGQY-PISTVEDVVTLAKPEGLWLNVQHDAFYQQHNLSMSSYLLSLSKTVKVD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 204 FISSPEVNFFKKIAGRFGRNGPSLVFRFLGQDEFEPTTNRTYGSILSNLTFVKTFASGILVPKSYILPLDDQQYLLPHTS 283
Cdd:cd08603  160 YISSPEVGFLKSIGGRVGRNGTKLVFRFLDKDDVEPSTNQTYGSILKNLTFIKTFASGILVPKSYIWPVDSDQYLQPATS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 284 LVQDAHKAGLEVFVSGFANDIDIAHDYSFDPVSEYLSFVDNGNFSVDGVLSDFPITASAS 343
Cdd:cd08603  240 LVQDAHKAGLEVYASGFANDFDISYNYSYDPVAEYLSFVGNGNFSVDGVLSDFPITASEA 299
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 360-660 1.28e-144

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: 425.93  E-value: 1.28e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 360 FLVITKDGASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLGNSTTVSLTAFRNRSTTVPELGSLGAIY 439
Cdd:cd08571    1 PLVIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPKRKKTYVVEGQSTSGIF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 440 TFSLTWAEIQTLTPAISNPYRVtsLFRNPKQKNAGKLFSLSDFLSLAKNSTsLSGVLISVENAAYLREEQGLDVVKAVLD 519
Cdd:cd08571   81 SFDLTWAEIQTLKPIISNPFSV--LFRNPRNDNAGKILTLEDFLTLAKPKS-LSGVWINVENAAFLAEHKGLLSVDAVLT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 520 TLTQTGYSNsTATKVMIQSTNSSVLVDFKKQ---SQYETVYKVEENIRDILDSAIEDIKKFADAVVIQKLSVFPV-AQSF 595
Cdd:cd08571  158 SLSKAGYDQ-TAKKVYISSPDSSVLKSFKKRvgtKLVFRVLDVDDTEPDTLLSNLTEIKKFASGVLVPKSYIWPVdSDSF 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219892334 596 ITTQTNVVEKLQKSQLPVYVELFQNEFLSQPYDFFADATVEINSYITGA-GINGTITEFPFTAARY 660
Cdd:cd08571  237 LTPQTSVVQDAHKAGLEVYVSGFANEFVSLAYDYSADPTLEILSFVGNGnSVDGVITDFPATAARA 302
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 44-342 2.11e-117

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: 355.83  E-value: 2.11e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  44 PLVIARGGFSGLFPDSSYDAYNFAILTSvpDAVLWCDVQLTKDALGICFPDLTMRNSSSIEAVYPTRQKSYPVNGVPTSG 123
Cdd:cd08571    1 PLVIARGGASGDYPDSTDLAYQKAISDG--ADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPKRKKTYVVEGQSTSG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 124 WFTIDFSLKDLKDVNLIRGILSRSEK---FDGNSNPIMTVQSVSTQMKP---SFFWLNVQHDAFYAQH--NLSMSSFLVA 195
Cdd:cd08571   79 IFSFDLTWAEIQTLKPIISNPFSVLFrnpRNDNAGKILTLEDFLTLAKPkslSGVWINVENAAFLAEHkgLLSVDAVLTS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 196 ASKTVL-----IDFISSPEVNFFKKIAGRfgrNGPSLVFRFLGQDEFEPTTnrtygsILSNLTFVKTFASGILVPKSYIL 270
Cdd:cd08571  159 LSKAGYdqtakKVYISSPDSSVLKSFKKR---VGTKLVFRVLDVDDTEPDT------LLSNLTEIKKFASGVLVPKSYIW 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219892334 271 PLDDQQYLLPHTSLVQDAHKAGLEVFVSGFANDID-IAHDYSFDPVSEYLSFVDNGNfSVDGVLSDFPITASA 342
Cdd:cd08571  230 PVDSDSFLTPQTSVVQDAHKAGLEVYVSGFANEFVsLAYDYSADPTLEILSFVGNGN-SVDGVITDFPATAAR 301
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 44-337 5.24e-33

