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Conserved domains on  [gi|518891225|ref|WP_020047100|]
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glycerophosphoryl diester phosphodiesterase [Rhizobium leguminosarum]

Protein Classification

glycerophosphoryl diester phosphodiesterase( domain architecture ID 10171129)

glycerophosphodiester phosphodiesterase catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which requires divalent cations, such as Mg2+, Co2+, or Mn2+, for its enzyme activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 15-244 6.32e-108

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: 310.69  E-value: 6.32e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  15 VQAHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWFSPK 94
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFSPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  95 FKGEPLPTLARVVSALGELGLNANVEIKQHAHHKSlgQLVKVVDRHLKARAAH-TEIMISSFDVAALRGMYEIDPSYELA 173
Cdd:cd08562   81 FAGEPIPTLADVLELARELGLGLNLEIKPDPGDEA--LTARVVAAALRELWPHaSKLLLSSFSLEALRAARRAAPELPLG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518891225 174 MLWSKLPADWTDILRSIPAKTIHLDYKALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITDDP 244
Cdd:cd08562  159 LLFDTLPADWLELLAALGAVSIHLNYRGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
 
Name Accession Description Interval E-value
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 15-244 6.32e-108

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: 310.69  E-value: 6.32e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  15 VQAHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWFSPK 94
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFSPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  95 FKGEPLPTLARVVSALGELGLNANVEIKQHAHHKSlgQLVKVVDRHLKARAAH-TEIMISSFDVAALRGMYEIDPSYELA 173
Cdd:cd08562   81 FAGEPIPTLADVLELARELGLGLNLEIKPDPGDEA--LTARVVAAALRELWPHaSKLLLSSFSLEALRAARRAAPELPLG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518891225 174 MLWSKLPADWTDILRSIPAKTIHLDYKALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITDDP 244
Cdd:cd08562  159 LLFDTLPADWLELLAALGAVSIHLNYRGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
15-244 8.56e-77

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 232.07  E-value: 8.56e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  15 VQAHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSwfSPK 94
Cdd:COG0584    5 IIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGS--GPD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  95 FKGEPLPTLARVVSALGeLGLNANVEIKQHAHHKSlgQLVKVVDRHLKARAAHTEIMISSFDVAALRGMYEIDPSYELAM 174
Cdd:COG0584   83 FAGERIPTLEEVLELVP-GDVGLNIEIKSPPAAEP--DLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 175 LWSKLPADWTDILRSIPAKTIHLDYKALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITDDP 244
Cdd:COG0584  160 LVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRP 229
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 17-242 4.36e-56

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 179.75  E-value: 4.36e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWFSPKFK 96
Cdd:PRK09454  12 AHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAAFA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  97 GEPLPTLARVVSALGELGLNANVEIKQHAHHKSL-GQLVKVVDRHLKARAAhTEIMISSFDVAALRGMYEIDPSYELAML 175
Cdd:PRK09454  92 GEPLPTLSQVAARCRAHGMAANIEIKPTTGREAEtGRVVALAARALWAGAA-VPPLLSSFSEDALEAARQAAPELPRGLL 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518891225 176 WSKLPADWTDILRSIPAKTIHLDYKALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITD 242
Cdd:PRK09454 171 LDEWPDDWLELTRRLGCVSLHLNHKLLDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTD 237
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 18-244 1.57e-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: 157.56  E-value: 1.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225   18 HRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWFSPKFKG 97
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225   98 EPL--PTLARVVSALGELGLNANVEIKQHA---HHKSLGQ---LVKVVDRHLKARAAHTEIMISSFDVAALRGMYEIDPS 169
Cdd:pfam03009  81 ERVpfPTLEEVLEFDWDVGFNIEIKIKPYVeaiAPEEGLIvkdLLLSVDEILAKKADPRRVIFSSFNPDELKRLRELAPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  170 YELAMLWSKLPADWTDI----LRSIPAK---TIHLDYKALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITD 242
Cdd:pfam03009 161 LPLVFLSSGRAYAEADLleraAAFAGAPallGEVALVDEALPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVITD 240


                  ..
gi 518891225  243 DP 244
Cdd:pfam03009 241 RP 242
 
Name Accession Description Interval E-value
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 15-244 6.32e-108

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: 310.69  E-value: 6.32e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  15 VQAHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWFSPK 94
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFSPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  95 FKGEPLPTLARVVSALGELGLNANVEIKQHAHHKSlgQLVKVVDRHLKARAAH-TEIMISSFDVAALRGMYEIDPSYELA 173
Cdd:cd08562   81 FAGEPIPTLADVLELARELGLGLNLEIKPDPGDEA--LTARVVAAALRELWPHaSKLLLSSFSLEALRAARRAAPELPLG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518891225 174 MLWSKLPADWTDILRSIPAKTIHLDYKALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITDDP 244
Cdd:cd08562  159 LLFDTLPADWLELLAALGAVSIHLNYRGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
15-244 8.56e-77

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 232.07  E-value: 8.56e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  15 VQAHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSwfSPK 94
Cdd:COG0584    5 IIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGS--GPD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  95 FKGEPLPTLARVVSALGeLGLNANVEIKQHAHHKSlgQLVKVVDRHLKARAAHTEIMISSFDVAALRGMYEIDPSYELAM 174
Cdd:COG0584   83 FAGERIPTLEEVLELVP-GDVGLNIEIKSPPAAEP--DLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 175 LWSKLPADWTDILRSIPAKTIHLDYKALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITDDP 244
Cdd:COG0584  160 LVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRP 229
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 17-244 4.74e-66

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: 204.33  E-value: 4.74e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWFSPKFK 96
Cdd:cd08563    5 AHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFDEKFT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  97 GEPLPTLARVVSALGELGLNANVEIKQHA-HHKSLGQLVKVVdrhLKARAAHTEIMISSFDVAALRGMYEIDPSYELAML 175
Cdd:cd08563   85 GEKIPTLEEVLDLLKDKDLLLNIEIKTDViHYPGIEKKVLEL---VKEYNLEDRVIFSSFNHESLKRLKKLDPKIKLALL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518891225 176 WSKLPADWTDILRSIPAKTIHLDYKALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITDDP 244
Cdd:cd08563  162 YETGLQDPKDYAKKIGADSLHPDFKLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 17-242 4.36e-56

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 179.75  E-value: 4.36e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWFSPKFK 96
Cdd:PRK09454  12 AHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAAFA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  97 GEPLPTLARVVSALGELGLNANVEIKQHAHHKSL-GQLVKVVDRHLKARAAhTEIMISSFDVAALRGMYEIDPSYELAML 175
Cdd:PRK09454  92 GEPLPTLSQVAARCRAHGMAANIEIKPTTGREAEtGRVVALAARALWAGAA-VPPLLSSFSEDALEAARQAAPELPRGLL 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518891225 176 WSKLPADWTDILRSIPAKTIHLDYKALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITD 242
Cdd:PRK09454 171 LDEWPDDWLELTRRLGCVSLHLNHKLLDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTD 237
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 17-243 2.02e-49

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: 160.51  E-value: 2.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVsinrcssskgnladltasdldaidagswfspkfk 96
Cdd:cd08556    3 AHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHDI---------------------------------- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  97 geplPTLARVVSALGElGLNANVEIKQHAHHKSLG-QLVKVVDRHLkaraAHTEIMISSFDVAALRGMYEIDPSYELAML 175
Cdd:cd08556   49 ----PTLEEVLELVKG-GVGLNIELKEPTRYPGLEaKVAELLREYG----LEERVVVSSFDHEALRALKELDPEVPTGLL 119

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 176 WSKLPADWTD--ILRSIPAKTIHLDYKALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITDD 243
Cdd:cd08556  120 VDKPPLDPLLaeLARALGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITDD 189
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 18-244 1.57e-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: 157.56  E-value: 1.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225   18 HRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWFSPKFKG 97
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225   98 EPL--PTLARVVSALGELGLNANVEIKQHA---HHKSLGQ---LVKVVDRHLKARAAHTEIMISSFDVAALRGMYEIDPS 169
Cdd:pfam03009  81 ERVpfPTLEEVLEFDWDVGFNIEIKIKPYVeaiAPEEGLIvkdLLLSVDEILAKKADPRRVIFSSFNPDELKRLRELAPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  170 YELAMLWSKLPADWTDI----LRSIPAK---TIHLDYKALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITD 242
Cdd:pfam03009 161 LPLVFLSSGRAYAEADLleraAAFAGAPallGEVALVDEALPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVITD 240


                  ..
gi 518891225  243 DP 244
Cdd:pfam03009 241 RP 242
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 17-246 9.40e-46

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: 152.85  E-value: 9.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWFSPKFK 96
Cdd:cd08582    3 AHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGSWKGESYK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  97 GEPLPTLARVVSALGELGLNANVEIKqhaHHKSLGQLVKVVDRHLKARAAHTE-IMISSFDVAALRGMYEIDPSYELAML 175
Cdd:cd08582   83 GEKVPTLEEYLAIVPKYGKKLFIEIK---HPRRGPEAEEELLKLLKESGLLPEqIVIISFDAEALKRVRELAPTLETLWL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518891225 176 WS--KLPADWTDILRSIPAKTIHLDY-KALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITDDPSV 246
Cdd:cd08582  160 RNykSPKEDPRPLAKSGGAAGLDLSYeKKLNPAFIKALRDAGLKLNVWTVDDAEDAKRLIELGVDSITTNRPGR 233
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 15-244 7.08e-40

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: 138.16  E-value: 7.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  15 VQAHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWFSPK 94
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  95 --------FKGEPLPTLARVVSALGelGLNANVEIKQhAHHKSLGQLVKVVDRHlkarAAHTEIMISSFDVAALRGMYEI 166
Cdd:cd08561   81 ggrtypyrGQGIRIPTLEELFEAFP--DVRLNIEIKD-DGPAAAAALADLIERY----GAQDRVLVASFSDRVLRRFRRL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 167 DPS-------YELA--MLWSKLpADWTDILRSIPAKTIHLDYKALSIG---FLEEAVRRGIKVRAWTCNDP---RRLAsf 231
Cdd:cd08561  154 CPRvatsageGEVAafVLASRL-GLGSLYSPPYDALQIPVRYGGVPLVtprFVRAAHAAGLEVHVWTVNDPaemRRLL-- 230

                        250
                 ....*....|...
gi 518891225 232 wDVGLTGVITDDP 244
Cdd:cd08561  231 -DLGVDGIITDRP 242
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 17-244 8.40e-40

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: 136.91  E-value: 8.40e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWfspkFK 96
Cdd:cd08579    3 AHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIGEN----GH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  97 GEPLPTLARVVSALGELGLNANVEIKQHAHHKslGQLVKVVDRHLKARAAHTEIMISSFDVAALRGMYEIDPS----YEL 172
Cdd:cd08579   79 GAKIPSLDEYLALAKGLKQKLLIELKPHGHDS--PDLVEKFVKLYKQNLIENQHQVHSLDYRVIEKVKKLDPKiktgYIL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518891225 173 AMLWSKLPAdwtdilrsIPAKTIHLDYKALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITDDP 244
Cdd:cd08579  157 PFNIGNLPK--------TNVDFYSIEYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 14-244 1.40e-35

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: 127.43  E-value: 1.40e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  14 EVQAHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSIN----RCSSS------KGNLADLTASDLD 83
Cdd:cd08567    2 DLQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNpditRDPDGawlpyeGPALYELTLAEIK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  84 AIDAG-----SWFSPKF------KGEPLPTLARVVSALGELGLNA---NVEIKQHAHHKSLGQLVKV-VDRHLKA-RAAH 147
Cdd:cd08567   82 QLDVGekrpgSDYAKLFpeqipvPGTRIPTLEEVFALVEKYGNQKvrfNIETKSDPDRDILHPPPEEfVDAVLAViRKAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 148 TE--IMISSFDVAALRGMYEIDPSYELAML-WSKLPADWTDILRSIPAKTIHLDYKALSIGFLEEAVRRGIKVRAWTCND 224
Cdd:cd08567  162 LEdrVVLQSFDWRTLQEVRRLAPDIPTVALtEETTLGNLPRAAKKLGADIWSPYFTLVTKELVDEAHALGLKVVPWTVND 241

                        250       260
                 ....*....|....*....|
gi 518891225 225 PRRLASFWDVGLTGVITDDP 244
Cdd:cd08567  242 PEDMARLIDLGVDGIITDYP 261
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 18-244 2.70e-34

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: 122.79  E-value: 2.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  18 HRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDagswfspkFKG 97
Cdd:cd08568    5 HRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLH--------PGG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  98 EPLPTLARVVSALGELGLnANVEIKQ-HAHHKSLGQLVKvvdrhlkaRAAHTEIMISSFDVAALRGMYEIDPSYELAMLW 176
Cdd:cd08568   77 ELIPTLEEVFRALPNDAI-INVEIKDiDAVEPVLEIVEK--------FNALDRVIFSSFNHDALRELRKLDPDAKVGLLI 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 177 SKLPA--DWTDILRSIPAKTIHLDYKALS-IGF------LEEAVRRGIKVRAWTCNDPR---RLASFWDvgltGVITDDP 244
Cdd:cd08568  148 GEEEEgfSIPELHEKLKLYSLHVPIDAIGyIGFekfvelLRLLRKLGLKIVLWTVNDPElvpKLKGLVD----GVITDDV 223
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 17-244 9.37e-33

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: 118.97  E-value: 9.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDA--GSWFSPK 94
Cdd:cd08581    3 AHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVaePARFGSR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  95 FKGEPLPTLARVVSALGEL-GLNANVEIKQHAHHkSLGqLVKVVDRHLKARAA-HTEIMISSFDVAALRGMYEIdpsyel 172
Cdd:cd08581   83 FAGEPLPSLAAVVQWLAQHpQVTLFVEIKTESLD-RFG-LERVVDKVLRALPAvAAQRVLISFDYDLLALAKQQ------ 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518891225 173 amLWSKLP---ADWTDILRSIPAKtIHLDYKALSIGFL--EEAV-RRGIKVRAWTCNDPrRLASFWDV-GLTGVITDDP 244
Cdd:cd08581  155 --GGPRTGwvlPDWDDASLAEADE-LQPDYLFCDKNLLpdTGDLwAGTWKWVIYEVNEP-AEALALAArGVALIETDNI 229
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 17-244 2.18e-32

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: 118.90  E-value: 2.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWF--SPK 94
Cdd:cd08573    3 GHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHrlSSR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  95 FKGEPLPTLARVVSALGELGLNANVEIKQHAhHKSLGQLVKVVDRHlkaRAAHTEIMISSFDVAALRGMYEIDPSYELAM 174
Cdd:cd08573   83 FPGEKIPTLEEAVKECLENNLRMIFDVKSNS-SKLVDALKNLFKKY---PGLYDKAIVCSFNPIVIYKVRKADPKILTGL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 175 LWSKLPADWTDILRSIPAKTIH-------LDY-----------------------KALSIGFLEEAVRRGIKVRAWTCND 224
Cdd:cd08573  159 TWRPWFLSYTDDEGGPRRKSGWkhflysmLDVilewslhswlpyflgvsallihkDDISSAYVRYWRARGIRVIAWTVNT 238

                        250       260
                 ....*....|....*....|
gi 518891225 225 PRRLASFWDVGLTGVITDDP 244
Cdd:cd08573  239 PTEKQYFAKTLNVPYITDSL 258
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 17-246 3.65e-32

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: 118.47  E-value: 3.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAG-------- 88
Cdd:cd08575    5 AHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGygytfdgg 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  89 -SWFSPKFKGEPLPTLARVVSALGELGLnaNVEIKQHahhkSLGQLV-KVVDRHLKARAAHTeIMISSFDVAALRgmyEI 166
Cdd:cd08575   85 kTGYPRGGGDGRIPTLEEVFKAFPDTPI--NIDIKSP----DAEELIaAVLDLLEKYKREDR-TVWGSTNPEYLR---AL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 167 DPSYELAM--------LWSKLPADWTDILRSIPAKT----IHLDYKALSIGFLEEAV-----------------RRGIKV 217
Cdd:cd08575  155 HPENPNLFesfsmtrcLLLYLALGYTGLLPFVPIKEsffeIPRPVIVLETFTLGEGAsivaallwwpnlfdhlrKRGIQV 234

                        250       260       270
                 ....*....|....*....|....*....|..
gi 518891225 218 RAWTCN---DPRRLAsfwDVGLTGVITDDPSV 246
Cdd:cd08575  235 YLWVLNdeeDFEEAF---DLGADGVMTDSPTK 263
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 15-248 5.21e-28

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: 106.72  E-value: 5.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  15 VQAHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWFspk 94
Cdd:cd08565    1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLRDSF--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  95 fkGEPLPTLARVVSALGELGLNANVEIKQHAHHKSLGQLVKVVDRHLKARAAHTEIMISSFDVAALRGMYeidPSYELAM 174
Cdd:cd08565   78 --GEKIPTLEEVLALFAPSGLELHVEIKTDADGTPYPGAAALAAATLRRHGLLERSVLTSFDPAVLTEVR---KHPGVRT 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 175 LWSkLPADW-------TDILRSIPAKT----IHLDYKALSiGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGVITDD 243
Cdd:cd08565  153 LGS-VDEDMlerlggeLPFLTATALKAhivaVEQSLLAAT-WELVRAAVPGLRLGVWTVNDDSLIRYWLACGVRQLTTDR 230


                 ....*
gi 518891225 244 PSVYL 248
Cdd:cd08565  231 PDLAL 235
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 15-244 1.03e-27

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: 106.23  E-value: 1.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  15 VQAHRGAS-AIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWFSp 93
Cdd:cd08566    2 VVAHRGGWgAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKDGDG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  94 KFKGEPLPTLARVVSAL-GELGLnaNVEIKQhahhKSLGQLVKVVDRHlkaRAAHTEIMIsSFDVAALRGMYEIDPSYEL 172
Cdd:cd08566   81 EVTDEKVPTLEEALAWAkGKILL--NLDLKD----ADLDEVIALVKKH---GALDQVIFK-SYSEEQAKELRALAPEVML 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 173 aMLWSKLPADWTDILRSI------PAKTIHLDYKALSIGFLEEAVRRGIKV-------------RAWTCNDPRRLASFWD 233
Cdd:cd08566  151 -MPIVRDAEDLDEEEARAidalnlLAFEITFDDLDLPPLFDELLRALGIRVwvntlgdddtaglDRALSDPREVWGELVD 229

                        250
                 ....*....|.
gi 518891225 234 VGLTGVITDDP 244
Cdd:cd08566  230 AGVDVIQTDRP 240
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 17-247 1.89e-27

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: 105.86  E-value: 1.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCS--SSKGNLADLTASDLDAIDAGSWFS-- 92
Cdd:cd08601    5 AHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTniERPGPVKDYTLAEIKQLDAGSWFNka 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  93 ------PKFKGEPLPTLARVVSALGElglNANVEIKQHAHHKSLG---QLVKVVDRH--LKARAAHTEIMISSFDVAALR 161
Cdd:cd08601   85 ypeyarESYSGLKVPTLEEVIERYGG---RANYYIETKSPDLYPGmeeKLLATLDKYglLTDNLKNGQVIIQSFSKESLK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 162 GMYEIDPSYELAMLWSKLP-----ADWTDILRSIpAKTIHLDYKALSIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGL 236
Cdd:cd08601  162 KLHQLNPNIPLVQLLWYGEgaetyDKWLDEIKEY-AIGIGPSIADADPWMVHLIHKKGLLVHPYTVNEKADMIRLINWGV 240

                        250
                 ....*....|.
gi 518891225 237 TGVITDDPSVY 247
Cdd:cd08601  241 DGMFTNYPDRL 251
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 17-244 9.58e-24

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: 96.57  E-value: 9.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSsskgNLA----------------DLTAS 80
Cdd:cd08559    5 AHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTT----NVAehfpfrgrkdtgyfviDFTLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  81 DLDAIDAGSWFSPKFK--------GEPLPTLARVVSALGEL----GLNANV--EIKQHAHHKSLG-----QLVKVVDRH- 140
Cdd:cd08559   81 ELKTLRAGSWFNQRYPerapsyygGFKIPTLEEVIELAQGLnkstGRNVGIypETKHPTFHKQEGpdieeKLLEVLKKYg 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 141 LKARAAHteIMISSFDVAALRGMYEIDPSYELAMLWSKLPADWTDILRSIPAKTIHLDYK-----ALSIG---------- 205
Cdd:cd08559  161 YTGKNDP--VFIQSFEPESLKRLRNETPDIPLVQLIDYGDWAETDKKYTYAWLTTDAGLKeiakyADGIGpwksliiped 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 206 ---------FLEEAVRRGIKVRAWTCN------------DPRRLasFWDVGLTGVITDDP 244
Cdd:cd08559  239 sngllvptdLVKDAHKAGLLVHPYTFRnenlflapdfkqDMDAL--YNAAGVDGVFTDFP 296
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 17-244 9.38e-20

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: 84.58  E-value: 9.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTA----SDLDAIDAGSwfs 92
Cdd:cd08570    3 GHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDSTwdelSHLRTIEEPH--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  93 pkfkgEPLPTLARVVSALGELGLNA---NVEIKQHAH----HKSLGQLVKVVD--RHLKARaahteIMISSFDVAALRGM 163
Cdd:cd08570   80 -----QPMPTLKDVLEWLVEHELPDvklMLDIKRDNDpeilFKLIAEMLAVKPdlDFWRER-----IILGLWHLDFLKYG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 164 YEIDPSYELAMLWSKLPADWTDILRSIPAKTIHLDYKAL----SIGFLEEAVRRGIKVRAWTCNDPRRLASFWDVGLTGV 239
Cdd:cd08570  150 KEVLPGFPVFHIGFSLDYARHFLNYSEKLVGISMHFVSLwgpfGQAFLPELKKNGKKVFVWTVNTEEDMRYAIRLGVDGV 229


                 ....*
gi 518891225 240 ITDDP 244
Cdd:cd08570  230 ITDDP 234
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 18-156 3.32e-19

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: 84.25  E-value: 3.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  18 HRGA--------SAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKG---------------NL 74
Cdd:cd08572    5 HRGLgknyasgsLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSKTgsdegelievpihdlTL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  75 ADLTASDLDAI-----DAGSWFSPKFKGE--------PLPTLARVVSALGE-LGLnaNVEIK---QHAHHKSLGQ----L 133
Cdd:cd08572   85 EQLKELGLQHIsalkrKALTRKAKGPKPNpwgmdehdPFPTLQEVLEQVPKdLGF--NIEIKypqLLEDGEGELTpyfeR 162

                        170       180
                 ....*....|....*....|....*.
gi 518891225 134 VKVVDRHLKARAAHT---EIMISSFD 156
Cdd:cd08572  163 NAFVDTILAVVFEHAggrRIIFSSFD 188
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 17-246 2.21e-18

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: 82.26  E-value: 2.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDL----DAID----AG 88
Cdd:cd08612   31 SHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLppylEKLEvtfsPG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  89 SWFSPKFKGEPLPTLARVVSALGELGLnaNVEIKQHAHhkslgQLVKVVDRHLKARAAHTEIMISSFDVAALRGMYEIDP 168
Cdd:cd08612  111 DYCVPKGSDRRIPLLEEVFEAFPDTPI--NIDIKVEND-----ELIKKVSDLVRKYKREDITVWGSFNDEIVKKCHKENP 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 169 SyeLAMLWSK----LPADW--TDILRSIPAK----------TIHLDYKALSIGFLEEAV------------------RRG 214
Cdd:cd08612  184 N--IPLFFSLkrvlLLLLLyyTGLLPFIPIKesfleipmpsIFLKTYFPKSMSRLNRFVlflidwllmrpslfrhlqKRG 261

                        250       260       270
                 ....*....|....*....|....*....|..
gi 518891225 215 IKVRAWTCNDPRRLASFWDVGLTGVITDDPSV 246
Cdd:cd08612  262 IQVYGWVLNDEEEFERAFELGADGVMTDYPTK 293
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 5-243 8.54e-18

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: 80.74  E-value: 8.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225   5 EPRSGPRRSEVQAHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSK--------GNLAD 76
Cdd:cd08609   19 EENNLPPKPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKdvfpgrdaAGSNN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  77 LTASDLDAIDAGSWFSPKfkgEPLPTLARVvsalgelglnANVEIKQHAHHK--SLGQLVKVVDRH-------LKaRAAH 147
Cdd:cd08609   99 FTWTELKTLNAGSWFLER---RPFWTLSSL----------SEEDRREADNQTvpSLSELLDLAKKHnvsimfdLR-NENN 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 148 TEIMISSFDVAALRGMYEIDPSyeLAMLWSKLPADWTDILRSIPA----------------KTIHLDYKALSIGFLEEAV 211
Cdd:cd08609  165 SHVFYSSFVFYTLETILKLGIP--PDKVWWLPDEYRHDVMKMEPGfkqvygrqkemlmdggNFMNLPYQDLSALEIKELR 242

                        250       260       270
                 ....*....|....*....|....*....|..
gi 518891225 212 RRGIKVRAWTCNDPRRLASFWDVGLTGVITDD 243
Cdd:cd08609  243 KDNVSVNLWVVNEPWLFSLLWCSGVSSVTTNA 274
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 17-229 1.41e-17

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: 78.90  E-value: 1.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRG---ASAIAPENTIAAFRAAAEQGAEwVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIdagswfsp 93
Cdd:cd08585    8 AHRGlhdRDAGIPENSLSAFRAAAEAGYG-IELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRAL-------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  94 KFKG--EPLPTLARVVSAL-GELGLnaNVEIKqhAHHKSLGQLVKVVDRHLKARAAHTEIMisSFDVAALRGMYEIDPSY 170
Cdd:cd08585   79 RLLGtdEHIPTLDEVLELVaGRVPL--LIELK--SCGGGDGGLERRVLAALKDYKGPAAIM--SFDPRVVRWFRKLAPGI 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518891225 171 ELAMLWSKLPaDWTDILRSIPAKTIHL--------DYKALSIGFLEEAV------RRGIKVRAWTCNDPRRLA 229
Cdd:cd08585  153 PRGQLSEGSN-DEADPAFWNEALLSALfsnlltrpDFIAYHLDDLPNPFvtlaraLLGMPVIVWTVRTEEDIA 224
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 18-156 1.74e-16

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: 76.95  E-value: 1.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  18 HRG-------ASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGN----------LADLTAS 80
Cdd:cd08607    5 HRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDsdrddllevpVKDLTYE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  81 DLDAI-----------DAGSWF----SPKFKgePLPTLARVVSALGE-LGLnaNVEIK---QHAHHKSLGQLVKVVDRHL 141
Cdd:cd08607   85 QLKLLklfhisalkvkEYKSVEededPPEHQ--PFPTLSDVLESVPEdVGF--NIEIKwpqQQKDGSWESELFTYFDRNL 160

                        170       180
                 ....*....|....*....|....
gi 518891225 142 KA---------RAAHTEIMISSFD 156
Cdd:cd08607  161 FVdiilkivleHAGKRRIIFSSFD 184
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 17-243 1.12e-15

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: 73.88  E-value: 1.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKG---NLADLTAS-----DLDAIDAG 88
Cdd:cd08574    6 GHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVADvfpERAHERASmftwtDLQQLNAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  89 SWFS---PKFKGEPL-------------PTLARvvsaLGELGLNANVEI--------KQHAHHKS-LGQLVKVVdrhLKA 143
Cdd:cd08574   86 QWFLkddPFWTASSLsesdreeagnqsiPSLAE----LLRLAKKHNKSVifdlrrppPNHPYYQSyVNITLDTI---LAS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 144 RAAHTEIM-ISSFDVAALRGMyeiDPSYELAMLwSKLPAdwtDILRSIPAKTIHLDYKALSIGFLEEAVRRGIKVRAWTC 222
Cdd:cd08574  159 GIPQHQVFwLPDEYRALVRKV---APGFQQVSG-RKLPV---ESLRENGISRLNLEYSQLSAQEIREYSKANISVNLYVV 231

                        250       260
                 ....*....|....*....|.
gi 518891225 223 NDPRRLASFWDVGLTGVITDD 243
Cdd:cd08574  232 NEPWLYSLLWCSGVQSVTTNA 252
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 12-220 2.75e-15

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: 73.28  E-value: 2.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  12 RSEVQAHRGA--SAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIH--------DVSINRCSSSKGNLADLTASD 81
Cdd:cd08564    3 RPIIVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteddtnpDTSIQLDDSGFKNINDLSLDE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  82 L------DAIDAGSWFSPKFKGEPLPTLARVVSALGElGLNANVEIKqhahhkslGQLVKVVDRHLKARAAH---TEIMI 152
Cdd:cd08564   83 ItrlhfkQLFDEKPCGADEIKGEKIPTLEDVLVTFKD-KLKYNIELK--------GREVGLGERVLNLVEKYgmiLQVHF 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518891225 153 SSF---DVAALRGMYEIDP-SYELAMLWSKLPA-DWTDIL---RSIPAKTIHLDYKALSIGFLEEAVRRGIKVRAW 220
Cdd:cd08564  154 SSFlhyDRLDLLKALRPNKlNVPIALLFNEVKSpSPLDFLeqaKYYNATWVNFSYDFWTEEFVKKAHENGLKVMTY 229
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 17-109 5.57e-15

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: 72.36  E-value: 5.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNLADLTASDLDAIDAGSWFSP--- 93
Cdd:cd08580    5 AHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAGYNFKPegg 84

                         90
                 ....*....|....*....
gi 518891225  94 -KFKGEPL--PTLARVVSA 109
Cdd:cd08580   85 yPYRGKPVgiPTLEQVLRA 103
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 17-209 6.05e-13

Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Escherichia coli periplasmic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46), GlpQ, and similar proteins. GP-GDE plays an essential role in the metabolic pathway of E. coli. It catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. E. coli possesses two major G3P uptake systems: Glp and Ugp, which contain genes coding for two different GP-GDEs. GlpQ gene from the E. coli glp operon codes for a periplasmic phosphodiesterase GlpQ, which is the prototype of this family. GlpQ is a dimeric enzyme that hydrolyzes periplasmic glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), to the corresponding alcohols and G3P, which is subsequently transported into the cell through the GlpT transport system. Ca2+ is required for the enzymatic activity of GlpQ. This family also includes a surface-exposed lipoprotein, protein D (HPD), from Haemophilus influenza Type b and nontypeable strains, which shows very high sequence similarity with E. coli GlpQ. HPD has been characterized as a human immunoglobulin D-binding protein with glycerophosphodiester phosphodiesterase activity. It can hydrolyze phosphatidylcholine from host membranes to produce free choline on the lipopolysaccharides on the surface of pathogenic bacteria.


Pssm-ID: 176542 [Multi-domain]  Cd Length: 318  Bit Score: 67.03  E-value: 6.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSsskgNLA----------------DLTAS 80
Cdd:cd08600    5 AHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVT----NVAekfpdrkrkdgryyviDFTLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  81 DLDAIDAGSWFSPKF-KGEP--------------LPTLARVVSALGELG--LNANV----EIKQHAHHKSLGQ-LVKVVD 138
Cdd:cd08600   81 ELKSLSVTERFDIENgKKVQvypnrfplwksdfkIHTLEEEIELIQGLNksTGKNVgiypEIKAPWFHHQEGKdIAAATL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518891225 139 RHLKA---RAAHTEIMISSFDVAALRGM-YEIDPSYELAMLWSKLPA--DWTDILRSIPAKTIHLDYKAL-SIGFLEE 209
Cdd:cd08600  161 EVLKKygyTSKNDKVYLQTFDPNELKRIkNELLPKMGMDLKLVQLIAytDWGETQEKDPGGWVNYDYDWMfTKGGLKE 238
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 18-242 6.17e-13

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: 67.21  E-value: 6.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  18 HRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCS--------SSKGNLADLTASDLDAIDAGS 89
Cdd:cd08610   28 HRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTnigevqpeSACENPAFFNWDFLSTLNAGK 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  90 WFspkFKGEPLPTLARVVSALGELGLN------------ANVEIK-----------QHAH-HKSLGQLVKVVDRHLKARa 145
Cdd:cd08610  108 WF---VKPRPFYNMKPLSEADKERARNqsipklsnflrlAEKENKlvifdlyrpppKHPYrHTWIRRVLEVILNEVGIE- 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 146 AHTEIMISSFDVAALRGMyeiDPSYELAMlWSKLPADwtDILRSIPAKtIHLDYKALSIGFLEEAVRRGIKVRAWTCNDP 225
Cdd:cd08610  184 QHLVLWLPAHDRQYVQSV---APGFKQHV-GRKVPIE--TLLKNNISI-LNLAYKKLFSNDIRDYKAANIHTNVYVINEP 256

                        250
                 ....*....|....*..
gi 518891225 226 RRLASFWDVGLTGVITD 242
Cdd:cd08610  257 WLFSLAWCSGIHSVTTN 273
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 27-192 8.72e-13

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: 66.28  E-value: 8.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  27 ENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHD--VSINRCS---SSKgnLADLTASDLDAI--DAGSWFSPK----- 94
Cdd:cd08605   25 ENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDdfIVVERGGeveSSR--IRDLTLAELKALgpQAESTKTSTvalyr 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  95 FKGEP------------LPTLARVVSAL-GELGLNANVEIKQHAH------HKSLGQLVKVVDRHLKARaahtEIMISSF 155
Cdd:cd08605  103 KAKDPepepwimdvedsIPTLEEVFSEVpPSLGFNIELKFGDDNKteaeelVRELRAILAVCKQHAPGR----RIMFSSF 178

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 518891225 156 DVAALRGMYEIDPSYELAMLWSKLPADWTDILR-SIPA 192
Cdd:cd08605  179 DPDAAVLLRALQSLYPVMFLTDCGPYTHNDPRRnSIEA 216
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 17-244 2.03e-12

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: 65.40  E-value: 2.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCS--SSKGNLAD-LTASDLDAIDAGSWFS- 92
Cdd:cd08602    5 AHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTdvADHPEFADrKTTKTVDGVNVTGWFTe 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  93 --------------------PKFKGE-PLPTLARVVS-ALGELGLNANV-----EIKQHAHHKSLGQLvKVVDRHLKARA 145
Cdd:cd08602   85 dftlaelktlrarqrlpyrdQSYDGQfPIPTFEEIIAlAKAASAATGRTvgiypEIKHPTYFNAPLGL-PMEDKLLETLK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225 146 AH------TEIMISSFDVAALRGMYEI---------------------DPSYELAMLWSklPADWTDI----------LR 188
Cdd:cd08602  164 KYgytgkkAPVFIQSFEVTNLKYLRNKtdlplvqliddatippqdtpeGDSRTYADLTT--DAGLKEIatyadgigpwKD 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518891225 189 SIpAKTIHLDYKALSIGFLEEAVRRGIKVRAWTC-NDPRRLAS------------FWDVGLTGVITDDP 244
Cdd:cd08602  242 LI-IPSDANGRLGTPTDLVEDAHAAGLQVHPYTFrNENTFLPPdffgdpyaeyraFLDAGVDGLFTDFP 309
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 12-91 3.74e-11

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: 62.17  E-value: 3.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  12 RSEVQAHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKG---NLADLTAS-----DLD 83
Cdd:cd08608    1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRvfpERQYEDASmfnwtDLE 80


                 ....*...
gi 518891225  84 AIDAGSWF 91
Cdd:cd08608   81 RLNAGQWF 88
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 15-242 3.89e-11

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: 60.14  E-value: 3.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  15 VQAHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDvsinrcssskgnladltaSDLDAIDAGswFSPK 94
Cdd:cd08555    1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHG------------------PTLDRTTAG--ILPP 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  95 FKGEPLPTLARVVSALGElglNANVEIKQHAHHKSLGQLVKVVDRHLKAR---AAHTEIMISSFDVAalrgmyeIDPSYE 171
Cdd:cd08555   61 TLEEVLELIADYLKNPDY---TIILSLEIKQDSPEYDEFLAKVLKELRVYfdyDLRGKVVLSSFNAL-------GVDYYN 130

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518891225 172 LAMLWSKLPAdwtdilrsipaktihldykalsigFLEEAVRRGIKVRAWTCND-PRRLASFWDVGLTGVITD 242
Cdd:cd08555  131 FSSKLIKDTE------------------------LIASANKLGLLSRIWTVNDnNEIINKFLNLGVDGLITD 178
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 17-135 1.60e-10

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: 60.07  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  17 AHRG----------------ASAIAP------ENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRCSSSKGNL 74
Cdd:cd08613   28 AHRGlaqtfdregvendtctAERIDPpthdylENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSGVT 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  75 ADLTASDLDAIDAGSWFSPK------FKGE---PLPTLARVVSALGELGLNANVEIKQHAHHKSLGQLVK 135
Cdd:cd08613  108 RDHTMAELKTLDIGYGYTADggktfpFRGKgvgMMPTLDEVFAAFPDRRFLINFKSDDAAEGELLAEKLA 177
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 15-61 7.01e-09

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 55.45  E-value: 7.01e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 518891225  15 VQAHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHD 61
Cdd:PRK11143  29 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHD 75
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 27-155 8.93e-07

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: 48.98  E-value: 8.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  27 ENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHDVSINRcSSSKGNLADLTA---SDLDAIDAGSWFSPK-FKG----- 97
Cdd:cd08606   24 ENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSE-TGTDVPIHDLTLeqfLHLSRMKYTVDFKKKgFKGnsrgh 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518891225  98 ---EPLPTLARVVSALGElGLNANVEIK----QHAHHKSLGQL-------VKVVDRHLKARAAHTEIMISSF 155
Cdd:cd08606  103 siqAPFTTLEELLKKLPK-SVGFNIELKypmlHEAEEEEVAPVaielnafVDTVLEKVFDYGAGRNIIFSSF 173
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 15-161 2.09e-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: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  15 VQAHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVV-----------IHDVSINRCSSSKGNLA-------- 75
Cdd:cd08571    3 VIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPIClpsinldnsttIASVFPKRKKTYVVEGQstsgifsf 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891225  76 DLTASDLDAI--DAGSWFS-----PKFKG-EPLPTLARVVS---ALGELGLNANVeikQHAH----HKSLGQLVKVVDRH 140
Cdd:cd08571   83 DLTWAEIQTLkpIISNPFSvlfrnPRNDNaGKILTLEDFLTlakPKSLSGVWINV---ENAAflaeHKGLLSVDAVLTSL 159

                        170       180
                 ....*....|....*....|...
gi 518891225 141 LKARAAHT--EIMISSFDVAALR 161
Cdd:cd08571  160 SKAGYDQTakKVYISSPDSSVLK 182
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 10-61 1.42e-04

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


Pssm-ID: 176503  Cd Length: 356  Bit Score: 42.41  E-value: 1.42e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 518891225  10 PRRSEVQ-AHRGASAIAPENTIAAFRAAAEQGAEWVELDVALLADGTPVVIHD 61
Cdd:cd08560   13 FRKTDFSiGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHS 65
GDPD_2 pfam13653
Glycerophosphoryl diester phosphodiesterase family; This family also includes ...
 216-244 1.75e-04

Glycerophosphoryl diester phosphodiesterase family; This family also includes glycerophosphoryl diester phosphodiesterases as well as 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: 433380 [Multi-domain]  Cd Length: 30  Bit Score: 37.86  E-value: 1.75e-04
                          10        20
                  ....*....|....*....|....*....
gi 518891225  216 KVRAWTCNDPRRLASFWDVGLTGVITDDP 244
Cdd:pfam13653   1 KVRFWTIDNKAAWKELMRLGVDGLNTDDP 29
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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