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Conserved domains on  [gi|47575864|ref|NP_116004|]
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glycerophosphodiester phosphodiesterase 1 [Rattus norvegicus]

Protein Classification

glycerophosphodiester phosphodiesterase family protein( domain architecture ID 10171153)

glycerophosphodiester phosphodiesterase (GDPD) family protein similar to Homo sapiens glycerophosphodiester phosphodiesterase 1 (GDE1) that hydrolyzes the phosphodiester bond of glycerophosphodiesters such as glycerophosphoinositol (GroPIns) and glycerophosphoethanolamine (GroPEth), to yield a glycerol phosphate and an alcohol

EC:  3.1.4.-
Gene Ontology:  GO:0008081|GO:0006629

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 68-323 5.18e-152

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: 427.06  E-value: 5.18e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAANHRLRN 147
Cdd:cd08573   2 IGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRLSS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 148 EFPDERIPTLREAVTECLCHNLTIFFDVKGHADMASAALKNIYMEFPQLYNNSMVCSFLPEVIYKMRQTDQKVITALTHR 227
Cdd:cd08573  82 RFPGEKIPTLEEAVKECLENNLRMIFDVKSNSSKLVDALKNLFKKYPGLYDKAIVCSFNPIVIYKVRKADPKILTGLTWR 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 228 PWSLSHTGD-GKPRYSVFWKQSVFVVLDILLDWSMHNVLWYLCGISAFLMQKDFVSPDYLKKWSAKGIQVVSWTVNTFDE 306
Cdd:cd08573 162 PWFLSYTDDeGGPRRKSGWKHFLYSMLDVILEWSLHSWLPYFLGVSALLIHKDDISSAYVRYWRARGIRVIAWTVNTPTE 241

                       250
                ....*....|....*..
gi 47575864 307 KNYYESHLGSSYITDSM 323
Cdd:cd08573 242 KQYFAKTLNVPYITDSL 258
 
Name Accession Description Interval E-value
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 68-323 5.18e-152

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: 427.06  E-value: 5.18e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAANHRLRN 147
Cdd:cd08573   2 IGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRLSS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 148 EFPDERIPTLREAVTECLCHNLTIFFDVKGHADMASAALKNIYMEFPQLYNNSMVCSFLPEVIYKMRQTDQKVITALTHR 227
Cdd:cd08573  82 RFPGEKIPTLEEAVKECLENNLRMIFDVKSNSSKLVDALKNLFKKYPGLYDKAIVCSFNPIVIYKVRKADPKILTGLTWR 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 228 PWSLSHTGD-GKPRYSVFWKQSVFVVLDILLDWSMHNVLWYLCGISAFLMQKDFVSPDYLKKWSAKGIQVVSWTVNTFDE 306
Cdd:cd08573 162 PWFLSYTDDeGGPRRKSGWKHFLYSMLDVILEWSLHSWLPYFLGVSALLIHKDDISSAYVRYWRARGIRVIAWTVNTPTE 241

                       250
                ....*....|....*..
gi 47575864 307 KNYYESHLGSSYITDSM 323
Cdd:cd08573 242 KQYFAKTLNVPYITDSL 258
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
68-306 3.36e-51

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 169.66  E-value: 3.36e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAANHrlrn 147
Cdd:COG0584   6 IAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGSGP---- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 148 EFPDERIPTLREAVTECLcHNLTIFFDVK----GHADMASAALKNIymEFPQLYNNSMVCSFLPEVIYKMRQTDQKVITA 223
Cdd:COG0584  82 DFAGERIPTLEEVLELVP-GDVGLNIEIKsppaAEPDLAEAVAALL--KRYGLEDRVIVSSFDPEALRRLRELAPDVPLG 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 224 LthrpwslshtgdgkprysvfwkqsvfvvldiLLDWSMHNVLWYL--CGISAFLMQKDFVSPDYLKKWSAKGIQVVSWTV 301
Cdd:COG0584 159 L-------------------------------LVEELPADPLELAraLGADGVGPDYDLLTPELVAAAHAAGLKVHVWTV 207


                ....*
gi 47575864 302 NTFDE 306
Cdd:COG0584 208 NDPEE 212
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 70-306 2.43e-39

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: 139.07  E-value: 2.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864    70 HRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAANHrlRNEF 149
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGN--SGPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864   150 PDER--IPTLREAVTECLCHNLTIFFDVKghadmasaalknIYMEFPQLYNNSMVCSFLPEV--IYKMRQTDQKVItALT 225
Cdd:pfam03009  79 SGERvpFPTLEEVLEFDWDVGFNIEIKIK------------PYVEAIAPEEGLIVKDLLLSVdeILAKKADPRRVI-FSS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864   226 HRPWSLSHTGDGKPRYSVFwkqSVFVVLDILLDWSMHNVLWYLcGISAFLMQ---KDFVSPDYLKKWSAKGIQVVSWTVN 302
Cdd:pfam03009 146 FNPDELKRLRELAPKLPLV---FLSSGRAYAEADLLERAAAFA-GAPALLGEvalVDEALPDLVKRAHARGLVVHVWTVN 221


                  ....
gi 47575864   303 TFDE 306
Cdd:pfam03009 222 NEDE 225
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 68-169 1.31e-31

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 118.89  E-value: 1.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864   68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAANHRLRn 147
Cdd:PRK09454  11 VAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAA- 89

                         90       100
                 ....*....|....*....|..
gi 47575864  148 eFPDERIPTLREAVTECLCHNL 169
Cdd:PRK09454  90 -FAGEPLPTLSQVAARCRAHGM 110
 
Name Accession Description Interval E-value
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 68-323 5.18e-152

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: 427.06  E-value: 5.18e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAANHRLRN 147
Cdd:cd08573   2 IGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRLSS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 148 EFPDERIPTLREAVTECLCHNLTIFFDVKGHADMASAALKNIYMEFPQLYNNSMVCSFLPEVIYKMRQTDQKVITALTHR 227
Cdd:cd08573  82 RFPGEKIPTLEEAVKECLENNLRMIFDVKSNSSKLVDALKNLFKKYPGLYDKAIVCSFNPIVIYKVRKADPKILTGLTWR 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 228 PWSLSHTGD-GKPRYSVFWKQSVFVVLDILLDWSMHNVLWYLCGISAFLMQKDFVSPDYLKKWSAKGIQVVSWTVNTFDE 306
Cdd:cd08573 162 PWFLSYTDDeGGPRRKSGWKHFLYSMLDVILEWSLHSWLPYFLGVSALLIHKDDISSAYVRYWRARGIRVIAWTVNTPTE 241

                       250
                ....*....|....*..
gi 47575864 307 KNYYESHLGSSYITDSM 323
Cdd:cd08573 242 KQYFAKTLNVPYITDSL 258
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
68-306 3.36e-51

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 169.66  E-value: 3.36e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAANHrlrn 147
Cdd:COG0584   6 IAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGSGP---- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 148 EFPDERIPTLREAVTECLcHNLTIFFDVK----GHADMASAALKNIymEFPQLYNNSMVCSFLPEVIYKMRQTDQKVITA 223
Cdd:COG0584  82 DFAGERIPTLEEVLELVP-GDVGLNIEIKsppaAEPDLAEAVAALL--KRYGLEDRVIVSSFDPEALRRLRELAPDVPLG 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 224 LthrpwslshtgdgkprysvfwkqsvfvvldiLLDWSMHNVLWYL--CGISAFLMQKDFVSPDYLKKWSAKGIQVVSWTV 301
Cdd:COG0584 159 L-------------------------------LVEELPADPLELAraLGADGVGPDYDLLTPELVAAAHAAGLKVHVWTV 207


                ....*
gi 47575864 302 NTFDE 306
Cdd:COG0584 208 NDPEE 212
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 68-320 8.36e-41

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: 142.45  E-value: 8.36e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAANHrlRN 147
Cdd:cd08582   2 IAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIGSWK--GE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 148 EFPDERIPTLREAVTECLCHNLTIFFDVKGH--ADMASAALKNIYMEFPQLYNNSMVCSFLPEVIYKMRQTDQKVITALT 225
Cdd:cd08582  80 SYKGEKVPTLEEYLAIVPKYGKKLFIEIKHPrrGPEAEEELLKLLKESGLLPEQIVIISFDAEALKRVRELAPTLETLWL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 226 HRPWSLSHTGDGKPRYSVFWKqsvfvvLDILLDWSMHnvlwylcgisaflmqkdfvsPDYLKKWSAKGIQVVSWTVNTFD 305
Cdd:cd08582 160 RNYKSPKEDPRPLAKSGGAAG------LDLSYEKKLN--------------------PAFIKALRDAGLKLNVWTVDDAE 213

                       250
                ....*....|....*.
gi 47575864 306 E-KNYYEshLGSSYIT 320
Cdd:cd08582 214 DaKRLIE--LGVDSIT 227
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 70-306 2.43e-39

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: 139.07  E-value: 2.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864    70 HRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAANHrlRNEF 149
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGN--SGPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864   150 PDER--IPTLREAVTECLCHNLTIFFDVKghadmasaalknIYMEFPQLYNNSMVCSFLPEV--IYKMRQTDQKVItALT 225
Cdd:pfam03009  79 SGERvpFPTLEEVLEFDWDVGFNIEIKIK------------PYVEAIAPEEGLIVKDLLLSVdeILAKKADPRRVI-FSS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864   226 HRPWSLSHTGDGKPRYSVFwkqSVFVVLDILLDWSMHNVLWYLcGISAFLMQ---KDFVSPDYLKKWSAKGIQVVSWTVN 302
Cdd:pfam03009 146 FNPDELKRLRELAPKLPLV---FLSSGRAYAEADLLERAAAFA-GAPALLGEvalVDEALPDLVKRAHARGLVVHVWTVN 221


                  ....
gi 47575864   303 TFDE 306
Cdd:pfam03009 222 NEDE 225
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 68-224 1.07e-38

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: 136.97  E-value: 1.07e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNpaANHRLRN 147
Cdd:cd08562   2 IAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLD--AGSWFSP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 148 EFPDERIPTLREAVTECLCHNLTIFFDVK---GHADMASAALKNIYMEFPQLYNNSMVCSFLPEVIYKMRQTDQKVITAL 224
Cdd:cd08562  80 EFAGEPIPTLADVLELARELGLGLNLEIKpdpGDEALTARVVAAALRELWPHASKLLLSSFSLEALRAARRAAPELPLGL 159
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 68-321 1.92e-37

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: 133.45  E-value: 1.92e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNpaANHRLRN 147
Cdd:cd08563   4 FAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLD--AGSWFDE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 148 EFPDERIPTLREAVTECLCH----NLTIFFDVKGHADMASAALKNIyMEFpQLYNNSMVCSFLPEVIYKMRQTDQKVITA 223
Cdd:cd08563  82 KFTGEKIPTLEEVLDLLKDKdlllNIEIKTDVIHYPGIEKKVLELV-KEY-NLEDRVIFSSFNHESLKRLKKLDPKIKLA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 224 LthrpwsLSHTGdgkprysvfwkqsvfvvldilldwsMHNVLWYLCGISAflmqkDFVSPDY-------LKKWSAKGIQV 296
Cdd:cd08563 160 L------LYETG-------------------------LQDPKDYAKKIGA-----DSLHPDFkllteevVEELKKRGIPV 203

                       250       260
                ....*....|....*....|....*
gi 47575864 297 VSWTVNTFDEKNYYESHLGSSYITD 321
Cdd:cd08563 204 RLWTVNEEEDMKRLKDLGVDGIITN 228
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 67-306 2.52e-37

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: 133.92  E-value: 2.52e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  67 AIAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAANHRLR 146
Cdd:cd08561   1 VIAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 147 NE--FP----DERIPTLREaVTECLcHNLTIFFDVKGHA-DMASAALKNIYMEFPQlyNNSMVCSFLPEVIYKMRQTDQK 219
Cdd:cd08561  81 GGrtYPyrgqGIRIPTLEE-LFEAF-PDVRLNIEIKDDGpAAAAALADLIERYGAQ--DRVLVASFSDRVLRRFRRLCPR 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 220 VITALThrpwslshTGDGKPrysvfwkqsvFVVLDILLDWSmhnvlWYLCGISAFLM---QKDF--VSPDYLKKWSAKGI 294
Cdd:cd08561 157 VATSAG--------EGEVAA----------FVLASRLGLGS-----LYSPPYDALQIpvrYGGVplVTPRFVRAAHAAGL 213

                       250
                ....*....|..
gi 47575864 295 QVVSWTVNTFDE 306
Cdd:cd08561 214 EVHVWTVNDPAE 225
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 68-176 7.24e-37

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: 132.43  E-value: 7.24e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHD-APENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLnpaanhRLR 146
Cdd:cd08566   3 VAHRGGWGAgAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKL------RLK 76

                        90       100       110
                ....*....|....*....|....*....|...
gi 47575864 147 NEFP---DERIPTLREAVtECLCHNLTIFFDVK 176
Cdd:cd08566  77 DGDGevtDEKVPTLEEAL-AWAKGKILLNLDLK 108
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 68-321 2.07e-36

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: 129.69  E-value: 2.07e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDntvdrttdgsgrlcdltfeqvrklnpaanhrlrn 147
Cdd:cd08556   2 IAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD---------------------------------- 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 148 efpderIPTLREAVTECLcHNLTIFFDVKGHADMASAA--LKNIYMEFPqLYNNSMVCSFLPEVIYKMRQTDQKVITALT 225
Cdd:cd08556  48 ------IPTLEEVLELVK-GGVGLNIELKEPTRYPGLEakVAELLREYG-LEERVVVSSFDHEALRALKELDPEVPTGLL 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 226 HRPWSLSHTGDGKPRYsvfwkqsvfvvldilldwsmhnvlwylCGISAFLMQKDFVSPDYLKKWSAKGIQVVSWTVNTFD 305
Cdd:cd08556 120 VDKPPLDPLLAELARA---------------------------LGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPE 172

                       250
                ....*....|....*.
gi 47575864 306 EKNYYESHLGSSYITD 321
Cdd:cd08556 173 DARRLLALGVDGIITD 188
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 68-169 1.31e-31

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 118.89  E-value: 1.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864   68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAANHRLRn 147
Cdd:PRK09454  11 VAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAA- 89

                         90       100
                 ....*....|....*....|..
gi 47575864  148 eFPDERIPTLREAVTECLCHNL 169
Cdd:PRK09454  90 -FAGEPLPTLSQVAARCRAHGM 110
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 68-179 2.90e-29

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: 112.04  E-value: 2.90e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAANHRLRN 147
Cdd:cd08581   2 VAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVAEPARFGS 81

                        90       100       110
                ....*....|....*....|....*....|....
gi 47575864 148 EFPDERIPTLrEAVTECLCHN--LTIFFDVKGHA 179
Cdd:cd08581  82 RFAGEPLPSL-AAVVQWLAQHpqVTLFVEIKTES 114
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 68-160 6.53e-28

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: 109.23  E-value: 6.53e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPA----ANH 143
Cdd:cd08575   4 IAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGygytFDG 83

                        90       100
                ....*....|....*....|
gi 47575864 144 RLRNEFP---DERIPTLREA 160
Cdd:cd08575  84 GKTGYPRgggDGRIPTLEEV 103
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 68-219 1.66e-27

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: 106.86  E-value: 1.66e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNpaanhrLRN 147
Cdd:cd08579   2 IAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLT------IGE 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47575864 148 EFPDERIPTLREAVTECLCHNLTIFFDVKGH----ADMASAALKNIY---MEfpqlyNNSMVCSFLPEVIYKMRQTDQK 219
Cdd:cd08579  76 NGHGAKIPSLDEYLALAKGLKQKLLIELKPHghdsPDLVEKFVKLYKqnlIE-----NQHQVHSLDYRVIEKVKKLDPK 149
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 67-303 8.80e-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 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: 100.09  E-value: 8.80e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  67 AIAHRG---GSHDAPENTLAAIRQAAKNGaTGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLnpaanh 143
Cdd:cd08585   6 PIAHRGlhdRDAGIPENSLSAFRAAAEAG-YGIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRAL------ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 144 RLRNEfpDERIPTLREaVTECLCHNLTIFFDVKGH--ADMA-SAALKNIYMEFPQLYnnsMVCSFLPEVIYKMRQTDQKV 220
Cdd:cd08585  79 RLLGT--DEHIPTLDE-VLELVAGRVPLLIELKSCggGDGGlERRVLAALKDYKGPA---AIMSFDPRVVRWFRKLAPGI 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 221 ITALTHRPWSLShtgdgkpRYSVFWKQSVFVVLdilldwsmhnvlwylcgISAFLMQKDFVS--PDYLKKWSAK------ 292
Cdd:cd08585 153 PRGQLSEGSNDE-------ADPAFWNEALLSAL-----------------FSNLLTRPDFIAyhLDDLPNPFVTlarall 208

                       250
                ....*....|.
gi 47575864 293 GIQVVSWTVNT 303
Cdd:cd08585 209 GMPVIVWTVRT 219
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 68-233 5.82e-24

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: 97.86  E-value: 5.82e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLnpaanhRLRN 147
Cdd:cd08565   2 AGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKAL------RLRD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 148 EFpDERIPTLRE-----AVTECLCHnLTIFFDVKGH-----ADMASAALKNIymefpQLYNNSMVCSFLPEVIYKMRqtd 217
Cdd:cd08565  76 SF-GEKIPTLEEvlalfAPSGLELH-VEIKTDADGTpypgaAALAAATLRRH-----GLLERSVLTSFDPAVLTEVR--- 145

                       170
                ....*....|....*...
gi 47575864 218 qkvitALTHRP--WSLSH 233
Cdd:cd08565 146 -----KHPGVRtlGSVDE 158
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 65-159 2.28e-23

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: 97.00  E-value: 2.28e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  65 VSAIAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGS--GRLCDLTFEQVRKL----- 137
Cdd:cd08601   1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIErpGPVKDYTLAEIKQLdagsw 80

                        90       100
                ....*....|....*....|...
gi 47575864 138 -NPAANHRLRNEFPDERIPTLRE 159
Cdd:cd08601  81 fNKAYPEYARESYSGLKVPTLEE 103
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 68-176 3.78e-23

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: 96.24  E-value: 3.78e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAANHRLRN 147
Cdd:cd08580   4 VAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLNAGYNFKPEG 83

                        90       100       110
                ....*....|....*....|....*....|...
gi 47575864 148 E--FPDE--RIPTLREAVTEclCHNLTIFFDVK 176
Cdd:cd08580  84 GypYRGKpvGIPTLEQVLRA--FPDTPFILDMK 114
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 68-309 1.48e-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: 93.90  E-value: 1.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLNPAanhrlrn 147
Cdd:cd08568   3 LGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHPG------- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 148 efpDERIPTLREaVTECLCHNLTIFFDVKgHADMASAALKnIYMEFPQLyNNSMVCSFLPEVIYKMRqtdqkvitalthr 227
Cdd:cd08568  76 ---GELIPTLEE-VFRALPNDAIINVEIK-DIDAVEPVLE-IVEKFNAL-DRVIFSSFNHDALRELR------------- 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 228 pwslSHTGDGKPRYSVFWKQSVFVVLDILLD---WSMHnvLWylcgISAFLMQKDFVSPDYLKKWSAKGIQVVSWTVNtf 304
Cdd:cd08568 136 ----KLDPDAKVGLLIGEEEEGFSIPELHEKlklYSLH--VP----IDAIGYIGFEKFVELLRLLRKLGLKIVLWTVN-- 203


                ....*
gi 47575864 305 DEKNY 309
Cdd:cd08568 204 DPELV 208
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 68-321 5.81e-21

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: 89.59  E-value: 5.81e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDL-TFEQVRKLnpaanhRLR 146
Cdd:cd08570   2 IGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDsTWDELSHL------RTI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 147 NEfPDERIPTLREAVTECLCHNLT---IFFDVKghADMASAALKNIYMEFPQLYNNSmvcSFLPEviykmrqtdqKVITA 223
Cdd:cd08570  76 EE-PHQPMPTLKDVLEWLVEHELPdvkLMLDIK--RDNDPEILFKLIAEMLAVKPDL---DFWRE----------RIILG 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 224 LTHRPWsLSHTGDGKPRYSVFWkqsvfvvldILLDWS-MHNVLWYLCGISAFLM-QKDFVSP---DYLKKWSAKGIQVVS 298
Cdd:cd08570 140 LWHLDF-LKYGKEVLPGFPVFH---------IGFSLDyARHFLNYSEKLVGISMhFVSLWGPfgqAFLPELKKNGKKVFV 209

                       250       260
                ....*....|....*....|...
gi 47575864 299 WTVNTFDEKNYYESHLGSSYITD 321
Cdd:cd08570 210 WTVNTEEDMRYAIRLGVDGVITD 232
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 68-159 1.93e-19

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: 86.94  E-value: 1.93e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTD------------GSGRLCDLTFEQVR 135
Cdd:cd08559   4 IAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNvaehfpfrgrkdTGYFVIDFTLAELK 83

                        90       100       110
                ....*....|....*....|....*....|
gi 47575864 136 KLN--PAANHRLRNEFPDE----RIPTLRE 159
Cdd:cd08559  84 TLRagSWFNQRYPERAPSYyggfKIPTLEE 113
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 68-303 2.89e-16

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: 77.35  E-value: 2.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTV--DRTTDGSGR--------LCDLTFEQVRKL 137
Cdd:cd08567   4 QGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLnpDITRDPDGAwlpyegpaLYELTLAEIKQL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 138 ---------NPAANHRLRNEFPDERIPTLREavteclchnltiFFD-VKGHADMA--------SAALKNIYMEFPQLYnn 199
Cdd:cd08567  84 dvgekrpgsDYAKLFPEQIPVPGTRIPTLEE------------VFAlVEKYGNQKvrfnietkSDPDRDILHPPPEEF-- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 200 smvCSFLPEVIYKMRQTDQKVITALTHRPWSLSHTGDGKPRYS-VFWKQSVFVVLDILLDWSMHnvLWylcgiSAFLmqk 278
Cdd:cd08567 150 ---VDAVLAVIRKAGLEDRVVLQSFDWRTLQEVRRLAPDIPTVaLTEETTLGNLPRAAKKLGAD--IW-----SPYF--- 216

                       250       260
                ....*....|....*....|....*
gi 47575864 279 DFVSPDYLKKWSAKGIQVVSWTVNT 303
Cdd:cd08567 217 TLVTKELVDEAHALGLKVVPWTVND 241
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 68-176 4.36e-16

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: 76.58  E-value: 4.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGS----GRLC----DLTFEQVRKLN- 138
Cdd:cd08574   5 IGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVAdvfpERAHerasMFTWTDLQQLNa 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 47575864 139 --------P-----AANHRLRNEFPDERIPTLREAVTECLCHNLTIFFDVK 176
Cdd:cd08574  85 gqwflkddPfwtasSLSESDREEAGNQSIPSLAELLRLAKKHNKSVIFDLR 135
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 68-176 4.56e-15

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: 74.57  E-value: 4.56e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGS----GRLC----DLTFEQVRKLNP 139
Cdd:cd08609  30 VGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLRTTNVKdvfpGRDAagsnNFTWTELKTLNA 109

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 47575864 140 AA--------------NHRLRNEFPDERIPTLREAVTECLCHNLTIFFDVK 176
Cdd:cd08609 110 GSwflerrpfwtlsslSEEDRREADNQTVPSLSELLDLAKKHNVSIMFDLR 160
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 68-163 7.05e-15

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: 73.85  E-value: 7.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRG--------GSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTV---DRTTDGSGRLC-------DL 129
Cdd:cd08572   3 IGHRGlgknyasgSLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTIsvsEKSKTGSDEGElievpihDL 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 47575864 130 TFEQVRKLNPA--------ANHRLRNEFPDE--------RIPTLREAVTE 163
Cdd:cd08572  83 TLEQLKELGLQhisalkrkALTRKAKGPKPNpwgmdehdPFPTLQEVLEQ 132
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 60-159 8.31e-15

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: 73.79  E-value: 8.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  60 KPRDRVSAIAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFE------Q 133
Cdd:cd08612  22 KSPFPCRHISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYAdlppylE 101

                        90       100
                ....*....|....*....|....*.
gi 47575864 134 VRKLNPAANHRLRNEFPDERIPTLRE 159
Cdd:cd08612 102 KLEVTFSPGDYCVPKGSDRRIPLLEE 127
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 68-163 1.42e-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: 70.02  E-value: 1.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRG-------GSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTV---DRTTDGSGRLC-------DLT 130
Cdd:cd08607   3 VGHRGagnsytaASAVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLrvsLKSKGDSDRDDllevpvkDLT 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 47575864 131 FEQVRKLNPAanHRLR------------NEFPDERI-PTLREAVTE 163
Cdd:cd08607  83 YEQLKLLKLF--HISAlkvkeyksveedEDPPEHQPfPTLSDVLES 126
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 68-214 3.68e-12

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: 65.90  E-value: 3.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRG-----GSHDAP------ENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTV---DRTTDGSGRLCDLTFEQ 133
Cdd:cd08605   3 IGHRGlgmnrASHQPSvgpgirENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIvveRGGEVESSRIRDLTLAE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 134 VRKLNPAA--------NHRLRNEFP---------DERIPTLREAVTEC---LCHNLTIFFDVKGHADMAS--AALKNIYM 191
Cdd:cd08605  83 LKALGPQAestktstvALYRKAKDPepepwimdvEDSIPTLEEVFSEVppsLGFNIELKFGDDNKTEAEElvRELRAILA 162

                       170       180
                ....*....|....*....|....*
gi 47575864 192 EFPQLYNNSMV--CSFLPEVIYKMR 214
Cdd:cd08605 163 VCKQHAPGRRImfSSFDPDAAVLLR 187
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 68-123 8.05e-12

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: 62.84  E-value: 8.05e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGS 123
Cdd:cd08555   2 LSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGI 57
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 68-138 8.33e-12

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: 65.25  E-value: 8.33e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLN 138
Cdd:cd08608   5 IGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYEDASMFN 75
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 68-159 1.68e-11

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: 63.86  E-value: 1.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRL--------------------- 126
Cdd:cd08602   4 IAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADHPefadrkttktvdgvnvtgwft 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 47575864 127 CDLTFEQVRKLnpaanhRLRNEFPDER--------IPTLRE 159
Cdd:cd08602  84 EDFTLAELKTL------RARQRLPYRDqsydgqfpIPTFEE 118
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 51-121 1.71e-11

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE6 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE6 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 4 (GDPD4)) and their metazoan homologs. Mammalian GDE6 is a transmembrane protein predominantly expressed in the spermatocytes of testis. Although the specific physiological function of mammalian GDE6 has not been elucidated, its different pattern of tissue distribution suggests it might play a critical role in the completion of meiosis during male germ cell differentiation.


Pssm-ID: 176552 [Multi-domain]  Cd Length: 316  Bit Score: 64.12  E-value: 1.71e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47575864  51 PSRRALQVLKPRDRVsaIAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTD 121
Cdd:cd08610  11 PCIREKETLGPKPTI--IGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTN 79
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 74-138 3.93e-11

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: 62.76  E-value: 3.93e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47575864  74 SHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGSGRLCDLTFEQVRKLN 138
Cdd:cd08613  55 THDYLENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELKTLD 119
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 68-159 5.63e-11

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: 62.41  E-value: 5.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTT------------DGSGRLCDLTFEQVR 135
Cdd:cd08600   4 IAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTnvaekfpdrkrkDGRYYVIDFTLDELK 83

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 47575864 136 KLNPAANHRLR---------NEFP----DERIPTLRE 159
Cdd:cd08600  84 SLSVTERFDIEngkkvqvypNRFPlwksDFKIHTLEE 120
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 64-312 7.04e-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: 61.72  E-value: 7.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  64 RVSAIAHRG-GSHD-APENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMH---DNTVDRTT-----DGSGRLCDLTFEQ 133
Cdd:cd08564   3 RPIIVGHRGaGCSTlYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteDDTNPDTSiqlddSGFKNINDLSLDE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 134 VRKLN----PAANHRLRNEFPDERIPTLREAVTECLcHNLTIFFDVKGHADMASAALKNIYMEFPQLYnNSMVCSFL--- 206
Cdd:cd08564  83 ITRLHfkqlFDEKPCGADEIKGEKIPTLEDVLVTFK-DKLKYNIELKGREVGLGERVLNLVEKYGMIL-QVHFSSFLhyd 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864 207 -PEVIYKMRQTDQKVITALthrpwslshtgdgkprysVFWKQSVFVVLDILLDWSMHNVLWylCGISaflmqKDFVSPDY 285
Cdd:cd08564 161 rLDLLKALRPNKLNVPIAL------------------LFNEVKSPSPLDFLEQAKYYNATW--VNFS-----YDFWTEEF 215

                       250       260       270
                ....*....|....*....|....*....|..
gi 47575864 286 LKKWSAKGIQVVSWTVNTFDE-----KNYYES 312
Cdd:cd08564 216 VKKAHENGLKVMTYFDEPVNDneedyKVYLEL 247
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 68-159 2.62e-09

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 57.76  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864   68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRTTDGS----------GR--LCDLTFEQVR 135
Cdd:PRK11143  30 IAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAerfpdrarkdGRyyAIDFTLDEIK 109

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 47575864  136 KLNPAANHRLR---------NEFP----DERIPTLRE 159
Cdd:PRK11143 110 SLKFTEGFDIEngkkvqvypGRFPmgksDFRVHTFEE 146
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 65-133 3.44e-07

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


Pssm-ID: 176548 [Multi-domain]  Cd Length: 286  Bit Score: 50.91  E-value: 3.44e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47575864  65 VSAIAHRG-GSHDAP-------ENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHDNTVDRT-TDGSgrLCDLTFEQ 133
Cdd:cd08606   2 VQVIGHRGlGKNTAErkslqlgENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETgTDVP--IHDLTLEQ 77
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 68-140 5.25e-06

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


Pssm-ID: 176546  Cd Length: 300  Bit Score: 47.33  E-value: 5.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHD-NTVDRTTDGSGRLC------------------D 128
Cdd:cd08604   4 ISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSiNLINSTTVATSKFSnrattvpeigstsgiftfD 83

                        90
                ....*....|..
gi 47575864 129 LTFEQVRKLNPA 140
Cdd:cd08604  84 LTWSEIQTLKPA 95
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 68-162 6.28e-06

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


Pssm-ID: 176513  Cd Length: 302  Bit Score: 47.28  E-value: 6.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47575864  68 IAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPV------LMHDNTVDRTT------------DGSGRLC-D 128
Cdd:cd08571   4 IARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPIclpsinLDNSTTIASVFpkrkktyvvegqSTSGIFSfD 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 47575864 129 LTFEQVRKLNPA----ANHRLRNEFPD--ERIPTLREAVT 162
Cdd:cd08571  84 LTWAEIQTLKPIisnpFSVLFRNPRNDnaGKILTLEDFLT 123
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 67-121 3.32e-05

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: 45.10  E-value: 3.32e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 47575864  67 AIAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHD-NTVDRTTD 121
Cdd:cd08560  19 SIGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSqCDLHTTTN 74
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 68-113 2.83e-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: 41.52  E-value: 2.83e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 47575864  68 IAHRGGSHDAPE--NTLAAIRQAAKNGATGVELDIEFTSDGVPVLMHD 113
Cdd:cd08583   2 IAHAMGGIDGKTytNSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHS 49
GDPD_like_SMaseD_PLD cd08576
Glycerophosphodiester phosphodiesterase-like domain of spider venom sphingomyelinases D, ...
 67-127 3.21e-04

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


Pssm-ID: 176518 [Multi-domain]  Cd Length: 265  Bit Score: 41.54  E-value: 3.21e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47575864  67 AIAHRggshdapENTLAAIRQAAKNGATGVELDIEFTSDGVPVLM-HDNTVDrttdgSGRLC 127
Cdd:cd08576   2 AIAHM-------VNDLEGVDDALDHGANAIEIDVTFWSNGTGWWAdHDVPCD-----CFRGC 51
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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