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Conserved domains on  [gi|515948746|ref|WP_017379329|]
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glycerophosphodiester phosphodiesterase [Paenisporosarcina sp. TG-14]

Protein Classification

glycerophosphodiester phosphodiesterase( domain architecture ID 10171128)

glycerophosphodiester phosphodiesterase hydrolyzes deacylated phospholipids to glycerol 3-phosphate and the corresponding alcohols

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
44-297 9.95e-102

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: 298.02  E-value: 9.95e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  44 ILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQFVND 123
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 124 H-QEFEYRGQGETVITLRELFEEFPQMLINIDMKDSPETyegslIPSKLWRLIEELNVQNRIVVTSFYDEQIDRFNLYAQ 202
Cdd:cd08561   81 GgRTYPYRGQGIRIPTLEELFEAFPDVRLNIEIKDDGPA-----AAAALADLIERYGAQDRVLVASFSDRVLRRFRRLCP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 203 nSVALGAGVKEVRKAYSAFTSQFGHLYHPRADVVQIPVKSGVFPLDSEGFINFLTNLNVSVHYWTINDSQTIERLLQLGA 282
Cdd:cd08561  156 -RVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLGV 234
                        250
                 ....*....|....*
gi 515948746 283 KGIITDRPDLALSLL 297
Cdd:cd08561  235 DGIITDRPDLLLEVL 249
 
Name Accession Description Interval E-value
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
44-297 9.95e-102

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: 298.02  E-value: 9.95e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  44 ILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQFVND 123
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 124 H-QEFEYRGQGETVITLRELFEEFPQMLINIDMKDSPETyegslIPSKLWRLIEELNVQNRIVVTSFYDEQIDRFNLYAQ 202
Cdd:cd08561   81 GgRTYPYRGQGIRIPTLEELFEAFPDVRLNIEIKDDGPA-----AAAALADLIERYGAQDRVLVASFSDRVLRRFRRLCP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 203 nSVALGAGVKEVRKAYSAFTSQFGHLYHPRADVVQIPVKSGVFPLDSEGFINFLTNLNVSVHYWTINDSQTIERLLQLGA 282
Cdd:cd08561  156 -RVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLGV 234
                        250
                 ....*....|....*
gi 515948746 283 KGIITDRPDLALSLL 297
Cdd:cd08561  235 DGIITDRPDLLLEVL 249
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
40-297 5.96e-77

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 234.38  E-value: 5.96e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  40 EHPIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQ 119
Cdd:COG0584    1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 120 fvndhqefeYRGQGETVITLRELFEEFP-QMLINIDMKDSPETYEGslIPSKLWRLIEELNVQNRIVVTSFYDEQIDRFN 198
Cdd:COG0584   81 ---------PDFAGERIPTLEEVLELVPgDVGLNIEIKSPPAAEPD--LAEAVAALLKRYGLEDRVIVSSFDPEALRRLR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 199 LYAQNsVALGAGVKEVRKAYSAFTSQFG-HLYHPRADVVqipvksgvfpldSEGFINFLTNLNVSVHYWTINDSQTIERL 277
Cdd:COG0584  150 ELAPD-VPLGLLVEELPADPLELARALGaDGVGPDYDLL------------TPELVAAAHAAGLKVHVWTVNDPEEMRRL 216
                        250       260
                 ....*....|....*....|
gi 515948746 278 LQLGAKGIITDRPDLALSLL 297
Cdd:COG0584  217 LDLGVDGIITDRPDLLRAVL 236
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
47-292 6.63e-32

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: 118.66  E-value: 6.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746   47 HRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQFVNdhqe 126
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSG---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  127 fEYRGQGETVITLRELFEEFPQM--LINIDMKDSPEtyegslIPSKLWRLIEELNVQ-NRIVVTSFYDEQ---IDRFNLY 200
Cdd:pfam03009  77 -PLSGERVPFPTLEEVLEFDWDVgfNIEIKIKPYVE------AIAPEEGLIVKDLLLsVDEILAKKADPRrviFSSFNPD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  201 AQNSVALGAGVKEVRKAYSAFTSQFGHLYHPRADVVQIPVKSGVFPL---DSEGFINFLTNLNVSVHYWTINDSQTIERL 277
Cdd:pfam03009 150 ELKRLRELAPKLPLVFLSSGRAYAEADLLERAAAFAGAPALLGEVALvdeALPDLVKRAHARGLVVHVWTVNNEDEMKRL 229
                         250
                  ....*....|....*
gi 515948746  278 LQLGAKGIITDRPDL 292
Cdd:pfam03009 230 LELGVDGVITDRPDT 244
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
42-292 1.17e-22

