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Conserved domains on  [gi|1333697150|ref|XP_023501476|]
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glycerophosphodiester phosphodiesterase domain-containing protein 5 isoform X6 [Equus caballus]

Protein Classification

PI-PLC domain-containing protein( domain architecture ID 49489)

PI-PLC (phosphoinositide-specific phospholipase C) domain-containing protein may hydrolyze the membrane lipid phosphatidylinositol to produce phosphorylated myo-inositol and diacylglycerol

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_GDPD_SF super family cl14615
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 227-576 0e+00

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.


The actual alignment was detected with superfamily member cd08608:

Pssm-ID: 472694  Cd Length: 351  Bit Score: 671.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 227 KPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPELARRPAAMLNWTVLQ 306
Cdd:cd08608     1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYEDASMFNWTDLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 307 RLNAGQWFLKTDPFWTASSLSPSDHREAQNQSICSLAELLELVK-GNATLLLNLRDPPREHPYRGTFLNFTLEALLRSGI 385
Cdd:cd08608    81 RLNAGQWFLKDDPFWTAQSLSPSDRKEAGNQSVCSLAELLELAKrYNASVLLNLRRPPPNHPYHQSWINLTLKTILASGI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 386 PQHQVMWLPNRQRPLVRKVAPGFQQTSGSKEAAASLRRGHIQWLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLFSLL 465
Cdd:cd08608   161 PQEQVMWTPDWQRKLVRKVAPGFQQTSGEKLPVASLRERGITRLNLRYTQASAQEIRDYSASNLSVNLYTVNEPWLYSLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 466 WCAGVPSVTSDNSHTLSQVSSPLWIMPPDEYCLMWVTADLVSFTLIVGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRD 545
Cdd:cd08608   241 WCSGVPSVTSDASHVLRKVPFPLWLMPPDEYCLIWITSDLISFAVIVGIFIFQKWRLGGIRSYNPEQIMLSAAVRRSSRD 320

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1333697150 546 VSIMKEKLIFSEISDGMEVSDELSVCSDNSY 576
Cdd:cd08608   321 VNIMKEKLIFSEINNGVETTDELSLCSDNGY 351
 
Name Accession Description Interval E-value
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 227-576 0e+00

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE2 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 5 (GDPD5)) and their metazoan homologs. Mammalian GDE2 is transmembrane protein primarily expressed in mature neurons. It is a mammalian homolog of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Mammalian GDE2 selectively hydrolyzes glycerophosphocholine (GPC) and has been characterized as GPC-GDE (EC 3.1.4.2) that contributes to osmotic regulation of cellular GPC. Mammalian GDE2 functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE2 also plays a critical role for retinoid-induced neuronal outgrowth. The catalytic activity of GDPD domain is essential for mammalian GDE2 cellular function.


Pssm-ID: 176550  Cd Length: 351  Bit Score: 671.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 227 KPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPELARRPAAMLNWTVLQ 306
Cdd:cd08608     1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYEDASMFNWTDLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 307 RLNAGQWFLKTDPFWTASSLSPSDHREAQNQSICSLAELLELVK-GNATLLLNLRDPPREHPYRGTFLNFTLEALLRSGI 385
Cdd:cd08608    81 RLNAGQWFLKDDPFWTAQSLSPSDRKEAGNQSVCSLAELLELAKrYNASVLLNLRRPPPNHPYHQSWINLTLKTILASGI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 386 PQHQVMWLPNRQRPLVRKVAPGFQQTSGSKEAAASLRRGHIQWLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLFSLL 465
Cdd:cd08608   161 PQEQVMWTPDWQRKLVRKVAPGFQQTSGEKLPVASLRERGITRLNLRYTQASAQEIRDYSASNLSVNLYTVNEPWLYSLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 466 WCAGVPSVTSDNSHTLSQVSSPLWIMPPDEYCLMWVTADLVSFTLIVGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRD 545
Cdd:cd08608   241 WCSGVPSVTSDASHVLRKVPFPLWLMPPDEYCLIWITSDLISFAVIVGIFIFQKWRLGGIRSYNPEQIMLSAAVRRSSRD 320

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1333697150 546 VSIMKEKLIFSEISDGMEVSDELSVCSDNSY 576
Cdd:cd08608   321 VNIMKEKLIFSEINNGVETTDELSLCSDNGY 351
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
226-484 3.91e-35

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 132.69  E-value: 3.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 226 PKPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVeelfpelaRRPAAMLNWTVL 305
Cdd:COG0584     1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNG--------TGRVADLTLAEL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 306 QRLNAGqwflktdpfwtasslspsDHREAQNQSICSLAELLELVKGNATLLLNLRDPPREHPyrgTFLNFTLEALLRSGI 385
Cdd:COG0584    73 RQLDAG------------------SGPDFAGERIPTLEEVLELVPGDVGLNIEIKSPPAAEP---DLAEAVAALLKRYGL 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 386 pQHQVM----WLPNRQRplVRKVAPGFQ----QTSGSKEAAASLRRGHIQWLNLRYTQVSHQELRDYASWNLSVNLYTVN 457
Cdd:COG0584   132 -EDRVIvssfDPEALRR--LRELAPDVPlgllVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVN 208

                         250       260
                  ....*....|....*....|....*..
gi 1333697150 458 APWLFSLLWCAGVPSVTSDNSHTLSQV 484
Cdd:COG0584   209 DPEEMRRLLDLGVDGIITDRPDLLRAV 235
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 226-314 2.26e-16

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 79.21  E-value: 2.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 226 PKPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNveelfpelARRPAAMLNWTVL 305
Cdd:PRK09454    6 PYPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSN--------GWGVAGELTWQDL 77


                  ....*....
gi 1333697150 306 QRLNAGQWF 314
Cdd:PRK09454   78 AQLDAGSWF 86
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 233-316 4.91e-15

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: 75.13  E-value: 4.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 233 HRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVeelfpelaRRPAAMLNWTVLQRLNAGQ 312
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDG--------AGYVRDLTLEELKRLDIGA 72


                  ....
gi 1333697150 313 WFLK 316
Cdd:pfam03009  73 GNSG 76
 
Name Accession Description Interval E-value
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 227-576 0e+00

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE2 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 5 (GDPD5)) and their metazoan homologs. Mammalian GDE2 is transmembrane protein primarily expressed in mature neurons. It is a mammalian homolog of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Mammalian GDE2 selectively hydrolyzes glycerophosphocholine (GPC) and has been characterized as GPC-GDE (EC 3.1.4.2) that contributes to osmotic regulation of cellular GPC. Mammalian GDE2 functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE2 also plays a critical role for retinoid-induced neuronal outgrowth. The catalytic activity of GDPD domain is essential for mammalian GDE2 cellular function.


Pssm-ID: 176550  Cd Length: 351  Bit Score: 671.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 227 KPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPELARRPAAMLNWTVLQ 306
Cdd:cd08608     1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYEDASMFNWTDLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 307 RLNAGQWFLKTDPFWTASSLSPSDHREAQNQSICSLAELLELVK-GNATLLLNLRDPPREHPYRGTFLNFTLEALLRSGI 385
Cdd:cd08608    81 RLNAGQWFLKDDPFWTAQSLSPSDRKEAGNQSVCSLAELLELAKrYNASVLLNLRRPPPNHPYHQSWINLTLKTILASGI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 386 PQHQVMWLPNRQRPLVRKVAPGFQQTSGSKEAAASLRRGHIQWLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLFSLL 465
Cdd:cd08608   161 PQEQVMWTPDWQRKLVRKVAPGFQQTSGEKLPVASLRERGITRLNLRYTQASAQEIRDYSASNLSVNLYTVNEPWLYSLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 466 WCAGVPSVTSDNSHTLSQVSSPLWIMPPDEYCLMWVTADLVSFTLIVGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRD 545
Cdd:cd08608   241 WCSGVPSVTSDASHVLRKVPFPLWLMPPDEYCLIWITSDLISFAVIVGIFIFQKWRLGGIRSYNPEQIMLSAAVRRSSRD 320

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1333697150 546 VSIMKEKLIFSEISDGMEVSDELSVCSDNSY 576
Cdd:cd08608   321 VNIMKEKLIFSEINNGVETTDELSLCSDNGY 351
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 227-477 8.62e-159

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: 454.84  E-value: 8.62e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 227 KPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPELARRPAAMLNWTVLQ 306
Cdd:cd08574     1 KPALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVADVFPERAHERASMFTWTDLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 307 RLNAGQWFLKTDPFWTASSLSPSDHREAQNQSICSLAELLELVK-GNATLLLNLRDPPREHPYRGTFLNFTLEALLRSGI 385
Cdd:cd08574    81 QLNAGQWFLKDDPFWTASSLSESDREEAGNQSIPSLAELLRLAKkHNKSVIFDLRRPPPNHPYYQSYVNITLDTILASGI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 386 PQHQVMWLPNRQRPLVRKVAPGFQQTSGSKEAAASLRRGHIQWLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLFSLL 465
Cdd:cd08574   161 PQHQVFWLPDEYRALVRKVAPGFQQVSGRKLPVESLRENGISRLNLEYSQLSAQEIREYSKANISVNLYVVNEPWLYSLL 240

                         250
                  ....*....|..
gi 1333697150 466 WCAGVPSVTSDN 477
Cdd:cd08574   241 WCSGVQSVTTNA 252
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 206-517 4.00e-127

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: 376.52  E-value: 4.00e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 206 LYLAPLSISSPCIMEKKDLGPKPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNV 285
Cdd:cd08610     1 LYLIPLGIYSPCIREKETLGPKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 286 EELFPELARRPAAMLNWTVLQRLNAGQWFLKTDPFWTASSLSPSDHREAQNQSICSLAELLELV-KGNATLLLNLRDPPR 364
Cdd:cd08610    81 GEVQPESACENPAFFNWDFLSTLNAGKWFVKPRPFYNMKPLSEADKERARNQSIPKLSNFLRLAeKENKLVIFDLYRPPP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 365 EHPYRGTFLNFTLEALL-RSGIPQHQVMWLPNRQRPLVRKVAPGFQQTSGSKEAAASLRRGHIQWLNLRYTQVSHQELRD 443
Cdd:cd08610   161 KHPYRHTWIRRVLEVILnEVGIEQHLVLWLPAHDRQYVQSVAPGFKQHVGRKVPIETLLKNNISILNLAYKKLFSNDIRD 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333697150 444 YASWNLSVNLYTVNAPWLFSLLWCAGVPSVTSDNSHTLSQVSSPLWIMPPDEYCLMWVTADLVSFTLIVGIFVL 517
Cdd:cd08610   241 YKAANIHTNVYVINEPWLFSLAWCSGIHSVTTNNIHLLKQLDHPHFFMTPKFYVFMWLLADIISVLFIVLIFCF 314
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 202-518 5.84e-123

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: 365.79  E-value: 5.84e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 202 VVFALYLAPLSISSPCIMEKKDLGPKPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRR 281
Cdd:cd08609     1 VSAAVYLAPLAICSPCIMEENNLPPKPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 282 TTNVEELFPELARRPAAMLNWTVLQRLNAGQWFLKTDPFWTASSLSPSDHREAQNQSICSLAELLELVKG-NATLLLNLR 360
Cdd:cd08609    81 TTNVKDVFPGRDAAGSNNFTWTELKTLNAGSWFLERRPFWTLSSLSEEDRREADNQTVPSLSELLDLAKKhNVSIMFDLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 361 DPPREHPYRGTFLNFTLEALLRSGIPQHQVMWLPNRQRPLVRKVAPGFQQTSGSKEAaasLRRGHIQWLNLRYTQVSHQE 440
Cdd:cd08609   161 NENNSHVFYSSFVFYTLETILKLGIPPDKVWWLPDEYRHDVMKMEPGFKQVYGRQKE---MLMDGGNFMNLPYQDLSALE 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333697150 441 LRDYASWNLSVNLYTVNAPWLFSLLWCAGVPSVTSDNSHTLSQVSSPLWIMPPDEYCLMWVTADLVSFTLIVGIFVLQ 518
Cdd:cd08609   238 IKELRKDNVSVNLWVVNEPWLFSLLWCSGVSSVTTNACQLLKDMSKPIWLLEPNTYLGIWIATDCVSLLLMLWLFLLQ 315
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
226-484 3.91e-35

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 132.69  E-value: 3.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 226 PKPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVeelfpelaRRPAAMLNWTVL 305
Cdd:COG0584     1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNG--------TGRVADLTLAEL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 306 QRLNAGqwflktdpfwtasslspsDHREAQNQSICSLAELLELVKGNATLLLNLRDPPREHPyrgTFLNFTLEALLRSGI 385
Cdd:COG0584    73 RQLDAG------------------SGPDFAGERIPTLEEVLELVPGDVGLNIEIKSPPAAEP---DLAEAVAALLKRYGL 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 386 pQHQVM----WLPNRQRplVRKVAPGFQ----QTSGSKEAAASLRRGHIQWLNLRYTQVSHQELRDYASWNLSVNLYTVN 457
Cdd:COG0584   132 -EDRVIvssfDPEALRR--LRELAPDVPlgllVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVN 208

                         250       260
                  ....*....|....*....|....*..
gi 1333697150 458 APWLFSLLWCAGVPSVTSDNSHTLSQV 484
Cdd:COG0584   209 DPEEMRRLLDLGVDGIITDRPDLLRAV 235
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 230-477 4.98e-24

Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic glycerophosphodiester phosphodiesterase UgpQ and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Escherichia coli cytosolic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46), UgpQ, and similar proteins. GP-GDE plays an essential role in the metabolic pathway of E. coli. It catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols, which are major sources of carbon and phosphate. E. coli possesses two major G3P uptake systems: Glp and Ugp, which contain genes coding for two distinct GP-GDEs. UgpQ gene from the E. coli ugp operon codes for a cytosolic phosphodiesterase GlpQ, which is the prototype of this family. Various glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), can only be hydrolyzed by UgpQ during transport at the inner side of the cytoplasmic membrane to alcohols and G3P, which is a source of phosphate. In contrast to Ca2+-dependent periplasmic phosphodiesterase GlpQ, cytosolic phosphodiesterase UgpQ requires divalent cations, such as Mg2+, Co2+, or Mn2+, for its enzyme activity.


Pssm-ID: 176505 [Multi-domain]  Cd Length: 229  Bit Score: 100.76  E-value: 4.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 230 LIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNveelfpelARRPAAMLNWTVLQRLN 309
Cdd:cd08562     1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTN--------GSGAVTELTWAELAQLD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 310 AGQWFlktdpfwtasslSPsdhrEAQNQSICSLAELLELVKGNAtLLLNLrdpprE-HPYRGTflnftlEALLRSGIPQH 388
Cdd:cd08562    73 AGSWF------------SP----EFAGEPIPTLADVLELARELG-LGLNL-----EiKPDPGD------EALTARVVAAA 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 389 -QVMWlPNRQRPLV-----------RKVAPGFQQ-------TSGSKEAAASLRrghIQWLNLRYTQVSHQELRDYASWNL 449
Cdd:cd08562   125 lRELW-PHASKLLLssfslealraaRRAAPELPLgllfdtlPADWLELLAALG---AVSIHLNYRGLTEEQVKALKDAGY 200

                         250       260
                  ....*....|....*....|....*...
gi 1333697150 450 SVNLYTVNAPWLFSLLWCAGVPSVTSDN 477
Cdd:cd08562   201 KLLVYTVNDPARAAELLEWGVDAIFTDR 228
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 230-477 3.44e-21

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: 91.56  E-value: 3.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 230 LIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDatlrrttnveelfpelarrpaamlnwtvlqrln 309
Cdd:cd08556     1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 310 agqwflktdpfwtasslspsdhreaqnqsICSLAELLELVKGNATLLLNLRDPPREHpyrgTFLNFTLEALLRSGIPQ-- 387
Cdd:cd08556    48 -----------------------------IPTLEEVLELVKGGVGLNIELKEPTRYP----GLEAKVAELLREYGLEErv 94

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 388 ------HQVMWLPNRQRPLVRK---VAPGFQQTSGSKEAaaslRRGHIQWLNLRYTQVSHQELRDYASWNLSVNLYTVNA 458
Cdd:cd08556    95 vvssfdHEALRALKELDPEVPTgllVDKPPLDPLLAELA----RALGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVND 170

                         250
                  ....*....|....*....
gi 1333697150 459 PWLFSLLWCAGVPSVTSDN 477
Cdd:cd08556   171 PEDARRLLALGVDGIITDD 189
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 228-358 8.08e-21

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: 93.11  E-value: 8.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 228 PALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPELARrpaAMLNWTV--- 304
Cdd:cd08559     1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVAEHFPFRGR---KDTGYFVidf 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333697150 305 ----LQRLNAGQWFLKTDPFwtasslspSDHREAQNQSICSLAELLELVKGNATLLLN 358
Cdd:cd08559    78 tlaeLKTLRAGSWFNQRYPE--------RAPSYYGGFKIPTLEEVIELAQGLNKSTGR 127
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 228-362 6.65e-18

Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46) from Staphylococcus aureus, Bacillus subtilis and similar proteins. Members in this family show very high sequence similarity to Escherichia coli periplasmic phosphodiesterase GlpQ, which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176543 [Multi-domain]  Cd Length: 256  Bit Score: 83.91  E-value: 6.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 228 PALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEelfpelARRPAAMLNWTVLQR 307
Cdd:cd08601     1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIE------RPGPVKDYTLAEIKQ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333697150 308 LNAGQWFLKTDPFWTASSLSpsdhreaqNQSICSLAELLELVKGNATLLLNLRDP 362
Cdd:cd08601    75 LDAGSWFNKAYPEYARESYS--------GLKVPTLEEVIERYGGRANYYIETKSP 121
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 230-476 7.74e-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: 176524 [Multi-domain]  Cd Length: 233  Bit Score: 83.13  E-value: 7.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 230 LIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVeelfpelaRRPAAMLNWTVLQRLN 309
Cdd:cd08582     1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGG--------DGAVSDLTLAELRKLD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 310 AGQWflktdpfwtasslspsDHREAQNQSICSLAELLELV-KGNATLLLNLRDPPREHPyrgtFLNFTLEALLRSGIPQH 388
Cdd:cd08582    73 IGSW----------------KGESYKGEKVPTLEEYLAIVpKYGKKLFIEIKHPRRGPE----AEEELLKLLKESGLLPE 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 389 QVMWLPNRQRPL--VRKVAPGFQ-----QTSGSKEAAASLRRGHIQW-LNLRYTQVSHQE----LRDYAswnLSVNLYTV 456
Cdd:cd08582   133 QIVIISFDAEALkrVRELAPTLEtlwlrNYKSPKEDPRPLAKSGGAAgLDLSYEKKLNPAfikaLRDAG---LKLNVWTV 209

                         250       260
                  ....*....|....*....|....
gi 1333697150 457 N----APWLFSLlwcaGVPSVTSD 476
Cdd:cd08582   210 DdaedAKRLIEL----GVDSITTN 229
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 230-476 2.19e-17

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: 81.45  E-value: 2.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 230 LIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPELarrpaamlnwTV--LQR 307
Cdd:cd08563     3 IFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDL----------TLeeLKK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 308 LNAGQWFlktdpfwtasslspsdHREAQNQSICSLAELLELVKGNaTLLLNLRDPPREHPYRGtflnftLEALLRSGIPQ 387
Cdd:cd08563    73 LDAGSWF----------------DEKFTGEKIPTLEEVLDLLKDK-DLLLNIEIKTDVIHYPG------IEKKVLELVKE 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 388 HQvmwLPNR-----------QRplVRKVAP----GFQQTSGSKEAAASLRRGHIQWLNLRYTQVSHQELRDYASWNLSVN 452
Cdd:cd08563   130 YN---LEDRvifssfnheslKR--LKKLDPkiklALLYETGLQDPKDYAKKIGADSLHPDFKLLTEEVVEELKKRGIPVR 204

                         250       260
                  ....*....|....*....|....
gi 1333697150 453 LYTVNAPWLFSLLWCAGVPSVTSD 476
Cdd:cd08563   205 LWTVNEEEDMKRLKDLGVDGIITN 228
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 226-314 2.26e-16

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 79.21  E-value: 2.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 226 PKPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNveelfpelARRPAAMLNWTVL 305
Cdd:PRK09454    6 PYPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSN--------GWGVAGELTWQDL 77


                  ....*....
gi 1333697150 306 QRLNAGQWF 314
Cdd:PRK09454   78 AQLDAGSWF 86
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 231-347 1.53e-15

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: 76.53  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 231 IGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNveelfpelARRPAAMLNWTVLQRLNA 310
Cdd:cd08561     2 IAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTD--------GTGPVADLTLAELRRLDA 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1333697150 311 GQWFlKTDPFWTASslspsdhREAQNQSICSLAELLE 347
Cdd:cd08561    74 GYHF-TDDGGRTYP-------YRGQGIRIPTLEELFE 102
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 233-316 4.91e-15

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: 75.13  E-value: 4.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 233 HRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVeelfpelaRRPAAMLNWTVLQRLNAGQ 312
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDG--------AGYVRDLTLEELKRLDIGA 72


                  ....
gi 1333697150 313 WFLK 316
Cdd:pfam03009  73 GNSG 76
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 230-311 6.61e-15

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: 74.99  E-value: 6.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 230 LIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPElarrpaamLNWTVLQRLN 309
Cdd:cd08573     1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAE--------LTWEELRKLN 72


                  ..
gi 1333697150 310 AG 311
Cdd:cd08573    73 AA 74
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 230-369 1.17e-14

Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (AtGDE, EC 3.1.4.46) and its uncharacterized eukaryotic homolgoues. Members in this family shows high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. AtGDE exists as a hexamer that is a trimer of dimers, which is unique among current known GDPD family members. However, it remains unclear if the hexamer plays a physiological role in AtGDE enzymatic function.


Pssm-ID: 176509 [Multi-domain]  Cd Length: 240  Bit Score: 73.88  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 230 LIGHRGAPM-LAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPElarrpaamLNWTVLQRL 308
Cdd:cd08566     2 VVAHRGGWGaGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSD--------LTLAEIRKL 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333697150 309 NAGQWFlktdpfwtasslspsdhREAQNQSICSLAELLELVKGNATLLLNLRDPPREHPYR 369
Cdd:cd08566    74 RLKDGD-----------------GEVTDEKVPTLEEALAWAKGKILLNLDLKDADLDEVIA 117
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 230-327 9.08e-14

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: 70.82  E-value: 9.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 230 LIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPELARRPAAMLnwtvlqRLN 309
Cdd:cd08581     1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSL------RVA 74

                          90
                  ....*....|....*...
gi 1333697150 310 AGQWFLKTDPFWTASSLS 327
Cdd:cd08581    75 EPARFGSRFAGEPLPSLA 92
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 231-295 2.44e-12

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: 68.19  E-value: 2.44e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333697150 231 IGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPELARR 295
Cdd:cd08600     4 IAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKRK 68
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 228-476 3.08e-12

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: 66.95  E-value: 3.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 228 PALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTT--NVEELFPELARRPAAMLNWTVL 305
Cdd:cd08567     1 FDLQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDItrDPDGAWLPYEGPALYELTLAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 306 QRLNAGQwflkTDPFWTASSLSPsDHREAQNQSICSLAELLELVK--GNATLLLNLR-----DPPREHPYRGTFLNFTLE 378
Cdd:cd08567    81 KQLDVGE----KRPGSDYAKLFP-EQIPVPGTRIPTLEEVFALVEkyGNQKVRFNIEtksdpDRDILHPPPEEFVDAVLA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 379 ALLRSGIPQ--------HQVMWLPNRQRPLVRKVAPGFQQTSGS-KEAAASLrRGHIQW-----LNLRYTQVSHQElrdy 444
Cdd:cd08567   156 VIRKAGLEDrvvlqsfdWRTLQEVRRLAPDIPTVALTEETTLGNlPRAAKKL-GADIWSpyftlVTKELVDEAHAL---- 230

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1333697150 445 aswNLSVNLYTVNAPWLFSLLWCAGVPSVTSD 476
Cdd:cd08567   231 ---GLKVVPWTVNDPEDMARLIDLGVDGIITD 259
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 228-347 8.84e-12

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: 65.70  E-value: 8.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 228 PALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPElarrpaamLNWTVLQR 307
Cdd:cd08575     1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSD--------LTYAELPP 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1333697150 308 LNAGqWFLKTDPFWTASslspsdHREAQNQSICSLAELLE 347
Cdd:cd08575    73 LDAG-YGYTFDGGKTGY------PRGGGDGRIPTLEEVFK 105
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 230-286 3.68e-11

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: 63.09  E-value: 3.68e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333697150 230 LIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVE 286
Cdd:cd08568     2 ILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVD 58
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 231-371 1.74e-10

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


Pssm-ID: 176508 [Multi-domain]  Cd Length: 235  Bit Score: 61.27  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 231 IGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPELarrpaamlnwtvlqrlna 310
Cdd:cd08565     2 AGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDL------------------ 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333697150 311 gqwflktdpfwTASSLSPSDHREAQNQSICSLAELLELVKGNATLL-LNLRDPPREHPYRGT 371
Cdd:cd08565    64 -----------TLAERKALRLRDSFGEKIPTLEEVLALFAPSGLELhVEIKTDADGTPYPGA 114
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 228-295 2.32e-10

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: 61.93  E-value: 2.32e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333697150 228 PALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELfPELARR 295
Cdd:cd08602     1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVADH-PEFADR 67
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 211-294 4.40e-10

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 61.61  E-value: 4.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 211 LSISSPCIMEKKDLGPKPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFP 290
Cdd:PRK11143   10 LAALLAGSAAAAADSAEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDQLVVLHDHYLDRVTDVAERFP 89


                  ....
gi 1333697150 291 ELAR 294
Cdd:PRK11143   90 DRAR 93
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 231-476 1.07e-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: 59.16  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 231 IGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPELArrpaamlNWTVLQRlna 310
Cdd:cd08570     2 IGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDS-------TWDELSH--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 311 gqwfLKTdpfwtasslspsdhREAQNQSICSLAELLELVK--GNATLLLNL---RDPPREHpyrgtfLNFTLEALLRSGI 385
Cdd:cd08570    72 ----LRT--------------IEEPHQPMPTLKDVLEWLVehELPDVKLMLdikRDNDPEI------LFKLIAEMLAVKP 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 386 P----QHQVM---WLPNRQRPLVRkVAPGFQQT--SGSKEAAAslrrgHIQWLNLRYTQVS----------HQELRDYA- 445
Cdd:cd08570   128 DldfwRERIIlglWHLDFLKYGKE-VLPGFPVFhiGFSLDYAR-----HFLNYSEKLVGISmhfvslwgpfGQAFLPELk 201

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1333697150 446 SWNLSVNLYTVNAPWLFSLLWCAGVPSVTSD 476
Cdd:cd08570   202 KNGKKVFVWTVNTEEDMRYAIRLGVDGVITD 232
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 228-318 6.04e-09

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: 57.34  E-value: 6.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 228 PALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEElfpelarrPAAMLNWTVLQR 307
Cdd:cd08580     1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSG--------AVSAYTAAQLAT 72

                          90
                  ....*....|.
gi 1333697150 308 LNAGqWFLKTD 318
Cdd:cd08580    73 LNAG-YNFKPE 82
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 231-365 1.08e-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: 53.10  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 231 IGHRG---APMLAPEHTLMSFRKALEqKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPELarrPAAMLnwtvlqr 307
Cdd:cd08585     7 IAHRGlhdRDAGIPENSLSAFRAAAE-AGYGIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEEL---TAAEL------- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333697150 308 lnagqwflktdpfwTASSLSPSDHReaqnqsICSLAELLELVKGNATLLLNLRDPPRE 365
Cdd:cd08585    76 --------------RALRLLGTDEH------IPTLDEVLELVAGRVPLLIELKSCGGG 113
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 231-324 4.79e-06

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: 47.43  E-value: 4.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 231 IGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNV------EELFpELARRPAAMLNWTV 304
Cdd:cd08555     2 LSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGilpptlEEVL-ELIADYLKNPDYTI 80

                          90       100
                  ....*....|....*....|
gi 1333697150 305 LQRLNagqwfLKTDPFWTAS 324
Cdd:cd08555    81 ILSLE-----IKQDSPEYDE 95
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 231-293 1.24e-05

Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic phosphodiesterase (GlpQ) include uncharacterized proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and their hypothetical homologs. Members in this subfamily show high sequence similarity to Escherichia coli periplasmic phosphodiesterase GlpQ, which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176503  Cd Length: 356  Bit Score: 47.80  E-value: 1.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333697150 231 IGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDAT-LRRTTNVeELFPELA 293
Cdd:cd08560    20 IGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSQCdLHTTTNI-LAIPELA 82
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 226-275 5.09e-05

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: 45.16  E-value: 5.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333697150 226 PKPALIGHRGA--PMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMH 275
Cdd:cd08564     2 VRPIIVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFH 53
GDPD_SHV3_repeat_2 cd08604
Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester ...
 228-353 6.00e-04

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


Pssm-ID: 176546  Cd Length: 300  Bit Score: 42.32  E-value: 6.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 228 PALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNV-EELF-------PELARRPAAM 299
Cdd:cd08604     1 PLIISHNGASGDYPGCTDLAYQKAVKDGADVIDCSVQMSKDGVPFCLDSINLINSTTVaTSKFsnrattvPEIGSTSGIF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333697150 300 ---LNWTVLQRLNAgqwfLKTDPfWTASSLSpSDHREAQNQSICSLAELLELVKGNA 353
Cdd:cd08604    81 tfdLTWSEIQTLKP----AISNP-YSVTGLF-RNPANKNAGKFLTLSDFLDLAKNKS 131
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 229-347 6.20e-04

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: 42.27  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 229 ALIGHRGAPM--------LAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPELARRPAAM- 299
Cdd:cd08572     1 LVIGHRGLGKnyasgslaGIRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTISVSEKSKTGSDEGELIEVPIh 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333697150 300 -LNWTVLQRLNAGQWFLKTDPFWTASSLSPSDHREAQ--NQSICSLAELLE 347
Cdd:cd08572    81 dLTLEQLKELGLQHISALKRKALTRKAKGPKPNPWGMdeHDPFPTLQEVLE 131
GDPD_SHV3_plant cd08571
Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like ...
 228-367 1.21e-03

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


Pssm-ID: 176513  Cd Length: 302  Bit Score: 41.12  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333697150 228 PALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADVTISLDGVPFLMHDATLRRTTNVEELFPELARRPAAM-------- 299
Cdd:cd08571     1 PLVIARGGASGDYPDSTDLAYQKAISDGADVLDCDVQLTKDGVPICLPSINLDNSTTIASVFPKRKKTYVVEgqstsgif 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333697150 300 ---LNWTVLQRLNAgqwfLKTDPFwtasSLSPSDHREAQNQSICSLAELLELVKGNAT--LLLNLRDPP--REHP 367
Cdd:cd08571    81 sfdLTWAEIQTLKP----IISNPF----SVLFRNPRNDNAGKILTLEDFLTLAKPKSLsgVWINVENAAflAEHK 147
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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