NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1093444235|ref|WP_070823831|]
View 

MULTISPECIES: glycerophosphodiester phosphodiesterase family protein [Staphylococcus]

Protein Classification

glycerophosphodiester phosphodiesterase( domain architecture ID 11426576)

glycerophosphodiester phosphodiesterase catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols

CATH:  3.20.20.190
EC:  3.1.4.-
Gene Ontology:  GO:0008081|GO:0006629|GO:0046872
PubMed:  38491249

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
12-245 8.14e-86

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


:

Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 254.79  E-value: 8.14e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGikWGDA 91
Cdd:COG0584     5 IIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAG--SGPD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 FKGTRISKLEDILQLARqYSKILLIELKVP-QQYPGIEDMLLDVLDRYHMPKRqVILQSFDEESVRSIASKTTEYKLGVL 170
Cdd:COG0584    83 FAGERIPTLEEVLELVP-GDVGLNIEIKSPpAAEPDLAEAVAALLKRYGLEDR-VIVSSFDPEALRRLRELAPDVPLGLL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093444235 171 ISKkkywhRLPNFEDISQ--YADYINPNYSIVTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGIITDIPDEL 245
Cdd:COG0584   161 VEE-----LPADPLELARalGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLL 232
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
12-245 8.14e-86

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 254.79  E-value: 8.14e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGikWGDA 91
Cdd:COG0584     5 IIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAG--SGPD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 FKGTRISKLEDILQLARqYSKILLIELKVP-QQYPGIEDMLLDVLDRYHMPKRqVILQSFDEESVRSIASKTTEYKLGVL 170
Cdd:COG0584    83 FAGERIPTLEEVLELVP-GDVGLNIEIKSPpAAEPDLAEAVAALLKRYGLEDR-VIVSSFDPEALRRLRELAPDVPLGLL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093444235 171 ISKkkywhRLPNFEDISQ--YADYINPNYSIVTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGIITDIPDEL 245
Cdd:COG0584   161 VEE-----LPADPLELARalGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLL 232
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 12-242 1.44e-71

Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermoanaerobacter tengcongensis glycerophosphodiester phosphodiesterase (TtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Despite the fact that most of GDPD family members exist as the monomer, TtGDE can function as a dimeric unit. Its catalytic mechanism is based on the general base-acid catalysis, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). A divalent metal cation is required for the enzyme activity of TtGDE.


Pssm-ID: 176506 [Multi-domain]  Cd Length: 230  Bit Score: 218.58  E-value: 1.44e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKWGDA 91
Cdd:cd08563     3 IFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFDEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 FKGTRISKLEDILQLARQYSKILLIELKVPQ-QYPGIEDMLLDVLDRYHMPKRqVILQSFDEESVRSIASKTTEYKLGVL 170
Cdd:cd08563    83 FTGEKIPTLEEVLDLLKDKDLLLNIEIKTDViHYPGIEKKVLELVKEYNLEDR-VIFSSFNHESLKRLKKLDPKIKLALL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093444235 171 iskkkYWHrlpNFEDISQY-----ADYINPNYSIVTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGIITDIP 242
Cdd:cd08563   162 -----YET---GLQDPKDYakkigADSLHPDFKLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 15-244 2.77e-47

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: 156.79  E-value: 2.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  15 HRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKWGDAFKG 94
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  95 TRISK--LEDILQLARQYSKILLIELKVPQQYPGIEDML--------LDVLDRYHMPKRQVILQSFDEESVRSIASKTTE 164
Cdd:pfam03009  81 ERVPFptLEEVLEFDWDVGFNIEIKIKPYVEAIAPEEGLivkdlllsVDEILAKKADPRRVIFSSFNPDELKRLRELAPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 165 YKLGVLISKKKYWHRLPNFEDIsQYAD-----YINPNYSIVTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGIIT 239
Cdd:pfam03009 161 LPLVFLSSGRAYAEADLLERAA-AFAGapallGEVALVDEALPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVIT 239


                  ....*
gi 1093444235 240 DIPDE 244
Cdd:pfam03009 240 DRPDT 244
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 12-245 2.41e-34

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 123.51  E-value: 2.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKWGDA 91
Cdd:PRK09454   10 IVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 FKGTRISKLEDILQLARQYSKILLIELKvPQqyPGIED-----MLLDVLDRYHMPKRQVILQSFDEESVRSIASKTTEYK 166
Cdd:PRK09454   90 FAGEPLPTLSQVAARCRAHGMAANIEIK-PT--TGREAetgrvVALAARALWAGAAVPPLLSSFSEDALEAARQAAPELP 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 167 LGVLISK-KKYWH-RLPNFEDISqyadyINPNYSIVTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGIITDIPDE 244
Cdd:PRK09454  167 RGLLLDEwPDDWLeLTRRLGCVS-----LHLNHKLLDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTDRIDL 241


                  .
gi 1093444235 245 L 245
Cdd:PRK09454  242 I 242
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
12-245 8.14e-86

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 254.79  E-value: 8.14e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGikWGDA 91
Cdd:COG0584     5 IIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAG--SGPD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 FKGTRISKLEDILQLARqYSKILLIELKVP-QQYPGIEDMLLDVLDRYHMPKRqVILQSFDEESVRSIASKTTEYKLGVL 170
Cdd:COG0584    83 FAGERIPTLEEVLELVP-GDVGLNIEIKSPpAAEPDLAEAVAALLKRYGLEDR-VIVSSFDPEALRRLRELAPDVPLGLL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093444235 171 ISKkkywhRLPNFEDISQ--YADYINPNYSIVTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGIITDIPDEL 245
Cdd:COG0584   161 VEE-----LPADPLELARalGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLL 232
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 12-242 1.44e-71

Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermoanaerobacter tengcongensis glycerophosphodiester phosphodiesterase (TtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Despite the fact that most of GDPD family members exist as the monomer, TtGDE can function as a dimeric unit. Its catalytic mechanism is based on the general base-acid catalysis, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). A divalent metal cation is required for the enzyme activity of TtGDE.


