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Conserved domains on  [gi|8920573|gb|AAF81295|]
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Contains similarity to MAP3K-like protein kinase from Arabidopsis thaliana gb|Z99707 [Arabidopsis thaliana]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 66-333 7.93e-113

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: 328.91  E-value: 7.93e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573   66 QFSIVNNSMPFNKYAFLTTHNSYAIEGKA-LHVATQEDTIVQQLNSGVRALMLDTYDYEGDVWFCHSFDEQCfeftKFNR 144
Cdd:cd08588   2 NGSPALCDRTYDEYTFLTTHNSFANSEDAfFLAPNQEDDITKQLDDGVRGLMLDIHDANGGLRLCHSVCGLG----DGGP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573  145 AIDTFKEIFAFLTANPSEIVTLILEDYVKS-QNGLTKVFTDSGLKKFWFPVQNMPIGGQDWPLVKDMVANNHRLIVFTSA 223
Cdd:cd08588  78 LSDVLREVVDFLDANPNEVVTLFLEDYVSPgPLLRSKLFRVAGLTDLVYVPDAMPWAGSDWPTLGEMIDANKRLLVFTDN 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573  224 KSKQ-ETEGIAYQWNYMVENQYGDDGVKPDECSNRADSALLTDKT---KALVSVNHFKTVPVKILT--CEENSEQLLDMI 297
Cdd:cd08588 158 EDVStEPPGVMYQFDYTVENPFSVGGDDDWSCTVRRGSGPLSRIApgfRRLFLMNHFRDVPVPITAanDNNGDGLLLRHL 237

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 8920573  298 KTCYVAAGNRWANFVAVNFYKRsngGGTFQAIDKLN 333
Cdd:cd08588 238 NNCRPAAGGRKPNFVAVDFYNI---GDAFEAVDELN 270
 
Name Accession Description Interval E-value
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 66-333 7.93e-113

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: 328.91  E-value: 7.93e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573   66 QFSIVNNSMPFNKYAFLTTHNSYAIEGKA-LHVATQEDTIVQQLNSGVRALMLDTYDYEGDVWFCHSFDEQCfeftKFNR 144
Cdd:cd08588   2 NGSPALCDRTYDEYTFLTTHNSFANSEDAfFLAPNQEDDITKQLDDGVRGLMLDIHDANGGLRLCHSVCGLG----DGGP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573  145 AIDTFKEIFAFLTANPSEIVTLILEDYVKS-QNGLTKVFTDSGLKKFWFPVQNMPIGGQDWPLVKDMVANNHRLIVFTSA 223
Cdd:cd08588  78 LSDVLREVVDFLDANPNEVVTLFLEDYVSPgPLLRSKLFRVAGLTDLVYVPDAMPWAGSDWPTLGEMIDANKRLLVFTDN 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573  224 KSKQ-ETEGIAYQWNYMVENQYGDDGVKPDECSNRADSALLTDKT---KALVSVNHFKTVPVKILT--CEENSEQLLDMI 297
Cdd:cd08588 158 EDVStEPPGVMYQFDYTVENPFSVGGDDDWSCTVRRGSGPLSRIApgfRRLFLMNHFRDVPVPITAanDNNGDGLLLRHL 237

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 8920573  298 KTCYVAAGNRWANFVAVNFYKRsngGGTFQAIDKLN 333
Cdd:cd08588 238 NNCRPAAGGRKPNFVAVDFYNI---GDAFEAVDELN 270
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 75-183 9.67e-05

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


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 41.88  E-value: 9.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573      75 PFNKYAFLTTHNSYAIeGKALHVATQEDTIVQQLNSGVRALMLDTYDYE-GDVWFCHSFDeqcfeFT---KFNRAIDTFK 150
Cdd:smart00148   4 PLSHYFIPSSHNTYLT-GKQLWGESSVEGYIQALDAGCRCVELDCWDGPdGEPVIYHGHT-----FTlpiKLSEVLEAIK 77

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 8920573     151 EifaFLTANPSEIVTLILEDYVK--SQNGLTKVFT 183
Cdd:smart00148  78 D---FAFVTSPYPVILSLENHCSpdQQAKMAQMFK 109
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 73-184 8.27e-03

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: 36.33  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573     73 SMPFNKYAFLTTHNSYaIEGKALHVATQEDTIVQQLNSGVRALMLDTYDYE-GDVWFCHSfdeqcFEFT---KFNRAIDT 148
Cdd:pfam00388   2 SQPLSHYFISSSHNTY-LTGDQLTGESSVEAYIRALLRGCRCVELDCWDGPdGEPVVYHG-----YTLTskiPFRDVLEA 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 8920573    149 FKEiFAFltANPSEIVTLILEDY--VKSQNGLTKVFTD 184
Cdd:pfam00388  76 IKD-YAF--VTSPYPVILSLENHcsPEQQKKMAEILKE 110
 
Name Accession Description Interval E-value
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 66-333 7.93e-113

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: 328.91  E-value: 7.93e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573   66 QFSIVNNSMPFNKYAFLTTHNSYAIEGKA-LHVATQEDTIVQQLNSGVRALMLDTYDYEGDVWFCHSFDEQCfeftKFNR 144
Cdd:cd08588   2 NGSPALCDRTYDEYTFLTTHNSFANSEDAfFLAPNQEDDITKQLDDGVRGLMLDIHDANGGLRLCHSVCGLG----DGGP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573  145 AIDTFKEIFAFLTANPSEIVTLILEDYVKS-QNGLTKVFTDSGLKKFWFPVQNMPIGGQDWPLVKDMVANNHRLIVFTSA 223
Cdd:cd08588  78 LSDVLREVVDFLDANPNEVVTLFLEDYVSPgPLLRSKLFRVAGLTDLVYVPDAMPWAGSDWPTLGEMIDANKRLLVFTDN 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573  224 KSKQ-ETEGIAYQWNYMVENQYGDDGVKPDECSNRADSALLTDKT---KALVSVNHFKTVPVKILT--CEENSEQLLDMI 297
Cdd:cd08588 158 EDVStEPPGVMYQFDYTVENPFSVGGDDDWSCTVRRGSGPLSRIApgfRRLFLMNHFRDVPVPITAanDNNGDGLLLRHL 237

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 8920573  298 KTCYVAAGNRWANFVAVNFYKRsngGGTFQAIDKLN 333
Cdd:cd08588 238 NNCRPAAGGRKPNFVAVDFYNI---GDAFEAVDELN 270
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 71-333 8.50e-47

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: 159.57  E-value: 8.50e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573   71 NNSMPFNKYAFLTTHNSYAIEGKALH------VATQEDTIVQQLNSGVRALMLDTYDY--EGDVWFCHSFDEQCFEFtkf 142
Cdd:cd08557   4 LDDLPLSQLSIPGTHNSYAYTIDGNSpivskwSKTQDLSITDQLDAGVRYLDLRVAYDpdDGDLYVCHGLFLLNGQT--- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573  143 nrAIDTFKEIFAFLTANPSEIVTLILEDYVKSQNGLTKVFTDSGLKKFWFPVQNMPIGGQD-WPLVKDMVAnNHRLIVFT 221
Cdd:cd08557  81 --LEDVLNEVKDFLDAHPSEVVILDLEHEYGGDNGEDHDELDALLRDVLGDPLYRPPVRAGgWPTLGELRA-GKRVLLFY 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573  222 SAKSKQetEGIAYQWNYMVENQYGDDGVKPDECSNRADSALLTDKTKALVSVNHFKTVPVKILTC-----EENSEQLLDM 296
Cdd:cd08557 158 FGGDDS--SGGYDWGSLNIQDPYANGTDKLESLKAFLNSALASPRSADFFYVNQASLTPGRITIAvagslYTVATRANPA 235

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 8920573  297 IKTCYVAAGN--RWANFVAVNFYkrsNGGGTFQAIDKLN 333
Cdd:cd08557 236 LYEWLKEDGSgaSGPNIVATDFV---DVGDLIDAVIRLN 271
PI-PLCc_Rv2075c_like cd08590
Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This ...
 70-224 8.82e-14

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: 70.51  E-value: 8.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573   70 VNNSMPFNKYAFLTTHNSY---------AIEGKALHVATQEDTIVQQLNSGVRALMLDTYDYEGDVWFCHSFDEQ--CFE 138
Cdd:cd08590   4 LDSNAPLCQAQILGTHNSYnsraygygnRYHGVRYLDPNQELSITDQLDLGARFLELDVHWTTGDLRLCHGGDHGylGVC 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573  139 FTKFNRAIDTFKEIFAFLTANPSEIVTLILEDYV------------KSQNGlTKVFTDSGLKKFwfpvqnmpIGGQDWPL 206
Cdd:cd08590  84 SSEDRLFEDGLNEIADWLNANPDEVVILYLEDHGdggkddelnallNDAFG-DLLYTPSDCDDL--------QGLPNWPT 154

                       170
                ....*....|....*...
gi 8920573  207 VKDMVANNHRLIVFTSAK 224
Cdd:cd08590 155 KEDMLNSGKQVVLATGGG 172
PI-PLCXDc_like cd08587
Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and ...
 99-220 4.14e-07

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: 50.80  E-value: 4.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573   99 TQEDTIVQQLNSGVRalmldtY---------DYEGDVWFCHSFDEQCfeftkfnrAIDTF-KEIFAFLTANPSEIVTL-I 167
Cdd:cd08587  52 TQSLSIYDQLEAGIR------YfdlrvaykpDSENKLYFVHGLYSGE--------PVDEVlEDVNDFLDEHPKEVVILdF 117

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8920573  168 LEDYVKSQNG----------LTKVFTDSGLkkfwfpvqnmPIGGQDW-PLVKDMVANNHRLIVF 220
Cdd:cd08587 118 NHFYGMDDKSpedheklvelLEDIFGDKLC----------PRDSDLLdVTLADLWESGKRVIVF 171
PI-PLCc_BcPLC_like cd08586
Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar ...
 84-210 9.72e-06

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: 46.51  E-value: 9.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573   84 THNSYAIEGKALHVA-TQEDTIVQQLNSGVRAlmLD---TYDYEGDVWFCHSfdeQCFEFTKFNraiDTFKEIFAFLTAN 159
Cdd:cd08586  18 THDSGALHGGLSSSVqCQDWSIAEQLNAGIRF--LDirlRLIDNNDLAIHHG---PFYQGLTFG---DVLNECYSFLDAN 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 8920573  160 PSEIVTLIL-EDYvkSQNGLTKVFTDSGLKKFWFPVQNMPIGGQDWPLVKDM 210
Cdd:cd08586  90 PSETIIMSLkQEG--SGDGNTDSFAEIFKEYLDNYPSYFYYTESKIPTLGEV 139
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 75-183 9.67e-05

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


Pssm-ID: 197543 [Multi-domain]  Cd Length: 143  Bit Score: 41.88  E-value: 9.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573      75 PFNKYAFLTTHNSYAIeGKALHVATQEDTIVQQLNSGVRALMLDTYDYE-GDVWFCHSFDeqcfeFT---KFNRAIDTFK 150
Cdd:smart00148   4 PLSHYFIPSSHNTYLT-GKQLWGESSVEGYIQALDAGCRCVELDCWDGPdGEPVIYHGHT-----FTlpiKLSEVLEAIK 77

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 8920573     151 EifaFLTANPSEIVTLILEDYVK--SQNGLTKVFT 183
Cdd:smart00148  78 D---FAFVTSPYPVILSLENHCSpdQQAKMAQMFK 109
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 73-182 1.13e-04

Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This subfamily corresponds to the catalytic domain present in prokaryotic and eukaryotic phosphoinositide-specific phospholipase C (PI-PLC), which is a ubiquitous enzyme catalyzing the cleavage of the sn3-phosphodiester bond in the membrane phosphoinositides (phosphatidylinositol, PI; Phosphatidylinositol-4-phosphate, PIP; phosphatidylinositol 4,5-bisphosphate, PIP2) to yield inositol phosphates (inositol monosphosphate, InsP; inositol diphosphate, InsP2; inositol trisphosphate, InsP3) and diacylglycerol (DAG). The higher eukaryotic PI-PLCs (EC 3.1.4.11) have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. They play a critical role in most signal transduction pathways, controlling numerous cellular events, such as cell growth, proliferation, excitation and secretion. These PI-PLCs strictly require Ca2+ for their catalytic activity. They display a clear preference towards the hydrolysis of the more highly phosphorylated PI-analogues, PIP2 and PIP, to generate two important second messengers, InsP3 and DAG. InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. In contrast, bacterial PI-PLCs contain a single catalytic domain. Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. They participate in Ca2+-independent PI metabolism. They are characterized as phosphatidylinositol-specific phospholipase C (EC 4.6.1.13) that selectively hydrolyze PI, not PIP or PIP2. The TIM-barrel type catalytic domain in bacterial PI-PLCs is very similar to the one in eukaryotic PI-PLCs, in which the catalytic domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. The catalytic mechanism of both prokaryotic and eukaryotic PI-PLCs is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes a distinctly different type of eukaryotic PLC, glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC), an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG), releasing dimyristyl glycerol (DMG), which may facilitate the evasion of the protozoan to the host#s immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs, but not mammalian PI-PLCs.


Pssm-ID: 176497 [Multi-domain]  Cd Length: 274  Bit Score: 43.41  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573   73 SMPFNKYAFLTTHNSYAIEG----KALHVATQEDTIVQQLNSGVRALMLDTYDYEGDVWFCHsfdeQCFEFTK--FNRAI 146
Cdd:cd00137   5 TQPLAHYSIPGTHDTYLTAGqftiKQVWGLTQTEMYRQQLLSGCRCVDIRCWDGKPEEPIIY----HGPTFLDifLKEVI 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 8920573  147 DTFKEifaFLTANPSEIVTLILEDYVKSQNGLTKVF 182
Cdd:cd00137  81 EAIAQ---FLKKNPPETIIMSLKNEVDSMDSFQAKM 113
PI-PLCXDc_like_1 cd08620
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 75-166 3.81e-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: 41.61  E-value: 3.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573   75 PFNKYAFLTTHNS--YAIEGKALhvaTQEDTIVQQLNSGVRAL---------MLDTYDYEGDVWFCHSFDEqcfeftkfN 143
Cdd:cd08620   8 PFNRFVLPGAHDAgmNGMTNLSV---TQKDNVSTQLALGARYFdfrpgylwpQTRVLVLLNDLYHQHNMIP--------G 76

                        90       100
                ....*....|....*....|....
gi 8920573  144 RAIDTF-KEIFAFLTANPSEIVTL 166
Cdd:cd08620  77 QGFDTFlQDVVTFLKANPTEIVVV 100
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 99-166 4.74e-04

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: 41.46  E-value: 4.74e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8920573   99 TQEDTIVQQLNSGVR--ALMLDTYDYEGDVWFCHS-FDEQCFEFtkfnraidtFKEIFAFLTANPSEIVTL 166
Cdd:cd08616  59 TQSLTITEQLEAGIRyfDLRIATKPKDNDLYFVHGlYGILVKEI---------LEEINDFLTEHPKEVVIL 120
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 73-184 8.27e-03

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: 36.33  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8920573     73 SMPFNKYAFLTTHNSYaIEGKALHVATQEDTIVQQLNSGVRALMLDTYDYE-GDVWFCHSfdeqcFEFT---KFNRAIDT 148
Cdd:pfam00388   2 SQPLSHYFISSSHNTY-LTGDQLTGESSVEAYIRALLRGCRCVELDCWDGPdGEPVVYHG-----YTLTskiPFRDVLEA 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 8920573    149 FKEiFAFltANPSEIVTLILEDY--VKSQNGLTKVFTD 184
Cdd:pfam00388  76 IKD-YAF--VTSPYPVILSLENHcsPEQQKKMAEILKE 110
 
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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