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Conserved domains on  [gi|240256218|ref|NP_001078503|]
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PLC-like phosphodiesterases superfamily protein [Arabidopsis thaliana]

Protein Classification

PI-PLC domain-containing protein( domain architecture ID 10171182)

PI-PLC (phosphoinositide-specific phospholipase C) domain-containing protein may hydrolyze the membrane lipid phosphatidylinositol to produce phosphorylated myo-inositol and diacylglycerol; similar to Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130

Graphical summary

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List of domain hits

 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 ...
 61-335 1.21e-97

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: 292.31  E-value: 1.21e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218  61 NPTSKVNGLPFNKYSWLTTHNSYAITGANSATGSflvspkNQEDSITNQLKNGVRGIMLDTYDFQNDIWLCHSTGGTCfn 140
Cdd:cd08588    2 NGSPALCDRTYDEYTFLTTHNSFANSEDAFFLAP------NQEDDITKQLDDGVRGLMLDIHDANGGLRLCHSVCGLG-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218 141 ftAFQPAINALKEINDFLESNLSEIVTIILEDYVKS-QMGLTNVFNASGLSKFLLPISRMPKDGTDWPTVDDMVKQNQRL 219
Cdd:cd08588   74 --DGGPLSDVLREVVDFLDANPNEVVTLFLEDYVSPgPLLRSKLFRVAGLTDLVYVPDAMPWAGSDWPTLGEMIDANKRL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218 220 VVFTSKKDKE-ASEGLAYQWNYMVENQYGNDGMKDGSCSSRSESSSLDTMS---RSLVFQNYFETSPNSTQA--CADNSS 293
Cdd:cd08588  152 LVFTDNEDVStEPPGVMYQFDYTVENPFSVGGDDDWSCTVRRGSGPLSRIApgfRRLFLMNHFRDVPVPITAanDNNGDG 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 240256218 294 PLIEMMRTCHEAAGKRWPNFIAVDFYQRsdsGGAAEAVDEAN 335
Cdd:cd08588  232 LLLRHLNNCRPAAGGRKPNFVAVDFYNI---GDAFEAVDELN 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 ...
 61-335 1.21e-97

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: 292.31  E-value: 1.21e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218  61 NPTSKVNGLPFNKYSWLTTHNSYAITGANSATGSflvspkNQEDSITNQLKNGVRGIMLDTYDFQNDIWLCHSTGGTCfn 140
Cdd:cd08588    2 NGSPALCDRTYDEYTFLTTHNSFANSEDAFFLAP------NQEDDITKQLDDGVRGLMLDIHDANGGLRLCHSVCGLG-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218 141 ftAFQPAINALKEINDFLESNLSEIVTIILEDYVKS-QMGLTNVFNASGLSKFLLPISRMPKDGTDWPTVDDMVKQNQRL 219
Cdd:cd08588   74 --DGGPLSDVLREVVDFLDANPNEVVTLFLEDYVSPgPLLRSKLFRVAGLTDLVYVPDAMPWAGSDWPTLGEMIDANKRL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218 220 VVFTSKKDKE-ASEGLAYQWNYMVENQYGNDGMKDGSCSSRSESSSLDTMS---RSLVFQNYFETSPNSTQA--CADNSS 293
Cdd:cd08588  152 LVFTDNEDVStEPPGVMYQFDYTVENPFSVGGDDDWSCTVRRGSGPLSRIApgfRRLFLMNHFRDVPVPITAanDNNGDG 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 240256218 294 PLIEMMRTCHEAAGKRWPNFIAVDFYQRsdsGGAAEAVDEAN 335
Cdd:cd08588  232 LLLRHLNNCRPAAGGRKPNFVAVDFYNI---GDAFEAVDELN 270
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 68-184 9.55e-05

Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. These enzymes contain 2 regions (X and Y) which together form a TIM barrel-like structure containing the active site residues. Phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The bacterial enzyme appears to be a homologue of the mammalian PLCs.


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 42.27  E-value: 9.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218    68 GLPFNKYSWLTTHNSYaiTGANSATGsflvspKNQEDSITNQLKNGVRGIMLDTYD-FQNDIWLCHStggtcFNFTAFQP 146
Cdd:smart00148   2 DKPLSHYFIPSSHNTY--LTGKQLWG------ESSVEGYIQALDAGCRCVELDCWDgPDGEPVIYHG-----HTFTLPIK 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 240256218   147 AINALKEINDFLESNLSEIVTIILEDYVK--SQMGLTNVF 184
Cdd:smart00148  69 LSEVLEAIKDFAFVTSPYPVILSLENHCSpdQQAKMAQMF 108
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 70-172 3.64e-04

Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to form a single structural unit.


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 40.57  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218   70 PFNKYSWLTTHNSYAitgansaTGSFLVSpKNQEDSITNQLKNGVRGIMLDTYDF-QNDIWLCHstGGTcfnFTAFQPAI 148
Cdd:pfam00388   4 PLSHYFISSSHNTYL-------TGDQLTG-ESSVEAYIRALLRGCRCVELDCWDGpDGEPVVYH--GYT---LTSKIPFR 70

                          90       100
                  ....*....|....*....|....
gi 240256218  149 NALKEINDFLESNLSEIVTIILED 172
Cdd:pfam00388  71 DVLEAIKDYAFVTSPYPVILSLEN 94
 
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 ...
 61-335 1.21e-97

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: 292.31  E-value: 1.21e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218  61 NPTSKVNGLPFNKYSWLTTHNSYAITGANSATGSflvspkNQEDSITNQLKNGVRGIMLDTYDFQNDIWLCHSTGGTCfn 140
Cdd:cd08588    2 NGSPALCDRTYDEYTFLTTHNSFANSEDAFFLAP------NQEDDITKQLDDGVRGLMLDIHDANGGLRLCHSVCGLG-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218 141 ftAFQPAINALKEINDFLESNLSEIVTIILEDYVKS-QMGLTNVFNASGLSKFLLPISRMPKDGTDWPTVDDMVKQNQRL 219
Cdd:cd08588   74 --DGGPLSDVLREVVDFLDANPNEVVTLFLEDYVSPgPLLRSKLFRVAGLTDLVYVPDAMPWAGSDWPTLGEMIDANKRL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218 220 VVFTSKKDKE-ASEGLAYQWNYMVENQYGNDGMKDGSCSSRSESSSLDTMS---RSLVFQNYFETSPNSTQA--CADNSS 293
Cdd:cd08588  152 LVFTDNEDVStEPPGVMYQFDYTVENPFSVGGDDDWSCTVRRGSGPLSRIApgfRRLFLMNHFRDVPVPITAanDNNGDG 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 240256218 294 PLIEMMRTCHEAAGKRWPNFIAVDFYQRsdsGGAAEAVDEAN 335
Cdd:cd08588  232 LLLRHLNNCRPAAGGRKPNFVAVDFYNI---GDAFEAVDELN 270
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 69-335 1.95e-44

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: 155.33  E-value: 1.95e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218  69 LPFNKYSWLTTHNSYAITGANSATGSFLVSpKNQEDSITNQLKNGVRGIMLD--TYDFQNDIWLCHStggtcFNFTAFQP 146
Cdd:cd08557    7 LPLSQLSIPGTHNSYAYTIDGNSPIVSKWS-KTQDLSITDQLDAGVRYLDLRvaYDPDDGDLYVCHG-----LFLLNGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218 147 AINALKEINDFLESNLSEIVTIILEDYVKSQMGLTNVFNASGLSKFLLPISRMPKDGTD-WPTVDDMVkQNQRLVVFTSk 225
Cdd:cd08557   81 LEDVLNEVKDFLDAHPSEVVILDLEHEYGGDNGEDHDELDALLRDVLGDPLYRPPVRAGgWPTLGELR-AGKRVLLFYF- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218 226 kDKEASEGLAYQWNYMVENQYGNDGMKDGSCSSRSESSSLDTMSRSLVFQNYFETSPNSTQACADNS---------SPLI 296
Cdd:cd08557  159 -GGDDSSGGYDWGSLNIQDPYANGTDKLESLKAFLNSALASPRSADFFYVNQASLTPGRITIAVAGSlytvatranPALY 237

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 240256218 297 EMMRTCHeaAGKRWPNFIAVDFYqrsDSGGAAEAVDEAN 335
Cdd:cd08557  238 EWLKEDG--SGASGPNIVATDFV---DVGDLIDAVIRLN 271
PI-PLCc_Rv2075c_like cd08590
Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This ...
 67-230 1.05e-16

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: 79.37  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218  67 NGLPFNKYSWLTTHNSY---AITGANSATGSFLVSPkNQEDSITNQLKNGVRGIMLDTYDFQNDIWLCH-STGGTCFNFT 142
Cdd:cd08590    6 SNAPLCQAQILGTHNSYnsrAYGYGNRYHGVRYLDP-NQELSITDQLDLGARFLELDVHWTTGDLRLCHgGDHGYLGVCS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218 143 AFQPAINA-LKEINDFLESNLSEIVTIILEDYV------------KSQMGlTNVFNASGLskfllpisRMPKDGTDWPTV 209
Cdd:cd08590   85 SEDRLFEDgLNEIADWLNANPDEVVILYLEDHGdggkddelnallNDAFG-DLLYTPSDC--------DDLQGLPNWPTK 155

                        170       180
                 ....*....|....*....|.
gi 240256218 210 DDMVKQNQRLVVFTSKKDKEA 230
Cdd:cd08590  156 EDMLNSGKQVVLATGGGCSGA 176
PI-PLCXDc_like cd08587
Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and ...
 64-323 2.12e-11

Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and similar proteins; This family corresponds to the catalytic domain present in phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD) which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs mainly found in eukaryota. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) 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 and their bacterial homologs contain a single TIM-barrel type catalytic domain, X domain, which is more 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.


Pssm-ID: 176529  Cd Length: 288  Bit Score: 64.29  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218  64 SKVNGLPFNKYSWLTTHNSyaitGANSATGSFLVSP-----------------KNQEDSITNQLKNGVRgimldtY-DFQ 125
Cdd:cd08587    2 SAIGDLPLRDLVIPGSHDS----GMYTINGDSPVGPdqpefgkiakgivrkwsVTQSLSIYDQLEAGIR------YfDLR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218 126 --------NDIWLCHSTGGTCfnftAFQPAinaLKEINDFLESNLSEIVtiILeDYvkSQMGLTNVFNASGLSKFLLPIS 197
Cdd:cd08587   72 vaykpdseNKLYFVHGLYSGE----PVDEV---LEDVNDFLDEHPKEVV--IL-DF--NHFYGMDDKSPEDHEKLVELLE 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218 198 RM------PKDGTDW-PTVDDMVKQNQRLVVFTskKDKEASEGLAYQ-WNYMVENqYGN----DGMKDGSCSSRSESSSL 265
Cdd:cd08587  140 DIfgdklcPRDSDLLdVTLADLWESGKRVIVFY--DDDLASEGPYLWpSPYIPDP-WANtddpQKLIDFLENKLKERRRP 216

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256218 266 D---------TMSRSLVFQNYFETSPNSTQACADNssPLIEMMRTchEAAGKRWPNFIAVDFYQRSD 323
Cdd:cd08587  217 DkffvlqwilTPQASTIVLGLFSGLLKKLALRANP--ALLEWLRE--QLPGQDGPNIILNDFVDLGE 279
PI-PLCc_BcPLC_like cd08586
Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar ...
 79-212 3.11e-07

Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar proteins; This subfamily corresponds to the catalytic domain present in Bacillus cereus phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and its sequence homologs found in bacteria and 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. Their 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. This family also includes some uncharacterized eukaryotic homologs, which contains a single TIM-barrel type catalytic domain, X domain. They are similar to bacterial PI-PLCs, and distinct from typical eukaryotic PI-PLCs, which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains, and strictly require Ca2+ for their catalytic activities. The prototype of this family is Bacillus cereus PI-PLC, which has a moderate thermal stability and is active as a monomer.


Pssm-ID: 176528  Cd Length: 279  Bit Score: 51.52  E-value: 3.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218  79 THNSYAITGANSatgsflVSPKNQEDSITNQLKNGVRgiMLD---TYDFQNDIWLCHSTGGTCFNFTafqpaiNALKEIN 155
Cdd:cd08586   18 THDSGALHGGLS------SSVQCQDWSIAEQLNAGIR--FLDirlRLIDNNDLAIHHGPFYQGLTFG------DVLNECY 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218 156 DFLESNLSEivTIIL---EDYvkSQMGLTNVFNASGLSKFLLPISRMPKDGTDWPTVDDM 212
Cdd:cd08586   84 SFLDANPSE--TIIMslkQEG--SGDGNTDSFAEIFKEYLDNYPSYFYYTESKIPTLGEV 139
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 68-184 9.55e-05

Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. These enzymes contain 2 regions (X and Y) which together form a TIM barrel-like structure containing the active site residues. Phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The bacterial enzyme appears to be a homologue of the mammalian PLCs.


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 42.27  E-value: 9.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218    68 GLPFNKYSWLTTHNSYaiTGANSATGsflvspKNQEDSITNQLKNGVRGIMLDTYD-FQNDIWLCHStggtcFNFTAFQP 146
Cdd:smart00148   2 DKPLSHYFIPSSHNTY--LTGKQLWG------ESSVEGYIQALDAGCRCVELDCWDgPDGEPVIYHG-----HTFTLPIK 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 240256218   147 AINALKEINDFLESNLSEIVTIILEDYVK--SQMGLTNVF 184
Cdd:smart00148  69 LSEVLEAIKDFAFVTSPYPVILSLENHCSpdQQAKMAQMF 108
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 70-172 3.64e-04

Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to form a single structural unit.


Pssm-ID: 459795 [Multi-domain]  Cd Length: 142  Bit Score: 40.57  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218   70 PFNKYSWLTTHNSYAitgansaTGSFLVSpKNQEDSITNQLKNGVRGIMLDTYDF-QNDIWLCHstGGTcfnFTAFQPAI 148
Cdd:pfam00388   4 PLSHYFISSSHNTYL-------TGDQLTG-ESSVEAYIRALLRGCRCVELDCWDGpDGEPVVYH--GYT---LTSKIPFR 70

                          90       100
                  ....*....|....*....|....
gi 240256218  149 NALKEINDFLESNLSEIVTIILED 172
Cdd:pfam00388  71 DVLEAIKDYAFVTSPYPVILSLEN 94
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 70-176 7.19e-04

Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This subfamily corresponds to the catalytic domain present in prokaryotic and eukaryotic phosphoinositide-specific phospholipase C (PI-PLC), which is a ubiquitous enzyme catalyzing the cleavage of the sn3-phosphodiester bond in the membrane phosphoinositides (phosphatidylinositol, PI; Phosphatidylinositol-4-phosphate, PIP; phosphatidylinositol 4,5-bisphosphate, PIP2) to yield inositol phosphates (inositol monosphosphate, InsP; inositol diphosphate, InsP2; inositol trisphosphate, InsP3) and diacylglycerol (DAG). The higher eukaryotic PI-PLCs (EC 3.1.4.11) have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. They play a critical role in most signal transduction pathways, controlling numerous cellular events, such as cell growth, proliferation, excitation and secretion. These PI-PLCs strictly require Ca2+ for their catalytic activity. They display a clear preference towards the hydrolysis of the more highly phosphorylated PI-analogues, PIP2 and PIP, to generate two important second messengers, InsP3 and DAG. InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. In contrast, bacterial PI-PLCs contain a single catalytic domain. Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. They participate in Ca2+-independent PI metabolism. They are characterized as phosphatidylinositol-specific phospholipase C (EC 4.6.1.13) that selectively hydrolyze PI, not PIP or PIP2. The TIM-barrel type catalytic domain in bacterial PI-PLCs is very similar to the one in eukaryotic PI-PLCs, in which the catalytic domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. The catalytic mechanism of both prokaryotic and eukaryotic PI-PLCs is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily 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: 176497 [Multi-domain]  Cd Length: 274  Bit Score: 41.10  E-value: 7.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218  70 PFNKYSWLTTHNSYAITGANSATGSFLVSpknQEDSITNQLKNGVRGIMLDTYD-FQNDIWLCHstgGTCFNFTAFQPAI 148
Cdd:cd00137    7 PLAHYSIPGTHDTYLTAGQFTIKQVWGLT---QTEMYRQQLLSGCRCVDIRCWDgKPEEPIIYH---GPTFLDIFLKEVI 80

                         90       100
                 ....*....|....*....|....*...
gi 240256218 149 NAlkeINDFLESNLSEIVTIILEDYVKS 176
Cdd:cd00137   81 EA---IAQFLKKNPPETIIMSLKNEVDS 105
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 100-222 2.10e-03

Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This subfamily corresponds to the catalytic domain present in a group of phosphatidylinositol-specific phospholipase C X domain containing 1 (PI-PLCXD1), 2 (PI-PLCXD2) and 3 (PI-PLCXD3), which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs found in vertebrates. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has 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, members in this group contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176555  Cd Length: 290  Bit Score: 39.53  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256218 100 KNQEDSITNQLKNGVRgiMLD----TYDFQNDIWLCHST-GGTCFNftafqpainALKEINDFLESNLSEIVtiIL---- 170
Cdd:cd08616   58 KTQSLTITEQLEAGIR--YFDlriaTKPKDNDLYFVHGLyGILVKE---------ILEEINDFLTEHPKEVV--ILdfnh 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 240256218 171 ------EDYVKSQMGLTNVFNasglsKFLLPISRMPKDgtdwPTVDDMVKQNQRLVVF 222
Cdd:cd08616  125 fygmteEDHEKLLKMIKSIFG-----KKLCPRDPDLLN----VTLEYLWEKGYQVIVF 173
 
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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