Pssm-ID: 176506 [Multi-domain]  Cd Length: 230  Bit Score: 218.58  E-value: 1.44e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKWGDA 91
Cdd:cd08563     3 IFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFDEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 FKGTRISKLEDILQLARQYSKILLIELKVPQ-QYPGIEDMLLDVLDRYHMPKRqVILQSFDEESVRSIASKTTEYKLGVL 170
Cdd:cd08563    83 FTGEKIPTLEEVLDLLKDKDLLLNIEIKTDViHYPGIEKKVLELVKEYNLEDR-VIFSSFNHESLKRLKKLDPKIKLALL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093444235 171 iskkkYWHrlpNFEDISQY-----ADYINPNYSIVTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGIITDIP 242
Cdd:cd08563   162 -----YET---GLQDPKDYakkigADSLHPDFKLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 12-248 7.55e-62

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: 194.40  E-value: 7.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKW--- 88
Cdd:cd08561     1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFtdd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  89 -GDAF----KGTRISKLEDILQL---ARqyskiLLIELKvpQQYPGIEDMLLDVLDRYHMPKRqVILQSFDEESVR---- 156
Cdd:cd08561    81 gGRTYpyrgQGIRIPTLEELFEAfpdVR-----LNIEIK--DDGPAAAAALADLIERYGAQDR-VLVASFSDRVLRrfrr 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 157 ---SIASKTTEYKLG--VLISKKKYWHRLPNFEDISQyadyINPNYS---IVTKKFIDGAHQVNLKVMPYTVNEAKAAQS 228
Cdd:cd08561   153 lcpRVATSAGEGEVAafVLASRLGLGSLYSPPYDALQ----IPVRYGgvpLVTPRFVRAAHAAGLEVHVWTVNDPAEMRR 228

                         250       260
                  ....*....|....*....|
gi 1093444235 229 LIKLGVDGIITDIPDELFQL 248
Cdd:cd08561   229 LLDLGVDGIITDRPDLLLEV 248
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 12-243 1.07e-59

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


Pssm-ID: 176524 [Multi-domain]  Cd Length: 233  Bit Score: 188.29  E-value: 1.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKWGDA 91
Cdd:cd08582     1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGSWKGES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 FKGTRISKLEDILQLARQYSKILLIELKVPQQYPGIEDMLLDVLDRYHMPKRQVILQSFDEESVRSI--ASKTTE-YKLG 168
Cdd:cd08582    81 YKGEKVPTLEEYLAIVPKYGKKLFIEIKHPRRGPEAEEELLKLLKESGLLPEQIVIISFDAEALKRVreLAPTLEtLWLR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093444235 169 VLISKK---KYWHRLPNFEDISqyadyINPNYSIvTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGIITDIPD 243
Cdd:cd08582   161 NYKSPKedpRPLAKSGGAAGLD-----LSYEKKL-NPAFIKALRDAGLKLNVWTVDDAEDAKRLIELGVDSITTNRPG 232
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 12-240 1.31e-59

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: 186.70  E-value: 1.31e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDdtidrtsngrgkvidytyeqlqqfdfgikwgda 91
Cdd:cd08556     1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 fkgtrISKLEDILQLARQySKILLIELKVPQQYPGIEDMLLDVLDRYHMPKRqVILQSFDEESVRSIASKTTEYKLGVLI 171
Cdd:cd08556    48 -----IPTLEEVLELVKG-GVGLNIELKEPTRYPGLEAKVAELLREYGLEER-VVVSSFDHEALRALKELDPEVPTGLLV 120

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093444235 172 SKKKYWHRLPnFEDISQYADYINPNYSIVTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGIITD 240
Cdd:cd08556   121 DKPPLDPLLA-ELARALGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITD 188
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 12-242 7.36e-59

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: 185.89  E-value: 7.36e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKWGDA 91
Cdd:cd08562     1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFSPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 FKGTRISKLEDILQLARQYSKILLIELKVpqqYPGIEDMLLDVLD----RYHMPKRQVILQSFDEESVRSIASKTTEYKL 167
Cdd:cd08562    81 FAGEPIPTLADVLELARELGLGLNLEIKP---DPGDEALTARVVAaalrELWPHASKLLLSSFSLEALRAARRAAPELPL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 168 GVLiskkkyWHRLPnfEDISQYADY-----INPNYSIVTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGIITDIP 242
Cdd:cd08562   158 GLL------FDTLP--ADWLELLAAlgavsIHLNYRGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 10-248 4.74e-52

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: 169.42  E-value: 4.74e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  10 FSIVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGR--GKVIDYTYEQLQQFDFGiK 87
Cdd:cd08601     1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIErpGPVKDYTLAEIKQLDAG-S 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  88 W---------GDAFKGTRISKLEDILQLARQYSKiLLIELKVPQQYPGIEDMLLDVLDRY-----HMPKRQVILQSFDEE 153
Cdd:cd08601    80 WfnkaypeyaRESYSGLKVPTLEEVIERYGGRAN-YYIETKSPDLYPGMEEKLLATLDKYglltdNLKNGQVIIQSFSKE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 154 SVRSIASKTTEYKLGVLISKKKywhrLPNF--EDISQYADY---INPNYSIVTKKFIDGAHQVNLKVMPYTVNEAKAAQS 228
Cdd:cd08601   159 SLKKLHQLNPNIPLVQLLWYGE----GAETydKWLDEIKEYaigIGPSIADADPWMVHLIHKKGLLVHPYTVNEKADMIR 234

                         250       260
                  ....*....|....*....|
gi 1093444235 229 LIKLGVDGIITDIPDELFQL 248
Cdd:cd08601   235 LINWGVDGMFTNYPDRLKEV 254
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 12-242 2.46e-48

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial glycerophosphodiester phosphodiesterases. In addition to a C-terminal GDPD domain, most members in this family have an N-terminus that functions as a membrane anchor.


