NCBI Conserved Domain Search

Conserved domains on [gi|1958658729|ref|XP_038941976|]

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lysophospholipase D GDPD1 isoform X1 [Rattus norvegicus]

Protein Classification

glycerophosphodiester phosphodiesterase family protein( domain architecture ID 10171264)

glycerophosphodiester phosphodiesterase (GDPD) family protein similar to Homo sapiens lysophospholipase D GDPD1/GDE4 and GDPD3/GDE7, which hydrolyze lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines glycerophosphodiester phosphodiesterase 1

CATH: 3.20.20.190

EC: 3.1.4.-

Gene Ontology: GO:0008081|GO:0006629|GO:0046872|GO:0004622

SCOP: 4000418

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

GDPD_GDE4

cd08612

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

14-320

0e+00

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: 516.00 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  14 GGYLVTSFLLLKYPALLHQRKKQRFLSRHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKR 93
Cdd:cd08612     1 GGYIATSYFLLRNPTLLHKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  94 STGVNVNVSDLKYCELPPYLCKLDVPFQRGSSgtrtitaCKCEGTDTRIPLLKEVFEAFPETPINIDIKVNNNVLIQKVS 173
Cdd:cd08612    81 SCGVDKLVSDLNYADLPPYLEKLEVTFSPGDY-------CVPKGSDRRIPLLEEVFEAFPDTPINIDIKVENDELIKKVS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 174 ELVKQYKREHLTVWGNASSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPHII 253
Cdd:cd08612   154 DLVRKYKREDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYFPKSM 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958658729 254 SKGHKFLIWLSDTLLMRKALFDHLTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPTKLKEFLNN 320
Cdd:cd08612   234 SRLNRFVLFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLREFLDK 300

Name

Accession

Description

Interval

E-value

GDPD_GDE4

cd08612

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

14-320

0e+00

Pssm-ID: 176553 [Multi-domain] Cd Length: 300 Bit Score: 516.00 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  14 GGYLVTSFLLLKYPALLHQRKKQRFLSRHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKR 93
Cdd:cd08612     1 GGYIATSYFLLRNPTLLHKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  94 STGVNVNVSDLKYCELPPYLCKLDVPFQRGSSgtrtitaCKCEGTDTRIPLLKEVFEAFPETPINIDIKVNNNVLIQKVS 173
Cdd:cd08612    81 SCGVDKLVSDLNYADLPPYLEKLEVTFSPGDY-------CVPKGSDRRIPLLEEVFEAFPDTPINIDIKVENDELIKKVS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 174 ELVKQYKREHLTVWGNASSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPHII 253
Cdd:cd08612   154 DLVRKYKREDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYFPKSM 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958658729 254 SKGHKFLIWLSDTLLMRKALFDHLTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPTKLKEFLNN 320
Cdd:cd08612   234 SRLNRFVLFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLREFLDK 300

UgpQ

COG0584

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];

43-319

1.02e-51

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];

Pssm-ID: 440349 [Multi-domain] Cd Length: 238 Bit Score: 170.82 E-value: 1.02e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCElppyLCKLDVpfqr 122
Cdd:COG0584     6 IAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAE----LRQLDA---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 123 GSSGtrtitackcEGTDTRIPLLKEVFEAFP-ETPINIDIKVNNNV---LIQKVSELVKQYKREHLTVWGNASSEIVDKC 198
Cdd:COG0584    78 GSGP---------DFAGERIPTLEEVLELVPgDVGLNIEIKSPPAAepdLAEAVAALLKRYGLEDRVIVSSFDPEALRRL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 199 YKENSDIPilfslqRVLLilglffTGLLPFVPIReqffeipmpsiILKLKEPHIISKGHKFLiwlsdtllmRKALFDHLT 278
Cdd:COG0584   149 RELAPDVP------LGLL------VEELPADPLE-----------LARALGADGVGPDYDLL---------TPELVAAAH 196

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958658729 279 ARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPTKLKEFLN 319
Cdd:COG0584   197 AAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRAVLR 237

GDPD

pfam03009

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

45-311

2.43e-31

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: 117.89 E-value: 2.43e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  45 HRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELP--PYLCKLDVPFQr 122
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKrlDIGAGNSGPLS- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 123 gssgtrtitackceGTDTRIPLLKEVFEAFPETPINIDIKVnnnvliqkvsELVKQYKREHLTVWGNASSEIVDKCYKEN 202
Cdd:pfam03009  80 --------------GERVPFPTLEEVLEFDWDVGFNIEIKI----------KPYVEAIAPEEGLIVKDLLLSVDEILAKK 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 203 SD-IPILFSLQRVLLILGLffTGLLPFVPIREQFFEIPMPSIILKLKE-PHIISKGHKFLIWLSDTLLMRkaLFDHLTAR 280
Cdd:pfam03009 136 ADpRRVIFSSFNPDELKRL--RELAPKLPLVFLSSGRAYAEADLLERAaAFAGAPALLGEVALVDEALPD--LVKRAHAR 211

