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Conserved domains on  [gi|518065658|ref|WP_019235866|]
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MULTISPECIES: glycerophosphodiester phosphodiesterase [Staphylococcus]

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 ...
 49-302 3.66e-100

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: 294.16  E-value: 3.66e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  49 FAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYYFTDIN 128
Cdd:cd08561    2 IAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDDG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 129 -RQYPYRGHsDAKILTFEELLELYPEMYINVDLKDhpdsyEGAIAPEVLYHQISKHQAEHRVLVTSFHKEQIERFDQLSk 207
Cdd:cd08561   82 gRTYPYRGQ-GIRIPTLEELFEAFPDVRLNIEIKD-----DGPAAAAALADLIERYGAQDRVLVASFSDRVLRRFRRLC- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 208 GTVAIGASQSEVTEAFIKFNTFRGNTYHPKANTFQMPIEFKGIRLTSARFIKWLTLLNIVPGYYGINSIDLMTDLYQKGA 287
Cdd:cd08561  155 PRVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLGV 234

                        250
                 ....*....|....*
gi 518065658 288 HTLVTDRPDLAQQFK 302
Cdd:cd08561  235 DGIITDRPDLLLEVL 249
 
Name Accession Description Interval E-value
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 49-302 3.66e-100

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: 294.16  E-value: 3.66e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  49 FAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYYFTDIN 128
Cdd:cd08561    2 IAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDDG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 129 -RQYPYRGHsDAKILTFEELLELYPEMYINVDLKDhpdsyEGAIAPEVLYHQISKHQAEHRVLVTSFHKEQIERFDQLSk 207
Cdd:cd08561   82 gRTYPYRGQ-GIRIPTLEELFEAFPDVRLNIEIKD-----DGPAAAAALADLIERYGAQDRVLVASFSDRVLRRFRRLC- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 208 GTVAIGASQSEVTEAFIKFNTFRGNTYHPKANTFQMPIEFKGIRLTSARFIKWLTLLNIVPGYYGINSIDLMTDLYQKGA 287
Cdd:cd08561  155 PRVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLGV 234

                        250
                 ....*....|....*
gi 518065658 288 HTLVTDRPDLAQQFK 302
Cdd:cd08561  235 DGIITDRPDLLLEVL 249
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
46-301 1.79e-65

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 205.49  E-value: 1.79e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  46 PYLFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYyft 125
Cdd:COG0584    3 PLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGS--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 126 dinrqypYRGHSDAKILTFEELLELYP-EMYINVDLKDHPDSYEGAIapEVLYHQISKHQAEHRVLVTSFHKEQIERFDQ 204
Cdd:COG0584   80 -------GPDFAGERIPTLEEVLELVPgDVGLNIEIKSPPAAEPDLA--EAVAALLKRYGLEDRVIVSSFDPEALRRLRE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 205 LSKGtVAIGASQSEVTEAFIKFN-TFRGNTYHPkantfqmpiefkGIRLTSARFIKWLTLLNIVPGYYGINSIDLMTDLY 283
Cdd:COG0584  151 LAPD-VPLGLLVEELPADPLELArALGADGVGP------------DYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLL 217

                        250
                 ....*....|....*...
gi 518065658 284 QKGAHTLVTDRPDLAQQF 301
Cdd:COG0584  218 DLGVDGIITDRPDLLRAV 235
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 51-297 3.64e-27

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: 106.33  E-value: 3.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658   51 HRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGyyftdINRQ 130
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIG-----AGNS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  131 YPYRGHsDAKILTFEELLELYPEMYINVDLKdhPDSYEGAIAPEVLYHQ----------ISKHQAEHRVLVTSFHKEQIE 200
Cdd:pfam03009  76 GPLSGE-RVPFPTLEEVLEFDWDVGFNIEIK--IKPYVEAIAPEEGLIVkdlllsvdeiLAKKADPRRVIFSSFNPDELK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  201 RFDQLSKgTVAIGASQSEVTEAFIKfntfRGNTYHPKANTFQMPIEFKGIRLTSARFIKWLTLLNIVPGYYGINSIDLMT 280
Cdd:pfam03009 153 RLRELAP-KLPLVFLSSGRAYAEAD----LLERAAAFAGAPALLGEVALVDEALPDLVKRAHARGLVVHVWTVNNEDEMK 227