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: 129.73  E-value: 5.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  44 PLVIARGGFSGLFPDSSYDAYNFAILTSVpDaVLWCDVQLTKDALGICFPDLTMRNSSSIEAV--YPTRQKSYPVNGVPT 121
Cdd:cd08602    1 PLVIAHRGASGYRPEHTLAAYQLAIEQGA-D-FIEPDLVSTKDGVLICRHEPELSGTTDVADHpeFADRKTTKTVDGVNV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 122 SGWFTIDFSLKDLKDVNLIRGILSRSEKFDGNSnPIMTVQSV--------STQMKPSFFWLNVQHDAFYAQH-NLSMSSF 192
Cdd:cd08602   79 TGWFTEDFTLAELKTLRARQRLPYRDQSYDGQF-PIPTFEEIialakaasAATGRTVGIYPEIKHPTYFNAPlGLPMEDK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 193 LVA---------ASKTVlidFISSPEVNFFKKIAGRfgrNGPSLVFRFLG----QDEFEPTTNRTYGSILSN--LTFVKT 257
Cdd:cd08602  158 LLEtlkkygytgKKAPV---FIQSFEVTNLKYLRNK---TDLPLVQLIDDatipPQDTPEGDSRTYADLTTDagLKEIAT 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 258 FASGILVPKSYILPLDDQQYLLPHTSLVQDAHKAGLEVFVSGFAN-DIDIAHDYSFDPVSEYLSFVDNGnfsVDGVLSDF 336
Cdd:cd08602  232 YADGIGPWKDLIIPSDANGRLGTPTDLVEDAHAAGLQVHPYTFRNeNTFLPPDFFGDPYAEYRAFLDAG---VDGLFTDF 308


                 .
gi 219892334 337 P 337
Cdd:cd08602  309 P 309
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 360-654 9.88e-28

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: 114.32  E-value: 9.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 360 FLVITKDGASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLGNSTTV-SLTAFRNRSTT-----VPELG 433
Cdd:cd08602    1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVaDHPEFADRKTTktvdgVNVTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 434 slgaIYTFSLTWAEIQTLTPAISNPYRVTS---LFRNPkqknagklfSLSDFLSLAKNSTSLS----GVLISVENAAYLR 506
Cdd:cd08602   81 ----WFTEDFTLAELKTLRARQRLPYRDQSydgQFPIP---------TFEEIIALAKAASAATgrtvGIYPEIKHPTYFN 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 507 EEQGLDVVKAVLDTLTQTGYSNSTAtKVMIQS------------TNSS--VLVDFKKQSQYETVYKVEENIRDIL-DSAI 571
Cdd:cd08602  148 APLGLPMEDKLLETLKKYGYTGKKA-PVFIQSfevtnlkylrnkTDLPlvQLIDDATIPPQDTPEGDSRTYADLTtDAGL 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 572 EDIKKFADAVVIQKLSVFPV-AQSFITTQTNVVEKLQKSQLPVYVELFQNE--FLsqPYDFFADATVEINSYITgAGING 648
Cdd:cd08602  227 KEIATYADGIGPWKDLIIPSdANGRLGTPTDLVEDAHAAGLQVHPYTFRNEntFL--PPDFFGDPYAEYRAFLD-AGVDG 303


                 ....*.
gi 219892334 649 TITEFP 654
Cdd:cd08602  304 LFTDFP 309
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 360-654 1.29e-26

Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in bacterial and eukaryotic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ. GP-GDEs are involved in glycerol metabolism and catalyze the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. In E. coli, there are two major G3P uptake systems: Glp and Ugp, which contain genes coding for two different GP-GDEs. GlpQ gene from the glp operon codes for a periplasmic phosphodiesterase GlpQ. GlpQ is a dimeric enzyme that hydrolyzes periplasmic glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), to the corresponding alcohols and G3P, which is subsequently transported into the cell through the GlpT transport system. Ca2+ is required for GlpQ enzymatic activity. This subfamily also includes some GP-GDEs in higher plants and their eukaryotic homologs, which show very high sequence similarities with bacterial periplasmic GP-GDEs.


