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Conserved domains on  [gi|568918607|ref|XP_006500339|]
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glycerophosphocholine phosphodiesterase GPCPD1 isoform X1 [Mus musculus]

Protein Classification

glycerophosphodiester phosphodiesterase family protein( domain architecture ID 10171259)

glycerophosphodiester phosphodiesterase (GDPD) family protein similar to GDPD domain region of GPCPD1/GDE5 that may be involved in the negative regulation of skeletal muscle differentiation, independently of its glycerophosphocholine phosphodiesterase activity

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_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 138-437 0e+00

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: 512.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 138 LDVGHRGAGNSTTTAKlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKKfvhtqkyEADPVE 217
Cdd:cd08607    1 LDVGHRGAGNSYTAAS-AVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKG-------DSDRDD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 218 LFEIPVKELTFDQLQLLKLSHVTALKTKDRKQSlyEEENFFSENQPFPSLKMVLESLPENVGFNIEIKWICQHRDGVWDG 297
Cdd:cd08607   73 LLEVPVKDLTYEQLKLLKLFHISALKVKEYKSV--EEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKDGSWES 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 298 NLSTYFDMNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIYPELMDLRSRTTPIAMSFAQ 377
Cdd:cd08607  151 ELFTYFDRNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPEFMDLRTRTFEIAVNFAQ 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 378 FENILGINAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNDPENRRKLKEFGVNGLIYDRI 437
Cdd:cd08607  231 AEELLGVNLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDRI 290
 
Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 138-437 0e+00

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: 512.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 138 LDVGHRGAGNSTTTAKlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKKfvhtqkyEADPVE 217
Cdd:cd08607    1 LDVGHRGAGNSYTAAS-AVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKG-------DSDRDD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 218 LFEIPVKELTFDQLQLLKLSHVTALKTKDRKQSlyEEENFFSENQPFPSLKMVLESLPENVGFNIEIKWICQHRDGVWDG 297
Cdd:cd08607   73 LLEVPVKDLTYEQLKLLKLFHISALKVKEYKSV--EEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKDGSWES 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 298 NLSTYFDMNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIYPELMDLRSRTTPIAMSFAQ 377
Cdd:cd08607  151 ELFTYFDRNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPEFMDLRTRTFEIAVNFAQ 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 378 FENILGINAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNDPENRRKLKEFGVNGLIYDRI 437
Cdd:cd08607  231 AEELLGVNLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDRI 290
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 142-437 1.39e-47

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: 164.88  E-value: 1.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607  142 HRGAGNSTTtaklakvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKKFvhtqkyeadpvelfei 221
Cdd:pfam03009   1 HRGASGSYP--------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGY---------------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607  222 pVKELTFDQLQLLKLSHVtalktkdRKQSLYEEENffsenqPFPSLKMVLEsLPENVGFNIEIKWICQHRDGVWDGNLSt 301
Cdd:pfam03009  57 -VRDLTLEELKRLDIGAG-------NSGPLSGERV------PFPTLEEVLE-FDWDVGFNIEIKIKPYVEAIAPEEGLI- 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607  302 YFDMNVFLDIILKtvlENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTqgkSDIYPELMDLRSRTTPiamsFAQFENI 381
Cdd:pfam03009 121 VKDLLLSVDEILA---KKADPRRVIFSSFNPDELKRLRELAPKLPLVFLS---SGRAYAEADLLERAAA----FAGAPAL 190

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568918607  382 LGINAHTEDllRNPSYVQEAKAKGLVIFCWGDdtNDPENRRKLKEFGVNGLIYDRI 437
Cdd:pfam03009 191 LGEVALVDE--ALPDLVKRAHARGLVVHVWTV--NNEDEMKRLLELGVDGVITDRP 242
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
133-437 1.37e-39

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 143.47  E-value: 1.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 133 KPRIpldVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTccltMKRKKFVHTqkye 212
Cdd:COG0584    2 RPLI---IAHRGAS--------GLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPT----LDRTTNGTG---- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 213 adpvelfeiPVKELTFDQLQLLKLSHVTALKtkdrkqslyeeenffseNQPFPSLKMVLESLPENVGFNIEIKwicqhrd 292
Cdd:COG0584   63 ---------RVADLTLAELRQLDAGSGPDFA-----------------GERIPTLEEVLELVPGDVGLNIEIK------- 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 293 gvwdgnlSTYFDMNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTqgkSDIYPELMDLRSRTtpia 372
Cdd:COG0584  110 -------SPPAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLV---EELPADPLELARAL---- 175

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568918607 373 msfaqfeNILGINAHTEDLlrNPSYVQEAKAKGLVIFCWgddT-NDPENRRKLKEFGVNGLIYDRI 437
Cdd:COG0584  176 -------GADGVGPDYDLL--TPELVAAAHAAGLKVHVW---TvNDPEEMRRLLDLGVDGIITDRP 229
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 134-195 1.97e-10

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 61.11  E-value: 1.97e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918607 134 PRIpldVGHRGAGnstttaKLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLT 195
Cdd:PRK09454   8 PRI---VAHRGGG------KLAP--ENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDT 58
 
Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 138-437 0e+00

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: 512.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 138 LDVGHRGAGNSTTTAKlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKKfvhtqkyEADPVE 217
Cdd:cd08607    1 LDVGHRGAGNSYTAAS-AVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKG-------DSDRDD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 218 LFEIPVKELTFDQLQLLKLSHVTALKTKDRKQSlyEEENFFSENQPFPSLKMVLESLPENVGFNIEIKWICQHRDGVWDG 297
Cdd:cd08607   73 LLEVPVKDLTYEQLKLLKLFHISALKVKEYKSV--EEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKDGSWES 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 298 NLSTYFDMNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIYPELMDLRSRTTPIAMSFAQ 377
Cdd:cd08607  151 ELFTYFDRNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPEFMDLRTRTFEIAVNFAQ 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 378 FENILGINAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNDPENRRKLKEFGVNGLIYDRI 437
Cdd:cd08607  231 AEELLGVNLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDRI 290
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 138-437 9.61e-150

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: 429.39  E-value: 9.61e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 138 LDVGHRGAGNSTTTAKLAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKKFvhtqkyeADPVE 217
Cdd:cd08572    1 LVIGHRGLGKNYASGSLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSKTG-------SDEGE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 218 LFEIPVKELTFDQLQLLKLSHVTALKTKDRKQSL---YEEENFFSENQPFPSLKMVLESLPENVGFNIEIKWICQHRDGv 294
Cdd:cd08572   74 LIEVPIHDLTLEQLKELGLQHISALKRKALTRKAkgpKPNPWGMDEHDPFPTLQEVLEQVPKDLGFNIEIKYPQLLEDG- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 295 wDGNLSTYFDMNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIyPELMDLRSRTTPIAMS 374
Cdd:cd08572  153 -EGELTPYFERNAFVDTILAVVFEHAGGRRIIFSSFDPDICIMLRLKQNKYPVLFLTNGGTNE-VEHMDPRRRSLQAAVN 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568918607 375 FAQFENILGINAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNDPENRRKLKEFGVNGLIYDRI 437
Cdd:cd08572  231 FALAEGLLGVVLHAEDLLKNPSLISLVKALGLVLFTYGDDNNDPENVKKQKELGVDGVIYDRV 293
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 140-437 1.75e-59

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: 197.67  E-value: 1.75e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 140 VGHRGAGNSTTTAKLAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMkrkkfvhtqkyeadpvelF 219
Cdd:cd08606    5 IGHRGLGKNTAERKSLQLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETG------------------T 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 220 EIPVKELTFDQ-LQLLKLSHVTALKTKDRKQSLYEEenffSENQPFPSLKMVLESLPENVGFNIEIKWICQHrDGVWDGN 298
Cdd:cd08606   67 DVPIHDLTLEQfLHLSRMKYTVDFKKKGFKGNSRGH----SIQAPFTTLEELLKKLPKSVGFNIELKYPMLH-EAEEEEV 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 299 LSTYFDMNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSdiyPELMDLRSRTTPIAMSFAQF 378
Cdd:cd08606  142 APVAIELNAFVDTVLEKVFDYGAGRNIIFSSFTPDICILLSLKQPGYPVLFLTEAGK---APDMDVRAASLQEAIRFAKQ 218

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568918607 379 ENILGINAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNDPENRRKLKEFGVNGLIYDRI 437
Cdd:cd08606  219 WNLLGLVSAAEPLVMCPRLIQVVKRSGLVCVSYGVLNNDPENAKTQVKAGVDAVIVDSV 277
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 142-437 1.39e-47

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: 164.88  E-value: 1.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607  142 HRGAGNSTTtaklakvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKKFvhtqkyeadpvelfei 221
Cdd:pfam03009   1 HRGASGSYP--------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGY---------------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607  222 pVKELTFDQLQLLKLSHVtalktkdRKQSLYEEENffsenqPFPSLKMVLEsLPENVGFNIEIKWICQHRDGVWDGNLSt 301
Cdd:pfam03009  57 -VRDLTLEELKRLDIGAG-------NSGPLSGERV------PFPTLEEVLE-FDWDVGFNIEIKIKPYVEAIAPEEGLI- 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607  302 YFDMNVFLDIILKtvlENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTqgkSDIYPELMDLRSRTTPiamsFAQFENI 381
Cdd:pfam03009 121 VKDLLLSVDEILA---KKADPRRVIFSSFNPDELKRLRELAPKLPLVFLS---SGRAYAEADLLERAAA----FAGAPAL 190

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568918607  382 LGINAHTEDllRNPSYVQEAKAKGLVIFCWGDdtNDPENRRKLKEFGVNGLIYDRI 437
Cdd:pfam03009 191 LGEVALVDE--ALPDLVKRAHARGLVVHVWTV--NNEDEMKRLLELGVDGVITDRP 242
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 140-437 3.18e-47

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: 165.28  E-value: 3.18e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 140 VGHRGAGNSTTTAKL---AKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccltmkrkKFVHTQkyEADPV 216
Cdd:cd08605    3 IGHRGLGMNRASHQPsvgPGIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHD----------DFIVVE--RGGEV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 217 ELFEIpvKELTFDQLQLLKLShvtALKTKDRKQSLYEeenFFSENQP----------FPSLKMVLESLPENVGFNIEIKW 286
Cdd:cd08605   71 ESSRI--RDLTLAELKALGPQ---AESTKTSTVALYR---KAKDPEPepwimdvedsIPTLEEVFSEVPPSLGFNIELKF 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 287 icqhrdgvWDGNLSTYFDMNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIYpelMDLRS 366
Cdd:cd08605  143 --------GDDNKTEAEELVRELRAILAVCKQHAPGRRIMFSSFDPDAAVLLRALQSLYPVMFLTDCGPYTH---NDPRR 211

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568918607 367 RTTPIAMSFAQFENILGINAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNDPENRRKLKEFGVNGLIYDRI 437
Cdd:cd08605  212 NSIEAAIQVALEGGLQGIVSEVKVLLRNPTAVSLVKASGLELGTYGKLNNDAEAVERQADLGVDGVIVDHV 282
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
133-437 1.37e-39

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 143.47  E-value: 1.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 133 KPRIpldVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTccltMKRKKFVHTqkye 212
Cdd:COG0584    2 RPLI---IAHRGAS--------GLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPT----LDRTTNGTG---- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 213 adpvelfeiPVKELTFDQLQLLKLSHVTALKtkdrkqslyeeenffseNQPFPSLKMVLESLPENVGFNIEIKwicqhrd 292
Cdd:COG0584   63 ---------RVADLTLAELRQLDAGSGPDFA-----------------GERIPTLEEVLELVPGDVGLNIEIK------- 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 293 gvwdgnlSTYFDMNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTqgkSDIYPELMDLRSRTtpia 372
Cdd:COG0584  110 -------SPPAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLV---EELPADPLELARAL---- 175

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568918607 373 msfaqfeNILGINAHTEDLlrNPSYVQEAKAKGLVIFCWgddT-NDPENRRKLKEFGVNGLIYDRI 437
Cdd:COG0584  176 -------GADGVGPDYDLL--TPELVAAAHAAGLKVHVW---TvNDPEEMRRLLDLGVDGIITDRP 229
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 140-436 3.08e-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: 132.77  E-value: 3.08e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 140 VGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLtccltmkrkkfvhtqkyeadpvelf 219
Cdd:cd08556    2 IAHRGAS--------GEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHDI------------------------- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 220 eipvkeltfdqlqllklshvtalktkdrkqslyeeenffsenqpfPSLKMVLESLPENVGFNIEIKWICQHRDgvwdgnl 299
Cdd:cd08556   49 ---------------------------------------------PTLEEVLELVKGGVGLNIELKEPTRYPG------- 76

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 300 styfDMNVFLDIILKTVLENsgkrRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIYPELMDLRSRttpiamsfaqfe 379
Cdd:cd08556   77 ----LEAKVAELLREYGLEE----RVVVSSFDHEALRALKELDPEVPTGLLVDKPPLDPLLAELARAL------------ 136

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568918607 380 NILGINAHteDLLRNPSYVQEAKAKGLVIFCWGDdtNDPENRRKLKEFGVNGLIYDR 436
Cdd:cd08556  137 GADAVNPH--YKLLTPELVRAAHAAGLKVYVWTV--NDPEDARRLLALGVDGIITDD 189
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 140-437 4.24e-24

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: 100.37  E-value: 4.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 140 VGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTC--CLTMKRkkfvhtqkyeadpve 217
Cdd:cd08562    2 IAHRGAS--------SLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLdrTTNGSG--------------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 218 lfeiPVKELTFDQLQLLKLSHvtalktkdrkqslyeeenFFSE---NQPFPSLKMVLESLPE-NVGFNIEIKwICQHRDg 293
Cdd:cd08562   59 ----AVTELTWAELAQLDAGS------------------WFSPefaGEPIPTLADVLELARElGLGLNLEIK-PDPGDE- 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 294 vwdgnlstyFDMNVFLDIILKTVleNSGKRRIVFSSFDADICTMVRQKQNKYPILFLTqgksdiypelmdlrsrTTPIAM 373
Cdd:cd08562  115 ---------ALTARVVAAALREL--WPHASKLLLSSFSLEALRAARRAAPELPLGLLF----------------DTLPAD 167

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568918607 374 SFAQFENILGINAHTEDLLRNPSYVQEAKAKGLVIFCWgddT-NDPENRRKLKEFGVNGLIYDRI 437
Cdd:cd08562  168 WLELLAALGAVSIHLNYRGLTEEQVKALKDAGYKLLVY---TvNDPARAAELLEWGVDAIFTDRP 229
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 141-436 6.20e-22

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: 95.07  E-value: 6.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 141 GHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKKFVHTQKYEadpvelfE 220
Cdd:cd08567    5 GHRGAR--------GLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDITRDPDGAWLPYE-------G 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 221 IPVKELTFDQLQLLKlshVTALKTKDRKQSLYEEENFFsENQPFPSLKMVLESLPENVG----FNIEIKWICQHRDGVWD 296
Cdd:cd08567   70 PALYELTLAEIKQLD---VGEKRPGSDYAKLFPEQIPV-PGTRIPTLEEVFALVEKYGNqkvrFNIETKSDPDRDILHPP 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 297 GnlstyfdmNVFLDIILKtVLENSGK-RRIVFSSFDADICTMVRQKQNKYPILFLTQGKsdiypelmdlRSRTTPIAMSF 375
Cdd:cd08567  146 P--------EEFVDAVLA-VIRKAGLeDRVVLQSFDWRTLQEVRRLAPDIPTVALTEET----------TLGNLPRAAKK 206

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568918607 376 AQFEnilgINAHTEDLLrNPSYVQEAKAKGLVIFCWGddTNDPENRRKLKEFGVNGLIYDR 436
Cdd:cd08567  207 LGAD----IWSPYFTLV-TKELVDEAHALGLKVVPWT--VNDPEDMARLIDLGVDGIITDY 260
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 141-435 7.11e-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: 7.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 141 GHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKKFVHtqkyeadpvelfe 220
Cdd:cd08568    4 GHRGYR--------AKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHD----ENLKRVGGVD------------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 221 IPVKELTFDQLQLLKLshvtalktkdrkqslyeeenffsENQPFPSLKMVLESLPENVGFNIEIKWIcqhrDGVwdgnls 300
Cdd:cd08568   59 LKVKELTYKELKKLHP-----------------------GGELIPTLEEVFRALPNDAIINVEIKDI----DAV------ 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 301 tyfdmnvflDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIY-----PELMDLRSRTTPI-AMS 374
Cdd:cd08568  106 ---------EPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPDAKVGLLIGEEEEGFsipelHEKLKLYSLHVPIdAIG 176

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568918607 375 FAQFENILginahtedllrnpSYVQEAKAKGLVIFCWgdDTNDPENRRKLKEFgVNGLIYD 435
Cdd:cd08568  177 YIGFEKFV-------------ELLRLLRKLGLKIVLW--TVNDPELVPKLKGL-VDGVITD 221
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 140-436 7.22e-21

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: 91.22  E-value: 7.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 140 VGHRGAgnSTTtaklakVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKKFVHTqkyeadpvelf 219
Cdd:cd08582    2 IAHRGA--SAE------APENTLAAFELAWEQGADGIETDVRLTKDGELVCVHD----PTLKRTSGGDG----------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 220 eiPVKELTFDQLQLLKLShvtalktkDRKQSLYEEENffsenqpFPSLKMVLESLPE-NVGFNIEIKWicqhrdgvwdgn 298
Cdd:cd08582   59 --AVSDLTLAELRKLDIG--------SWKGESYKGEK-------VPTLEEYLAIVPKyGKKLFIEIKH------------ 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 299 lSTYFDMNVflDIILKTVLENSGKR-RIVFSSFDADICTMVRQKQNKYPILFLTQGKSDiypelmdlRSRTTPIAMSFaq 377
Cdd:cd08582  110 -PRRGPEAE--EELLKLLKESGLLPeQIVIISFDAEALKRVRELAPTLETLWLRNYKSP--------KEDPRPLAKSG-- 176

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 378 feNILGINAHTEDLLrNPSYVQEAKAKGLVIFCWgddT-NDPENRRKLKEFGVNGLIYDR 436
Cdd:cd08582  177 --GAAGLDLSYEKKL-NPAFIKALRDAGLKLNVW---TvDDAEDAKRLIELGVDSITTNR 230
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 141-435 2.21e-19

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: 86.84  E-value: 2.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 141 GHRGAgnstttakLAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKKFvhtqkyeadpvelfe 220
Cdd:cd08563    5 AHRGY--------SGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGY--------------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 221 ipVKELTFDQLQLLKLShvtalktkdrkqslyeeeNFFSENQPF---PSLKMVLESLPE-NVGFNIEIKwicqhrdgvwd 296
Cdd:cd08563   62 --VKDLTLEELKKLDAG------------------SWFDEKFTGekiPTLEEVLDLLKDkDLLLNIEIK----------- 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 297 gnlSTYFDMNVFLDIILKTVLENSGKRRIVFSSFDADicTMVRQKQ--NKYPILFLTQGKSDIYPElmdlrsrttpiams 374
Cdd:cd08563  111 ---TDVIHYPGIEKKVLELVKEYNLEDRVIFSSFNHE--SLKRLKKldPKIKLALLYETGLQDPKD-------------- 171

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918607 375 FAQFENILGINAHTEDLlrNPSYVQEAKAKGLVIFCWgddT-NDPENRRKLKEFGVNGLIYD 435
Cdd:cd08563  172 YAKKIGADSLHPDFKLL--TEEVVEELKKRGIPVRLW---TvNEEEDMKRLKDLGVDGIITN 228
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 159-437 2.79e-19

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: 87.66  E-value: 2.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 159 ENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLT-CCLTMKrkkfvhtqkyeadpvelfEIPVKELTFDQLQLLKLS 237
Cdd:cd08575   15 ENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDlDRLTGG------------------SGLVSDLTYAELPPLDAG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 238 -HVTAlkTKDRKQSLYEeenffSENQPFPSLKMVLESLPeNVGFNIEIKwicqhrdgvwdgnlstYFDMNVFLDIILKTV 316
Cdd:cd08575   77 yGYTF--DGGKTGYPRG-----GGDGRIPTLEEVFKAFP-DTPINIDIK----------------SPDAEELIAAVLDLL 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 317 LENSGKRRIVFSSFDADICtmvrQKQNKYPilfltqgksdiyPELMDLRSRTT-----------------PIAMSFAQF- 378
Cdd:cd08575  133 EKYKREDRTVWGSTNPEYL----RALHPEN------------PNLFESFSMTRclllylalgytgllpfvPIKESFFEIp 196

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568918607 379 -------ENILGINAHTED-LLRNPSYVQEAKAKGLVIFCWGddTNDPENRRKLKEFGVNGLIYDRI 437
Cdd:cd08575  197 rpvivleTFTLGEGASIVAaLLWWPNLFDHLRKRGIQVYLWV--LNDEEDFEEAFDLGADGVMTDSP 261
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 141-436 4.84e-17

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: 80.76  E-value: 4.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 141 GHRGAgnstttAKLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKKfvhtqkyeadpvelfe 220
Cdd:cd08561    3 AHRGG------AGLAP--ENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTG---------------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 221 iPVKELTFDQLQLLKLSHvtalKTKDRKQSLYEEENffsENQPFPSLKMVLESLPeNVGFNIEIKwicQHRDGVWDgnls 300
Cdd:cd08561   59 -PVADLTLAELRRLDAGY----HFTDDGGRTYPYRG---QGIRIPTLEELFEAFP-DVRLNIEIK---DDGPAAAA---- 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 301 tyfdmnVFLDIILKTVLENsgkrRIVFSSFDADIctmVRQKQNKYPILFLTQGKSDIYPELMDLRSRTTPIAMSFAQF-- 378
Cdd:cd08561  123 ------ALADLIERYGAQD----RVLVASFSDRV---LRRFRRLCPRVATSAGEGEVAAFVLASRLGLGSLYSPPYDAlq 189

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 379 --ENILGINahtedlLRNPSYVQEAKAKGLVIFCWGDdtNDPENRRKLKEFGVNGLIYDR 436
Cdd:cd08561  190 ipVRYGGVP------LVTPRFVRAAHAAGLEVHVWTV--NDPAEMRRLLDLGVDGIITDR 241
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 140-343 5.74e-17

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


Pssm-ID: 176523 [Multi-domain]  Cd Length: 229  Bit Score: 80.07  E-value: 5.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 140 VGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKKFVhtqkyeadpvelf 219
Cdd:cd08581    2 VAHRGYP--------ARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHD----DTLLRLTGV------------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 220 EIPVKELTFDQLQLLklshvtalktkdrkqSLYEEENFFS--ENQPFPSLKMV---LESLPEnVGFNIEIKWICQHRDGV 294
Cdd:cd08581   57 EGLLHELEDAELDSL---------------RVAEPARFGSrfAGEPLPSLAAVvqwLAQHPQ-VTLFVEIKTESLDRFGL 120

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568918607 295 wdgnlstyfdmNVFLDIILKtVLENSGKRRiVFSSFDADICTMVRQKQN 343
Cdd:cd08581  121 -----------ERVVDKVLR-ALPAVAAQR-VLISFDYDLLALAKQQGG 156
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 137-441 4.46e-16

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: 78.85  E-value: 4.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 137 PLDVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKKFVHtQKYEADPV 216
Cdd:cd08559    1 PLVIAHRGAS--------GYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHD----PTLDRTTNVA-EHFPFRGR 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 217 ELFEIPVKELTFDQLQLLKLSHVTALKTKDRKQSLYeeenffsENQPFPSLKMVLE-------SLPENVGFNIEIKwicq 289
Cdd:cd08559   68 KDTGYFVIDFTLAELKTLRAGSWFNQRYPERAPSYY-------GGFKIPTLEEVIElaqglnkSTGRNVGIYPETK---- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 290 hrdgvwdgnLSTYFDMNvFLDI--ILKTVLE----NSGKRRIVFSSFDADICTMVRQKQNKYPILFLT-QGKSDIYPELM 362
Cdd:cd08559  137 ---------HPTFHKQE-GPDIeeKLLEVLKkygyTGKNDPVFIQSFEPESLKRLRNETPDIPLVQLIdYGDWAETDKKY 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 363 DLRSRTTPIAMSF-AQFENILG------INAHTEDLLRNPSYVQEAKAKGLVIFCWgddTNDPENRRKLKEFGVNgliYD 435
Cdd:cd08559  207 TYAWLTTDAGLKEiAKYADGIGpwksliIPEDSNGLLVPTDLVKDAHKAGLLVHPY---TFRNENLFLAPDFKQD---MD 280


                 ....*.
gi 568918607 436 RIYDWM 441
Cdd:cd08559  281 ALYNAA 286
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 140-436 1.09e-15

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: 76.05  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 140 VGHRG-AGNSTttaklakvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKKFVHtqkyeadpvel 218
Cdd:cd08579    2 IAHRGvSSNGV---------ENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVW----------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 219 feipvkELTFDQLQLLKLShvtalktkdrkqslyeeENFFSEnqPFPSLKMVLE-SLPENVGFNIEIKWICQHRDGVwdg 297
Cdd:cd08579   62 ------DLTLEELKKLTIG-----------------ENGHGA--KIPSLDEYLAlAKGLKQKLLIELKPHGHDSPDL--- 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 298 nlstyfdMNVFLDIILKTVLENSgkrrIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIYPElmdlrsrttpiamSFAQ 377
Cdd:cd08579  114 -------VEKFVKLYKQNLIENQ----HQVHSLDYRVIEKVKKLDPKIKTGYILPFNIGNLPK-------------TNVD 169

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568918607 378 FENIlginahtEDLLRNPSYVQEAKAKGLVIFCWgdDTNDPENRRKLKEFGVNGLIYDR 436
Cdd:cd08579  170 FYSI-------EYSTLNKEFIRQAHQNGKKVYVW--TVNDPDDMQRYLAMGVDGIITDY 219
GDPD_NUC-2_fungi cd08578
Putative glycerophosphodiester phosphodiesterase domain of ankyrin repeat protein NUC-2 and ...
 131-434 8.26e-15

Putative glycerophosphodiester phosphodiesterase domain of ankyrin repeat protein NUC-2 and similar proteins; This subfamily corresponds to a putative glycerophosphodiester phosphodiesterase domain (GDPD) present in Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81. Some uncharacterized NUC-2 sequence homologs are also included in this family. NUC-2 plays an important role in the phosphate-regulated signal transduction pathway in Neurospora crassa. It shows high similarity to a cyclin-dependent kinase inhibitory protein PHO81, which is part of the phosphate regulatory cascade in S. cerevisiae. Both NUC-2 and PHO81 have multi-domain architecture, including an SPX N-terminal domain following by several ankyrin repeats and a putative C-terminal GDPD domain with unknown function. Although the putative GDPD domain displays sequence homology to that of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), the residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in members of this family, which suggests the function of putative GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs.


Pssm-ID: 176520  Cd Length: 300  Bit Score: 75.05  E-value: 8.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 131 YWKPRIPLDVGHRGAGNSTTTAklakvqentiaslrnaASHGAAFVEFDVHLSKDFVPVVYHDLTCcltmkrkkfvhtqk 210
Cdd:cd08578    3 YWKSTSGSDTQANKDGNSFVTA----------------SSLSGEYLRVKVCVLKDGTPVVAPEWFV-------------- 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 211 yeadPVELFEIPVKELTFDQLQLLKLSHV-----TALKTKDRKQSLyeeenffseNQPFPSLKMVLESLPENVGFNI--- 282
Cdd:cd08578   53 ----PVGGIKLLVSDLTAEQLESILDYSLddlnsEISDMVDLKRLL---------SSRVVSLETLLELLPPSIQLDIqvl 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 283 -----EIKWIcqhrdgvwDGNLSTYFDMNVFLDIILKTVLENSGK--------RRIVFSSFDADICTMVRQKQNKYPILF 349
Cdd:cd08578  120 fptaaEIASI--------PVKGSPLVDLNKFIDTVLLVVFDHARYlrhtpgstRSIVFSSCNPEVCTILNWKQPNFPVFF 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 350 -----------------LTQGKSDIYPELM---DLRSRTTPIAMSFAQFENILGINAHTEDLLRNPSYVQEAKAKGLVIF 409
Cdd:cd08578  192 amnglvrnndtlsfdtpHHLDSLAVDPQKLneaDPRSRSIKEAVRFAKNNNLLGLILPYSLLNIVPQLVESIKSRGLLLI 271

                        330       340
                 ....*....|....*....|....*
gi 568918607 410 CWGDDTNDPENrrKLKEFGVNGLIY 434
Cdd:cd08578  272 ASGEPESLIEV--AEAGDGINGVVT 294
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 140-436 9.53e-14

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: 70.79  E-value: 9.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 140 VGHRGAGNstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRkkfVHTQKyeadpvelf 219
Cdd:cd08566    3 VAHRGGWG-------AGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHD----DTLDR---TTNGK--------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 220 eIPVKELTFDQLQLLKlshvtaLKTKDRKQSlyeeenffseNQPFPSLKMVLESLPENVGFNIEIKWicqhrdgvwdgnl 299
Cdd:cd08566   60 -GKVSDLTLAEIRKLR------LKDGDGEVT----------DEKVPTLEEALAWAKGKILLNLDLKD------------- 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 300 styFDMNVFLDIILKTVLENsgkrRIVFSSFDADICTMVRQKQNKYPIlfltqgkSDIYPELMDLRSRTTPIAMsfaqFE 379
Cdd:cd08566  110 ---ADLDEVIALVKKHGALD----QVIFKSYSEEQAKELRALAPEVML-------MPIVRDAEDLDEEEARAID----AL 171

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568918607 380 NILGINAHTEDLLRNPSYVQEAKAKGLVIFC---WGDD--------TNDPENRRKLKEFGVNGLIYDR 436
Cdd:cd08566  172 NLLAFEITFDDLDLPPLFDELLRALGIRVWVntlGDDDtagldralSDPREVWGELVDAGVDVIQTDR 239
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 136-437 2.01e-12

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: 67.50  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 136 IPLDVGHRGAGNSTTTAklakvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYH---DLTCCLTMKRKKFVHTQKye 212
Cdd:cd08564    3 RPIIVGHRGAGCSTLYP------ENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteDDTNPDTSIQLDDSGFKN-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 213 adpvelfeipVKELTFDQLQLLKLSHVTALKTKDRKQSLYEEenffsenqpFPSLKMVLESLPENVGFNIEIKwicqhrd 292
Cdd:cd08564   75 ----------INDLSLDEITRLHFKQLFDEKPCGADEIKGEK---------IPTLEDVLVTFKDKLKYNIELK------- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 293 gvwdGNLStyfDMNVFldiILKTVLENSGKRRIVFSSFD----ADICTMVRQKQNKYPILFLtqgksdiypeLMDLRSRT 368
Cdd:cd08564  129 ----GREV---GLGER---VLNLVEKYGMILQVHFSSFLhydrLDLLKALRPNKLNVPIALL----------FNEVKSPS 188

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568918607 369 TPIAMSFAQFENILGinAHTEDLLRNPSYVQEAKAKGLVIFCW--GDDTNDPENRRKLKEFGVNGLIYDRI 437
Cdd:cd08564  189 PLDFLEQAKYYNATW--VNFSYDFWTEEFVKKAHENGLKVMTYfdEPVNDNEEDYKVYLELGVDCICPNDP 257
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 140-193 7.39e-11

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: 62.66  E-value: 7.39e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568918607 140 VGHRGAGNStttaklakVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHD 193
Cdd:cd08573    2 IGHRGAGHD--------APENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHD 47
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 140-436 1.89e-10

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


Pssm-ID: 176508 [Multi-domain]  Cd Length: 235  Bit Score: 60.88  E-value: 1.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 140 VGHRGAGNstttaklaKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKKFVHTqkyeadpvelf 219
Cdd:cd08565    2 AGHRGGRN--------LWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRD----------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 220 eipvkeltfdqlqlLKLSHVTALKTKDrkqslyeeenffSENQPFPSLKMVLESL-PENVGFNIEIKwicqhrdgvWDGN 298
Cdd:cd08565   63 --------------LTLAERKALRLRD------------SFGEKIPTLEEVLALFaPSGLELHVEIK---------TDAD 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 299 LSTYFDmnvFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSdiypELMDLRSRTTPIAmsfaqF 378
Cdd:cd08565  108 GTPYPG---AAALAAATLRRHGLLERSVLTSFDPAVLTEVRKHPGVRTLGSVDEDML----ERLGGELPFLTAT-----A 175

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568918607 379 ENILGINAHTEDLLRNPSYVQEAKaKGLVIFCWGddTNDPENRRKLKEFGVNGLIYDR 436
Cdd:cd08565  176 LKAHIVAVEQSLLAATWELVRAAV-PGLRLGVWT--VNDDSLIRYWLACGVRQLTTDR 230
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 134-195 1.97e-10

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 61.11  E-value: 1.97e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918607 134 PRIpldVGHRGAGnstttaKLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLT 195
Cdd:PRK09454   8 PRI---VAHRGGG------KLAP--ENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDT 58
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 140-436 1.67e-08

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: 54.36  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 140 VGHRGAgnstttakLAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKKfvhtqkyeadpVELF 219
Cdd:cd08555    2 LSHRGY--------SQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGIL-----------PPTL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 220 EIPVKeltfdqlqllklshvtalktkdrkqsLYEEENFFSenqpfpslkmvleslPENVGFNIEIKwicqhrdgvwdgnl 299
Cdd:cd08555   63 EEVLE--------------------------LIADYLKNP---------------DYTIILSLEIK-------------- 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 300 STYFDMNVFLDIILKTVLENSG---KRRIVFSSFDAdictmvrqkqnkypilfltqgksdiypelmdlrsrttpiamsfa 376
Cdd:cd08555   88 QDSPEYDEFLAKVLKELRVYFDydlRGKVVLSSFNA-------------------------------------------- 123

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 377 qfeNILGINAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNdPENRRKLKEFGVNGLIYDR 436
Cdd:cd08555  124 ---LGVDYYNFSSKLIKDTELIASANKLGLLSRIWTVNDN-NEIINKFLNLGVDGLITDF 179
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 140-193 8.16e-08

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: 52.99  E-value: 8.16e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568918607 140 VGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHD 193
Cdd:cd08570    2 IGHRGYK--------AKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHD 47
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 143-195 2.22e-07

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: 52.36  E-value: 2.22e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 143 RGAGNSTTTAklAKVQ-------ENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLT 195
Cdd:cd08613   39 EGVENDTCTA--ERIDppthdylENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWT 96
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 137-195 2.79e-07

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: 51.54  E-value: 2.79e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568918607 137 PLDVGHRGAgnstttAKLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLT 195
Cdd:cd08574    2 PALIGHRGA------PMLAP--ENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRT 52
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 137-436 3.09e-07

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: 51.55  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 137 PLDVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKkfvhtqkyeADPV 216
Cdd:cd08601    1 NAVIAHRGAS--------GYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHD----ETLDRT---------TNIE 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 217 elFEIPVKELTFDQLQLLklshvTALKTKDRKQSLYEEENFfsENQPFPSLKMVLESLPENVGFNIEIKwicqhrdgvwd 296
Cdd:cd08601   60 --RPGPVKDYTLAEIKQL-----DAGSWFNKAYPEYARESY--SGLKVPTLEEVIERYGGRANYYIETK----------- 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 297 gnLSTYF-DMNV-FLDIILKTVLE--NSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGK--SDIYPELMDL-RSRTT 369
Cdd:cd08601  120 --SPDLYpGMEEkLLATLDKYGLLtdNLKNGQVIIQSFSKESLKKLHQLNPNIPLVQLLWYGegAETYDKWLDEiKEYAI 197

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568918607 370 PIAMSFAQFenilginahtedllrNPSYVQEAKAKGLVIFCWgdDTNDPENRRKLKEFGVNGLIYDR 436
Cdd:cd08601  198 GIGPSIADA---------------DPWMVHLIHKKGLLVHPY--TVNEKADMIRLINWGVDGMFTNY 247
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 159-436 6.83e-07

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: 51.06  E-value: 6.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 159 ENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKKFVHTQKYEADPVELFEIPVkelTFDQlqllklSH 238
Cdd:cd08612   41 ENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLPPYLEKLEV---TFSP------GD 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 239 VTALKTKDRKqslyeeenffsenqpFPSLKMVLESLPeNVGFNIEIKwicqhrdgvwdgnlstyFDMNVFLDIILKTVLE 318
Cdd:cd08612  112 YCVPKGSDRR---------------IPLLEEVFEAFP-DTPINIDIK-----------------VENDELIKKVSDLVRK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 319 NSGKRRIVFSSFDADICTMVRQKQNKYPILF-LTQGK-------------SDIYPELMDLRSRTTPIAMSFAQFENILG- 383
Cdd:cd08612  159 YKREDITVWGSFNDEIVKKCHKENPNIPLFFsLKRVLlllllyytgllpfIPIKESFLEIPMPSIFLKTYFPKSMSRLNr 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568918607 384 -INAHTEDLLRNPSYVQEAKAKGLVIFCWgdDTNDPENRRKLKEFGVNGLIYDR 436
Cdd:cd08612  239 fVLFLIDWLLMRPSLFRHLQKRGIQVYGW--VLNDEEEFERAFELGADGVMTDY 290
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 140-293 3.73e-06

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: 48.09  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 140 VGHRGAGNSTTTaklakVQENTIASLRNAASHGAAFvEFDVHLSKDFVPVVYHDltccLTMKRKKFVhtqkyeadpvelf 219
Cdd:cd08585    7 IAHRGLHDRDAG-----IPENSLSAFRAAAEAGYGI-ELDVQLTADGEVVVFHD----DNLKRLTGV------------- 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568918607 220 EIPVKELTFDQLQLLKLshvtaLKTKDrkqslyeeenffsenqPFPSLKMVLESLPENVGFNIEIKwICQHRDG 293
Cdd:cd08585   64 EGRVEELTAAELRALRL-----LGTDE----------------HIPTLDEVLELVAGRVPLLIELK-SCGGGDG 115
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 137-285 6.30e-06

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: 47.71  E-value: 6.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 137 PLDVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYH--DLTccltmkrkkfVHTQKYEad 214
Cdd:cd08580    1 PLIVAHRGGT--------ADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRpsDLK----------SLTNGSG-- 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568918607 215 pvelfeiPVKELTFDQLQLLKLSHvtALKTKDrkqslyeEENFFSENQPFPSLKMVLESLPENVgFNIEIK 285
Cdd:cd08580   61 -------AVSAYTAAQLATLNAGY--NFKPEG-------GYPYRGKPVGIPTLEQVLRAFPDTP-FILDMK 114
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 137-285 7.83e-06

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: 47.77  E-value: 7.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 137 PLDVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTC-CLTMKRKKFVHTQK----- 210
Cdd:cd08600    1 KIIIAHRGAS--------GYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLdNVTNVAEKFPDRKRkdgry 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 211 YeadpvelfeipVKELTFDQLQLLKLSHVTALKTKDRKQsLYeeENFFSENQP---FPSLKMVLE-------SLPENVGF 280
Cdd:cd08600   73 Y-----------VIDFTLDELKSLSVTERFDIENGKKVQ-VY--PNRFPLWKSdfkIHTLEEEIEliqglnkSTGKNVGI 138


                 ....*
gi 568918607 281 NIEIK 285
Cdd:cd08600  139 YPEIK 143
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 134-314 8.13e-06

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: 47.61  E-value: 8.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 134 PRIPLDVGHRGAgnstttAKLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltCCLTmkRKKFVHTQKYEA 213
Cdd:cd08609   24 PPKPALVGHRGA------PMLAP--ENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHD--EGLL--RTTNVKDVFPGR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 214 DPVELFEIPVKELTfdqlQLLKLSHVTALKTKDRKQSLYEEENFFSENQPFPSLKMVLESLPENvgfNIEIKWicqhrDG 293
Cdd:cd08609   92 DAAGSNNFTWTELK----TLNAGSWFLERRPFWTLSSLSEEDRREADNQTVPSLSELLDLAKKH---NVSIMF-----DL 159

                        170       180
                 ....*....|....*....|...
gi 568918607 294 VWDGNLSTYFDMNVF--LDIILK 314
Cdd:cd08609  160 RNENNSHVFYSSFVFytLETILK 182
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 116-195 1.48e-05

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


Pssm-ID: 176552 [Multi-domain]  Cd Length: 316  Bit Score: 46.79  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 116 PLPGYSCSMQSSFSKYWKPRIpldVGHRGAgnstttAKLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLT 195
Cdd:cd08610    5 PLGIYSPCIREKETLGPKPTI---IGHRGA------PMLAP--ENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFT 73
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 137-381 1.16e-04

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: 44.21  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 137 PLDVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTM---KRKKFV-HTQKYE 212
Cdd:cd08602    1 PLVIAHRGAS--------GYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTdvaDHPEFAdRKTTKT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 213 ADPVELFEIPVKELTFDQlqllklshvtaLKTKDRKQSLYEEENFFSENQPFPSLKMVLE-------SLPENVGFNIEIK 285
Cdd:cd08602   73 VDGVNVTGWFTEDFTLAE-----------LKTLRARQRLPYRDQSYDGQFPIPTFEEIIAlakaasaATGRTVGIYPEIK 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918607 286 wicqHrdgvwdgnlSTYFDMNVFL---DIILKTVLEN--SGKRRIVF-SSFDADICTMVRQKQNkYPILFLTQGKSDIYP 359
Cdd:cd08602  142 ----H---------PTYFNAPLGLpmeDKLLETLKKYgyTGKKAPVFiQSFEVTNLKYLRNKTD-LPLVQLIDDATIPPQ 207

                        250       260
                 ....*....|....*....|..
gi 568918607 360 ELMDLRSRTTPIAMSFAQFENI 381
Cdd:cd08602  208 DTPEGDSRTYADLTTDAGLKEI 229
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 137-193 1.69e-03

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 40.81  E-value: 1.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568918607 137 PLDVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHD 193
Cdd:PRK11143  27 KIVIAHRGAS--------GYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHD 75
 
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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