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 94.24  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQFv 121
Cdd:PRK09454   8 PRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWF- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 122 ndHQEFeyrgQGETVITLRELFEEFPQ--MLINIDMKDSP--ETYEGSLIP---SKLWRlieelNVQNRIVVTSFYDEQI 194
Cdd:PRK09454  87 --SAAF----AGEPLPTLSQVAARCRAhgMAANIEIKPTTgrEAETGRVVAlaaRALWA-----GAAVPPLLSSFSEDAL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 195 DRfnlyAQNSV-ALGAG--VKEVRKAYSAFTSQFG----HLYHPRADvvqipvksgvfpldsEGFINFLTNLNVSVHYWT 267
Cdd:PRK09454 156 EA----ARQAApELPRGllLDEWPDDWLELTRRLGcvslHLNHKLLD---------------EARVAALKAAGLRILVYT 216
                        250       260
                 ....*....|....*....|....*
gi 515948746 268 INDSQTIERLLQLGAKGIITDRPDL 292
Cdd:PRK09454 217 VNDPARARELLRWGVDCICTDRIDL 241
 
Name Accession Description Interval E-value
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
44-297 9.95e-102

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: 298.02  E-value: 9.95e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  44 ILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQFVND 123
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 124 H-QEFEYRGQGETVITLRELFEEFPQMLINIDMKDSPETyegslIPSKLWRLIEELNVQNRIVVTSFYDEQIDRFNLYAQ 202
Cdd:cd08561   81 GgRTYPYRGQGIRIPTLEELFEAFPDVRLNIEIKDDGPA-----AAAALADLIERYGAQDRVLVASFSDRVLRRFRRLCP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 203 nSVALGAGVKEVRKAYSAFTSQFGHLYHPRADVVQIPVKSGVFPLDSEGFINFLTNLNVSVHYWTINDSQTIERLLQLGA 282
Cdd:cd08561  156 -RVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLGV 234
                        250
                 ....*....|....*
gi 515948746 283 KGIITDRPDLALSLL 297
Cdd:cd08561  235 DGIITDRPDLLLEVL 249
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
40-297 5.96e-77

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 234.38  E-value: 5.96e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  40 EHPIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQ 119
Cdd:COG0584    1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 120 fvndhqefeYRGQGETVITLRELFEEFP-QMLINIDMKDSPETYEGslIPSKLWRLIEELNVQNRIVVTSFYDEQIDRFN 198
Cdd:COG0584   81 ---------PDFAGERIPTLEEVLELVPgDVGLNIEIKSPPAAEPD--LAEAVAALLKRYGLEDRVIVSSFDPEALRRLR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 199 LYAQNsVALGAGVKEVRKAYSAFTSQFG-HLYHPRADVVqipvksgvfpldSEGFINFLTNLNVSVHYWTINDSQTIERL 277
Cdd:COG0584  150 ELAPD-VPLGLLVEELPADPLELARALGaDGVGPDYDLL------------TPELVAAAHAAGLKVHVWTVNDPEEMRRL 216
                        250       260
                 ....*....|....*....|
gi 515948746 278 LQLGAKGIITDRPDLALSLL 297
Cdd:COG0584  217 LDLGVDGIITDRPDLLRAVL 236
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
42-290 3.48e-56

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: 181.22  E-value: 3.48e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYqfv 121
Cdd:cd08563    1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGS--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 122 ndhqEFEYRGQGETVITLRELFEEFPQ--MLINIDMKDSPETYEGslIPSKLWRLIEELNVQNRIVVTSFYDEQIDRfnL 199
Cdd:cd08563   78 ----WFDEKFTGEKIPTLEEVLDLLKDkdLLLNIEIKTDVIHYPG--IEKKVLELVKEYNLEDRVIFSSFNHESLKR--L 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 200 YA-QNSVALGAGVKEVRKAYSAFTSQFGHL-YHPRadvvqipvksgvFPLDSEGFINFLTNLNVSVHYWTINDSQTIERL 277
Cdd:cd08563  150 KKlDPKIKLALLYETGLQDPKDYAKKIGADsLHPD------------FKLLTEEVVEELKKRGIPVRLWTVNEEEDMKRL 217
                        250
                 ....*....|...
gi 515948746 278 LQLGAKGIITDRP 290
Cdd:cd08563  218 KDLGVDGIITNYP 230
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
42-293 2.06e-54

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: 177.79  E-value: 2.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQFV 121
Cdd:cd08575    1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 122 NDHQEFEY-RGQGETVI-TLRELFEEFPQMLINIDMKdSPETYEgsLIpSKLWRLIEELNVQNRIVVTSFYDEQIDRFNL 199
Cdd:cd08575   81 FDGGKTGYpRGGGDGRIpTLEEVFKAFPDTPINIDIK-SPDAEE--LI-AAVLDLLEKYKREDRTVWGSTNPEYLRALHP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 200 YAQNsVALGAGVKEVRKAYSAFtsqFGHLYHP----RADVVQIPVKSGVFPLDSEGFINFLTNL--------------NV 261
Cdd:cd08575  157 ENPN-LFESFSMTRCLLLYLAL---GYTGLLPfvpiKESFFEIPRPVIVLETFTLGEGASIVAAllwwpnlfdhlrkrGI 232
                        250       260       270
                 ....*....|....*....|....*....|..
gi 515948746 262 SVHYWTINDSQTIERLLQLGAKGIITDRPDLA 293
Cdd:cd08575  233 QVYLWVLNDEEDFEEAFDLGADGVMTDSPTKL 264
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
43-290 1.61e-39

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: 138.59  E-value: 1.61e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  43 IILAHRGGSL-IAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQFv 121
Cdd:cd08566    1 LVVAHRGGWGaGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKDGD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 122 ndhqefeYRGQGETVITLRELFEEFPQ-MLINIDMKDSPetyegsliPSKLWRLIEELNVQNRIVVTSFYDEQIDRFNLY 200
Cdd:cd08566   80 -------GEVTDEKVPTLEEALAWAKGkILLNLDLKDAD--------LDEVIALVKKHGALDQVIFKSYSEEQAKELRAL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 201 AQN-----SVALGAGVKEVRKAY------SAFTSQFGHLYHPRAdVVQIPVKSGVfpldsEGFINFLTNLNVSVH-YWTI 268
Cdd:cd08566  145 APEvmlmpIVRDAEDLDEEEARAidalnlLAFEITFDDLDLPPL-FDELLRALGI-----RVWVNTLGDDDTAGLdRALS 218
                        250       260
                 ....*....|....*....|..
gi 515948746 269 NDSQTIERLLQLGAKGIITDRP 290
Cdd:cd08566  219 DPREVWGELVDAGVDVIQTDRP 240
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
44-290 2.00e-39

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: 137.74  E-value: 2.00e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  44 ILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQFVnd 123
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFS-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 124 hQEFeyrgQGETVITLRELFEEFP--QMLINIDMKDSPETyeGSLIPSKLWRLIEELNVQN-RIVVTSFydeqidrfnly 200
Cdd:cd08562   79 -PEF----AGEPIPTLADVLELARelGLGLNLEIKPDPGD--EALTARVVAAALRELWPHAsKLLLSSF----------- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 201 aqNSVALgagvKEVRKAYSAFtsQFGHLYH-----PRADVVQIPVKSgVFPLDS---EGFINFLTNLNVSVHYWTINDSQ 272
Cdd:cd08562  141 --SLEAL----RAARRAAPEL--PLGLLFDtlpadWLELLAALGAVS-IHLNYRgltEEQVKALKDAGYKLLVYTVNDPA 211
                        250
                 ....*....|....*...
gi 515948746 273 TIERLLQLGAKGIITDRP 290
Cdd:cd08562  212 RAAELLEWGVDAIFTDRP 229
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
44-294 5.23e-39

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: 137.15  E-value: 5.23e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  44 ILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYqfvnd 123
Cdd:cd08565    1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLRD----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 124 hqefeyrGQGETVITLRELFEEF--PQMLINIDMKDSP--ETYEGslIPSKLWRLIEELNVQNRIVVTSFYDEQIDRFNL 199
Cdd:cd08565   76 -------SFGEKIPTLEEVLALFapSGLELHVEIKTDAdgTPYPG--AAALAAATLRRHGLLERSVLTSFDPAVLTEVRK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 200 YAQNSVALGAGVKEVRKAySAFTSQFGHLYHPrADVVQIPVKsgVFPLDSEGFINFLTNLNVSVhyWTINDSQTIERLLQ 279
Cdd:cd08565  147 HPGVRTLGSVDEDMLERL-GGELPFLTATALK-AHIVAVEQS--LLAATWELVRAAVPGLRLGV--WTVNDDSLIRYWLA 220
                        250
                 ....*....|....*
gi 515948746 280 LGAKGIITDRPDLAL 294
Cdd:cd08565  221 CGVRQLTTDRPDLAL 235
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
44-292 3.09e-38

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: 135.13  E-value: 3.09e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  44 ILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQFVND 123
Cdd:cd08582    1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGSWKGES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 124 HqefeyrgQGETVITLRELFEEFPQ--MLINIDMKdsPETYEGSLIPSkLWRLIEELNV-QNRIVVTSFYDEQIdrfnly 200
Cdd:cd08582   81 Y-------KGEKVPTLEEYLAIVPKygKKLFIEIK--HPRRGPEAEEE-LLKLLKESGLlPEQIVIISFDAEAL------ 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 201 aqnsvalgagvKEVRKAYSAFTSQF-----GHLYHPRADVVQIpVKSGV-----FPLDSEgFINFLTNLNVSVHYWTIND 270
Cdd:cd08582  145 -----------KRVRELAPTLETLWlrnykSPKEDPRPLAKSG-GAAGLdlsyeKKLNPA-FIKALRDAGLKLNVWTVDD 211
                        250       260
                 ....*....|....*....|..
gi 515948746 271 SQTIERLLQLGAKGIITDRPDL 292
Cdd:cd08582  212 AEDAKRLIELGVDSITTNRPGR 233
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
44-289 5.60e-37

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: 130.46  E-value: 5.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  44 ILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDeyvdrttdgsgrvadltlselkafdlgyqfvnd 123
Cdd:cd08556    1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 124 hqefeyrgqgetVITLRELFEEFPQ-MLINIDMKDSPETYEgslIPSKLWRLIEELNVQNRIVVTSFYDEQIDRFNLYAQ 202
Cdd:cd08556   48 ------------IPTLEEVLELVKGgVGLNIELKEPTRYPG---LEAKVAELLREYGLEERVVVSSFDHEALRALKELDP 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 203 NsVALGAGVkevrkaYSAFTSQFGHLYHPRADVVQIPVKsgvFPLDSEGFINFLTNLNVSVHYWTINDSQTIERLLQLGA 282
Cdd:cd08556  113 E-VPTGLLV------DKPPLDPLLAELARALGADAVNPH---YKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGV 182

                 ....*..
gi 515948746 283 KGIITDR 289
Cdd:cd08556  183 DGIITDD 189
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
46-290 7.70e-37

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: 133.11  E-value: 7.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  46 AHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAF--DLGYQFVND 123
Cdd:cd08612   31 SHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLPPYleKLEVTFSPG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 124 HQEFEyRGQGETVITLRELFEEFPQMLINIDMKdspetYEGSLIPSKLWRLIEELNVQNRIVVTSFYDEQIDRfnLYAQN 203
Cdd:cd08612  111 DYCVP-KGSDRRIPLLEEVFEAFPDTPINIDIK-----VENDELIKKVSDLVRKYKREDITVWGSFNDEIVKK--CHKEN 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 204 -SVALGAGVKEVRKAYSAFTSQFGHLYHPRADVVQIPVKSGVFPLD-------SEGFINFLTNL--------------NV 261
Cdd:cd08612  183 pNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYfpksmsrLNRFVLFLIDWllmrpslfrhlqkrGI 262
                        250       260
                 ....*....|....*....|....*....
gi 515948746 262 SVHYWTINDSQTIERLLQLGAKGIITDRP 290
Cdd:cd08612  263 QVYGWVLNDEEEFERAFELGADGVMTDYP 291
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
43-290 2.48e-32

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: 119.33  E-value: 2.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  43 IILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGyqfvn 122
Cdd:cd08568    1 IILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHPG----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 123 dhqefeyrgqGETVITLRELFEEFPQM-LINIDMKDsPETYEGSLipsklwRLIEELNVQNRIVVTSFYDEQIDRFNLYA 201
Cdd:cd08568   76 ----------GELIPTLEEVFRALPNDaIINVEIKD-IDAVEPVL------EIVEKFNALDRVIFSSFNHDALRELRKLD 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 202 QNSvALGAGVKEVRKAYSAFTSQFGH-LYHpradvVQIPVKsGVFPLDSEGFINFLT---NLNVSVHYWTINDSQTIERL 277
Cdd:cd08568  139 PDA-KVGLLIGEEEEGFSIPELHEKLkLYS-----LHVPID-AIGYIGFEKFVELLRllrKLGLKIVLWTVNDPELVPKL 211
                        250
                 ....*....|...
gi 515948746 278 LQLgAKGIITDRP 290
Cdd:cd08568  212 KGL-VDGVITDDV 223
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
47-292 6.63e-32

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: 118.66  E-value: 6.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746   47 HRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQFVNdhqe 126
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSG---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  127 fEYRGQGETVITLRELFEEFPQM--LINIDMKDSPEtyegslIPSKLWRLIEELNVQ-NRIVVTSFYDEQ---IDRFNLY 200
Cdd:pfam03009  77 -PLSGERVPFPTLEEVLEFDWDVgfNIEIKIKPYVE------AIAPEEGLIVKDLLLsVDEILAKKADPRrviFSSFNPD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  201 AQNSVALGAGVKEVRKAYSAFTSQFGHLYHPRADVVQIPVKSGVFPL---DSEGFINFLTNLNVSVHYWTINDSQTIERL 277
Cdd:pfam03009 150 ELKRLRELAPKLPLVFLSSGRAYAEADLLERAAAFAGAPALLGEVALvdeALPDLVKRAHARGLVVHVWTVNNEDEMKRL 229
                         250
                  ....*....|....*
gi 515948746  278 LQLGAKGIITDRPDL 292
Cdd:pfam03009 230 LELGVDGVITDRPDT 244
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
42-297 1.87e-31

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: 117.80  E-value: 1.87e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGS--GRVADLTLSELKAFDLGYQ 119
Cdd:cd08601    1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIErpGPVKDYTLAEIKQLDAGSW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 120 FVNDHQEF---EYRGQgeTVITLRELFEEF-PQMLINIDMKdSPETYEGslIPSKLWRLIEELNVQN------RIVVTSF 189
Cdd:cd08601   81 FNKAYPEYareSYSGL--KVPTLEEVIERYgGRANYYIETK-SPDLYPG--MEEKLLATLDKYGLLTdnlkngQVIIQSF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 190 YDEQIDRfnLYAQNS----VALgAGVKEVRKAYSAFTsQFGHLYhprADVVqipvkSGVFPLDSEGFINFLTNLNVSVHY 265
Cdd:cd08601  156 SKESLKK--LHQLNPniplVQL-LWYGEGAETYDKWL-DEIKEY---AIGI-----GPSIADADPWMVHLIHKKGLLVHP 223
                        250       260       270
                 ....*....|....*....|....*....|..
gi 515948746 266 WTINDSQTIERLLQLGAKGIITDRPDLALSLL 297
Cdd:cd08601  224 YTVNEKADMIRLINWGVDGMFTNYPDRLKEVL 255
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
46-292 1.66e-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: 115.49  E-value: 1.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  46 AHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYV--DRTTDGSGR--------VADLTLSELKAFD 115
Cdd:cd08567    5 GHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLnpDITRDPDGAwlpyegpaLYELTLAEIKQLD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 116 LGYQFVNDHQEFEYRGQ----GETVITLRELFEEFP-----QMLINIDMKDSPE----TYEGSLIPSKLWRLIEELNVQN 182
Cdd:cd08567   85 VGEKRPGSDYAKLFPEQipvpGTRIPTLEEVFALVEkygnqKVRFNIETKSDPDrdilHPPPEEFVDAVLAVIRKAGLED 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 183 RIVVTSFYDEqidrfnlyaqnsvALgagvKEVRKAY-----SAFTSQfghlyHPRADVVQIPVKSG------VFPLDSEG 251
Cdd:cd08567  165 RVVLQSFDWR-------------TL----QEVRRLApdiptVALTEE-----TTLGNLPRAAKKLGadiwspYFTLVTKE 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 515948746 252 FINFLTNLNVSVHYWTINDSQTIERLLQLGAKGIITDRPDL 292
Cdd:cd08567  223 LVDEAHALGLKVVPWTVNDPEDMARLIDLGVDGIITDYPDL 263
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
42-202 6.72e-27

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: 105.87  E-value: 6.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQFV 121
Cdd:cd08580    1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAGYNFK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 122 NDHQEFeYRGQGETVITLRELFEEFPQMLINIDMKDSPetyeGSLIPSKLWRLIEELNVQNRIVVTSFYDEQIDRFNLYA 201
Cdd:cd08580   81 PEGGYP-YRGKPVGIPTLEQVLRAFPDTPFILDMKSLP----ADPQAKAVARVLERENAWSRVRIYSTNADYQDALAPYP 155

                 .
gi 515948746 202 Q 202
Cdd:cd08580  156 Q 156
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
44-290 8.77e-27

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: 104.55  E-value: 8.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  44 ILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLgyqfvnd 123
Cdd:cd08579    1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTI------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 124 HQEfeyrGQGETVITLRELFEEFPQMLI--NIDMKDSPeTYEGSLIpSKLWRLIEELNVQNRIVVTSFyDEQIdrfnlya 201
Cdd:cd08579   74 GEN----GHGAKIPSLDEYLALAKGLKQklLIELKPHG-HDSPDLV-EKFVKLYKQNLIENQHQVHSL-DYRV------- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 202 qnsvalgagVKEVRKAY-SAFTS-----QFGHLYHPRADVVQIPvksgVFPLDSEgFINFLTNLNVSVHYWTINDSQTIE 275
Cdd:cd08579  140 ---------IEKVKKLDpKIKTGyilpfNIGNLPKTNVDFYSIE----YSTLNKE-FIRQAHQNGKKVYVWTVNDPDDMQ 205
                        250
                 ....*....|....*
gi 515948746 276 RLLQLGAKGIITDRP 290
Cdd:cd08579  206 RYLAMGVDGIITDYP 220
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
44-190 1.14e-26

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: 105.03  E-value: 1.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  44 ILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQFvND 123
Cdd:cd08573    1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKH-RL 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 124 HQEFeyrgQGETVITLRELFEEFPQ--MLINIDMKDSPETYEGSLIPsklwrLIEELN-VQNRIVVTSFY 190
Cdd:cd08573   80 SSRF----PGEKIPTLEEAVKECLEnnLRMIFDVKSNSSKLVDALKN-----LFKKYPgLYDKAIVCSFN 140
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
42-292 1.17e-22

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 94.24  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLGYQFv 121
Cdd:PRK09454   8 PRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWF- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 122 ndHQEFeyrgQGETVITLRELFEEFPQ--MLINIDMKDSP--ETYEGSLIP---SKLWRlieelNVQNRIVVTSFYDEQI 194
Cdd:PRK09454  87 --SAAF----AGEPLPTLSQVAARCRAhgMAANIEIKPTTgrEAETGRVVAlaaRALWA-----GAAVPPLLSSFSEDAL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 195 DRfnlyAQNSV-ALGAG--VKEVRKAYSAFTSQFG----HLYHPRADvvqipvksgvfpldsEGFINFLTNLNVSVHYWT 267
Cdd:PRK09454 156 EA----ARQAApELPRGllLDEWPDDWLELTRRLGcvslHLNHKLLD---------------EARVAALKAAGLRILVYT 216
                        250       260
                 ....*....|....*....|....*
gi 515948746 268 INDSQTIERLLQLGAKGIITDRPDL 292
Cdd:PRK09454 217 VNDPARARELLRWGVDCICTDRIDL 241
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
42-297 4.50e-22

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: 92.92  E-value: 4.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRGG--SLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFH--DEYVDRTT------DGSGRVADLTLSEL 111
Cdd:cd08564    4 PIIVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgtEDDTNPDTsiqlddSGFKNINDLSLDEI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 112 KAFDlgyqfVNDHQE----FEYRGQGETVITLRELFEEF-PQMLINIDMKDSP-ETYEGSLipsklwRLIEELNVQNRIV 185
Cdd:cd08564   84 TRLH-----FKQLFDekpcGADEIKGEKIPTLEDVLVTFkDKLKYNIELKGREvGLGERVL------NLVEKYGMILQVH 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 186 VTSFY-DEQIDRFNLYAQNSVALgagvkevrkaysaftsQFGHL--YHPRADVVQI----------PVkSGVFPLDSEGF 252
Cdd:cd08564  153 FSSFLhYDRLDLLKALRPNKLNV----------------PIALLfnEVKSPSPLDFleqakyynatWV-NFSYDFWTEEF 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 515948746 253 INFLTNLNVSVH-YWT---INDSQTIERLLQLGAKGIITDRPDLALSLL 297
Cdd:cd08564  216 VKKAHENGLKVMtYFDepvNDNEEDYKVYLELGVDCICPNDPVLLVNFL 264
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
42-197 4.52e-22

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: 93.58  E-value: 4.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRG----------------GSLIAP------ENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDG 99
Cdd:cd08613   24 PKLLAHRGlaqtfdregvendtctAERIDPpthdylENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 100 SGRVADLTLSELKAFDLGYQFVNDHQE-FEYRGQGETVI-TLRELFEEFP--QMLINIDMKDSPetyEGSLIPSKLWRLI 175
Cdd:cd08613  104 SGVTRDHTMAELKTLDIGYGYTADGGKtFPFRGKGVGMMpTLDEVFAAFPdrRFLINFKSDDAA---EGELLAEKLATLP 180
                        170       180
                 ....*....|....*....|....
gi 515948746 176 EElnvqnRIVVTSFY--DEQIDRF 197
Cdd:cd08613  181 RK-----RLQVLTVYggDKPIAAL 199
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
41-166 2.47e-19

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: 2.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  41 HPIilAHRG---GSLIAPENSMVAFKKSAELGVhGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFDLG 117
Cdd:cd08585    5 RPI--AHRGlhdRDAGIPENSLSAFRAAAEAGY-GIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRLL 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515948746 118 yqfvndhqefeyrGQGETVITLRELFEEFPQ--MLInIDMKdSPETYEGSL 166
Cdd:cd08585   82 -------------GTDEHIPTLDEVLELVAGrvPLL-IELK-SCGGGDGGL 117
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
42-144 7.45e-19

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: 84.63  E-value: 7.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTD------------GSGRVADLTLS 109
Cdd:cd08559    1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNvaehfpfrgrkdTGYFVIDFTLA 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 515948746 110 ELKAFDLGYQFVndhQEFEYRGQ----GETVITLRELFE 144
Cdd:cd08559   81 ELKTLRAGSWFN---QRYPERAPsyygGFKIPTLEEVIE 116
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
44-290 3.09e-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: 78.80  E-value: 3.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  44 ILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLT----LSELKAFDLGYQ 119
Cdd:cd08570    1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDStwdeLSHLRTIEEPHQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 120 FvndhqefeyrgqgetVITLRELFEEF-----PQMLINIDMK-DSPetyegsliPSKLWRLI-EELNVQN-------RIV 185
Cdd:cd08570   81 P---------------MPTLKDVLEWLvehelPDVKLMLDIKrDND--------PEILFKLIaEMLAVKPdldfwreRII 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 186 V----TSFYD------EQIDRFN-----LYAQNSVALGAGVKEVRKAYSAFTSQFGHlyhpradvvqipvksgvfpldse 250
Cdd:cd08570  138 LglwhLDFLKygkevlPGFPVFHigfslDYARHFLNYSEKLVGISMHFVSLWGPFGQ----------------------- 194
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 515948746 251 GFINFLTNLNVSVHYWTINDSQTIERLLQLGAKGIITDRP 290
Cdd:cd08570  195 AFLPELKKNGKKVFVWTVNTEEDMRYAIRLGVDGVITDDP 234
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
44-290 4.50e-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 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: 78.53  E-value: 4.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  44 ILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGRVADLTLSELKAFdlgyqFVND 123
Cdd:cd08581    1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSL-----RVAE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 124 HQEFEYRGQGETVITLRELFE---EFPQMLINIDMK-DSPETYEGSLIPSKLWRLIEELNVQnrIVVTSFYDEQIDRfnL 199
Cdd:cd08581   76 PARFGSRFAGEPLPSLAAVVQwlaQHPQVTLFVEIKtESLDRFGLERVVDKVLRALPAVAAQ--RVLISFDYDLLAL--A 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 200 YAQNSVALGAGVKEVRKAYSAFTSQFGHLYHpRADVVQIPVKSGVFPLDSEGFInfltnlnvsvhyWTINDSQTIERLLQ 279
Cdd:cd08581  152 KQQGGPRTGWVLPDWDDASLAEADELQPDYL-FCDKNLLPDTGDLWAGTWKWVI------------YEVNEPAEALALAA 218
                        250
                 ....*....|.
gi 515948746 280 LGAKGIITDRP 290
Cdd:cd08581  219 RGVALIETDNI 229
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
44-289 5.96e-17

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: 77.09  E-value: 5.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  44 ILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSgrvADLTLSELKAFDLGYQFVND 123
Cdd:cd08555    1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGI---LPPTLEEVLELIADYLKNPD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 124 hqefeyrgqgETVItlrelfeefpqmlINIDMKdspetYEGSLIPSKLWRLIEELNVQ------NRIVVTSFYDEQIDRF 197
Cdd:cd08555   78 ----------YTII-------------LSLEIK-----QDSPEYDEFLAKVLKELRVYfdydlrGKVVLSSFNALGVDYY 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 198 NLYAQNSVaLGAGVKEVRKaysaftsqfghlyhpradvvqipvksgvfpldsegfinfltnLNVSVHYWTINDS-QTIER 276
Cdd:cd08555  130 NFSSKLIK-DTELIASANK------------------------------------------LGLLSRIWTVNDNnEIINK 166
                        250
                 ....*....|...
gi 515948746 277 LLQLGAKGIITDR 289
Cdd:cd08555  167 FLNLGVDGLITDF 179
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
42-162 3.67e-13

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: 68.80  E-value: 3.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGS----GRVA----DLTLSELKA 113
Cdd:cd08609   27 PALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKdvfpGRDAagsnNFTWTELKT 106
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 114 FDLGYQFVNDH---------QEFEYRGQGETVITLRELFEEFPQMLINI--DMKDSPETY 162
Cdd:cd08609  107 LNAGSWFLERRpfwtlsslsEEDRREADNQTVPSLSELLDLAKKHNVSImfDLRNENNSH 166
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
42-98 1.85e-11

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: 63.09  E-value: 1.85e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTD 98
Cdd:cd08574    2 PALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTN 58
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
42-112 2.67e-11

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: 63.18  E-value: 2.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTT------------DGSGRVADLTLS 109
Cdd:cd08600    1 KIIIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTnvaekfpdrkrkDGRYYVIDFTLD 80

                 ...
gi 515948746 110 ELK 112
Cdd:cd08600   81 ELK 83
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
42-112 1.38e-09

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: 58.08  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGSGR------------------- 102
Cdd:cd08602    1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHpefadrkttktvdgvnvtg 80
                         90
                 ....*....|..
gi 515948746 103 --VADLTLSELK 112
Cdd:cd08602   81 wfTEDFTLAELK 92
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
42-112 3.05e-09

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 57.38  E-value: 3.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTDGS----------GR--VADLTLS 109
Cdd:PRK11143  27 KIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAerfpdrarkdGRyyAIDFTLD 106

                 ...
gi 515948746 110 ELK 112
Cdd:PRK11143 107 EIK 109
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
42-98 3.50e-09

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: 56.81  E-value: 3.50e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTD 98
Cdd:cd08610   23 PTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTN 79
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
57-288 1.09e-06

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: 48.84  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  57 NSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYvdrttdgsgrvaDLTLSELKAFDLGYQFVNDHQEFE---YRGQG 133
Cdd:cd08583   16 NSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHSWD------------ESLLKQLGLPTSKNTKPLSYEEFKskkIYGKY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 134 ETV--ITLRELFEEFPQMLINIDMKDSpETYEGSLIPSKLWRLIEELN--VQNRIVVTSFYDEQIDR-FNLYAQNSVALG 208
Cdd:cd08583   84 TPMdfKDVIDLLKKYPDVYIVTDTKQD-DDNDIKKLYEYIVKEAKEVDpdLLDRVIPQIYNEEMYEAiMSIYPFKSVIYT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 209 AGVKEVRKAYS--AFTSQFGHlyhpraDVVQIPVKSgvfplDSEGFINFLTNLNVSVHYWTINDSQTIERLLQLGAKGII 286
Cdd:cd08583  163 LYRQDSIRLDEiiAFCYENGI------KAVTISKNY-----VNDKLIEKLNKAGIYVYVYTINDLKDAQEYKKLGVYGIY 231

                 ..
gi 515948746 287 TD 288
Cdd:cd08583  232 TD 233
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
42-98 1.12e-06

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: 49.46  E-value: 1.12e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515948746  42 PIILAHRGGSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRTTD 98
Cdd:cd08608    2 PAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTN 58
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
56-163 1.32e-06

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


Pssm-ID: 176547 [Multi-domain]  Cd Length: 282  Bit Score: 48.95  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  56 ENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYV---DRTTDGSGRVADLTLSELKAfdLGYQFVN--DHQEFEYR 130
Cdd:cd08605   25 ENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIvveRGGEVESSRIRDLTLAELKA--LGPQAEStkTSTVALYR 102
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 515948746 131 GQGETVI------------TLRELFEEFPQML-INIDMK-DSPETYE 163
Cdd:cd08605  103 KAKDPEPepwimdvedsipTLEEVFSEVPPSLgFNIELKfGDDNKTE 149
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
47-289 2.97e-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: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  47 HRG-------GSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDeYVDRTTD----GSGR-------VADLTL 108
Cdd:cd08607    5 HRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHD-FTLRVSLkskgDSDRddllevpVKDLTY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 109 SELKAFDLGYQFVNDHQEFEYRGQGETVI------TLRELFEEFPQML-INIDMK------------DSPETYEGSLIPS 169
Cdd:cd08607   84 EQLKLLKLFHISALKVKEYKSVEEDEDPPehqpfpTLSDVLESVPEDVgFNIEIKwpqqqkdgswesELFTYFDRNLFVD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746 170 KLWRLIEELNVQNRIVVTSFyDEQIDRFNLYAQNS---VALGAGVkevrkaysafTSQFGHLYHPRADVVQIPVKS---- 242
Cdd:cd08607  164 IILKIVLEHAGKRRIIFSSF-DADICTMLRFKQNKypvLFLTQGK----------TQRYPEFMDLRTRTFEIAVNFaqae 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515948746 243 ---GVFPLDSE-----GFINFLTNLNVSVHYW--TINDSQTIERLLQLGAKGIITDR 289
Cdd:cd08607  233 ellGVNLHSEDllkdpSQIELAKSLGLVVFCWgdDLNDPENRKKLKELGVDGLIYDR 289
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
47-156 9.11e-06

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: 46.50  E-value: 9.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  47 HRG--------GSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYV-----DRTTDGSG-----RVADLTL 108
Cdd:cd08572    5 HRGlgknyasgSLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTIsvsekSKTGSDEGelievPIHDLTL 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515948746 109 SELKAFDLgYQFVNDHQEFEYRGQGETVI------------TLRELFEEFPQML-INIDMK 156
Cdd:cd08572   85 EQLKELGL-QHISALKRKALTRKAKGPKPnpwgmdehdpfpTLQEVLEQVPKDLgFNIEIK 144
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
42-156 4.24e-05

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: 44.36  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515948746  42 PIILAHRG--------GSLIAPENSMVAFKKSAELGVHGFEIDIRLTKNEEIIVFHDEYVDRT-TDGSgrVADLTLSELk 112
Cdd:cd08606    2 VQVIGHRGlgkntaerKSLQLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETgTDVP--IHDLTLEQF- 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515948746 113 afdLGYQFVNDHQEFEYRG-----QGETV----ITLRELFEEFPQML-INIDMK 156
Cdd:cd08606   79 ---LHLSRMKYTVDFKKKGfkgnsRGHSIqapfTTLEELLKKLPKSVgFNIELK 129
GDPD_2 pfam13653
Glycerophosphoryl diester phosphodiesterase family; This family also includes ...
262-291 9.16e-05

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: 39.02  E-value: 9.16e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 515948746  262 SVHYWTINDSQTIERLLQLGAKGIITDRPD 291
Cdd:pfam13653   1 KVRFWTIDNKAAWKELMRLGVDGLNTDDPE 30
 
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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