Pssm-ID: 176502 [Multi-domain]  Cd Length: 296  Bit Score: 110.44  E-value: 1.29e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 360 FLVITKDGASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLGNSTTV-SLTAFRNRSTTvpelgslgAI 438
Cdd:cd08559    1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVaEHFPFRGRKDT--------GY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 439 YTFSLTWAEIQTLtpaisnpyRVTSLF------RNPKQKNAGKLFSLSDFLSLAKNSTSLS----GVLISVENAAYLREE 508
Cdd:cd08559   73 FVIDFTLAELKTL--------RAGSWFnqrypeRAPSYYGGFKIPTLEEVIELAQGLNKSTgrnvGIYPETKHPTFHKQE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 509 qGLDVVKAVLDTLTQTGYsNSTATKVMIQS--TNSSV-------------LVDFKKQSQYETVYKVEEnirDILDSAIED 573
Cdd:cd08559  145 -GPDIEEKLLEVLKKYGY-TGKNDPVFIQSfePESLKrlrnetpdiplvqLIDYGDWAETDKKYTYAW---LTTDAGLKE 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 574 IKKFADAVVIQKLSVFPVAQSFITTQTNVVEKLQKSQLPVYVELFQNEFLSQPYDFFADATVEINSyitgAGINGTITEF 653
Cdd:cd08559  220 IAKYADGIGPWKSLIIPEDSNGLLVPTDLVKDAHKAGLLVHPYTFRNENLFLAPDFKQDMDALYNA----AGVDGVFTDF 295


                 .
gi 219892334 654 P 654
Cdd:cd08559  296 P 296
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 44-337 2.88e-25

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: 106.59  E-value: 2.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  44 PLVIARGGFSGLFPDSSYDAYNFAILTSVPdaVLWCDVQLTKDALGICFPDLTMRNSSSIEAVYPTRqksypvnGVPTSG 123
Cdd:cd08559    1 PLVIAHRGASGYAPEHTLAAYALAIEMGAD--YIEQDLVMTKDGVLVARHDPTLDRTTNVAEHFPFR-------GRKDTG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 124 WFTIDFSLKDLKDVNLIRGILSRSEKFDGNSN---PIMTVQ---------SVSTQMKPSFFwLNVQHDAFYAQHNLSMSS 191
Cdd:cd08559   72 YFVIDFTLAELKTLRAGSWFNQRYPERAPSYYggfKIPTLEevielaqglNKSTGRNVGIY-PETKHPTFHKQEGPDIEE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 192 FLVAA-------SKTVLIdFISSPEVNFFKKIAGRFGrNGPsLVFRFLGQDEFEPTTNRTYGSILSN--LTFVKTFASGI 262
Cdd:cd08559  151 KLLEVlkkygytGKNDPV-FIQSFEPESLKRLRNETP-DIP-LVQLIDYGDWAETDKKYTYAWLTTDagLKEIAKYADGI 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 263 LVPKSYILPlDDQQYLLPHTSLVQDAHKAGLEVfvsgfandidiaHDYSFDPVSEYLSFVDNGNFS-------VDGVLSD 335
Cdd:cd08559  228 GPWKSLIIP-EDSNGLLVPTDLVKDAHKAGLLV------------HPYTFRNENLFLAPDFKQDMDalynaagVDGVFTD 294


                 ..
gi 219892334 336 FP 337
Cdd:cd08559  295 FP 296
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 44-340 3.49e-21

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


Pssm-ID: 176546  Cd Length: 300  Bit Score: 94.71  E-value: 3.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  44 PLVIARGGFSGLFPDSSYDAYNFAIltsvPDA--VLWCDVQLTKDALGICFPDLTMRNSSSI-EAVYPTRQKSYPVNGvP 120
Cdd:cd08604    1 PLIISHNGASGDYPGCTDLAYQKAV----KDGadVIDCSVQMSKDGVPFCLDSINLINSTTVaTSKFSNRATTVPEIG-S 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 121 TSGWFTIDFSLKDLKDVnliRGILSRSEKFDG--------NSNPIMTV---------QSVSTQMkpsffwLNVQHDAFYA 183
Cdd:cd08604   76 TSGIFTFDLTWSEIQTL---KPAISNPYSVTGlfrnpankNAGKFLTLsdfldlaknKSLSGVL------INVENAAYLA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 184 QH-NLSMSSFLVAA----------SKTVLIDFISSPEVNFFKKiagrfgRNGPSLVFRflgqdefeptTNRTYGSIL-SN 251
Cdd:cd08604  147 EKkGLDVVDAVLDAltnagydnqtAQKVLIQSTDSSVLAAFKK------QISYERVYV----------VDETIRDASdSS 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 252 LTFVKTFASGILVPKSYILPLDdQQYLLPHTSLVQDAHKAGLEVFVSGFAND-IDIAHDYSFDPVSEYLSFVdnGNFSVD 330
Cdd:cd08604  211 IEEIKKFADAVVIDRGSVFPVS-TSFLTRQTNVVEKLQSANLTVYVEVLRNEfVSLAFDFFADPTVEINSYV--QGAGVD 287

