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Conserved domains on  [gi|1012713373|ref|WP_062816908|]
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MULTISPECIES: glycerophosphodiester phosphodiesterase family protein [unclassified Alcanivorax]

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

CATH:  3.20.20.190
EC:  3.1.4.-
Gene Ontology:  GO:0008081|GO:0006629|GO:0046872
PubMed:  38491249

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];
1-235 6.19e-19

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


:

Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 82.22  E-value: 6.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   1 MDVIWISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQ-----CLRH 75
Cdd:COG0584     1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAElrqldAGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373  76 RLHDGQPLLTF-EHFAHTFTDQRWILDIKPESAARTLAALRHWADQQQKGdwlcRQARFLLW--HPEHTRLLRQHFPAAI 152
Cdd:COG0584    81 PDFAGERIPTLeEVLELVPGDVGLNIEIKSPPAAEPDLAEAVAALLKRYG----LEDRVIVSsfDPEALRRLRELAPDVP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373 153 TMapqtecrraglsLLMGLRPLAAIRAGRTYSLPPVFHGLPLFRHSLVDAYHRLGGRVLAFLPEGREQQRQALRSGVDEI 232
Cdd:COG0584   157 LG------------LLVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGI 224


                  ...
gi 1012713373 233 LSN 235
Cdd:COG0584   225 ITD 227
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
1-235 6.19e-19

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 82.22  E-value: 6.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   1 MDVIWISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQ-----CLRH 75
Cdd:COG0584     1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAElrqldAGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373  76 RLHDGQPLLTF-EHFAHTFTDQRWILDIKPESAARTLAALRHWADQQQKGdwlcRQARFLLW--HPEHTRLLRQHFPAAI 152
Cdd:COG0584    81 PDFAGERIPTLeEVLELVPGDVGLNIEIKSPPAAEPDLAEAVAALLKRYG----LEDRVIVSsfDPEALRRLRELAPDVP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373 153 TMapqtecrraglsLLMGLRPLAAIRAGRTYSLPPVFHGLPLFRHSLVDAYHRLGGRVLAFLPEGREQQRQALRSGVDEI 232
Cdd:COG0584   157 LG------------LLVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGI 224


                  ...
gi 1012713373 233 LSN 235
Cdd:COG0584   225 ITD 227
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 6-235 6.07e-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: 71.52  E-value: 6.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQCLRHRL-------- 77
Cdd:cd08561     2 IAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAgyhftddg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373  78 -------HDGQPLLTFEHFAHTFTDQRWILDIKPE--SAARTLAAL--RHWAdqqqkgdwlcrQARFLL--WHPEHTRLL 144
Cdd:cd08561    82 grtypyrGQGIRIPTLEELFEAFPDVRLNIEIKDDgpAAAAALADLieRYGA-----------QDRVLVasFSDRVLRRF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373 145 RQHFPAAITMAPQTECRRAGLSLLMGLRPLAAiRAGRTYSLPPVFHGLPLFRHSLVDAYHRLGGRVLAFLPEGREQQRQA 224
Cdd:cd08561   151 RRLCPRVATSAGEGEVAAFVLASRLGLGSLYS-PPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRL 229

                         250
                  ....*....|.
gi 1012713373 225 LRSGVDEILSN 235
Cdd:cd08561   230 LDLGVDGIITD 240
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 8-235 1.07e-06

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: 48.17  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   8 HRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQcLRHR----------L 77
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEE-LKRLdigagnsgplS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373  78 HDGQPLLTFEHFAHTFTDQRWILDIKPESaarTLAALRHWADQQQK-----------GDWLCRQARFLLWHPEHTRLLRQ 146
Cdd:pfam03009  80 GERVPFPTLEEVLEFDWDVGFNIEIKIKP---YVEAIAPEEGLIVKdlllsvdeilaKKADPRRVIFSSFNPDELKRLRE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373 147 HFPaAITMAPQTECRRAGLSLLMGLRPLAAIRAGRTYSLPPVFHGLPlfrhSLVDAYHRLGGRVLAFLPEGREQQRQALR 226
Cdd:pfam03009 157 LAP-KLPLVFLSSGRAYAEADLLERAAAFAGAPALLGEVALVDEALP----DLVKRAHARGLVVHVWTVNNEDEMKRLLE 231


                  ....*....
gi 1012713373 227 SGVDEILSN 235
Cdd:pfam03009 232 LGVDGVITD 240
 
Name Accession Description Interval E-value
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
1-235 6.19e-19

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 82.22  E-value: 6.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   1 MDVIWISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQ-----CLRH 75
Cdd:COG0584     1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAElrqldAGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373  76 RLHDGQPLLTF-EHFAHTFTDQRWILDIKPESAARTLAALRHWADQQQKGdwlcRQARFLLW--HPEHTRLLRQHFPAAI 152
Cdd:COG0584    81 PDFAGERIPTLeEVLELVPGDVGLNIEIKSPPAAEPDLAEAVAALLKRYG----LEDRVIVSsfDPEALRRLRELAPDVP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373 153 TMapqtecrraglsLLMGLRPLAAIRAGRTYSLPPVFHGLPLFRHSLVDAYHRLGGRVLAFLPEGREQQRQALRSGVDEI 232
Cdd:COG0584   157 LG------------LLVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGI 224


                  ...
gi 1012713373 233 LSN 235
Cdd:COG0584   225 ITD 227
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 6-235 6.07e-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: 71.52  E-value: 6.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQCLRHRL-------- 77
Cdd:cd08561     2 IAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLDAgyhftddg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373  78 -------HDGQPLLTFEHFAHTFTDQRWILDIKPE--SAARTLAAL--RHWAdqqqkgdwlcrQARFLL--WHPEHTRLL 144
Cdd:cd08561    82 grtypyrGQGIRIPTLEELFEAFPDVRLNIEIKDDgpAAAAALADLieRYGA-----------QDRVLVasFSDRVLRRF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373 145 RQHFPAAITMAPQTECRRAGLSLLMGLRPLAAiRAGRTYSLPPVFHGLPLFRHSLVDAYHRLGGRVLAFLPEGREQQRQA 224
Cdd:cd08561   151 RRLCPRVATSAGEGEVAAFVLASRLGLGSLYS-PPYDALQIPVRYGGVPLVTPRFVRAAHAAGLEVHVWTVNDPAEMRRL 229

                         250
                  ....*....|.
gi 1012713373 225 LRSGVDEILSN 235
Cdd:cd08561   230 LDLGVDGIITD 240
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 6-189 4.88e-13

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: 66.17  E-value: 4.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   6 ISHRGLH-QRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQCLRHRLHDGQPLL 84
Cdd:cd08566     3 VAHRGGWgAGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKDGDGEV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373  85 TFEHFAhTFTD------QRWI--LDIKPESAARTLAALRHwADQQqkgdwlcRQARFLLWHPEHTRLLRQHFPAAITMA- 155
Cdd:cd08566    83 TDEKVP-TLEEalawakGKILlnLDLKDADLDEVIALVKK-HGAL-------DQVIFKSYSEEQAKELRALAPEVMLMPi 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1012713373 156 --PQTECRRAGLSLLMGLRPLAAIRAGRTYSLPPVF 189
Cdd:cd08566   154 vrDAEDLDEEEARAIDALNLLAFEITFDDLDLPPLF 189
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 6-149 6.70e-12

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: 63.01  E-value: 6.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGshavIEDMDRDQC-------LRHRLH 78
Cdd:cd08570     2 IGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFG----KDGLIIDDStwdelshLRTIEE 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1012713373  79 DGQPLLTFEHFAHTFTDQR----WI-LDIKPESAARTLaaLRHWADQ-QQKGDWLCRQARFLL--WHPEHTRLLRQHFP 149
Cdd:cd08570    78 PHQPMPTLKDVLEWLVEHElpdvKLmLDIKRDNDPEIL--FKLIAEMlAVKPDLDFWRERIILglWHLDFLKYGKEVLP 154
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 6-235 2.35e-10

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: 59.15  E-value: 2.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMD----------------- 68
Cdd:cd08575     4 IAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTyaelppldagygytfdg 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373  69 -RDQCLRHRLHDGQPLLT--FEHFAHTftdqRWILDIK----PESAARTLAALRHWadqqqkgdwlcRQARFLLW---HP 138
Cdd:cd08575    84 gKTGYPRGGGDGRIPTLEevFKAFPDT----PINIDIKspdaEELIAAVLDLLEKY-----------KREDRTVWgstNP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373 139 EHTRLLRQHFPAAITMAPQTECRraGLSLLMGLRPLAAIRAGRTYSL----PPVFH-----GLPLF-------RHSLVDA 202
Cdd:cd08575   149 EYLRALHPENPNLFESFSMTRCL--LLYLALGYTGLLPFVPIKESFFeiprPVIVLetftlGEGASivaallwWPNLFDH 226

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1012713373 203 YHRLGGRVLAFLPEGREQQRQALRSGVDEILSN 235
Cdd:cd08575   227 LRKRGIQVYLWVLNDEEDFEEAFDLGADGVMTD 259
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 5-105 6.66e-09

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: 54.63  E-value: 6.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   5 WISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQCLRHRL------- 77
Cdd:cd08582     1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIgswkges 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1012713373  78 HDGQPLLTFEHFAHTFTD--QRWILDIKPE 105
Cdd:cd08582    81 YKGEKVPTLEEYLAIVPKygKKLFIEIKHP 110
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 6-116 8.61e-08

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: 51.49  E-value: 8.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQCLR------HRLHD 79
Cdd:cd08573     2 IGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKlnaaakHRLSS 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1012713373  80 GQP---LLTFEHF-----AHtftDQRWILDIKpESAARTLAALRH 116
Cdd:cd08573    82 RFPgekIPTLEEAvkeclEN---NLRMIFDVK-SNSSKLVDALKN 122
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 6-68 1.92e-07

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE4 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1)) and similar proteins. Mammalian GDE4 is a transmembrane protein whose cellular function has not yet been elucidated. It is expressed widely, including in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. It is also expressed in the growth cones in neuroblastoma Neuro2a cells, which suggests GDE4 may play some distinct role from other members of the GDE family.


Pssm-ID: 176553 [Multi-domain]  Cd Length: 300  Bit Score: 50.68  E-value: 1.92e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMD 68
Cdd:cd08612    30 ISHRGGSGENLENTMEAFEHAVKVGTDMLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLN 92
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 6-235 2.25e-07

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: 49.57  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDaslirttgshaviedmdrdqclrhrlhdgqpLLT 85
Cdd:cd08556     2 IAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD-------------------------------IPT 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373  86 FEHFAHTFTDQRWI-LDIK-----PESAARTLAALRHWADQQqkgdwlcrqaRFLL--WHPEHTRLLRQHFPAAITMapq 157
Cdd:cd08556    51 LEEVLELVKGGVGLnIELKeptryPGLEAKVAELLREYGLEE----------RVVVssFDHEALRALKELDPEVPTG--- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373 158 tecrraglsLLMGLRPLAAIRAGRTYSLPPVF--HGLPLFRHSLVDAYHRLGGRVLAFLPEGREQQRQALRSGVDEILSN 235
Cdd:cd08556   118 ---------LLVDKPPLDPLLAELARALGADAvnPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITD 188
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 6-115 2.31e-07

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: 50.09  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQCLRHRLHDGQPLL- 84
Cdd:cd08565     2 AGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLRDSFGEKi 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1012713373  85 -TFEHFAHTFTDQRWIL--DIK--------PESAARTLAALR 115
Cdd:cd08565    82 pTLEEVLALFAPSGLELhvEIKtdadgtpyPGAAALAAATLR 123
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 8-235 1.07e-06

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: 48.17  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   8 HRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQcLRHR----------L 77
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEE-LKRLdigagnsgplS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373  78 HDGQPLLTFEHFAHTFTDQRWILDIKPESaarTLAALRHWADQQQK-----------GDWLCRQARFLLWHPEHTRLLRQ 146
Cdd:pfam03009  80 GERVPFPTLEEVLEFDWDVGFNIEIKIKP---YVEAIAPEEGLIVKdlllsvdeilaKKADPRRVIFSSFNPDELKRLRE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373 147 HFPaAITMAPQTECRRAGLSLLMGLRPLAAIRAGRTYSLPPVFHGLPlfrhSLVDAYHRLGGRVLAFLPEGREQQRQALR 226
Cdd:pfam03009 157 LAP-KLPLVFLSSGRAYAEADLLERAAAFAGAPALLGEVALVDEALP----DLVKRAHARGLVVHVWTVNNEDEMKRLLE 231


                  ....*....
gi 1012713373 227 SGVDEILSN 235
Cdd:pfam03009 232 LGVDGVITD 240
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 4-108 6.81e-06

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: 45.75  E-value: 6.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   4 IWISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQcLRhRLH-DGQP 82
Cdd:cd08568     1 IILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKE-LK-KLHpGGEL 78

                          90       100
                  ....*....|....*....|....*..
gi 1012713373  83 LLTFEHFAHTFTDQRWI-LDIKPESAA 108
Cdd:cd08568    79 IPTLEEVFRALPNDAIInVEIKDIDAV 105
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 6-109 7.17e-06

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity 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: 45.79  E-value: 7.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQCLRHRLHD------ 79
Cdd:cd08581     2 VAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVAEparfgs 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1012713373  80 ---GQPLLTFEHFAHTFTDQRWI---LDIKPESAAR 109
Cdd:cd08581    82 rfaGEPLPSLAAVVQWLAQHPQVtlfVEIKTESLDR 117
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 6-104 1.46e-05

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: 44.46  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQCLRHRLHD---GQP 82
Cdd:cd08579     2 IAHRGVSSNGVENTLEALEAAIKAKPDYVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIGEnghGAK 81

                          90       100
                  ....*....|....*....|....*
gi 1012713373  83 LLTFEHF---AHTFtDQRWILDIKP 104
Cdd:cd08579    82 IPSLDEYlalAKGL-KQKLLIELKP 105
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 6-80 1.81e-05

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: 44.62  E-value: 1.81e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1012713373   6 ISHRGLHQR-HG--ENSLhAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQCLRHRLHDG 80
Cdd:cd08585     7 IAHRGLHDRdAGipENSL-SAFRAAAEAGYGIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRLLGT 83
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 6-71 2.76e-04

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: 41.05  E-value: 2.76e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQ 71
Cdd:cd08562     2 IAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAE 67
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 6-87 1.18e-03

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: 39.08  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAVIEDMDRDQcLR--------HRL 77
Cdd:cd08563     4 FAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEE-LKkldagswfDEK 82

                          90
                  ....*....|
gi 1012713373  78 HDGQPLLTFE 87
Cdd:cd08563    83 FTGEKIPTLE 92
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 34-67 3.07e-03

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: 38.07  E-value: 3.07e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1012713373  34 LETDLRTTHDGQIVLHHDASLIRTTG--SHAVIEDM 67
Cdd:cd08601    32 IELDLQMTKDGVLVAMHDETLDRTTNieRPGPVKDY 67
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 6-59 6.22e-03

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: 36.64  E-value: 6.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTG 59
Cdd:cd08555     2 LSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTA 55
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 6-122 8.21e-03

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: 36.78  E-value: 8.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012713373   6 ISHRGLHQRHGENSLHAFEAAAEAGFHTLETDLRTTHDGQIVLHHDASLIRTTGSHAViedMDRDQCLRHRLHDGQPLlt 85
Cdd:cd08610    26 IGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNIGEV---QPESACENPAFFNWDFL-- 100

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1012713373  86 fehfaHTFTDQRWILDIKPESAARTLAAlrhwADQQQ 122
Cdd:cd08610   101 -----STLNAGKWFVKPRPFYNMKPLSE----ADKER 128
 
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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