                         250
                  ....*....|....*..
gi 518065658  281 DLYQKGAHTLVTDRPDL 297
Cdd:pfam03009 228 RLLELGVDGVITDRPDT 244
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 46-124 5.70e-24

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 97.70  E-value: 5.70e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518065658  46 PYLFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYYF 124
Cdd:PRK09454   8 PRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWF 86
 
Name Accession Description Interval E-value
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 49-302 3.66e-100

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: 294.16  E-value: 3.66e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  49 FAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYYFTDIN 128
Cdd:cd08561    2 IAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDDG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 129 -RQYPYRGHsDAKILTFEELLELYPEMYINVDLKDhpdsyEGAIAPEVLYHQISKHQAEHRVLVTSFHKEQIERFDQLSk 207
Cdd:cd08561   82 gRTYPYRGQ-GIRIPTLEELFEAFPDVRLNIEIKD-----DGPAAAAALADLIERYGAQDRVLVASFSDRVLRRFRRLC- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 208 GTVAIGASQSEVTEAFIKFNTFRGNTYHPKANTFQMPIEFKGIRLTSARFIKWLTLLNIVPGYYGINSIDLMTDLYQKGA 287
Cdd:cd08561  155 PRVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLGV 234

                        250
                 ....*....|....*
gi 518065658 288 HTLVTDRPDLAQQFK 302
Cdd:cd08561  235 DGIITDRPDLLLEVL 249
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
46-301 1.79e-65

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 205.49  E-value: 1.79e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  46 PYLFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYyft 125
Cdd:COG0584    3 PLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGS--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 126 dinrqypYRGHSDAKILTFEELLELYP-EMYINVDLKDHPDSYEGAIapEVLYHQISKHQAEHRVLVTSFHKEQIERFDQ 204
Cdd:COG0584   80 -------GPDFAGERIPTLEEVLELVPgDVGLNIEIKSPPAAEPDLA--EAVAALLKRYGLEDRVIVSSFDPEALRRLRE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 205 LSKGtVAIGASQSEVTEAFIKFN-TFRGNTYHPkantfqmpiefkGIRLTSARFIKWLTLLNIVPGYYGINSIDLMTDLY 283
Cdd:COG0584  151 LAPD-VPLGLLVEELPADPLELArALGADGVGP------------DYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLL 217

                        250
                 ....*....|....*...
gi 518065658 284 QKGAHTLVTDRPDLAQQF 301
Cdd:COG0584  218 DLGVDGIITDRPDLLRAV 235
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 46-295 2.64e-53

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: 173.90  E-value: 2.64e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  46 PYLFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYYFT 125
Cdd:cd08563    1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 126 dinrqypyRGHSDAKILTFEELLELYPE--MYINVDLKDHPDSYEGAIapEVLYHQISKHQAEHRVLVTSFHKEQIERFD 203
Cdd:cd08563   81 --------EKFTGEKIPTLEEVLDLLKDkdLLLNIEIKTDVIHYPGIE--KKVLELVKEYNLEDRVIFSSFNHESLKRLK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 204 QLskgtvaigasQSEVTEAFIkfntFRGNTYHPKANTFQMPIEF--KGIRLTSARFIKWLTLLNIVPGYYGINSIDLMTD 281
Cdd:cd08563  151 KL----------DPKIKLALL----YETGLQDPKDYAKKIGADSlhPDFKLLTEEVVEELKKRGIPVRLWTVNEEEDMKR 216

                        250
                 ....*....|....
gi 518065658 282 LYQKGAHTLVTDRP 295
Cdd:cd08563  217 LKDLGVDGIITNYP 230
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 46-204 4.31e-43

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: 148.52  E-value: 4.31e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  46 PYLFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYYFT 125
Cdd:cd08575    1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGYT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 126 -DINRQYPYRGHSDAKILTFEELLELYPEMYINVDLKDHPDsyeGAIAPEVLyHQISKHQAEHRVLVTSFHKEQIERFDQ 204
Cdd:cd08575   81 fDGGKTGYPRGGGDGRIPTLEEVFKAFPDTPINIDIKSPDA---EELIAAVL-DLLEKYKREDRTVWGSTNPEYLRALHP 156
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 50-208 4.01e-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: 137.43  E-value: 4.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  50 AHRGG-MAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGyyftdiN 128
Cdd:cd08566    4 AHRGGwGAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLK------D 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 129 RQYPyrgHSDAKILTFEELLELYPE-MYINVDLKDhpdsyegAIAPEVlYHQISKHQAEHRVLVTSFHKEQIERFDQLSK 207
Cdd:cd08566   78 GDGE---VTDEKVPTLEEALAWAKGkILLNLDLKD-------ADLDEV-IALVKKHGALDQVIFKSYSEEQAKELRALAP 146


                 .
gi 518065658 208 G 208
Cdd:cd08566  147 E 147
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 50-298 1.80e-34

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: 125.21  E-value: 1.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  50 AHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYYFTDinr 129
Cdd:cd08565    3 GHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLRDSFGE--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 130 qypyrghsdaKILTFEELLELY--PEMYINVDLKDHPDS--YEGAIAPEVlyHQISKHQAEHRVLVTSFHKEQIERFDQL 205
Cdd:cd08565   80 ----------KIPTLEEVLALFapSGLELHVEIKTDADGtpYPGAAALAA--ATLRRHGLLERSVLTSFDPAVLTEVRKH 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 206 SKGTVAIGASQSEVTEAFiKFNTFRGNTYHPkanTFQMPIEFKGIRLTSARFIKWLTLLNIvpGYYGINSIDLMTDLYQK 285
Cdd:cd08565  148 PGVRTLGSVDEDMLERLG-GELPFLTATALK---AHIVAVEQSLLAATWELVRAAVPGLRL--GVWTVNDDSLIRYWLAC 221

                        250
                 ....*....|...
gi 518065658 286 GAHTLVTDRPDLA 298
Cdd:cd08565  222 GVRQLTTDRPDLA 234
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 48-197 4.09e-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: 121.56  E-value: 4.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  48 LFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYYFtdi 127
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWF--- 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518065658 128 NRQYpyrghSDAKILTFEELLELYPEMYINVDLKDHPDSYEGAIAPEVLYHQISKHQAEH-RVLVTSFHKE 197
Cdd:cd08562   78 SPEF-----AGEPIPTLADVLELARELGLGLNLEIKPDPGDEALTARVVAAALRELWPHAsKLLLSSFSLE 143
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 46-207 2.02e-30

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: 115.50  E-value: 2.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  46 PYLFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYYFT 125
Cdd:cd08580    1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAGYNFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 126 DINrQYPYRGHSdAKILTFEELLELYPEMYINVDLKDHP-DSYEGAIAPEvlyhqISKHQAEHRVLVTSFHKEQIERFDQ 204
Cdd:cd08580   81 PEG-GYPYRGKP-VGIPTLEQVLRAFPDTPFILDMKSLPaDPQAKAVARV-----LERENAWSRVRIYSTNADYQDALAP 153


                 ...
gi 518065658 205 LSK 207
Cdd:cd08580  154 YPQ 156
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 50-297 2.95e-30

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: 113.95  E-value: 2.95e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  50 AHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYYFTDinr 129
Cdd:cd08582    3 AHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGSWKGE--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 130 qypyrGHSDAKILTFEELLELYPE--MYINVDLKDHPdsYEGAIAPEVL--YHQISKHQaeHRVLVTSFHKEQIERFDQL 205
Cdd:cd08582   80 -----SYKGEKVPTLEEYLAIVPKygKKLFIEIKHPR--RGPEAEEELLklLKESGLLP--EQIVIISFDAEALKRVREL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 206 SKGT----VAIGASQSEVTEAFIKFNTFRGNTYHPKANtfqmpiefkgirlTSARFIKwlTLLNIVPGYYG--INSIDLM 279
Cdd:cd08582  151 APTLetlwLRNYKSPKEDPRPLAKSGGAAGLDLSYEKK-------------LNPAFIK--ALRDAGLKLNVwtVDDAEDA 215

                        250
                 ....*....|....*...
gi 518065658 280 TDLYQKGAHTLVTDRPDL 297
Cdd:cd08582  216 KRLIELGVDSITTNRPGR 233
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 48-195 1.01e-29

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


Pssm-ID: 176515 [Multi-domain]  Cd Length: 258  Bit Score: 113.51  E-value: 1.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  48 LFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYYFTDI 127
Cdd:cd08573    1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRLS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518065658 128 NRqypyrgHSDAKILTFEE----LLELYPEMYInvDLKDHPDSyegaiAPEVLYHQISKH-QAEHRVLVTSFH 195
Cdd:cd08573   81 SR------FPGEKIPTLEEavkeCLENNLRMIF--DVKSNSSK-----LVDALKNLFKKYpGLYDKAIVCSFN 140
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 50-236 2.59e-29

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: 112.41  E-value: 2.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  50 AHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGS--GKVCEHTLAELRKLDAGYYFtdi 127
Cdd:cd08601    5 AHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIErpGPVKDYTLAEIKQLDAGSWF--- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 128 NRQYPYRG---HSDAKILTFEELLELY---PEMYInvDLKDhPDSYEGaIAPEVL-----YHQISKHQAEHRVLVTSFHK 196
Cdd:cd08601   82 NKAYPEYAresYSGLKVPTLEEVIERYggrANYYI--ETKS-PDLYPG-MEEKLLatldkYGLLTDNLKNGQVIIQSFSK 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518065658 197 EQIER--------------------------FDQLSKGTVAIGASQSEVTEAFIKFNTFRGNTYHP 236
Cdd:cd08601  158 ESLKKlhqlnpniplvqllwygegaetydkwLDEIKEYAIGIGPSIADADPWMVHLIHKKGLLVHP 223
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 51-297 3.64e-27

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: 106.33  E-value: 3.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658   51 HRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGyyftdINRQ 130
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIG-----AGNS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  131 YPYRGHsDAKILTFEELLELYPEMYINVDLKdhPDSYEGAIAPEVLYHQ----------ISKHQAEHRVLVTSFHKEQIE 200
Cdd:pfam03009  76 GPLSGE-RVPFPTLEEVLEFDWDVGFNIEIK--IKPYVEAIAPEEGLIVkdlllsvdeiLAKKADPRRVIFSSFNPDELK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  201 RFDQLSKgTVAIGASQSEVTEAFIKfntfRGNTYHPKANTFQMPIEFKGIRLTSARFIKWLTLLNIVPGYYGINSIDLMT 280
Cdd:pfam03009 153 RLRELAP-KLPLVFLSSGRAYAEAD----LLERAAAFAGAPALLGEVALVDEALPDLVKRAHARGLVVHVWTVNNEDEMK 227

                         250
                  ....*....|....*..
gi 518065658  281 DLYQKGAHTLVTDRPDL 297
Cdd:pfam03009 228 RLLELGVDGVITDRPDT 244
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 51-266 7.34e-26

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: 102.38  E-value: 7.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  51 HRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGyyftdinrq 130
Cdd:cd08568    5 HRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHPG--------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 131 ypyrghsDAKILTFEELLELYPEMYI-NVDLKDhPDsyegaiAPEVLYHQISKHQAEHRVLVTSFHKEQIERFDQLSKGT 209
Cdd:cd08568   76 -------GELIPTLEEVFRALPNDAIiNVEIKD-ID------AVEPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPDA 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 210 vAIGASQSEVTEAFIKFNTFRG-NTY--HPKANTFQMpIEFKGIRltsaRFIKWLTLLNI 266
Cdd:cd08568  142 -KVGLLIGEEEEGFSIPELHEKlKLYslHVPIDAIGY-IGFEKFV----ELLRLLRKLGL 195
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 48-294 1.01e-25

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: 100.80  E-value: 1.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  48 LFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDatvdrttngsgkvcehtlaelrkldagyyftdi 127
Cdd:cd08556    1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 128 nrqypyrghsdakILTFEELLELYPE-MYINVDLKDHPDSYEgaIAPEVLyHQISKHQAEHRVLVTSFHKEQIERFDQLS 206
Cdd:cd08556   48 -------------IPTLEEVLELVKGgVGLNIELKEPTRYPG--LEAKVA-ELLREYGLEERVVVSSFDHEALRALKELD 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 207 KGtVAIGASQSEVTEAFIKFNT---FRGNTYHPKAntfqmpiefkgiRLTSARFIKWLTLLNIVPGYYGINSIDLMTDLY 283
Cdd:cd08556  112 PE-VPTGLLVDKPPLDPLLAELaraLGADAVNPHY------------KLLTPELVRAAHAAGLKVYVWTVNDPEDARRLL 178

                        250
                 ....*....|.
gi 518065658 284 QKGAHTLVTDR 294
Cdd:cd08556  179 ALGVDGIITDD 189
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 46-151 1.28e-24

Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in bacterial and eukaryotic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ. GP-GDEs are involved in glycerol metabolism and catalyze the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. In E. coli, there are two major G3P uptake systems: Glp and Ugp, which contain genes coding for two different GP-GDEs. GlpQ gene from the glp operon codes for a periplasmic phosphodiesterase GlpQ. GlpQ is a dimeric enzyme that hydrolyzes periplasmic glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), to the corresponding alcohols and G3P, which is subsequently transported into the cell through the GlpT transport system. Ca2+ is required for GlpQ enzymatic activity. This subfamily also includes some GP-GDEs in higher plants and their eukaryotic homologs, which show very high sequence similarities with bacterial periplasmic GP-GDEs.


Pssm-ID: 176502 [Multi-domain]  Cd Length: 296  Bit Score: 100.43  E-value: 1.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  46 PYLFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTN------------GSGKVCEHTLA 113
Cdd:cd08559    1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNvaehfpfrgrkdTGYFVIDFTLA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 518065658 114 ELRKLDAGYYFtdiNRQYPYRGHS---DAKILTFEELLELY 151
Cdd:cd08559   81 ELKTLRAGSWF---NQRYPERAPSyygGFKIPTLEEVIELA 118
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 46-124 5.70e-24

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 97.70  E-value: 5.70e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518065658  46 PYLFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYYF 124
Cdd:PRK09454   8 PRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWF 86
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 45-188 3.92e-23

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: 96.66  E-value: 3.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  45 APYLFAHRGgMAVRPEQTKLAFDN-----------------------AVQYGVDGFETDVRLTKDKALIVFHDATVDRTT 101
Cdd:cd08613   23 KPKLLAHRG-LAQTFDREGVENDTctaeridppthdylentiasmqaAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 102 NGSGKVCEHTLAELRKLDAGYYFT-DINRQYPYRGHSDAKILTFEELLELYPEMYINVDLKDHpDSYEGaiapEVLYHQI 180
Cdd:cd08613  102 DGSGVTRDHTMAELKTLDIGYGYTaDGGKTFPFRGKGVGMMPTLDEVFAAFPDRRFLINFKSD-DAAEG----ELLAEKL 176


                 ....*...
gi 518065658 181 SKHQAEHR 188
Cdd:cd08613  177 ATLPRKRL 184
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 50-202 1.94e-22

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: 94.59  E-value: 1.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  50 AHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAEL----RKLDagyyFT 125
Cdd:cd08612   31 SHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLppylEKLE----VT 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 126 DINRQYPYRGHSDAKILTFEELLELYPEMYINVDLKDHPDsyegaiapeVLYHQIS----KHQAEHRVLVTSFHKEQIER 201
Cdd:cd08612  107 FSPGDYCVPKGSDRRIPLLEEVFEAFPDTPINIDIKVEND---------ELIKKVSdlvrKYKREDITVWGSFNDEIVKK 177


                 .
gi 518065658 202 F 202
Cdd:cd08612  178 C 178
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 50-161 3.06e-22

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: 92.67  E-value: 3.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  50 AHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVC-EHTLAELRKLDAgyyftdin 128
Cdd:cd08570    3 GHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIdDSTWDELSHLRT-------- 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 518065658 129 rqypyRGHSDAKILTFEELLEL-----YPEMYINVDLK 161
Cdd:cd08570   75 -----IEEPHQPMPTLKDVLEWlveheLPDVKLMLDIK 107
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 48-194 1.58e-21

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: 91.60  E-value: 1.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  48 LFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATV--DRTTNGSGK--------VCEHTLAELRK 117
Cdd:cd08567    3 LQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLnpDITRDPDGAwlpyegpaLYELTLAEIKQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 118 LDAGY--YFTDINRQYP-YRGHSDAKILTFEELLEL-----YPEMYINVDLKDHPDSYEGAIAPE----VLYHQISKHQA 185
Cdd:cd08567   83 LDVGEkrPGSDYAKLFPeQIPVPGTRIPTLEEVFALvekygNQKVRFNIETKSDPDRDILHPPPEefvdAVLAVIRKAGL 162


                 ....*....
gi 518065658 186 EHRVLVTSF 194
Cdd:cd08567  163 EDRVVLQSF 171
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 50-295 9.64e-20

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: 85.68  E-value: 9.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  50 AHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGyyftdinr 129
Cdd:cd08579    3 AHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIG-------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 130 qypyRGHSDAKILTFEELLELY--PEMYINVDLKDHPDSYEGAiAPEVLyHQISKHQAEHRVLVTSFHKEQIERFDQLsk 207
Cdd:cd08579   75 ----ENGHGAKIPSLDEYLALAkgLKQKLLIELKPHGHDSPDL-VEKFV-KLYKQNLIENQHQVHSLDYRVIEKVKKL-- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 208 gtvaigasqsevteafikfntfrgntyHPKANT-FQMPIEFKGIRLTSARFIK----WLT--LLNIVPGY------YGIN 274
Cdd:cd08579  147 ---------------------------DPKIKTgYILPFNIGNLPKTNVDFYSieysTLNkeFIRQAHQNgkkvyvWTVN 199

                        250       260
                 ....*....|....*....|.
gi 518065658 275 SIDLMTDLYQKGAHTLVTDRP 295
Cdd:cd08579  200 DPDDMQRYLAMGVDGIITDYP 220
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 49-235 1.17e-18

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: 83.14  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  49 FAHRG--GMAVR-PEQTKLAFDNAVQYGVdGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAgyyft 125
Cdd:cd08585    7 IAHRGlhDRDAGiPENSLSAFRAAAEAGY-GIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRL----- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 126 dinrqypyrGHSDAKILTFEELLELYP-EMYINVDLKDHPDsYEGAIAPEVLyhQISKHQAEHrVLVTSFHKEQIERFDQ 204
Cdd:cd08585   81 ---------LGTDEHIPTLDEVLELVAgRVPLLIELKSCGG-GDGGLERRVL--AALKDYKGP-AAIMSFDPRVVRWFRK 147

                        170       180       190
                 ....*....|....*....|....*....|.
gi 518065658 205 LSKGTVAIGASQSEVTEAFIKFNTFRGNTYH 235
Cdd:cd08585  148 LAPGIPRGQLSEGSNDEADPAFWNEALLSAL 178
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 45-193 1.46e-18

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: 83.13  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  45 APYLFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGS----GKVCEH----TLAELR 116
Cdd:cd08574    1 KPALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVAdvfpERAHERasmfTWTDLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 117 KLDAGYYFTdinRQYPYRG-----HSDA------KILTFEELLELYPE--MYINVDL----KDHP--DSYEGAIAPEVLY 177
Cdd:cd08574   81 QLNAGQWFL---KDDPFWTasslsESDReeagnqSIPSLAELLRLAKKhnKSVIFDLrrppPNHPyyQSYVNITLDTILA 157

                        170       180
                 ....*....|....*....|.
gi 518065658 178 HQISKHQ-----AEHRVLVTS 193
Cdd:cd08574  158 SGIPQHQvfwlpDEYRALVRK 178
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 48-213 5.70e-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: 78.14  E-value: 5.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  48 LFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTLAELRKLDAGYyftdi 127
Cdd:cd08581    1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVAE----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 128 nRQYPYRGHSDAKILTFEELLEL---YPEMYINVDLKDHPDSYEG--AIAPEVLyhQISKHQAEHRVLVtSFHKEQIERF 202
Cdd:cd08581   76 -PARFGSRFAGEPLPSLAAVVQWlaqHPQVTLFVEIKTESLDRFGleRVVDKVL--RALPAVAAQRVLI-SFDYDLLALA 151

                        170
                 ....*....|.
gi 518065658 203 DQLskGTVAIG 213
Cdd:cd08581  152 KQQ--GGPRTG 160
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 50-154 9.35e-15

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: 73.19  E-value: 9.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  50 AHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTN------------GSGKVCEHTLAELRK 117
Cdd:cd08600    5 AHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNvaekfpdrkrkdGRYYVIDFTLDELKS 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 518065658 118 LDAGYYFTDINR----QYPYR---GHSDAKILTFEELLELYPEM 154
Cdd:cd08600   85 LSVTERFDIENGkkvqVYPNRfplWKSDFKIHTLEEEIELIQGL 128
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 46-162 1.41e-14

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: 72.72  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  46 PYLFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNgsgkVCEH--------------- 110
Cdd:cd08602    1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTD----VADHpefadrkttktvdgv 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 111 ----------TLAELRKLDAgyyftdinRQ-YPYRGHS-DAK--ILTFEELLEL--------------YPEM----YINV 158
Cdd:cd08602   77 nvtgwftedfTLAELKTLRA--------RQrLPYRDQSyDGQfpIPTFEEIIALakaasaatgrtvgiYPEIkhptYFNA 148


                 ....
gi 518065658 159 DLKD 162
Cdd:cd08602  149 PLGL 152
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 33-167 6.44e-14

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: 71.11  E-value: 6.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  33 EINAIPPffsgvAPYLFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEH-- 110
Cdd:cd08609   19 EENNLPP-----KPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKDVFPGRda 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518065658 111 ------TLAELRKLDAGYYFTdinRQYPYRG-----HSD------AKILTFEELLELYPEMYINV--DLKDHPDSY 167
Cdd:cd08609   94 agsnnfTWTELKTLNAGSWFL---ERRPFWTlsslsEEDrreadnQTVPSLSELLDLAKKHNVSImfDLRNENNSH 166
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 44-199 7.04e-12

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: 64.42  E-value: 7.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  44 VAPYLFAHRG-GMAVR-PEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFH---DATVDRTT-----NGSGKVCEHTLA 113
Cdd:cd08564    2 VRPIIVGHRGaGCSTLyPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteDDTNPDTSiqlddSGFKNINDLSLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 114 ELRKLDAGYYFtdINRQYPYRGHSDAKILTFEELLELY-PEMYINVDLKdhpdsyegaiAPEVLYHQ-----ISKHQAEH 187
Cdd:cd08564   82 EITRLHFKQLF--DEKPCGADEIKGEKIPTLEDVLVTFkDKLKYNIELK----------GREVGLGErvlnlVEKYGMIL 149

                        170
                 ....*....|...
gi 518065658 188 RVLVTSF-HKEQI 199
Cdd:cd08564  150 QVHFSSFlHYDRL 162
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 43-102 4.34e-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: 62.58  E-value: 4.34e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  43 GVAPYLFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTN 102
Cdd:cd08610   20 GPKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTN 79
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 50-150 1.03e-10

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 61.61  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  50 AHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGK------------VCEHTLAELRK 117
Cdd:PRK11143  31 AHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAERfpdrarkdgryyAIDFTLDEIKS 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 518065658 118 LDAGYYF-TDINRQ---YPYR---GHSDAKILTFEELLEL 150
Cdd:PRK11143 111 LKFTEGFdIENGKKvqvYPGRfpmGKSDFRVHTFEEEIEF 150
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 50-195 2.28e-10

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: 58.60  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  50 AHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTngsgkvcehtlaelrkldagyyftdinr 129
Cdd:cd08555    3 SHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTT---------------------------- 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518065658 130 qypyrghSDAKILTFEELLELYPEMY------INVDLKDHPDSYEGAIAPEVL---YHQISKHQAEHRVLVTSFH 195
Cdd:cd08555   55 -------AGILPPTLEEVLELIADYLknpdytIILSLEIKQDSPEYDEFLAKVlkeLRVYFDYDLRGKVVLSSFN 122
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 45-184 2.35e-10

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: 60.63  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  45 APYLFAHRGGMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEHTL--------AELR 116
Cdd:cd08608    1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYedasmfnwTDLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 117 KLDAGYYF--TDINRQYPYRGHSDAK------ILTFEELLELYPEMYINVDLK------DHP--DSYEGAIAPEVLYHQI 180
Cdd:cd08608   81 RLNAGQWFlkDDPFWTAQSLSPSDRKeagnqsVCSLAELLELAKRYNASVLLNlrrpppNHPyhQSWINLTLKTILASGI 160


                 ....
gi 518065658 181 SKHQ 184
Cdd:cd08608  161 PQEQ 164
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 50-195 6.51e-08

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: 52.80  E-value: 6.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  50 AHRG-GMAVRP----------EQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNG---SGKVCEHTLAEL 115
Cdd:cd08605    4 GHRGlGMNRAShqpsvgpgirENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVERGGeveSSRIRDLTLAEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658 116 RKLD-----------AGYYFTDINRQYPYRGHSDAKILTFEELLELYP-EMYINVDLK-DHPDSYEgaiaPEVLYHQIS- 181
Cdd:cd08605   84 KALGpqaestktstvALYRKAKDPEPEPWIMDVEDSIPTLEEVFSEVPpSLGFNIELKfGDDNKTE----AEELVRELRa 159

                        170       180
                 ....*....|....*....|
gi 518065658 182 ------KHQAEHRVLVTSFH 195
Cdd:cd08605  160 ilavckQHAPGRRIMFSSFD 179
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 51-161 3.77e-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: 47.66  E-value: 3.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  51 HRG-GM-------AVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATVDRTTNGSGKVCEH----------TL 112
Cdd:cd08572    5 HRGlGKnyasgslAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSKTGSDEGelievpihdlTL 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518065658 113 AELRKLDaGYYFTDINRQYPYRGHSDAKIL-----------TFEELLE-LYPEMYINVDLK 161
Cdd:cd08572   85 EQLKELG-LQHISALKRKALTRKAKGPKPNpwgmdehdpfpTLQEVLEqVPKDLGFNIEIK 144
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 51-119 1.61e-05

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: 45.75  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518065658  51 HRG-------GMAVRPEQTKLAFDNAVQYGVDGFETDVRLTKDKALIVFHDATV---DRTTNGSGKVC-------EHTLA 113
Cdd:cd08607    5 HRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLrvsLKSKGDSDRDDllevpvkDLTYE 84


                 ....*.
gi 518065658 114 ELRKLD 119
Cdd:cd08607   85 QLKLLK 90
 
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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