Pssm-ID: 176521 [Multi-domain]  Cd Length: 220  Bit Score: 158.86  E-value: 2.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKwgda 91
Cdd:cd08579     1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIGEN---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 FKGTRISKLEDILQLARQYSKILLIELKVPQQYPgiEDMLLDVLDRYH--MPKRQVILQSFDEESVRSIASKTTEYKLGV 169
Cdd:cd08579    77 GHGAKIPSLDEYLALAKGLKQKLLIELKPHGHDS--PDLVEKFVKLYKqnLIENQHQVHSLDYRVIEKVKKLDPKIKTGY 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093444235 170 LISkkkywhrlPNFEDISQY-ADYINPNYSIVTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGIITDIP 242
Cdd:cd08579   155 ILP--------FNIGNLPKTnVDFYSIEYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 10-242 1.60e-47

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: 158.98  E-value: 1.60e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  10 FSIVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSN------------GRGKVIDYTYE 77
Cdd:cd08559     1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNvaehfpfrgrkdTGYFVIDFTLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  78 QLQQFDFGiKWGDAFKGTR---------ISKLEDILQLARQYSKILL------IELKVP----QQYPGIEDMLLDVLDRY 138
Cdd:cd08559    81 ELKTLRAG-SWFNQRYPERapsyyggfkIPTLEEVIELAQGLNKSTGrnvgiyPETKHPtfhkQEGPDIEEKLLEVLKKY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 139 HM--PKRQVILQSFDEESVRSIASKTTEYKLGVLISKKKyWHRLPNF------------EDISQYADYINPNYSIVTKK- 203
Cdd:cd08559   160 GYtgKNDPVFIQSFEPESLKRLRNETPDIPLVQLIDYGD-WAETDKKytyawlttdaglKEIAKYADGIGPWKSLIIPEd 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1093444235 204 ---------FIDGAHQVNLKVMPYTVNE------AKAAQSLIKL----GVDGIITDIP 242
Cdd:cd08559   239 sngllvptdLVKDAHKAGLLVHPYTFRNenlflaPDFKQDMDALynaaGVDGVFTDFP 296
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 15-244 2.77e-47

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: 156.79  E-value: 2.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  15 HRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKWGDAFKG 94
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  95 TRISK--LEDILQLARQYSKILLIELKVPQQYPGIEDML--------LDVLDRYHMPKRQVILQSFDEESVRSIASKTTE 164
Cdd:pfam03009  81 ERVPFptLEEVLEFDWDVGFNIEIKIKPYVEAIAPEEGLivkdlllsVDEILAKKADPRRVIFSSFNPDELKRLRELAPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 165 YKLGVLISKKKYWHRLPNFEDIsQYAD-----YINPNYSIVTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGIIT 239
Cdd:pfam03009 161 LPLVFLSSGRAYAEADLLERAA-AFAGapallGEVALVDEALPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVIT 239


                  ....*
gi 1093444235 240 DIPDE 244
Cdd:pfam03009 240 DRPDT 244
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 10-243 1.45e-46

Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and similar proteins. The prototype of this CD is a putative GP-GDE from Silicibacter pomeroyi (SpGDE). It shows high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176510 [Multi-domain]  Cd Length: 263  Bit Score: 155.55  E-value: 1.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  10 FSIVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTI--DRTSNGRGKVIDY--------TYEQL 79
Cdd:cd08567     1 FDLQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLnpDITRDPDGAWLPYegpalyelTLAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  80 QQFDFGIKWGD-----------AFKGTRISKLEDILQLARQYSK---ILLIELKVPQQYPG-------IEDMLLDVLDRY 138
Cdd:cd08567    81 KQLDVGEKRPGsdyaklfpeqiPVPGTRIPTLEEVFALVEKYGNqkvRFNIETKSDPDRDIlhpppeeFVDAVLAVIRKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 139 HMPKRqVILQSFDEESVRSIASKTTEYKLGVLISKKkywhRLPNFEDISQY--ADYINPNYSIVTKKFIDGAHQVNLKVM 216
Cdd:cd08567   161 GLEDR-VVLQSFDWRTLQEVRRLAPDIPTVALTEET----TLGNLPRAAKKlgADIWSPYFTLVTKELVDEAHALGLKVV 235

                         250       260
                  ....*....|....*....|....*..
gi 1093444235 217 PYTVNEAKAAQSLIKLGVDGIITDIPD 243
Cdd:cd08567   236 PWTVNDPEDMARLIDLGVDGIITDYPD 262
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 12-242 1.00e-41

Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (AtGDE, EC 3.1.4.46) and its uncharacterized eukaryotic homolgoues. Members in this family shows high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. AtGDE exists as a hexamer that is a trimer of dimers, which is unique among current known GDPD family members. However, it remains unclear if the hexamer plays a physiological role in AtGDE enzymatic function.


Pssm-ID: 176509 [Multi-domain]  Cd Length: 240  Bit Score: 142.44  E-value: 1.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLS-KRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKWGd 90
Cdd:cd08566     2 VVAHRGGWgAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKDGDG- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  91 AFKGTRISKLEDILQLARQysKILL-IELKvpqqyPGIEDMLLDVLDRYHMpKRQVILQSFDEESVRSIASKTTEYKLGV 169
Cdd:cd08566    81 EVTDEKVPTLEEALAWAKG--KILLnLDLK-----DADLDEVIALVKKHGA-LDQVIFKSYSEEQAKELRALAPEVMLMP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 170 LISKKKywhrlPNFEDISQYADYINPNYSIVTKK-------FIDGAHQVNLKVMPYTVNEAKAA-------------QSL 229
Cdd:cd08566   153 IVRDAE-----DLDEEEARAIDALNLLAFEITFDdldlpplFDELLRALGIRVWVNTLGDDDTAgldralsdprevwGEL 227

                         250
                  ....*....|...
gi 1093444235 230 IKLGVDGIITDIP 242
Cdd:cd08566   228 VDAGVDVIQTDRP 240
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 12-242 4.11e-41

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: 140.55  E-value: 4.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQF--DFGIKWG 89
Cdd:cd08581     1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLrvAEPARFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  90 DAFKGTRISKLEDILQ-LARQYSKILLIELKVPQ-QYPGIE---DMLLDVLDRYHmpkRQVILQSFDEESVRsIASKTTE 164
Cdd:cd08581    81 SRFAGEPLPSLAAVVQwLAQHPQVTLFVEIKTESlDRFGLErvvDKVLRALPAVA---AQRVLISFDYDLLA-LAKQQGG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 165 YKLGVLiskkkywhrLPNFEDIS-QYADYINPNYSIVTKK--FIDGA-HQVNLKVMPYTVNEAKAAQSLIKLGVDGIITD 240
Cdd:cd08581   157 PRTGWV---------LPDWDDASlAEADELQPDYLFCDKNllPDTGDlWAGTWKWVIYEVNEPAEALALAARGVALIETD 227


