NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|578116615|gb|EUK77873|]
View 

glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus M0316]

Protein Classification

glycerophosphodiester phosphodiesterase( domain architecture ID 11426576)

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

CATH:  3.20.20.190
EC:  3.1.4.-
Gene Ontology:  GO:0008081|GO:0006629|GO:0046872
PubMed:  38491249

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
11-247 2.39e-83

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


:

Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 248.63  E-value: 2.39e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  11 QIVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSYKDv 90
Cdd:COG0584    4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGSGPD- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  91 aFKGERIPTLDEVLSLClKYDKKLLIELKSPN-LYPEIECKLLAFLEEKKVDAtQVVIQSFDIECIEKLNTLGSIYELGV 169
Cdd:COG0584   83 -FAGERIPTLEEVLELV-PGDVGLNIEIKSPPaAEPDLAEAVAALLKRYGLED-RVIVSSFDPEALRRLRELAPDVPLGL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578116615 170 LCSKRNYWYkkpnFSRIAQI-ASYVNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITDNPKLFIK 247
Cdd:COG0584  160 LVEELPADP----LELARALgADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRA 234
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
11-247 2.39e-83

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 248.63  E-value: 2.39e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  11 QIVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSYKDv 90
Cdd:COG0584    4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGSGPD- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  91 aFKGERIPTLDEVLSLClKYDKKLLIELKSPN-LYPEIECKLLAFLEEKKVDAtQVVIQSFDIECIEKLNTLGSIYELGV 169
Cdd:COG0584   83 -FAGERIPTLEEVLELV-PGDVGLNIEIKSPPaAEPDLAEAVAALLKRYGLED-RVIVSSFDPEALRRLRELAPDVPLGL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578116615 170 LCSKRNYWYkkpnFSRIAQI-ASYVNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITDNPKLFIK 247
Cdd:COG0584  160 LVEELPADP----LELARALgADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRA 234
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 11-242 2.46e-66

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: 205.10  E-value: 2.46e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  11 QIVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSYKDV 90
Cdd:cd08563    2 LIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFDE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  91 AFKGERIPTLDEVLSLCLKYDKKLLIELKSP-NLYPEIECKLLAFLEEKKVDaTQVVIQSFDIECIEKLNTLGSIYELGV 169
Cdd:cd08563   82 KFTGEKIPTLEEVLDLLKDKDLLLNIEIKTDvIHYPGIEKKVLELVKEYNLE-DRVIFSSFNHESLKRLKKLDPKIKLAL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578116615 170 LcskrnYW-YKKPNFSRIAQI-ASYVNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITDNP 242
Cdd:cd08563  161 L-----YEtGLQDPKDYAKKIgADSLHPDFKLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 15-242 2.46e-49

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: 162.18  E-value: 2.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615   15 HRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSYKDVAFKG 94
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615   95 ER--IPTLDEVLSLCLKYDKKLLIELKSPNLYPEIEC------KLLAFLE--EKKVDATQVVIQSFDIECIEKLNTLGSI 164
Cdd:pfam03009  81 ERvpFPTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEEglivkdLLLSVDEilAKKADPRRVIFSSFNPDELKRLRELAPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  165 YELGVLCSKRNYWY--KKPNFSRIAQIASY--VNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITD 240
Cdd:pfam03009 161 LPLVFLSSGRAYAEadLLERAAAFAGAPALlgEVALVDEALPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVITD 240


                  ..
gi 578116615  241 NP 242
Cdd:pfam03009 241 RP 242
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 12-245 2.54e-31

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 115.81  E-value: 2.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSYKDVA 91
Cdd:PRK09454  10 IVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  92 FKGERIPTLDEVLSLCLKYDKKLLIELKsPNLYPEIECKLLAFLEEKKVDATQVV---IQSFDIECIEKLNTLGSIYELG 168
Cdd:PRK09454  90 FAGEPLPTLSQVAARCRAHGMAANIEIK-PTTGREAETGRVVALAARALWAGAAVpplLSSFSEDALEAARQAAPELPRG 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578116615 169 VLCSK-RNYWykkpnFSRIAQI-ASYVNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITDNPKLF 245
Cdd:PRK09454 169 LLLDEwPDDW-----LELTRRLgCVSLHLNHKLLDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTDRIDLI 242
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
11-247 2.39e-83

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 248.63  E-value: 2.39e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  11 QIVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSYKDv 90
Cdd:COG0584    4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGSGPD- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  91 aFKGERIPTLDEVLSLClKYDKKLLIELKSPN-LYPEIECKLLAFLEEKKVDAtQVVIQSFDIECIEKLNTLGSIYELGV 169
Cdd:COG0584   83 -FAGERIPTLEEVLELV-PGDVGLNIEIKSPPaAEPDLAEAVAALLKRYGLED-RVIVSSFDPEALRRLRELAPDVPLGL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578116615 170 LCSKRNYWYkkpnFSRIAQI-ASYVNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITDNPKLFIK 247
Cdd:COG0584  160 LVEELPADP----LELARALgADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLLRA 234
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 11-242 2.46e-66

