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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813  27 LCPRLWDVPLHHLSIPGSHDTMTYCLNKKSPISHEESrlLQLLNKALPCITRPVVLKWSVTQALDVTEQLDAGVRYLDLR 106
Cdd:cd08616     1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQS--VQNLVKVFPCIFKKIVKKWSKTQSLTITEQLEAGIRYFDLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813 107 IAHMLEgsEKNLHFVHMVYTTALVE--------------EV--------------------------------------- 133
Cdd:cd08616    79 IATKPK--DNDLYFVHGLYGILVKEileeindfltehpkEVvildfnhfygmteedhekllkmiksifgkklcprdpdll 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813 134 -PTLRQLWSRGQQVIVSYED-ESSLRRHHELWPGVPYWWGNRVKTEALIRYLETMKSCGRPGGLFVAGINLTENLQYVL- 210
Cdd:cd08616   157 nVTLEYLWEKGYQVIVFYHDpVAKKPPYLWPSDAIPSPWPNTTDPKKLIQFLETTLKERRPPGFHVSQGILTPDVKTILr 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1634229813 211 AHPSESLEKMTLPNLPRLSAWVREQCPGPGSrCTNIIAGDFIGADGFVSDVIALN 265
Cdd:cd08616   237 HLTSGLLKTLTLRALPKLLEWLRKQEPGSGQ-GVNIIIADFVDLDEFIDTVIALN 290

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813  27 LCPRLWDVPLHHLSIPGSHDTMTYCLNKKSPISHEESrlLQLLNKALPCITRPVVLKWSVTQALDVTEQLDAGVRYLDLR 106
Cdd:cd08616     1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQS--VQNLVKVFPCIFKKIVKKWSKTQSLTITEQLEAGIRYFDLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813 107 IAHMLEgsEKNLHFVHMVYTTALVE--------------EV--------------------------------------- 133
Cdd:cd08616    79 IATKPK--DNDLYFVHGLYGILVKEileeindfltehpkEVvildfnhfygmteedhekllkmiksifgkklcprdpdll 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813 134 -PTLRQLWSRGQQVIVSYED-ESSLRRHHELWPGVPYWWGNRVKTEALIRYLETMKSCGRPGGLFVAGINLTENLQYVL- 210
Cdd:cd08616   157 nVTLEYLWEKGYQVIVFYHDpVAKKPPYLWPSDAIPSPWPNTTDPKKLIQFLETTLKERRPPGFHVSQGILTPDVKTILr 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1634229813 211 AHPSESLEKMTLPNLPRLSAWVREQCPGPGSrCTNIIAGDFIGADGFVSDVIALN 265
Cdd:cd08616   237 HLTSGLLKTLTLRALPKLLEWLRKQEPGSGQ-GVNIIIADFVDLDEFIDTVIALN 290

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1634229813   33 DVPLHHLSIPGSHDTmtyclnkkspisheesrllQLLNKALpcitrpvvlkWSVTQALDVTEQLDAGVRYLDLRI 107
Cdd:smart00148   2 DKPLSHYFIPSSHNT-------------------YLTGKQL----------WGESSVEGYIQALDAGCRCVELDC 47

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813  27 LCPRLWDVPLHHLSIPGSHDTMTYCLNKKSPISHEESrlLQLLNKALPCITRPVVLKWSVTQALDVTEQLDAGVRYLDLR 106
Cdd:cd08616     1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQS--VQNLVKVFPCIFKKIVKKWSKTQSLTITEQLEAGIRYFDLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813 107 IAHMLEgsEKNLHFVHMVYTTALVE--------------EV--------------------------------------- 133
Cdd:cd08616    79 IATKPK--DNDLYFVHGLYGILVKEileeindfltehpkEVvildfnhfygmteedhekllkmiksifgkklcprdpdll 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813 134 -PTLRQLWSRGQQVIVSYED-ESSLRRHHELWPGVPYWWGNRVKTEALIRYLETMKSCGRPGGLFVAGINLTENLQYVL- 210
Cdd:cd08616   157 nVTLEYLWEKGYQVIVFYHDpVAKKPPYLWPSDAIPSPWPNTTDPKKLIQFLETTLKERRPPGFHVSQGILTPDVKTILr 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1634229813 211 AHPSESLEKMTLPNLPRLSAWVREQCPGPGSrCTNIIAGDFIGADGFVSDVIALN 265
Cdd:cd08616   237 HLTSGLLKTLTLRALPKLLEWLRKQEPGSGQ-GVNIIIADFVDLDEFIDTVIALN 290

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813  29 PRLWDVPLHHLSIPGSHDTMTYCLNKKSPIsheesrllqllnkalpcitrpvVLKWSVTQALDVTEQLDAGVRYLDLRIA 108
Cdd:cd08557     2 ALLDDLPLSQLSIPGTHNSYAYTIDGNSPI----------------------VSKWSKTQDLSITDQLDAGVRYLDLRVA 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813 109 HMleGSEKNLHFVHMVYTTA--LVEEV----------------------------------------------------- 133
Cdd:cd08557    60 YD--PDDGDLYVCHGLFLLNgqTLEDVlnevkdfldahpsevvildleheyggdngedhdeldallrdvlgdplyrppvr 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813 134 ----PTLRQLWsRGQQVIVSYEDESSLRR-HHELWPGVPYWWGN-RVKTEALIRYLETMKSCGR-PGGLFVAGINLTENL 206
Cdd:cd08557   138 aggwPTLGELR-AGKRVLLFYFGGDDSSGgYDWGSLNIQDPYANgTDKLESLKAFLNSALASPRsADFFYVNQASLTPGR 216

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1634229813 207 QYVLAHPseSLEKMTLPNLPRLSAWVREQcpGPGSRCTNIIAGDFIGADGFVSDVIALN 265
Cdd:cd08557   217 ITIAVAG--SLYTVATRANPALYEWLKED--GSGASGPNIVATDFVDVGDLIDAVIRLN 271

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813  24 MSALCPrlwDVPLHHLSIPGSHDTMTYclnkkspisheesrllqllNKALPCITRpvvlkwsvTQALDVTEQLDAGVRYL 103
Cdd:cd08586     1 MSALPD---DTPLSELSIPGTHDSGAL-------------------HGGLSSSVQ--------CQDWSIAEQLNAGIRFL 50

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1634229813 104 DLRIAHMLEGsekNLHFVH-MVYTTALVEEV 133
Cdd:cd08586    51 DIRLRLIDNN---DLAIHHgPFYQGLTFGDV 78

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634229813  33 DVPLHHLSIPGSHDTMTYClnkkspisheesrlLQLlnkalpcitrPVVLKWSVTQALDVTEQLDAGVRYLDLRiAHMLE 112
Cdd:cd00137     5 TQPLAHYSIPGTHDTYLTA--------------GQF----------TIKQVWGLTQTEMYRQQLLSGCRCVDIR-CWDGK 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1634229813 113 GSEKNLHfvH-MVYTTALVEEV-PTLRQLWSRG--QQVIVSYEDESSL 156
Cdd:cd00137    60 PEEPIIY--HgPTFLDIFLKEViEAIAQFLKKNppETIIMSLKNEVDS 105

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1634229813   33 DVPLHHLSIPGSHDTmtyclnkkspisheesrllQLLNKALpcitrpvvlkWSVTQALDVTEQLDAGVRYLDLRI 107
Cdd:smart00148   2 DKPLSHYFIPSSHNT-------------------YLTGKQL----------WGESSVEGYIQALDAGCRCVELDC 47