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Conserved domains on  [gi|344196589|gb|ACA63311|]
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putative glycerophosphoryl diester phosphodiesterase [Lactobacillus phage c5]

Protein Classification

glycerophosphodiester phosphodiesterase( domain architecture ID 11426576)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
376-611 3.35e-47

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


:

Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 168.12  E-value: 3.35e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 376 LPIAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGTEltqpvKIGERMLVELNAY 455
Cdd:COG0584    4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLD---RTTNGTG-----RVADLTLAELRQL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 456 DYGiyKSEIFKGLNICTFEDIIKFARRtGATVHAELKQQYTDEQ--CQVLLDIVSKYRMANKVGWQAFDHSSLGYIASHD 533
Cdd:COG0584   76 DAG--SGPDFAGERIPTLEEVLELVPG-DVGLNIEIKSPPAAEPdlAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 534 ENAQLELLAGSITDDLIAEGkKRLNgkrkvVLSVG---QGVTQRLVDQAHSEGFDVYVWTVDDIDGAKKLINMGVDGIMT 610
Cdd:COG0584  153 PDVPLGLLVEELPADPLELA-RALG-----ADGVGpdyDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIIT 226


                 .
gi 344196589 611 N 611
Cdd:COG0584  227 D 227
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
376-611 3.35e-47

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 168.12  E-value: 3.35e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 376 LPIAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGTEltqpvKIGERMLVELNAY 455
Cdd:COG0584    4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLD---RTTNGTG-----RVADLTLAELRQL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 456 DYGiyKSEIFKGLNICTFEDIIKFARRtGATVHAELKQQYTDEQ--CQVLLDIVSKYRMANKVGWQAFDHSSLGYIASHD 533
Cdd:COG0584   76 DAG--SGPDFAGERIPTLEEVLELVPG-DVGLNIEIKSPPAAEPdlAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 534 ENAQLELLAGSITDDLIAEGkKRLNgkrkvVLSVG---QGVTQRLVDQAHSEGFDVYVWTVDDIDGAKKLINMGVDGIMT 610
Cdd:COG0584  153 PDVPLGLLVEELPADPLELA-RALG-----ADGVGpdyDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIIT 226


                 .
gi 344196589 611 N 611
Cdd:COG0584  227 D 227
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 378-611 7.35e-38

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: 140.09  E-value: 7.35e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDatinsiarnsdgteltqpvkigermlvelnaydy 457
Cdd:cd08556    2 IAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD---------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 458 giykseifkglnICTFEDIIKFARRtGATVHAELKQ-QYTDEQCQVLLDIVSKYRMANKVGWQAFDHSSLGYIASHDENA 536
Cdd:cd08556   48 ------------IPTLEEVLELVKG-GVGLNIELKEpTRYPGLEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEV 114

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 344196589 537 QLELLAGSITDDLIAEGKKRLNGKRKVVLSVgQGVTQRLVDQAHSEGFDVYVWTVDDIDGAKKLINMGVDGIMTN 611
Cdd:cd08556  115 PTGLLVDKPPLDPLLAELARALGADAVNPHY-KLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITD 188
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 380-616 2.53e-26

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: 108.64  E-value: 2.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589  380 HRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGteltqPVKIGERMLVELNAYDYGI 459
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLD---RTTDG-----AGYVRDLTLEELKRLDIGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589  460 YKSEIFKG--LNICTFEDIIKFARRTGATVHAELKQ----------QYTDEQCQVLLDIVSKYRMANKVGWQAFDHSSLG 527
Cdd:pfam03009  73 GNSGPLSGerVPFPTLEEVLEFDWDVGFNIEIKIKPyveaiapeegLIVKDLLLSVDEILAKKADPRRVIFSSFNPDELK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589  528 YIasHDENAQLELLAGSITDDLIAEGKKRLNGKR---KVVLSVG---QGVTQRLVDQAHSEGFDVYVWTVDDIDGAKKLI 601
Cdd:pfam03009 153 RL--RELAPKLPLVFLSSGRAYAEADLLERAAAFagaPALLGEValvDEALPDLVKRAHARGLVVHVWTVNNEDEMKRLL 230

                         250
                  ....*....|....*
gi 344196589  602 NMGVDGIMTNgHIDL 616
Cdd:pfam03009 231 ELGVDGVITD-RPDT 244
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 378-616 4.38e-17

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 81.91  E-value: 4.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGTEltqpvKIGERMLVELNAYDY 457
Cdd:PRK09454  11 VAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLE---RTSNGWG-----VAGELTWQDLAQLDA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 458 GIYKSEIFKGLNICTFEDI--------------IK----FARRTGATVHAELKQQYTDEQCQVLLdivskyrmankvgwQ 519
Cdd:PRK09454  83 GSWFSAAFAGEPLPTLSQVaarcrahgmaanieIKpttgREAETGRVVALAARALWAGAAVPPLL--------------S 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 520 AFDHSSLGyiASHDenAQLELLAGSITDDLIAEGKKRLNGKRKVVLSVGQ-GVTQRLVDQAHSEGFDVYVWTVDDIDGAK 598
Cdd:PRK09454 149 SFSEDALE--AARQ--AAPELPRGLLLDEWPDDWLELTRRLGCVSLHLNHkLLDEARVAALKAAGLRILVYTVNDPARAR 224

                        250
                 ....*....|....*...
gi 344196589 599 KLINMGVDGIMTNgHIDL 616
Cdd:PRK09454 225 ELLRWGVDCICTD-RIDL 241
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
376-611 3.35e-47

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 168.12  E-value: 3.35e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 376 LPIAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGTEltqpvKIGERMLVELNAY 455
Cdd:COG0584    4 LIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLD---RTTNGTG-----RVADLTLAELRQL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 456 DYGiyKSEIFKGLNICTFEDIIKFARRtGATVHAELKQQYTDEQ--CQVLLDIVSKYRMANKVGWQAFDHSSLGYIASHD 533
Cdd:COG0584   76 DAG--SGPDFAGERIPTLEEVLELVPG-DVGLNIEIKSPPAAEPdlAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 534 ENAQLELLAGSITDDLIAEGkKRLNgkrkvVLSVG---QGVTQRLVDQAHSEGFDVYVWTVDDIDGAKKLINMGVDGIMT 610
Cdd:COG0584  153 PDVPLGLLVEELPADPLELA-RALG-----ADGVGpdyDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIIT 226


                 .
gi 344196589 611 N 611
Cdd:COG0584  227 D 227
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 378-611 7.35e-38

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: 140.09  E-value: 7.35e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDatinsiarnsdgteltqpvkigermlvelnaydy 457
Cdd:cd08556    2 IAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD---------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 458 giykseifkglnICTFEDIIKFARRtGATVHAELKQ-QYTDEQCQVLLDIVSKYRMANKVGWQAFDHSSLGYIASHDENA 536
Cdd:cd08556   48 ------------IPTLEEVLELVKG-GVGLNIELKEpTRYPGLEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEV 114

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 344196589 537 QLELLAGSITDDLIAEGKKRLNGKRKVVLSVgQGVTQRLVDQAHSEGFDVYVWTVDDIDGAKKLINMGVDGIMTN 611
Cdd:cd08556  115 PTGLLVDKPPLDPLLAELARALGADAVNPHY-KLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITD 188
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 378-611 8.10e-33

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: 127.05  E-value: 8.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINSIArNSDGteltqpvKIGERMLVELNAYDY 457
Cdd:cd08582    2 IAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTS-GGDG-------AVSDLTLAELRKLDI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 458 GIYKSEIFKGLNICTFEDIIKFARRTGATVHAELKQ-QYTDEQCQVLLDIVSKYR-MANKVGWQAFDHSSLGYIASHDEN 535
Cdd:cd08582   74 GSWKGESYKGEKVPTLEEYLAIVPKYGKKLFIEIKHpRRGPEAEEELLKLLKESGlLPEQIVIISFDAEALKRVRELAPT 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 344196589 536 AQLELLAGSITDDLIAEGKKRLNGKRKVVLSVGQGVTQRLVDQAHSEGFDVYVWTVDDIDGAKKLINMGVDGIMTN 611
Cdd:cd08582  154 LETLWLRNYKSPKEDPRPLAKSGGAAGLDLSYEKKLNPAFIKALRDAGLKLNVWTVDDAEDAKRLIELGVDSITTN 229
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 378-611 4.65e-30

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: 118.81  E-value: 4.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGTELtqpvkIGERMLVELNAYDY 457
Cdd:cd08563    4 FAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVD---RTTNGKGY-----VKDLTLEELKKLDA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 458 GIYKSEIFKGLNICTFEDIIKFARRTGATVHAELKQQYTD----EqcQVLLDIVSKYRMANKVGWQAFDHSSLGYIASHD 533
Cdd:cd08563   76 GSWFDEKFTGEKIPTLEEVLDLLKDKDLLLNIEIKTDVIHypgiE--KKVLELVKEYNLEDRVIFSSFNHESLKRLKKLD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 534 ENAQLELLAGSITDDLIAEGKKR----LNGKRKVvlsvgqgVTQRLVDQAHSEGFDVYVWTVDDIDGAKKLINMGVDGIM 609
Cdd:cd08563  154 PKIKLALLYETGLQDPKDYAKKIgadsLHPDFKL-------LTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGII 226


                 ..
gi 344196589 610 TN 611
Cdd:cd08563  227 TN 228
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 378-620 1.05e-29

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: 118.51  E-value: 1.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGTEltqpvKIGERMLVELNAYDY 457
Cdd:cd08561    2 IAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLD---RTTDGTG-----PVADLTLAELRRLDA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 458 G----IYKSEIF----KGLNICTFEDIikFARRTGATVHAELKQQYTDEQcQVLLDIVSKYRMANKVGWQAFDHSSLGYI 529
Cdd:cd08561   74 GyhftDDGGRTYpyrgQGIRIPTLEEL--FEAFPDVRLNIEIKDDGPAAA-AALADLIERYGAQDRVLVASFSDRVLRRF 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 530 ----------ASHDENAQLELLAGSITDDLIAegkkrlNGKRKVVLSVGQG----VTQRLVDQAHSEGFDVYVWTVDDID 595
Cdd:cd08561  151 rrlcprvatsAGEGEVAAFVLASRLGLGSLYS------PPYDALQIPVRYGgvplVTPRFVRAAHAAGLEVHVWTVNDPA 224

                        250       260
                 ....*....|....*....|....*
gi 344196589 596 GAKKLINMGVDGIMTnghiDLPNLL 620
Cdd:cd08561  225 EMRRLLDLGVDGIIT----DRPDLL 245
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 378-610 4.64e-28

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: 113.09  E-value: 4.64e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGTEltqpvKIGERMLVELNAYDY 457
Cdd:cd08562    2 IAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLD---RTTNGSG-----AVTELTWAELAQLDA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 458 GIYKSEIFKGLNICTFEDIIKFARRTGATVHAELK-----QQYTDEQC-QVLLDIVSkyrMANKVGWQAFDHSSLGYIAS 531
Cdd:cd08562   74 GSWFSPEFAGEPIPTLADVLELARELGLGLNLEIKpdpgdEALTARVVaAALRELWP---HASKLLLSSFSLEALRAARR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 532 HDENAQLELLagsiTDDLIAEGKKRLNGKRKVVLSVGQ-GVTQRLVDQAHSEGFDVYVWTVDDIDGAKKLINMGVDGIMT 610
Cdd:cd08562  151 AAPELPLGLL----FDTLPADWLELLAALGAVSIHLNYrGLTEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFT 226
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 378-619 4.83e-27

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: 111.25  E-value: 4.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATIN-SIARNSDGTELT-QPVKIGERMLVELNAY 455
Cdd:cd08567    4 QGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNpDITRDPDGAWLPyEGPALYELTLAEIKQL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 456 DYG----------IYKSEIF-KGLNICTFEDIIKFARRTGAT---VHAELK-----QQYT---DEQCQVLLDIVSKYRMA 513
Cdd:cd08567   84 DVGekrpgsdyakLFPEQIPvPGTRIPTLEEVFALVEKYGNQkvrFNIETKsdpdrDILHpppEEFVDAVLAVIRKAGLE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 514 NKVGWQAFDHSSLGYIASHDENAQLELLAGSITDDLIAEGKKRLNGkrKVVLSVGQGVTQRLVDQAHSEGFDVYVWTVDD 593
Cdd:cd08567  164 DRVVLQSFDWRTLQEVRRLAPDIPTVALTEETTLGNLPRAAKKLGA--DIWSPYFTLVTKELVDEAHALGLKVVPWTVND 241

                        250       260
                 ....*....|....*....|....*.
gi 344196589 594 IDGAKKLINMGVDGIMTnghiDLPNL 619
Cdd:cd08567  242 PEDMARLIDLGVDGIIT----DYPDL 263
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 380-616 2.53e-26

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: 108.64  E-value: 2.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589  380 HRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGteltqPVKIGERMLVELNAYDYGI 459
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLD---RTTDG-----AGYVRDLTLEELKRLDIGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589  460 YKSEIFKG--LNICTFEDIIKFARRTGATVHAELKQ----------QYTDEQCQVLLDIVSKYRMANKVGWQAFDHSSLG 527
Cdd:pfam03009  73 GNSGPLSGerVPFPTLEEVLEFDWDVGFNIEIKIKPyveaiapeegLIVKDLLLSVDEILAKKADPRRVIFSSFNPDELK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589  528 YIasHDENAQLELLAGSITDDLIAEGKKRLNGKR---KVVLSVG---QGVTQRLVDQAHSEGFDVYVWTVDDIDGAKKLI 601
Cdd:pfam03009 153 RL--RELAPKLPLVFLSSGRAYAEADLLERAAAFagaPALLGEValvDEALPDLVKRAHARGLVVHVWTVNNEDEMKRLL 230

                         250
                  ....*....|....*
gi 344196589  602 NMGVDGIMTNgHIDL 616
Cdd:pfam03009 231 ELGVDGVITD-RPDT 244
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 375-622 9.26e-24

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: 101.62  E-value: 9.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 375 ILPIAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGtelTQPVKIGERMLVELNA 454
Cdd:cd08601    1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLD---RTTNI---ERPGPVKDYTLAEIKQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 455 YD--------YGIYKSEIFKGLNICTFEDII-KFARRTGATVHAELKQQYTDEQCQvLLDIVSKYRMAN------KVGWQ 519
Cdd:cd08601   75 LDagswfnkaYPEYARESYSGLKVPTLEEVIeRYGGRANYYIETKSPDLYPGMEEK-LLATLDKYGLLTdnlkngQVIIQ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 520 AFDHSSLGYIASHDENAQLELLAG-----SITDDLIAEGKKRLNGkrkvvlsVG---QGVTQRLVDQAHSEGFDVYVWTV 591
Cdd:cd08601  154 SFSKESLKKLHQLNPNIPLVQLLWygegaETYDKWLDEIKEYAIG-------IGpsiADADPWMVHLIHKKGLLVHPYTV 226

                        250       260       270
                 ....*....|....*....|....*....|.
gi 344196589 592 DDIDGAKKLINMGVDGIMTNghidLPNLLSS 622
Cdd:cd08601  227 NEKADMIRLINWGVDGMFTN----YPDRLKE 253
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 378-611 1.82e-22

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: 98.88  E-value: 1.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGTELTQPVKIGER-------MLV 450
Cdd:cd08559    4 IAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLD---RTTNVAEHFPFRGRKDTgyfvidfTLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 451 ELNAYDYGIYKSEIFK--------GLNICTFEDIIKFAR----RTGATVH--AELK------QQYTD-EqcQVLLDIVSK 509
Cdd:cd08559   81 ELKTLRAGSWFNQRYPerapsyygGFKIPTLEEVIELAQglnkSTGRNVGiyPETKhptfhkQEGPDiE--EKLLEVLKK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 510 YRMANK---VGWQAFDHSSLGYIASHDENAQLELLAG---------------SITDDLIAEGKKRLNG----KRKVV--L 565
Cdd:cd08559  159 YGYTGKndpVFIQSFEPESLKRLRNETPDIPLVQLIDygdwaetdkkytyawLTTDAGLKEIAKYADGigpwKSLIIpeD 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 344196589 566 SVGQGVTQRLVDQAHSEGFDVYVWTVDDID---------GAKKLIN-MGVDGIMTN 611
Cdd:cd08559  239 SNGLLVPTDLVKDAHKAGLLVHPYTFRNENlflapdfkqDMDALYNaAGVDGVFTD 294
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 378-611 3.94e-22

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: 95.69  E-value: 3.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINSIA-RNSDGTELTqpvkigermLVELNAYD 456
Cdd:cd08579    2 IAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAgVNKKVWDLT---------LEELKKLT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 457 YGiyksEIFKGLNICTFEDIIKFARRTGATVHAELK--QQYTDEQCQVLLDIVSKYRMANKVGWQAFDHSSLGYIasHDE 534
Cdd:cd08579   73 IG----ENGHGAKIPSLDEYLALAKGLKQKLLIELKphGHDSPDLVEKFVKLYKQNLIENQHQVHSLDYRVIEKV--KKL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 535 NAQLE---LLAGSITDDliaeGKKRLNGkrkvvLSVGQG-VTQRLVDQAHSEGFDVYVWTVDDIDGAKKLINMGVDGIMT 610
Cdd:cd08579  147 DPKIKtgyILPFNIGNL----PKTNVDF-----YSIEYStLNKEFIRQAHQNGKKVYVWTVNDPDDMQRYLAMGVDGIIT 217


                 .
gi 344196589 611 N 611
Cdd:cd08579  218 D 218
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 378-610 1.16e-17

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: 83.12  E-value: 1.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNS-IAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGTEltqpvKIGERMLVELNAYD 456
Cdd:cd08566    3 VAHRGGWGaGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLD---RTTNGKG-----KVSDLTLAEIRKLR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 457 YGIyKSEIFKGLNICTFEDIIKFARRTgATVHAELKQQYTDEqcqvLLDIVSKYRMANKVGWQAFDHSSLGYIASHDENA 536
Cdd:cd08566   75 LKD-GDGEVTDEKVPTLEEALAWAKGK-ILLNLDLKDADLDE----VIALVKKHGALDQVIFKSYSEEQAKELRALAPEV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 537 QLELLAGSITDDLIAEgKKRLNGKR--KVVLSVGQGVTQRLVDQA-HSEGFDVYVWTVDDIDGAK-------------KL 600
Cdd:cd08566  149 MLMPIVRDAEDLDEEE-ARAIDALNllAFEITFDDLDLPPLFDELlRALGIRVWVNTLGDDDTAGldralsdprevwgEL 227

                        250
                 ....*....|
gi 344196589 601 INMGVDGIMT 610
Cdd:cd08566  228 VDAGVDVIQT 237
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 378-616 4.38e-17

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 81.91  E-value: 4.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGTEltqpvKIGERMLVELNAYDY 457
Cdd:PRK09454  11 VAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLE---RTSNGWG-----VAGELTWQDLAQLDA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 458 GIYKSEIFKGLNICTFEDI--------------IK----FARRTGATVHAELKQQYTDEQCQVLLdivskyrmankvgwQ 519
Cdd:PRK09454  83 GSWFSAAFAGEPLPTLSQVaarcrahgmaanieIKpttgREAETGRVVALAARALWAGAAVPPLL--------------S 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 520 AFDHSSLGyiASHDenAQLELLAGSITDDLIAEGKKRLNGKRKVVLSVGQ-GVTQRLVDQAHSEGFDVYVWTVDDIDGAK 598
Cdd:PRK09454 149 SFSEDALE--AARQ--AAPELPRGLLLDEWPDDWLELTRRLGCVSLHLNHkLLDEARVAALKAAGLRILVYTVNDPARAR 224

                        250
                 ....*....|....*...
gi 344196589 599 KLINMGVDGIMTNgHIDL 616
Cdd:PRK09454 225 ELLRWGVDCICTD-RIDL 241
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 378-610 1.90e-15

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: 78.11  E-value: 1.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINS--------------IARNSDGTELT---- 439
Cdd:cd08602    4 IAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGttdvadhpefadrkTTKTVDGVNVTgwft 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 440 --------QPVKIGERMLVELNAYDyGIYKseifkglnICTFEDIIKFAR----RTGATV--HAELKQQYTDEQC----- 500
Cdd:cd08602   84 edftlaelKTLRARQRLPYRDQSYD-GQFP--------IPTFEEIIALAKaasaATGRTVgiYPEIKHPTYFNAPlglpm 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 501 -QVLLDIVSKYRMANK---VGWQAFDHSSLGYIASHDENAQLELLAGS------------------ITDDLIAEGKKRLN 558
Cdd:cd08602  155 eDKLLETLKKYGYTGKkapVFIQSFEVTNLKYLRNKTDLPLVQLIDDAtippqdtpegdsrtyadlTTDAGLKEIATYAD 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 344196589 559 G----KRKVVLSVGQGVT---QRLVDQAHSEGFDVYVWTV-------------DDIDGAKKLINMGVDGIMT 610
Cdd:cd08602  235 GigpwKDLIIPSDANGRLgtpTDLVEDAHAAGLQVHPYTFrnentflppdffgDPYAEYRAFLDAGVDGLFT 306
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 378-611 2.81e-13

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: 70.05  E-value: 2.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINSIArnsdgtelTQPVKIGERMLVELNAY-- 455
Cdd:cd08581    2 VAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLT--------GVEGLLHELEDAELDSLrv 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 456 DYGIYKSEIFKGLNICTFEDIIK-FARRTGATVHAELKQQYTDE-QCQVLLDIVSK--YRMANKVGWQAFDHSSLGYIAS 531
Cdd:cd08581   74 AEPARFGSRFAGEPLPSLAAVVQwLAQHPQVTLFVEIKTESLDRfGLERVVDKVLRalPAVAAQRVLISFDYDLLALAKQ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 532 HD-----------ENAQLELLAGSITDDLIAEgKKRLNGKRKVvlsvgqgvtqrlvdqaHSEGFDVYVWTVDDIDGAKKL 600
Cdd:cd08581  154 QGgprtgwvlpdwDDASLAEADELQPDYLFCD-KNLLPDTGDL----------------WAGTWKWVIYEVNEPAEALAL 216

                        250
                 ....*....|.
gi 344196589 601 INMGVDGIMTN 611
Cdd:cd08581  217 AARGVALIETD 227
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 378-484 1.10e-12

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: 68.82  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINsiaRNSDGTeltqpVKIGERMLVE---LNA 454
Cdd:cd08573    2 IGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVD---RTTDGT-----GLVAELTWEElrkLNA 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 344196589 455 YDYGIYKSEiFKGLNICTFEDIIKFARRTG 484
Cdd:cd08573   74 AAKHRLSSR-FPGEKIPTLEEAVKECLENN 102
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 377-548 6.86e-12

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: 66.19  E-value: 6.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 377 PIAHRGL---NSIAPEESLEAYSLAVRSGYKdIECDIYFTEDGIPVLHHDATINSIArNSDG--TELTQPvkigermlvE 451
Cdd:cd08585    6 PIAHRGLhdrDAGIPENSLSAFRAAAEAGYG-IELDVQLTADGEVVVFHDDNLKRLT-GVEGrvEELTAA---------E 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 452 LNAYDygiykseiFKGLN--ICTFEDIIKF-ARRtgATVHAELKQQY--TDEQCQVLLDIVSKYRMAnkVGWQAFDHSSL 526
Cdd:cd08585   75 LRALR--------LLGTDehIPTLDEVLELvAGR--VPLLIELKSCGggDGGLERRVLAALKDYKGP--AAIMSFDPRVV 142

                        170       180
                 ....*....|....*....|..
gi 344196589 527 GYIASHDENAQLELLAGSITDD 548
Cdd:cd08585  143 RWFRKLAPGIPRGQLSEGSNDE 164
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 378-516 1.33e-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: 50.79  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINSIArNSDGteltqpvKIGERMLVELNAYDY 457
Cdd:cd08580    4 VAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLT-NGSG-------AVSAYTAAQLATLNA 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 344196589 458 GI---YKSEIF---KGLNICTFEDIIkfaRRTGAT-VHAELKQQYTDEQCQVLLDIVSKYRMANKV 516
Cdd:cd08580   76 GYnfkPEGGYPyrgKPVGIPTLEQVL---RAFPDTpFILDMKSLPADPQAKAVARVLERENAWSRV 138
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 378-611 4.42e-05

Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases; This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues.


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 45.75  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 378 IAHR--GLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATINSIARNSDGTEL-TQPVKIGERMlvelNA 454
Cdd:cd08583    2 IAHAmgGIDGKTYTNSLDAFEHNYKKGYRVFEVDLSLTSDGVLVARHSWDESLLKQLGLPTSKnTKPLSYEEFK----SK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 455 YDYGIYKseifkglnICTFEDIIKFARR---------TGATVHAELKQQYTD------EQCQVLLD--IVSKY--RMANK 515
Cdd:cd08583   78 KIYGKYT--------PMDFKDVIDLLKKypdvyivtdTKQDDDNDIKKLYEYivkeakEVDPDLLDrvIPQIYneEMYEA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 516 V-GWQAFDHSSLGYIASHDENAQlELLAGSITDDL--IAEGKKRLNGKrkvvlsvgqgvtqrLVDQAHSEGFDVYVWTVD 592
Cdd:cd08583  150 ImSIYPFKSVIYTLYRQDSIRLD-EIIAFCYENGIkaVTISKNYVNDK--------------LIEKLNKAGIYVYVYTIN 214

                        250
                 ....*....|....*....
gi 344196589 593 DIDGAKKLINMGVDGIMTN 611
Cdd:cd08583  215 DLKDAQEYKKLGVYGIYTD 233
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 378-446 6.16e-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: 46.26  E-value: 6.16e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHD-----ATINSIARNSDGTELTQPVKIGE 446
Cdd:cd08560   20 IGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSqcdlhTTTNILAIPELAAKCTQPFTPAN 93
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 377-611 2.21e-04

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: 42.81  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 377 PIAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDAT-INSIARNSDgteltqpvkigERMLVELNAY 455
Cdd:cd08555    1 VLSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTlDRTTAGILP-----------PTLEEVLELI 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344196589 456 -DYGIYKSEiFKGLNICTFEDiIKFARRTGATVHAELKQQYTDEqcqvlldivskyrMANKVGWQAFDHSSLGYIASHDE 534
Cdd:cd08555   70 aDYLKNPDY-TIILSLEIKQD-SPEYDEFLAKVLKELRVYFDYD-------------LRGKVVLSSFNALGVDYYNFSSK 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 344196589 535 NAqlellagsitddliaegkkrlngkrkvvlsvgqgVTQRLVDQAHSEGFDVYVWTVDDIDGA-KKLINMGVDGIMTN 611
Cdd:cd08555  135 LI----------------------------------KDTELIASANKLGLLSRIWTVNDNNEIiNKFLNLGVDGLITD 178
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 378-426 4.43e-04

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: 43.32  E-value: 4.43e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATI 426
Cdd:cd08610   26 IGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTL 74
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 378-425 6.18e-04

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: 42.29  E-value: 6.18e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDAT 425
Cdd:cd08574    5 IGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRT 52
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 378-427 7.13e-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: 42.65  E-value: 7.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 344196589 378 IAHRGL-NSIA-------PEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATIN 427
Cdd:cd08572    3 IGHRGLgKNYAsgslagiRENTIASFLAAAKHGADMVEFDVQLTKDGVPVIYHDFTIS 60
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 378-426 1.13e-03

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: 42.14  E-value: 1.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHDATI 426
Cdd:cd08608    5 IGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTL 53
GDPD_2 pfam13653
Glycerophosphoryl diester phosphodiesterase family; This family also includes ...
 586-611 2.48e-03

Glycerophosphoryl diester phosphodiesterase family; This family also includes glycerophosphoryl diester phosphodiesterases as well as 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: 433380 [Multi-domain]  Cd Length: 30  Bit Score: 35.94  E-value: 2.48e-03
                          10        20
                  ....*....|....*....|....*.
gi 344196589  586 VYVWTVDDIDGAKKLINMGVDGIMTN 611
Cdd:pfam13653   2 VRFWTIDNKAAWKELMRLGVDGLNTD 27
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 378-423 6.54e-03

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: 39.52  E-value: 6.54e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 344196589 378 IAHRGLNSIAPEESLEAYSLAVRSGYKDIECDIYFTEDGIPVLHHD 423
Cdd:cd08609   30 VGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHD 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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