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: 205.10  E-value: 2.46e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  11 QIVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSYKDV 90
Cdd:cd08563    2 LIFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLDAGSWFDE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  91 AFKGERIPTLDEVLSLCLKYDKKLLIELKSP-NLYPEIECKLLAFLEEKKVDaTQVVIQSFDIECIEKLNTLGSIYELGV 169
Cdd:cd08563   82 KFTGEKIPTLEEVLDLLKDKDLLLNIEIKTDvIHYPGIEKKVLELVKEYNLE-DRVIFSSFNHESLKRLKKLDPKIKLAL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578116615 170 LcskrnYW-YKKPNFSRIAQI-ASYVNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITDNP 242
Cdd:cd08563  161 L-----YEtGLQDPKDYAKKIgADSLHPDFKLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 12-241 1.13e-60

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: 189.40  E-value: 1.13e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDetidrtsdgkgriadytlsqlksfdfgsykdva 91
Cdd:cd08556    1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  92 fkgerIPTLDEVLSLCLKyDKKLLIELKSPNLYPEIECKLLAFLEeKKVDATQVVIQSFDIECIEKLNTLGSIYELGVLC 171
Cdd:cd08556   48 -----IPTLEEVLELVKG-GVGLNIELKEPTRYPGLEAKVAELLR-EYGLEERVVVSSFDHEALRALKELDPEVPTGLLV 120

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 172 SKRNYWYKKPNFSRIAQiASYVNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITDN 241
Cdd:cd08556  121 DKPPLDPLLAELARALG-ADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITDD 189
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 12-242 5.82e-57

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: 181.27  E-value: 5.82e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSYKDVA 91
Cdd:cd08562    1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDAGSWFSPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  92 FKGERIPTLDEVLSLCLKYDKKLLIELKSPNLYPEIECKLLA-FLEEKKVDATQVVIQSFDIECIEKLNTLGSIYELGVL 170
Cdd:cd08562   81 FAGEPIPTLADVLELARELGLGLNLEIKPDPGDEALTARVVAaALRELWPHASKLLLSSFSLEALRAARRAAPELPLGLL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578116615 171 cskrnyWYKKPN--FSRIAQI-ASYVNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITDNP 242
Cdd:cd08562  161 ------FDTLPAdwLELLAALgAVSIHLNYRGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 12-242 3.02e-55

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: 177.12  E-value: 3.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSYKDVA 91
Cdd:cd08582    1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGSWKGES 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  92 FKGERIPTLDEVLSLCLKYDKKLLIELKSPNLYPEIECKLLAFLEEKKVDATQVVIQSFDIECIEKLNTLGSIYELGVLc 171
Cdd:cd08582   81 YKGEKVPTLEEYLAIVPKYGKKLFIEIKHPRRGPEAEEELLKLLKESGLLPEQIVIISFDAEALKRVRELAPTLETLWL- 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578116615 172 skRNYWYKKPNFSRIAQIASYVNPNYALVARK---FVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITDNP 242
Cdd:cd08582  160 --RNYKSPKEDPRPLAKSGGAAGLDLSYEKKLnpaFIKALRDAGLKLNVWTVDDAEDAKRLIELGVDSITTNRP 231
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 12-247 5.75e-50

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: 163.97  E-value: 5.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFG------ 85
Cdd:cd08561    1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGyhftdd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  86 --SYKDVAFKGERIPTLDEVLSLClkYDKKLLIELKSPNlyPEIECKLLAFLEEKkvDAT-QVVIQSFDIECIEKLN--- 159
Cdd:cd08561   81 ggRTYPYRGQGIRIPTLEELFEAF--PDVRLNIEIKDDG--PAAAAALADLIERY--GAQdRVLVASFSDRVLRRFRrlc 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 160 ----TLGSIYELGVLCSKRN---YWYKKPNFSRIaQIASYVNPnYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQM 232
Cdd:cd08561  155 prvaTSAGEGEVAAFVLASRlglGSLYSPPYDAL-QIPVRYGG-VPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRLLDL 232

                        250
                 ....*....|....*
gi 578116615 233 GVDGLITDNPKLFIK 247
Cdd:cd08561  233 GVDGIITDRPDLLLE 247
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 12-245 1.15e-49

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: 163.26  E-value: 1.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDG--KGRIADYTLSQLKSFDFGS--- 86
Cdd:cd08601    3 VIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIerPGPVKDYTLAEIKQLDAGSwfn 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  87 -----YKDVAFKGERIPTLDEVLSLcLKYDKKLLIELKSPNLYPEIECKLLAFLEE-----KKVDATQVVIQSFDIECIE 156
Cdd:cd08601   83 kaypeYARESYSGLKVPTLEEVIER-YGGRANYYIETKSPDLYPGMEEKLLATLDKyglltDNLKNGQVIIQSFSKESLK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 157 KLNTLGSIYELGVLcskrnYWYKKP---NFSRIAQIASY---VNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLR 230
Cdd:cd08601  162 KLHQLNPNIPLVQL-----LWYGEGaetYDKWLDEIKEYaigIGPSIADADPWMVHLIHKKGLLVHPYTVNEKADMIRLI 236

