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Conserved domains on  [gi|18425155|ref|NP_569045|]
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PLC-like phosphodiesterases superfamily protein [Arabidopsis thaliana]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 71-346 9.78e-114

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: 334.30  E-value: 9.78e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155  71 TSPTSIINGLPFNKYTWLMTHNAFSNANAPllpgveRITFYNQEDTITNQLQNGVRGLMLDMYDFNNDIWLCHSLRGQCf 150
Cdd:cd08588   1 CNGSPALCDRTYDEYTFLTTHNSFANSEDA------FFLAPNQEDDITKQLDDGVRGLMLDIHDANGGLRLCHSVCGLG- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155 151 nftAFQPAINILREVEAFLSQNPTEIVTIIIEDYVHR-PKGLSTLFANAGLDKYWFPVSKMPRKGEDWPTVTDMVQENHR 229
Cdd:cd08588  74 ---DGGPLSDVLREVVDFLDANPNEVVTLFLEDYVSPgPLLRSKLFRVAGLTDLVYVPDAMPWAGSDWPTLGEMIDANKR 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155 230 LLVFTSVAAKE-DEEGVAYQWRYMVENESGDPGVKRGSCPNRKESQPLNSKS---SSLFLMNYFPTYPVEKDA--CKEHS 303
Cdd:cd08588 151 LLVFTDNEDVStEPPGVMYQFDYTVENPFSVGGDDDWSCTVRRGSGPLSRIApgfRRLFLMNHFRDVPVPITAanDNNGD 230

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 18425155 304 APLAEMVGTCLKSGGNRMPNFLAVNFYMRsdgGGVFEILDRMN 346
Cdd:cd08588 231 GLLLRHLNNCRPAAGGRKPNFVAVDFYNI---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 ...
 71-346 9.78e-114

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: 334.30  E-value: 9.78e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155  71 TSPTSIINGLPFNKYTWLMTHNAFSNANAPllpgveRITFYNQEDTITNQLQNGVRGLMLDMYDFNNDIWLCHSLRGQCf 150
Cdd:cd08588   1 CNGSPALCDRTYDEYTFLTTHNSFANSEDA------FFLAPNQEDDITKQLDDGVRGLMLDIHDANGGLRLCHSVCGLG- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155 151 nftAFQPAINILREVEAFLSQNPTEIVTIIIEDYVHR-PKGLSTLFANAGLDKYWFPVSKMPRKGEDWPTVTDMVQENHR 229
Cdd:cd08588  74 ---DGGPLSDVLREVVDFLDANPNEVVTLFLEDYVSPgPLLRSKLFRVAGLTDLVYVPDAMPWAGSDWPTLGEMIDANKR 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155 230 LLVFTSVAAKE-DEEGVAYQWRYMVENESGDPGVKRGSCPNRKESQPLNSKS---SSLFLMNYFPTYPVEKDA--CKEHS 303
Cdd:cd08588 151 LLVFTDNEDVStEPPGVMYQFDYTVENPFSVGGDDDWSCTVRRGSGPLSRIApgfRRLFLMNHFRDVPVPITAanDNNGD 230

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 18425155 304 APLAEMVGTCLKSGGNRMPNFLAVNFYMRsdgGGVFEILDRMN 346
Cdd:cd08588 231 GLLLRHLNNCRPAAGGRKPNFVAVDFYNI---GDAFEAVDELN 270
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 113-183 3.82e-03

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: 37.65  E-value: 3.82e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18425155    113 QEDTITNQLQNGVRGLMLDMYD-FNNDIWLCHSlrgqcFNFTAFQPAINILREVEAFLSQNPTEIVTIIIED 183
Cdd:smart00148  28 SVEGYIQALDAGCRCVELDCWDgPDGEPVIYHG-----HTFTLPIKLSEVLEAIKDFAFVTSPYPVILSLEN 94
 
Name Accession Description Interval E-value
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 71-346 9.78e-114

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: 334.30  E-value: 9.78e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155  71 TSPTSIINGLPFNKYTWLMTHNAFSNANAPllpgveRITFYNQEDTITNQLQNGVRGLMLDMYDFNNDIWLCHSLRGQCf 150
Cdd:cd08588   1 CNGSPALCDRTYDEYTFLTTHNSFANSEDA------FFLAPNQEDDITKQLDDGVRGLMLDIHDANGGLRLCHSVCGLG- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155 151 nftAFQPAINILREVEAFLSQNPTEIVTIIIEDYVHR-PKGLSTLFANAGLDKYWFPVSKMPRKGEDWPTVTDMVQENHR 229
Cdd:cd08588  74 ---DGGPLSDVLREVVDFLDANPNEVVTLFLEDYVSPgPLLRSKLFRVAGLTDLVYVPDAMPWAGSDWPTLGEMIDANKR 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155 230 LLVFTSVAAKE-DEEGVAYQWRYMVENESGDPGVKRGSCPNRKESQPLNSKS---SSLFLMNYFPTYPVEKDA--CKEHS 303
Cdd:cd08588 151 LLVFTDNEDVStEPPGVMYQFDYTVENPFSVGGDDDWSCTVRRGSGPLSRIApgfRRLFLMNHFRDVPVPITAanDNNGD 230

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 18425155 304 APLAEMVGTCLKSGGNRMPNFLAVNFYMRsdgGGVFEILDRMN 346
Cdd:cd08588 231 GLLLRHLNNCRPAAGGRKPNFVAVDFYNI---GDAFEAVDELN 270
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 75-346 5.68e-46

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: 159.95  E-value: 5.68e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155  75 SIINGLPFNKYTWLMTHNAFSNANAPLLPGVERITfYNQEDTITNQLQNGVRGLMLDM--YDFNNDIWLCHSLRGQCFnf 152
Cdd:cd08557   2 ALLDDLPLSQLSIPGTHNSYAYTIDGNSPIVSKWS-KTQDLSITDQLDAGVRYLDLRVayDPDDGDLYVCHGLFLLNG-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155 153 tafQPAINILREVEAFLSQNPTEIVTIIIEDYVHRPKGLSTLFANAGLDKYWFPVSKMPRKGED-WPTVTDMVQeNHRLL 231
Cdd:cd08557  79 ---QTLEDVLNEVKDFLDAHPSEVVILDLEHEYGGDNGEDHDELDALLRDVLGDPLYRPPVRAGgWPTLGELRA-GKRVL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155 232 VFTSVAAkeDEEGVAYQWRYMVENESGDPGVKRGSCPNRKESQPLNSKSSSLFLMNYFPTYPVEKDACKEHS-----APL 306
Cdd:cd08557 155 LFYFGGD--DSSGGYDWGSLNIQDPYANGTDKLESLKAFLNSALASPRSADFFYVNQASLTPGRITIAVAGSlytvaTRA 232

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 18425155 307 AEMVGTCLK--SGGNRMPNFLAVNFYmrsDGGGVFEILDRMN 346
Cdd:cd08557 233 NPALYEWLKedGSGASGPNIVATDFV---DVGDLIDAVIRLN 271
PI-PLCc_Rv2075c_like cd08590
Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This ...
 78-266 8.08e-18

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: 82.84  E-value: 8.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155  78 NGLPFNKYTWLMTHNAF---SNANAPLLPGVeRITFYNQEDTITNQLQNGVRGLMLDMYDFNNDIWLCHSL-RGQCFNFT 153
Cdd:cd08590   6 SNAPLCQAQILGTHNSYnsrAYGYGNRYHGV-RYLDPNQELSITDQLDLGARFLELDVHWTTGDLRLCHGGdHGYLGVCS 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155 154 AFQPAIN-ILREVEAFLSQNPTEIVTIIIEDY--VHRPKGLSTLFANAGLDKYWFPVSKMPRKGE-DWPTVTDMVQENHR 229
Cdd:cd08590  85 SEDRLFEdGLNEIADWLNANPDEVVILYLEDHgdGGKDDELNALLNDAFGDLLYTPSDCDDLQGLpNWPTKEDMLNSGKQ 164

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 18425155 230 LLVFTSvaakeDEEGVAYQWRYMVENESGDPGVKRGS 266
Cdd:cd08590 165 VVLATG-----GGCSGAQGMYNRKEFADTQPSNFRPY 196
PI-PLCXDc_like cd08587
Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and ...
 75-233 5.05e-10

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: 60.05  E-value: 5.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155  75 SIINGLPFNKYTWLMTHNAFS---NANAPLLPGVERITFY----------NQEDTITNQLQNGVRglmldmY-DF----- 135
Cdd:cd08587   2 SAIGDLPLRDLVIPGSHDSGMytiNGDSPVGPDQPEFGKIakgivrkwsvTQSLSIYDQLEAGIR------YfDLrvayk 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155 136 ---NNDIWLCHslrgqcfNFTAFQPAINILREVEAFLSQNPTEIVTI-IIEDYVHRPKG----------LSTLFANAGLd 201
Cdd:cd08587  76 pdsENKLYFVH-------GLYSGEPVDEVLEDVNDFLDEHPKEVVILdFNHFYGMDDKSpedheklvelLEDIFGDKLC- 147

                       170       180       190
                ....*....|....*....|....*....|...
gi 18425155 202 kywfpvskmPRKGEDW-PTVTDMVQENHRLLVF 233
Cdd:cd08587 148 ---------PRDSDLLdVTLADLWESGKRVIVF 171
PI-PLCc_BcPLC_like cd08586
Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar ...
 112-223 1.40e-08

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: 55.75  E-value: 1.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155 112 NQEDTITNQLQNGVRglMLDM---YDFNNDIWLCHslrGQCFNFTAFQpaiNILREVEAFLSQNPTEivTIII---EDYv 185
Cdd:cd08586  34 CQDWSIAEQLNAGIR--FLDIrlrLIDNNDLAIHH---GPFYQGLTFG---DVLNECYSFLDANPSE--TIIMslkQEG- 102

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 18425155 186 hRPKGLSTLFANAGLDKYWFPVSKMPRKGEDWPTVTDM 223
Cdd:cd08586 103 -SGDGNTDSFAEIFKEYLDNYPSYFYYTESKIPTLGEV 139
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 90-177 2.42e-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: 42.61  E-value: 2.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155  90 THNAFS---NANAPLLPGVERITFY----------------NQEDTITNQLQNGVR--GLMLDMYDFNNDIWLCHSLRGQ 148
Cdd:cd08616  18 SHDSFTysiDKQSPVSPDQSVQNLVkvfpcifkkivkkwskTQSLTITEQLEAGIRyfDLRIATKPKDNDLYFVHGLYGI 97

                        90       100
                ....*....|....*....|....*....
gi 18425155 149 CFNftafqpaiNILREVEAFLSQNPTEIV 177
Cdd:cd08616  98 LVK--------EILEEINDFLTEHPKEVV 118
PI-PLCXDc_like_1 cd08620
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 96-181 2.72e-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: 42.38  E-value: 2.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18425155  96 NANAPL----LPGVERITFY-------NQEDTITNQLQNGVRglmldMYDF-----NNDIWLCHSLRGQCF--NFTAFQP 157
Cdd:cd08620   4 PAQQPFnrfvLPGAHDAGMNgmtnlsvTQKDNVSTQLALGAR-----YFDFrpgylWPQTRVLVLLNDLYHqhNMIPGQG 78

                        90       100
                ....*....|....*....|....
gi 18425155 158 AINILREVEAFLSQNPTEIVTIII 181
Cdd:cd08620  79 FDTFLQDVVTFLKANPTEIVVVHI 102
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 113-183 3.82e-03

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: 37.65  E-value: 3.82e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18425155    113 QEDTITNQLQNGVRGLMLDMYD-FNNDIWLCHSlrgqcFNFTAFQPAINILREVEAFLSQNPTEIVTIIIED 183
Cdd:smart00148  28 SVEGYIQALDAGCRCVELDCWDgPDGEPVIYHG-----HTFTLPIKLSEVLEAIKDFAFVTSPYPVILSLEN 94
 
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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