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Conserved domains on  [gi|446643945|ref|WP_000721291|]
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MULTISPECIES: phosphatidylinositol-specific phospholipase C [Bacillus]

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 3.67e-87

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: 268.00  E-value: 3.67e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945  51 MSKLEDTKRISELSIPGTHGSMALHGAsfiDENLTRNQTMPLPQQFNAGIRYVDMRVKRV-KNSFAMQHGIVNQKAMFED 129
Cdd:cd08586    1 MSALPDDTPLSELSIPGTHDSGALHGG---LSSSVQCQDWSIAEQLNAGIRFLDIRLRLIdNNDLAIHHGPFYQGLTFGD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 130 VLKETIQFLRDNPHETILMRLKEETDPENGSQSFEEIFKSYKDRNVSYFWepnsvpFSERNNPKLGDIRGKIVILQNFAA 209
Cdd:cd08586   78 VLNECYSFLDANPSETIIMSLKQEGSGDGNTDSFAEIFKEYLDNYPSYFY------YTESKIPTLGEVRGKIVLLRRFDG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 210 SQEYG---------------INYESLNIQDNFEVSAGPDgMYEKWSAVKNQLLKA-NNDSNNNHIYLNHFSGTGGAtalw 273
Cdd:cd08586  152 DDEGGgynnggpddtlftinIDNGTLYIQDFYEVSTAED-IEKKWNAIKAHLDKAaSNSSSSNKLYINFTSGSGGG---- 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 274 nnyypwfvasgkenrdtgsnpqliqknttnewkdFPRDTNGQVFYGGMNTMGTDFILQG-GIRHSGIIAADFPGP--GLI 350
Cdd:cd08586  227 ----------------------------------FPLGGGPGKYAEGINPLLYNYLKENnGRGRLGIVIMDFPGAdwDLI 272


                 ....*..
gi 446643945 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 3.67e-87

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: 268.00  E-value: 3.67e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945  51 MSKLEDTKRISELSIPGTHGSMALHGAsfiDENLTRNQTMPLPQQFNAGIRYVDMRVKRV-KNSFAMQHGIVNQKAMFED 129
Cdd:cd08586    1 MSALPDDTPLSELSIPGTHDSGALHGG---LSSSVQCQDWSIAEQLNAGIRFLDIRLRLIdNNDLAIHHGPFYQGLTFGD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 130 VLKETIQFLRDNPHETILMRLKEETDPENGSQSFEEIFKSYKDRNVSYFWepnsvpFSERNNPKLGDIRGKIVILQNFAA 209
Cdd:cd08586   78 VLNECYSFLDANPSETIIMSLKQEGSGDGNTDSFAEIFKEYLDNYPSYFY------YTESKIPTLGEVRGKIVLLRRFDG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 210 SQEYG---------------INYESLNIQDNFEVSAGPDgMYEKWSAVKNQLLKA-NNDSNNNHIYLNHFSGTGGAtalw 273
Cdd:cd08586  152 DDEGGgynnggpddtlftinIDNGTLYIQDFYEVSTAED-IEKKWNAIKAHLDKAaSNSSSSNKLYINFTSGSGGG---- 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 274 nnyypwfvasgkenrdtgsnpqliqknttnewkdFPRDTNGQVFYGGMNTMGTDFILQG-GIRHSGIIAADFPGP--GLI 350
Cdd:cd08586  227 ----------------------------------FPLGGGPGKYAEGINPLLYNYLKENnGRGRLGIVIMDFPGAdwDLI 272


                 ....*..
gi 446643945 351 DSIIKLN 357
Cdd:cd08586  273 QLIIGTN 279
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 56-204 2.49e-12

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: 64.22  E-value: 2.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945    56 DTKRISELSIPGTHGSMaLHGASFIDENltrnQTMPLPQQFNAGIRYVDMRVKRVKN-SFAMQHG-IVNQKAMFEDVLKE 133
Cdd:smart00148   1 MDKPLSHYFIPSSHNTY-LTGKQLWGES----SVEGYIQALDAGCRCVELDCWDGPDgEPVIYHGhTFTLPIKLSEVLEA 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446643945   134 TIQFLRDNPHETILMRLKEETDPENGS---QSFEEIFKSYkdrnvsYFWEPNSVpfSERNNPKLGDIRGKIVIL 204
Cdd:smart00148  76 IKDFAFVTSPYPVILSLENHCSPDQQAkmaQMFKEIFGDM------LYTPPLTS--SLEVLPSPEQLRGKILLK 141
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 63-203 3.99e-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: 3.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945   63 LSIPGTHGSMALHGASFidenLTRNQ------TMPLPQQFNAGIRYVDMRVKRVKNSFAM-QHG-IVNQKAMFEDVLKET 134
Cdd:pfam00388   1 MSQPLSHYFISSSHNTY----LTGDQltgessVEAYIRALLRGCRCVELDCWDGPDGEPVvYHGyTLTSKIPFRDVLEAI 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446643945  135 IQFLRDNPHETILMRLKEETDPENGS---QSFEEIFKSYkdrnvsYFWEPNSVPFSErnNPKLGDIRGKIVI 203
Cdd:pfam00388  77 KDYAFVTSPYPVILSLENHCSPEQQKkmaEILKEIFGDM------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 3.67e-87

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: 268.00  E-value: 3.67e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945  51 MSKLEDTKRISELSIPGTHGSMALHGAsfiDENLTRNQTMPLPQQFNAGIRYVDMRVKRV-KNSFAMQHGIVNQKAMFED 129
Cdd:cd08586    1 MSALPDDTPLSELSIPGTHDSGALHGG---LSSSVQCQDWSIAEQLNAGIRFLDIRLRLIdNNDLAIHHGPFYQGLTFGD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 130 VLKETIQFLRDNPHETILMRLKEETDPENGSQSFEEIFKSYKDRNVSYFWepnsvpFSERNNPKLGDIRGKIVILQNFAA 209
Cdd:cd08586   78 VLNECYSFLDANPSETIIMSLKQEGSGDGNTDSFAEIFKEYLDNYPSYFY------YTESKIPTLGEVRGKIVLLRRFDG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 210 SQEYG---------------INYESLNIQDNFEVSAGPDgMYEKWSAVKNQLLKA-NNDSNNNHIYLNHFSGTGGAtalw 273
Cdd:cd08586  152 DDEGGgynnggpddtlftinIDNGTLYIQDFYEVSTAED-IEKKWNAIKAHLDKAaSNSSSSNKLYINFTSGSGGG---- 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 274 nnyypwfvasgkenrdtgsnpqliqknttnewkdFPRDTNGQVFYGGMNTMGTDFILQG-GIRHSGIIAADFPGP--GLI 350
Cdd:cd08586  227 ----------------------------------FPLGGGPGKYAEGINPLLYNYLKENnGRGRLGIVIMDFPGAdwDLI 272


                 ....*..
gi 446643945 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 3.81e-54

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: 182.29  E-value: 3.81e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945  56 DTKRISELSIPGTHGSMALHGA--SFIDENLTRNQTMPLPQQFNAGIRYVDMRV--KRVKNSFAMQHGIVNQ-KAMFEDV 130
Cdd:cd08557    5 DDLPLSQLSIPGTHNSYAYTIDgnSPIVSKWSKTQDLSITDQLDAGVRYLDLRVayDPDDGDLYVCHGLFLLnGQTLEDV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 131 LKETIQFLRDNPHETILMRLKEETDPENGSQ--SFEEIFKSYKDRNVSYFWEPNSvpfserNNPKLGDIR-GKIVILQNF 207
Cdd:cd08557   85 LNEVKDFLDAHPSEVVILDLEHEYGGDNGEDhdELDALLRDVLGDPLYRPPVRAG------GWPTLGELRaGKRVLLFYF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 208 AASQEYGINY-ESLNIQDNFEVSagpdgmYEKWSAVKNQLLKA-NNDSNNNHIYLNHFSGTGGATalwnnyyPWFVASGK 285
Cdd:cd08557  159 GGDDSSGGYDwGSLNIQDPYANG------TDKLESLKAFLNSAlASPRSADFFYVNQASLTPGRI-------TIAVAGSL 225

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446643945 286 ENRDTGSNPQLIQKNTTNEWkdfprdtngqvfyggmntmgtdfilqgGIRHSGIIAADFPGPG-LIDSIIKLN 357
Cdd:cd08557  226 YTVATRANPALYEWLKEDGS---------------------------GASGPNIVATDFVDVGdLIDAVIRLN 271
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 54-288 3.18e-29

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: 115.82  E-value: 3.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945  54 LEDTKRISELSIPGTHGSMALHGASFIDENLTRNQTMPLPQQFNAGIRYVDMRVKRVK-NSFAMQHGIVNQKAMFEDVLK 132
Cdd:cd00137    2 HPDTQPLAHYSIPGTHDTYLTAGQFTIKQVWGLTQTEMYRQQLLSGCRCVDIRCWDGKpEEPIIYHGPTFLDIFLKEVIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 133 ETIQFLRDNPHETILMRLKEETDPENGSQS-FEEIFKSYKDRNVSYFWEPNSVPfsernNPKLGDIRGKIVILQNFAASQ 211
Cdd:cd00137   82 AIAQFLKKNPPETIIMSLKNEVDSMDSFQAkMAEYCRTIFGDMLLTPPLKPTVP-----LPSLEDLRGKILLLNKKNGFS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 212 EYGInYESLNIQDNFEVSAGPDGMYEK--------WSAVKNQLLKANND---SNNNHIYLNHFSGTGGATALW------N 274
Cdd:cd00137  157 GPTG-SSNDTGFVSFEFSTQKNRSYNIssqdeykaYDDEKVKLIKATVQfvdYNKNQLSRNYPSGTSGGTAWYyyamdsN 235

                        250
                 ....*....|....
gi 446643945 275 NYYPWFVASGKENR 288
Cdd:cd00137  236 NYMPQMFWNANPAG 249
PI-PLCXDc_like cd08587
Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and ...
 58-357 2.91e-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: 70.06  E-value: 2.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945  58 KRISELSIPGTHGSMA--LHGAS--------------FIDENLTRNQTMPLPQQFNAGIRYVDMRV---KRVKNSFAMQH 118
Cdd:cd08587    7 LPLRDLVIPGSHDSGMytINGDSpvgpdqpefgkiakGIVRKWSVTQSLSIYDQLEAGIRYFDLRVaykPDSENKLYFVH 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 119 GIVnQKAMFEDVLKETIQFLRDNPHETILMRLKEETDPENGSQSF--------EEIFKSYKDRNVSYFWepnsvpfsern 190
Cdd:cd08587   87 GLY-SGEPVDEVLEDVNDFLDEHPKEVVILDFNHFYGMDDKSPEDheklvellEDIFGDKLCPRDSDLL----------- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 191 NPKLGDI--RGKIVILqnfaasqeyGINYESLNIQDNFEVSagpDGMYEKWSAVK--NQLLKANNDSNNNHIYLNHFSGT 266
Cdd:cd08587  155 DVTLADLweSGKRVIV---------FYDDDLASEGPYLWPS---PYIPDPWANTDdpQKLIDFLENKLKERRRPDKFFVL 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 267 GG-ATAlwnnyYPWFVASGkenrdTGSNPQLIQKNTTN----EWkdfprdtngqvFYGGMNtmGTDFILqggirhsgIIA 341
Cdd:cd08587  223 QWiLTP-----QASTIVLG-----LFSGLLKKLALRANpallEW-----------LREQLP--GQDGPN--------IIL 271

                        330
                 ....*....|....*..
gi 446643945 342 ADF-PGPGLIDSIIKLN 357
Cdd:cd08587  272 NDFvDLGEFIDLAIALN 288
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 56-204 2.49e-12

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: 64.22  E-value: 2.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945    56 DTKRISELSIPGTHGSMaLHGASFIDENltrnQTMPLPQQFNAGIRYVDMRVKRVKN-SFAMQHG-IVNQKAMFEDVLKE 133
Cdd:smart00148   1 MDKPLSHYFIPSSHNTY-LTGKQLWGES----SVEGYIQALDAGCRCVELDCWDGPDgEPVIYHGhTFTLPIKLSEVLEA 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446643945   134 TIQFLRDNPHETILMRLKEETDPENGS---QSFEEIFKSYkdrnvsYFWEPNSVpfSERNNPKLGDIRGKIVIL 204
Cdd:smart00148  76 IKDFAFVTSPYPVILSLENHCSPDQQAkmaQMFKEIFGDM------LYTPPLTS--SLEVLPSPEQLRGKILLK 141
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 63-203 3.99e-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: 3.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945   63 LSIPGTHGSMALHGASFidenLTRNQ------TMPLPQQFNAGIRYVDMRVKRVKNSFAM-QHG-IVNQKAMFEDVLKET 134
Cdd:pfam00388   1 MSQPLSHYFISSSHNTY----LTGDQltgessVEAYIRALLRGCRCVELDCWDGPDGEPVvYHGyTLTSKIPFRDVLEAI 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446643945  135 IQFLRDNPHETILMRLKEETDPENGS---QSFEEIFKSYkdrnvsYFWEPNSVPFSErnNPKLGDIRGKIVI 203
Cdd:pfam00388  77 KDYAFVTSPYPVILSLENHCSPEQQKkmaEILKEIFGDM------LYTPPLDDDLTE--LPSPEDLKGKILI 140
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 52-147 9.56e-08

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: 53.40  E-value: 9.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945  52 SKLEDtKRISELSIPGTHGSMAlhgaSFIDEN----------------------------LTrnQTMPLPQQFNAGIRYV 103
Cdd:cd08616    3 EKLKD-KPLTNLAIPGSHDSFT----YSIDKQspvspdqsvqnlvkvfpcifkkivkkwsKT--QSLTITEQLEAGIRYF 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446643945 104 DMRV--KRVKNSFAMQHGIVNQKamFEDVLKETIQFLRDNPHETIL 147
Cdd:cd08616   76 DLRIatKPKDNDLYFVHGLYGIL--VKEILEEINDFLTEHPKEVVI 119
PI-PLCXDc_CG14945_like cd08622
Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to ...
 59-218 2.59e-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: 51.95  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945  59 RISELSIPGTHGSMALHGASFIDENLTR----NQTMPLPQQFNAGIRYVDMRVKRVKNS---FAMQHGIVNQKAMFEdVL 131
Cdd:cd08622    8 RIKDLFIPGTHNSAAYDTNSNANESLVDkyllTQDLDIWTQLVHGIRYLDLRVGYYPDSpdnFWINHDLVRIVPLLT-VL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 132 KETIQFLrDNPHETILMRLKE-----ETDPENGSQSFEEIFKSYKD----RNVSYFWepnsvpfsernNPKLGDI--RGK 200
Cdd:cd08622   87 NDVRNFV-QNTGEIVVLDFHRfpvgfHSHPEVHDELISLLRQELGDlilrRSRNYGW-----------GPTLSEIwaRRK 154

                        170
                 ....*....|....*...
gi 446643945 201 IVILqnfAASQEYGINYE 218
Cdd:cd08622  155 RVII---CYDHEYFVRES 169
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 49-218 3.17e-07

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: 51.56  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945  49 NWMSKLEDtKRISELSIPGTHGSMALHGASFIdenLTRNQTMPLPQQFNAGIR--YVDMRV--KRVKnsfaMQHGIVNQK 124
Cdd:cd08588    2 NGSPALCD-RTYDEYTFLTTHNSFANSEDAFF---LAPNQEDDITKQLDDGVRglMLDIHDanGGLR----LCHSVCGLG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 125 A--MFEDVLKETIQFLRDNPHE--TILMRLKEETDPENGSQSFEEifksykDRNVSYFWEPNSVPFSERNNPKLGDIR-- 198
Cdd:cd08588   74 DggPLSDVLREVVDFLDANPNEvvTLFLEDYVSPGPLLRSKLFRV------AGLTDLVYVPDAMPWAGSDWPTLGEMIda 147

                        170       180
                 ....*....|....*....|...
gi 446643945 199 GK--IVILQNFAASQE-YGINYE 218
Cdd:cd08588  148 NKrlLVFTDNEDVSTEpPGVMYQ 170
PI-PLCXDc_plant cd08619
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing ...
 49-357 7.37e-07

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: 50.63  E-value: 7.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945  49 NWMSKLEDTK-----RISELSIPGTHGSMALH-GASFIDENLTRNQTMPLPQQFNAGIRYVDMrvkRVKNSFAMQHGIVn 122
Cdd:cd08619   13 EWMSLSQLKAmdsslKLRDIVWPGTHDSATNKiGIPKVSRPFARCQSLSIYNQLCSGARVLDI---RVQEDRRVCHGCL- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 123 QKAMFEDVLKETIQFLRDNPHETILMRLKEETD----PENGSQSFEEIFKSYKDRNVSYFWEPnsvpfsernnpkLGDIR 198
Cdd:cd08619   89 KTYPVDVVLNDIKRFLSETKSEFVILEIRTEYGhedpPQFDLWLVEQLGDHLIHQDDSVFSKT------------LAELL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 199 GKIVIL----QNFAASQEYGINYESLNIQDNFEVSAGPDGMYEkwSAVKNqLLKANNDSNNNHIYlnhfsgtggatalwn 274
Cdd:cd08619  157 PKRVICiwkpRKSPAPAVGSPLWSSAYLKDNWIDTDLPVTKFE--SNIKN-LLEQPPQDSRKYFY--------------- 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945 275 nyypwfvasGKENRDTGS--NPQLIQKNTTNEWKDFPRDTNGQVFYGGMNTmgtdfilqggirHSGIIAADFPGPGLIDS 352
Cdd:cd08619  219 ---------RVENTVTPQfdNPILCVKPVTRRISQYARLFIPEVFKRGLAD------------RLQIFSLDFIDLDFVDA 277


                 ....*
gi 446643945 353 IIKLN 357
Cdd:cd08619  278 CIGLT 282
PI-PLCXDc_like_2 cd08621
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 56-150 2.93e-06

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: 48.91  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945  56 DTKRISELSIPGTHGS-MA-LHG---ASFIDENLTRNQTMPLPQQFNAGIRYVDMRVKRVKN----------SFAMQHGI 120
Cdd:cd08621    5 KDRPLRHIVMPGTHDSgMSsLTGglwPVDGNDSNTQTQGLSIYDQLRAGARYFDIRPVITHGgelwtghyngEDASAQGA 84

                         90       100       110
                 ....*....|....*....|....*....|
gi 446643945 121 VNQkaMFEDVLKETIQFLRDNPHETILMRL 150
Cdd:cd08621   85 NGE--SLDDILDEVNRFTDENPGELVILNF 112
PI-PLCXDc_like_1 cd08620
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 58-175 2.80e-05

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: 45.85  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945  58 KRISELSIPGTHGSmalhGASFIDeNLTRNQTMPLPQQFNAGIRYVDMRVKRVKNSFAM---------QHGiVNQKAMFE 128
Cdd:cd08620    7 QPFNRFVLPGAHDA----GMNGMT-NLSVTQKDNVSTQLALGARYFDFRPGYLWPQTRVlvllndlyhQHN-MIPGQGFD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446643945 129 DVLKETIQFLRDNPHETILMRL------KEETDPENGSQS--FEEIFKSYKDRNV 175
Cdd:cd08620   81 TFLQDVVTFLKANPTEIVVVHItwdgfdNDCARPSAQEVVeaLAQALASAKVGYV 135
PI-PLCc_Rv2075c_like cd08590
Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This ...
 65-204 3.36e-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: 42.39  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446643945  65 IPGTHGSMALHGASFIDEN-----LTRNQTMPLPQQFNAGIRYVDMRV----KRVKNSFAMQHGIVNQKA----MFEDVL 131
Cdd:cd08590   15 ILGTHNSYNSRAYGYGNRYhgvryLDPNQELSITDQLDLGARFLELDVhwttGDLRLCHGGDHGYLGVCSsedrLFEDGL 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446643945 132 KETIQFLRDNPHETILMRLKEETDPEngsqSFEEIFKSYKDRNVSYFWEPNS--VPFSERNNPKLGDIR--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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