                        250
                 ....*....|....*
gi 578116615 231 QMGVDGLITDNPKLF 245
Cdd:cd08601  237 NWGVDGMFTNYPDRL 251
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 15-242 2.46e-49

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: 162.18  E-value: 2.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615   15 HRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSYKDVAFKG 94
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGNSGPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615   95 ER--IPTLDEVLSLCLKYDKKLLIELKSPNLYPEIEC------KLLAFLE--EKKVDATQVVIQSFDIECIEKLNTLGSI 164
Cdd:pfam03009  81 ERvpFPTLEEVLEFDWDVGFNIEIKIKPYVEAIAPEEglivkdLLLSVDEilAKKADPRRVIFSSFNPDELKRLRELAPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  165 YELGVLCSKRNYWY--KKPNFSRIAQIASY--VNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITD 240
Cdd:pfam03009 161 LPLVFLSSGRAYAEadLLERAAAFAGAPALlgEVALVDEALPDLVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVITD 240


                  ..
gi 578116615  241 NP 242
Cdd:pfam03009 241 RP 242
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 12-242 1.13e-41

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: 141.53  E-value: 1.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSYkdva 91
Cdd:cd08579    1 IIAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIGEN---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  92 FKGERIPTLDEVLSLCLKYDKKLLIELK-SPNLYPEIECKLLAFLEEKKVdATQVVIQSFDIECIEKLNTL------GSI 164
Cdd:cd08579   77 GHGAKIPSLDEYLALAKGLKQKLLIELKpHGHDSPDLVEKFVKLYKQNLI-ENQHQVHSLDYRVIEKVKKLdpkiktGYI 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578116615 165 YELgvlcSKRNYWYKKPNFSRIaqiasyvnpNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITDNP 242
Cdd:cd08579  156 LPF----NIGNLPKTNVDFYSI---------EYSTLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 12-242 4.10e-39

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: 137.40  E-value: 4.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSD------------GKGRIADYTLSQL 79
Cdd:cd08559    3 VIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNvaehfpfrgrkdTGYFVIDFTLAEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  80 KSFDFGSYKDVAFK--------GERIPTLDEVLSLCLKYDKKLL------IELKSPN----LYPEIECKLLAFLEEKKVD 141
Cdd:cd08559   83 KTLRAGSWFNQRYPerapsyygGFKIPTLEEVIELAQGLNKSTGrnvgiyPETKHPTfhkqEGPDIEEKLLEVLKKYGYT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 142 AT--QVVIQSFDIECIEKLNT---------LGSIYELGVLCSKRNYWYKKpNFSRIAQIASYV-------------NPNY 197
Cdd:cd08559  163 GKndPVFIQSFEPESLKRLRNetpdiplvqLIDYGDWAETDKKYTYAWLT-TDAGLKEIAKYAdgigpwksliipeDSNG 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578116615 198 ALVARKFVDKAHHHQLQVMPYTVNKLKTGEK----------LRQMGVDGLITDNP 242
Cdd:cd08559  242 LLVPTDLVKDAHKAGLLVHPYTFRNENLFLApdfkqdmdalYNAAGVDGVFTDFP 296
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 10-244 5.97e-39

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: 135.90  E-value: 5.97e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  10 LQIVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETID----RTSDGKGR------IADYTLSQL 79
Cdd:cd08567    1 FDLQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNpditRDPDGAWLpyegpaLYELTLAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  80 KSFDFGS----------YKD-VAFKGERIPTLDEVLSLCLKYDKK---LLIELKSPNLYP-------EIECKLLAFLEEK 138
Cdd:cd08567   81 KQLDVGEkrpgsdyaklFPEqIPVPGTRIPTLEEVFALVEKYGNQkvrFNIETKSDPDRDilhpppeEFVDAVLAVIRKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 139 KVDAtQVVIQSFDIECIEKLNTLGSIYELGVLCSKRnywyKKPNFSRIAQIAS--YVNPNYALVARKFVDKAHHHQLQVM 216
Cdd:cd08567  161 GLED-RVVLQSFDWRTLQEVRRLAPDIPTVALTEET----TLGNLPRAAKKLGadIWSPYFTLVTKELVDEAHALGLKVV 235

                        250       260
                 ....*....|....*....|....*...
gi 578116615 217 PYTVNKLKTGEKLRQMGVDGLITDNPKL 244
Cdd:cd08567  236 PWTVNDPEDMARLIDLGVDGIITDYPDL 263
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 11-242 3.02e-35

