NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|581792053|gb|EVR95216|]
View 

1-phosphatidylinositol phosphodiesterase [Staphylococcus aureus M1472]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 38-327 1.22e-91

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: 274.55  E-value: 1.22e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  38 MSKLDESKHLTEINMPGSHDSGSFTLTDpvkSVWAKTQGKDYLTQMKSGVRFFDIRGRASADNMISVHHGMVYLHHELGK 117
Cdd:cd08586    1 MSALPDDTPLSELSIPGTHDSGALHGGL---SSSVQCQDWSIAEQLNAGIRFLDIRLRLIDNNDLAIHHGPFYQGLTFGD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 118 FLDDAKYYLSAYPNETIVMSMKKDYDSDSKvTKTFEEIFREYYYNNPQYqnlFYTGSNANPTLKETKGKIVLFNRMGGTY 197
Cdd:cd08586   78 VLNECYSFLDANPSETIIMSLKQEGSGDGN-TDSFAEIFKEYLDNYPSY---FYYTESKIPTLGEVRGKIVLLRRFDGDD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 198 iksgygaDTSGIQWADNATFETKINNGSLNLKVQDEYK----DYYDKKVEAVKNLLAKAKTDSNKDN-VYVNFLSVASGG 272
Cdd:cd08586  154 -------EGGGYNNGGPDDTLFTINIDNGTLYIQDFYEvstaEDIEKKWNAIKAHLDKAASNSSSSNkLYINFTSGSGGG 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 581792053 273 SAF-NSTYNYASHINPEIAKTIKEN-GKARTGWLIVDYAGYPWpgydDIVSEIIDSN 327
Cdd:cd08586  227 FPLgGGPGKYAEGINPLLYNYLKENnGRGRLGIVIMDFPGADW----DLIQLIIGTN 279
 
Name Accession Description Interval E-value
PI-PLCc_BcPLC_like cd08586
Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar ...
 38-327 1.22e-91

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: 274.55  E-value: 1.22e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  38 MSKLDESKHLTEINMPGSHDSGSFTLTDpvkSVWAKTQGKDYLTQMKSGVRFFDIRGRASADNMISVHHGMVYLHHELGK 117
Cdd:cd08586    1 MSALPDDTPLSELSIPGTHDSGALHGGL---SSSVQCQDWSIAEQLNAGIRFLDIRLRLIDNNDLAIHHGPFYQGLTFGD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 118 FLDDAKYYLSAYPNETIVMSMKKDYDSDSKvTKTFEEIFREYYYNNPQYqnlFYTGSNANPTLKETKGKIVLFNRMGGTY 197
Cdd:cd08586   78 VLNECYSFLDANPSETIIMSLKQEGSGDGN-TDSFAEIFKEYLDNYPSY---FYYTESKIPTLGEVRGKIVLLRRFDGDD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 198 iksgygaDTSGIQWADNATFETKINNGSLNLKVQDEYK----DYYDKKVEAVKNLLAKAKTDSNKDN-VYVNFLSVASGG 272
Cdd:cd08586  154 -------EGGGYNNGGPDDTLFTINIDNGTLYIQDFYEvstaEDIEKKWNAIKAHLDKAASNSSSSNkLYINFTSGSGGG 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 581792053 273 SAF-NSTYNYASHINPEIAKTIKEN-GKARTGWLIVDYAGYPWpgydDIVSEIIDSN 327
Cdd:cd08586  227 FPLgGGPGKYAEGINPLLYNYLKENnGRGRLGIVIMDFPGADW----DLIQLIIGTN 279
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 43-192 4.36e-51

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: 165.92  E-value: 4.36e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053    43 ESKHLTEINMPGSHDsgsftLTDPVKSVWAKTQGKDYLTQMKSGVRFFDIRGRASADNMISVHHGM-VYLHHELGKFLDD 121
Cdd:smart00148   1 MDKPLSHYFIPSSHN-----TYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDGPDGEPVIYHGHtFTLPIKLSEVLEA 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581792053   122 AKYYLSAYPNETIVMSMKKD--YDSDSKVTKTFEEIFREYYYNNPQYQNLFYtgsnaNPTLKETKGKIVLFNR 192
Cdd:smart00148  76 IKDFAFVTSPYPVILSLENHcsPDQQAKMAQMFKEIFGDMLYTPPLTSSLEV-----LPSPEQLRGKILLKVR 143
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 51-191 5.91e-31

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: 113.75  E-value: 5.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053   51 NMPGSHDSGSFTLTDPVKS--VWAKTQGKDYLTQMKSGVRFFDIRGRASADNMISVHHGMVYL-HHELGKFLDDAKYYLS 127
Cdd:pfam00388   2 SQPLSHYFISSSHNTYLTGdqLTGESSVEAYIRALLRGCRCVELDCWDGPDGEPVVYHGYTLTsKIPFRDVLEAIKDYAF 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581792053  128 AYPNETIVMSMKKDY--DSDSKVTKTFEEIFREYYYNNPQYQnlfytGSNANPTLKETKGKIVLFN 191
Cdd:pfam00388  82 VTSPYPVILSLENHCspEQQKKMAEILKEIFGDMLYTPPLDD-----DLTELPSPEDLKGKILIKG 142
PTZ00268 PTZ00268
glycosylphosphatidylinositol-specific phospholipase C; Provisional
 33-157 2.60e-06

glycosylphosphatidylinositol-specific phospholipase C; Provisional


Pssm-ID: 140294  Cd Length: 380  Bit Score: 48.73  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  33 SPENWMSKLD---ESKHLTEINMPGSHDSGS---------------FTLTDPVK------------SVWAKTQGKDYLTQ 82
Cdd:PTZ00268  14 HPQSWMHDLRsfiGEMAITQVCLVGSHNAASygihkdspfgadapgFLLGDSVVaslsrflfrgisASWSKCQGMSVRAQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  83 MKSGVRFFDIRGRASADNMISVHHGMVYLHHELGKFLDDAKYYLS--AYPNETIVMSMKKDY---DSDSKvTKTFEEIFR 157
Cdd:PTZ00268  94 LDHGVRYLDLRVATNPEDANRLYISHTQISVPLADVLEDVKAFLNdpSSANEFIVLDFQHLYltdDSDGK-GKFFRELDR 172
 
Name Accession Description Interval E-value
PI-PLCc_BcPLC_like cd08586
Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar ...
 38-327 1.22e-91

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: 274.55  E-value: 1.22e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  38 MSKLDESKHLTEINMPGSHDSGSFTLTDpvkSVWAKTQGKDYLTQMKSGVRFFDIRGRASADNMISVHHGMVYLHHELGK 117
Cdd:cd08586    1 MSALPDDTPLSELSIPGTHDSGALHGGL---SSSVQCQDWSIAEQLNAGIRFLDIRLRLIDNNDLAIHHGPFYQGLTFGD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 118 FLDDAKYYLSAYPNETIVMSMKKDYDSDSKvTKTFEEIFREYYYNNPQYqnlFYTGSNANPTLKETKGKIVLFNRMGGTY 197
Cdd:cd08586   78 VLNECYSFLDANPSETIIMSLKQEGSGDGN-TDSFAEIFKEYLDNYPSY---FYYTESKIPTLGEVRGKIVLLRRFDGDD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 198 iksgygaDTSGIQWADNATFETKINNGSLNLKVQDEYK----DYYDKKVEAVKNLLAKAKTDSNKDN-VYVNFLSVASGG 272
Cdd:cd08586  154 -------EGGGYNNGGPDDTLFTINIDNGTLYIQDFYEvstaEDIEKKWNAIKAHLDKAASNSSSSNkLYINFTSGSGGG 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 581792053 273 SAF-NSTYNYASHINPEIAKTIKEN-GKARTGWLIVDYAGYPWpgydDIVSEIIDSN 327
Cdd:cd08586  227 FPLgGGPGKYAEGINPLLYNYLKENnGRGRLGIVIMDFPGADW----DLIQLIIGTN 279
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 43-192 4.36e-51

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: 165.92  E-value: 4.36e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053    43 ESKHLTEINMPGSHDsgsftLTDPVKSVWAKTQGKDYLTQMKSGVRFFDIRGRASADNMISVHHGM-VYLHHELGKFLDD 121
Cdd:smart00148   1 MDKPLSHYFIPSSHN-----TYLTGKQLWGESSVEGYIQALDAGCRCVELDCWDGPDGEPVIYHGHtFTLPIKLSEVLEA 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581792053   122 AKYYLSAYPNETIVMSMKKD--YDSDSKVTKTFEEIFREYYYNNPQYQNLFYtgsnaNPTLKETKGKIVLFNR 192
Cdd:smart00148  76 IKDFAFVTSPYPVILSLENHcsPDQQAKMAQMFKEIFGDMLYTPPLTSSLEV-----LPSPEQLRGKILLKVR 143
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 41-327 6.22e-51

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: 170.14  E-value: 6.22e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  41 LDESKHLTEINMPGSHDSGSFTLTDPVKSVWAKTQGKDYLTQMKSGVRFFDIRGRASADNMISVHHGMVYLHHELGKFLD 120
Cdd:cd00137    2 HPDTQPLAHYSIPGTHDTYLTAGQFTIKQVWGLTQTEMYRQQLLSGCRCVDIRCWDGKPEEPIIYHGPTFLDIFLKEVIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 121 DAKYYLSAYPNETIVMSMKKDYDSDSKVTKTFEEIFREYYynNPQYQNLFYTGSNANPTLKETKGKIVLFNRMGGTYIKS 200
Cdd:cd00137   82 AIAQFLKKNPPETIIMSLKNEVDSMDSFQAKMAEYCRTIF--GDMLLTPPLKPTVPLPSLEDLRGKILLLNKKNGFSGPT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 201 GYGADTsgiqWADNATFETKInNGSLNLKVQDEYKDYYDKKVEAVKNllAKAKTDSNKDNVYVNFLSVASGGSAFnstYN 280
Cdd:cd00137  160 GSSNDT----GFVSFEFSTQK-NRSYNISSQDEYKAYDDEKVKLIKA--TVQFVDYNKNQLSRNYPSGTSGGTAW---YY 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 581792053 281 YASHINPEIAKTIKENGKARTGWLIVDYAGYPWPgyDDIVSEIIDSN 327
Cdd:cd00137  230 YAMDSNNYMPQMFWNANPAGCGIVILDFQTMDLP--MQQYMAVIEFN 274
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 39-327 8.33e-48

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: 161.88  E-value: 8.33e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  39 SKLDESKHLTEINMPGSHDSGSFTLTD--PVKSVWAKTQGKDYLTQMKSGVRFFDIR-GRASADNMISVHHGMVYL-HHE 114
Cdd:cd08557    1 PALLDDLPLSQLSIPGTHNSYAYTIDGnsPIVSKWSKTQDLSITDQLDAGVRYLDLRvAYDPDDGDLYVCHGLFLLnGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 115 LGKFLDDAKYYLSAYPNETIVMSMKKDYDSDSK-VTKTFEEIFREYYYNnpqYQNLFYTGSNANPTLKE-TKGKIVLFNR 192
Cdd:cd08557   81 LEDVLNEVKDFLDAHPSEVVILDLEHEYGGDNGeDHDELDALLRDVLGD---PLYRPPVRAGGWPTLGElRAGKRVLLFY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 193 mggtyiksgygadtsgiqwadNATFETKINNGSLNLKVQDEYKDYYDKKVEAVKNLLAKAKTDSNKDNVYVNFLSVASGG 272
Cdd:cd08557  158 ---------------------FGGDDSSGGYDWGSLNIQDPYANGTDKLESLKAFLNSALASPRSADFFYVNQASLTPGR 216

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 273 SAF---NSTYNYASHINPEIAKTIKEN--GKARTGWLIVDYagypwPGYDDIVSEIIDSN 327
Cdd:cd08557  217 ITIavaGSLYTVATRANPALYEWLKEDgsGASGPNIVATDF-----VDVGDLIDAVIRLN 271
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 51-191 5.91e-31

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: 113.75  E-value: 5.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053   51 NMPGSHDSGSFTLTDPVKS--VWAKTQGKDYLTQMKSGVRFFDIRGRASADNMISVHHGMVYL-HHELGKFLDDAKYYLS 127
Cdd:pfam00388   2 SQPLSHYFISSSHNTYLTGdqLTGESSVEAYIRALLRGCRCVELDCWDGPDGEPVVYHGYTLTsKIPFRDVLEAIKDYAF 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581792053  128 AYPNETIVMSMKKDY--DSDSKVTKTFEEIFREYYYNNPQYQnlfytGSNANPTLKETKGKIVLFN 191
Cdd:pfam00388  82 VTSPYPVILSLENHCspEQQKKMAEILKEIFGDMLYTPPLDD-----DLTELPSPEDLKGKILIKG 142
PI-PLCXDc_like cd08587
Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and ...
 44-327 4.31e-19

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: 85.47  E-value: 4.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  44 SKHLTEINMPGSHDSGSFTLTDP-------------VKSV---WAKTQGKDYLTQMKSGVRFFDIR--GRASADNMISVH 105
Cdd:cd08587    6 DLPLRDLVIPGSHDSGMYTINGDspvgpdqpefgkiAKGIvrkWSVTQSLSIYDQLEAGIRYFDLRvaYKPDSENKLYFV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 106 HGMvYLHHELGKFLDDAKYYLSAYPNETIVMSMKKDYDSDSKVTKTFEEIFREYYYNNPQYQNLfYTGSNANPTLKE--T 183
Cdd:cd08587   86 HGL-YSGEPVDEVLEDVNDFLDEHPKEVVILDFNHFYGMDDKSPEDHEKLVELLEDIFGDKLCP-RDSDLLDVTLADlwE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 184 KGK-IVLFNRmGGTYIKSGYGADTSGIQ--WADNATFEtkinngslnlkvqdeykdyydkkvEAVKNLLAKAKTDSNKDN 260
Cdd:cd08587  164 SGKrVIVFYD-DDLASEGPYLWPSPYIPdpWANTDDPQ------------------------KLIDFLENKLKERRRPDK 218

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581792053 261 VYV-------NFLSVAsGGSAFNSTYNYASHINPEIAKTIKENGKARTGWLIV--DYAGYPwpgydDIVSEIIDSN 327
Cdd:cd08587  219 FFVlqwiltpQASTIV-LGLFSGLLKKLALRANPALLEWLREQLPGQDGPNIIlnDFVDLG-----EFIDLAIALN 288
PI-PLCXDc_like_2 cd08621
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 44-158 3.33e-13

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: 68.94  E-value: 3.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  44 SKHLTEINMPGSHDSGSFTLTD-----PVKSVWAKTQGKDYLTQMKSGVRFFDIRgrasadnMISVHHGMVYLHHELGKF 118
Cdd:cd08621    6 DRPLRHIVMPGTHDSGMSSLTGglwpvDGNDSNTQTQGLSIYDQLRAGARYFDIR-------PVITHGGELWTGHYNGED 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 581792053 119 --------------LDDAKYYLSAYPNETIVMSMKKDYDSDSKV-----TKTFEEIFRE 158
Cdd:cd08621   79 asaqgangeslddiLDEVNRFTDENPGELVILNFSHILNTDNGDgrpfsAEEWEKIFDE 137
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 44-135 2.16e-10

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: 60.33  E-value: 2.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  44 SKHLTEINMPGSHDSGSFTLT-------------------DPVKSV---WAKTQGKDYLTQMKSGVRFFDIR--GRASAD 99
Cdd:cd08616    7 DKPLTNLAIPGSHDSFTYSIDkqspvspdqsvqnlvkvfpCIFKKIvkkWSKTQSLTITEQLEAGIRYFDLRiaTKPKDN 86

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 581792053 100 NMISVHhgMVYlHHELGKFLDDAKYYLSAYPNETIV 135
Cdd:cd08616   87 DLYFVH--GLY-GILVKEILEEINDFLTEHPKEVVI 119
PI-PLCXDc_plant cd08619
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing ...
 27-153 4.38e-09

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: 56.41  E-value: 4.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  27 SDSLSKSPENWMSKL-----DESKHLTEINMPGSHDSGSFTLTDP-VKSVWAKTQGKDYLTQMKSGVRFFDIRgraSADN 100
Cdd:cd08619    4 CDFHTDDHKEWMSLSqlkamDSSLKLRDIVWPGTHDSATNKIGIPkVSRPFARCQSLSIYNQLCSGARVLDIR---VQED 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053 101 mISVHHGMVYlHHELGKFLDDAKYYLSAYPNETIVMSMKKDYDSDS-------KVTKTFE 153
Cdd:cd08619   81 -RRVCHGCLK-TYPVDVVLNDIKRFLSETKSEFVILEIRTEYGHEDppqfdlwLVEQLGD 138
PI-PLCXDc_like_1 cd08620
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 52-141 4.46e-08

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: 53.55  E-value: 4.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  52 MPGSHDSGSFTLTDpvksvWAKTQGKDYLTQMKSGVRFFDIRGrASADNMISVHHGM--VYLHH------ELGKFLDDAK 123
Cdd:cd08620   14 LPGAHDAGMNGMTN-----LSVTQKDNVSTQLALGARYFDFRP-GYLWPQTRVLVLLndLYHQHnmipgqGFDTFLQDVV 87

                         90
                 ....*....|....*...
gi 581792053 124 YYLSAYPNETIVMSMKKD 141
Cdd:cd08620   88 TFLKANPTEIVVVHITWD 105
PTZ00268 PTZ00268
glycosylphosphatidylinositol-specific phospholipase C; Provisional
 33-157 2.60e-06

glycosylphosphatidylinositol-specific phospholipase C; Provisional


Pssm-ID: 140294  Cd Length: 380  Bit Score: 48.73  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  33 SPENWMSKLD---ESKHLTEINMPGSHDSGS---------------FTLTDPVK------------SVWAKTQGKDYLTQ 82
Cdd:PTZ00268  14 HPQSWMHDLRsfiGEMAITQVCLVGSHNAASygihkdspfgadapgFLLGDSVVaslsrflfrgisASWSKCQGMSVRAQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  83 MKSGVRFFDIRGRASADNMISVHHGMVYLHHELGKFLDDAKYYLS--AYPNETIVMSMKKDY---DSDSKvTKTFEEIFR 157
Cdd:PTZ00268  94 LDHGVRYLDLRVATNPEDANRLYISHTQISVPLADVLEDVKAFLNdpSSANEFIVLDFQHLYltdDSDGK-GKFFRELDR 172
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 53-162 6.27e-05

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


Pssm-ID: 176498 [Multi-domain]  Cd Length: 179  Bit Score: 42.81  E-value: 6.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  53 PGSHDSGSFTLTDpvksvwakTQGKDYLTQMKSGVRFFDIRGRASADNMISVHHGM-------VYLHHELGKFLDDAKYY 125
Cdd:cd08555    1 VLSHRGYSQNGQE--------NTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPtldrttaGILPPTLEEVLELIADY 72

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 581792053 126 LSaYPNETIVMSMKKDYDSDS--KVTKTFEEIFREYYYN 162
Cdd:cd08555   73 LK-NPDYTIILSLEIKQDSPEydEFLAKVLKELRVYFDY 110
PI-PLCXDc_CG14945_like cd08622
Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to ...
 47-136 7.32e-05

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: 43.86  E-value: 7.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581792053  47 LTEINMPGSHDSGSFTLTDPVKSVWAK----TQGKDYLTQMKSGVRFFDIR---GRASADNMISVHHGMvyLHHELGKFL 119
Cdd:cd08622    9 IKDLFIPGTHNSAAYDTNSNANESLVDkyllTQDLDIWTQLVHGIRYLDLRvgyYPDSPDNFWINHDLV--RIVPLLTVL 86

                         90
                 ....*....|....*..
gi 581792053 120 DDAKYYLSAyPNETIVM 136
Cdd:cd08622   87 NDVRNFVQN-TGEIVVL 102
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH