NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|597517940|ref|NP_001277980|]
View 

glycerophosphocholine phosphodiesterase GPCPD1 isoform 1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 138-430 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: 519.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 138 LDVGHRGAGNSTTTAKlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKYEADPVELFEIPVK 217
Cdd:cd08607    1 LDVGHRGAGNSYTAAS-AVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSDRDDLLEVPVK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 218 ELTFDQLQLLKLSHVTALKTKDRKQSlyEEENFFSENQPFPSLKMVLESLPENVGFNIEIKWICQHRDGVWDGNLSTYFD 297
Cdd:cd08607   80 DLTYEQLKLLKLFHISALKVKEYKSV--EEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKDGSWESELFTYFD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 298 MNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIYPELMDLRSRTTPIAMSFAQFENILGI 377
Cdd:cd08607  158 RNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPEFMDLRTRTFEIAVNFAQAEELLGV 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 597517940 378 NAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNDPENRRKLKEFGVNGLIYDRI 430
Cdd:cd08607  238 NLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDRI 290
 
Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 138-430 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: 519.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 138 LDVGHRGAGNSTTTAKlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKYEADPVELFEIPVK 217
Cdd:cd08607    1 LDVGHRGAGNSYTAAS-AVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSDRDDLLEVPVK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 218 ELTFDQLQLLKLSHVTALKTKDRKQSlyEEENFFSENQPFPSLKMVLESLPENVGFNIEIKWICQHRDGVWDGNLSTYFD 297
Cdd:cd08607   80 DLTYEQLKLLKLFHISALKVKEYKSV--EEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKDGSWESELFTYFD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 298 MNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIYPELMDLRSRTTPIAMSFAQFENILGI 377
Cdd:cd08607  158 RNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPEFMDLRTRTFEIAVNFAQAEELLGV 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 597517940 378 NAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNDPENRRKLKEFGVNGLIYDRI 430
Cdd:cd08607  238 NLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDRI 290
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 142-430 9.25e-49

Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes of glycerophosphoryl diester phosphodiesterase (GDPD) - periplasmic and cytosolic. This family also includes agrocinopine synthase, the similarity to GDPD has been noted. This family appears to have weak but not significant matches to mammalian phospholipase C pfam00388, which suggests that this family may adopt a TIM barrel fold.


Pssm-ID: 397241 [Multi-domain]  Cd Length: 244  Bit Score: 167.96  E-value: 9.25e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940  142 HRGAGNSTTtaklakvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKYEADPvelfeiPVKELTF 221
Cdd:pfam03009   1 HRGASGSYP--------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHD----FNLDRTTDGAG------YVRDLTL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940  222 DQLQLLKLSHVtalktkdRKQSLYEEENffsenqPFPSLKMVLEsLPENVGFNIEIKWICQHRDGVWDGNLStYFDMNVF 301
Cdd:pfam03009  63 EELKRLDIGAG-------NSGPLSGERV------PFPTLEEVLE-FDWDVGFNIEIKIKPYVEAIAPEEGLI-VKDLLLS 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940  302 LDIILKtvlENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTqgkSDIYPELMDLRSRTTPiamsFAQFENILGINAHT 381
Cdd:pfam03009 128 VDEILA---KKADPRRVIFSSFNPDELKRLRELAPKLPLVFLS---SGRAYAEADLLERAAA----FAGAPALLGEVALV 197

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 597517940  382 EDllRNPSYVQEAKAKGLVIFCWGDdtNDPENRRKLKEFGVNGLIYDRI 430
Cdd:pfam03009 198 DE--ALPDLVKRAHARGLVVHVWTV--NNEDEMKRLLELGVDGVITDRP 242
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
133-430 2.72e-40

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 145.01  E-value: 2.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 133 KPRIpldVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKYEADpvelf 212
Cdd:COG0584    2 RPLI---IAHRGAS--------GLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHD----PTLDRTTNGT----- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 213 eIPVKELTFDQLQLLKLSHVTALKtkdrkqslyeeenffseNQPFPSLKMVLESLPENVGFNIEIKwicqhrdgvwdgnl 292
Cdd:COG0584   62 -GRVADLTLAELRQLDAGSGPDFA-----------------GERIPTLEEVLELVPGDVGLNIEIK-------------- 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 293 STYFDMNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTqgkSDIYPELMDLRSRTtpiamsfaqfe 372
Cdd:COG0584  110 SPPAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLV---EELPADPLELARAL----------- 175

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 597517940 373 NILGINAHTEDLlrNPSYVQEAKAKGLVIFCWgddT-NDPENRRKLKEFGVNGLIYDRI 430
Cdd:COG0584  176 GADGVGPDYDLL--TPELVAAAHAAGLKVHVW---TvNDPEEMRRLLDLGVDGIITDRP 229
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 134-430 1.19e-10

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 61.88  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 134 PRIpldVGHRGAGnstttaKLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKYeadpvelfe 213
Cdd:PRK09454   8 PRI---VAHRGGG------KLAP--ENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWG--------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 214 iPVKELTFDQLQllklshvtALKTKDRKQSLYEEEnffsenqPFPSLKMVLESLPENvGF--NIEIKWI--CQHRDG--V 287
Cdd:PRK09454  68 -VAGELTWQDLA--------QLDAGSWFSAAFAGE-------PLPTLSQVAARCRAH-GMaaNIEIKPTtgREAETGrvV 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 288 WDGNLSTYFDMNVFLdiilktvlensgkrriVFSSFDADICTMVRQKQNKYPILFLtqgkSDIYPElmDLRSRTTPIAms 367
Cdd:PRK09454 131 ALAARALWAGAAVPP----------------LLSSFSEDALEAARQAAPELPRGLL----LDEWPD--DWLELTRRLG-- 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597517940 368 faqfenILGINAHTEDLlrNPSYVQEAKAKGLVIFCWgdDTNDPENRRKLKEFGVNGLIYDRI 430
Cdd:PRK09454 187 ------CVSLHLNHKLL--DEARVAALKAAGLRILVY--TVNDPARARELLRWGVDCICTDRI 239
 
Name Accession Description Interval E-value
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 138-430 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: 519.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 138 LDVGHRGAGNSTTTAKlAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKYEADPVELFEIPVK 217
Cdd:cd08607    1 LDVGHRGAGNSYTAAS-AVVRENTIASFLQAAEHGADMVEFDVQLTKDLVPVVYHDFTLRVSLKSKGDSDRDDLLEVPVK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 218 ELTFDQLQLLKLSHVTALKTKDRKQSlyEEENFFSENQPFPSLKMVLESLPENVGFNIEIKWICQHRDGVWDGNLSTYFD 297
Cdd:cd08607   80 DLTYEQLKLLKLFHISALKVKEYKSV--EEDEDPPEHQPFPTLSDVLESVPEDVGFNIEIKWPQQQKDGSWESELFTYFD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 298 MNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIYPELMDLRSRTTPIAMSFAQFENILGI 377
Cdd:cd08607  158 RNLFVDIILKIVLEHAGKRRIIFSSFDADICTMLRFKQNKYPVLFLTQGKTQRYPEFMDLRTRTFEIAVNFAQAEELLGV 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 597517940 378 NAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNDPENRRKLKEFGVNGLIYDRI 430
Cdd:cd08607  238 NLHSEDLLKDPSQIELAKSLGLVVFCWGDDLNDPENRKKLKELGVDGLIYDRI 290
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 138-430 3.33e-152

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: 435.17  E-value: 3.33e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 138 LDVGHRGAGNSTTTAKLAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKYEADPVELFEIPVK 217
Cdd:cd08572    1 LVIGHRGLGKNYASGSLAGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSKTGSDEGELIEVPIH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 218 ELTFDQLQLLKLSHVTALKTKDRKQSL---YEEENFFSENQPFPSLKMVLESLPENVGFNIEIKWICQHRDGvwDGNLST 294
Cdd:cd08572   81 DLTLEQLKELGLQHISALKRKALTRKAkgpKPNPWGMDEHDPFPTLQEVLEQVPKDLGFNIEIKYPQLLEDG--EGELTP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 295 YFDMNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIyPELMDLRSRTTPIAMSFAQFENI 374
Cdd:cd08572  159 YFERNAFVDTILAVVFEHAGGRRIIFSSFDPDICIMLRLKQNKYPVLFLTNGGTNE-VEHMDPRRRSLQAAVNFALAEGL 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 597517940 375 LGINAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNDPENRRKLKEFGVNGLIYDRI 430
Cdd:cd08572  238 LGVVLHAEDLLKNPSLISLVKALGLVLFTYGDDNNDPENVKKQKELGVDGVIYDRV 293
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 140-430 1.33e-60

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: 200.36  E-value: 1.33e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 140 VGHRGAGNSTTTAKLAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMkrkyeadpvelFEIPVKEL 219
Cdd:cd08606    5 IGHRGLGKNTAERKSLQLGENTVESFILAASLGASYVEVDVQLTKDLVPVIYHDFLVSETG-----------TDVPIHDL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 220 TFDQ-LQLLKLSHVTALKTKDRKQSLYEEenffSENQPFPSLKMVLESLPENVGFNIEIKWICQHrDGVWDGNLSTYFDM 298
Cdd:cd08606   74 TLEQfLHLSRMKYTVDFKKKGFKGNSRGH----SIQAPFTTLEELLKKLPKSVGFNIELKYPMLH-EAEEEEVAPVAIEL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 299 NVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSdiyPELMDLRSRTTPIAMSFAQFENILGIN 378
Cdd:cd08606  149 NAFVDTVLEKVFDYGAGRNIIFSSFTPDICILLSLKQPGYPVLFLTEAGK---APDMDVRAASLQEAIRFAKQWNLLGLV 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 597517940 379 AHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNDPENRRKLKEFGVNGLIYDRI 430
Cdd:cd08606  226 SAAEPLVMCPRLIQVVKRSGLVCVSYGVLNNDPENAKTQVKAGVDAVIVDSV 277
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 142-430 9.25e-49

Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes of glycerophosphoryl diester phosphodiesterase (GDPD) - periplasmic and cytosolic. This family also includes agrocinopine synthase, the similarity to GDPD has been noted. This family appears to have weak but not significant matches to mammalian phospholipase C pfam00388, which suggests that this family may adopt a TIM barrel fold.


Pssm-ID: 397241 [Multi-domain]  Cd Length: 244  Bit Score: 167.96  E-value: 9.25e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940  142 HRGAGNSTTtaklakvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKYEADPvelfeiPVKELTF 221
Cdd:pfam03009   1 HRGASGSYP--------ENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHD----FNLDRTTDGAG------YVRDLTL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940  222 DQLQLLKLSHVtalktkdRKQSLYEEENffsenqPFPSLKMVLEsLPENVGFNIEIKWICQHRDGVWDGNLStYFDMNVF 301
Cdd:pfam03009  63 EELKRLDIGAG-------NSGPLSGERV------PFPTLEEVLE-FDWDVGFNIEIKIKPYVEAIAPEEGLI-VKDLLLS 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940  302 LDIILKtvlENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTqgkSDIYPELMDLRSRTTPiamsFAQFENILGINAHT 381
Cdd:pfam03009 128 VDEILA---KKADPRRVIFSSFNPDELKRLRELAPKLPLVFLS---SGRAYAEADLLERAAA----FAGAPALLGEVALV 197

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 597517940  382 EDllRNPSYVQEAKAKGLVIFCWGDdtNDPENRRKLKEFGVNGLIYDRI 430
Cdd:pfam03009 198 DE--ALPDLVKRAHARGLVVHVWTV--NNEDEMKRLLELGVDGVITDRP 242
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 140-430 1.45e-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: 166.05  E-value: 1.45e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 140 VGHRGAGNSTTTAKL---AKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTmkrkyEADPVELFEIpv 216
Cdd:cd08605    3 IGHRGLGMNRASHQPsvgPGIRENTIASFIAASKFGADFVEFDVQVTRDGVPVIWHDDFIVVE-----RGGEVESSRI-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 217 KELTFDQLQLLKLShvtALKTKDRKQSLYEeenFFSENQP----------FPSLKMVLESLPENVGFNIEIKWicqhrdg 286
Cdd:cd08605   76 RDLTLAELKALGPQ---AESTKTSTVALYR---KAKDPEPepwimdvedsIPTLEEVFSEVPPSLGFNIELKF------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 287 vWDGNLSTYFDMNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIYpelMDLRSRTTPIAM 366
Cdd:cd08605  143 -GDDNKTEAEELVRELRAILAVCKQHAPGRRIMFSSFDPDAAVLLRALQSLYPVMFLTDCGPYTH---NDPRRNSIEAAI 218

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597517940 367 SFAQFENILGINAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNDPENRRKLKEFGVNGLIYDRI 430
Cdd:cd08605  219 QVALEGGLQGIVSEVKVLLRNPTAVSLVKASGLELGTYGKLNNDAEAVERQADLGVDGVIVDHV 282
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
133-430 2.72e-40

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 145.01  E-value: 2.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 133 KPRIpldVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKYEADpvelf 212
Cdd:COG0584    2 RPLI---IAHRGAS--------GLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHD----PTLDRTTNGT----- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 213 eIPVKELTFDQLQLLKLSHVTALKtkdrkqslyeeenffseNQPFPSLKMVLESLPENVGFNIEIKwicqhrdgvwdgnl 292
Cdd:COG0584   62 -GRVADLTLAELRQLDAGSGPDFA-----------------GERIPTLEEVLELVPGDVGLNIEIK-------------- 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 293 STYFDMNVFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTqgkSDIYPELMDLRSRTtpiamsfaqfe 372
Cdd:COG0584  110 SPPAAEPDLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGLLV---EELPADPLELARAL----------- 175

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 597517940 373 NILGINAHTEDLlrNPSYVQEAKAKGLVIFCWgddT-NDPENRRKLKEFGVNGLIYDRI 430
Cdd:COG0584  176 GADGVGPDYDLL--TPELVAAAHAAGLKVHVW---TvNDPEEMRRLLDLGVDGIITDRP 229
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 140-429 2.79e-37

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: 135.47  E-value: 2.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 140 VGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLtccltmkrkyeadpvelfeipvkel 219
Cdd:cd08556    2 IAHRGAS--------GEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHDI------------------------- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 220 tfdqlqllklshvtalktkdrkqslyeeenffsenqpfPSLKMVLESLPENVGFNIEIKWICQHRDgvwdgnlstyfDMN 299
Cdd:cd08556   49 --------------------------------------PTLEEVLELVKGGVGLNIELKEPTRYPG-----------LEA 79

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 300 VFLDIILKTVLENsgkrRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIYPELMDLRSRttpiamsfaqfeNILGINA 379
Cdd:cd08556   80 KVAELLREYGLEE----RVVVSSFDHEALRALKELDPEVPTGLLVDKPPLDPLLAELARAL------------GADAVNP 143

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 597517940 380 HteDLLRNPSYVQEAKAKGLVIFCWGDdtNDPENRRKLKEFGVNGLIYDR 429
Cdd:cd08556  144 H--YKLLTPELVRAAHAAGLKVYVWTV--NDPEDARRLLALGVDGIITDD 189
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 140-430 4.46e-25

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: 103.07  E-value: 4.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 140 VGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTC--CLTMKRkyeadpvelfeiPVK 217
Cdd:cd08562    2 IAHRGAS--------SLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLdrTTNGSG------------AVT 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 218 ELTFDQLQLLKLSHvtalktkdrkqslyeeenFFSE---NQPFPSLKMVLESLPE-NVGFNIEIKwICQHRDgvwdgnls 293
Cdd:cd08562   62 ELTWAELAQLDAGS------------------WFSPefaGEPIPTLADVLELARElGLGLNLEIK-PDPGDE-------- 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 294 tyFDMNVFLDIILKTVleNSGKRRIVFSSFDADICTMVRQKQNKYPILFLTqgksdiypelmdlrsrTTPIAMSFAQFEN 373
Cdd:cd08562  115 --ALTARVVAAALREL--WPHASKLLLSSFSLEALRAARRAAPELPLGLLF----------------DTLPADWLELLAA 174

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 597517940 374 ILGINAHTEDLLRNPSYVQEAKAKGLVIFCWgddT-NDPENRRKLKEFGVNGLIYDRI 430
Cdd:cd08562  175 LGAVSIHLNYRGLTEEQVKALKDAGYKLLVY---TvNDPARAAELLEWGVDAIFTDRP 229
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 141-428 7.13e-24

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: 99.68  E-value: 7.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 141 GHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKYEADpvelfeIPVKELT 220
Cdd:cd08568    4 GHRGYR--------AKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHD----ENLKRVGGVD------LKVKELT 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 221 FDQLQLLKLshvtalktkdrkqslyeeenffsENQPFPSLKMVLESLPENVGFNIEIKWIcqhrDGVwdgnlstyfdmnv 300
Cdd:cd08568   66 YKELKKLHP-----------------------GGELIPTLEEVFRALPNDAIINVEIKDI----DAV------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 301 flDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIY-----PELMDLRSRTTPI-AMSFAQFENI 374
Cdd:cd08568  106 --EPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPDAKVGLLIGEEEEGFsipelHEKLKLYSLHVPIdAIGYIGFEKF 183

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 597517940 375 LginahtedllrnpSYVQEAKAKGLVIFCWgdDTNDPENRRKLKEFgVNGLIYD 428
Cdd:cd08568  184 V-------------ELLRLLRKLGLKIVLW--TVNDPELVPKLKGL-VDGVITD 221
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 140-429 2.05e-22

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity 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: 95.84  E-value: 2.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 140 VGHRGAgnSTTtaklakVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKYEADPvelfeiPVKEL 219
Cdd:cd08582    2 IAHRGA--SAE------APENTLAAFELAWEQGADGIETDVRLTKDGELVCVHD----PTLKRTSGGDG------AVSDL 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 220 TFDQLQLLKLShvtalktkDRKQSLYEEENffsenqpFPSLKMVLESLPE-NVGFNIEIKWicqhrdgvwdgnlSTYFDM 298
Cdd:cd08582   64 TLAELRKLDIG--------SWKGESYKGEK-------VPTLEEYLAIVPKyGKKLFIEIKH-------------PRRGPE 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 299 NVflDIILKTVLENSGKR-RIVFSSFDADICTMVRQKQNKYPILFLTQGKSDiypelmdlRSRTTPIAMSFaqfeNILGI 377
Cdd:cd08582  116 AE--EELLKLLKESGLLPeQIVIISFDAEALKRVRELAPTLETLWLRNYKSP--------KEDPRPLAKSG----GAAGL 181

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 597517940 378 NAHTEDLLrNPSYVQEAKAKGLVIFCWgddT-NDPENRRKLKEFGVNGLIYDR 429
Cdd:cd08582  182 DLSYEKKL-NPAFIKALRDAGLKLNVW---TvDDAEDAKRLIELGVDSITTNR 230
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 141-429 1.14e-21

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: 94.30  E-value: 1.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 141 GHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHD--LTCCLTMKRKYEADPVElfEIPVKE 218
Cdd:cd08567    5 GHRGAR--------GLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDpkLNPDITRDPDGAWLPYE--GPALYE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 219 LTFDQLQLLKlshVTALKTKDRKQSLYEEENFFsENQPFPSLKMVLESLPENVG----FNIEIKWICQHRDGVWDGnlst 294
Cdd:cd08567   75 LTLAEIKQLD---VGEKRPGSDYAKLFPEQIPV-PGTRIPTLEEVFALVEKYGNqkvrFNIETKSDPDRDILHPPP---- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 295 yfdmNVFLDIILKtVLENSGK-RRIVFSSFDADICTMVRQKQNKYPILFLTQGKsdiypelmdlRSRTTPIAMSFAQFEn 373
Cdd:cd08567  147 ----EEFVDAVLA-VIRKAGLeDRVVLQSFDWRTLQEVRRLAPDIPTVALTEET----------TLGNLPRAAKKLGAD- 210

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 597517940 374 ilgINAHTEDLLrNPSYVQEAKAKGLVIFCWGddTNDPENRRKLKEFGVNGLIYDR 429
Cdd:cd08567  211 ---IWSPYFTLV-TKELVDEAHALGLKVVPWT--VNDPEDMARLIDLGVDGIITDY 260
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 159-430 3.17e-20

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: 90.35  E-value: 3.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 159 ENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLT-CCLTMKrkyeadpvelfEIPVKELTFDQLQLLKLS-HVTAlk 236
Cdd:cd08575   15 ENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDlDRLTGG-----------SGLVSDLTYAELPPLDAGyGYTF-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 237 TKDRKQSLYEeenffSENQPFPSLKMVLESLPeNVGFNIEIKwicqhrdgvwdgnlstYFDMNVFLDIILKTVLENSGKR 316
Cdd:cd08575   82 DGGKTGYPRG-----GGDGRIPTLEEVFKAFP-DTPINIDIK----------------SPDAEELIAAVLDLLEKYKRED 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 317 RIVFSSFDADICtmvrQKQNKYPilfltqgksdiyPELMDLRSRTT-----------------PIAMSFAQF-------- 371
Cdd:cd08575  140 RTVWGSTNPEYL----RALHPEN------------PNLFESFSMTRclllylalgytgllpfvPIKESFFEIprpvivle 203

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 372 ENILGINAHTED-LLRNPSYVQEAKAKGLVIFCWGddTNDPENRRKLKEFGVNGLIYDRI 430
Cdd:cd08575  204 TFTLGEGASIVAaLLWWPNLFDHLRKRGIQVYLWV--LNDEEDFEEAFDLGADGVMTDSP 261
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 141-428 2.01e-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: 87.23  E-value: 2.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 141 GHRGAgnstttakLAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKYEadpvelfeipVKELT 220
Cdd:cd08563    5 AHRGY--------SGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGY----------VKDLT 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 221 FDQLQLLKLShvtalktkdrkqslyeeeNFFSENQPF---PSLKMVLESLPE-NVGFNIEIKwicqhrdgvwdgnlSTYF 296
Cdd:cd08563   67 LEELKKLDAG------------------SWFDEKFTGekiPTLEEVLDLLKDkDLLLNIEIK--------------TDVI 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 297 DMNVFLDIILKTVLENSGKRRIVFSSFDADicTMVRQKQ--NKYPILFLTQGKSDIYPElmdlrsrttpiamsFAQFENI 374
Cdd:cd08563  115 HYPGIEKKVLELVKEYNLEDRVIFSSFNHE--SLKRLKKldPKIKLALLYETGLQDPKD--------------YAKKIGA 178

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 597517940 375 LGINAHTEDLlrNPSYVQEAKAKGLVIFCWgddT-NDPENRRKLKEFGVNGLIYD 428
Cdd:cd08563  179 DSLHPDFKLL--TEEVVEELKKRGIPVRLW---TvNEEEDMKRLKDLGVDGIITN 228
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 140-336 6.58e-18

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: 82.77  E-value: 6.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 140 VGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKYEAdpvelfEIPVKEL 219
Cdd:cd08581    2 VAHRGYP--------ARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHD----DTLLRLTGV------EGLLHEL 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 220 TFDQLQLLklshvtalktkdrkqSLYEEENFFS--ENQPFPSLKMV---LESLPEnVGFNIEIKWICQHRDGVwdgnlst 294
Cdd:cd08581   64 EDAELDSL---------------RVAEPARFGSrfAGEPLPSLAAVvqwLAQHPQ-VTLFVEIKTESLDRFGL------- 120

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 597517940 295 yfdmNVFLDIILKtVLENSGKRRiVFSSFDADICTMVRQKQN 336
Cdd:cd08581  121 ----ERVVDKVLR-ALPAVAAQR-VLISFDYDLLALAKQQGG 156
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 141-429 8.11e-18

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: 82.69  E-value: 8.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 141 GHRGAgnstttAKLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTccltmkrkyeADPVELFEIPVKELT 220
Cdd:cd08561    3 AHRGG------AGLAP--ENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDET----------LDRTTDGTGPVADLT 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 221 FDQLQLLKLSHvtalKTKDRKQSLYEEENffsENQPFPSLKMVLESLPeNVGFNIEIKwicQHRDGVWDgnlstyfdmnV 300
Cdd:cd08561   65 LAELRRLDAGY----HFTDDGGRTYPYRG---QGIRIPTLEELFEAFP-DVRLNIEIK---DDGPAAAA----------A 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 301 FLDIILKTVLENsgkrRIVFSSFDADIctmVRQKQNKYPILFLTQGKSDIYPELMDLRSRTTPIAMSFAQF----ENILG 376
Cdd:cd08561  124 LADLIERYGAQD----RVLVASFSDRV---LRRFRRLCPRVATSAGEGEVAAFVLASRLGLGSLYSPPYDAlqipVRYGG 196

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 597517940 377 INahtedlLRNPSYVQEAKAKGLVIFCWGDdtNDPENRRKLKEFGVNGLIYDR 429
Cdd:cd08561  197 VP------LVTPRFVRAAHAAGLEVHVWTV--NDPAEMRRLLDLGVDGIITDR 241
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 137-434 2.23e-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: 79.62  E-value: 2.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 137 PLDVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLT--MKRKYEADPVELFEI 214
Cdd:cd08559    1 PLVIAHRGAS--------GYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTtnVAEHFPFRGRKDTGY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 215 PVKELTFDQLQLLKLSHVTALKTKDRKQSLYeeenffsENQPFPSLKMVLE-------SLPENVGFNIEIKwicqhrdgv 287
Cdd:cd08559   73 FVIDFTLAELKTLRAGSWFNQRYPERAPSYY-------GGFKIPTLEEVIElaqglnkSTGRNVGIYPETK--------- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 288 wdgnLSTYFDMNvFLDI--ILKTVLE----NSGKRRIVFSSFDADICTMVRQKQNKYPILFLT-QGKSDIYPELMDLRSR 360
Cdd:cd08559  137 ----HPTFHKQE-GPDIeeKLLEVLKkygyTGKNDPVFIQSFEPESLKRLRNETPDIPLVQLIdYGDWAETDKKYTYAWL 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 361 TTPIAMSF-AQFENILG------INAHTEDLLRNPSYVQEAKAKGLVIFCWgddTNDPENRRKLKEFGVNgliYDRIYDW 433
Cdd:cd08559  212 TTDAGLKEiAKYADGIGpwksliIPEDSNGLLVPTDLVKDAHKAGLLVHPY---TFRNENLFLAPDFKQD---MDALYNA 285


                 .
gi 597517940 434 M 434
Cdd:cd08559  286 A 286
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 140-429 2.60e-16

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: 77.97  E-value: 2.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 140 VGHRG-AGNSTttaklakvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCC-LTMKRKyeadpvelfeiPVK 217
Cdd:cd08579    2 IAHRGvSSNGV---------ENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKrLAGVNK-----------KVW 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 218 ELTFDQLQLLKLShvtalktkdrkqslyeeENFFSEnqPFPSLKMVLE-SLPENVGFNIEIKWICQHRDGVwdgnlstyf 296
Cdd:cd08579   62 DLTLEELKKLTIG-----------------ENGHGA--KIPSLDEYLAlAKGLKQKLLIELKPHGHDSPDL--------- 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 297 dMNVFLDIILKTVLENSgkrrIVFSSFDADICTMVRQKQNKYPILFLTQGKSDIYPElmdlrsrttpiamSFAQFENIlg 376
Cdd:cd08579  114 -VEKFVKLYKQNLIENQ----HQVHSLDYRVIEKVKKLDPKIKTGYILPFNIGNLPK-------------TNVDFYSI-- 173

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 597517940 377 inahtEDLLRNPSYVQEAKAKGLVIFCWgdDTNDPENRRKLKEFGVNGLIYDR 429
Cdd:cd08579  174 -----EYSTLNKEFIRQAHQNGKKVYVW--TVNDPDDMQRYLAMGVDGIITDY 219
GDPD_NUC-2_fungi cd08578
Putative glycerophosphodiester phosphodiesterase domain of ankyrin repeat protein NUC-2 and ...
 131-427 1.21e-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: 77.36  E-value: 1.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 131 YWKPRIPLDVGHRGAGNSTTTAklakvqentiaslrnaASHGAAFVEFDVHLSKDFVPVVYHDLTCcltmkrkyeadPVE 210
Cdd:cd08578    3 YWKSTSGSDTQANKDGNSFVTA----------------SSLSGEYLRVKVCVLKDGTPVVAPEWFV-----------PVG 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 211 LFEIPVKELTFDQLQLLKLSHV-----TALKTKDRKQSLyeeenffseNQPFPSLKMVLESLPENVGFNI--------EI 277
Cdd:cd08578   56 GIKLLVSDLTAEQLESILDYSLddlnsEISDMVDLKRLL---------SSRVVSLETLLELLPPSIQLDIqvlfptaaEI 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 278 KWIcqhrdgvwDGNLSTYFDMNVFLDIILKTVLENSGK--------RRIVFSSFDADICTMVRQKQNKYPILF------- 342
Cdd:cd08578  127 ASI--------PVKGSPLVDLNKFIDTVLLVVFDHARYlrhtpgstRSIVFSSCNPEVCTILNWKQPNFPVFFamnglvr 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 343 ----------LTQGKSDIYPELM---DLRSRTTPIAMSFAQFENILGINAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTN 409
Cdd:cd08578  199 nndtlsfdtpHHLDSLAVDPQKLneaDPRSRSIKEAVRFAKNNNLLGLILPYSLLNIVPQLVESIKSRGLLLIASGEPES 278

                        330
                 ....*....|....*...
gi 597517940 410 DPENrrKLKEFGVNGLIY 427
Cdd:cd08578  279 LIEV--AEAGDGINGVVT 294
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 140-429 8.48e-15

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: 73.88  E-value: 8.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 140 VGHRGAGNstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKYEADpvelfeIPVKEL 219
Cdd:cd08566    3 VAHRGGWG-------AGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHD----DTLDRTTNGK------GKVSDL 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 220 TFDQLQLLKlshvtaLKTKDRKQSlyeeenffseNQPFPSLKMVLESLPENVGFNIEIKWicqhrdgvwdgnlstyFDMN 299
Cdd:cd08566   66 TLAEIRKLR------LKDGDGEVT----------DEKVPTLEEALAWAKGKILLNLDLKD----------------ADLD 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 300 VFLDIILKTVLENsgkrRIVFSSFDADICTMVRQKQNKYPIlfltqgkSDIYPELMDLRSRTTPIAMsfaqFENILGINA 379
Cdd:cd08566  114 EVIALVKKHGALD----QVIFKSYSEEQAKELRALAPEVML-------MPIVRDAEDLDEEEARAID----ALNLLAFEI 178

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597517940 380 HTEDLLRNPSYVQEAKAKGLVIFC---WGDD--------TNDPENRRKLKEFGVNGLIYDR 429
Cdd:cd08566  179 TFDDLDLPPLFDELLRALGIRVWVntlGDDDtagldralSDPREVWGELVDAGVDVIQTDR 239
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 136-430 4.19e-13

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: 69.42  E-value: 4.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 136 IPLDVGHRGAGNSTTTAklakvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYH---DLTCCLTMKRKYEADPVElf 212
Cdd:cd08564    3 RPIIVGHRGAGCSTLYP------ENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHgteDDTNPDTSIQLDDSGFKN-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 213 eipVKELTFDQLQLLKLSHVTALKTKDRKQSLYEEenffsenqpFPSLKMVLESLPENVGFNIEIKwicqhrdgvwdGNL 292
Cdd:cd08564   75 ---INDLSLDEITRLHFKQLFDEKPCGADEIKGEK---------IPTLEDVLVTFKDKLKYNIELK-----------GRE 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 293 StyfDMNVFldiILKTVLENSGKRRIVFSSFD----ADICTMVRQKQNKYPILFLtqgksdiypeLMDLRSRTTPIAMSF 368
Cdd:cd08564  132 V---GLGER---VLNLVEKYGMILQVHFSSFLhydrLDLLKALRPNKLNVPIALL----------FNEVKSPSPLDFLEQ 195

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597517940 369 AQFENILGinAHTEDLLRNPSYVQEAKAKGLVIFCW--GDDTNDPENRRKLKEFGVNGLIYDRI 430
Cdd:cd08564  196 AKYYNATW--VNFSYDFWTEEFVKKAHENGLKVMTYfdEPVNDNEEDYKVYLELGVDCICPNDP 257
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 140-429 2.03e-11

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: 63.96  E-value: 2.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 140 VGHRGAGNstttaklaKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKYEADPvelfeiPVKEL 219
Cdd:cd08565    2 AGHRGGRN--------LWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHD----PTLDRTTHGTG------AVRDL 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 220 TfdqlqllkLSHVTALKTKDrkqslyeeenffSENQPFPSLKMVLESL-PENVGFNIEIKwicqhrdgvWDGNLSTYFDm 298
Cdd:cd08565   64 T--------LAERKALRLRD------------SFGEKIPTLEEVLALFaPSGLELHVEIK---------TDADGTPYPG- 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 299 nvFLDIILKTVLENSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGKSdiypELMDLRSRTTPIAmsfaqFENILGIN 378
Cdd:cd08565  114 --AAALAAATLRRHGLLERSVLTSFDPAVLTEVRKHPGVRTLGSVDEDML----ERLGGELPFLTAT-----ALKAHIVA 182

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 597517940 379 AHTEDLLRNPSYVQEAKaKGLVIFCWGddTNDPENRRKLKEFGVNGLIYDR 429
Cdd:cd08565  183 VEQSLLAATWELVRAAV-PGLRLGVWT--VNDDSLIRYWLACGVRQLTTDR 230
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 140-230 6.01e-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: 6.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 140 VGHRGAGNStttaklakVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKYEADPVelfeipVKEL 219
Cdd:cd08573    2 IGHRGAGHD--------APENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHD----DTVDRTTDGTGL------VAEL 63

                         90
                 ....*....|.
gi 597517940 220 TFDQLQLLKLS 230
Cdd:cd08573   64 TWEELRKLNAA 74
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 134-430 1.19e-10

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 61.88  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 134 PRIpldVGHRGAGnstttaKLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKYeadpvelfe 213
Cdd:PRK09454   8 PRI---VAHRGGG------KLAP--ENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSNGWG--------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 214 iPVKELTFDQLQllklshvtALKTKDRKQSLYEEEnffsenqPFPSLKMVLESLPENvGF--NIEIKWI--CQHRDG--V 287
Cdd:PRK09454  68 -VAGELTWQDLA--------QLDAGSWFSAAFAGE-------PLPTLSQVAARCRAH-GMaaNIEIKPTtgREAETGrvV 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 288 WDGNLSTYFDMNVFLdiilktvlensgkrriVFSSFDADICTMVRQKQNKYPILFLtqgkSDIYPElmDLRSRTTPIAms 367
Cdd:PRK09454 131 ALAARALWAGAAVPP----------------LLSSFSEDALEAARQAAPELPRGLL----LDEWPD--DWLELTRRLG-- 186

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597517940 368 faqfenILGINAHTEDLlrNPSYVQEAKAKGLVIFCWgdDTNDPENRRKLKEFGVNGLIYDRI 430
Cdd:PRK09454 187 ------CVSLHLNHKLL--DEARVAALKAAGLRILVY--TVNDPARARELLRWGVDCICTDRI 239
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 140-429 2.01e-09

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: 56.68  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 140 VGHRGAgnstttakLAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTMKRKYEADPVELFEipvkel 219
Cdd:cd08555    2 LSHRGY--------SQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGILPPTLEEVLE------ 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 220 tfdqlqllklshvtalktkdrkqsLYEEENFFSenqpfpslkmvleslPENVGFNIEIKwicqhrdgvwdgnlSTYFDMN 299
Cdd:cd08555   68 ------------------------LIADYLKNP---------------DYTIILSLEIK--------------QDSPEYD 94

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 300 VFLDIILKTVLENSG---KRRIVFSSFDAdictmvrqkqnkypilfltqgksdiypelmdlrsrttpiamsfaqfeNILG 376
Cdd:cd08555   95 EFLAKVLKELRVYFDydlRGKVVLSSFNA-----------------------------------------------LGVD 127

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 597517940 377 INAHTEDLLRNPSYVQEAKAKGLVIFCWGDDTNdPENRRKLKEFGVNGLIYDR 429
Cdd:cd08555  128 YYNFSSKLIKDTELIASANKLGLLSRIWTVNDN-NEIINKFLNLGVDGLITDF 179
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 137-429 7.47e-09

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: 56.56  E-value: 7.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 137 PLDVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKYEADpvelFEIPV 216
Cdd:cd08601    1 NAVIAHRGAS--------GYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHD----ETLDRTTNIE----RPGPV 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 217 KELTFDQLQLLklshvTALKTKDRKQSLYEEENFfsENQPFPSLKMVLESLPENVGFNIEIKwicqhrdgvwdgnLSTYF 296
Cdd:cd08601   65 KDYTLAEIKQL-----DAGSWFNKAYPEYARESY--SGLKVPTLEEVIERYGGRANYYIETK-------------SPDLY 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 297 -DMNV-FLDIILKTVLE--NSGKRRIVFSSFDADICTMVRQKQNKYPILFLTQGK--SDIYPELMDL-RSRTTPIAMSFA 369
Cdd:cd08601  125 pGMEEkLLATLDKYGLLtdNLKNGQVIIQSFSKESLKKLHQLNPNIPLVQLLWYGegAETYDKWLDEiKEYAIGIGPSIA 204

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 370 QFenilginahtedllrNPSYVQEAKAKGLVIFCWgdDTNDPENRRKLKEFGVNGLIYDR 429
Cdd:cd08601  205 DA---------------DPWMVHLIHKKGLLVHPY--TVNEKADMIRLINWGVDGMFTNY 247
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 140-428 7.57e-09

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: 56.08  E-value: 7.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 140 VGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltccLTMKRKYEADPVElfeipVKEL 219
Cdd:cd08570    2 IGHRGYK--------AKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHD----PNLKRCFGKDGLI-----IDDS 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 220 TFDQLQLlklshvtaLKTKDrkqslyeeenffSENQPFPSLKMVLEslpenvgfnieikWICQH-RDGVWdgnlstyfdm 298
Cdd:cd08570   65 TWDELSH--------LRTIE------------EPHQPMPTLKDVLE-------------WLVEHeLPDVK---------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 299 nVFLDI--------ILKTVLE--------NSGKRRIVFSSFDADIctmvrqkqnkypILFLTQGKS--DIYPELMDLRsr 360
Cdd:cd08570  102 -LMLDIkrdndpeiLFKLIAEmlavkpdlDFWRERIILGLWHLDF------------LKYGKEVLPgfPVFHIGFSLD-- 166

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 597517940 361 ttpIAMSFAQF-ENILGINAH-----TEDLLRnpsYVQEAKAKGLVIFCWgddT-NDPENRRKLKEFGVNGLIYD 428
Cdd:cd08570  167 ---YARHFLNYsEKLVGISMHfvslwGPFGQA---FLPELKKNGKKVFVW---TvNTEEDMRYAIRLGVDGVITD 232
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 143-195 2.18e-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: 2.18e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 143 RGAGNSTTTAklAKVQ-------ENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLT 195
Cdd:cd08613   39 EGVENDTCTA--ERIDppthdylENTIASMQAAFDAGADVVELDVHPTKDGEFAVFHDWT 96
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 137-195 2.66e-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: 51.92  E-value: 2.66e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 597517940 137 PLDVGHRGAgnstttAKLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLT 195
Cdd:cd08574    2 PALIGHRGA------PMLAP--ENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRT 52
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 159-429 3.09e-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: 51.83  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 159 ENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCC-LTMKRKYeadpvelfeipVKELTFDQLQLLKLSHVTALKT 237
Cdd:cd08612   41 ENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLrSCGVDKL-----------VSDLNYADLPPYLEKLEVTFSP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 238 KDRKQSLYeeenffsENQPFPSLKMVLESLPeNVGFNIEIKwicqhrdgvwdgnlstyFDMNVFLDIILKTVLENSGKRR 317
Cdd:cd08612  110 GDYCVPKG-------SDRRIPLLEEVFEAFP-DTPINIDIK-----------------VENDELIKKVSDLVRKYKREDI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 318 IVFSSFDADICTMVRQKQNKYPILF-LTQGK-------------SDIYPELMDLRSRTTPIAMSFAQFENILG--INAHT 381
Cdd:cd08612  165 TVWGSFNDEIVKKCHKENPNIPLFFsLKRVLlllllyytgllpfIPIKESFLEIPMPSIFLKTYFPKSMSRLNrfVLFLI 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 597517940 382 EDLLRNPSYVQEAKAKGLVIFCWgdDTNDPENRRKLKEFGVNGLIYDR 429
Cdd:cd08612  245 DWLLMRPSLFRHLQKRGIQVYGW--VLNDEEEFERAFELGADGVMTDY 290
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 140-286 4.79e-07

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: 50.78  E-value: 4.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 140 VGHRGAGNSTTTaklakVQENTIASLRNAASHGAAFvEFDVHLSKDFVPVVYHDltccLTMKRKYEADPvelfeiPVKEL 219
Cdd:cd08585    7 IAHRGLHDRDAG-----IPENSLSAFRAAAEAGYGI-ELDVQLTADGEVVVFHD----DNLKRLTGVEG------RVEEL 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597517940 220 TFDQLQLLKLshvtaLKTKDrkqslyeeenffsenqPFPSLKMVLESLPENVGFNIEIKwICQHRDG 286
Cdd:cd08585   71 TAAELRALRL-----LGTDE----------------HIPTLDEVLELVAGRVPLLIELK-SCGGGDG 115
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 134-307 1.14e-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: 50.31  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 134 PRIPLDVGHRGAgnstttAKLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDltCCLTmkRKYEADPVELFE 213
Cdd:cd08609   24 PPKPALVGHRGA------PMLAP--ENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHD--EGLL--RTTNVKDVFPGR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 214 IPVKELTFDQLQLLKLSHVTALKTKD---RKQSLYEEENFFSENQPFPSLKMVLESLPENvgfNIEIKWicqhrDGVWDG 290
Cdd:cd08609   92 DAAGSNNFTWTELKTLNAGSWFLERRpfwTLSSLSEEDRREADNQTVPSLSELLDLAKKH---NVSIMF-----DLRNEN 163

                        170
                 ....*....|....*....
gi 597517940 291 NLSTYFDMNVF--LDIILK 307
Cdd:cd08609  164 NSHVFYSSFVFytLETILK 182
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 137-278 2.88e-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: 48.86  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 137 PLDVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYH--DLTcCLTMKrkyeadpvelfEI 214
Cdd:cd08580    1 PLIVAHRGGT--------ADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRpsDLK-SLTNG-----------SG 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597517940 215 PVKELTFDQLQLLKLSHvtALKTKDrkqslyeEENFFSENQPFPSLKMVLESLPENVgFNIEIK 278
Cdd:cd08580   61 AVSAYTAAQLATLNAGY--NFKPEG-------GYPYRGKPVGIPTLEQVLRAFPDTP-FILDMK 114
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 137-278 9.92e-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: 47.39  E-value: 9.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 137 PLDVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCcltmkrKYEADPVELFeiP- 215
Cdd:cd08600    1 KIIIAHRGAS--------GYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYL------DNVTNVAEKF--Pd 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 216 ---------VKELTFDQLQLLKLSHVTALKTKDRKQsLYeeENFFSENQP---FPSLKMVLE-------SLPENVGFNIE 276
Cdd:cd08600   65 rkrkdgryyVIDFTLDELKSLSVTERFDIENGKKVQ-VY--PNRFPLWKSdfkIHTLEEEIEliqglnkSTGKNVGIYPE 141


                 ..
gi 597517940 277 IK 278
Cdd:cd08600  142 IK 143
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 116-195 1.44e-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: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 116 PLPGYSCSMQSSFSKYWKPRIpldVGHRGAgnstttAKLAKvqENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLT 195
Cdd:cd08610    5 PLGIYSPCIREKETLGPKPTI---IGHRGA------PMLAP--ENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFT 73
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 137-374 2.20e-05

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: 46.52  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 137 PLDVGHRGAGnstttaklAKVQENTIASLRNAASHGAAFVEFDVHLSKDFVPVVYHDLTCCLTM-----------KRKYE 205
Cdd:cd08602    1 PLVIAHRGAS--------GYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTdvadhpefadrKTTKT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 206 ADPVELFEIPVKELTFDQlqllklshvtaLKTKDRKQSLYEEENFFSENQPFPSLKMVLE-------SLPENVGFNIEIK 278
Cdd:cd08602   73 VDGVNVTGWFTEDFTLAE-----------LKTLRARQRLPYRDQSYDGQFPIPTFEEIIAlakaasaATGRTVGIYPEIK 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517940 279 wicqHrdgvwdgnlSTYFDMNVFL---DIILKTVLEN--SGKRRIVF-SSFDADICTMVRQKQNkYPILFLTQGKSDIYP 352
Cdd:cd08602  142 ----H---------PTYFNAPLGLpmeDKLLETLKKYgyTGKKAPVFiQSFEVTNLKYLRNKTD-LPLVQLIDDATIPPQ 207

                        250       260
                 ....*....|....*....|..
gi 597517940 353 ELMDLRSRTTPIAMSFAQFENI 374
Cdd:cd08602  208 DTPEGDSRTYADLTTDAGLKEI 229
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 137-193 1.66e-03

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 40.81  E-value: 1.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 597517940 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH