NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|505189193|ref|WP_015376295|]
View 

MULTISPECIES: glycerophosphodiester phosphodiesterase [Serratia]

Protein Classification

glycerophosphoryl diester phosphodiesterase( domain architecture ID 11484184)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 1-245 8.59e-172

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


:

Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 472.89  E-value: 8.59e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   1 MTRPWPYPHIVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQL 80
Cdd:PRK09454   1 MMSNWPYPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  81 DAGNWYSSAFKGERLPLLSEVAERCREHGLMANIEIKPTTGSDDETGRVVALAARLLWQGQ-TDPLLSSFSVEALAAAQR 159
Cdd:PRK09454  81 DAGSWFSAAFAGEPLPTLSQVAARCRAHGMAANIEIKPTTGREAETGRVVALAARALWAGAaVPPLLSSFSEDALEAARQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 160 TVPDLPRGLLLEDWDDNWRELTERLDCVSLHIDHKALTAERVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTDRID 239
Cdd:PRK09454 161 AAPELPRGLLLDEWPDDWLELTRRLGCVSLHLNHKLLDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTDRID 240


                 ....*.
gi 505189193 240 LIGPEF 245
Cdd:PRK09454 241 LIGPDF 246
 
Name Accession Description Interval E-value
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 1-245 8.59e-172

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 472.89  E-value: 8.59e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   1 MTRPWPYPHIVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQL 80
Cdd:PRK09454   1 MMSNWPYPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  81 DAGNWYSSAFKGERLPLLSEVAERCREHGLMANIEIKPTTGSDDETGRVVALAARLLWQGQ-TDPLLSSFSVEALAAAQR 159
Cdd:PRK09454  81 DAGSWFSAAFAGEPLPTLSQVAARCRAHGMAANIEIKPTTGREAETGRVVALAARALWAGAaVPPLLSSFSEDALEAARQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 160 TVPDLPRGLLLEDWDDNWRELTERLDCVSLHIDHKALTAERVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTDRID 239
Cdd:PRK09454 161 AAPELPRGLLLDEWPDDWLELTRRLGCVSLHLNHKLLDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTDRID 240


                 ....*.
gi 505189193 240 LIGPEF 245
Cdd:PRK09454 241 LIGPDF 246
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 10-238 9.04e-120

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: 340.74  E-value: 9.04e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGNWYSSA 89
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFSPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  90 FKGERLPLLSEVAERCREHGLMANIEIKPTTGSDDETGRVVALAARLLWQGQTDPLLSSFSVEALAAAQRTVPDLPRGLL 169
Cdd:cd08562   81 FAGEPIPTLADVLELARELGLGLNLEIKPDPGDEALTARVVAAALRELWPHASKLLLSSFSLEALRAARRAAPELPLGLL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505189193 170 LEDWDDNWRELTERLDCVSLHIDHKALTAERVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTDRI 238
Cdd:cd08562  161 FDTLPADWLELLAALGAVSIHLNYRGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
6-241 5.80e-82

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 245.16  E-value: 5.80e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   6 PYPHIVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGnw 85
Cdd:COG0584    1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAG-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  86 YSSAFKGERLPLLSEVAERCReHGLMANIEIKPTTGSDDETG-RVVALAARLLWQGQTdpLLSSFSVEALAAAQRTVPDL 164
Cdd:COG0584   79 SGPDFAGERIPTLEEVLELVP-GDVGLNIEIKSPPAAEPDLAeAVAALLKRYGLEDRV--IVSSFDPEALRRLRELAPDV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505189193 165 PRGLLLEDWDDNWRELTERLDCVSLHIDHKALTAERVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTDRIDLI 241
Cdd:COG0584  156 PLGLLVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLL 232
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 13-240 5.59e-54

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: 174.13  E-value: 5.59e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   13 HRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGNWYSSAFKG 92
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   93 ERL--PLLSEVAERCREHGLMANIEIKPT--TGSDDETGRVVALAA----RLLWQGQTDPL-LSSFSVEALAAAQRTVPD 163
Cdd:pfam03009  81 ERVpfPTLEEVLEFDWDVGFNIEIKIKPYveAIAPEEGLIVKDLLLsvdeILAKKADPRRViFSSFNPDELKRLRELAPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  164 LPRGLLLED----WDDNWRELTERLDCVSLHIDHKALT---AERVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTD 236
Cdd:pfam03009 161 LPLVFLSSGrayaEADLLERAAAFAGAPALLGEVALVDealPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVITD 240


                  ....
gi 505189193  237 RIDL 240
Cdd:pfam03009 241 RPDT 244
 
Name Accession Description Interval E-value
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 1-245 8.59e-172