                  ..
gi 1093444235 241 IP 242
Cdd:cd08581   228 NI 229
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 12-243 1.72e-35

Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (pAtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176508 [Multi-domain]  Cd Length: 235  Bit Score: 126.36  E-value: 1.72e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKWGDA 91
Cdd:cd08565     1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLRDSFGEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 fkgtrISKLEDILQLaRQYSKILL-IELK---VPQQYPGIEDMLLDVLDRYHMPKRQViLQSFDEESVRSIASKTTEYKL 167
Cdd:cd08565    81 -----IPTLEEVLAL-FAPSGLELhVEIKtdaDGTPYPGAAALAAATLRRHGLLERSV-LTSFDPAVLTEVRKHPGVRTL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 168 GVLisKKKYWHRLPNFEDISQYADyiNPNYSIVTKKFIDGAHQV-------NLKVMPYTVNEAKAAQSLIKLGVDGIITD 240
Cdd:cd08565   154 GSV--DEDMLERLGGELPFLTATA--LKAHIVAVEQSLLAATWElvraavpGLRLGVWTVNDDSLIRYWLACGVRQLTTD 229


                  ...
gi 1093444235 241 IPD 243
Cdd:cd08565   230 RPD 232
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 12-245 2.41e-34

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 123.51  E-value: 2.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKWGDA 91
Cdd:PRK09454   10 IVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 FKGTRISKLEDILQLARQYSKILLIELKvPQqyPGIED-----MLLDVLDRYHMPKRQVILQSFDEESVRSIASKTTEYK 166
Cdd:PRK09454   90 FAGEPLPTLSQVAARCRAHGMAANIEIK-PT--TGREAetgrvVALAARALWAGAAVPPLLSSFSEDALEAARQAAPELP 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 167 LGVLISK-KKYWH-RLPNFEDISqyadyINPNYSIVTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGIITDIPDE 244
Cdd:PRK09454  167 RGLLLDEwPDDWLeLTRRLGCVS-----LHLNHKLLDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTDRIDL 241


                  .
gi 1093444235 245 L 245
Cdd:PRK09454  242 I 242
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 12-243 1.85e-32

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: 120.57  E-value: 1.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSN------------GRGKVIDYTYEQL 79
Cdd:cd08600     3 IIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNvaekfpdrkrkdGRYYVIDFTLDEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  80 QQFD----FGIKWGDAFK-----------GTRISKLEDILQLARQYSKI------LLIELKVP----QQYPGIEDMLLDV 134
Cdd:cd08600    83 KSLSvterFDIENGKKVQvypnrfplwksDFKIHTLEEEIELIQGLNKStgknvgIYPEIKAPwfhhQEGKDIAAATLEV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 135 LDRYHMPKRQ--VILQSFDEESVRSIASK-----TTEYKLGVLISKKKyWHRLPNFED-------------------ISQ 188
Cdd:cd08600   163 LKKYGYTSKNdkVYLQTFDPNELKRIKNEllpkmGMDLKLVQLIAYTD-WGETQEKDPggwvnydydwmftkgglkeIAK 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093444235 189 YADYINPNYSIVTKK-----------FIDGAHQVNLKVMPYTVNE------AKAAQSL-----IKLGVDGIITDIPD 243
Cdd:cd08600   242 YADGVGPWYSMIIEEksskgnivltdLVKDAHEAGLEVHPYTVRKdalpeyAKDADQLldallNKAGVDGVFTDFPD 318
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 12-245 6.85e-31

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: 115.01  E-value: 6.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIK---- 87
Cdd:cd08575     3 HIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGytfd 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  88 --WGDAF---KGTRISKLEDILQlaRQYSKILLIELKVPQQYPGIEdMLLDVLDRYhmpKRQ--VILQSFDEESVRSIA- 159
Cdd:cd08575    83 ggKTGYPrggGDGRIPTLEEVFK--AFPDTPINIDIKSPDAEELIA-AVLDLLEKY---KREdrTVWGSTNPEYLRALHp 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 160 -------SKTTEYKLGVLISkkKYWHRLPNFEDISQYAdYINPNYSIVTKKFIDGA------------------HQVNLK 214
Cdd:cd08575   157 enpnlfeSFSMTRCLLLYLA--LGYTGLLPFVPIKESF-FEIPRPVIVLETFTLGEgasivaallwwpnlfdhlRKRGIQ 233

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1093444235 215 VMPYTVNEAKAAQSLIKLGVDGIITDIPDEL 245
Cdd:cd08575   234 VYLWVLNDEEDFEEAFDLGADGVMTDSPTKL 264
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 12-240 5.73e-25

Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermotoga maritime glycerophosphodiester phosphodiesterase (TmGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. TmGDE exists as a monomer that might be the biologically relevant form.


Pssm-ID: 176511 [Multi-domain]  Cd Length: 226  Bit Score: 98.52  E-value: 5.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGikwgda 91
Cdd:cd08568     2 ILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHPG------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 fkGTRISKLEDILqLARQYSKILLIELKVPQQYpgieDMLLDVLDRYHMPKRqVILQSFDEESVRSIASKTTEYKLGVLI 171
Cdd:cd08568    76 --GELIPTLEEVF-RALPNDAIINVEIKDIDAV----EPVLEIVEKFNALDR-VIFSSFNHDALRELRKLDPDAKVGLLI 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 172 SKKkywHRLPNFEDIS------------QYADYINPNYsivTKKFIDGAHQVNLKVMPYTVNEAKAAQsLIKLGVDGIIT 239
Cdd:cd08568   148 GEE---EEGFSIPELHeklklyslhvpiDAIGYIGFEK---FVELLRLLRKLGLKIVLWTVNDPELVP-KLKGLVDGVIT 220


                  .
gi 1093444235 240 D 240
Cdd:cd08568   221 D 221
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 12-242 2.72e-22

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: 93.13  E-value: 2.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSN-----------------GRGK---- 70
Cdd:cd08602     3 VIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDvadhpefadrkttktvdGVNVtgwf 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  71 VIDYTYEQL-------------QQFDfgikwgDAFKgtrISKLEDILQLARQYSKILL------IELKVP---QQYPG-- 126
Cdd:cd08602    83 TEDFTLAELktlrarqrlpyrdQSYD------GQFP---IPTFEEIIALAKAASAATGrtvgiyPEIKHPtyfNAPLGlp 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 127 IEDMLLDVLDRYHM--PKRQVILQSFDEESVRSIASKTtEYKLGVLIS-------------KKKYWHRLPN--FEDISQY 189
Cdd:cd08602   154 MEDKLLETLKKYGYtgKKAPVFIQSFEVTNLKYLRNKT-DLPLVQLIDdatippqdtpegdSRTYADLTTDagLKEIATY 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093444235 190 ADYINPNYSIVTK-----------KFIDGAHQVNLKVMPYTV-NEA------------KAAQSLIKLGVDGIITDIP 242
Cdd:cd08602   233 ADGIGPWKDLIIPsdangrlgtptDLVEDAHAAGLQVHPYTFrNENtflppdffgdpyAEYRAFLDAGVDGLFTDFP 309
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 13-181 2.84e-22

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


Pssm-ID: 176527 [Multi-domain]  Cd Length: 237  Bit Score: 91.62  E-value: 2.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  13 VAHRGL---SKRYPENSYIGLKAALE--LPIdmlEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFdfgik 87
Cdd:cd08585     7 IAHRGLhdrDAGIPENSLSAFRAAAEagYGI---ELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRAL----- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  88 wgdAFKGT--RISKLEDILQLARQYSKiLLIELKVPQQYPG-IEDMLLDVLDRYHMPkrqVILQSFDEESVRSIASKTTE 164
Cdd:cd08585    79 ---RLLGTdeHIPTLDEVLELVAGRVP-LLIELKSCGGGDGgLERRVLAALKDYKGP---AAIMSFDPRVVRWFRKLAPG 151

                         170       180
                  ....*....|....*....|
gi 1093444235 165 YKLGVLIS---KKKYWHRLP 181
Cdd:cd08585   152 IPRGQLSEgsnDEADPAFWN 171
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 12-119 8.74e-22

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE1 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE1 (also known as MIR16, membrane interacting protein of RGS16) and their metazoan homologs. GDE1 is widely expressed in mammalian tissues, including the heart, brain, liver, and kidney. It shows sequence homology to bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. GDE1 has been characterized as GPI-GDE (EC 3.1.4.44) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate glycerol phosphate and inositol. It functions as an integral membrane-bound glycoprotein interacting with regulator of G protein signaling protein RGS16, and is modulated by G protein-coupled receptor (GPCR) signaling. In addition, GDE1 may interact with PRA1 domain family, member 2 (PRAF2, also known as JM4), which is an interacting protein of the G protein-coupled chemokine receptor CCR5. The catalytic activity, which is dependent on the integrity of the GDPD domain, is required for GDE1 cellular function.


Pssm-ID: 176515 [Multi-domain]  Cd Length: 258  Bit Score: 90.78  E-value: 8.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKWGDA 91
Cdd:cd08573     1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRLS 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1093444235  92 --FKGTRISKLEDILQLARQYSKILLIELK 119
Cdd:cd08573    81 srFPGEKIPTLEEAVKECLENNLRMIFDVK 110
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 11-245 9.16e-21

Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative Galdieria sulphuraria glycerophosphodiester phosphodiesterase (GsGDE, EC 3.1.4.46) and its uncharacterized eukaryotic homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176507 [Multi-domain]  Cd Length: 265  Bit Score: 88.30  E-value: 9.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  11 SIVAHRGL--SKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIH---DDTIDRTS-----NGRGKVIDYTYEQLQ 80
Cdd:cd08564     5 IIVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteDDTNPDTSiqlddSGFKNINDLSLDEIT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  81 QFDFGIKW------GDAFKGTRISKLEDILQLARQYSKiLLIELKVPQQypGIEDMLLDVLDRYHMPKrQVILQSFDEES 154
Cdd:cd08564    85 RLHFKQLFdekpcgADEIKGEKIPTLEDVLVTFKDKLK-YNIELKGREV--GLGERVLNLVEKYGMIL-QVHFSSFLHYD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 155 V----RSIASKTTEYKLGVLISKkkywHRLPNFEDISQYADYINPN-----YSIVTKKFIDGAHQVNLKVMPY---TVNE 222
Cdd:cd08564   161 RldllKALRPNKLNVPIALLFNE----VKSPSPLDFLEQAKYYNATwvnfsYDFWTEEFVKKAHENGLKVMTYfdePVND 236

                         250       260
                  ....*....|....*....|....
gi 1093444235 223 AKAA-QSLIKLGVDGIITDIPDEL 245
Cdd:cd08564   237 NEEDyKVYLELGVDCICPNDPVLL 260
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 12-242 9.58e-19

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: 81.88  E-value: 9.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVI-DYTYEQLQQFDfGIKWGD 90
Cdd:cd08570     1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIdDSTWDELSHLR-TIEEPH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  91 AfkgtRISKLEDILQLARQYS----KILLiELKV---PQQYPGIEDMLLDVLDRYHMPKRQVILQSFDEESVRSiaskTT 163
Cdd:cd08570    80 Q----PMPTLKDVLEWLVEHElpdvKLML-DIKRdndPEILFKLIAEMLAVKPDLDFWRERIILGLWHLDFLKY----GK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 164 EYKLGVLISkkkywHRLPNFEDISQYADYINPNYSI----------VTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLG 233
Cdd:cd08570   151 EVLPGFPVF-----HIGFSLDYARHFLNYSEKLVGIsmhfvslwgpFGQAFLPELKKNGKKVFVWTVNTEEDMRYAIRLG 225


                  ....*....
gi 1093444235 234 VDGIITDIP 242
Cdd:cd08570   226 VDGVITDDP 234
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 12-243 3.78e-18

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 82.03  E-value: 3.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSN------------GRGKVIDYTYEQL 79
Cdd:PRK11143   29 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDvaerfpdrarkdGRYYAIDFTLDEI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  80 QQFD----FGIKWGDAFKGT-----------RISKLEDILQLARQYSKI------LLIELKVP----QQYPGIEDMLLDV 134
Cdd:PRK11143  109 KSLKftegFDIENGKKVQVYpgrfpmgksdfRVHTFEEEIEFIQGLNHStgknigIYPEIKAPwfhhQEGKDIAAKVLEV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 135 LDRYHMPKRQ--VILQSFDEESVRSIAS----------------------KTTEYKLGVLISKKKY-WHRLPN-FEDISQ 188
Cdd:PRK11143  189 LKKYGYTGKDdkVYLQCFDANELKRIKNelepkmgmdlklvqliaytdwnETQEKQPDGKWVNYNYdWMFKPGaMKEVAK 268

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093444235 189 YADYINPNY-----------SIVTKKFIDGAHQVNLKVMPYTVNE---AKAAQS--------LIKLGVDGIITDIPD 243
Cdd:PRK11143  269 YADGIGPDYhmlvdetstpgNIKLTGMVKEAHQAKLVVHPYTVRAdqlPEYATDvnqlydilYNQAGVDGVFTDFPD 345
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 12-240 3.28e-17

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins. GDE5 is widely expressed in mammalian tissues, with highest expression in spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176514 [Multi-domain]  Cd Length: 293  Bit Score: 78.86  E-value: 3.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRY--------PENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTI-----DRTSNGRGKVIDY---- 74
Cdd:cd08572     2 VIGHRGLGKNYasgslagiRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTIsvsekSKTGSDEGELIEVpihd 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  75 -TYEQLQQ-------------------FDFGIKWGDAFKgTRISKLEDILqlaRQYSKIL--LIELKVPQQYPGIEDMLL 132
Cdd:cd08572    82 lTLEQLKElglqhisalkrkaltrkakGPKPNPWGMDEH-DPFPTLQEVL---EQVPKDLgfNIEIKYPQLLEDGEGELT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 133 DVLDRYHM------------PKRQVILQSFDEESVrsiasktteyklgVLISKKKywHRLPNF------EDISQYAD--- 191
Cdd:cd08572   158 PYFERNAFvdtilavvfehaGGRRIIFSSFDPDIC-------------IMLRLKQ--NKYPVLfltnggTNEVEHMDprr 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093444235 192 ----------------YINPNYSIV--TKKFIDGAHQVNLKVMPY--TVNEAKAAQSLIKLGVDGIITD 240
Cdd:cd08572   223 rslqaavnfalaegllGVVLHAEDLlkNPSLISLVKALGLVLFTYgdDNNDPENVKKQKELGVDGVIYD 291
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 12-240 4.21e-16

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


Pssm-ID: 176498 [Multi-domain]  Cd Length: 179  Bit Score: 73.62  E-value: 4.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTsngrgkvidytyeqlqqfdfgikwgda 91
Cdd:cd08555     1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRT--------------------------- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  92 FKGTRISKLEDILQLARQYSK------ILLIELKVP-QQYPGIEDMLLDVLDRYHMP--KRQVILQSFDEESVrsiaskt 162
Cdd:cd08555    54 TAGILPPTLEEVLELIADYLKnpdytiILSLEIKQDsPEYDEFLAKVLKELRVYFDYdlRGKVVLSSFNALGV------- 126

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093444235 163 TEYKLGVLiskkkywhrlpnfedisqyadyinpnySIVTKKFIDGAHQVNLKVMPYTVNEA-KAAQSLIKLGVDGIITD 240
Cdd:cd08555   127 DYYNFSSK---------------------------LIKDTELIASANKLGLLSRIWTVNDNnEIINKFLNLGVDGLITD 178
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 12-144 2.62e-15

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of mammalian glycerophosphodiester phosphodiesterase GDE4; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial homologs of mammalian GDE4, a transmembrane protein whose cellular function has not been elucidated yet.


Pssm-ID: 176554 [Multi-domain]  Cd Length: 309  Bit Score: 73.55  E-value: 2.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRY-----------------PENSYI-----GLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRG 69
Cdd:cd08613    26 LLAHRGLAQTFdregvendtctaeridpPTHDYLentiaSMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  70 KVIDYTYEQLQQFDFGIKW-GDA-----FKGTRISKLEDILQLARQY-SKILLIELKVPQQYPGieDMLLDVLDRyHMPK 142
Cdd:cd08613   106 VTRDHTMAELKTLDIGYGYtADGgktfpFRGKGVGMMPTLDEVFAAFpDRRFLINFKSDDAAEG--ELLAEKLAT-LPRK 182


                  ..
gi 1093444235 143 RQ 144
Cdd:cd08613   183 RL 184
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 12-121 2.51e-14

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: 70.43  E-value: 2.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFGIKW--- 88
Cdd:cd08580     3 IVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAGYNFkpe 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1093444235  89 -GDAF--KGTRISKLEDILqlaRQYSKILLI-ELKVP 121
Cdd:cd08580    83 gGYPYrgKPVGIPTLEQVL---RAFPDTPFIlDMKSL 116
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 12-222 2.53e-14

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: 70.03  E-value: 2.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSN------GRGKV--IDYTYEQLQQFD 83
Cdd:cd08574     4 LIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNvadvfpERAHEraSMFTWTDLQQLN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  84 FGiKW---GDAFKGT--------------RISKLEDILQLARQYSKILLIELKVPQQ----YPGIEDMLLDVLDRYHMPK 142
Cdd:cd08574    84 AG-QWflkDDPFWTAsslsesdreeagnqSIPSLAELLRLAKKHNKSVIFDLRRPPPnhpyYQSYVNITLDTILASGIPQ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 143 RQVI-LQSFDEESVRSIASktteyklGVlisKKKYWHRLPNFEDISQYADYINPNYSIVTKKFIDGAHQVNLKVMPYTVN 221
Cdd:cd08574   163 HQVFwLPDEYRALVRKVAP-------GF---QQVSGRKLPVESLRENGISRLNLEYSQLSAQEIREYSKANISVNLYVVN 232


                  .
gi 1093444235 222 E 222
Cdd:cd08574   233 E 233
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 13-105 2.08e-13

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE4 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1)) and similar proteins. Mammalian GDE4 is a transmembrane protein whose cellular function has not yet been elucidated. It is expressed widely, including in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. It is also expressed in the growth cones in neuroblastoma Neuro2a cells, which suggests GDE4 may play some distinct role from other members of the GDE family.


Pssm-ID: 176553 [Multi-domain]  Cd Length: 300  Bit Score: 68.40  E-value: 2.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  13 VAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQ--------QFDF 84
Cdd:cd08612    30 ISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLPpyleklevTFSP 109

                          90       100
                  ....*....|....*....|.
gi 1093444235  85 GIKWGDAFKGTRISKLEDILQ 105
Cdd:cd08612   110 GDYCVPKGSDRRIPLLEEVFE 130
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 13-151 1.18e-09

Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester phosphodiesterase GDE5 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative mammalian GDE5 and similar proteins. Mammalian GDE5 is widely expressed in mammalian tissues, with highest expression in the spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. In addition to C-terminal GDPD domain, all members in this subfamily have a starch binding domain (CBM20) in the N-terminus, which suggests these proteins may play a distinct role in glycerol metabolism.


Pssm-ID: 176549 [Multi-domain]  Cd Length: 290  Bit Score: 57.30  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  13 VAHRGLSKRY-------PENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTI----DRTSNGRGK------VIDYT 75
Cdd:cd08607     3 VGHRGAGNSYtaasavvRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLrvslKSKGDSDRDdllevpVKDLT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  76 YEQLQQFDFGIKwgDAFKGTRISKLEDIL---------QLARQYSKI-----LLIELKVPQQYPG--IEDMLLDVLDR-- 137
Cdd:cd08607    83 YEQLKLLKLFHI--SALKVKEYKSVEEDEdppehqpfpTLSDVLESVpedvgFNIEIKWPQQQKDgsWESELFTYFDRnl 160

                         170       180
                  ....*....|....*....|....
gi 1093444235 138 ----------YHMPKRQVILQSFD 151
Cdd:cd08607   161 fvdiilkivlEHAGKRRIIFSSFD 184
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 11-240 1.37e-09

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: 57.24  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  11 SIVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSN------GRGKV--IDYTYEQLQQF 82
Cdd:cd08609    28 ALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNvkdvfpGRDAAgsNNFTWTELKTL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  83 DFGiKW---------------GDAFKGTR--ISKLEDILQLARQYSKILLIELKVPQQ----YPGIEDMLLDVLDRYHMP 141
Cdd:cd08609   108 NAG-SWflerrpfwtlsslseEDRREADNqtVPSLSELLDLAKKHNVSIMFDLRNENNshvfYSSFVFYTLETILKLGIP 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 142 KRQVI-LQSFDEESVRSIASktteyklGVlisKKKYWHRLPNFEDISQyadYINPNYSIVTKKFIDGAHQVNLKVMPYTV 220
Cdd:cd08609   187 PDKVWwLPDEYRHDVMKMEP-------GF---KQVYGRQKEMLMDGGN---FMNLPYQDLSALEIKELRKDNVSVNLWVV 253

                         250       260
                  ....*....|....*....|
gi 1093444235 221 NEAKAAQSLIKLGVDGIITD 240
Cdd:cd08609   254 NEPWLFSLLWCSGVSSVTTN 273
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 11-248 1.61e-09

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: 57.16  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  11 SIVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNGRGKVIDYTYEQLQQFDFG----I 86
Cdd:cd08608     3 AIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYEDASMFNWTdlerL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  87 KWGDAFKGT--------------------RISKLEDILQLARQYSKILLIELK-VPQQYPGIEDML---LDVLDRYHMPK 142
Cdd:cd08608    83 NAGQWFLKDdpfwtaqslspsdrkeagnqSVCSLAELLELAKRYNASVLLNLRrPPPNHPYHQSWInltLKTILASGIPQ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 143 RQVI-LQSFDEESVRSIA---SKTTEYKLGVLISKKKYWHRLpnfedisqyadyiNPNYSIVTKKFIDGAHQVNLKVMPY 218
Cdd:cd08608   163 EQVMwTPDWQRKLVRKVApgfQQTSGEKLPVASLRERGITRL-------------NLRYTQASAQEIRDYSASNLSVNLY 229

                         250       260       270
                  ....*....|....*....|....*....|
gi 1093444235 219 TVNEAKAAQSLIKLGVDGIITDIPDELFQL 248
Cdd:cd08608   230 TVNEPWLYSLLWCSGVPSVTSDASHVLRKV 259
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 8-58 1.41e-07

Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic phosphodiesterase (GlpQ) include uncharacterized proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and their hypothetical homologs. Members in this subfamily show high sequence similarity to Escherichia coli periplasmic phosphodiesterase GlpQ, which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176503  Cd Length: 356  Bit Score: 51.27  E-value: 1.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1093444235   8 STFSIvAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHD 58
Cdd:cd08560    16 TDFSI-GHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHS 65
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 11-240 1.52e-06

Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester phosphodiesterase-like proteins similar to mammalian GDE5; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized plant glycerophosphodiester phosphodiesterase (GP-PDE)-like proteins. Members in this family show very high sequence homology to mammalian glycerophosphodiester phosphodiesterase GDE5 and are distantly related to plant GP-PDEs.


Pssm-ID: 176547 [Multi-domain]  Cd Length: 282  Bit Score: 48.18  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  11 SIVAHRGLSK--------RYP---ENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNG---RGKVIDYTY 76
Cdd:cd08605     1 AVIGHRGLGMnrashqpsVGPgirENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVERGGeveSSRIRDLTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  77 EQLQQF------------DFGIKWGDAFKGTRISKLED-ILQLARQYSKI-----LLIELKVPQQYPGIEDMLLDVLD-- 136
Cdd:cd08605    81 AELKALgpqaestktstvALYRKAKDPEPEPWIMDVEDsIPTLEEVFSEVppslgFNIELKFGDDNKTEAEELVRELRai 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 137 ----RYHMPKRQVILQSFDEESVRSIASKTTEYKLGVLISKKKYWHRLP---------------NFEDISQYADYINPNY 197
Cdd:cd08605   161 lavcKQHAPGRRIMFSSFDPDAAVLLRALQSLYPVMFLTDCGPYTHNDPrrnsieaaiqvalegGLQGIVSEVKVLLRNP 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1093444235 198 SIVTKkfidgAHQVNLKVMPYTV--NEAKAAQSLIKLGVDGIITD 240
Cdd:cd08605   241 TAVSL-----VKASGLELGTYGKlnNDAEAVERQADLGVDGVIVD 280
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 12-242 2.05e-06