                        330
                 ....*....|
gi 219892334 331 GVLSDFPITA 340
Cdd:cd08604  288 GFITEFPATA 297
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 367-654 1.58e-19

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: 88.61  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  367 GASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLgnsttvsltafrNRSTTVpelgslgAIYTFSLTWA 446
Cdd:pfam03009   3 GASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNL------------DRTTDG-------AGYVRDLTLE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  447 EIQTLTPAISNPYrvtslfrnPKQKNAGKLFSLSDFLSLAKNSTSLSGVLISVENAAYLREEqgLDVVKAVLDTLTQTGY 526
Cdd:pfam03009  64 ELKRLDIGAGNSG--------PLSGERVPFPTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEE--GLIVKDLLLSVDEILA 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  527 SNSTATKVMIQSTNSSVLVDFkkqSQYETVYKVEENIRDILDSaiEDIKKFADAVVIQKLSVFPVAQSFITTQTNVVEKL 606
Cdd:pfam03009 134 KKADPRRVIFSSFNPDELKRL---RELAPKLPLVFLSSGRAYA--EADLLERAAAFAGAPALLGEVALVDEALPDLVKRA 208

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 219892334  607 QKSQLPVYVelfqneflsqpYdffadaTVEINSYIT---GAGINGTITEFP 654
Cdd:pfam03009 209 HARGLVVHV-----------W------TVNNEDEMKrllELGVDGVITDRP 242
GDPD_SHV3_repeat_1 cd08603
Glycerophosphodiester phosphodiesterase domain repeat 1 of glycerophosphodiester ...
 361-659 3.94e-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: 79.74  E-value: 3.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 361 LVITKDGASGDYPGCTDLAYKKAIKDGAD--VIDCSVQLSSDGTPFCLSSIDLGNSTTVSlTAFRNRSTTVPELG-SLGA 437
Cdd:cd08603    2 LVIARGGFSGLFPDSSLFAYQFAASSSSPdvALWCDLQLTKDGVGICLPDLNLDNSTTIA-RVYPKRKKTYSVNGvSTKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 438 IYTFSLTWAEIQTLT---PAISNPYRVTSLFrnpkqknagKLFSLSDFLSLAKnstsLSGVLISVENAAYLReEQGLDVV 514
Cdd:cd08603   81 WFSVDFTLAELQQVTliqGIFSRTPIFDGQY---------PISTVEDVVTLAK----PEGLWLNVQHDAFYQ-QHNLSMS 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 515 KAVLDTLTQTG--YSNST---------------ATKVMIQSTNSSVLVDFKKQSQYEtvykveenirdiLDSAIEDIKKF 577
Cdd:cd08603  147 SYLLSLSKTVKvdYISSPevgflksiggrvgrnGTKLVFRFLDKDDVEPSTNQTYGS------------ILKNLTFIKTF 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 578 ADAVVIQKLSVFPVAQS-FITTQTNVVEKLQKSQLPVYVELFQNEFLSqPYDFFADATVEINSYITGAG--INGTITEFP 654
Cdd:cd08603  215 ASGILVPKSYIWPVDSDqYLQPATSLVQDAHKAGLEVYASGFANDFDI-SYNYSYDPVAEYLSFVGNGNfsVDGVLSDFP 293


                 ....*
gi 219892334 655 FTAAR 659
Cdd:cd08603  294 ITASE 298
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
367-662 1.51e-15

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 76.83  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 367 GASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLgnsttvsltafrNRSTTVPelgslGAIYTFslTWA 446
Cdd:COG0584   10 GASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTL------------DRTTNGT-----GRVADL--TLA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 447 EIQTLTpaisnpyrvtslFRNPKQKNAGKLFSLSDFLSLAKNstslsGVLISVE--NAAYLREeqglDVVKAVLDTLTQT 524
Cdd:COG0584   71 ELRQLD------------AGSGPDFAGERIPTLEEVLELVPG-----DVGLNIEikSPPAAEP----DLAEAVAALLKRY 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 525 GYSNstatKVMIQSTNSSVLVDFKKQ-SQYETVYKVEENIRDILDSAIEDikkFADAVviqklsvfPVAQSFITTQtnVV 603
Cdd:COG0584  130 GLED----RVIVSSFDPEALRRLRELaPDVPLGLLVEELPADPLELARAL---GADGV--------GPDYDLLTPE--LV 192

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 219892334 604 EKLQKSQLPVYVelfqneflsqpydFFADATVEINSYItGAGINGTITEFPFTAARYKR 662
Cdd:COG0584  193 AAAHAAGLKVHV-------------WTVNDPEEMRRLL-DLGVDGIITDRPDLLRAVLR 237
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 362-653 5.67e-15

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: 73.84  E-value: 5.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 362 VITKDGASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIdlgnsttvsltafrnrsttvpelgslgaiytf 441
Cdd:cd08556    1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHDI-------------------------------- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 442 sltwaeiqtltpaisnpyrvtslfrnpkqknagklFSLSDFLSLAKNstslsGVLISVENAAYLREEqglDVVKAVLDTL 521
Cdd:cd08556   49 -----------------------------------PTLEEVLELVKG-----GVGLNIELKEPTRYP---GLEAKVAELL 85

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 522 TQTGysnsTATKVMIQSTNSSVLVDFKKQSQYETVYKVEENIRDILDSAIEDIKKFADAVVIQKLSVFPvaqsfittqtN 601
Cdd:cd08556   86 REYG----LEERVVVSSFDHEALRALKELDPEVPTGLLVDKPPLDPLLAELARALGADAVNPHYKLLTP----------E 151

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 219892334 602 VVEKLQKSQLPVYVELFQNEflsqpydffadatvEINSYITGAGINGTITEF 653
Cdd:cd08556  152 LVRAAHAAGLKVYVWTVNDP--------------EDARRLLALGVDGIITDD 189
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 360-654 9.19e-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: 9.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 360 FLVITKDGASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLGNSTTVSlTAFRNRSTtvpelgSLGAIY 439
Cdd:cd08600    1 KIIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVA-EKFPDRKR------KDGRYY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 440 TFSLTWAEIQTLtpaisnpyRVTSLF-------------RNPKQKNAGKLFSLSDFLSLAK--NSTSLSGVLISVE-NAA 503
Cdd:cd08600   74 VIDFTLDELKSL--------SVTERFdiengkkvqvypnRFPLWKSDFKIHTLEEEIELIQglNKSTGKNVGIYPEiKAP 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 504 YLREEQGLDVVKAVLDTLTQTGYSNStATKVMIQSTNSSVLVDFKKQ--SQYETVYKV---------EENIRDILDS--- 569
Cdd:cd08600  146 WFHHQEGKDIAAATLEVLKKYGYTSK-NDKVYLQTFDPNELKRIKNEllPKMGMDLKLvqliaytdwGETQEKDPGGwvn 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 570 ----------AIEDIKKFADAVVIQKLSVF-PVAQSFITTQTNVVEKLQKSQLPVYVELFQNEFLSQpydFFADATVEIN 638
Cdd:cd08600  225 ydydwmftkgGLKEIAKYADGVGPWYSMIIeEKSSKGNIVLTDLVKDAHEAGLEVHPYTVRKDALPE---YAKDADQLLD 301

                        330
                 ....*....|....*.
gi 219892334 639 SYITGAGINGTITEFP 654
Cdd:cd08600  302 ALLNKAGVDGVFTDFP 317
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 338-660 2.90e-06

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 50.06  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 338 ITASASLDCFSHvgrNATKQVDFLVITKDGASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLGNSTTV 417
Cdd:PRK11143   8 LLLAALLAGSAA---AAADSAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 418 SlTAFRNRSTTVpelgslGAIYTFSLTWAEIQTLtpaisnpyRVTSLF--RNPKQ-KNAGKLFSL--SDF---------- 482
Cdd:PRK11143  85 A-ERFPDRARKD------GRYYAIDFTLDEIKSL--------KFTEGFdiENGKKvQVYPGRFPMgkSDFrvhtfeeeie 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 483 ------LSLAKNstslSGVLISVEnAAYLREEQGLDVVKAVLDTLTQTGYSNSTAtKVMIQSTNSSVL------------ 544
Cdd:PRK11143 150 fiqglnHSTGKN----IGIYPEIK-APWFHHQEGKDIAAKVLEVLKKYGYTGKDD-KVYLQCFDANELkriknelepkmg 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 545 VDFK------KQSQYET-VYKVEENIRDI------LDSAIEDIKKFADAV------VIQKLSvfpvaQSFITTQTNVVEK 605
Cdd:PRK11143 224 MDLKlvqliaYTDWNETqEKQPDGKWVNYnydwmfKPGAMKEVAKYADGIgpdyhmLVDETS-----TPGNIKLTGMVKE 298

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219892334 606 LQKSQLPVYvelfqneflsqPYDFFADAtveINSYITG-----------AGINGTITEFPFTAARY 660
Cdd:PRK11143 299 AHQAKLVVH-----------PYTVRADQ---LPEYATDvnqlydilynqAGVDGVFTDFPDKAVKF 350
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 360-581 3.49e-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: 49.24  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 360 FLVITKDGASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTpfclssidlgnsttvsLTAFR----NRSTTVPELGSL 435
Cdd:cd08601    1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGV----------------LVAMHdetlDRTTNIERPGPV 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 436 GaiytfSLTWAEIQTLTpaisnpyrVTSLF--RNPKQKNAG----KLFSLSDFLSLAKNstslsgvlisveNAAYLREEQ 509
Cdd:cd08601   65 K-----DYTLAEIKQLD--------AGSWFnkAYPEYARESysglKVPTLEEVIERYGG------------RANYYIETK 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 510 GLDVV----KAVLDTLTQTGYSNSTAT--KVMIQStnssvlvdFKKQS---------QYETVYKVEE-NIRDILDSAIED 573
Cdd:cd08601  120 SPDLYpgmeEKLLATLDKYGLLTDNLKngQVIIQS--------FSKESlkklhqlnpNIPLVQLLWYgEGAETYDKWLDE 191


                 ....*...
gi 219892334 574 IKKFADAV 581
Cdd:cd08601  192 IKEYAIGI 199
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 44-337 6.41e-06

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: 48.93  E-value: 6.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334  44 PLVIARGGFSGLFPDSSYDAYNFAILTSVPdaVLWCDVQLTKDALGICFPDLTMRNSSSIEAVYPTRQKsypvngvPTSG 123
Cdd:cd08600    1 KIIIAHRGASGYLPEHTLEAKALAYAQGAD--YLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKR-------KDGR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 124 WFTIDFSLKDLKDvnlirgiLSRSEKFD----------GNSNP--------------IMTVQS----------VSTQMKP 169
Cdd:cd08600   72 YYVIDFTLDELKS-------LSVTERFDiengkkvqvyPNRFPlwksdfkihtleeeIELIQGlnkstgknvgIYPEIKA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 170 SFFW-----------LNVQHDAFYAQHN--LSMSSFLVAASKTVLIDFISSPEVNFfkKIAGRFGRN--GPSLVFRFLGQ 234
Cdd:cd08600  145 PWFHhqegkdiaaatLEVLKKYGYTSKNdkVYLQTFDPNELKRIKNELLPKMGMDL--KLVQLIAYTdwGETQEKDPGGW 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 235 DEFEPTTNRTYGsilsNLTFVKTFASGILVPKSYILPLDDQQYLLPHTSLVQDAHKAGLEVfvsgfandidiaHDYSF-- 312
Cdd:cd08600  223 VNYDYDWMFTKG----GLKEIAKYADGVGPWYSMIIEEKSSKGNIVLTDLVKDAHEAGLEV------------HPYTVrk 286

                        330       340       350
                 ....*....|....*....|....*....|.
gi 219892334 313 DPVSEYLSFVDN------GNFSVDGVLSDFP 337
Cdd:cd08600  287 DALPEYAKDADQlldallNKAGVDGVFTDFP 317
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 361-555 7.48e-06

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: 48.09  E-value: 7.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 361 LVITKDGASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLgNSTTvsltafrnrsttvpelGSLGAIYT 440
Cdd:cd08580    2 LIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDL-KSLT----------------NGSGAVSA 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 441 FslTWAEIQTLTPAISNPYRVTSLFRnpkQKNAGkLFSLSDFLslaknsTSLSGVLISVENAAYLREEQgldvVKAVLDT 520
Cdd:cd08580   65 Y--TAAQLATLNAGYNFKPEGGYPYR---GKPVG-IPTLEQVL------RAFPDTPFILDMKSLPADPQ----AKAVARV 128

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 219892334 521 LTQTGYSNstatKVMIQSTNSSVLVDFKKQSQYET 555
Cdd:cd08580  129 LERENAWS----RVRIYSTNADYQDALAPYPQARL 159
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 367-550 2.04e-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: 43.75  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 367 GASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLGNSTTVSltafrnrsttvpelgslgaIYTFSLTWA 446
Cdd:cd08575    8 GGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGS-------------------GLVSDLTYA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 447 EIQTLTPAisnpYRVT---SLFRNPKQKNAGKLFSLSDFLslaknsTSLSGVLISVEnaayLREEQGLDVVKAVLDTLTQ 523
Cdd:cd08575   69 ELPPLDAG----YGYTfdgGKTGYPRGGGDGRIPTLEEVF------KAFPDTPINID----IKSPDAEELIAAVLDLLEK 134

                        170       180
                 ....*....|....*....|....*..
gi 219892334 524 TGYSNstatKVMIQSTNSSVLVDFKKQ 550
Cdd:cd08575  135 YKRED----RTVWGSTNPEYLRALHPE 157
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 367-418 3.99e-04

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: 42.70  E-value: 3.99e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 219892334 367 GASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLGNSTTVS 418
Cdd:cd08581    6 GYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVE 57
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 367-570 8.76e-04

Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic glycerophosphodiester phosphodiesterase UgpQ and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Escherichia coli cytosolic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46), UgpQ, and similar proteins. GP-GDE plays an essential role in the metabolic pathway of E. coli. It catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. E. coli possesses two major G3P uptake systems: Glp and Ugp, which contain genes coding for two distinct GP-GDEs. UgpQ gene from the E. coli ugp operon codes for a cytosolic phosphodiesterase GlpQ, which is the prototype of this family. Various glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), can only be hydrolyzed by UgpQ during transport at the inner side of the cytoplasmic membrane to alcohols and G3P, which is a source of phosphate. In contrast to Ca2+-dependent periplasmic phosphodiesterase GlpQ, cytosolic phosphodiesterase UgpQ requires divalent cations, such as Mg2+, Co2+, or Mn2+, for its enzyme activity.


Pssm-ID: 176505 [Multi-domain]  Cd Length: 229  Bit Score: 41.44  E-value: 8.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 367 GASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCL--SSIDlgnsttvsltafrnRSTTvpelgSLGAIYtfSLT 444
Cdd:cd08562    6 GASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIhdDTLD--------------RTTN-----GSGAVT--ELT 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 445 WAEIQTLtpaisnpyrvtslfrnpkqkNAGKLFS----------LSDFLSLAKNstslSGVLISVE-NAAYLREEQGLDV 513
Cdd:cd08562   65 WAELAQL--------------------DAGSWFSpefagepiptLADVLELARE----LGLGLNLEiKPDPGDEALTARV 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 219892334 514 VKAVLDTLtqtgysNSTATKVMIQSTNSSVLVDFKKQ-SQYETVYKVEENIRDILDSA 570
Cdd:cd08562  121 VAAALREL------WPHASKLLLSSFSLEALRAARRAaPELPLGLLFDTLPADWLELL 172
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 367-489 1.50e-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: 41.45  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219892334 367 GASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLGNSTTVSlTAFRNRSTtvpeLGSLgaiytfSLTWA 446
Cdd:cd08609   34 GAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVK-DVFPGRDA----AGSN------NFTWT 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 219892334 447 EIQTLTPAI----SNPYRVTSLFRNPKQKNAG--KLFSLSDFLSLAKNS 489
Cdd:cd08609  103 ELKTLNAGSwfleRRPFWTLSSLSEEDRREADnqTVPSLSELLDLAKKH 151
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
281-346 3.00e-03

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 39.85  E-value: 3.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219892334 281 HTSLVQDAHKAGLEVFVsgfandidiahdYSFDPVSEYLSFVDNGnfsVDGVLSDFPITASASLDC 346
Cdd:COG0584  188 TPELVAAAHAAGLKVHV------------WTVNDPEEMRRLLDLG---VDGIITDRPDLLRAVLRE 238
 
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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