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: 125.49  E-value: 3.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  11 QIVSHRGLPSD-FPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSyKD 89
Cdd:cd08566    1 LVVAHRGGWGAgAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKD-GD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  90 VAFKGERIPTLDEVLSLClkyDKKLLIEL-KSPNLYPEIecklLAFLEEKKvDATQVVIQSFDIECIEKLNTLGSIYELG 168
Cdd:cd08566   80 GEVTDEKVPTLEEALAWA---KGKILLNLdLKDADLDEV----IALVKKHG-ALDQVIFKSYSEEQAKELRALAPEVMLM 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 169 VLCSKRNYWYKKPNFSRIAQ--IASYVNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTG-------------EKLRQMG 233
Cdd:cd08566  152 PIVRDAEDLDEEEARAIDALnlLAFEITFDDLDLPPLFDELLRALGIRVWVNTLGDDDTAgldralsdprevwGELVDAG 231


                 ....*....
gi 578116615 234 VDGLITDNP 242
Cdd:cd08566  232 VDVIQTDRP 240
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 11-159 8.99e-35

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: 125.02  E-value: 8.99e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  11 QIVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFD------F 84
Cdd:cd08575    2 LHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDagygytF 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578116615  85 GSYKDVAFKGE---RIPTLDEVLSlclKY-DKKLLIELKSPNLYPEIEcKLLAFLEEKKVdATQVVIQSFDIECIEKLN 159
Cdd:cd08575   82 DGGKTGYPRGGgdgRIPTLEEVFK---AFpDTPINIDIKSPDAEELIA-AVLDLLEKYKR-EDRTVWGSTNPEYLRALH 155
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 12-244 1.86e-33

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: 120.97  E-value: 1.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGsYKDva 91
Cdd:cd08565    1 IAGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLR-DSF-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  92 fkGERIPTLDEVLSLCLKYDKKLLIELKS---PNLYPEIECKLLAFLEEKKVdATQVVIQSFDIECIEKLNTLGSIYELG 168
Cdd:cd08565   78 --GEKIPTLEEVLALFAPSGLELHVEIKTdadGTPYPGAAALAAATLRRHGL-LERSVLTSFDPAVLTEVRKHPGVRTLG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 169 VLCSKRNywYKKPNFSRIAQIASY----VNPNYALVARKFVD-KAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITDNPK 243
Cdd:cd08565  155 SVDEDML--ERLGGELPFLTATALkahiVAVEQSLLAATWELvRAAVPGLRLGVWTVNDDSLIRYWLACGVRQLTTDRPD 232


                 .
gi 578116615 244 L 244
Cdd:cd08565  233 L 233
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 12-245 2.54e-31

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 115.81  E-value: 2.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSYKDVA 91
Cdd:PRK09454  10 IVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  92 FKGERIPTLDEVLSLCLKYDKKLLIELKsPNLYPEIECKLLAFLEEKKVDATQVV---IQSFDIECIEKLNTLGSIYELG 168
Cdd:PRK09454  90 FAGEPLPTLSQVAARCRAHGMAANIEIK-PTTGREAETGRVVALAARALWAGAAVpplLSSFSEDALEAARQAAPELPRG 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578116615 169 VLCSK-RNYWykkpnFSRIAQI-ASYVNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITDNPKLF 245
Cdd:PRK09454 169 LLLDEwPDDW-----LELTRRLgCVSLHLNHKLLDEARVAALKAAGLRILVYTVNDPARARELLRWGVDCICTDRIDLI 242
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 12-242 1.66e-28

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: 107.80  E-value: 1.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFD------FG 85
Cdd:cd08581    1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRvaeparFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  86 SykdvAFKGERIPTLDEVLSLCLKYDK-KLLIELKSPNL-YPEIECKLLAFLEEKKVDATQVVIQSFDIECIEKLNTLGs 163
Cdd:cd08581   81 S----RFAGEPLPSLAAVVQWLAQHPQvTLFVEIKTESLdRFGLERVVDKVLRALPAVAAQRVLISFDYDLLALAKQQG- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 164 IYELGVLCSKrnywYKKPNFSRIAQI-ASYVNPNYALVARkfVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITDNP 242
Cdd:cd08581  156 GPRTGWVLPD----WDDASLAEADELqPDYLFCDKNLLPD--TGDLWAGTWKWVIYEVNEPAEALALAARGVALIETDNI 229
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 12-120 1.76e-26

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: 103.11  E-value: 1.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFG---SYK 88
Cdd:cd08573    1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAakhRLS 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 578116615  89 DvAFKGERIPTLDEVLSLCLKYDKKLLIELKS 120
Cdd:cd08573   81 S-RFPGEKIPTLEEAVKECLENNLRMIFDVKS 111
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 12-242 1.06e-22

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL206cp and uncharacterized hypothetical homologs existing in fungi. The product of S. cerevisiae ORF YPL206c (PGC1), YPL206cp (Pgc1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL206cp is an integral membrane protein with a single GDPD domain following by a short hydrophobic C-terminal tail that may function as a membrane anchor. This protein plays an essential role in the regulation of the cardiolipin (CL) biosynthetic pathway in yeast by removing the excess phosphatidylglycerol (PG) content of membranes via a phospholipase C-type degradation mechanism. YPL206cp has been characterized as a PG-specific phospholipase C that selectively catalyzes the cleavage of PG, not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate. Members in this family are distantly related to S. cerevisiae YPL110cp, which selectively hydrolyzes glycerophosphocholine (GPC), not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate, and has been characterized as a cytoplasmic GPC-specific phosphodiesterase.


Pssm-ID: 176512 [Multi-domain]  Cd Length: 234  Bit Score: 92.67  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYT----LSQLKSFDFGSy 87
Cdd:cd08570    1 VIGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDStwdeLSHLRTIEEPH- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  88 kdvafkgERIPTLDEVLSLCLKY---DKKLLIELKSPNLyPEIECKLLAFLEEKKVD-------------------ATQV 145
Cdd:cd08570   80 -------QPMPTLKDVLEWLVEHelpDVKLMLDIKRDND-PEILFKLIAEMLAVKPDldfwreriilglwhldflkYGKE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 146 VIQSFDIECIeklntlgsiyELGVLCSKRNYWYKKPNFSriaqiasyVNPNYALVA----RKFVDKAHHHQLQVMPYTVN 221
Cdd:cd08570  152 VLPGFPVFHI----------GFSLDYARHFLNYSEKLVG--------ISMHFVSLWgpfgQAFLPELKKNGKKVFVWTVN 213

                        250       260
                 ....*....|....*....|.
gi 578116615 222 KLKTGEKLRQMGVDGLITDNP 242
Cdd:cd08570  214 TEEDMRYAIRLGVDGVITDDP 234
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 12-245 2.41e-22

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: 91.59  E-value: 2.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGsykdva 91
Cdd:cd08568    2 ILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHPG------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  92 fkGERIPTLDEVLSLcLKYDKKLLIELKspnlypEIEC--KLLAFLEEKKVDAtQVVIQSFDIECIEKLNTLGSIYELGV 169
Cdd:cd08568   76 --GELIPTLEEVFRA-LPNDAIINVEIK------DIDAvePVLEIVEKFNALD-RVIFSSFNHDALRELRKLDPDAKVGL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 170 LCSKRNYWYKKPNFSRIAQIASyVNPNYALV-------ARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMgVDGLITDNP 242
Cdd:cd08568  146 LIGEEEEGFSIPELHEKLKLYS-LHVPIDAIgyigfekFVELLRLLRKLGLKIVLWTVNDPELVPKLKGL-VDGVITDDV 223


                 ...
gi 578116615 243 KLF 245
Cdd:cd08568  224 EKI 226
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 13-151 8.36e-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: 90.07  E-value: 8.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  13 VSHRGLPS---DFPENTMVGYREVMGLNVAmLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFGSykd 89
Cdd:cd08585    7 IAHRGLHDrdaGIPENSLSAFRAAAEAGYG-IELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRLLG--- 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578116615  90 vafKGERIPTLDEVLSLclkYDKK--LLIELKSPNLYPE-IECKLLAFLEEKKVDAtqvVIQSFD 151
Cdd:cd08585   83 ---TDEHIPTLDEVLEL---VAGRvpLLIELKSCGGGDGgLERRVLAALKDYKGPA---AIMSFD 138
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 11-133 5.53e-20

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: 86.65  E-value: 5.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  11 QIVSHRGLPSDF-----------------P-----ENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGK 68
Cdd:cd08613   25 KLLAHRGLAQTFdregvendtctaeridpPthdylENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGS 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578116615  69 GRIADYTLSQLKSFDFG-SY-----KDVAFKGE---RIPTLDEVLSLClkYDKKLLIELKSPNLypeIECKLLA 133
Cdd:cd08613  105 GVTRDHTMAELKTLDIGyGYtadggKTFPFRGKgvgMMPTLDEVFAAF--PDRRFLINFKSDDA---AEGELLA 173
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 11-242 1.62e-19

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: 85.43  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  11 QIVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDG------KGRIA------------ 72
Cdd:cd08602    2 LVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVadhpefADRKTtktvdgvnvtgw 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  73 ---DYTLSQLKSF---DFGSYKDVAFKGE-RIPTLDEVLSLCLKYDKKLL------IELKSPNLYPE-----IECKLLAF 134
Cdd:cd08602   82 fteDFTLAELKTLrarQRLPYRDQSYDGQfPIPTFEEIIALAKAASAATGrtvgiyPEIKHPTYFNAplglpMEDKLLET 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 135 LEE---KKVDATqVVIQSFDIECIEKLNTL------------GSIYELGVLCSKRNYWYK--KPNFSRIAQIASYVNP-- 195
Cdd:cd08602  162 LKKygyTGKKAP-VFIQSFEVTNLKYLRNKtdlplvqliddaTIPPQDTPEGDSRTYADLttDAGLKEIATYADGIGPwk 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578116615 196 ---------NYALVARKFVDKAHHHQLQVMPYTV-------------NKLKTGEKLRQMGVDGLITDNP 242
Cdd:cd08602  241 dliipsdanGRLGTPTDLVEDAHAAGLQVHPYTFrnentflppdffgDPYAEYRAFLDAGVDGLFTDFP 309
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 12-242 7.23e-19

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: 83.59  E-value: 7.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTS------------DGKGRIADYTLSQL 79
Cdd:cd08600    3 IIAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTnvaekfpdrkrkDGRYYVIDFTLDEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  80 KS------FDFGSYKDVAFKGER---------IPTLDEVLSLCLKYDKK------LLIELKSPNLYPE----IECKLLAF 134
Cdd:cd08600   83 KSlsvterFDIENGKKVQVYPNRfplwksdfkIHTLEEEIELIQGLNKStgknvgIYPEIKAPWFHHQegkdIAAATLEV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 135 LEEKKVD--ATQVVIQSFDIECIEKL-NTLGSIYELGV----LCSKR------------------NYWYKKPNFSRIAQI 189
Cdd:cd08600  163 LKKYGYTskNDKVYLQTFDPNELKRIkNELLPKMGMDLklvqLIAYTdwgetqekdpggwvnydyDWMFTKGGLKEIAKY 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578116615 190 ASYVNPNYALVARK-----------FVDKAHHHQLQVMPYTVNKLKTGEK-----------LRQMGVDGLITDNP 242
Cdd:cd08600  243 ADGVGPWYSMIIEEksskgnivltdLVKDAHEAGLEVHPYTVRKDALPEYakdadqlldalLNKAGVDGVFTDFP 317
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 11-160 8.03e-19

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial protein Rv2277c and similar proteins. Members in this subfamily are bacterial homologous of mammalian GDE4, a transmembrane protein whose cellular function has not yet been elucidated.


Pssm-ID: 176522 [Multi-domain]  Cd Length: 263  Bit Score: 82.76  E-value: 8.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  11 QIVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADYTLSQLKSFDFG---SY 87
Cdd:cd08580    2 LIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAGynfKP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578116615  88 KDVAF---KGERIPTLDEVLSlclKYDKKLLI-ELKSPNlyPEIECKLLAFLEEKKVDATQVVIQSFDIECIEKLNT 160
Cdd:cd08580   82 EGGYPyrgKPVGIPTLEQVLR---AFPDTPFIlDMKSLP--ADPQAKAVARVLERENAWSRVRIYSTNADYQDALAP 153
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 12-246 5.31e-18

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: 80.59  E-value: 5.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSD--FPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIH---DETIDRTS-----DGKGRIADYTLSQLKS 81
Cdd:cd08564    6 IVGHRGAGCStlYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteDDTNPDTSiqlddSGFKNINDLSLDEITR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  82 FDFGSYKDVAF------KGERIPTLDEVLSLC---LKYDkkllIELKSPNLypEIECKLLAFLEEKKvDATQVVIQSFdi 152
Cdd:cd08564   86 LHFKQLFDEKPcgadeiKGEKIPTLEDVLVTFkdkLKYN----IELKGREV--GLGERVLNLVEKYG-MILQVHFSSF-- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 153 ecieklNTLGSIYELGVLCSKRN-------YWYKK----PNFSRIAQI--ASYVNPNYALVARKFVDKAHHHQLQVMPY- 218
Cdd:cd08564  157 ------LHYDRLDLLKALRPNKLnvpiallFNEVKspspLDFLEQAKYynATWVNFSYDFWTEEFVKKAHENGLKVMTYf 230

                        250       260       270
                 ....*....|....*....|....*....|.
gi 578116615 219 ---TVNKLKTGEKLRQMGVDGLITDNPKLFI 246
Cdd:cd08564  231 depVNDNEEDYKVYLELGVDCICPNDPVLLV 261
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 11-241 1.21e-16

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: 77.32  E-value: 1.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  11 QIVSHRGL--------PSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETI-----DRTSDGKGRIADY--- 74
Cdd:cd08572    1 LVIGHRGLgknyasgsLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTIsvsekSKTGSDEGELIEVpih 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  75 --TLSQLKSF----------DFGSYKDVAFKGE--------RIPTLDEVLSlclKYDKKL--LIELKSPNLYPEIECKLL 132
Cdd:cd08572   81 dlTLEQLKELglqhisalkrKALTRKAKGPKPNpwgmdehdPFPTLQEVLE---QVPKDLgfNIEIKYPQLLEDGEGELT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 133 AFLE-EKKVDAT-QVVIQ----------SFDIE-CI---EKLN-------TLGSIYELGVLCSKRNYWYKKPNFSRIAQI 189
Cdd:cd08572  158 PYFErNAFVDTIlAVVFEhaggrriifsSFDPDiCImlrLKQNkypvlflTNGGTNEVEHMDPRRRSLQAAVNFALAEGL 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578116615 190 AsYVNPNYALVARK--FVDKAHHHQLQVMPY--TVNKLKTGEKLRQMGVDGLITDN 241
Cdd:cd08572  238 L-GVVLHAEDLLKNpsLISLVKALGLVLFTYgdDNNDPENVKKQKELGVDGVIYDR 292
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 13-245 8.25e-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: 74.94  E-value: 8.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  13 VSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGRIADY-------TLSQLK-SFDF 84
Cdd:cd08612   30 ISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLnyadlppYLEKLEvTFSP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  85 GSYKDVAFKGERIPTLDEVLSlclKY-DKKLLIELKSPNlyPEIECKLLAFLEE-KKVDATqvVIQSFDIECIEKLN--- 159
Cdd:cd08612  110 GDYCVPKGSDRRIPLLEEVFE---AFpDTPINIDIKVEN--DELIKKVSDLVRKyKREDIT--VWGSFNDEIVKKCHken 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 160 --------------TLGSIYeLGVL--------------CSKRNYWYKKPNFSRIAQIASYVnPNYALVARKFVDKAHHH 211
Cdd:cd08612  183 pniplffslkrvllLLLLYY-TGLLpfipikesfleipmPSIFLKTYFPKSMSRLNRFVLFL-IDWLLMRPSLFRHLQKR 260

                        250       260       270
                 ....*....|....*....|....*....|....
gi 578116615 212 QLQVMPYTVNKLKTGEKLRQMGVDGLITDNPKLF 245
Cdd:cd08612  261 GIQVYGWVLNDEEEFERAFELGADGVMTDYPTKL 294
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 12-247 4.17e-15

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 73.55  E-value: 4.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTS------------DGKGRIADYTLSQL 79
Cdd:PRK11143  29 VIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTdvaerfpdrarkDGRYYAIDFTLDEI 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  80 KS------FDFGSYKDVA-FKGE--------RIPTLDEVLSL------CLKYDKKLLIELKSPNLYPE----IECKLLAF 134
Cdd:PRK11143 109 KSlkftegFDIENGKKVQvYPGRfpmgksdfRVHTFEEEIEFiqglnhSTGKNIGIYPEIKAPWFHHQegkdIAAKVLEV 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 135 LEE----KKVDAtqVVIQSFDIECIEKLNT--------------------LGSIYELGVLCSKRNY---WYKKPN-FSRI 186
Cdd:PRK11143 189 LKKygytGKDDK--VYLQCFDANELKRIKNelepkmgmdlklvqliaytdWNETQEKQPDGKWVNYnydWMFKPGaMKEV 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 187 AQIASYVNPNY-ALVARK----------FVDKAHHHQLQVMPYTVNK------LKTGEKLR-----QMGVDGLITDNPKL 244
Cdd:PRK11143 267 AKYADGIGPDYhMLVDETstpgnikltgMVKEAHQAKLVVHPYTVRAdqlpeyATDVNQLYdilynQAGVDGVFTDFPDK 346


                 ...
gi 578116615 245 FIK 247
Cdd:PRK11143 347 AVK 349
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 12-240 9.63e-15

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: 70.16  E-value: 9.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKgriadytlsqlksfdfgsykdva 91
Cdd:cd08555    1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGI----------------------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  92 fkgeRIPTLDEVLSLC------LKYDKKLLIELKSPNL-YPEIECKLLAFLEEKKVD--ATQVVIQSFDIECIEKLntlg 162
Cdd:cd08555   58 ----LPPTLEEVLELIadylknPDYTIILSLEIKQDSPeYDEFLAKVLKELRVYFDYdlRGKVVLSSFNALGVDYY---- 129

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578116615 163 siyelgvlcskrnywykkpNFSRIAQIASyvnpnyalvarKFVDKAHHHQLQVMPYTVNK-LKTGEKLRQMGVDGLITD 240
Cdd:cd08555  130 -------------------NFSSKLIKDT-----------ELIASANKLGLLSRIWTVNDnNEIINKFLNLGVDGLITD 178
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 13-240 8.15e-13

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: 66.55  E-value: 8.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  13 VSHRGLPSDF-------PENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKGR----------IADYT 75
Cdd:cd08607    3 VGHRGAGNSYtaasavvRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDsdrddllevpVKDLT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  76 LSQLKSFDF--------GSYKDVAFKGER-----IPTLDEVLSlclKYDKKL--LIELKSPNLYP--EIECKLLAFLEEK 138
Cdd:cd08607   83 YEQLKLLKLfhisalkvKEYKSVEEDEDPpehqpFPTLSDVLE---SVPEDVgfNIEIKWPQQQKdgSWESELFTYFDRN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 139 K-VDAT-QVVIQ----------SFDIECIEKLNTLGSIYELGVLC-SKRNYW--YKKP---------NFSRIAQIASyVN 194
Cdd:cd08607  160 LfVDIIlKIVLEhagkrriifsSFDADICTMLRFKQNKYPVLFLTqGKTQRYpeFMDLrtrtfeiavNFAQAEELLG-VN 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 578116615 195 PNYALVARK--FVDKAHHHQLQVMPY--TVNKLKTGEKLRQMGVDGLITD 240
Cdd:cd08607  239 LHSEDLLKDpsQIELAKSLGLVVFCWgdDLNDPENRKKLKELGVDGLIYD 288
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 1-122 1.19e-12

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: 66.10  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615   1 MTLNKLKDELQIVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGK----GRIA---- 72
Cdd:cd08609   18 MEENNLPPKPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKdvfpGRDAagsn 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578116615  73 DYTLSQLKSFDFGSY----------------KDVAFKGERIPTLDEVLSLCLKYDKKLLIELKSPN 122
Cdd:cd08609   98 NFTWTELKTLNAGSWflerrpfwtlsslseeDRREADNQTVPSLSELLDLAKKHNVSIMFDLRNEN 163
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 11-122 1.66e-09

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: 56.55  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  11 QIVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDGKG--------RIADYTLSQLKSF 82
Cdd:cd08574    3 ALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVADvfperaheRASMFTWTDLQQL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578116615  83 DFG---------------SYKD-VAFKGERIPTLDEVLSLCLKYDKKLLIELKSPN 122
Cdd:cd08574   83 NAGqwflkddpfwtasslSESDrEEAGNQSIPSLAELLRLAKKHNKSVIFDLRRPP 138
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 6-187 8.80e-06

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: 45.88  E-value: 8.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615   6 LKDELQI------------VSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDE-------------- 59
Cdd:cd08560    1 LKDKLLScaekpfrktdfsIGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSQcdlhtttnilaipe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  60 ------------TIDRTSDGKGRIADYTLSQLKS-------FDFGSYKDVAFKG-------------ERIPTLDEVLSLC 107
Cdd:cd08560   81 laakctqpftpaNATKPASAECCTSDITLAEFKSlcgkmdaSNPSATTPEEYQNgtpdwrtdlyatcGTLMTHKESIALF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 108 LKYDKKLLIELKSPNL------------YPEiecKLLAFLEEKKVDATQVVIQSFDIECIEklntlgsiyelgvlcskrn 175
Cdd:cd08560  161 KSLGVKMTPELKSPSVpmpfdgnytqedYAQ---QMIDEYKEAGVPPSRVWPQSFNLDDIF------------------- 218

                        250
                 ....*....|...
gi 578116615 176 YWYKK-PNFSRIA 187
Cdd:cd08560  219 YWIKNePDFGRQA 231
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 12-121 2.05e-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: 44.86  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  12 IVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTS--------DGKGRIADYTLSQLKSFD 83
Cdd:cd08610   25 IIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTnigevqpeSACENPAFFNWDFLSTLN 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578116615  84 FGSY--KDVAF--------------KGERIPTLDEVLSLCLKYDKKLLIELKSP 121
Cdd:cd08610  105 AGKWfvKPRPFynmkplseadkeraRNQSIPKLSNFLRLAEKENKLVIFDLYRP 158
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 11-66 2.39e-05

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: 44.84  E-value: 2.39e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578116615  11 QIVSHRGLPSDFPENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSD 66
Cdd:cd08608    3 AIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTN 58
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 11-137 4.51e-04

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: 40.51  E-value: 4.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  11 QIVSHRGLPSDFP--------ENTMVGYREVMGLNVAMLEIDVHLTKDQHFVVIHDETIDRTSDgKGRIADYTLSQLKSF 82
Cdd:cd08606    3 QVIGHRGLGKNTAerkslqlgENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETGT-DVPIHDLTLEQFLHL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578116615  83 DFGSY----KDVAFKGER--------IPTLDEVLSLcLKYDKKLLIELKSPNLYPEIECKLLAFLEE 137
Cdd:cd08606   82 SRMKYtvdfKKKGFKGNSrghsiqapFTTLEELLKK-LPKSVGFNIELKYPMLHEAEEEEVAPVAIE 147
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 40-240 5.54e-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: 39.98  E-value: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615  40 MLEIDVHLTKDQHFVVIHDETiDRTSDGKGRIADYTLSQLKSFDF------GSYKDVAFKgeriptldEVLSLCLKY-DK 112
Cdd:cd08583   31 VFEVDLSLTSDGVLVARHSWD-ESLLKQLGLPTSKNTKPLSYEEFkskkiyGKYTPMDFK--------DVIDLLKKYpDV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578116615 113 KLLIELKS--PNLYPEIECKLLAFLEEKKVDA-TQVVIQSFDIECIEKLNtlgSIYELGvlcSKRNYWYKKP-------- 181
Cdd:cd08583  102 YIVTDTKQddDNDIKKLYEYIVKEAKEVDPDLlDRVIPQIYNEEMYEAIM---SIYPFK---SVIYTLYRQDsirldeii 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578116615 182 NFSRIAQIASyVNPNYALVARKFVDKAHHHQLQVMPYTVNKLKTGEKLRQMGVDGLITD 240
Cdd:cd08583  176 AFCYENGIKA-VTISKNYVNDKLIEKLNKAGIYVYVYTINDLKDAQEYKKLGVYGIYTD 233
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH