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Conserved domains on  [gi|736016516|gb|AJA46649|]
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glycerophosphoryl diester phosphodiesterase [Clostridium pasteurianum DSM 525 = ATCC 6013]

Protein Classification

glycerophosphodiester phosphodiesterase( domain architecture ID 10171130)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 4-234 6.45e-112

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: 321.04  E-value: 6.45e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   4 SLNIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFG 83
Cdd:cd08563    1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  84 EEFKNTSIPDIDEFMDYVKDKNLLVNIELKNGIINYKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKEIDSSIKTGL 163
Cdd:cd08563   81 EKFTGEKIPTLEEVLDLLKDKDLLLNIEIKTDVIHYPGIEKKVLELVKEYNLEDRVIFSSFNHESLKRLKKLDPKIKLAL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736016516 164 LYAANIYKVHEYAQKVSADALHPYFpSVMNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELGIDGIITNYP 234
Cdd:cd08563  161 LYETGLQDPKDYAKKIGADSLHPDF-KLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230
 
Name Accession Description Interval E-value
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 4-234 6.45e-112

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: 321.04  E-value: 6.45e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   4 SLNIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFG 83
Cdd:cd08563    1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  84 EEFKNTSIPDIDEFMDYVKDKNLLVNIELKNGIINYKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKEIDSSIKTGL 163
Cdd:cd08563   81 EKFTGEKIPTLEEVLDLLKDKDLLLNIEIKTDVIHYPGIEKKVLELVKEYNLEDRVIFSSFNHESLKRLKKLDPKIKLAL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736016516 164 LYAANIYKVHEYAQKVSADALHPYFpSVMNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELGIDGIITNYP 234
Cdd:cd08563  161 LYETGLQDPKDYAKKIGADSLHPDF-KLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
5-243 1.05e-96

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 282.53  E-value: 1.05e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   5 LNIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGikFGE 84
Cdd:COG0584    4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAG--SGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  85 EFKNTSIPDIDEFMDYVKdKNLLVNIELKNGIINYKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKEIDSSIKTGLL 164
Cdd:COG0584   82 DFAGERIPTLEEVLELVP-GDVGLNIEIKSPPAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736016516 165 YAANIYKVHEYAQKVSADALHPYFPSVmNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELGIDGIITNYPDVLKRIIDE 243
Cdd:COG0584  161 VEELPADPLELARALGADGVGPDYDLL-TPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRAVLRE 238
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 9-236 2.96e-61

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: 192.62  E-value: 2.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516    9 HRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFGEEF-- 86
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLsg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   87 KNTSIPDIDEFMDYVKDKNLLVNIELKN--------GIINYKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKEIDSS 158
Cdd:pfam03009  81 ERVPFPTLEEVLEFDWDVGFNIEIKIKPyveaiapeEGLIVKDLLLSVDEILAKKADPRRVIFSSFNPDELKRLRELAPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  159 IKTGLLYAANIYK----VHEYAQKVSADALHPYFPSV--MNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELGIDGIITN 232
Cdd:pfam03009 161 LPLVFLSSGRAYAeadlLERAAAFAGAPALLGEVALVdeALPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVITD 240


                  ....
gi 736016516  233 YPDV 236
Cdd:pfam03009 241 RPDT 244
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 7-237 4.67e-32

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 117.73  E-value: 4.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGfSGKY-PENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFGEE 85
Cdd:PRK09454  11 VAHRG-GGKLaPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  86 FKNTSIPDIDEFMDYVKDKNLLVNIELK--NGiinyknLEKRIIEKI------YEYGLKDNVILSSFNHYSMVKVKEIDS 157
Cdd:PRK09454  90 FAGEPLPTLSQVAARCRAHGMAANIEIKptTG------REAETGRVValaaraLWAGAAVPPLLSSFSEDALEAARQAAP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 158 SIKTGLLYAANIYKVHEYAQKVSADALHPYFpSVMNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELGIDGIITNYPDVL 237
Cdd:PRK09454 164 ELPRGLLLDEWPDDWLELTRRLGCVSLHLNH-KLLDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTDRIDLI 242
 
Name Accession Description Interval E-value
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 4-234 6.45e-112

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: 321.04  E-value: 6.45e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   4 SLNIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFG 83
Cdd:cd08563    1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  84 EEFKNTSIPDIDEFMDYVKDKNLLVNIELKNGIINYKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKEIDSSIKTGL 163
Cdd:cd08563   81 EKFTGEKIPTLEEVLDLLKDKDLLLNIEIKTDVIHYPGIEKKVLELVKEYNLEDRVIFSSFNHESLKRLKKLDPKIKLAL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736016516 164 LYAANIYKVHEYAQKVSADALHPYFpSVMNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELGIDGIITNYP 234
Cdd:cd08563  161 LYETGLQDPKDYAKKIGADSLHPDF-KLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
5-243 1.05e-96

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 282.53  E-value: 1.05e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   5 LNIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGikFGE 84
Cdd:COG0584    4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAG--SGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  85 EFKNTSIPDIDEFMDYVKdKNLLVNIELKNGIINYKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKEIDSSIKTGLL 164
Cdd:COG0584   82 DFAGERIPTLEEVLELVP-GDVGLNIEIKSPPAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736016516 165 YAANIYKVHEYAQKVSADALHPYFPSVmNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELGIDGIITNYPDVLKRIIDE 243
Cdd:COG0584  161 VEELPADPLELARALGADGVGPDYDLL-TPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRAVLRE 238
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 7-234 8.78e-67

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: 206.30  E-value: 8.78e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFGEEF 86
Cdd:cd08562    2 IAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFSPEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  87 KNTSIPDIDEFMDYVKDKNLLVNIELKNGIINYKNLEKRIIEKIYEYGL-KDNVILSSFNHYSMVKVKEIDSSIKTGLLY 165
Cdd:cd08562   82 AGEPIPTLADVLELARELGLGLNLEIKPDPGDEALTARVVAAALRELWPhASKLLLSSFSLEALRAARRAAPELPLGLLF 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 166 AANIYKVHEYAQKVSADALHP-YfpSVMNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELGIDGIITNYP 234
Cdd:cd08562  162 DTLPADWLELLAALGAVSIHLnY--RGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 7-233 9.25e-64

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: 197.10  E-value: 9.25e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDemvyrttngqgsikdltydeikkldagikfgeef 86
Cdd:cd08556    2 IAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD---------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  87 kntsIPDIDEFMDYVKDKnLLVNIELKnGIINYKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKEIDSSIKTGLLYA 166
Cdd:cd08556   48 ----IPTLEEVLELVKGG-VGLNIELK-EPTRYPGLEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVPTGLLVD 121

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736016516 167 --ANIYKVHEYAQKVSADALHPYFPSVmNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELGIDGIITNY 233
Cdd:cd08556  122 kpPLDPLLAELARALGADAVNPHYKLL-TPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITDD 189
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 7-236 3.95e-63

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: 197.15  E-value: 3.95e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFGEEF 86
Cdd:cd08582    2 IAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGSWKGESY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  87 KNTSIPDIDEFMDYVKDKNLLVNIELKNGIINYKNLEkRIIEKIYEYGLKD-NVILSSFNHYSMVKVKEIDSSIKTGLLY 165
Cdd:cd08582   82 KGEKVPTLEEYLAIVPKYGKKLFIEIKHPRRGPEAEE-ELLKLLKESGLLPeQIVIISFDAEALKRVRELAPTLETLWLR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736016516 166 AANIYKV--HEYAQKVSADALHPYFPSVMNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELGIDGIITNYPDV 236
Cdd:cd08582  161 NYKSPKEdpRPLAKSGGAAGLDLSYEKKLNPAFIKALRDAGLKLNVWTVDDAEDAKRLIELGVDSITTNRPGR 233
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 9-236 2.96e-61

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: 192.62  E-value: 2.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516    9 HRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFGEEF-- 86
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLsg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   87 KNTSIPDIDEFMDYVKDKNLLVNIELKN--------GIINYKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKEIDSS 158
Cdd:pfam03009  81 ERVPFPTLEEVLEFDWDVGFNIEIKIKPyveaiapeEGLIVKDLLLSVDEILAKKADPRRVIFSSFNPDELKRLRELAPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  159 IKTGLLYAANIYK----VHEYAQKVSADALHPYFPSV--MNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELGIDGIITN 232
Cdd:pfam03009 161 LPLVFLSSGRAYAeadlLERAAAFAGAPALLGEVALVdeALPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVITD 240


                  ....
gi 736016516  233 YPDV 236
Cdd:pfam03009 241 RPDT 244
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 6-241 4.39e-61

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: 192.47  E-value: 4.39e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   6 NIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKF--- 82
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFtdd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  83 -GEEF----KNTSIPDIDEFMDyvKDKNLLVNIELKNgiiNYKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKEIDS 157
Cdd:cd08561   81 gGRTYpyrgQGIRIPTLEELFE--AFPDVRLNIEIKD---DGPAAAAALADLIERYGAQDRVLVASFSDRVLRRFRRLCP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 158 SIKT--------GLLYAANIYKVHEYaqKVSADALH-PYFPS---VMNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELG 225
Cdd:cd08561  156 RVATsagegevaAFVLASRLGLGSLY--SPPYDALQiPVRYGgvpLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDLG 233

                        250
                 ....*....|....*.
gi 736016516 226 IDGIITNYPDVLKRII 241
Cdd:cd08561  234 VDGIITDRPDLLLEVL 249
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 7-236 2.30e-55

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: 178.27  E-value: 2.30e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVY----RTTNGQGS------IKDLTYDEIKKL 76
Cdd:cd08567    4 QGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNpditRDPDGAWLpyegpaLYELTLAEIKQL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  77 DAG-IKFGEE----------FKNTSIPDIDEFMDYVK---DKNLLVNIELK------NGIINYKNLEKRIIEKIYEYGLK 136
Cdd:cd08567   84 DVGeKRPGSDyaklfpeqipVPGTRIPTLEEVFALVEkygNQKVRFNIETKsdpdrdILHPPPEEFVDAVLAVIRKAGLE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 137 DNVILSSFNHYSMVKVKEIDSSIKTGLLYA-ANIYKVHEYAQKVSADALHPYFPSVmNEDIVKEIKDSNIAINTYTVNEE 215
Cdd:cd08567  164 DRVVLQSFDWRTLQEVRRLAPDIPTVALTEeTTLGNLPRAAKKLGADIWSPYFTLV-TKELVDEAHALGLKVVPWTVNDP 242

                        250       260
                 ....*....|....*....|.
gi 736016516 216 KYMRRLMELGIDGIITNYPDV 236
Cdd:cd08567  243 EDMARLIDLGVDGIITDYPDL 263
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 7-234 6.09e-51

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: 165.41  E-value: 6.09e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAgikfGEEF 86
Cdd:cd08579    2 IAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTI----GENG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  87 KNTSIPDIDEFMDYVKDKNLLVNIELKNGIINYKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKEIDSSIKTGLLYA 166
Cdd:cd08579   78 HGAKIPSLDEYLALAKGLKQKLLIELKPHGHDSPDLVEKFVKLYKQNLIENQHQVHSLDYRVIEKVKKLDPKIKTGYILP 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736016516 167 ANI-----YKVHEYAQKVsadalhpyfpSVMNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELGIDGIITNYP 234
Cdd:cd08579  158 FNIgnlpkTNVDFYSIEY----------STLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 5-242 2.29e-50

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: 165.18  E-value: 2.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   5 LNIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQ--GSIKDLTYDEIKKLDAGIKF 82
Cdd:cd08601    2 AVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIErpGPVKDYTLAEIKQLDAGSWF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  83 GE--------EFKNTSIPDIDE-FMDYVKDKNLLvnIELKNGIInYKNLEKRIIEKIYEYGL------KDNVILSSFNHY 147
Cdd:cd08601   82 NKaypeyareSYSGLKVPTLEEvIERYGGRANYY--IETKSPDL-YPGMEEKLLATLDKYGLltdnlkNGQVIIQSFSKE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 148 SMVKVKEIDSSIKTGLL---------YAANIYKVHEYaqkvsADALHPYFPSVmNEDIVKEIKDSNIAINTYTVNEEKYM 218
Cdd:cd08601  159 SLKKLHQLNPNIPLVQLlwygegaetYDKWLDEIKEY-----AIGIGPSIADA-DPWMVHLIHKKGLLVHPYTVNEKADM 232

                        250       260
                 ....*....|....*....|....
gi 736016516 219 RRLMELGIDGIITNYPDVLKRIID 242
Cdd:cd08601  233 IRLINWGVDGMFTNYPDRLKEVLK 256
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 7-234 1.08e-42

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: 144.75  E-value: 1.08e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFgeef 86
Cdd:cd08568    3 LGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHPGGEL---- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  87 kntsIPDIDEFMDYVkDKNLLVNIELKNgiinyKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKEIDSSIKTGLL-- 164
Cdd:cd08568   79 ----IPTLEEVFRAL-PNDAIINVEIKD-----IDAVEPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPDAKVGLLig 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736016516 165 YAANIYKVHEYAQKVSADALH------PYFPSVMNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELgIDGIITNYP 234
Cdd:cd08568  149 EEEEGFSIPELHEKLKLYSLHvpidaiGYIGFEKFVELLRLLRKLGLKIVLWTVNDPELVPKLKGL-VDGVITDDV 223
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 5-234 1.80e-41

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: 143.57  E-value: 1.80e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   5 LNIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTN------------GQGSIKDLTYDE 72
Cdd:cd08559    2 LVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNvaehfpfrgrkdTGYFVIDFTLAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  73 IKKLDAGIKFGEEFKNT--------SIPDIDEFMDYVKDKNLLVN------IELKN---GIINYKNLEKRIIEKIYEYGL 135
Cdd:cd08559   82 LKTLRAGSWFNQRYPERapsyyggfKIPTLEEVIELAQGLNKSTGrnvgiyPETKHptfHKQEGPDIEEKLLEVLKKYGY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 136 ---KDNVILSSFNHYSMVKVKEIDSSIKTGLLYA----ANIYKVHEYAQKVS----------ADALHPYFPSVMNE---- 194
Cdd:cd08559  162 tgkNDPVFIQSFEPESLKRLRNETPDIPLVQLIDygdwAETDKKYTYAWLTTdaglkeiakyADGIGPWKSLIIPEdsng 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 736016516 195 -----DIVKEIKDSNIAINTYTVNEEKY---------MRRLME-LGIDGIITNYP 234
Cdd:cd08559  242 llvptDLVKDAHKAGLLVHPYTFRNENLflapdfkqdMDALYNaAGVDGVFTDFP 296
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 5-237 2.45e-41

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: 142.36  E-value: 2.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   5 LNIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKF-- 82
Cdd:cd08575    2 LHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGYtf 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  83 --GEEF-----KNTSIPDIDE-FMDYvkdKNLLVNIELKNGiiNYKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKE 154
Cdd:cd08575   82 dgGKTGyprggGDGRIPTLEEvFKAF---PDTPINIDIKSP--DAEELIAAVLDLLEKYKREDRTVWGSTNPEYLRALHP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 155 IDSSIK-----------------TGLLYAANI----YKVHEYAQKVSADALHPYFPSV----MNEDIVKEIKDSNIAINT 209
Cdd:cd08575  157 ENPNLFesfsmtrclllylalgyTGLLPFVPIkesfFEIPRPVIVLETFTLGEGASIVaallWWPNLFDHLRKRGIQVYL 236

                        250       260
                 ....*....|....*....|....*...
gi 736016516 210 YTVNEEKYMRRLMELGIDGIITNYPDVL 237
Cdd:cd08575  237 WVLNDEEDFEEAFDLGADGVMTDSPTKL 264
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 7-234 4.60e-41

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: 141.24  E-value: 4.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFG--E 84
Cdd:cd08573    2 IGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRlsS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  85 EFKNTSIPDIDEFMDYVKDKNLLVNIELKNgiiNYKNLEKRIIEKIYEY-GLKDNVILSSFNHYSMVKVKEIDSSIKTGL 163
Cdd:cd08573   82 RFPGEKIPTLEEAVKECLENNLRMIFDVKS---NSSKLVDALKNLFKKYpGLYDKAIVCSFNPIVIYKVRKADPKILTGL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 164 lyaanIYKVHEYAQKVSA-----------------DALH--------PYFPSV----MNEDI-----VKEIKDSNIAINT 209
Cdd:cd08573  159 -----TWRPWFLSYTDDEggprrksgwkhflysmlDVILewslhswlPYFLGVsallIHKDDissayVRYWRARGIRVIA 233

                        250       260
                 ....*....|....*....|....*...
gi 736016516 210 YTVN---EEKYMRRLMELgidGIITNYP 234
Cdd:cd08573  234 WTVNtptEKQYFAKTLNV---PYITDSL 258
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 7-234 1.63e-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: 136.66  E-value: 1.63e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGK-YPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFGeE 85
Cdd:cd08566    3 VAHRGGWGAgAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKDGDG-E 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  86 FKNTSIPDIDEFMDYVKDKnLLVNIELKNGIInyknleKRIIEKIYEYGLKDNVILSSFNHYSMVKVKEIDssikTGLLY 165
Cdd:cd08566   82 VTDEKVPTLEEALAWAKGK-ILLNLDLKDADL------DEVIALVKKHGALDQVIFKSYSEEQAKELRALA----PEVML 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 166 AANIYKVH--EYAQKVSADALHPY-----FPSVMNEDIVKEIKDSN---IAINTY------------TVNEEKYmRRLME 223
Cdd:cd08566  151 MPIVRDAEdlDEEEARAIDALNLLafeitFDDLDLPPLFDELLRALgirVWVNTLgdddtagldralSDPREVW-GELVD 229

                        250
                 ....*....|.
gi 736016516 224 LGIDGIITNYP 234
Cdd:cd08566  230 AGVDVIQTDRP 240
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 6-234 1.75e-39

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: 136.58  E-value: 1.75e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   6 NIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQG-SIKDLTYDEIKKLDAgIKFGE 84
Cdd:cd08570    1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGlIIDDSTWDELSHLRT-IEEPH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  85 EFKNTSIPDIDEFMDYV-KDKNLLVNIELKNGII--------------NYKNLEKRII-----EKIYEYGLKdnvILSSF 144
Cdd:cd08570   80 QPMPTLKDVLEWLVEHElPDVKLMLDIKRDNDPEilfkliaemlavkpDLDFWRERIIlglwhLDFLKYGKE---VLPGF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 145 NHYsmvkvkeidsSIKTGLLYAAniyKVHEYAQKVSADALHpyFPSVMNE---DIVKEIKDSNIAINTYTVNEEKYMRRL 221
Cdd:cd08570  157 PVF----------HIGFSLDYAR---HFLNYSEKLVGISMH--FVSLWGPfgqAFLPELKKNGKKVFVWTVNTEEDMRYA 221

                        250
                 ....*....|...
gi 736016516 222 MELGIDGIITNYP 234
Cdd:cd08570  222 IRLGVDGVITDDP 234
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 7-236 3.78e-39

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


Pssm-ID: 176508 [Multi-domain]  Cd Length: 235  Bit Score: 135.61  E-value: 3.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFGEef 86
Cdd:cd08565    2 AGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLRDSFGE-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  87 kntSIPDIDEFMDYVKDKNLLVNIELKNGIIN--YKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKEI--------- 155
Cdd:cd08565   80 ---KIPTLEEVLALFAPSGLELHVEIKTDADGtpYPGAAALAAATLRRHGLLERSVLTSFDPAVLTEVRKHpgvrtlgsv 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 156 --DSSIKTGLLYAANIY---KVHEYAQKVSADALHPyfpsvmneDIVKEIKdSNIAINTYTVNEEKYMRRLMELGIDGII 230
Cdd:cd08565  157 deDMLERLGGELPFLTAtalKAHIVAVEQSLLAATW--------ELVRAAV-PGLRLGVWTVNDDSLIRYWLACGVRQLT 227


                 ....*.
gi 736016516 231 TNYPDV 236
Cdd:cd08565  228 TDRPDL 233
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 1-234 1.58e-33

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: 121.81  E-value: 1.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   1 MVKSLNIAHRG--FSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCH--------DEMVYRTTNGQGSIKDLTY 70
Cdd:cd08564    1 MVRPIIVGHRGagCSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteddtnpDTSIQLDDSGFKNINDLSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  71 DEIKKL------DAGIKFGEEFKNTSIPDIDEFMDYVKDKnLLVNIELKNgiiNYKNLEKRIIEKIYEYGLKDNVILSSF 144
Cdd:cd08564   81 DEITRLhfkqlfDEKPCGADEIKGEKIPTLEDVLVTFKDK-LKYNIELKG---REVGLGERVLNLVEKYGMILQVHFSSF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 145 NHYSMVK-VKEIDS---SIKTGLLY----AANIYKVHEYAQKVSADALHPYFpSVMNEDIVKEIKDSNIAINTYTV---- 212
Cdd:cd08564  157 LHYDRLDlLKALRPnklNVPIALLFnevkSPSPLDFLEQAKYYNATWVNFSY-DFWTEEFVKKAHENGLKVMTYFDepvn 235

                        250       260
                 ....*....|....*....|...
gi 736016516 213 -NEEKYmRRLMELGIDGIITNYP 234
Cdd:cd08564  236 dNEEDY-KVYLELGVDCICPNDP 257
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 3-243 1.70e-33

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: 122.71  E-value: 1.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   3 KSLNIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKF 82
Cdd:cd08612   26 PCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLPPYLEKLEV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  83 --------GEEFKNTSIPDIDEFMDyvKDKNLLVNIELKNgiiNYKNLEKRIIEKIYEYGLKDNVILSSFNHYSMVKVKE 154
Cdd:cd08612  106 tfspgdycVPKGSDRRIPLLEEVFE--AFPDTPINIDIKV---ENDELIKKVSDLVRKYKREDITVWGSFNDEIVKKCHK 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 155 IDSSIK----------------TGLL------------YAANIYKVHEYAQKVSADA---LHPYFPSVMNEDIVKEIKDS 203
Cdd:cd08612  181 ENPNIPlffslkrvllllllyyTGLLpfipikesfleiPMPSIFLKTYFPKSMSRLNrfvLFLIDWLLMRPSLFRHLQKR 260

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 736016516 204 NIAINTYTVNEEKYMRRLMELGIDGIITNYPDVLKRIIDE 243
Cdd:cd08612  261 GIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLREFLDK 300
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 7-237 4.67e-32

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 117.73  E-value: 4.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGfSGKY-PENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFGEE 85
Cdd:PRK09454  11 VAHRG-GGKLaPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  86 FKNTSIPDIDEFMDYVKDKNLLVNIELK--NGiinyknLEKRIIEKI------YEYGLKDNVILSSFNHYSMVKVKEIDS 157
Cdd:PRK09454  90 FAGEPLPTLSQVAARCRAHGMAANIEIKptTG------REAETGRVValaaraLWAGAAVPPLLSSFSEDALEAARQAAP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 158 SIKTGLLYAANIYKVHEYAQKVSADALHPYFpSVMNEDIVKEIKDSNIAINTYTVNEEKYMRRLMELGIDGIITNYPDVL 237
Cdd:PRK09454 164 ELPRGLLLDEWPDDWLELTRRLGCVSLHLNH-KLLDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTDRIDLI 242
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 7-234 1.68e-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: 176523 [Multi-domain]  Cd Length: 229  Bit Score: 113.20  E-value: 1.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDA--GIKFGE 84
Cdd:cd08581    2 VAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVaePARFGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  85 EFKNTSIPDIDEFMDYVKDK-NLLVNIELKNGIINYKNLEkRIIEKIYE--YGLKDNVILSSFNHYSMVKVKEIdSSIKT 161
Cdd:cd08581   82 RFAGEPLPSLAAVVQWLAQHpQVTLFVEIKTESLDRFGLE-RVVDKVLRalPAVAAQRVLISFDYDLLALAKQQ-GGPRT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 162 G-LLYAANIykvheyAQKVSADALHP-YFpsVMNEDIVKEIKD-----SNIAIntYTVNEEKYMRRLMELGIDGIITNYP 234
Cdd:cd08581  160 GwVLPDWDD------ASLAEADELQPdYL--FCDKNLLPDTGDlwagtWKWVI--YEVNEPAEALALAARGVALIETDNI 229
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 3-215 3.98e-25

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: 99.69  E-value: 3.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   3 KSLNIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNgqgsIKDL------------TY 70
Cdd:cd08574    1 KPALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTN----VADVfperaherasmfTW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  71 DEIKKLDAGIKF----------------GEEFKNTSIPDIDEFMDYVKDKNLLVNIELKNGIIN---YKNLEKRIIEKIY 131
Cdd:cd08574   77 TDLQQLNAGQWFlkddpfwtasslsesdREEAGNQSIPSLAELLRLAKKHNKSVIFDLRRPPPNhpyYQSYVNITLDTIL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 132 EYGLKDNVILSSFNHY-SMVKVKeidssiktgllyAANIYKVheYAQKVSADALHPYFPSVMN--------EDIvKEIKD 202
Cdd:cd08574  157 ASGIPQHQVFWLPDEYrALVRKV------------APGFQQV--SGRKLPVESLRENGISRLNleysqlsaQEI-REYSK 221

                        250
                 ....*....|...
gi 736016516 203 SNIAINTYTVNEE 215
Cdd:cd08574  222 ANISVNLYVVNEP 234
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 7-164 1.50e-23

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: 95.08  E-value: 1.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGK---YPENTMIAFRKAVEAGCdGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLdagikfg 83
Cdd:cd08585    7 IAHRGLHDRdagIPENSLSAFRAAAEAGY-GIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRAL------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  84 eEFKNTS--IPDIDEFMDYVKDKNLLVnIELKNGIINYKNLEKRIIEKIYEYglKDNVILSSFNHYSMVKVKEIDSSIKT 161
Cdd:cd08585   79 -RLLGTDehIPTLDEVLELVAGRVPLL-IELKSCGGGDGGLERRVLAALKDY--KGPAAIMSFDPRVVRWFRKLAPGIPR 154


                 ...
gi 736016516 162 GLL 164
Cdd:cd08585  155 GQL 157
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 6-233 1.43e-21

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: 88.26  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   6 NIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGqgsIKDLTYDEIkkldagIKFGEE 85
Cdd:cd08555    1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAG---ILPPTLEEV------LELIAD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  86 FKNTSIPDIdefmdyvkdknlLVNIELKNGIINYKNLEKRIIE---KIYEYGLKDNVILSSFNHYSMVKVKEIDSSIKTG 162
Cdd:cd08555   72 YLKNPDYTI------------ILSLEIKQDSPEYDEFLAKVLKelrVYFDYDLRGKVVLSSFNALGVDYYNFSSKLIKDT 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736016516 163 LLyaaniykvheyaqkvsadalhpyfpsvmnediVKEIKDSNIAINTYTVNEEKYM-RRLMELGIDGIITNY 233
Cdd:cd08555  140 EL--------------------------------IASANKLGLLSRIWTVNDNNEIiNKFLNLGVDGLITDF 179
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 5-231 5.44e-21

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: 89.26  E-value: 5.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   5 LNIAHRGFsGK---------YPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGS----------I 65
Cdd:cd08572    1 LVIGHRGL-GKnyasgslagIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSKTGsdegelievpI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  66 KDLTYDEIKKL----------DAGIKFGEEFKN--------TSIPDIDEFMDYVkDKNLLVNIELKNGIINYKNLEK--- 124
Cdd:cd08572   80 HDLTLEQLKELglqhisalkrKALTRKAKGPKPnpwgmdehDPFPTLQEVLEQV-PKDLGFNIEIKYPQLLEDGEGEltp 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 125 ---------RIIEKIYEYGLKDNVILSSFNHY--SMVKVK----------EIDSSIKT-GLLYAANIYKVHEYAQK---- 178
Cdd:cd08572  159 yfernafvdTILAVVFEHAGGRRIIFSSFDPDicIMLRLKqnkypvlfltNGGTNEVEhMDPRRRSLQAAVNFALAegll 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 736016516 179 -VSADAlhpyFPSVMNEDIVKEIKDSNIAINTY--TVNEEKYMRRLMELGIDGIIT 231
Cdd:cd08572  239 gVVLHA----EDLLKNPSLISLVKALGLVLFTYgdDNNDPENVKKQKELGVDGVIY 290
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 5-234 6.04e-20

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: 86.58  E-value: 6.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   5 LNIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTN---------------GQGSIK--- 66
Cdd:cd08602    2 LVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDvadhpefadrkttktVDGVNVtgw 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  67 ---DLTYDEIKKLDAGIKFGEEFKNT----SIPDIDEFMDYVKDKNLLVN------IELKNGIinY------KNLEKRII 127
Cdd:cd08602   82 fteDFTLAELKTLRARQRLPYRDQSYdgqfPIPTFEEIIALAKAASAATGrtvgiyPEIKHPT--YfnaplgLPMEDKLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 128 EKIYEYGLKDN---VILSSFNHYSMVKVKEIDSSIKTGLLYAANIY-------KVHEYAQKVS----------ADALHPY 187
Cdd:cd08602  160 ETLKKYGYTGKkapVFIQSFEVTNLKYLRNKTDLPLVQLIDDATIPpqdtpegDSRTYADLTTdaglkeiatyADGIGPW 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 188 ----FPSVMNE------DIVKEIKDSNIAINTYTVNEEKY-------------MRRLMELGIDGIITNYP 234
Cdd:cd08602  240 kdliIPSDANGrlgtptDLVEDAHAAGLQVHPYTFRNENTflppdffgdpyaeYRAFLDAGVDGLFTDFP 309
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 7-96 8.61e-20

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: 85.46  E-value: 8.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKFGEEF 86
Cdd:cd08580    4 VAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAGYNFKPEG 83

                         90
                 ....*....|....*.
gi 736016516  87 ------KNTSIPDIDE 96
Cdd:cd08580   84 gypyrgKPVGIPTLEQ 99
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 7-240 5.43e-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: 84.20  E-value: 5.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSI--------KDLTYDEIKKLDA 78
Cdd:cd08609   30 VGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKDVFpgrdaagsNNFTWTELKTLNA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  79 GIKFGE----------------EFKNTSIPDIDEFMDYVKDKNLLVNIELK---NGIINYKNLEKRIIEKIYEYGLKDNV 139
Cdd:cd08609  110 GSWFLErrpfwtlsslseedrrEADNQTVPSLSELLDLAKKHNVSIMFDLRnenNSHVFYSSFVFYTLETILKLGIPPDK 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 140 IL---SSFNHysmvKVKEIDSSIKtgllyaaNIYKVHEYAQKVSADALHPYFPSVMNEDIvKEIKDSNIAINTYTVNEEK 216
Cdd:cd08609  190 VWwlpDEYRH----DVMKMEPGFK-------QVYGRQKEMLMDGGNFMNLPYQDLSALEI-KELRKDNVSVNLWVVNEPW 257

                        250       260
                 ....*....|....*....|....
gi 736016516 217 YMRRLMELGIDGIITNYPDVLKRI 240
Cdd:cd08609  258 LFSLLWCSGVSSVTTNACQLLKDM 281
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 7-235 2.19e-17

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: 79.74  E-value: 2.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTN------------GQGSIKDLTYDEIK 74
Cdd:cd08600    4 IAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNvaekfpdrkrkdGRYYVIDFTLDELK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  75 KL------DAGIKFGEEF---------KNTSIPDIDEFMDYVK------DKNLLVNIELKNGII---NYKNLEKRIIEKI 130
Cdd:cd08600   84 SLsvterfDIENGKKVQVypnrfplwkSDFKIHTLEEEIELIQglnkstGKNVGIYPEIKAPWFhhqEGKDIAAATLEVL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 131 YEYGLK---DNVILSSFNHYSMVKVKEI-----DSSIKTGLLYAAN--------------------IYKVHEYAQKVS-A 181
Cdd:cd08600  164 KKYGYTsknDKVYLQTFDPNELKRIKNEllpkmGMDLKLVQLIAYTdwgetqekdpggwvnydydwMFTKGGLKEIAKyA 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736016516 182 DALHPYFPSVMNE----------DIVKEIKDSNIAINTYTVNEE---KYMRRLMEL--------GIDGIITNYPD 235
Cdd:cd08600  244 DGVGPWYSMIIEEksskgnivltDLVKDAHEAGLEVHPYTVRKDalpEYAKDADQLldallnkaGVDGVFTDFPD 318
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 7-240 3.28e-17

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: 79.15  E-value: 3.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNgqgsIKDL------------TYDEIK 74
Cdd:cd08610   26 IGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTN----IGEVqpesacenpaffNWDFLS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  75 KLDAGIKF----------------GEEFKNTSIPDIDEFMDYVKDKNLLVNIELkngiinYKNLEK---------RIIEK 129
Cdd:cd08610  102 TLNAGKWFvkprpfynmkplseadKERARNQSIPKLSNFLRLAEKENKLVIFDL------YRPPPKhpyrhtwirRVLEV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 130 IY-EYGLKDNVILSSFNHYSMVkVKEIDSSIKTGLLYAANIykvhEYAQKVSADALHPYFPSVMNEDIvKEIKDSNIAIN 208
Cdd:cd08610  176 ILnEVGIEQHLVLWLPAHDRQY-VQSVAPGFKQHVGRKVPI----ETLLKNNISILNLAYKKLFSNDI-RDYKAANIHTN 249

                        250       260       270
                 ....*....|....*....|....*....|..
gi 736016516 209 TYTVNEEKYMRRLMELGIDGIITNYPDVLKRI 240
Cdd:cd08610  250 VYVINEPWLFSLAWCSGIHSVTTNNIHLLKQL 281
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 5-230 2.09e-15

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: 73.87  E-value: 2.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   5 LNIAHRG-------FSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGS----------IKD 67
Cdd:cd08607    1 LDVGHRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDsdrddllevpVKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  68 LTYDEIKKLD-AGIKFGEEFKNTSIPDIDEFMDYVK-----------DKNLLVNIELK------NG--------IINYKN 121
Cdd:cd08607   81 LTYEQLKLLKlFHISALKVKEYKSVEEDEDPPEHQPfptlsdvlesvPEDVGFNIEIKwpqqqkDGsweselftYFDRNL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 122 LEKRIIEKIYEYGLKDNVILSSFnhysmvkvkeiDSSIKTGLLYAANIYKVHEYAQKVS------ADALHPYFPSVMN-- 193
Cdd:cd08607  161 FVDIILKIVLEHAGKRRIIFSSF-----------DADICTMLRFKQNKYPVLFLTQGKTqrypefMDLRTRTFEIAVNfa 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 736016516 194 ------------EDI------VKEIKDSNIAINTY--TVNEEKYMRRLMELGIDGII 230
Cdd:cd08607  230 qaeellgvnlhsEDLlkdpsqIELAKSLGLVVFCWgdDLNDPENRKKLKELGVDGLI 286
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 16-110 3.99e-15

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: 73.16  E-value: 3.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  16 YPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYDEIKKLDAGIKF----GEEF--KNT 89
Cdd:cd08613   58 YLENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELKTLDIGYGYtadgGKTFpfRGK 137

                         90       100
                 ....*....|....*....|....
gi 736016516  90 SI---PDIDEFMDYVKDKNLLVNI 110
Cdd:cd08613  138 GVgmmPTLDEVFAAFPDRRFLINF 161
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 7-240 2.54e-11

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE2 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 5 (GDPD5)) and their metazoan homologs. Mammalian GDE2 is transmembrane protein primarily expressed in mature neurons. It is a mammalian homolog of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Mammalian GDE2 selectively hydrolyzes glycerophosphocholine (GPC) and has been characterized as GPC-GDE (EC 3.1.4.2) that contributes to osmotic regulation of cellular GPC. Mammalian GDE2 functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE2 also plays a critical role for retinoid-induced neuronal outgrowth. The catalytic activity of GDPD domain is essential for mammalian GDE2 cellular function.


Pssm-ID: 176550  Cd Length: 351  Bit Score: 62.55  E-value: 2.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNGQGSIKDLTYD--------EIKKLDA 78
Cdd:cd08608    5 IGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYEdasmfnwtDLERLNA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  79 GIKF----------------GEEFKNTSIPDIDEFMDYVKDKNLLVNIELKNGIINYKNLEKRI---IEKIYEYGLKDN- 138
Cdd:cd08608   85 GQWFlkddpfwtaqslspsdRKEAGNQSVCSLAELLELAKRYNASVLLNLRRPPPNHPYHQSWInltLKTILASGIPQEq 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 139 VILSSFNHYSMVKvkeidsSIKTGLLYAANiykvheyaQKVSADALHP--------YFPSVMNEDIvKEIKDSNIAINTY 210
Cdd:cd08608  165 VMWTPDWQRKLVR------KVAPGFQQTSG--------EKLPVASLRErgitrlnlRYTQASAQEI-RDYSASNLSVNLY 229

                        250       260       270
                 ....*....|....*....|....*....|
gi 736016516 211 TVNEEKYMRRLMELGIDGIITNYPDVLKRI 240
Cdd:cd08608  230 TVNEPWLYSLLWCSGVPSVTSDASHVLRKV 259
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 7-239 2.55e-11

Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 2 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play important an role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens. This CD includes domain II (the second GDPD domain of SHV3 and SVLs), which is necessary for SHV3 function.


Pssm-ID: 176546  Cd Length: 300  Bit Score: 62.36  E-value: 2.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGaIVVCHD--EMVYRTTNGQGSIK------------------ 66
Cdd:cd08604    4 ISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDG-VPFCLDsiNLINSTTVATSKFSnrattvpeigstsgiftf 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  67 DLTYDEIKKLDAGIK--FGEE--FKNTS------IPDIDEFMDYVKDKNL---LVNIELKNGIINYKNLE------KRII 127
Cdd:cd08604   83 DLTWSEIQTLKPAISnpYSVTglFRNPAnknagkFLTLSDFLDLAKNKSLsgvLINVENAAYLAEKKGLDvvdavlDALT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 128 EKIYEYGLKDNVILSSFNHYSMVKVKEidsSIKTGLLYAANiYKVHEYAQ------KVSADALHPYFPSVMNED------ 195
Cdd:cd08604  163 NAGYDNQTAQKVLIQSTDSSVLAAFKK---QISYERVYVVD-ETIRDASDssieeiKKFADAVVIDRGSVFPVStsfltr 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736016516 196 ---IVKEIKDSNIAINTYTVNEEkYMRR---------------LMELGIDGIITNYPDVLKR 239
Cdd:cd08604  239 qtnVVEKLQSANLTVYVEVLRNE-FVSLafdffadptveinsyVQGAGVDGFITEFPATAAR 299
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 7-87 7.36e-11

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 61.23  E-value: 7.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTN------------GQGSIKDLTYDEIK 74
Cdd:PRK11143  30 IAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDvaerfpdrarkdGRYYAIDFTLDEIK 109

                         90
                 ....*....|...
gi 736016516  75 KLdagiKFGEEFK 87
Cdd:PRK11143 110 SL----KFTEGFD 118
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 7-232 1.01e-10

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: 60.50  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFsGK------------YPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRTTNG---QGSIKDLTYD 71
Cdd:cd08605    3 IGHRGL-GMnrashqpsvgpgIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVERGGeveSSRIRDLTLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  72 EIKKLD-----------AGIKFGEEFK--------NTSIPDIDEFMDYVkDKNLLVNIELKNGIINYKNLE------KRI 126
Cdd:cd08605   82 ELKALGpqaestktstvALYRKAKDPEpepwimdvEDSIPTLEEVFSEV-PPSLGFNIELKFGDDNKTEAEelvrelRAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 127 IEKIYEYGLKDNVILSSFNHYSMVKVKEIDSSIKTGLLYAANIYkVH--------EYAQKVSADA----LHPYFPSVMNE 194
Cdd:cd08605  161 LAVCKQHAPGRRIMFSSFDPDAAVLLRALQSLYPVMFLTDCGPY-THndprrnsiEAAIQVALEGglqgIVSEVKVLLRN 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 736016516 195 -DIVKEIKDSNIAINTYTV--NEEKYMRRLMELGIDGIITN 232
Cdd:cd08605  240 pTAVSLVKASGLELGTYGKlnNDAEAVERQADLGVDGVIVD 280
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 7-111 1.45e-10

Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase (GDPD) domain present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs), which may play an important role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both, SHV3 and SVLs, have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs, which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition, the two tandem repeats show low sequence similarity to each other, suggesting they have different biochemical function. Most members of this family are Arabidopsis-specific gene products. To date, SHV3 orthologues are only found in Physcomitrella patens.


Pssm-ID: 176513  Cd Length: 302  Bit Score: 59.99  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGaIVVCHDE-------------MVYRTT------NGQG--SI 65
Cdd:cd08571    4 IARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDG-VPICLPSinldnsttiasvfPKRKKTyvvegqSTSGifSF 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 736016516  66 kDLTYDEI--KKLDAGIKFGEEFKNT------SIPDIDEFMDYVKDKN---LLVNIE 111
Cdd:cd08571   83 -DLTWAEIqtLKPIISNPFSVLFRNPrndnagKILTLEDFLTLAKPKSlsgVWINVE 138
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 7-145 1.62e-07

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL110cp and other uncharacterized fungal homologs. The product of S. cerevisiae ORF YPL110c (GDE1), YPL110cp (Gde1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL110cp has been characterized as a cytoplasmic glycerophosphocholine (GPC)-specific phosphodiesterase that selectively hydrolyzes GPC, not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate. YPL110cp has multi-domain architecture, including not only C-terminal GDPD, but also an SPX N-terminal domain along with several ankyrin repeats, which implies that YPL110cp may mediate protein-protein interactions in a variety of proteins and play a role in maintaining cellular phosphate levels. Members in this family are distantly related to S. cerevisiae YPL206cp, which selectively catalyzes the cleavage of phosphatidylglycerol (PG), not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate, and has been characterized as a PG-specific phospholipase C.


Pssm-ID: 176548 [Multi-domain]  Cd Length: 286  Bit Score: 50.91  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHRGFSGKYP--------ENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEMVYRT-TNGQgsIKDLTYDEIkkLD 77
Cdd:cd08606    5 IGHRGLGKNTAerkslqlgENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETgTDVP--IHDLTLEQF--LH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  78 AG-IKFGEEFK------NTSIPDIDEFMDYVKD------KNLLVNIELKNGI-------------INYKNLEKRIIEKIY 131
Cdd:cd08606   81 LSrMKYTVDFKkkgfkgNSRGHSIQAPFTTLEEllkklpKSVGFNIELKYPMlheaeeeevapvaIELNAFVDTVLEKVF 160

                        170
                 ....*....|....
gi 736016516 132 EYGLKDNVILSSFN 145
Cdd:cd08606  161 DYGAGRNIIFSSFT 174
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 7-233 3.51e-06

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


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 46.52  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516   7 IAHR--GFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDemvyRTTNGQGSIKDLTYDEIKKLDAgikfgE 84
Cdd:cd08583    2 IAHAmgGIDGKTYTNSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHS----WDESLLKQLGLPTSKNTKPLSY-----E 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  85 EFKNTSI------PDIDEFMDYVKDKNLLVNIelkngiINYKNLEKRIIEKIYEYGLK----------DNVILSSFNHYS 148
Cdd:cd08583   73 EFKSKKIygkytpMDFKDVIDLLKKYPDVYIV------TDTKQDDDNDIKKLYEYIVKeakevdpdllDRVIPQIYNEEM 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516 149 MVKVKEI----DSSIKTGLLYAANIYKVHEYAQKVSADALHPYFPSVmNEDIVKEIKDSNIAINTYTVNEEKYMRRLMEL 224
Cdd:cd08583  147 YEAIMSIypfkSVIYTLYRQDSIRLDEIIAFCYENGIKAVTISKNYV-NDKLIEKLNKAGIYVYVYTINDLKDAQEYKKL 225


                 ....*....
gi 736016516 225 GIDGIITNY 233
Cdd:cd08583  226 GVYGIYTDF 234
GDPD_like_SMaseD_PLD cd08576
Glycerophosphodiester phosphodiesterase-like domain of spider venom sphingomyelinases D, ...
 209-245 2.16e-05

Glycerophosphodiester phosphodiesterase-like domain of spider venom sphingomyelinases D, bacterial phospholipase D, and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase-like domain (GDPD-like) present in sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.4) from spider venom, the Corynebacterium pseudotuberculosis Phospholipase D (PLD)-like protein from pathogenic bacteria, and the Ajellomyces capsulatus H143 PLD-like protein from ascomycetes. Spider SMases D and bacterial PLD proteins catalyze the Mg2+-dependent hydrolysis of sphingomyelin producing choline and ceramide 1-phosphate (C1P), which possess a number of biological functions, such as regulating cell proliferation and apoptosis, participating in inflammatory responses, and playing a key role in phagocytosis. In the presence of Mg2+, SMases D can function as lysophospholipase D and hydrolyze lysophosphatidylcholine (LPC) to choline and lysophosphatidic acid (LPA), which is a multifunctional phospholipid involved in platelet aggregation, endothelial hyperpermeability, and pro-inflammatory responses. Loxosceles spider venoms' SMases D are the principal toxins responsible for dermonecrosis and complement dependent haemolysis induced by spider venom. Due to amino acid substitutions at the entrance to the active-site pocket, some members lack activity. The typical GDPD domain consists of a TIM barrel and a small insertion domain named as the GDPD-insertion (GDPD-I) domain, which is specific for GDPD proteins. Although proteins in this family contain a non-typical GDPD domain which lacks the GDPD-I, their catalytic mechanisms are based on Mg2+-dependent acid-base reactions similar to GDPD proteins. They might be divergent members of the GDPD family. Moreover, this family does not belong to phospholipase D (PLD) superfamily, since it lacks the conserved HKD sequence motif that characterizes the catalytic center of the PLD superfamily. It belongs to the superfamily of PLC-like phosphodiesterases.


Pssm-ID: 176518 [Multi-domain]  Cd Length: 265  Bit Score: 44.62  E-value: 2.16e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 736016516 209 TYTVNEEKYMRRLMELGIDGIITNYPDVLKRIIDESE 245
Cdd:cd08576  214 GWTSDKGSSVRKLLRLGVDGIITNYPKRIIDVLKESE 250
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 4-60 4.26e-04

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


Pssm-ID: 176503  Cd Length: 356  Bit Score: 40.87  E-value: 4.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 736016516   4 SLNIAHRGFSGKYPENTMIAFRKAVEAGCDGIETDVHITKDGAIVVCHDEM-VYRTTN 60
Cdd:cd08560   17 DFSIGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSQCdLHTTTN 74
GDPD_2 pfam13653
Glycerophosphoryl diester phosphodiesterase family; This family also includes ...
 207-235 8.38e-04

Glycerophosphoryl diester phosphodiesterase family; This family also includes glycerophosphoryl diester phosphodiesterases as well as agrocinopine synthase, the similarity to GDPD has been noted. This family appears to have weak but not significant matches to mammalian phospholipase C pfam00388, which suggests that this family may adopt a TIM barrel fold.


Pssm-ID: 433380 [Multi-domain]  Cd Length: 30  Bit Score: 35.94  E-value: 8.38e-04
                          10        20
                  ....*....|....*....|....*....
gi 736016516  207 INTYTVNEEKYMRRLMELGIDGIITNYPD 235
Cdd:pfam13653   2 VRFWTIDNKAAWKELMRLGVDGLNTDDPE 30
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 66-142 1.13e-03

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 38.35  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736016516  66 KDLTYDEIKKL-----DAGIKF-----GEEFKNtsiPDIDEFMDYVKDKNLLVNIelkngIINYKNLEKRIIEKIYEYGL 135
Cdd:COG0535   27 GELSTEEAKRIldelaELGVKVvgltgGEPLLR---PDLFELVEYAKELGIRVNL-----STNGTLLTEELAERLAEAGL 98


                 ....*..
gi 736016516 136 kDNVILS 142
Cdd:COG0535   99 -DHVTIS 104
 
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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