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Conserved domains on  [gi|446956302|ref|WP_001033558|]
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MULTISPECIES: phosphatidylinositol-specific phospholipase C [Bacillus cereus group]

Protein Classification

phosphatidylinositol-specific phospholipase C( domain architecture ID 10171166)

phosphatidylinositol-specific phospholipase C participates in Ca2+-independent phosphatidylinositol (PI) metabolism, hydrolyzing the membrane lipid PI to produce phosphorylated myo-inositol and diacylglycerol; may function as virulence factors in some pathogenic bacteria

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_BcPLC_like cd08586
Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar ...
 51-357 1.69e-88

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: 271.47  E-value: 1.69e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302  51 MSKVEDSTKLSKISIPGTHGTMALHGAsflDENLTRNQTMSLPQQLNSGIRYVDMRVKRV-KDSFAMYHGIVNQKAMFED 129
Cdd:cd08586    1 MSALPDDTPLSELSIPGTHDSGALHGG---LSSSVQCQDWSIAEQLNAGIRFLDIRLRLIdNNDLAIHHGPFYQGLTFGD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 130 VLKEAIQFLKDYPTETILMRLKEETTPESGSLSFEEIFLKYKNVNASYFWDPNSvqtsdrNNPTLGDIRGKIVILQNFTS 209
Cdd:cd08586   78 VLNECYSFLDANPSETIIMSLKQEGSGDGNTDSFAEIFKEYLDNYPSYFYYTES------KIPTLGEVRGKIVLLRRFDG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 210 SQLYG---------------IDYESLNIQDKFEIGSgPDEIYGKWNAVKSHLQNANTN-FNNGKIYLNHFSGTGGatafl 273
Cdd:cd08586  152 DDEGGgynnggpddtlftinIDNGTLYIQDFYEVST-AEDIEKKWNAIKAHLDKAASNsSSSNKLYINFTSGSGG----- 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 274 nnvypWFVASGkenrntdsspkliqtnfthewsdfprdrSGQIYYGGMNTLGTELL-HQGEIKHVGIIAADFPGP--GLI 350
Cdd:cd08586  226 -----GFPLGG----------------------------GPGKYAEGINPLLYNYLkENNGRGRLGIVIMDFPGAdwDLI 272


                 ....*..
gi 446956302 351 DSIIKLN 357
Cdd:cd08586  273 QLIIGTN 279
 
Name Accession Description Interval E-value
PI-PLCc_BcPLC_like cd08586
Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar ...
 51-357 1.69e-88

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: 271.47  E-value: 1.69e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302  51 MSKVEDSTKLSKISIPGTHGTMALHGAsflDENLTRNQTMSLPQQLNSGIRYVDMRVKRV-KDSFAMYHGIVNQKAMFED 129
Cdd:cd08586    1 MSALPDDTPLSELSIPGTHDSGALHGG---LSSSVQCQDWSIAEQLNAGIRFLDIRLRLIdNNDLAIHHGPFYQGLTFGD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 130 VLKEAIQFLKDYPTETILMRLKEETTPESGSLSFEEIFLKYKNVNASYFWDPNSvqtsdrNNPTLGDIRGKIVILQNFTS 209
Cdd:cd08586   78 VLNECYSFLDANPSETIIMSLKQEGSGDGNTDSFAEIFKEYLDNYPSYFYYTES------KIPTLGEVRGKIVLLRRFDG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 210 SQLYG---------------IDYESLNIQDKFEIGSgPDEIYGKWNAVKSHLQNANTN-FNNGKIYLNHFSGTGGatafl 273
Cdd:cd08586  152 DDEGGgynnggpddtlftinIDNGTLYIQDFYEVST-AEDIEKKWNAIKAHLDKAASNsSSSNKLYINFTSGSGG----- 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 274 nnvypWFVASGkenrntdsspkliqtnfthewsdfprdrSGQIYYGGMNTLGTELL-HQGEIKHVGIIAADFPGP--GLI 350
Cdd:cd08586  226 -----GFPLGG----------------------------GPGKYAEGINPLLYNYLkENNGRGRLGIVIMDFPGAdwDLI 272


                 ....*..
gi 446956302 351 DSIIKLN 357
Cdd:cd08586  273 QLIIGTN 279
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 60-204 1.64e-14

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: 70.39  E-value: 1.64e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302    60 LSKISIPGTHGTMaLHGASFLDENltrnQTMSLPQQLNSGIRYVDMRVKRVKD-SFAMYHG-IVNQKAMFEDVLKEAIQF 137
Cdd:smart00148   5 LSHYFIPSSHNTY-LTGKQLWGES----SVEGYIQALDAGCRCVELDCWDGPDgEPVIYHGhTFTLPIKLSEVLEAIKDF 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302   138 LKDYPTETILMRLKEETTPESGSL---SFEEIFLKYknvnasYFWDPnsVQTSDRNNPTLGDIRGKIVIL 204
Cdd:smart00148  80 AFVTSPYPVILSLENHCSPDQQAKmaqMFKEIFGDM------LYTPP--LTSSLEVLPSPEQLRGKILLK 141
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 64-203 4.31e-11

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: 60.60  E-value: 4.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302   64 SIPGTHGTMALHGASFLDEN--LTRNQTMSLPQQLNSGIRYVDMRVKRVKDSFAM-YHG-IVNQKAMFEDVLKEAIQFLK 139
Cdd:pfam00388   2 SQPLSHYFISSSHNTYLTGDqlTGESSVEAYIRALLRGCRCVELDCWDGPDGEPVvYHGyTLTSKIPFRDVLEAIKDYAF 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446956302  140 DYPTETILMRLKEETTPESGSL---SFEEIFLKYknvnasYFWDPNSVQTSDrnNPTLGDIRGKIVI 203
Cdd:pfam00388  82 VTSPYPVILSLENHCSPEQQKKmaeILKEIFGDM------LYTPPLDDDLTE--LPSPEDLKGKILI 140
 
Name Accession Description Interval E-value
PI-PLCc_BcPLC_like cd08586
Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar ...
 51-357 1.69e-88

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: 271.47  E-value: 1.69e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302  51 MSKVEDSTKLSKISIPGTHGTMALHGAsflDENLTRNQTMSLPQQLNSGIRYVDMRVKRV-KDSFAMYHGIVNQKAMFED 129
Cdd:cd08586    1 MSALPDDTPLSELSIPGTHDSGALHGG---LSSSVQCQDWSIAEQLNAGIRFLDIRLRLIdNNDLAIHHGPFYQGLTFGD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 130 VLKEAIQFLKDYPTETILMRLKEETTPESGSLSFEEIFLKYKNVNASYFWDPNSvqtsdrNNPTLGDIRGKIVILQNFTS 209
Cdd:cd08586   78 VLNECYSFLDANPSETIIMSLKQEGSGDGNTDSFAEIFKEYLDNYPSYFYYTES------KIPTLGEVRGKIVLLRRFDG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 210 SQLYG---------------IDYESLNIQDKFEIGSgPDEIYGKWNAVKSHLQNANTN-FNNGKIYLNHFSGTGGatafl 273
Cdd:cd08586  152 DDEGGgynnggpddtlftinIDNGTLYIQDFYEVST-AEDIEKKWNAIKAHLDKAASNsSSSNKLYINFTSGSGG----- 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 274 nnvypWFVASGkenrntdsspkliqtnfthewsdfprdrSGQIYYGGMNTLGTELL-HQGEIKHVGIIAADFPGP--GLI 350
Cdd:cd08586  226 -----GFPLGG----------------------------GPGKYAEGINPLLYNYLkENNGRGRLGIVIMDFPGAdwDLI 272


                 ....*..
gi 446956302 351 DSIIKLN 357
Cdd:cd08586  273 QLIIGTN 279
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 56-357 5.80e-55

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: 184.60  E-value: 5.80e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302  56 DSTKLSKISIPGTHGTMALHGA--SFLDENLTRNQTMSLPQQLNSGIRYVDMRV--KRVKDSFAMYHGIVNQ-KAMFEDV 130
Cdd:cd08557    5 DDLPLSQLSIPGTHNSYAYTIDgnSPIVSKWSKTQDLSITDQLDAGVRYLDLRVayDPDDGDLYVCHGLFLLnGQTLEDV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 131 LKEAIQFLKDYPTETILMRLKEETTPESGS--LSFEEIFLKYKNVNASYFWDPNSvqtsdrNNPTLGDIR-GKIVILQNF 207
Cdd:cd08557   85 LNEVKDFLDAHPSEVVILDLEHEYGGDNGEdhDELDALLRDVLGDPLYRPPVRAG------GWPTLGELRaGKRVLLFYF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 208 -TSSQLYGIDYESLNIQDKFEIGsgpdeiYGKWNAVKSHLQNANTNF-NNGKIYLNHFSGTGGATAFLNNVYPWFVASGk 285
Cdd:cd08557  159 gGDDSSGGYDWGSLNIQDPYANG------TDKLESLKAFLNSALASPrSADFFYVNQASLTPGRITIAVAGSLYTVATR- 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446956302 286 enrntdsspkliQTNFTHEWsdFPRDRSGQiyyggmntlgtellhqgeiKHVGIIAADFPGPG-LIDSIIKLN 357
Cdd:cd08557  232 ------------ANPALYEW--LKEDGSGA-------------------SGPNIVATDFVDVGdLIDAVIRLN 271
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 56-288 1.70e-27

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: 110.82  E-value: 1.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302  56 DSTKLSKISIPGTHGTMALHGASFLDENLTRNQTMSLPQQLNSGIRYVDMRVKRVKD-SFAMYHGIVNQKAMFEDVLKEA 134
Cdd:cd00137    4 DTQPLAHYSIPGTHDTYLTAGQFTIKQVWGLTQTEMYRQQLLSGCRCVDIRCWDGKPeEPIIYHGPTFLDIFLKEVIEAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 135 IQFLKDYPTETILMRLKEEttpESGSLSFEEIFLKYKNVNASYFWDPNSVQTSDRnNPTLGDIRGKIVILQNFT------ 208
Cdd:cd00137   84 AQFLKKNPPETIIMSLKNE---VDSMDSFQAKMAEYCRTIFGDMLLTPPLKPTVP-LPSLEDLRGKILLLNKKNgfsgpt 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 209 -SSQLYGIDYES----------LNIQDKFEigsGPDEiyGKWNAVKSHLQNANTNFNngKIYLNHFSGTGGATA------ 271
Cdd:cd00137  160 gSSNDTGFVSFEfstqknrsynISSQDEYK---AYDD--EKVKLIKATVQFVDYNKN--QLSRNYPSGTSGGTAwyyyam 232

                        250
                 ....*....|....*..
gi 446956302 272 FLNNVYPWFVASGKENR 288
Cdd:cd00137  233 DSNNYMPQMFWNANPAG 249
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 60-204 1.64e-14

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: 70.39  E-value: 1.64e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302    60 LSKISIPGTHGTMaLHGASFLDENltrnQTMSLPQQLNSGIRYVDMRVKRVKD-SFAMYHG-IVNQKAMFEDVLKEAIQF 137
Cdd:smart00148   5 LSHYFIPSSHNTY-LTGKQLWGES----SVEGYIQALDAGCRCVELDCWDGPDgEPVIYHGhTFTLPIKLSEVLEAIKDF 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302   138 LKDYPTETILMRLKEETTPESGSL---SFEEIFLKYknvnasYFWDPnsVQTSDRNNPTLGDIRGKIVIL 204
Cdd:smart00148  80 AFVTSPYPVILSLENHCSPDQQAKmaqMFKEIFGDM------LYTPP--LTSSLEVLPSPEQLRGKILLK 141
PI-PLCXDc_like cd08587
Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and ...
 57-204 2.10e-13

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: 70.45  E-value: 2.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302  57 STKLSKISIPGTH--GT--------------MALHGASFLDENLTRNQTMSLPQQLNSGIRYVDMRV---KRVKDSFAMY 117
Cdd:cd08587    6 DLPLRDLVIPGSHdsGMytingdspvgpdqpEFGKIAKGIVRKWSVTQSLSIYDQLEAGIRYFDLRVaykPDSENKLYFV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 118 HGIVnQKAMFEDVLKEAIQFLKDYPTETILMRLKEETTPESGSLSF-EEIFLKYKNVNAsyfwDPNSVQTSDRNNPTLGD 196
Cdd:cd08587   86 HGLY-SGEPVDEVLEDVNDFLDEHPKEVVILDFNHFYGMDDKSPEDhEKLVELLEDIFG----DKLCPRDSDLLDVTLAD 160

                        170
                 ....*....|
gi 446956302 197 I--RGKIVIL 204
Cdd:cd08587  161 LweSGKRVIV 170
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 64-203 4.31e-11

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: 60.60  E-value: 4.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302   64 SIPGTHGTMALHGASFLDEN--LTRNQTMSLPQQLNSGIRYVDMRVKRVKDSFAM-YHG-IVNQKAMFEDVLKEAIQFLK 139
Cdd:pfam00388   2 SQPLSHYFISSSHNTYLTGDqlTGESSVEAYIRALLRGCRCVELDCWDGPDGEPVvYHGyTLTSKIPFRDVLEAIKDYAF 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446956302  140 DYPTETILMRLKEETTPESGSL---SFEEIFLKYknvnasYFWDPNSVQTSDrnNPTLGDIRGKIVI 203
Cdd:pfam00388  82 VTSPYPVILSLENHCSPEQQKKmaeILKEIFGDM------LYTPPLDDDLTE--LPSPEDLKGKILI 140
PI-PLCXDc_like_2 cd08621
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 56-150 9.59e-10

Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins; This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). 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, eukaryotic PI-PLCXDs 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: 176558  Cd Length: 300  Bit Score: 59.70  E-value: 9.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302  56 DSTKLSKISIPGTH--GTMALHG---ASFLDENLTRNQTMSLPQQLNSGIRYVDMRVKRVKD-SFAMYH-------GIVN 122
Cdd:cd08621    5 KDRPLRHIVMPGTHdsGMSSLTGglwPVDGNDSNTQTQGLSIYDQLRAGARYFDIRPVITHGgELWTGHyngedasAQGA 84

                         90       100
                 ....*....|....*....|....*...
gi 446956302 123 QKAMFEDVLKEAIQFLKDYPTETILMRL 150
Cdd:cd08621   85 NGESLDDILDEVNRFTDENPGELVILNF 112
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 57-196 7.43e-09

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: 56.57  E-value: 7.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302  57 STKLSKISIPGTHGTMALHGASFLdenLTRNQTMSLPQQLNSGIR--YVDMRV--KRVKdsfaMYHGIVNQKA--MFEDV 130
Cdd:cd08588    9 DRTYDEYTFLTTHNSFANSEDAFF---LAPNQEDDITKQLDDGVRglMLDIHDanGGLR----LCHSVCGLGDggPLSDV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 131 LKEAIQFLKDYPTE--TILMrlkeETTPESGSLSFEEIFlkykNVN--ASYFWDPNSVQTSDRNNPTLGD 196
Cdd:cd08588   82 LREVVDFLDANPNEvvTLFL----EDYVSPGPLLRSKLF----RVAglTDLVYVPDAMPWAGSDWPTLGE 143
PI-PLCXDc_plant cd08619
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing ...
 50-153 6.75e-08

Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing proteins found in plants; The CD corresponds to the catalytic domain present in uncharacterized plant phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). 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, plant PI-PLCXDs 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 plant PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176556  Cd Length: 285  Bit Score: 53.71  E-value: 6.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302  50 WMSKVE-----DSTKLSKISIPGTHGTMALH-GASFLDENLTRNQTMSLPQQLNSGIRYVDMrvkRVKDSFAMYHGIVnQ 123
Cdd:cd08619   14 WMSLSQlkamdSSLKLRDIVWPGTHDSATNKiGIPKVSRPFARCQSLSIYNQLCSGARVLDI---RVQEDRRVCHGCL-K 89

                         90       100       110
                 ....*....|....*....|....*....|
gi 446956302 124 KAMFEDVLKEAIQFLKDYPTETILMRLKEE 153
Cdd:cd08619   90 TYPVDVVLNDIKRFLSETKSEFVILEIRTE 119
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 57-147 3.07e-07

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: 51.86  E-value: 3.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302  57 STKLSKISIPGTHGTMAlhgaSFLDEN----------------------------LTrnQTMSLPQQLNSGIRYVDMRV- 107
Cdd:cd08616    7 DKPLTNLAIPGSHDSFT----YSIDKQspvspdqsvqnlvkvfpcifkkivkkwsKT--QSLTITEQLEAGIRYFDLRIa 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446956302 108 -KRVKDSFAMYHGIVNQKamFEDVLKEAIQFLKDYPTETIL 147
Cdd:cd08616   81 tKPKDNDLYFVHGLYGIL--VKEILEEINDFLTEHPKEVVI 119
PI-PLCXDc_CG14945_like cd08622
Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to ...
 59-357 5.82e-07

Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to phosphatidylinositol-specific phospholipase C, X domain containing; This subfamily corresponds to the catalytic domain present in uncharacterized metazoan Drosophila melanogaster CG14945-like proteins, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). 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, eukaryotic PI-PLCXDs 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: 176559  Cd Length: 276  Bit Score: 50.79  E-value: 5.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302  59 KLSKISIPGTHGTMALHGASFLDENLTR----NQTMSLPQQLNSGIRYVDMRVKR---VKDSFAMYHGIVNQKAMFEdVL 131
Cdd:cd08622    8 RIKDLFIPGTHNSAAYDTNSNANESLVDkyllTQDLDIWTQLVHGIRYLDLRVGYypdSPDNFWINHDLVRIVPLLT-VL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 132 KEAIQFLKDyPTETILMRLKEETTpesGSLSFEEIFLKYKNVNASYFWD----PNSVQTSDrnnPTLGDI--RGKIVILq 205
Cdd:cd08622   87 NDVRNFVQN-TGEIVVLDFHRFPV---GFHSHPEVHDELISLLRQELGDlilrRSRNYGWG---PTLSEIwaRRKRVII- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 206 nftssqLYGIDYeslniqdkfeIGSGPDEIYGKWNAVKSHLQNANTNFNngkiylnhfsgtggataFLNNVYpwfvasgK 285
Cdd:cd08622  159 ------CYDHEY----------FVRESDWLWPPVQQKWGNVQTLDDLKS-----------------YLRKLI-------S 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 286 ENRNTDSSPKLIQTNFTHEWSDF-------PRDRSGQIYYGGMNTLGTELLHQgeikhVGIIAADF-PGPGLIDSIIKLN 357
Cdd:cd08622  199 QPHRFTNPPVSLMAELTPVPWDIisdrlgnLRKLADIVNRKLTRWYRDEWGYN-----ANIVATDFfLGTNIIDVAIETN 273
PI-PLCXDc_like_1 cd08620
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 83-301 1.79e-04

Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins; This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). 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, eukaryotic PI-PLCXDs 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: 176557  Cd Length: 281  Bit Score: 43.15  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302  83 NLTRNQTMSLPQQLNSGIRYVDMRVKRVKDSFA-------MYHgivnQKAM-----FEDVLKEAIQFLKDYPTETILMRL 150
Cdd:cd08620   27 NLSVTQKDNVSTQLALGARYFDFRPGYLWPQTRvlvllndLYH----QHNMipgqgFDTFLQDVVTFLKANPTEIVVVHI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 151 ------KEETTPESGSLsfEEIFLKyknVNASYFWDPNSVQTSDRNNPTLGDIR--GKIVILqnftssqLYGI--DYESL 220
Cdd:cd08620  103 twdgfdNDCARPSAQEV--VEALAQ---ALASAKVGYVTSGTVSDLAASYAQLRqtGKRLIV-------LFGDadKYDSY 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302 221 NiqDKFEIGSGPDEIYGKWNAVKS-----------HLQNANTNFNNGKIY-LNHFSGTGG---AT--AFLNNVYPWFVAS 283
Cdd:cd08620  171 S--DEDYATSDPQPIIDALNKMLAegqsgydytvlQLQATASSTKKGLAAaILSGSHAGSpllATkaMFDSATLPWLREN 248

                        250
                 ....*....|....*...
gi 446956302 284 GKeNRNTDSSPKLIQTNF 301
Cdd:cd08620  249 VL-ARLGDDPLVVLMNDF 265
PI-PLCc_Rv2075c_like cd08590
Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This ...
 65-204 4.02e-04

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: 42.01  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446956302  65 IPGTHGTMALHGASFLDEN-----LTRNQTMSLPQQLNSGIRYVDMRV----KRVKDSFAMYHGIVNQKA----MFEDVL 131
Cdd:cd08590   15 ILGTHNSYNSRAYGYGNRYhgvryLDPNQELSITDQLDLGARFLELDVhwttGDLRLCHGGDHGYLGVCSsedrLFEDGL 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446956302 132 KEAIQFLKDYPTETILMRLKEETTPEsgslSFEEIFLKYKNVNASYFWDPNS--VQTSDRNNPTLGDIR--GKIVIL 204
Cdd:cd08590   95 NEIADWLNANPDEVVILYLEDHGDGG----KDDELNALLNDAFGDLLYTPSDcdDLQGLPNWPTKEDMLnsGKQVVL 167
 
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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