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Conserved domains on  [gi|663499484|gb|AIE90409|]
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putative integral membrane protein [uncultured marine group II/III euryarchaeote AD1000_02_H02]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_GDPD_SF super family cl14615
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 9-278 8.55e-52

Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases superfamily; The PI-PLC-like phosphodiesterases superfamily represents the catalytic domains of bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11), glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria, as well as their uncharacterized homologs found in organisms ranging from bacteria and archaea to metazoans, plants, and fungi. PI-PLCs are ubiquitous enzymes hydrolyzing the membrane lipid phosphoinositides to yield two important second messengers, inositol phosphates and diacylglycerol (DAG). GP-GDEs play essential roles in glycerol metabolism and catalyze the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols that are major sources of carbon and phosphate. Both, PI-PLCs and GP-GDEs, can hydrolyze the 3'-5' phosphodiester bonds in different substrates, and utilize a similar mechanism of general base and acid catalysis with conserved histidine residues, which consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81, glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs). The residues essential for enzyme activities and metal binding are not conserved in these sequence homologs, which might suggest that the function of catalytic domains in these proteins might be distinct from those in typical PLC-like phosphodiesterases.


The actual alignment was detected with superfamily member cd08588:

Pssm-ID: 472694  Cd Length: 270  Bit Score: 170.97  E-value: 8.55e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484   9 CHGMAEYCLRNYDNFTFPETHNSYATIEDGVWMAMNHYTALKAQWEGGIRAYMLDTHHLSKedtdveDVRFCHGDPDstf 88
Cdd:cd08588    1 CNGSPALCDRTYDEYTFLTTHNSFANSEDAFFLAPNQEDDITKQLDDGVRGLMLDIHDANG------GLRLCHSVCG--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484  89 lhpcIYSEVDAYAWLRQLGSLMNNSSGDVVSLLLENYV-PGEHL-EVLFNQTGILDRVFVHQ----PGQPWPSIGDMVLN 162
Cdd:cd08588   72 ----LGDGGPLSDVLREVVDFLDANPNEVVTLFLEDYVsPGPLLrSKLFRVAGLTDLVYVPDampwAGSDWPTLGEMIDA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484 163 GTDLVVYWDYQHDER-YPWLHHAWTHSWDTPYGEQEQSEMSCRIGRGDGV----QPVWH----LNNWLSSiygfADPVRA 233
Cdd:cd08588  148 NKRLLVFTDNEDVSTePPGVMYQFDYTVENPFSVGGDDDWSCTVRRGSGPlsriAPGFRrlflMNHFRDV----PVPITA 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 663499484 234 GQVNDYDTLMERALG-CWEEVGDR-PTFIAVDYWEDGEITNVTITLN 278
Cdd:cd08588  224 ANDNNGDGLLLRHLNnCRPAAGGRkPNFVAVDFYNIGDAFEAVDELN 270
 
Name Accession Description Interval E-value
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 9-278 8.55e-52

Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its uncharacterized homologs; This subfamily corresponds to the catalytic domain present in Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its uncharacterized homologs. Members in this family show high sequence similarity to bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), which participates in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG).


Pssm-ID: 176530  Cd Length: 270  Bit Score: 170.97  E-value: 8.55e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484   9 CHGMAEYCLRNYDNFTFPETHNSYATIEDGVWMAMNHYTALKAQWEGGIRAYMLDTHHLSKedtdveDVRFCHGDPDstf 88
Cdd:cd08588    1 CNGSPALCDRTYDEYTFLTTHNSFANSEDAFFLAPNQEDDITKQLDDGVRGLMLDIHDANG------GLRLCHSVCG--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484  89 lhpcIYSEVDAYAWLRQLGSLMNNSSGDVVSLLLENYV-PGEHL-EVLFNQTGILDRVFVHQ----PGQPWPSIGDMVLN 162
Cdd:cd08588   72 ----LGDGGPLSDVLREVVDFLDANPNEVVTLFLEDYVsPGPLLrSKLFRVAGLTDLVYVPDampwAGSDWPTLGEMIDA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484 163 GTDLVVYWDYQHDER-YPWLHHAWTHSWDTPYGEQEQSEMSCRIGRGDGV----QPVWH----LNNWLSSiygfADPVRA 233
Cdd:cd08588  148 NKRLLVFTDNEDVSTePPGVMYQFDYTVENPFSVGGDDDWSCTVRRGSGPlsriAPGFRrlflMNHFRDV----PVPITA 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 663499484 234 GQVNDYDTLMERALG-CWEEVGDR-PTFIAVDYWEDGEITNVTITLN 278
Cdd:cd08588  224 ANDNNGDGLLLRHLNnCRPAAGGRkPNFVAVDFYNIGDAFEAVDELN 270
 
Name Accession Description Interval E-value
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 9-278 8.55e-52

Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its uncharacterized homologs; This subfamily corresponds to the catalytic domain present in Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its uncharacterized homologs. Members in this family show high sequence similarity to bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), which participates in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG).


Pssm-ID: 176530  Cd Length: 270  Bit Score: 170.97  E-value: 8.55e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484   9 CHGMAEYCLRNYDNFTFPETHNSYATIEDGVWMAMNHYTALKAQWEGGIRAYMLDTHHLSKedtdveDVRFCHGDPDstf 88
Cdd:cd08588    1 CNGSPALCDRTYDEYTFLTTHNSFANSEDAFFLAPNQEDDITKQLDDGVRGLMLDIHDANG------GLRLCHSVCG--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484  89 lhpcIYSEVDAYAWLRQLGSLMNNSSGDVVSLLLENYV-PGEHL-EVLFNQTGILDRVFVHQ----PGQPWPSIGDMVLN 162
Cdd:cd08588   72 ----LGDGGPLSDVLREVVDFLDANPNEVVTLFLEDYVsPGPLLrSKLFRVAGLTDLVYVPDampwAGSDWPTLGEMIDA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484 163 GTDLVVYWDYQHDER-YPWLHHAWTHSWDTPYGEQEQSEMSCRIGRGDGV----QPVWH----LNNWLSSiygfADPVRA 233
Cdd:cd08588  148 NKRLLVFTDNEDVSTePPGVMYQFDYTVENPFSVGGDDDWSCTVRRGSGPlsriAPGFRrlflMNHFRDV----PVPITA 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 663499484 234 GQVNDYDTLMERALG-CWEEVGDR-PTFIAVDYWEDGEITNVTITLN 278
Cdd:cd08588  224 ANDNNGDGLLLRHLNnCRPAAGGRkPNFVAVDFYNIGDAFEAVDELN 270
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 20-278 1.76e-14

Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar proteins; This subfamily corresponds to the catalytic domain present in bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and their sequence homologs found in eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Its catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. Eukaryotic homologs in this family are named as phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). They are distinct from the typical eukaryotic phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11), which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, which is closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs. This family also includes a distinctly different type of eukaryotic PLC, glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC), an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG), releasing dimyristyl glycerol (DMG), which may facilitate the evasion of the protozoan to the host's immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs, but not mammalian PI-PLCs.


Pssm-ID: 176500 [Multi-domain]  Cd Length: 271  Bit Score: 71.74  E-value: 1.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484  20 YDNFTFPETHNSYA-----TIEDGVWMAMNHYTALKAQWEGGIRAYMLDTHHlskeDTDVEDVRFCHGdPDSTFLHPciY 94
Cdd:cd08557    9 LSQLSIPGTHNSYAytidgNSPIVSKWSKTQDLSITDQLDAGVRYLDLRVAY----DPDDGDLYVCHG-LFLLNGQT--L 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484  95 SEV--DAYAWLRQlgslmnnSSGDVVSLLLENYVPGEHLEVLFNQTGILDRVFVHQPGQP------WPSIGDMVLNGTDL 166
Cdd:cd08557   82 EDVlnEVKDFLDA-------HPSEVVILDLEHEYGGDNGEDHDELDALLRDVLGDPLYRPpvraggWPTLGELRAGKRVL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484 167 VVYwdyQHDERYPWLHHAWTHSWDTPYGEQEQSEMSCRIGRGDGVQ-----PVWHLNNWLSSIYGFaDPVRAGQVNDYDT 241
Cdd:cd08557  155 LFY---FGGDDSSGGYDWGSLNIQDPYANGTDKLESLKAFLNSALAsprsaDFFYVNQASLTPGRI-TIAVAGSLYTVAT 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 663499484 242 LMERALG-CWEEVG---DRPTFIAVDYWEDGEITNVTITLN 278
Cdd:cd08557  231 RANPALYeWLKEDGsgaSGPNIVATDFVDVGDLIDAVIRLN 271
PI-PLCc_Rv2075c_like cd08590
Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This ...
 23-179 5.18e-06

Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This subfamily corresponds to the catalytic domain present in uncharacterized Mycobacterium tuberculosis Rv2075c and its homologs. Members in this family are more closely related to the Streptomyces antibioticus phosphatidylinositol-specific phospholipase C1(SaPLC1)-like proteins rather than the typical bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). In contrast, SaPLC1-like proteins have two Ca2+-chelating amino acid substitutions which convert them to metal-dependent bacterial PI-PLC. Rv2075c and its homologs have the same amino acid substitutions as well, which might suggest they have metal-dependent PI-PLC activity.


Pssm-ID: 176532  Cd Length: 267  Bit Score: 47.02  E-value: 5.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484  23 FTFPETHNSYATIEDG-----VWMAM---NHYTALKAQWEGGIRAYMLDTHHLSKedtdveDVRFCHGdpdSTFLHPCIY 94
Cdd:cd08590   13 AQILGTHNSYNSRAYGygnryHGVRYldpNQELSITDQLDLGARFLELDVHWTTG------DLRLCHG---GDHGYLGVC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499484  95 SEVDAY--AWLRQLGSLMNNSSGDVVSLLLENYVPGEHLEVLFNQ--TGILDRVFVHQ------PGQPWPSIGDMVLNGT 164
Cdd:cd08590   84 SSEDRLfeDGLNEIADWLNANPDEVVILYLEDHGDGGKDDELNALlnDAFGDLLYTPSdcddlqGLPNWPTKEDMLNSGK 163

                        170       180
                 ....*....|....*....|.
gi 663499484 165 DLVV------YWDYQHDERYP 179
Cdd:cd08590  164 QVVLatgggcSGAQGMYNRKE 184
 
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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