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958658729 281 GIQVYIWVLNEEHEYKRAFDLGATGVMTDYP 311
Cdd:pfam03009 212 GLVVHVWTVNNEDEMKRLLELGVDGVITDRP 242

ugpQ

PRK09454

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional

39-95

3.03e-08

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional

Pssm-ID: 236524 [Multi-domain] Cd Length: 249 Bit Score: 53.79 E-value: 3.03e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958658729  39 LSRHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRST 95
Cdd:PRK09454    7 YPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTS 63

Name

Accession

Description

Interval

E-value

GDPD_GDE4

cd08612

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

14-320

0e+00

Pssm-ID: 176553 [Multi-domain] Cd Length: 300 Bit Score: 516.00 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  14 GGYLVTSFLLLKYPALLHQRKKQRFLSRHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKR 93
Cdd:cd08612     1 GGYIATSYFLLRNPTLLHKKKKSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  94 STGVNVNVSDLKYCELPPYLCKLDVPFQRGSSgtrtitaCKCEGTDTRIPLLKEVFEAFPETPINIDIKVNNNVLIQKVS 173
Cdd:cd08612    81 SCGVDKLVSDLNYADLPPYLEKLEVTFSPGDY-------CVPKGSDRRIPLLEEVFEAFPDTPINIDIKVENDELIKKVS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 174 ELVKQYKREHLTVWGNASSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPHII 253
Cdd:cd08612   154 DLVRKYKREDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFLEIPMPSIFLKTYFPKSM 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958658729 254 SKGHKFLIWLSDTLLMRKALFDHLTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPTKLKEFLNN 320
Cdd:cd08612   234 SRLNRFVLFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLREFLDK 300

GDPD_GDE4_like

cd08575

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

41-314

8.22e-140

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: 395.82 E-value: 8.22e-140

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  41 RHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPPYLCKLDVPF 120
Cdd:cd08575     2 LHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGYTF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 121 QRGSSGtrtitaCKCEGTDTRIPLLKEVFEAFPETPINIDIKVNN-NVLIQKVSELVKQYKREHLTVWGNASSEIVDKCY 199
Cdd:cd08575    82 DGGKTG------YPRGGGDGRIPTLEEVFKAFPDTPINIDIKSPDaEELIAAVLDLLEKYKREDRTVWGSTNPEYLRALH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 200 KENSDIPILFSLQRVLL-ILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPhiiskghKFLIWLSDTLLMRKALFDHLT 278
Cdd:cd08575   156 PENPNLFESFSMTRCLLlYLALGYTGLLPFVPIKESFFEIPRPVIVLETFTL-------GEGASIVAALLWWPNLFDHLR 228

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958658729 279 ARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPTKL 314
Cdd:cd08575   229 KRGIQVYLWVLNDEEDFEEAFDLGADGVMTDSPTKL 264

GDPD_cytoplasmic_ScUgpQ2_like

cd08561

Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...

42-318

1.33e-55

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: 180.92 E-value: 1.33e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  42 HISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVPFQ 121
Cdd:cd08561     1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELR----RLDAGYH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 122 RGSSGTRTItacKCEGTDTRIPLLKEVFEAFPETPINIDIKVNNNVLIQKVSELVKQYKREHLTVWGNASSEIVDKCYKE 201
Cdd:cd08561    77 FTDDGGRTY---PYRGQGIRIPTLEELFEAFPDVRLNIEIKDDGPAAAAALADLIERYGAQDRVLVASFSDRVLRRFRRL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 202 NSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPHIISKGHkfliwlsdtllmrkalfdhltARG 281
Cdd:cd08561   154 CPRVATSAGEGEVAAFVLASRLGLGSLYSPPYDALQIPVRYGGVPLVTPRFVRAAH---------------------AAG 212

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958658729 282 IQVYIWVLNEEHEYKRAFDLGATGVMTDYPTKLKEFL 318
Cdd:cd08561   213 LEVHVWTVNDPAEMRRLLDLGVDGIITDRPDLLLEVL 249

UgpQ

COG0584

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];

43-319

1.02e-51

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];

Pssm-ID: 440349 [Multi-domain] Cd Length: 238 Bit Score: 170.82 E-value: 1.02e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCElppyLCKLDVpfqr 122
Cdd:COG0584     6 IAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAE----LRQLDA---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 123 GSSGtrtitackcEGTDTRIPLLKEVFEAFP-ETPINIDIKVNNNV---LIQKVSELVKQYKREHLTVWGNASSEIVDKC 198
Cdd:COG0584    78 GSGP---------DFAGERIPTLEEVLELVPgDVGLNIEIKSPPAAepdLAEAVAALLKRYGLEDRVIVSSFDPEALRRL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 199 YKENSDIPilfslqRVLLilglffTGLLPFVPIReqffeipmpsiILKLKEPHIISKGHKFLiwlsdtllmRKALFDHLT 278
Cdd:COG0584   149 RELAPDVP------LGLL------VEELPADPLE-----------LARALGADGVGPDYDLL---------TPELVAAAH 196

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958658729 279 ARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPTKLKEFLN 319
Cdd:COG0584   197 AAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRAVLR 237

GDPD

cd08556

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

43-310

1.17e-34

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: 124.68 E-value: 1.17e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDanlkrstgvnvnvsdlkycelppylckldvpfqr 122
Cdd:cd08556     2 IAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD---------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 123 gssgtrtitackcegtdtrIPLLKEVFEAFPE-TPINIDIKVNN--NVLIQKVSELVKQYKREHLTVWGNASSEIVDKCY 199
Cdd:cd08556    48 -------------------IPTLEEVLELVKGgVGLNIELKEPTryPGLEAKVAELLREYGLEERVVVSSFDHEALRALK 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 200 KENSDIPIlfslqrvllilGLFFTGLLPFVPIREQFFEIPMPSIILKLKephiiskghkfliwlsdtlLMRKALFDHLTA 279
Cdd:cd08556   109 ELDPEVPT-----------GLLVDKPPLDPLLAELARALGADAVNPHYK-------------------LLTPELVRAAHA 158

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958658729 280 RGIQVYIWVLNEEHEYKRAFDLGATGVMTDY 310
Cdd:cd08556   159 AGLKVYVWTVNDPEDARRLLALGVDGIITDD 189

GDPD_TtGDE_like

cd08563

Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...

43-311

1.25e-31

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: 118.04 E-value: 1.25e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCElppyLCKLD--VPF 120
Cdd:cd08563     4 FAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEE----LKKLDagSWF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 121 QRgssgtrtitackcEGTDTRIPLLKEVFEAFPETPINIDIKVNNNV-----LIQKVSELVKQYKREHLTVWgnaSS--- 192
Cdd:cd08563    80 DE-------------KFTGEKIPTLEEVLDLLKDKDLLLNIEIKTDVihypgIEKKVLELVKEYNLEDRVIF---SSfnh 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 193 EIVDKCYKENSDIPIlfslqrvllilglfftGLLpfvpireqfFEIpmpsiilKLKEPHIISKGHKFLIWLSDTLLMRKA 272
Cdd:cd08563   144 ESLKRLKKLDPKIKL----------------ALL---------YET-------GLQDPKDYAKKIGADSLHPDFKLLTEE 191

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958658729 273 LFDHLTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYP 311
Cdd:cd08563   192 VVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230

GDPD

pfam03009

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

45-311

2.43e-31

Pssm-ID: 397241 [Multi-domain] Cd Length: 244 Bit Score: 117.89 E-value: 2.43e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  45 HRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELP--PYLCKLDVPFQr 122
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKrlDIGAGNSGPLS- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 123 gssgtrtitackceGTDTRIPLLKEVFEAFPETPINIDIKVnnnvliqkvsELVKQYKREHLTVWGNASSEIVDKCYKEN 202
Cdd:pfam03009  80 --------------GERVPFPTLEEVLEFDWDVGFNIEIKI----------KPYVEAIAPEEGLIVKDLLLSVDEILAKK 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 203 SD-IPILFSLQRVLLILGLffTGLLPFVPIREQFFEIPMPSIILKLKE-PHIISKGHKFLIWLSDTLLMRkaLFDHLTAR 280
Cdd:pfam03009 136 ADpRRVIFSSFNPDELKRL--RELAPKLPLVFLSSGRAYAEADLLERAaAFAGAPALLGEVALVDEALPD--LVKRAHAR 211

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958658729 281 GIQVYIWVLNEEHEYKRAFDLGATGVMTDYP 311
Cdd:pfam03009 212 GLVVHVWTVNNEDEMKRLLELGVDGVITDRP 242

GDPD_memb_like

cd08579

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...

43-311

3.83e-31

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: 116.49 E-value: 3.83e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVpfqr 122
Cdd:cd08579     2 IAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELK----KLTI---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 123 gssgtrtitacKCEGTDTRIPLLKEVFEAF--PETPINIDIKVNNNV---LIQKVSELVKQYKREHLTVWGNASSEIVDK 197
Cdd:cd08579    74 -----------GENGHGAKIPSLDEYLALAkgLKQKLLIELKPHGHDspdLVEKFVKLYKQNLIENQHQVHSLDYRVIEK 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 198 CYKENSDIPilfslqrVLLILGLFFTGlLPFVPIreQFFEIPMPSIilklkEPHIISKGHKfliwlsdtllmrkalfdhl 277
Cdd:cd08579   143 VKKLDPKIK-------TGYILPFNIGN-LPKTNV--DFYSIEYSTL-----NKEFIRQAHQ------------------- 188

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958658729 278 taRGIQVYIWVLNEEHEYKRAFDLGATGVMTDYP 311
Cdd:cd08579   189 --NGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220

GDPD_TmGDE_like

cd08568

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

43-314

4.79e-30

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: 113.93 E-value: 4.79e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVPFQr 122
Cdd:cd08568     3 LGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELK----KLHPGGE- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 123 gssgtrtitackcegtdtRIPLLKEVFEAFPETPI-NIDIKVNNNVliQKVSELVKQYKREHLTVWGNASSEIVDKCYKE 201
Cdd:cd08568    78 ------------------LIPTLEEVFRALPNDAIiNVEIKDIDAV--EPVLEIVEKFNALDRVIFSSFNHDALRELRKL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 202 NSDipilfslqrvlLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPHIIS--KGHKFLIWLsdtllmRKalfdhlta 279
Cdd:cd08568   138 DPD-----------AKVGLLIGEEEEGFSIPELHEKLKLYSLHVPIDAIGYIGfeKFVELLRLL------RK-------- 192

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958658729 280 RGIQVYIWVLNEEHEYKRAFDLgATGVMTDYPTKL 314
Cdd:cd08568   193 LGLKIVLWTVNDPELVPKLKGL-VDGVITDDVEKI 226

GDPD_YPL206cp_fungi

cd08570

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...

43-311

5.14e-30

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: 113.86 E-value: 5.14e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYcelPPYLCKLdvpfqr 122
Cdd:cd08570     2 IGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDST---WDELSHL------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 123 gssgtRTItackcEGTDTRIPLLKEVFEAF-----PETPINIDIKVNNN--VLIQKVSELVKQYK-----REHLtVWGNA 190
Cdd:cd08570    73 -----RTI-----EEPHQPMPTLKDVLEWLvehelPDVKLMLDIKRDNDpeILFKLIAEMLAVKPdldfwRERI-ILGLW 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 191 SSEIVDKCYKENSDIP---ILFSLqrvllilglfftgllpfvPIREQFFEIPmpsiiLKLkepHIISKGHKfLIWLSDtl 267
Cdd:cd08570   142 HLDFLKYGKEVLPGFPvfhIGFSL------------------DYARHFLNYS-----EKL---VGISMHFV-SLWGPF-- 192

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958658729 268 lmRKALFDHLTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYP 311
Cdd:cd08570   193 --GQAFLPELKKNGKKVFVWTVNTEEDMRYAIRLGVDGVITDDP 234

GDPD_like_2

cd08582

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...

43-312

9.77e-25

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: 99.70 E-value: 9.77e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVPFQR 122
Cdd:cd08582     2 IAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELR----KLDIGSWK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 123 GSSgtrtitackceGTDTRIPLLKEVFEAFPETP--INIDIKVNNNVLiqKVSELVKQykrehltvwgnasseIVDKCYK 200
Cdd:cd08582    78 GES-----------YKGEKVPTLEEYLAIVPKYGkkLFIEIKHPRRGP--EAEEELLK---------------LLKESGL 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 201 ENSDIPILfSLQRVLLILglfftgllpfvpIREQFFEIP---MPSIILKLKEPHIISKGHKFL-IWLSDTLLMRKALFDH 276
Cdd:cd08582   130 LPEQIVII-SFDAEALKR------------VRELAPTLEtlwLRNYKSPKEDPRPLAKSGGAAgLDLSYEKKLNPAFIKA 196

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958658729 277 LTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPT 312
Cdd:cd08582   197 LRDAGLKLNVWTVDDAEDAKRLIELGVDSITTNRPG 232

GDPD_SpGDE_like

cd08567

Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...

45-311

1.81e-23

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: 97.00 E-value: 1.81e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  45 HRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHD----------ANLKRSTGVNVNVSDLKYCEL----- 109
Cdd:cd08567     6 HRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDpklnpditrdPDGAWLPYEGPALYELTLAEIkqldv 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 110 ----PPYLCKLDVPFQRGSSGtrtitackcegtdTRIPLLKEVFEAFP-----ETPINIDIKVNNN---------VLIQK 171
Cdd:cd08567    86 gekrPGSDYAKLFPEQIPVPG-------------TRIPTLEEVFALVEkygnqKVRFNIETKSDPDrdilhpppeEFVDA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 172 VSELVKQYKREHLTV-----WgnASSEIVDKCYkensdiPilfSLQRVLLILGLFFTGLlpfvpireqffeipmPSIILK 246
Cdd:cd08567   153 VLAVIRKAGLEDRVVlqsfdW--RTLQEVRRLA------P---DIPTVALTEETTLGNL---------------PRAAKK 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958658729 247 LkephiiskghKFLIWLSDTLLMRKALFDHLTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYP 311
Cdd:cd08567   207 L----------GADIWSPYFTLVTKELVDEAHALGLKVVPWTVNDPEDMARLIDLGVDGIITDYP 261

GDPD_AtGDE_like

cd08566

Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...

43-311

8.46e-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: 94.68 E-value: 8.46e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENL-ENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELppYLCKLDVPFQ 121
Cdd:cd08566     3 VAHRGGWGAGApENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEI--RKLRLKDGDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 122 RgssgtrtitackceGTDTRIPLLKEVFEAFPE-TPINIDIKvnnNVLIQKVSELVKQYK-REHLTVWGNASSEivdkcY 199
Cdd:cd08566    81 E--------------VTDEKVPTLEEALAWAKGkILLNLDLK---DADLDEVIALVKKHGaLDQVIFKSYSEEQ-----A 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 200 KENSDIpilfsLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPH--IISKGHKFL---IWlsdtllmrkalF 274
Cdd:cd08566   139 KELRAL-----APEVMLMPIVRDAEDLDEEEARAIDALNLLAFEITFDDLDLppLFDELLRALgirVW-----------V 202

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958658729 275 DHLTARGIQVYIWVLNE-EHEYKRAFDLGATGVMTDYP 311
Cdd:cd08566   203 NTLGDDDTAGLDRALSDpREVWGELVDAGVDVIQTDRP 240

GDPD_like_3

cd08585

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...

41-180

6.15e-22

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: 92.39 E-value: 6.15e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  41 RHISHRGGAGENL---ENTMAAFQHAVTIGTDmLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELppylckld 117
Cdd:cd08585     5 RPIAHRGLHDRDAgipENSLSAFRAAAEAGYG-IELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAEL-------- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958658729 118 vpfqrgssgtrtiTACKCEGTDTRIPLLKEVFEAFP-ETPINIDIKV---NNNVLIQKVSELVKQYK 180
Cdd:cd08585    76 -------------RALRLLGTDEHIPTLDEVLELVAgRVPLLIELKScggGDGGLERRVLAALKDYK 129

GDPD_EcUgpQ_like

cd08562

Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...

43-311

4.49e-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: 4.49e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDV--PF 120
Cdd:cd08562     2 IAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELA----QLDAgsWF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 121 QRgssgtrtitackcEGTDTRIPLLKEVFEAFPETPI--NIDIKVNNnvliQKVSELVKQYKREHLTVWGNA-----SS- 192
Cdd:cd08562    78 SP-------------EFAGEPIPTLADVLELARELGLglNLEIKPDP----GDEALTARVVAAALRELWPHAsklllSSf 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 193 --EIVDKCYKENSDIPilfslqrvlliLGLFFTGLLPfvPIREQFFEIPMPSIIL---KLKEPHIiskghkfliwlsdtl 267
Cdd:cd08562   141 slEALRAARRAAPELP-----------LGLLFDTLPA--DWLELLAALGAVSIHLnyrGLTEEQV--------------- 192

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958658729 268 lmrKAlfdhLTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYP 311
Cdd:cd08562   193 ---KA----LKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229

GDPD_pAtGDE_like

cd08565

Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...

43-312

2.07e-18

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

Pssm-ID: 176508 [Multi-domain] Cd Length: 235 Bit Score: 82.45 E-value: 2.07e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVPfqr 122
Cdd:cd08565     2 AGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERK----ALRLR--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 123 gssgtrtitackcEGTDTRIPLLKEVFEAFPETPI--NIDIKVNNNV-----LIQKVSELVKQYKREHLTVWGNASSEIV 195
Cdd:cd08565    75 -------------DSFGEKIPTLEEVLALFAPSGLelHVEIKTDADGtpypgAAALAAATLRRHGLLERSVLTSFDPAVL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 196 DKCYKENSdIPILFSL-QRVLLILGlfftGLLPFVPIReqffeipmpsiilklKEP-HIISKGHKFLIwlsDTLLMRKAl 273
Cdd:cd08565   142 TEVRKHPG-VRTLGSVdEDMLERLG----GELPFLTAT---------------ALKaHIVAVEQSLLA---ATWELVRA- 197

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958658729 274 fdhlTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPT 312
Cdd:cd08565   198 ----AVPGLRLGVWTVNDDSLIRYWLACGVRQLTTDRPD 232

GDPD_SaGlpQ_like

cd08601

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

43-318

5.95e-18

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: 81.59 E-value: 5.95e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVN--VSDLKYCELPpylcKLDVpf 120
Cdd:cd08601     4 IAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIERPgpVKDYTLAEIK----QLDA-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 121 qrGSSGTRT-ITACKCEGTDTRIPLLKEVFEAF-PETPINIDIKVNN-NVLIQKvsELVKQYKREHLTVWGNASSEIV-- 195
Cdd:cd08601    78 --GSWFNKAyPEYARESYSGLKVPTLEEVIERYgGRANYYIETKSPDlYPGMEE--KLLATLDKYGLLTDNLKNGQVIiq 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 196 -------DKCYKENSDIPILfslqrvllilglfftgllpfvpireQFFEIPMPSIILKLKephiISKGHKFLIWLSDTL- 267
Cdd:cd08601   154 sfskeslKKLHQLNPNIPLV-------------------------QLLWYGEGAETYDKW----LDEIKEYAIGIGPSIa 204

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958658729 268 LMRKALFDHLTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPTKLKEFL 318
Cdd:cd08601   205 DADPWMVHLIHKKGLLVHPYTVNEKADMIRLINWGVDGMFTNYPDRLKEVL 255

GDPD_GDE1

cd08573

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

43-311

1.37e-17

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: 80.77 E-value: 1.37e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCElppyLCKLDVpfqr 122
Cdd:cd08573     2 IGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEE----LRKLNA---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 123 gssGTRTITACKCEGtdTRIPLLKEVFEAFPE--TPINIDIKVNNNVLIQKVSELVKQYKRehltVWGNA--SS---EIV 195
Cdd:cd08573    74 ---AAKHRLSSRFPG--EKIPTLEEAVKECLEnnLRMIFDVKSNSSKLVDALKNLFKKYPG----LYDKAivCSfnpIVI 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 196 DKCYKENSDIpilfslqrvllILGL-----FFTGLLPFVPIR-EQFFEIPMPSIILKLKEPHIiskgHKFLIWL--SDTL 267
Cdd:cd08573   145 YKVRKADPKI-----------LTGLtwrpwFLSYTDDEGGPRrKSGWKHFLYSMLDVILEWSL----HSWLPYFlgVSAL 209

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958658729 268 LMRK-----ALFDHLTARGIQVYIWVLNEEHEyKRAF--DLGATgVMTDYP 311
Cdd:cd08573   210 LIHKddissAYVRYWRARGIRVIAWTVNTPTE-KQYFakTLNVP-YITDSL 258

GDPD_Rv2277c_like

cd08580

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...

43-176

7.55e-15

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: 73.13 E-value: 7.55e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVPFQ- 121
Cdd:cd08580     4 VAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLA----TLNAGYNf 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958658729 122 --RGSSGTRtitackceGTDTRIPLLKEVFEAFPETPINIDIK-VNNNVLIQKVSELV 176
Cdd:cd08580    80 kpEGGYPYR--------GKPVGIPTLEQVLRAFPDTPFILDMKsLPADPQAKAVARVL 129

GDPD_GDE5_like

cd08572

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

42-162

9.08e-14

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: 70.39 E-value: 9.08e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  42 HISHRGgAGEN---------LENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHD----------ANLKRSTGVNVNVS 102
Cdd:cd08572     2 VIGHRG-LGKNyasgslagiRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDftisvsekskTGSDEGELIEVPIH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 103 DLKYCELppylckLDVPFQRGSSGTRTITACKCEGT---------DTRIPLLKEVFEAFPE-TPINIDIK 162
Cdd:cd08572    81 DLTLEQL------KELGLQHISALKRKALTRKAKGPkpnpwgmdeHDPFPTLQEVLEQVPKdLGFNIEIK 144

GDPD_GDE5

cd08607

Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...

42-162

1.20e-12

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: 67.32 E-value: 1.20e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  42 HISHRGgAGENL--------ENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHD----ANLKRSTGVN------VNVSD 103
Cdd:cd08607     2 DVGHRG-AGNSYtaasavvrENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDftlrVSLKSKGDSDrddlleVPVKD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958658729 104 LKYCELPpyLCKLDVpFQRGSSGTRTITACKCEGTDTRI-PLLKEVFEAFPE-TPINIDIK 162
Cdd:cd08607    81 LTYEQLK--LLKLFH-ISALKVKEYKSVEEDEDPPEHQPfPTLSDVLESVPEdVGFNIEIK 138

GDPD_like_1

cd08581

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...

43-174

1.40e-12

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: 66.20 E-value: 1.40e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPPYLCKLDVPFQR 122
Cdd:cd08581     2 VAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVAEPARFGS 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958658729 123 GSSGtrtitackcegtdTRIPLLKEVFEA---FPETPINIDIKVNN------NVLIQKVSE 174
Cdd:cd08581    82 RFAG-------------EPLPSLAAVVQWlaqHPQVTLFVEIKTESldrfglERVVDKVLR 129

GDPD_GDE4_like_1

cd08613

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...

53-188

2.47e-12

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: 66.23 E-value: 2.47e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  53 LENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVPFQRGSSGTRTIta 132
Cdd:cd08613    59 LENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELK----TLDIGYGYTADGGKTF-- 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958658729 133 cKCEGTDT-RIPLLKEVFEAFPETPINIDIKVNN----NVLIQKVSELvKQYKREHLTVWG 188
Cdd:cd08613   133 -PFRGKGVgMMPTLDEVFAAFPDRRFLINFKSDDaaegELLAEKLATL-PRKRLQVLTVYG 191

GDPD_GsGDE_like

cd08564

Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...

45-319

1.52e-11

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: 63.65 E-value: 1.52e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  45 HRGGAGENL--ENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSH--------DANLKRSTGVNVNVSDLKYCELPPYLC 114
Cdd:cd08564     9 HRGAGCSTLypENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteddtnpDTSIQLDDSGFKNINDLSLDEITRLHF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 115 KldVPFQRGSSGtrtitacKCEGTDTRIPLLKEVFEAF-PETPINIDIKVNNNVLIQKVSELVKQYKrehltvwgnasse 193
Cdd:cd08564    89 K--QLFDEKPCG-------ADEIKGEKIPTLEDVLVTFkDKLKYNIELKGREVGLGERVLNLVEKYG------------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 194 ivdkcYKENSDIPILFSLQRVLLILGLFFTGLLpfVPIREQFFEIPMPSIILKLKEphiISKGHKFLIWLSDTLLMRKAL 273
Cdd:cd08564   147 -----MILQVHFSSFLHYDRLDLLKALRPNKLN--VPIALLFNEVKSPSPLDFLEQ---AKYYNATWVNFSYDFWTEEFV 216

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958658729 274 FdHLTARGIQVYIW----VLNEEHEYKRAFDLGATGVMTDYPTKLKEFLN 319
Cdd:cd08564   217 K-KAHENGLKVMTYfdepVNDNEEDYKVYLELGVDCICPNDPVLLVNFLK 265

GDPD_periplasmic_GlpQ_like

cd08559

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

43-97

8.92e-11

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: 61.52 E-value: 8.92e-11

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGV 97
Cdd:cd08559     4 IAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNV 58

PI-PLCc_GDPD_SF

cd08555

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

43-181

5.71e-10

Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases superfamily; The PI-PLC-like phosphodiesterases superfamily represents the catalytic domains of bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11), glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria, as well as their uncharacterized homologs found in organisms ranging from bacteria and archaea to metazoans, plants, and fungi. PI-PLCs are ubiquitous enzymes hydrolyzing the membrane lipid phosphoinositides to yield two important second messengers, inositol phosphates and diacylglycerol (DAG). GP-GDEs play essential roles in glycerol metabolism and catalyze the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols that are major sources of carbon and phosphate. Both, PI-PLCs and GP-GDEs, can hydrolyze the 3'-5' phosphodiester bonds in different substrates, and utilize a similar mechanism of general base and acid catalysis with conserved histidine residues, which consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81, glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs). The residues essential for enzyme activities and metal binding are not conserved in these sequence homologs, which might suggest that the function of catalytic domains in these proteins might be distinct from those in typical PLC-like phosphodiesterases.

Pssm-ID: 176498 [Multi-domain] Cd Length: 179 Bit Score: 57.83 E-value: 5.71e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGvnvnvsdlkyCELPPYLCKLdvpfqr 122
Cdd:cd08555     2 LSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTA----------GILPPTLEEV------ 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 123 gssgtrtitackcegtdtrIPLLKEVFEAFPETPI-NIDIKVNNNVLIQKVSELVKQYKR 181
Cdd:cd08555    66 -------------------LELIADYLKNPDYTIIlSLEIKQDSPEYDEFLAKVLKELRV 106

GDPD_ScGlpQ1_like

cd08602

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

43-105

1.75e-08

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: 55.00 E-value: 1.75e-08

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTgvnvNVSDLK 105
Cdd:cd08602     4 IAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTT----DVADHP 62

ugpQ

PRK09454

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional

39-95

3.03e-08

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional

Pssm-ID: 236524 [Multi-domain] Cd Length: 249 Bit Score: 53.79 E-value: 3.03e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958658729  39 LSRHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRST 95
Cdd:PRK09454    7 YPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTS 63

GDPD_EcGlpQ_like

cd08600

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

43-97

5.65e-08

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: 53.55 E-value: 5.65e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGV 97
Cdd:cd08600     4 IAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNV 58

glpQ

PRK11143

glycerophosphodiester phosphodiesterase; Provisional

43-97

9.41e-07

glycerophosphodiester phosphodiesterase; Provisional

Pssm-ID: 236859 [Multi-domain] Cd Length: 355 Bit Score: 49.67 E-value: 9.41e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGV 97
Cdd:PRK11143   30 IAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDV 84

GDPD_GDE6

cd08610

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

43-97

1.64e-05

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: 46.02 E-value: 1.64e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGV 97
Cdd:cd08610    26 IGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNI 80

GDPD_YPL110cp_fungi

cd08606

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...

43-232

2.97e-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: 2.97e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGgAGENL---------ENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRsTGVNVNVSDLKyceLPPYL 113
Cdd:cd08606     5 IGHRG-LGKNTaerkslqlgENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSE-TGTDVPIHDLT---LEQFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 114 ----CKLDVPFQ-RGSSG-TRTITACKCEGTdtriplLKEVFEAFPET-PINIDIK----------------VNNNVLIQ 170
Cdd:cd08606    80 hlsrMKYTVDFKkKGFKGnSRGHSIQAPFTT------LEELLKKLPKSvGFNIELKypmlheaeeeevapvaIELNAFVD 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958658729 171 KVSELVKQYkrehltvwgNASSEIVDKCYkeNSDIPILFSL-QRVLLILGLFFTGLLPFVPIR 232
Cdd:cd08606   154 TVLEKVFDY---------GAGRNIIFSSF--TPDICILLSLkQPGYPVLFLTEAGKAPDMDVR 205

GDPD_GDE5_like_1_plant

cd08605

Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...

43-164

6.23e-05

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

Pssm-ID: 176547 [Multi-domain] Cd Length: 282 Bit Score: 43.94 E-value: 6.23e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGgAGENL------------ENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVN---VSDLKYC 107
Cdd:cd08605     3 IGHRG-LGMNRashqpsvgpgirENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVERGGEVEssrIRDLTLA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958658729 108 ELppylcKLDVPFQRGSSGTRTITACKCEGT---------DTRIPLLKEVFEAFP-ETPINIDIKVN 164
Cdd:cd08605    82 EL-----KALGPQAESTKTSTVALYRKAKDPepepwimdvEDSIPTLEEVFSEVPpSLGFNIELKFG 143

GDPD_GDE3

cd08609

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...

43-166

2.92e-04

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: 41.83 E-value: 2.92e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGV-------------NVNVSDLKYCEL 109
Cdd:cd08609    30 VGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVkdvfpgrdaagsnNFTWTELKTLNA 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958658729 110 PPYLCKLDvPF---QRGSSGTRTitackcEGTDTRIPLLKEVFEAFPETPINI--DIKVNNN 166
Cdd:cd08609   110 GSWFLERR-PFwtlSSLSEEDRR------EADNQTVPSLSELLDLAKKHNVSImfDLRNENN 164

GDPD_2

pfam13653

Glycerophosphoryl diester phosphodiesterase family; This family also includes ...

283-312

3.47e-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: 37.48 E-value: 3.47e-04

                          10        20        30
                  ....*....|....*....|....*....|
gi 1958658729 283 QVYIWVLNEEHEYKRAFDLGATGVMTDYPT 312
Cdd:pfam13653   1 KVRFWTIDNKAAWKELMRLGVDGLNTDDPE 30

PI-PLCc_GDPD_SF_unchar1

cd08583

Uncharacterized hypothetical proteins similar to the catalytic domains of ...

43-313

3.68e-04

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

Pssm-ID: 176525 [Multi-domain] Cd Length: 237 Bit Score: 41.13 E-value: 3.68e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729  43 ISHRGGA--GENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSH--DANLKRSTGVNV--NVSDLKYCEL---PPYl 113
Cdd:cd08583     2 IAHAMGGidGKTYTNSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHswDESLLKQLGLPTskNTKPLSYEEFkskKIY- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 114 ckldvpfqrGSSGTRTItackcegtDTRIPLLKEvfeaFPETPINIDIKVNNNVLIQKVSE-LVKQYKRehltvwgnASS 192
Cdd:cd08583    81 ---------GKYTPMDF--------KDVIDLLKK----YPDVYIVTDTKQDDDNDIKKLYEyIVKEAKE--------VDP 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958658729 193 EIVDKCYKENSDIPILFSLQRVLLILGLFFTgllpfvPIREQffEIPMPSIILKLKEPHIiskghkFLIWLSDTLLMRKA 272
Cdd:cd08583   132 DLLDRVIPQIYNEEMYEAIMSIYPFKSVIYT------LYRQD--SIRLDEIIAFCYENGI------KAVTISKNYVNDKL 197

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958658729 273 LfDHLTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPTK 313
Cdd:cd08583   198 I-EKLNKAGIYVYVYTINDLKDAQEYKKLGVYGIYTDFLTE 237

GDPD_EcGlpQ_like_1

cd08560

Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...

34-90

2.41e-03

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: 39.33 E-value: 2.41e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958658729  34 KKQRFlsrHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDAN 90
Cdd:cd08560    14 RKTDF---SIGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSQC 67

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