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 472.89  E-value: 8.59e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   1 MTRPWPYPHIVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQL 80
Cdd:PRK09454   1 MMSNWPYPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  81 DAGNWYSSAFKGERLPLLSEVAERCREHGLMANIEIKPTTGSDDETGRVVALAARLLWQGQ-TDPLLSSFSVEALAAAQR 159
Cdd:PRK09454  81 DAGSWFSAAFAGEPLPTLSQVAARCRAHGMAANIEIKPTTGREAETGRVVALAARALWAGAaVPPLLSSFSEDALEAARQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 160 TVPDLPRGLLLEDWDDNWRELTERLDCVSLHIDHKALTAERVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTDRID 239
Cdd:PRK09454 161 AAPELPRGLLLDEWPDDWLELTRRLGCVSLHLNHKLLDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTDRID 240


                 ....*.
gi 505189193 240 LIGPEF 245
Cdd:PRK09454 241 LIGPDF 246
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 10-238 9.04e-120

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: 340.74  E-value: 9.04e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGNWYSSA 89
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFSPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  90 FKGERLPLLSEVAERCREHGLMANIEIKPTTGSDDETGRVVALAARLLWQGQTDPLLSSFSVEALAAAQRTVPDLPRGLL 169
Cdd:cd08562   81 FAGEPIPTLADVLELARELGLGLNLEIKPDPGDEALTARVVAAALRELWPHASKLLLSSFSLEALRAARRAAPELPLGLL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505189193 170 LEDWDDNWRELTERLDCVSLHIDHKALTAERVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTDRI 238
Cdd:cd08562  161 FDTLPADWLELLAALGAVSIHLNYRGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
6-241 5.80e-82

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 245.16  E-value: 5.80e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   6 PYPHIVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGnw 85
Cdd:COG0584    1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAG-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  86 YSSAFKGERLPLLSEVAERCReHGLMANIEIKPTTGSDDETG-RVVALAARLLWQGQTdpLLSSFSVEALAAAQRTVPDL 164
Cdd:COG0584   79 SGPDFAGERIPTLEEVLELVP-GDVGLNIEIKSPPAAEPDLAeAVAALLKRYGLEDRV--IVSSFDPEALRRLRELAPDV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505189193 165 PRGLLLEDWDDNWRELTERLDCVSLHIDHKALTAERVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTDRIDLI 241
Cdd:COG0584  156 PLGLLVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLL 232
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 13-240 5.59e-54

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: 174.13  E-value: 5.59e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   13 HRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGNWYSSAFKG 92
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   93 ERL--PLLSEVAERCREHGLMANIEIKPT--TGSDDETGRVVALAA----RLLWQGQTDPL-LSSFSVEALAAAQRTVPD 163
Cdd:pfam03009  81 ERVpfPTLEEVLEFDWDVGFNIEIKIKPYveAIAPEEGLIVKDLLLsvdeILAKKADPRRViFSSFNPDELKRLRELAPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  164 LPRGLLLED----WDDNWRELTERLDCVSLHIDHKALT---AERVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTD 236
Cdd:pfam03009 161 LPLVFLSSGrayaEADLLERAAAFAGAPALLGEVALVDealPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVITD 240


                  ....
gi 505189193  237 RIDL 240
Cdd:pfam03009 241 RPDT 244
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 10-236 9.62e-52

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: 167.73  E-value: 9.62e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGNWYSSA 89
Cdd:cd08563    3 IFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFDEK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  90 FKGERLPLLSEVAERCREHGLMANIEIKpTTGSDDEtG---RVVALAARLLWQGQTdpLLSSFSVEALAAAQRTVPDLPR 166
Cdd:cd08563   83 FTGEKIPTLEEVLDLLKDKDLLLNIEIK-TDVIHYP-GiekKVLELVKEYNLEDRV--IFSSFNHESLKRLKKLDPKIKL 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 167 GLLLEDWDDNWRELTERLDCVSLHIDHKALTAERVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTD 236
Cdd:cd08563  159 ALLYETGLQDPKDYAKKIGADSLHPDFKLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITN 228
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 10-237 1.12e-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: 161.28  E-value: 1.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDdtldrtsngwgvagelpwdklvqldagnwyssa 89
Cdd:cd08556    1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  90 fkgerLPLLSEVAERCREHGLMaNIEIKPTTGSDDETGRVVALAARLLWQGQTdpLLSSFSVEALAAAQRTVPDLPRGLL 169
Cdd:cd08556   48 -----IPTLEEVLELVKGGVGL-NIELKEPTRYPGLEAKVAELLREYGLEERV--VVSSFDHEALRALKELDPEVPTGLL 119

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 170 LEDWDDNWR--ELTERLDCVSLHIDHKALTAERVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTDR 237
Cdd:cd08556  120 VDKPPLDPLlaELARALGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITDD 189
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 10-237 1.85e-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: 154.39  E-value: 1.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGNWYSSA 89
Cdd:cd08582    1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGSWKGES 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  90 FKGERLPLLSEVAERCREHGLMANIEIK-PTTGSDDETGRVVALAARLLWQGQTdpLLSSFSVEALAAAQRTVPDLPRGL 168
Cdd:cd08582   81 YKGEKVPTLEEYLAIVPKYGKKLFIEIKhPRRGPEAEEELLKLLKESGLLPEQI--VIISFDAEALKRVRELAPTLETLW 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505189193 169 LLEDWDDNWRELTERLDC----VSLHIDHKaLTAERVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTDR 237
Cdd:cd08582  159 LRNYKSPKEDPRPLAKSGgaagLDLSYEKK-LNPAFIKALRDAGLKLNVWTVDDAEDAKRLIELGVDSITTNR 230
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 10-237 7.42e-41

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


Pssm-ID: 176509 [Multi-domain]  Cd Length: 240  Bit Score: 140.13  E-value: 7.42e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGG-GSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGNWySS 88
Cdd:cd08566    2 VVAHRGGwGAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKDG-DG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  89 AFKGERLPLLSEVAERCREHGLMaNIEIKpttgsDDETGRVVALAARLLWQGQTdpLLSSFSVEALAAAQRTVPDLPRGL 168
Cdd:cd08566   81 EVTDEKVPTLEEALAWAKGKILL-NLDLK-----DADLDEVIALVKKHGALDQV--IFKSYSEEQAKELRALAPEVMLMP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 169 LLEDWDDNWRELTERLDCVSLHI-----DHKALTAERVKALKDAGLRILVYTVNQPDRARL-------------LLDWGV 230
Cdd:cd08566  153 IVRDAEDLDEEEARAIDALNLLAfeitfDDLDLPPLFDELLRALGIRVWVNTLGDDDTAGLdralsdprevwgeLVDAGV 232


                 ....*..
gi 505189193 231 DCICTDR 237
Cdd:cd08566  233 DVIQTDR 239
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 10-240 9.12e-39

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: 135.14  E-value: 9.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGW--GVAGELPWDKLVQLDAGNWYS 87
Cdd:cd08601    3 VIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIErpGPVKDYTLAEIKQLDAGSWFN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  88 SA--------FKGERLPLLSEVAERCREHglmAN--IEIK-PTTGSDDETgRVVALAARLLWQGQTDP----LLSSFSVE 152
Cdd:cd08601   83 KAypeyaresYSGLKVPTLEEVIERYGGR---ANyyIETKsPDLYPGMEE-KLLATLDKYGLLTDNLKngqvIIQSFSKE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 153 ALAAAQRTVPDLPRGLLLedWDDNWRELTE-RLD-----CVSLHIDHKALTAERVKALKDAGLRILVYTVNQPDRARLLL 226
Cdd:cd08601  159 SLKKLHQLNPNIPLVQLL--WYGEGAETYDkWLDeikeyAIGIGPSIADADPWMVHLIHKKGLLVHPYTVNEKADMIRLI 236

                        250
                 ....*....|....
gi 505189193 227 DWGVDCICTDRIDL 240
Cdd:cd08601  237 NWGVDGMFTNYPDR 250
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 10-240 2.89e-37

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: 131.23  E-value: 2.89e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGNW---- 85
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHftdd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  86 ----YSSAFKGERLPLLSEVAERCREHGLmaNIEIKpttgsDDETGRVVALAARLLWQGQTDP-LLSSFSVEALAAAQRT 160
Cdd:cd08561   81 ggrtYPYRGQGIRIPTLEELFEAFPDVRL--NIEIK-----DDGPAAAAALADLIERYGAQDRvLVASFSDRVLRRFRRL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 161 VPDLP--------RGLLLEDWDDNWRELTERLDCVSLHIDHKAL---TAERVKALKDAGLRILVYTVNQPDRARLLLDWG 229
Cdd:cd08561  154 CPRVAtsagegevAAFVLASRLGLGSLYSPPYDALQIPVRYGGVplvTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLG 233

                        250
                 ....*....|.
gi 505189193 230 VDCICTDRIDL 240
Cdd:cd08561  234 VDGIITDRPDL 244
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 10-237 2.76e-33

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: 119.96  E-value: 2.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGNWyssa 89
Cdd:cd08579    1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIGEN---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  90 FKGERLPLLSEVAERCREHGLMANIEIKPT-TGSDDETGRVVALAARLLWQGQTdpLLSSFSVEALAAAQRTVPDLPRGL 168
Cdd:cd08579   77 GHGAKIPSLDEYLALAKGLKQKLLIELKPHgHDSPDLVEKFVKLYKQNLIENQH--QVHSLDYRVIEKVKKLDPKIKTGY 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 169 LLEdwdDNWREL-TERLDCVSlhIDHKALTAERVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTDR 237
Cdd:cd08579  155 ILP---FNIGNLpKTNVDFYS--IEYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDY 219
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 10-240 1.70e-31

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: 115.58  E-value: 1.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGNWYssa 89
Cdd:cd08565    1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLRDSF--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  90 fkGERLPLLSEVAERCREHGLMANIEIKPTTGSDDETGrVVALAARLLWQGQTDP--LLSSFSVEALAAAqRTVPDLPRG 167
Cdd:cd08565   78 --GEKIPTLEEVLALFAPSGLELHVEIKTDADGTPYPG-AAALAAATLRRHGLLErsVLTSFDPAVLTEV-RKHPGVRTL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 168 LLLedwDDNWREL-----------TERLDCVSLHIDHKALTAERVKALKDaGLRILVYTVNQPDRARLLLDWGVDCICTD 236
Cdd:cd08565  154 GSV---DEDMLERlggelpfltatALKAHIVAVEQSLLAATWELVRAAVP-GLRLGVWTVNDDSLIRYWLACGVRQLTTD 229


                 ....
gi 505189193 237 RIDL 240
Cdd:cd08565  230 RPDL 233
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 8-240 4.78e-30

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: 112.79  E-value: 4.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   8 PHIVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLD----RTSNG-WGVAGELPW-----DKL 77
Cdd:cd08567    1 FDLQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNpditRDPDGaWLPYEGPALyeltlAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  78 VQLDAG-----NWYSSAF------KGERLPLLSEVAERCREHGLMA---NIEIKPTTGSDDETGRVVALAARLL------ 137
Cdd:cd08567   81 KQLDVGekrpgSDYAKLFpeqipvPGTRIPTLEEVFALVEKYGNQKvrfNIETKSDPDRDILHPPPEEFVDAVLavirka 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 138 -WQGQTdpLLSSFSVEALAAAQRTVPDLPRGLL-----LEDWDDNWRELTerLDCVSlhIDHKALTAERVKALKDAGLRI 211
Cdd:cd08567  161 gLEDRV--VLQSFDWRTLQEVRRLAPDIPTVALteettLGNLPRAAKKLG--ADIWS--PYFTLVTKELVDEAHALGLKV 234

                        250       260
                 ....*....|....*....|....*....
gi 505189193 212 LVYTVNQPDRARLLLDWGVDCICTDRIDL 240
Cdd:cd08567  235 VPWTVNDPEDMARLIDLGVDGIITDYPDL 263
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 10-117 1.22e-29

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: 111.58  E-value: 1.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDA--GNWYS 87
Cdd:cd08573    1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAaaKHRLS 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 505189193  88 SAFKGERLPLLSEVAERCREHGLMANIEIK 117
Cdd:cd08573   81 SRFPGEKIPTLEEAVKECLENNLRMIFDVK 110
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 10-238 3.62e-29

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: 109.34  E-value: 3.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTL----AAIDVGARHghkmIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDA--G 83
Cdd:cd08581    1 LVAHRGYPARYPENTLvgfrAAVDAGARF----VEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVaeP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  84 NWYSSAFKGERLPLLSEVAERCREH-GLMANIEIKPTtgSDDETG--RVVALAARLLWQGQTDPLLSSFSVEALAAAqRT 160
Cdd:cd08581   77 ARFGSRFAGEPLPSLAAVVQWLAQHpQVTLFVEIKTE--SLDRFGleRVVDKVLRALPAVAAQRVLISFDYDLLALA-KQ 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505189193 161 VPDLPRGLLLEDWDDNWRELTERLDCVSLHIDhKALTAErVKALKDAGLRILVYTVNQPDRARLLLDWGVDCICTDRI 238
Cdd:cd08581  154 QGGPRTGWVLPDWDDASLAEADELQPDYLFCD-KNLLPD-TGDLWAGTWKWVIYEVNEPAEALALAARGVALIETDNI 229
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 8-241 1.60e-26

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: 103.45  E-value: 1.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   8 PHIVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAG---- 83
Cdd:cd08575    1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGygyt 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  84 -----NWYSSAFKGERLPLLSEVAERCrEHGLMaNIEIKpttgsDDETGRVVALAARLL--WQGQTDPLLSSFSVEALAA 156
Cdd:cd08575   81 fdggkTGYPRGGGDGRIPTLEEVFKAF-PDTPI-NIDIK-----SPDAEELIAAVLDLLekYKREDRTVWGSTNPEYLRA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 157 AQRTVPDLP------RGLL----------LEDWDDNWREL--------TERLDCVSLHIDHKAL--TAERVKALKDAGLR 210
Cdd:cd08575  154 LHPENPNLFesfsmtRCLLlylalgytglLPFVPIKESFFeiprpvivLETFTLGEGASIVAALlwWPNLFDHLRKRGIQ 233

                        250       260       270
                 ....*....|....*....|....*....|.
gi 505189193 211 ILVYTVNQPDRARLLLDWGVDCICTDRIDLI 241
Cdd:cd08575  234 VYLWVLNDEEDFEEAFDLGADGVMTDSPTKL 264
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 10-236 7.01e-23

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: 92.75  E-value: 7.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTLA----AIDVGArHGhkmIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDagnw 85
Cdd:cd08568    2 ILGHRGYRAKYPENTLEafkkAIEYGA-DG---VELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLH---- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  86 yssaFKGERLPLLSEVAERCREHGLMaNIEIKpttgsDDETGR-VVALAARLLWQGQTdpLLSSFSVEALAAAQRTVPDL 164
Cdd:cd08568   74 ----PGGELIPTLEEVFRALPNDAII-NVEIK-----DIDAVEpVLEIVEKFNALDRV--IFSSFNHDALRELRKLDPDA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 165 PRGLLLEDWDD--NWRELTERLDCVSLHIDHKAL-------TAERVKALKDAGLRILVYTVNQPDRARLLLDWgVDCICT 235
Cdd:cd08568  142 KVGLLIGEEEEgfSIPELHEKLKLYSLHVPIDAIgyigfekFVELLRLLRKLGLKIVLWTVNDPELVPKLKGL-VDGVIT 220


                 .
gi 505189193 236 D 236
Cdd:cd08568  221 D 221
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 8-237 4.54e-22

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: 91.95  E-value: 4.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   8 PHIVAHRGGGSLAPENTLA----AIDVGArhghKMIEFDAKLAQDGQIFLLHDDTLDRTSN-------------GWGVaG 70
Cdd:cd08559    1 PLVIAHRGASGYAPEHTLAayalAIEMGA----DYIEQDLVMTKDGVLVARHDPTLDRTTNvaehfpfrgrkdtGYFV-I 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  71 ELPWDKLVQLDAGNWYSSAFK--------GERLPLLSEVAERCREHGLMAN------IEIK-PTTGSDDETG---RVVAL 132
Cdd:cd08559   76 DFTLAELKTLRAGSWFNQRYPerapsyygGFKIPTLEEVIELAQGLNKSTGrnvgiyPETKhPTFHKQEGPDieeKLLEV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 133 AARLLWQGQTDPL-LSSFSVEALAAAQRTVPDLPRGLLLedWDDNWRELTERLDC------------------------- 186
Cdd:cd08559  156 LKKYGYTGKNDPVfIQSFEPESLKRLRNETPDIPLVQLI--DYGDWAETDKKYTYawlttdaglkeiakyadgigpwksl 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505189193 187 -VSLHIDHKALTAERVKALKDAGLRILVYTVN----------QPDRARLLLDWGVDCICTDR 237
Cdd:cd08559  234 iIPEDSNGLLVPTDLVKDAHKAGLLVHPYTFRnenlflapdfKQDMDALYNAAGVDGVFTDF 295
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 6-238 4.30e-21

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


Pssm-ID: 176507 [Multi-domain]  Cd Length: 265  Bit Score: 89.07  E-value: 4.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   6 PYPHIVAHRGGGS--LAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLH---DDTLDRTS-----NGWGVAGELPWD 75
Cdd:cd08564    2 VRPIIVGHRGAGCstLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteDDTNPDTSiqlddSGFKNINDLSLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  76 KLVQLDAGNWYSSAF------KGERLPLLSEVAERCREhGLMANIEIKpttGSDDETG-RVVALAARLLWQGQTDplLSS 148
Cdd:cd08564   82 EITRLHFKQLFDEKPcgadeiKGEKIPTLEDVLVTFKD-KLKYNIELK---GREVGLGeRVLNLVEKYGMILQVH--FSS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 149 FS-VEALAAAQRTVPD---LPRGLLLedWDDNWRELTERLDCV------SLHIDHKALTAERVKALKDAGLRILVY-TVN 217
Cdd:cd08564  156 FLhYDRLDLLKALRPNklnVPIALLF--NEVKSPSPLDFLEQAkyynatWVNFSYDFWTEEFVKKAHENGLKVMTYfDEP 233

                        250       260
                 ....*....|....*....|....
gi 505189193 218 QPDRA---RLLLDWGVDCICTDRI 238
Cdd:cd08564  234 VNDNEedyKVYLELGVDCICPNDP 257
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 11-226 9.80e-20

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: 84.68  E-value: 9.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  11 VAHRGGGSLA---PENTLAAIDVGARHGHKmIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGNwys 87
Cdd:cd08585    7 IAHRGLHDRDagiPENSLSAFRAAAEAGYG-IELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRLLG--- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  88 safKGERLPLLSEVAERCrEHGLMANIEIKPTTGSDDETGRVVAlAARLLWQGQTdpLLSSFSVEALAAAQRTVPDLPRG 167
Cdd:cd08585   83 ---TDEHIPTLDEVLELV-AGRVPLLIELKSCGGGDGGLERRVL-AALKDYKGPA--AIMSFDPRVVRWFRKLAPGIPRG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505189193 168 LLLEDWDDN--------------WRELTERLDCVSLHIDH-KALTAERVKALKdaGLRILVYTV-NQPDRARLLL 226
Cdd:cd08585  156 QLSEGSNDEadpafwneallsalFSNLLTRPDFIAYHLDDlPNPFVTLARALL--GMPVIVWTVrTEEDIARLKQ 228
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 10-236 1.63e-17

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: 78.42  E-value: 1.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTsngWGVAGELP----WDKLVQL---DA 82
Cdd:cd08570    1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRC---FGKDGLIIddstWDELSHLrtiEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  83 GNwyssafkgERLPLLSEVAE-----RCREHGLManIEIKPttgsDDETGRVVALAARLL--------WQGQTdpLLSSF 149
Cdd:cd08570   78 PH--------QPMPTLKDVLEwlvehELPDVKLM--LDIKR----DNDPEILFKLIAEMLavkpdldfWRERI--ILGLW 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 150 SVEALAAAQRTVPDLPRGLLLEDWDDNWRELTERLDCVSLHIDHKAL----TAERVKALKDAGLRILVYTVNQPDRARLL 225
Cdd:cd08570  142 HLDFLKYGKEVLPGFPVFHIGFSLDYARHFLNYSEKLVGISMHFVSLwgpfGQAFLPELKKNGKKVFVWTVNTEEDMRYA 221

                        250
                 ....*....|.
gi 505189193 226 LDWGVDCICTD 236
Cdd:cd08570  222 IRLGVDGVITD 232
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 6-236 5.36e-17

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: 78.43  E-value: 5.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   6 PYPHIVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNgwgVAGELP-----------W 74
Cdd:cd08609   25 PKPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTN---VKDVFPgrdaagsnnftW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  75 DKLVQLDAGNWY---------SSAFKGER-------LPLLSEVAERCREHGLMANIEIKPTTGSD-DETGRVVALAARLL 137
Cdd:cd08609  102 TELKTLNAGSWFlerrpfwtlSSLSEEDRreadnqtVPSLSELLDLAKKHNVSIMFDLRNENNSHvFYSSFVFYTLETIL 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 138 WQGQTDPLLSSFSVEALAAAQRTVPDLPrglllEDWDDNWRELTERLDCVSLhiDHKALTAERVKALKDAGLRILVYTVN 217
Cdd:cd08609  182 KLGIPPDKVWWLPDEYRHDVMKMEPGFK-----QVYGRQKEMLMDGGNFMNL--PYQDLSALEIKELRKDNVSVNLWVVN 254

                        250
                 ....*....|....*....
gi 505189193 218 QPDRARLLLDWGVDCICTD 236
Cdd:cd08609  255 EPWLFSLLWCSGVSSVTTN 273
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 5-135 1.03e-16

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: 77.64  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   5 WPYP--HIvAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSngwGVA---GELPWDKL-- 77
Cdd:cd08612   23 SPFPcrHI-SHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSC---GVDklvSDLNYADLpp 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505189193  78 ------VQLDAGNWYSSAFKGERLPLLSEVAERCrEHGLMaNIEIKptTGSDDETGRVVALAAR 135
Cdd:cd08612   99 ylekleVTFSPGDYCVPKGSDRRIPLLEEVFEAF-PDTPI-NIDIK--VENDELIKKVSDLVRK 158
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 8-109 2.31e-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: 73.11  E-value: 2.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   8 PHIVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNgwgVAGELP-----------WDK 76
Cdd:cd08574    2 PALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTN---VADVFPeraherasmftWTD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 505189193  77 LVQLDAGNWYSSA----------------FKGERLPLLSEVAERCREHG 109
Cdd:cd08574   79 LQQLNAGQWFLKDdpfwtasslsesdreeAGNQSIPSLAELLRLAKKHN 127
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 8-101 1.40e-14

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial protein Rv2277c and similar proteins. Members in this subfamily are bacterial homologous of mammalian GDE4, a transmembrane protein whose cellular function has not yet been elucidated.


Pssm-ID: 176522 [Multi-domain]  Cd Length: 263  Bit Score: 71.20  E-value: 1.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   8 PHIVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAG---- 83
Cdd:cd08580    1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAGynfk 80

                         90       100
                 ....*....|....*....|
gi 505189193  84 --NWYSSAFKGERLPLLSEV 101
Cdd:cd08580   81 peGGYPYRGKPVGIPTLEQV 100
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 6-241 1.05e-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: 69.13  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   6 PYPHIVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGV--------AGELPWDKL 77
Cdd:cd08610   21 PKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNIGEVqpesacenPAFFNWDFL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  78 VQLDAGNWYSSA--FKGERlPLLSEVAERCREHGLM--------ANIEIK---------PTTGSDDETGRVVALAARLLW 138
Cdd:cd08610  101 STLNAGKWFVKPrpFYNMK-PLSEADKERARNQSIPklsnflrlAEKENKlvifdlyrpPPKHPYRHTWIRRVLEVILNE 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 139 QGQTDPLLSSFSVEALAAAQRTVPD----LPRGLLLEDwddnwrelTERLDCVSLHIDHKALTAERVKALKDAGLRILVY 214
Cdd:cd08610  180 VGIEQHLVLWLPAHDRQYVQSVAPGfkqhVGRKVPIET--------LLKNNISILNLAYKKLFSNDIRDYKAANIHTNVY 251

                        250       260
                 ....*....|....*....|....*..
gi 505189193 215 TVNQPDRARLLLDWGVDCICTDRIDLI 241
Cdd:cd08610  252 VINEPWLFSLAWCSGIHSVTTNNIHLL 278
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 8-86 8.77e-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: 61.01  E-value: 8.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193   8 PHIVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNgwgVAGELP-----------WDK 76
Cdd:cd08608    2 PAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTN---VDRVFPerqyedasmfnWTD 78

                         90
                 ....*....|
gi 505189193  77 LVQLDAGNWY 86
Cdd:cd08608   79 LERLNAGQWF 88
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 22-131 6.80e-09

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: 55.06  E-value: 6.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  22 ENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAGELPWDKLVQLDAGNWYSS------AFKGE-- 93
Cdd:cd08613   60 ENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELKTLDIGYGYTAdggktfPFRGKgv 139

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 505189193  94 -RLPLLSEVAERCREHGLMANIEIKpttgsDDETGRVVA 131
Cdd:cd08613  140 gMMPTLDEVFAAFPDRRFLINFKSD-----DAAEGELLA 173
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 10-238 1.70e-08

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: 53.82  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRG-GGSLA-------PENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAG----------E 71
Cdd:cd08572    2 VIGHRGlGKNYAsgslagiRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSKTGSDegelievpihD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  72 LPWDKLVQL----------DAGNWYSSAFKGE--------RLPLLSEVAERCREH-GLmaNIEIK-PTTGSDDETGRVVA 131
Cdd:cd08572   82 LTLEQLKELglqhisalkrKALTRKAKGPKPNpwgmdehdPFPTLQEVLEQVPKDlGF--NIEIKyPQLLEDGEGELTPY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 132 LAARL--------LWQ--GQTDPLLSSFSVEA---LAAAQRTVPDlprgLLLEDWDDNWRE----------------LTE 182
Cdd:cd08572  160 FERNAfvdtilavVFEhaGGRRIIFSSFDPDIcimLRLKQNKYPV----LFLTNGGTNEVEhmdprrrslqaavnfaLAE 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 505189193 183 RLDCVSLHIDHKALTAERVKALKDAGLRILVY--TVNQPDRARLLLDWGVDCICTDRI 238
Cdd:cd08572  236 GLLGVVLHAEDLLKNPSLISLVKALGLVLFTYgdDNNDPENVKKQKELGVDGVIYDRV 293
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 10-237 1.79e-07

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: 49.74  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTsngwgvagelpwdklvqldagnwyssa 89
Cdd:cd08555    1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRT--------------------------- 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  90 FKGERLPLLSEVAERCREHGLMA------NIEIKPttgSDDETGRVVALAARLLWQGQTDPLLssfsvealaaaQRTVPD 163
Cdd:cd08555   54 TAGILPPTLEEVLELIADYLKNPdytiilSLEIKQ---DSPEYDEFLAKVLKELRVYFDYDLR-----------GKVVLS 119

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505189193 164 LPRGllLEDWDDNWRELTERLdcvslhidhkaltAERVKALKDAGLRILVYTVN-QPDRARLLLDWGVDCICTDR 237
Cdd:cd08555  120 SFNA--LGVDYYNFSSKLIKD-------------TELIASANKLGLLSRIWTVNdNNEIINKFLNLGVDGLITDF 179
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 10-73 1.46e-06

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


Pssm-ID: 176542 [Multi-domain]  Cd Length: 318  Bit Score: 48.16  E-value: 1.46e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNgwgVAGELP 73
Cdd:cd08600    3 IIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTN---VAEKFP 63
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 11-238 2.35e-06

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: 47.67  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  11 VAHRGGGS-------LAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNGWGVAG----------ELP 73
Cdd:cd08607    3 VGHRGAGNsytaasaVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSDrddllevpvkDLT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  74 WD-----KLVQLDAGNW--YSSAFKGERL------PLLSEVAERCREH-GLmaNIEIK-PT---TGSDDETGRV------ 129
Cdd:cd08607   83 YEqlkllKLFHISALKVkeYKSVEEDEDPpehqpfPTLSDVLESVPEDvGF--NIEIKwPQqqkDGSWESELFTyfdrnl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 130 ---VALAARLLWQGQTDPLLSSFSVEALAAAQRTVPDLPRGLLLEDWDDNWREL----------------TERLDCVSLH 190
Cdd:cd08607  161 fvdIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPEFmdlrtrtfeiavnfaqAEELLGVNLH 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 505189193 191 IDHKALTAERVKALKDAGLRILVY--TVNQPDRARLLLDWGVDCICTDRI 238
Cdd:cd08607  241 SEDLLKDPSQIELAKSLGLVVFCWgdDLNDPENRKKLKELGVDGLIYDRI 290
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 8-64 2.39e-06

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: 47.68  E-value: 2.39e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505189193   8 PHIVAHRGGGSLAPENTLA----AIDVGArhghKMIEFDAKLAQDGQIFLLHDDTLDRTSN 64
Cdd:cd08602    1 PLVIAHRGASGYRPEHTLAayqlAIEQGA----DFIEPDLVSTKDGVLICRHEPELSGTTD 57
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 10-73 2.34e-05

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 44.66  E-value: 2.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505189193  10 IVAHRGGGSLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDDTLDRTSNgwgVAGELP 73
Cdd:PRK11143  29 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTD---VAERFP 89
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 11-236 4.10e-04

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


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 40.36  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  11 VAHRGGG--SLAPENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDdtldrtsngWGVAGELPWDKLVQLDAGNWYSS 88
Cdd:cd08583    2 IAHAMGGidGKTYTNSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHS---------WDESLLKQLGLPTSKNTKPLSYE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193  89 AFK-----GERLPL-LSEVAERCREHglmANIEIKPTTGSDDETgRVVALAARLLWQGQTDP--LLSSFSV----EALAA 156
Cdd:cd08583   73 EFKskkiyGKYTPMdFKDVIDLLKKY---PDVYIVTDTKQDDDN-DIKKLYEYIVKEAKEVDpdLLDRVIPqiynEEMYE 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505189193 157 AQRTVPDLPRGLLL---EDWDDnwreLTERLD-------CVSLhIDHKALTAERVKALKDAGLRILVYTVNQPDRARLLL 226
Cdd:cd08583  149 AIMSIYPFKSVIYTlyrQDSIR----LDEIIAfcyengiKAVT-ISKNYVNDKLIEKLNKAGIYVYVYTINDLKDAQEYK 223

                        250
                 ....*....|
gi 505189193 227 DWGVDCICTD 236
Cdd:cd08583  224 KLGVYGIYTD 233
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 10-57 5.75e-03

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: 37.39  E-value: 5.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505189193  10 IVAHRGGG----SLAP-------ENTLAAIDVGARHGHKMIEFDAKLAQDGQIFLLHDD 57
Cdd:cd08605    2 VIGHRGLGmnraSHQPsvgpgirENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDD 60
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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