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Conserved domains on  [gi|1268908826|gb|PHL14398|]
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glycerophosphodiester phosphodiesterase [Enterococcus faecium]

Protein Classification

glycerophosphodiester phosphodiesterase( domain architecture ID 11426576)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
25-256 3.91e-44

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


:

Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 148.86  E-value: 3.91e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKfnLDTKNYPE 104
Cdd:COG0584     5 IIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQ--LDAGSGPD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 105 YvnKKVKIPTFEEAVKEIKKnNLIVNVDgSKGNWQDEH-FVNDIVNTLKQNSVYERSFFVLTDKKIRDEVVKNHPDCTVS 183
Cdd:COG0584    83 F--AGERIPTLEEVLELVPG-DVGLNIE-IKSPPAAEPdLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1268908826 184 WLYDqkNKLEDEIEQVKSYKKALLSVSNDAATEETINKLNKSGIEYQVYGVNDVKRFEVLKKSSVPIVETDEI 256
Cdd:COG0584   159 LLVE--ELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRP 229
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
25-256 3.91e-44

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 148.86  E-value: 3.91e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKfnLDTKNYPE 104
Cdd:COG0584     5 IIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQ--LDAGSGPD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 105 YvnKKVKIPTFEEAVKEIKKnNLIVNVDgSKGNWQDEH-FVNDIVNTLKQNSVYERSFFVLTDKKIRDEVVKNHPDCTVS 183
Cdd:COG0584    83 F--AGERIPTLEEVLELVPG-DVGLNIE-IKSPPAAEPdLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1268908826 184 WLYDqkNKLEDEIEQVKSYKKALLSVSNDAATEETINKLNKSGIEYQVYGVNDVKRFEVLKKSSVPIVETDEI 256
Cdd:COG0584   159 LLVE--ELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRP 229
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 25-236 2.34e-37

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: 131.66  E-value: 2.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAH-IIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNLDTKNYP 103
Cdd:cd08566     2 VVAHRGGWgAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKDGDGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 104 EyvnKKVKIPTFEEAVkEIKKNNLIVNVDGSKGNWQdehfvnDIVNTLKQNSVYERSFFVLTDKKIRDEVVKNHPDCTVS 183
Cdd:cd08566    82 V---TDEKVPTLEEAL-AWAKGKILLNLDLKDADLD------EVIALVKKHGALDQVIFKSYSEEQAKELRALAPEVMLM 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1268908826 184 WLYDQKNKLEDEIEQVKSYKKALLSVSND---AATEETINKLNKSGIEYQVYGVND 236
Cdd:cd08566   152 PIVRDAEDLDEEEARAIDALNLLAFEITFddlDLPPLFDELLRALGIRVWVNTLGD 207
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 25-131 1.06e-22

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 93.47  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKfnLDTKNY-- 102
Cdd:PRK09454   10 IVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQ--LDAGSWfs 87

                          90       100
                  ....*....|....*....|....*....
gi 1268908826 103 PEYVNKKVkiPTFEEAVKEIKKNNLIVNV 131
Cdd:PRK09454   88 AAFAGEPL--PTLSQVAARCRAHGMAANI 114
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 28-131 3.49e-21

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: 89.00  E-value: 3.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  28 HRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNLDTKNYPEYVN 107
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLSG 80

                          90       100
                  ....*....|....*....|....
gi 1268908826 108 KKVKIPTFEEAVKEIKKNNLIVNV 131
Cdd:pfam03009  81 ERVPFPTLEEVLEFDWDVGFNIEI 104
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
25-256 3.91e-44

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 148.86  E-value: 3.91e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKfnLDTKNYPE 104
Cdd:COG0584     5 IIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQ--LDAGSGPD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 105 YvnKKVKIPTFEEAVKEIKKnNLIVNVDgSKGNWQDEH-FVNDIVNTLKQNSVYERSFFVLTDKKIRDEVVKNHPDCTVS 183
Cdd:COG0584    83 F--AGERIPTLEEVLELVPG-DVGLNIE-IKSPPAAEPdLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1268908826 184 WLYDqkNKLEDEIEQVKSYKKALLSVSNDAATEETINKLNKSGIEYQVYGVNDVKRFEVLKKSSVPIVETDEI 256
Cdd:COG0584   159 LLVE--ELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRP 229
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 25-236 2.34e-37

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: 131.66  E-value: 2.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAH-IIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNLDTKNYP 103
Cdd:cd08566     2 VVAHRGGWgAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKDGDGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 104 EyvnKKVKIPTFEEAVkEIKKNNLIVNVDGSKGNWQdehfvnDIVNTLKQNSVYERSFFVLTDKKIRDEVVKNHPDCTVS 183
Cdd:cd08566    82 V---TDEKVPTLEEAL-AWAKGKILLNLDLKDADLD------EVIALVKKHGALDQVIFKSYSEEQAKELRALAPEVMLM 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1268908826 184 WLYDQKNKLEDEIEQVKSYKKALLSVSND---AATEETINKLNKSGIEYQVYGVND 236
Cdd:cd08566   152 PIVRDAEDLDEEEARAIDALNLLAFEITFddlDLPPLFDELLRALGIRVWVNTLGD 207
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 25-170 2.49e-35

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: 126.99  E-value: 2.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNLDTKNYPE 104
Cdd:cd08573     1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRLS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268908826 105 YVNKKVKIPTFEEAVKEIKKNNLIVNVDgSKGNwqDEHFVNDIVNTLKQ-NSVYER----SFFVLTDKKIR 170
Cdd:cd08573    81 SRFPGEKIPTLEEAVKECLENNLRMIFD-VKSN--SSKLVDALKNLFKKyPGLYDKaivcSFNPIVIYKVR 148
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 25-243 3.07e-33

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: 120.41  E-value: 3.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNLDTKNYPE 104
Cdd:cd08562     1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFSPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 105 YVNKkvKIPTFEEAVKEIKKNNLIVNVDgSKGNWQDEHFVNDIVNT-LKQNSVYER-----SFFVLTDKKIRDEVvknhP 178
Cdd:cd08562    81 FAGE--PIPTLADVLELARELGLGLNLE-IKPDPGDEALTARVVAAaLRELWPHASklllsSFSLEALRAARRAA----P 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1268908826 179 DCTVSWLYDQKNklEDEIEQVKSYKKALLSVSNDAATEETINKLNKSGIEYQVYGVNDVKRFEVL 243
Cdd:cd08562   154 ELPLGLLFDTLP--ADWLELLAALGAVSIHLNYRGLTEEQVKALKDAGYKLLVYTVNDPARAAEL 216
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 25-255 4.11e-31

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: 115.10  E-value: 4.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNLDTKNYPE 104
Cdd:cd08582     1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGSWKGES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 105 YvnKKVKIPTFEEAVKEIKKNN--LIVNVDGSKGNWQDEHFVNDIVN--TLKQNSVYERSFFVLTDKKIRDEVvknhPDC 180
Cdd:cd08582    81 Y--KGEKVPTLEEYLAIVPKYGkkLFIEIKHPRRGPEAEEELLKLLKesGLLPEQIVIISFDAEALKRVRELA----PTL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1268908826 181 TVSWLYDQKNKLEDEIEQVKSYKKALLSVSNDAA-TEETINKLNKSGIEYQVYGVNDVKRFEVLKKSSVPIVETDE 255
Cdd:cd08582   155 ETLWLRNYKSPKEDPRPLAKSGGAAGLDLSYEKKlNPAFIKALRDAGLKLNVWTVDDAEDAKRLIELGVDSITTNR 230
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 23-255 8.72e-26

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: 101.09  E-value: 8.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  23 TYLVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNLDTKNY 102
Cdd:cd08563     1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 103 PEYvnKKVKIPTFEEAVKEIKKNNLIVNVD--GSKGNWQD-EHFVNDIVNTLK-QNSVYERSFFVLTDKKIRdevvKNHP 178
Cdd:cd08563    81 EKF--TGEKIPTLEEVLDLLKDKDLLLNIEikTDVIHYPGiEKKVLELVKEYNlEDRVIFSSFNHESLKRLK----KLDP 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1268908826 179 DCTVSWLYDQknKLEDEIEQVKSYKKALLSVSNDAATEETINKLNKSGIEYQVYGVNDVKRFEVLKKSSVPIVETDE 255
Cdd:cd08563   155 KIKLALLYET--GLQDPKDYAKKIGADSLHPDFKLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNY 229
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 25-179 1.85e-25

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: 101.14  E-value: 1.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNL------- 97
Cdd:cd08575     3 HIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAgygytfd 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  98 DTKNYPEYVNKKVKIPTFEEAVKEIKKNNLIVNVdgsKGNWQDEhFVNDIVNTLKQNSVYERSFFVLTDKKIRDEVVKNH 177
Cdd:cd08575    83 GGKTGYPRGGGDGRIPTLEEVFKAFPDTPINIDI---KSPDAEE-LIAAVLDLLEKYKREDRTVWGSTNPEYLRALHPEN 158


                  ..
gi 1268908826 178 PD 179
Cdd:cd08575   159 PN 160
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 27-117 2.46e-25

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: 100.41  E-value: 2.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  27 AHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNL------DTK 100
Cdd:cd08561     3 AHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAgyhftdDGG 82

                          90
                  ....*....|....*..
gi 1268908826 101 NYPEYVNKKVKIPTFEE 117
Cdd:cd08561    83 RTYPYRGQGIRIPTLEE 99
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 25-254 3.15e-24

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: 95.79  E-value: 3.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDdtldrttdgtgkpetytikqlkkfnldtknype 104
Cdd:cd08556     1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 105 yvnkkvkIPTFEEAVKEIkKNNLIVNVDgSKGNWQDEHFVNDIVNTLKQNSVYERSFFVLTDKKIRDEVVKNHPDCTVSW 184
Cdd:cd08556    48 -------IPTLEEVLELV-KGGVGLNIE-LKEPTRYPGLEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVPTGL 118

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 185 LYDQKNKLEDEIEQVKSYKKALLSVSNDAATEETINKLNKSGIEYQVYGVNDVKRFEVLKKSSVPIVETD 254
Cdd:cd08556   119 LVDKPPLDPLLAELARALGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITD 188
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 25-131 1.06e-22

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 93.47  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKfnLDTKNY-- 102
Cdd:PRK09454   10 IVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQ--LDAGSWfs 87

                          90       100
                  ....*....|....*....|....*....
gi 1268908826 103 PEYVNKKVkiPTFEEAVKEIKKNNLIVNV 131
Cdd:PRK09454   88 AAFAGEPL--PTLSQVAARCRAHGMAANI 114
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 26-236 8.78e-22

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: 90.84  E-value: 8.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  26 VAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDG--TGKPETYTIKQLKK------FNl 97
Cdd:cd08601     4 IAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIerPGPVKDYTLAEIKQldagswFN- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  98 dtKNYPEYVNK---KVKIPTFEEAVKEIKKN-NLIVNvdgSKGNWQDEHFVNDIVNTLKQNSVYE----------RSFFV 163
Cdd:cd08601    83 --KAYPEYAREsysGLKVPTLEEVIERYGGRaNYYIE---TKSPDLYPGMEEKLLATLDKYGLLTdnlkngqviiQSFSK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1268908826 164 LTDKKIRDEvVKNHPDCTVSWLYDQKNKLEDEIEQVKSYKKAlLSVSNDAATEETINKLNKSGIEYQVYGVND 236
Cdd:cd08601   158 ESLKKLHQL-NPNIPLVQLLWYGEGAETYDKWLDEIKEYAIG-IGPSIADADPWMVHLIHKKGLLVHPYTVNE 228
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 25-254 2.16e-21

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: 89.67  E-value: 2.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTD--------GTGKPETYTIKQLKKFN 96
Cdd:cd08574     4 LIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNvadvfperAHERASMFTWTDLQQLN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  97 -----LDTKNYP--EYVNKKV-------KIPTFEEAVKEIKKNN--LIVNVDGSKGNWQDEH-FVNDIVNTLKQNSVYER 159
Cdd:cd08574    84 agqwfLKDDPFWtaSSLSESDreeagnqSIPSLAELLRLAKKHNksVIFDLRRPPPNHPYYQsYVNITLDTILASGIPQH 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 160 SFFVLTDKKiRDEVVKNHPDCTVSwlYDQKNKLEDEieqvKSYKKALLSVSNDAATEETINKLNKSGIEYQVYGVNDVKR 239
Cdd:cd08574   164 QVFWLPDEY-RALVRKVAPGFQQV--SGRKLPVESL----RENGISRLNLEYSQLSAQEIREYSKANISVNLYVVNEPWL 236

                         250
                  ....*....|....*
gi 1268908826 240 FEVLKKSSVPIVETD 254
Cdd:cd08574   237 YSLLWCSGVQSVTTN 251
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 28-131 3.49e-21

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: 89.00  E-value: 3.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  28 HRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNLDTKNYPEYVN 107
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLSG 80

                          90       100
                  ....*....|....*....|....
gi 1268908826 108 KKVKIPTFEEAVKEIKKNNLIVNV 131
Cdd:pfam03009  81 ERVPFPTLEEVLEFDWDVGFNIEI 104
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 25-171 5.24e-19

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: 83.53  E-value: 5.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNL-----DT 99
Cdd:cd08580     3 IVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAgynfkPE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1268908826 100 KNYPeYVNKKVKIPTFEEAVKEIKKNNLIVNVDGSKGNWQdehfVNDIVNTLKQNSVYERSFFVLTDKKIRD 171
Cdd:cd08580    83 GGYP-YRGKPVGIPTLEQVLRAFPDTPFILDMKSLPADPQ----AKAVARVLERENAWSRVRIYSTNADYQD 149
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 26-189 7.09e-19

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: 82.84  E-value: 7.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  26 VAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNLDtknypey 105
Cdd:cd08565     2 AGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLR------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 106 VNKKVKIPTFEEAVKEIKKNNLIVNVD-GSKGNWQD-EHFVNDIVNTLKQNSVYERSFFVLTDKKIRDEVVKnHPDCTVS 183
Cdd:cd08565    75 DSFGEKIPTLEEVLALFAPSGLELHVEiKTDADGTPyPGAAALAAATLRRHGLLERSVLTSFDPAVLTEVRK-HPGVRTL 153


                  ....*.
gi 1268908826 184 WLYDQK 189
Cdd:cd08565   154 GSVDED 159
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 25-254 7.82e-19

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: 83.82  E-value: 7.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGK-PE-------TYTIKQLKKFN 96
Cdd:cd08609    29 LVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKDVfPGrdaagsnNFTWTELKTLN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  97 -------------LDTKNYPEYVN-KKVKIPTFEEAVKEIKKNNLIVNVDGSKGNWQD---EHFVNDIVNTLKQNSVYER 159
Cdd:cd08609   109 agswflerrpfwtLSSLSEEDRREaDNQTVPSLSELLDLAKKHNVSIMFDLRNENNSHvfySSFVFYTLETILKLGIPPD 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 160 SFFVLTDkKIRDEVVKNHPDctVSWLYD-QKNKLEDEIEQVKsykkalLSVSNDAATEetINKLNKSGIEYQVYGVNDVK 238
Cdd:cd08609   189 KVWWLPD-EYRHDVMKMEPG--FKQVYGrQKEMLMDGGNFMN------LPYQDLSALE--IKELRKDNVSVNLWVVNEPW 257

                         250
                  ....*....|....*.
gi 1268908826 239 RFEVLKKSSVPIVETD 254
Cdd:cd08609   258 LFSLLWCSGVSSVTTN 273
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 25-154 9.79e-19

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: 81.82  E-value: 9.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNLDTKNYPE 104
Cdd:cd08579     1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIGENGHGA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1268908826 105 yvnkkvKIPTFEEAVKEIKKNN--LIVNVDGSKGNWQDehFVNDIVNTLKQN 154
Cdd:cd08579    81 ------KIPSLDEYLALAKGLKqkLLIELKPHGHDSPD--LVEKFVKLYKQN 124
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 25-254 1.27e-15

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: 74.27  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLD----RTTDGTGKPE--------TYT-IKQ 91
Cdd:cd08567     3 LQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNpditRDPDGAWLPYegpalyelTLAeIKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  92 L----KKFNLDT-KNYPEYVN-KKVKIPTFEE---AVKEIKKNNLIVNV------DGSKGNWQDEHFVNDIVNTLKQNSV 156
Cdd:cd08567    83 LdvgeKRPGSDYaKLFPEQIPvPGTRIPTLEEvfaLVEKYGNQKVRFNIetksdpDRDILHPPPEEFVDAVLAVIRKAGL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 157 YERSFFVLTDKKIRDEVVKNHPDCTVSWLYDQKnKLEDEIEQVKSYKKALLSVSNDAATEETINKLNKSGIEYQVYGVND 236
Cdd:cd08567   163 EDRVVLQSFDWRTLQEVRRLAPDIPTVALTEET-TLGNLPRAAKKLGADIWSPYFTLVTKELVDEAHALGLKVVPWTVND 241

                         250
                  ....*....|....*...
gi 1268908826 237 VKRFEVLKKSSVPIVETD 254
Cdd:cd08567   242 PEDMARLIDLGVDGIITD 259
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 28-256 3.16e-15

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: 72.72  E-value: 3.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  28 HRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNLDTKnypeyvn 107
Cdd:cd08568     5 HRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHPGGE------- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 108 kkvKIPTFEEAVKEIkKNNLIVNVDgskgnWQDEHFVNDIVNTLKQNSVYERSFFVLTDKKIRDEVVKNHPDCTVSWLYD 187
Cdd:cd08568    78 ---LIPTLEEVFRAL-PNDAIINVE-----IKDIDAVEPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPDAKVGLLIG 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1268908826 188 QKNKLEDEIEQVKSYKKALLSVSNDA-------ATEETINKLNKSGIEYQVYGVNDVKRFEVLkKSSVPIVETDEI 256
Cdd:cd08568   149 EEEEGFSIPELHEKLKLYSLHVPIDAigyigfeKFVELLRLLRKLGLKIVLWTVNDPELVPKL-KGLVDGVITDDV 223
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 26-126 6.66e-15

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: 72.69  E-value: 6.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  26 VAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPET------------YTIKQLK 93
Cdd:cd08559     4 IAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVAEHFPFrgrkdtgyfvidFTLAELK 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1268908826  94 KfnLDTKN-----YPEYV---NKKVKIPTFEEAVKEIKKNN 126
Cdd:cd08559    84 T--LRAGSwfnqrYPERApsyYGGFKIPTLEEVIELAQGLN 122
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 25-124 2.71e-14

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: 70.05  E-value: 2.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKFNLDtknYPE 104
Cdd:cd08581     1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVA---EPA 77

                          90       100
                  ....*....|....*....|...
gi 1268908826 105 YVNKKV---KIPTFEEAVKEIKK 124
Cdd:cd08581    78 RFGSRFagePLPSLAAVVQWLAQ 100
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 25-254 1.53e-13

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: 69.49  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQA---KILGYQAveiDVRTSRDGVNFLMHDDTLDRTTDGTGK-PE-------TYTIKQLK 93
Cdd:cd08608     4 IIGHRGAPMLAPENTLMSFQKAleqKVYGLQA---DVTISLDGVPFLMHDRTLRRTTNVDRVfPErqyedasMFNWTDLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  94 KFN----------------LDTKNYPEYVNKKVkiPTFEEAVKEIKKNN--LIVNVDGSKGNWQDEH-FVNDIVNTLKQN 154
Cdd:cd08608    81 RLNagqwflkddpfwtaqsLSPSDRKEAGNQSV--CSLAELLELAKRYNasVLLNLRRPPPNHPYHQsWINLTLKTILAS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 155 SVYERSFFVLTDKKiRDEVVKNHPdctvswLYDQKNKLEDEIEQVKSYKKALLSVSNDAATEETINKLNKSGIEYQVYGV 234
Cdd:cd08608   159 GIPQEQVMWTPDWQ-RKLVRKVAP------GFQQTSGEKLPVASLRERGITRLNLRYTQASAQEIRDYSASNLSVNLYTV 231

                         250       260
                  ....*....|....*....|
gi 1268908826 235 NDVKRFEVLKKSSVPIVETD 254
Cdd:cd08608   232 NEPWLYSLLWCSGVPSVTSD 251
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 26-124 2.61e-13

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: 67.25  E-value: 2.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  26 VAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTG-KPETYTIKQLKKfnLDTKNYPE 104
Cdd:cd08570     2 IGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGlIIDDSTWDELSH--LRTIEEPH 79

                          90       100
                  ....*....|....*....|
gi 1268908826 105 yvnkkVKIPTFEEAVKEIKK 124
Cdd:cd08570    80 -----QPMPTLKDVLEWLVE 94
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 26-118 3.49e-11

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: 61.57  E-value: 3.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  26 VAHRGAH---IIAPENTVESIHQAKILGYqAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPETYTIKQLKKfnLDTKNY 102
Cdd:cd08585     7 IAHRGLHdrdAGIPENSLSAFRAAAEAGY-GIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRA--LRLLGT 83

                          90
                  ....*....|....*.
gi 1268908826 103 PEYvnkkvkIPTFEEA 118
Cdd:cd08585    84 DEH------IPTLDEV 93
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 25-79 3.72e-11

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: 62.20  E-value: 3.72e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1268908826  25 LVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTD 79
Cdd:cd08610    25 IIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTN 79
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 25-131 3.46e-10

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


Pssm-ID: 176554 [Multi-domain]  Cd Length: 309  Bit Score: 59.30  E-value: 3.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGAH-----------------IIAP-----ENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTG 82
Cdd:cd08613    26 LLAHRGLAqtfdregvendtctaerIDPPthdylENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSG 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1268908826  83 KPETYTIKQLKKfnLDT---------KNYPeYVNKKV-KIPTFEEAVKEIKKNNLIVNV 131
Cdd:cd08613   106 VTRDHTMAELKT--LDIgygytadggKTFP-FRGKGVgMMPTLDEVFAAFPDRRFLINF 161
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 25-232 6.72e-10

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: 57.87  E-value: 6.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGA--HIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMH---DDTLDRTT-----DGTGKPETYTIKQLK- 93
Cdd:cd08564     6 IVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteDDTNPDTSiqlddSGFKNINDLSLDEITr 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  94 ---KFNLDTKNYPEYVNKKVKIPTFEEAVKEIkKNNLIVNVDgSKGNWQDEH-FVNDIVNTLK-QNSVYERSFFVLTDKK 168
Cdd:cd08564    86 lhfKQLFDEKPCGADEIKGEKIPTLEDVLVTF-KDKLKYNIE-LKGREVGLGeRVLNLVEKYGmILQVHFSSFLHYDRLD 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1268908826 169 IRDEVVKNHPDCTVSWLYDQ--KNKLEDEIEQVKSYKKALLSVSNDAATEETINKLNKSGIEYQVY 232
Cdd:cd08564   164 LLKALRPNKLNVPIALLFNEvkSPSPLDFLEQAKYYNATWVNFSYDFWTEEFVKKAHENGLKVMTY 229
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 26-126 3.95e-09

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: 56.25  E-value: 3.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  26 VAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGK-PE-----------TYTIKQLK 93
Cdd:cd08600     4 IAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKfPDrkrkdgryyviDFTLDELK 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1268908826  94 K-------FNLDTKNYPEYVNKK------VKIPTFEEAVKEIKKNN 126
Cdd:cd08600    84 SlsvterfDIENGKKVQVYPNRFplwksdFKIHTLEEEIELIQGLN 129
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 26-159 9.80e-08

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: 51.83  E-value: 9.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  26 VAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDgtgkpETYTIKQLK------------ 93
Cdd:cd08612    30 ISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCG-----VDKLVSDLNyadlppylekle 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1268908826  94 -KFNLDTKNYPeyVNKKVKIPTFEEAVKEIKknNLIVNVDgSKGNwqDEHFVNDIVNTLKQnsvYER 159
Cdd:cd08612   105 vTFSPGDYCVP--KGSDRRIPLLEEVFEAFP--DTPINID-IKVE--NDELIKKVSDLVRK---YKR 161
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 1-123 1.02e-07

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 51.98  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826   1 MLFTVLLTGCVSLANNwleHEGTYLVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDG 80
Cdd:PRK11143    8 LLLAALLAGSAAAAAD---SAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDV 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268908826  81 TGK-PE-----------TYT---IKQLK---KFNLDTKNY-PEYVNK------KVKIPTFEEAVKEIK 123
Cdd:PRK11143   85 AERfPDrarkdgryyaiDFTldeIKSLKfteGFDIENGKKvQVYPGRfpmgksDFRVHTFEEEIEFIQ 152
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 24-117 1.79e-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: 48.06  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  24 YLVAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGTGKPE------TYTI-------- 89
Cdd:cd08602     2 LVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHPEfadrktTKTVdgvnvtgw 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1268908826  90 -------KQLKKfnLDTK-----NYPEYvNKKVKIPTFEE 117
Cdd:cd08602    82 ftedftlAELKT--LRARqrlpyRDQSY-DGQFPIPTFEE 118
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 25-92 2.98e-05

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: 44.19  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  25 LVAHRGA------HIIA--PENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTL-----DRTTDGTGKPETYTIKQ 91
Cdd:cd08572     2 VIGHRGLgknyasGSLAgiRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTIsvsekSKTGSDEGELIEVPIHD 81


                  .
gi 1268908826  92 L 92
Cdd:cd08572    82 L 82
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 26-126 3.43e-05

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: 43.19  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  26 VAHRGAHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTTDGtGKPETYT--IKQLKKFNlDTKNYP 103
Cdd:cd08555     2 LSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAG-ILPPTLEevLELIADYL-KNPDYT 79

                          90       100
                  ....*....|....*....|....*....
gi 1268908826 104 EYVNKKVKIPTFEEA------VKEIKKNN 126
Cdd:cd08555    80 IILSLEIKQDSPEYDeflakvLKELRVYF 108
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 37-92 7.74e-05

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: 43.17  E-value: 7.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1268908826  37 ENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDtlDRTTDGTGKPETYTIKQL 92
Cdd:cd08605    25 ENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDD--FIVVERGGEVESSRIRDL 78
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 38-258 1.12e-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: 42.29  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  38 NTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTlDRTTDGTGKPETYTIKQLkkfnldtkNYPEYVNKKV----KIP 113
Cdd:cd08583    16 NSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHSWD-ESLLKQLGLPTSKNTKPL--------SYEEFKSKKIygkyTPM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826 114 TFEEAVKEIKKNNLIVNVDGSKGNWQDE--HFVNDIVNTLKQNS--VYERSFFVLTDKKIRDEVVKNHPDCTVSW-LYDQ 188
Cdd:cd08583    87 DFKDVIDLLKKYPDVYIVTDTKQDDDNDikKLYEYIVKEAKEVDpdLLDRVIPQIYNEEMYEAIMSIYPFKSVIYtLYRQ 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268908826 189 KNKLEDEI-EQVKSYKKALLSVSNDAATEETINKLNKSGIEYQVYGVNDVKRFEVLKKSSVPIVETDEINP 258
Cdd:cd08583   167 DSIRLDEIiAFCYENGIKAVTISKNYVNDKLIEKLNKAGIYVYVYTINDLKDAQEYKKLGVYGIYTDFLTE 237
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 26-98 1.67e-03

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: 39.20  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268908826  26 VAHRG-------AHIIAPENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTL----DRTTDGTGKP------ETYT 88
Cdd:cd08607     3 VGHRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLrvslKSKGDSDRDDllevpvKDLT 82

                          90
                  ....*....|
gi 1268908826  89 IKQLKKFNLD 98
Cdd:cd08607    83 YEQLKLLKLF 92
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 22-84 6.22e-03

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: 37.43  E-value: 6.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268908826  22 GTYLVAHRGAHIIAP--------ENTVESIHQAKILGYQAVEIDVRTSRDGVNFLMHDDTLDRTtdGTGKP 84
Cdd:cd08606     1 SVQVIGHRGLGKNTAerkslqlgENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSET--GTDVP 69
 
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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