NCBI Conserved Domain Search

Conserved domains on [gi|503994039|ref|WP_014228033|]

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MULTISPECIES: glycerophosphodiester phosphodiesterase family protein [Klebsiella]

Protein Classification

PI-PLC domain-containing protein( domain architecture ID 49489)

PI-PLC (phosphoinositide-specific phospholipase C) domain-containing protein may hydrolyze the membrane lipid phosphatidylinositol to produce phosphorylated myo-inositol and diacylglycerol

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

PI-PLCc_GDPD_SF super family

cl14615

Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...

20-282

4.26e-134

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.

The actual alignment was detected with superfamily member cd08580:

Pssm-ID: 472694 [Multi-domain] Cd Length: 263 Bit Score: 379.75 E-value: 4.26e-134

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGWTWG 99
Cdd:cd08580    1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAGYNFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 100 GE-THPWRGKNATIPTLQSVLEQWPQTFFYIDIKSPDADPaiMAARLSEVLQKTNSLSRVRVYSTEDRYIAALPASIPH- 177
Cdd:cd08580   81 PEgGYPYRGKPVGIPTLEQVLRAFPDTPFILDMKSLPADP--QAKAVARVLERENAWSRVRIYSTNADYQDALAPYPQAr 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 178 -FVSRGETRTKLANISLSHQCQPTAASGNeyWYGLELKRKVEVVEKFTLGEGVSPATLT-WDKEAMDCFRSQGKAHIVFF 255
Cdd:cd08580  159 lFESRDVTRTRLANVAMAHQCDLPPDSGA--WAGFELRRKVTVVETFTLGEGRSPVQATlWTPAAVDCFRRNSKVKIVLF 236

                        250       260
                 ....*....|....*....|....*..
gi 503994039 256 GINSADDFRTASELGADGVMVDSPAKA 282
Cdd:cd08580  237 GINTADDYRLAKCLGADAVMVDSPAAM 263

Name

Accession

Description

Interval

E-value

GDPD_Rv2277c_like

cd08580

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...

20-282

4.26e-134

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: 379.75 E-value: 4.26e-134

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGWTWG 99
Cdd:cd08580    1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAGYNFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 100 GE-THPWRGKNATIPTLQSVLEQWPQTFFYIDIKSPDADPaiMAARLSEVLQKTNSLSRVRVYSTEDRYIAALPASIPH- 177
Cdd:cd08580   81 PEgGYPYRGKPVGIPTLEQVLRAFPDTPFILDMKSLPADP--QAKAVARVLERENAWSRVRIYSTNADYQDALAPYPQAr 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 178 -FVSRGETRTKLANISLSHQCQPTAASGNeyWYGLELKRKVEVVEKFTLGEGVSPATLT-WDKEAMDCFRSQGKAHIVFF 255
Cdd:cd08580  159 lFESRDVTRTRLANVAMAHQCDLPPDSGA--WAGFELRRKVTVVETFTLGEGRSPVQATlWTPAAVDCFRRNSKVKIVLF 236

                        250       260
                 ....*....|....*....|....*..
gi 503994039 256 GINSADDFRTASELGADGVMVDSPAKA 282
Cdd:cd08580  237 GINTADDYRLAKCLGADAVMVDSPAAM 263

UgpQ

COG0584

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];

20-285

5.18e-56

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];

Pssm-ID: 440349 [Multi-domain] Cd Length: 238 Bit Score: 180.45 E-value: 5.18e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGWtwg 99
Cdd:COG0584    3 PLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGS--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 100 gethPWRGKNATIPTLQSVLEQWP-QTFFYIDIKSPDADPAIMAARLSEVLQKTNSLSRVRVYSTEDRYIAALpasiphf 178
Cdd:COG0584   80 ----GPDFAGERIPTLEEVLELVPgDVGLNIEIKSPPAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRL------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 179 vsrgetRTKLANISLShqcqptAASGNEYWYGLELKRKVEVvekftlgEGVSPATLTWDKEAMDCFRSQGKaHIVFFGIN 258
Cdd:COG0584  149 ------RELAPDVPLG------LLVEELPADPLELARALGA-------DGVGPDYDLLTPELVAAAHAAGL-KVHVWTVN 208

                        250       260
                 ....*....|....*....|....*..
gi 503994039 259 SADDFRTASELGADGVMVDSPAKAKAW 285
Cdd:COG0584  209 DPEEMRRLLDLGVDGIITDRPDLLRAV 235

GDPD

pfam03009

Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...

25-281

4.52e-22

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: 92.08 E-value: 4.52e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039   25 HRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGwtwGGETHP 104
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIG---AGNSGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  105 WRGKNATIPTLQSVLEQWPQTFFYIDIKSPDADPAIMAARLSEVLQKTNSLSRVRVY-STEDRYIAAL--PASIPHfvsr 181
Cdd:pfam03009  78 LSGERVPFPTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEEGLIVKDLLLSVDEILAKkADPRRVIFSSfnPDELKR---- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  182 geTRTKLANISLSHQCqptaaSGNEYWYGLELKRKVEVVEKFTLGEGVSPATLTWDKEAMDcFRSQGKAhiVF-FGINSA 260
Cdd:pfam03009 154 --LRELAPKLPLVFLS-----SGRAYAEADLLERAAAFAGAPALLGEVALVDEALPDLVKR-AHARGLV--VHvWTVNNE 223

                         250       260
                  ....*....|....*....|.
gi 503994039  261 DDFRTASELGADGVMVDSPAK 281
Cdd:pfam03009 224 DEMKRLLELGVDGVITDRPDT 244

ugpQ

PRK09454

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional

20-120

3.19e-09

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional

Pssm-ID: 236524 [Multi-domain] Cd Length: 249 Bit Score: 56.10 E-value: 3.19e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGwTWg 99
Cdd:PRK09454   8 PRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAG-SW- 85

                         90       100
                 ....*....|....*....|.
gi 503994039 100 getHPWRGKNATIPTLQSVLE 120
Cdd:PRK09454  86 ---FSAAFAGEPLPTLSQVAA 103

Name

Accession

Description

Interval

E-value

GDPD_Rv2277c_like

cd08580

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...

20-282

4.26e-134

Pssm-ID: 176522 [Multi-domain] Cd Length: 263 Bit Score: 379.75 E-value: 4.26e-134

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGWTWG 99
Cdd:cd08580    1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAGYNFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 100 GE-THPWRGKNATIPTLQSVLEQWPQTFFYIDIKSPDADPaiMAARLSEVLQKTNSLSRVRVYSTEDRYIAALPASIPH- 177
Cdd:cd08580   81 PEgGYPYRGKPVGIPTLEQVLRAFPDTPFILDMKSLPADP--QAKAVARVLERENAWSRVRIYSTNADYQDALAPYPQAr 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 178 -FVSRGETRTKLANISLSHQCQPTAASGNeyWYGLELKRKVEVVEKFTLGEGVSPATLT-WDKEAMDCFRSQGKAHIVFF 255
Cdd:cd08580  159 lFESRDVTRTRLANVAMAHQCDLPPDSGA--WAGFELRRKVTVVETFTLGEGRSPVQATlWTPAAVDCFRRNSKVKIVLF 236

                        250       260
                 ....*....|....*....|....*..
gi 503994039 256 GINSADDFRTASELGADGVMVDSPAKA 282
Cdd:cd08580  237 GINTADDYRLAKCLGADAVMVDSPAAM 263

GDPD_GDE4_like

cd08575

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

20-282

2.78e-97

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: 286.42 E-value: 2.78e-97

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGWTW- 98
Cdd:cd08575    1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGYt 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  99 --GGET-HPWRGKNATIPTLQSVLEQWPQTFFYIDIKSPDADPAImaARLSEVLQKTNSLSRVRVYSTEDRYIAALPASI 175
Cdd:cd08575   81 fdGGKTgYPRGGGDGRIPTLEEVFKAFPDTPINIDIKSPDAEELI--AAVLDLLEKYKREDRTVWGSTNPEYLRALHPEN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 176 PH-FVSRGETRTKLANISLSHQCQPTAASGNeyWYGLELKRKVEVVEKFTLGEGVS-PATLTWDKEAMDCFRSQGkAHIV 253
Cdd:cd08575  159 PNlFESFSMTRCLLLYLALGYTGLLPFVPIK--ESFFEIPRPVIVLETFTLGEGASiVAALLWWPNLFDHLRKRG-IQVY 235

                        250       260
                 ....*....|....*....|....*....
gi 503994039 254 FFGINSADDFRTASELGADGVMVDSPAKA 282
Cdd:cd08575  236 LWVLNDEEDFEEAFDLGADGVMTDSPTKL 264

UgpQ

COG0584

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];

20-285

5.18e-56

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];

Pssm-ID: 440349 [Multi-domain] Cd Length: 238 Bit Score: 180.45 E-value: 5.18e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGWtwg 99
Cdd:COG0584    3 PLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGS--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 100 gethPWRGKNATIPTLQSVLEQWP-QTFFYIDIKSPDADPAIMAARLSEVLQKTNSLSRVRVYSTEDRYIAALpasiphf 178
Cdd:COG0584   80 ----GPDFAGERIPTLEEVLELVPgDVGLNIEIKSPPAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRL------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 179 vsrgetRTKLANISLShqcqptAASGNEYWYGLELKRKVEVvekftlgEGVSPATLTWDKEAMDCFRSQGKaHIVFFGIN 258
Cdd:COG0584  149 ------RELAPDVPLG------LLVEELPADPLELARALGA-------DGVGPDYDLLTPELVAAAHAAGL-KVHVWTVN 208

                        250       260
                 ....*....|....*....|....*..
gi 503994039 259 SADDFRTASELGADGVMVDSPAKAKAW 285
Cdd:COG0584  209 DPEEMRRLLDLGVDGIITDRPDLLRAV 235

GDPD_cytoplasmic_ScUgpQ2_like

cd08561

Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...

23-284

5.50e-41

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: 142.01 E-value: 5.50e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  23 IAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGWTW---G 99
Cdd:cd08561    2 IAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFtddG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 100 GETHPWRGKNATIPTLQSVLEQWPQTFFYIDIKspDADPAImAARLSEVLQKTNSLSRVRVYSTED---RYIAALPASIP 176
Cdd:cd08561   82 GRTYPYRGQGIRIPTLEELFEAFPDVRLNIEIK--DDGPAA-AAALADLIERYGAQDRVLVASFSDrvlRRFRRLCPRVA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 177 HFVSRGETR--TKLANISLSHQCQP--TAASGNEYWYGLELkrkvevvekftlgegVSPATLTWdkeamdcFRSQGKaHI 252
Cdd:cd08561  159 TSAGEGEVAafVLASRLGLGSLYSPpyDALQIPVRYGGVPL---------------VTPRFVRA-------AHAAGL-EV 215

                        250       260       270
                 ....*....|....*....|....*....|..
gi 503994039 253 VFFGINSADDFRTASELGADGVMVDSPAKAKA 284
Cdd:cd08561  216 HVWTVNDPAEMRRLLDLGVDGIITDRPDLLLE 247

GDPD_SaGlpQ_like

cd08601

Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...

23-151

3.32e-25

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: 100.85 E-value: 3.32e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  23 IAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLS--ALTDHTGKISSFSAAELTRMDAGwTWGG 100
Cdd:cd08601    4 IAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDrtTNIERPGPVKDYTLAEIKQLDAG-SWFN 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 503994039 101 ETHPWRGK----NATIPTLQSVLEQW-PQTFFYIDIKSPDADPAiMAARLSEVLQK 151
Cdd:cd08601   83 KAYPEYAResysGLKVPTLEEVIERYgGRANYYIETKSPDLYPG-MEEKLLATLDK 137

GDPD

cd08556

Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...

22-277

2.16e-23

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: 94.25 E-value: 2.16e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  22 LIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYrpsdlsaltdHtgkissfsaaeltrmDagwtwgge 101
Cdd:cd08556    1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVI----------H---------------D-------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 102 thpwrgknatIPTLQSVLEQWPQ-TFFYIDIKSPDADPAImAARLSEVLQKTNSLSRVRVYSTEDRYIAALPASIPHFvs 180
Cdd:cd08556   48 ----------IPTLEEVLELVKGgVGLNIELKEPTRYPGL-EAKVAELLREYGLEERVVVSSFDHEALRALKELDPEV-- 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 181 rgetrtklanislshqcqPTAAsgneYWYGLELKRKVEVVEKFTLGEGVSPATLTWDKEAMDCFRSQGKAhIVFFGINSA 260
Cdd:cd08556  115 ------------------PTGL----LVDKPPLDPLLAELARALGADAVNPHYKLLTPELVRAAHAAGLK-VYVWTVNDP 171

                        250
                 ....*....|....*..
gi 503994039 261 DDFRTASELGADGVMVD 277
Cdd:cd08556  172 EDARRLLALGVDGIITD 188

GDPD_memb_like

cd08579

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...

22-176

5.65e-23

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: 93.76 E-value: 5.65e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  22 LIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGwTWGGE 101
Cdd:cd08579    1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIG-ENGHG 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503994039 102 THpwrgknatIPTLQSVLE---QWPQTfFYIDIKSPDADPAIMAARLSEVLQKTNSLSRVRVYSTEDRYIAALPASIP 176
Cdd:cd08579   80 AK--------IPSLDEYLAlakGLKQK-LLIELKPHGHDSPDLVEKFVKLYKQNLIENQHQVHSLDYRVIEKVKKLDP 148

GDPD_AtGDE_like

cd08566

Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...

21-171

7.77e-23

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: 93.91 E-value: 7.77e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  21 QLIAHRGGTGD-APENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGWTWG 99
Cdd:cd08566    1 LVVAHRGGWGAgAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKDGDG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994039 100 GEThpwrgkNATIPTLQSVLEQWPQ-TFFYIDIKSPDADPAImaarlsEVLQKTNSLSRVRVYSTEDRYIAAL 171
Cdd:cd08566   81 EVT------DEKVPTLEEALAWAKGkILLNLDLKDADLDEVI------ALVKKHGALDQVIFKSYSEEQAKEL 141

GDPD

pfam03009

Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...

25-281

4.52e-22

Pssm-ID: 397241 [Multi-domain] Cd Length: 244 Bit Score: 92.08 E-value: 4.52e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039   25 HRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGwtwGGETHP 104
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIG---AGNSGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  105 WRGKNATIPTLQSVLEQWPQTFFYIDIKSPDADPAIMAARLSEVLQKTNSLSRVRVY-STEDRYIAAL--PASIPHfvsr 181
Cdd:pfam03009  78 LSGERVPFPTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEEGLIVKDLLLSVDEILAKkADPRRVIFSSfnPDELKR---- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  182 geTRTKLANISLSHQCqptaaSGNEYWYGLELKRKVEVVEKFTLGEGVSPATLTWDKEAMDcFRSQGKAhiVF-FGINSA 260
Cdd:pfam03009 154 --LRELAPKLPLVFLS-----SGRAYAEADLLERAAAFAGAPALLGEVALVDEALPDLVKR-AHARGLV--VHvWTVNNE 223

                         250       260
                  ....*....|....*....|.
gi 503994039  261 DDFRTASELGADGVMVDSPAK 281
Cdd:pfam03009 224 DEMKRLLELGVDGVITDRPDT 244

GDPD_TtGDE_like

cd08563

Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...

20-279

1.68e-21

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: 90.31 E-value: 1.68e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGWTWG 99
Cdd:cd08563    1 TLIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 100 GethpwRGKNATIPTLQSVLEQWPQTFFY--IDIKSpDA--DPAImAARLSEVLQKTNSLSRVrVYSTEDRYiaalpasi 175
Cdd:cd08563   81 E-----KFTGEKIPTLEEVLDLLKDKDLLlnIEIKT-DVihYPGI-EKKVLELVKEYNLEDRV-IFSSFNHE-------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 176 phfvsrgetrtKLANIslsHQCQPTAASGNEYWYGL----ELKRKVEVvekftlgEGVSPATLTWDKEAMDCFRSQGKAH 251
Cdd:cd08563  145 -----------SLKRL---KKLDPKIKLALLYETGLqdpkDYAKKIGA-------DSLHPDFKLLTEEVVEELKKRGIPV 203

                        250       260
                 ....*....|....*....|....*...
gi 503994039 252 IVFFgINSADDFRTASELGADGVMVDSP 279
Cdd:cd08563  204 RLWT-VNEEEDMKRLKDLGVDGIITNYP 230

GDPD_like_1

cd08581

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...

22-150

9.15e-20

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity 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: 85.46 E-value: 9.15e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  22 LIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDA--GWTWG 99
Cdd:cd08581    1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVaePARFG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503994039 100 GETHPwrgknATIPTLQSV---LEQWPQTFFYIDIKSPDAD---PAIMAARLSEVLQ 150
Cdd:cd08581   81 SRFAG-----EPLPSLAAVvqwLAQHPQVTLFVEIKTESLDrfgLERVVDKVLRALP 132

GDPD_EcUgpQ_like

cd08562

Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...

22-120

2.50e-19

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: 84.20 E-value: 2.50e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  22 LIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGwTWGGE 101
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAG-SWFSP 79

                         90
                 ....*....|....*....
gi 503994039 102 thpwRGKNATIPTLQSVLE 120
Cdd:cd08562   80 ----EFAGEPIPTLADVLE 94

GDPD_GDE1

cd08573

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

22-155

3.31e-19

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: 84.62 E-value: 3.31e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  22 LIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAgwtwgGE 101
Cdd:cd08573    1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNA-----AA 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 503994039 102 THPWRGK--NATIPTLQSVLEQWPQ--TFFYIDIKSPDADpaiMAARLSEVLQKTNSL 155
Cdd:cd08573   76 KHRLSSRfpGEKIPTLEEAVKECLEnnLRMIFDVKSNSSK---LVDALKNLFKKYPGL 130

GDPD_GDE4_like_1

cd08613

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...

19-189

3.74e-19

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: 85.49 E-value: 3.74e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  19 APQLIAHRG----------------------GTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTD 76
Cdd:cd08613   23 KPKLLAHRGlaqtfdregvendtctaeridpPTHDYLENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  77 HTGKISSFSAAELTRMDAGWTW---GGETHPWRGKNA-TIPTLQSVLEQWPQTFFYIDIKSPDADPAI-MAARLSEVLQK 151
Cdd:cd08613  103 GSGVTRDHTMAELKTLDIGYGYtadGGKTFPFRGKGVgMMPTLDEVFAAFPDRRFLINFKSDDAAEGElLAEKLATLPRK 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 503994039 152 tnslsRVRVYST--EDRYIAALPASIP--HFVSRGETRTKLA 189
Cdd:cd08613  183 -----RLQVLTVygGDKPIAALRELTPdlRTLSKASMKDCLI 219

GDPD_periplasmic_GlpQ_like

cd08559

Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...

20-151

3.53e-18

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: 82.32 E-value: 3.53e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTD------------HTGKISSFSAA 87
Cdd:cd08559    1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNvaehfpfrgrkdTGYFVIDFTLA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994039  88 ELTRMDAGwTWGGETHPWRGK----NATIPTLQSVLE--------QWPQTFFYIDIKSPDADPAI---MAARLSEVLQK 151
Cdd:cd08559   81 ELKTLRAG-SWFNQRYPERAPsyygGFKIPTLEEVIElaqglnksTGRNVGIYPETKHPTFHKQEgpdIEEKLLEVLKK 158

GDPD_like_2

cd08582

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...

22-148

1.84e-17

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity to Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.

Pssm-ID: 176524 [Multi-domain] Cd Length: 233 Bit Score: 79.28 E-value: 1.84e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  22 LIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGwTWGGE 101
Cdd:cd08582    1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIG-SWKGE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 503994039 102 thpwRGKNATIPTLQSVLE---QWPQTFFyIDIKSPDADPAIMAARLSEV 148
Cdd:cd08582   80 ----SYKGEKVPTLEEYLAivpKYGKKLF-IEIKHPRRGPEAEEELLKLL 124

GDPD_like_3

cd08585

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...

23-149

7.01e-16

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: 75.05 E-value: 7.01e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  23 IAHRG---GTGDAPENTLPAIKLALEnKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRmdagwtwg 99
Cdd:cd08585    7 IAHRGlhdRDAGIPENSLSAFRAAAE-AGYGIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRA-------- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503994039 100 getHPWRGKNATIPTLQSVLEQWP-QTFFYIDIKSPDADPAIMAARLSEVL 149
Cdd:cd08585   78 ---LRLLGTDEHIPTLDEVLELVAgRVPLLIELKSCGGGDGGLERRVLAAL 125

GDPD_GDE4

cd08612

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

23-285

7.53e-16

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE4 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1)) and similar proteins. Mammalian GDE4 is a transmembrane protein whose cellular function has not yet been elucidated. It is expressed widely, including in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. It is also expressed in the growth cones in neuroblastoma Neuro2a cells, which suggests GDE4 may play some distinct role from other members of the GDE family.

Pssm-ID: 176553 [Multi-domain] Cd Length: 300 Bit Score: 75.71 E-value: 7.53e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  23 IAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAEL----TRMDAGWtW 98
Cdd:cd08612   30 ISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLppylEKLEVTF-S 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  99 GGETHPWRGKNATIPTLQSVLEQWPQTFFYIDIKSPDadpaimaarlSEVLQKTNSLsrVRVYSTEDryIAALPASIPHF 178
Cdd:cd08612  109 PGDYCVPKGSDRRIPLLEEVFEAFPDTPINIDIKVEN----------DELIKKVSDL--VRKYKRED--ITVWGSFNDEI 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 179 VSrgetRTKLANISLSHQCQPTAASGNEYWYGLELKRKVEVVEKFTLGEGVSPATLTWDKEAMDCFrSQGKAHIVFF--- 255
Cdd:cd08612  175 VK----KCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYFPKSMSRL-NRFVLFLIDWllm 249

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 503994039 256 -----------GI-------NSADDFRTASELGADGVMVDSPAKAKAW 285
Cdd:cd08612  250 rpslfrhlqkrGIqvygwvlNDEEEFERAFELGADGVMTDYPTKLREF 297

GDPD_TmGDE_like

cd08568

Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...

22-166

2.41e-14

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: 70.40 E-value: 2.41e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  22 LIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAgwtwGGE 101
Cdd:cd08568    2 ILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHP----GGE 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994039 102 thpwrgknaTIPTLQSVLEQWPQT-FFYIDIKSPDAdpaimAARLSEVLQKTNSLSRVrVYSTEDR 166
Cdd:cd08568   78 ---------LIPTLEEVFRALPNDaIINVEIKDIDA-----VEPVLEIVEKFNALDRV-IFSSFNH 128

GDPD_SpGDE_like

cd08567

Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...

20-279

3.03e-14

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: 70.80 E-value: 3.03e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALT--DHTGK--------ISSFSAAEL 89
Cdd:cd08567    1 FDLQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDItrDPDGAwlpyegpaLYELTLAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  90 TRMDAGWTWGGETHPWRGKNAT------IPTLQSVLE----QWPQTFFY-IDIKS------PDADPAIMAARLSEVLQKT 152
Cdd:cd08567   81 KQLDVGEKRPGSDYAKLFPEQIpvpgtrIPTLEEVFAlvekYGNQKVRFnIETKSdpdrdiLHPPPEEFVDAVLAVIRKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 153 NSLSRVRVYSTEDRyiaALPAsiphfvsrgetrtklanislSHQCQPTAASGneywYGLELKRKVEVVE--KFTLGEGVS 230
Cdd:cd08567  161 GLEDRVVLQSFDWR---TLQE--------------------VRRLAPDIPTV----ALTEETTLGNLPRaaKKLGADIWS 213

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 503994039 231 PATLTWDKEAMDCFRSQGkAHIVFFGINSADDFRTASELGADGVMVDSP 279
Cdd:cd08567  214 PYFTLVTKELVDEAHALG-LKVVPWTVNDPEDMARLIDLGVDGIITDYP 261

GDPD_GDE_2_3_6

cd08574

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

19-120

3.13e-13

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: 67.72 E-value: 3.13e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  19 APQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTD---------HTGKiSSFSAAEL 89
Cdd:cd08574    1 KPALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNvadvfperaHERA-SMFTWTDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 503994039  90 TRMDAG---------WTWGGETHP--WRGKNATIPTLQSVLE 120
Cdd:cd08574   80 QQLNAGqwflkddpfWTASSLSESdrEEAGNQSIPSLAELLR 121

GDPD_YPL206cp_fungi

cd08570

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...

23-279

8.59e-12

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: 63.39 E-value: 8.59e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  23 IAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSaaeltrmdagwTWGGET 102
Cdd:cd08570    2 IGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDS-----------TWDELS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 103 HpWRGKNA---TIPTLQSVLE-----QWPQTFFYIDIKsPDADPAIMAARLSEVLQKTNSLS----RVRVYSTEDRYIAA 170
Cdd:cd08570   71 H-LRTIEEphqPMPTLKDVLEwlvehELPDVKLMLDIK-RDNDPEILFKLIAEMLAVKPDLDfwreRIILGLWHLDFLKY 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039 171 LPASIPHFvsrgetrtKLANISLSHQCQptaasgneywyglelKRKVEVVEKFTlgeGVS---PATLT-WDKEAMDCFRS 246
Cdd:cd08570  149 GKEVLPGF--------PVFHIGFSLDYA---------------RHFLNYSEKLV---GISmhfVSLWGpFGQAFLPELKK 202

                        250       260       270
                 ....*....|....*....|....*....|....
gi 503994039 247 QGKAhiVF-FGINSADDFRTASELGADGVMVDSP 279
Cdd:cd08570  203 NGKK--VFvWTVNTEEDMRYAIRLGVDGVITDDP 234

GDPD_pAtGDE_like

cd08565

Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...

23-137

1.18e-10

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: 60.11 E-value: 1.18e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  23 IAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGWTWGget 102
Cdd:cd08565    2 AGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLRDSFG--- 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503994039 103 hpwrgknATIPTLQSVLE--QWPQTFFYIDIKsPDAD 137
Cdd:cd08565   79 -------EKIPTLEEVLAlfAPSGLELHVEIK-TDAD 107

GDPD_GDE3

cd08609

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

20-120

1.51e-10

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: 60.71 E-value: 1.51e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKI--------SSFSAAELTR 91
Cdd:cd08609   27 PALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKDVFpgrdaagsNNFTWTELKT 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 503994039  92 MDAG---------WTWGGETHPWR--GKNATIPTLQSVLE 120
Cdd:cd08609  107 LNAGswflerrpfWTLSSLSEEDRreADNQTVPSLSELLD 146

GDPD_GDE2

cd08608

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

19-120

1.07e-09

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: 58.32 E-value: 1.07e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  19 APQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKI--------SSFSAAELT 90
Cdd:cd08608    1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFperqyedaSMFNWTDLE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 503994039  91 RMDAG---------WTWG--GETHPWRGKNATIPTLQSVLE 120
Cdd:cd08608   81 RLNAGqwflkddpfWTAQslSPSDRKEAGNQSVCSLAELLE 121

ugpQ

PRK09454

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional

20-120

3.19e-09

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional

Pssm-ID: 236524 [Multi-domain] Cd Length: 249 Bit Score: 56.10 E-value: 3.19e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGKISSFSAAELTRMDAGwTWg 99
Cdd:PRK09454   8 PRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAG-SW- 85

                         90       100
                 ....*....|....*....|.
gi 503994039 100 getHPWRGKNATIPTLQSVLE 120
Cdd:PRK09454  86 ---FSAAFAGEPLPTLSQVAA 103

glpQ

PRK11143

glycerophosphodiester phosphodiesterase; Provisional

1-76

6.09e-08

glycerophosphodiester phosphodiesterase; Provisional

Pssm-ID: 236859 [Multi-domain] Cd Length: 355 Bit Score: 53.14 E-value: 6.09e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039   1 MKSILTALGLLIASSACAA-------PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSA 73
Cdd:PRK11143   1 LKNLSLALLLAALLAGSAAaaadsaeKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDR 80


                 ...
gi 503994039  74 LTD 76
Cdd:PRK11143  81 VTD 83

GDPD_GDE5_like

cd08572

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

21-135

9.67e-08

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins. GDE5 is widely expressed in mammalian tissues, with highest expression in spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.

Pssm-ID: 176514 [Multi-domain] Cd Length: 293 Bit Score: 52.28 E-value: 9.67e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  21 QLIAHRG--------GTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLY------------RPSDLSALTDHTgk 80
Cdd:cd08572    1 LVIGHRGlgknyasgSLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYhdftisvsekskTGSDEGELIEVP-- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503994039  81 ISSFSAAELTRM------------DAGWTWGGETHPWRGK-NATIPTLQSVLEQWPQTF-FYIDIKSPD 135
Cdd:cd08572   79 IHDLTLEQLKELglqhisalkrkaLTRKAKGPKPNPWGMDeHDPFPTLQEVLEQVPKDLgFNIEIKYPQ 147

GDPD_SHV3_plant

cd08571

Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...

20-76

3.30e-07

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: 50.75 E-value: 3.30e-07

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTD 76
Cdd:cd08571    1 PLVIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTT 57

GDPD_GDE6

cd08610

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

20-119

4.99e-07

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: 50.26 E-value: 4.99e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDhTGKISSFSAAE---------LT 90
Cdd:cd08610   23 PTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTN-IGEVQPESACEnpaffnwdfLS 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 503994039  91 RMDAGwTWGGETHPW------------RGKNATIPTLQSVL 119
Cdd:cd08610  102 TLNAG-KWFVKPRPFynmkplseadkeRARNQSIPKLSNFL 141

GDPD_EcGlpQ_like

cd08600

Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...

23-120

7.40e-07

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: 49.70 E-value: 7.40e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  23 IAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTDHTGK--------------------IS 82
Cdd:cd08600    4 IAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKfpdrkrkdgryyvidftldeLK 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 503994039  83 SFSAAEltRMDAGWTWGGETHPWR----GKNATIPTLQSVLE 120
Cdd:cd08600   84 SLSVTE--RFDIENGKKVQVYPNRfplwKSDFKIHTLEEEIE 123

GDPD_SHV3_repeat_2

cd08604

Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...

20-160

7.48e-07

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: 49.64 E-value: 7.48e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTdhTGKISSFSAAELTRMDAGWTWG 99
Cdd:cd08604    1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINST--TVATSKFSNRATTVPEIGSTSG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994039 100 GETH--PWrgknATIPTLQSVLEQ-WPQTFFYidiKSPDADPAIMAARLSE--VLQKTNSLSRVRV 160
Cdd:cd08604   79 IFTFdlTW----SEIQTLKPAISNpYSVTGLF---RNPANKNAGKFLTLSDflDLAKNKSLSGVLI 137

GDPD_ScGlpQ1_like

cd08602

Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...

20-120

1.98e-06

Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of putative bacterial and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ, as well as plant glycerophosphodiester phosphodiesterases (GP-PDEs), all of which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. The prototypes of this family include putative secreted phosphodiesterase encoded by gene glpQ1 (SCO1565) from the pho regulon in Streptomyces coelicolor genome, and in plants, two distinct Arabidopsis thaliana genes, AT5G08030 and AT1G74210, coding putative GP-PDEs from the cell walls and vacuoles, respectively.

Pssm-ID: 176544 [Multi-domain] Cd Length: 309 Bit Score: 48.45 E-value: 1.98e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLSALTD---H-----------------TG 79
Cdd:cd08602    1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDvadHpefadrkttktvdgvnvTG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 503994039  80 KISS-FSAAELTRMDAGWTWGGETHPWRGKnATIPTLQSVLE 120
Cdd:cd08602   81 WFTEdFTLAELKTLRARQRLPYRDQSYDGQ-FPIPTFEEIIA 121

GDPD_GsGDE_like

cd08564

Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...

20-162

4.78e-06

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: 47.08 E-value: 4.78e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  20 PQLIAHRGG--TGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYR--PSDLSALT------DHTGKISSFSAAEL 89
Cdd:cd08564    4 PIIVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgtEDDTNPDTsiqlddSGFKNINDLSLDEI 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994039  90 TRMDAGWTWGGETHP-WRGKNATIPTLQSVLEQWPQTFFY-IDIKSPDADpaiMAARLSEVLQKTNSLSRVRVYS 162
Cdd:cd08564   84 TRLHFKQLFDEKPCGaDEIKGEKIPTLEDVLVTFKDKLKYnIELKGREVG---LGERVLNLVEKYGMILQVHFSS 155

PI-PLCc_GDPD_SF

cd08555

Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...

23-151

1.12e-05

Pssm-ID: 176498 [Multi-domain] Cd Length: 179 Bit Score: 44.73 E-value: 1.12e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  23 IAHRGGTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRpsdlsaltDHTgkissfsaaeLTRMDAGWTWgget 102
Cdd:cd08555    2 LSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYH--------GPT----------LDRTTAGILP---- 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503994039 103 hpwrgknatiPTLQSVLE-------QWPQTF-FYIDIKSPDADPAIMAARLSEVLQK 151
Cdd:cd08555   60 ----------PTLEEVLEliadylkNPDYTIiLSLEIKQDSPEYDEFLAKVLKELRV 106

GDPD_GDE5

cd08607

Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...

23-134

1.80e-05

Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester phosphodiesterase GDE5 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative mammalian GDE5 and similar proteins. Mammalian GDE5 is widely expressed in mammalian tissues, with highest expression in the spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. In addition to C-terminal GDPD domain, all members in this subfamily have a starch binding domain (CBM20) in the N-terminus, which suggests these proteins may play a distinct role in glycerol metabolism.

Pssm-ID: 176549 [Multi-domain] Cd Length: 290 Bit Score: 45.36 E-value: 1.80e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  23 IAHRG-------GTGDAPENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRpsDLSALTDHTGKISS------------ 83
Cdd:cd08607    3 VGHRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYH--DFTLRVSLKSKGDSdrddllevpvkd 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994039  84 FSAAELTRMD----AGWTwgGETHPWRGKNATI------PTLQSVLEQWPQTF-FYIDIKSP 134
Cdd:cd08607   81 LTYEQLKLLKlfhiSALK--VKEYKSVEEDEDPpehqpfPTLSDVLESVPEDVgFNIEIKWP 140

GDPD_YPL110cp_fungi

cd08606

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...

19-168

2.38e-05

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

Pssm-ID: 176548 [Multi-domain] Cd Length: 286 Bit Score: 44.74 E-value: 2.38e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  19 APQLIAHRG-GTGDAP-------ENTLPAIKLALENKAEAIWITVQLSQDGVPVLYRPSDLS-ALTD---HTGKISSFSA 86
Cdd:cd08606    1 SVQVIGHRGlGKNTAErkslqlgENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSeTGTDvpiHDLTLEQFLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994039  87 AELTRMDAGWTWGGETHPWRGKNATIP--TLQSVLEQWPQTF-FYIDIKSPDADPAImAARLSEVLQKTNS-----LSRV 158
Cdd:cd08606   81 LSRMKYTVDFKKKGFKGNSRGHSIQAPftTLEELLKKLPKSVgFNIELKYPMLHEAE-EEEVAPVAIELNAfvdtvLEKV 159

                        170
                 ....*....|
gi 503994039 159 RVYSTEDRYI 168
Cdd:cd08606  160 FDYGAGRNII 169

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