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: 47.67  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKqLVVIHDD-------TIDRTSNGRGK-------------V 71
Cdd:cd08571     3 VIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDG-VPICLPSinldnstTIASVFPKRKKtyvvegqstsgifS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  72 IDYTYEQLQQF--DFGIKWGD-----AFKGT-RISKLEDILQLARQYSKI-LLIELKVP---QQYPGIeDMLLDVLD--- 136
Cdd:cd08571    82 FDLTWAEIQTLkpIISNPFSVlfrnpRNDNAgKILTLEDFLTLAKPKSLSgVWINVENAaflAEHKGL-LSVDAVLTsls 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 137 --RYHMPKRQVILQSfDEESV-RSIAS--KTTEYKLGVLISKKKYWHRLPNFEDISQYAD-------YINP----NYSIV 200
Cdd:cd08571   161 kaGYDQTAKKVYISS-PDSSVlKSFKKrvGTKLVFRVLDVDDTEPDTLLSNLTEIKKFASgvlvpksYIWPvdsdSFLTP 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1093444235 201 TKKFIDGAHQVNLKVMPYTVNEAKAAQS-------LIKL--------GVDGIITDIP 242
Cdd:cd08571   240 QTSVVQDAHKAGLEVYVSGFANEFVSLAydysadpTLEIlsfvgngnSVDGVITDFP 296
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 11-125 1.06e-04

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: 42.55  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  11 SIVAHRGLSKRYPENSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTSNgRGKVID---------YTYEQLQQ 81
Cdd:cd08610    24 TIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTN-IGEVQPesacenpafFNWDFLST 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093444235  82 FDFGiKW-----------------GDAFKGTRISKLEDILQLARQYSKILLIEL-KVPQQYP 125
Cdd:cd08610   103 LNAG-KWfvkprpfynmkplseadKERARNQSIPKLSNFLRLAEKENKLVIFDLyRPPPKHP 163
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 12-165 1.09e-04

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL110cp and other uncharacterized fungal homologs. The product of S. cerevisiae ORF YPL110c (GDE1), YPL110cp (Gde1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL110cp has been characterized as a cytoplasmic glycerophosphocholine (GPC)-specific phosphodiesterase that selectively hydrolyzes GPC, not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate. YPL110cp has multi-domain architecture, including not only C-terminal GDPD, but also an SPX N-terminal domain along with several ankyrin repeats, which implies that YPL110cp may mediate protein-protein interactions in a variety of proteins and play a role in maintaining cellular phosphate levels. Members in this family are distantly related to S. cerevisiae YPL206cp, which selectively catalyzes the cleavage of phosphatidylglycerol (PG), not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate, and has been characterized as a PG-specific phospholipase C.


Pssm-ID: 176548 [Multi-domain]  Cd Length: 286  Bit Score: 42.43  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  12 IVAHRGLSKRYPENSYIGL--------KAALELPIDMLEIDVHYTKDKQLVVIHDDTIDRTsngrGKVIDYTYEQLQQF- 82
Cdd:cd08606     4 VIGHRGLGKNTAERKSLQLgentvesfILAASLGASYVEVDVQLTKDLVPVIYHDFLVSET----GTDVPIHDLTLEQFl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  83 ---------DFGIKwgdAFKG-TR-------ISKLEDILQLARQySKILLIELKVPQQYPGIE--------------DML 131
Cdd:cd08606    80 hlsrmkytvDFKKK---GFKGnSRghsiqapFTTLEELLKKLPK-SVGFNIELKYPMLHEAEEeevapvaielnafvDTV 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1093444235 132 LDVLDRYHmPKRQVILQSFDEESVRSIASKTTEY 165
Cdd:cd08606   156 LEKVFDYG-AGRNIIFSSFTPDICILLSLKQPGY 188
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 25-240 5.43e-04

Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases; This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues.


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 39.98  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  25 NSYIGLKAALELPIDMLEIDVHYTKDKQLVVIHD------DTIDRTSNGRGKVIDY-------TYEQLQQFDFG--IKWG 89
Cdd:cd08583    16 NSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHSwdesllKQLGLPTSKNTKPLSYeefkskkIYGKYTPMDFKdvIDLL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235  90 DAFKGTRI---SKLEDILQLARQYSKIL---------LIELKVPQQYPgiEDMLLDVLDRYHMPKRQVILQSFDEESVRS 157
Cdd:cd08583    96 KKYPDVYIvtdTKQDDDNDIKKLYEYIVkeakevdpdLLDRVIPQIYN--EEMYEAIMSIYPFKSVIYTLYRQDSIRLDE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093444235 158 IASKTTEYKLGVLISKKKYwhrlpnfedisqyadyinpnysiVTKKFIDGAHQVNLKVMPYTVNEAKAAQSLIKLGVDGI 237
Cdd:cd08583   174 IIAFCYENGIKAVTISKNY-----------------------VNDKLIEKLNKAGIYVYVYTINDLKDAQEYKKLGVYGI 230


                  ...
gi 1093444235 238 ITD 240
Cdd:cd08583   231 YTD 233
DUF6067 pfam19543
Family of unknown function (DUF6067); This family of proteins is functionally uncharacterized. ...
 174-222 7.19e-03

Family of unknown function (DUF6067); This family of proteins is functionally uncharacterized. This family of proteins is mainly found in bacteria.


Pssm-ID: 437375  Cd Length: 967  Bit Score: 37.58  E-value: 7.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093444235 174 KKYWHRLPNFEDISQ---------YADYINP--NYSIVT----KKFIDGAHQVNLKV-MPYTVNE 222
Cdd:pfam19543 597 NRYYHAYSPLDDIKAtgatvinihHANAINPyiNYPFITadkmKAYIDEAHRKGLKVkIYYTVRE 661
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH