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Conserved domains on  [gi|1622969921|ref|XP_014982342|]
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PI-PLC X domain-containing protein 1 [Macaca mulatta]

Protein Classification

PI-PLC X domain-containing protein( domain architecture ID 10171267)

PI-PLC (phosphatidylinositol-specific phospholipase C) X domain-containing protein belongs to a small family of receptor-regulated phosphodiesterases that control many cellular processes by the regulation of cytosolic calcium and/or the activity of several protein kinases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 27-317 2.91e-135

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: 385.44  E-value: 2.91e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  27 LCPQLWDVPLHHLSIPGSHDTMTYCLNKKSPISHEESrlLQLLNKAFPCITHPVVLKWSVTQALDVTEQLDAGVRYLDLR 106
Cdd:cd08616     1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQS--VQNLVKVFPCIFKKIVKKWSKTQSLTITEQLEAGIRYFDLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 107 IAHMLEgsEKNLHFVHMVYTTaLVEDTLTEISEWLERHPREVVILACRNFEGLSEDLHEYLVACIKNIFGDMLCPRGEL- 185
Cdd:cd08616    79 IATKPK--DNDLYFVHGLYGI-LVKEILEEINDFLTEHPKEVVILDFNHFYGMTEEDHEKLLKMIKSIFGKKLCPRDPDl 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 186 --PTLRQLWSRGQQVIVSYED-ESSLGRHCELWPGIPYWWGNTAKTEALIRYLETMKSCGRPGGLFVAGTNLTENLQYVL 262
Cdd:cd08616   156 lnVTLEYLWEKGYQVIVFYHDpVAKKPPYLWPSDAIPSPWPNTTDPKKLIQFLETTLKERRPPGFHVSQGILTPDVKTIL 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622969921 263 -AHPSESLEKMTLPNLPRLSAWVREQHPGPGSrCTNVIAGDFVGADSFVGDVIALN 317
Cdd:cd08616   236 rHLTSGLLKTLTLRALPKLLEWLRKQEPGSGQ-GVNIIIADFVDLDEFIDTVIALN 290
 
Name Accession Description Interval E-value
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 27-317 2.91e-135

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: 385.44  E-value: 2.91e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  27 LCPQLWDVPLHHLSIPGSHDTMTYCLNKKSPISHEESrlLQLLNKAFPCITHPVVLKWSVTQALDVTEQLDAGVRYLDLR 106
Cdd:cd08616     1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQS--VQNLVKVFPCIFKKIVKKWSKTQSLTITEQLEAGIRYFDLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 107 IAHMLEgsEKNLHFVHMVYTTaLVEDTLTEISEWLERHPREVVILACRNFEGLSEDLHEYLVACIKNIFGDMLCPRGEL- 185
Cdd:cd08616    79 IATKPK--DNDLYFVHGLYGI-LVKEILEEINDFLTEHPKEVVILDFNHFYGMTEEDHEKLLKMIKSIFGKKLCPRDPDl 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 186 --PTLRQLWSRGQQVIVSYED-ESSLGRHCELWPGIPYWWGNTAKTEALIRYLETMKSCGRPGGLFVAGTNLTENLQYVL 262
Cdd:cd08616   156 lnVTLEYLWEKGYQVIVFYHDpVAKKPPYLWPSDAIPSPWPNTTDPKKLIQFLETTLKERRPPGFHVSQGILTPDVKTIL 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622969921 263 -AHPSESLEKMTLPNLPRLSAWVREQHPGPGSrCTNVIAGDFVGADSFVGDVIALN 317
Cdd:cd08616   236 rHLTSGLLKTLTLRALPKLLEWLRKQEPGSGQ-GVNIIIADFVDLDEFIDTVIALN 290
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 33-191 8.26e-10

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: 56.52  E-value: 8.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921   33 DVPLHHLSIPGSHDTmtyclnkkspisheesrllQLLNKAFpcithpvvlkWSVTQALDVTEQLDAGVRYLDLRIAHMLE 112
Cdd:smart00148   2 DKPLSHYFIPSSHNT-------------------YLTGKQL----------WGESSVEGYIQALDAGCRCVELDCWDGPD 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  113 GSEKnLHFVHMVYTTALVEDTLTEISEWLERHPREVVILACRNFegLSEDLHEYLVACIKNIFGDMLCPRG------ELP 186
Cdd:smart00148  53 GEPV-IYHGHTFTLPIKLSEVLEAIKDFAFVTSPYPVILSLENH--CSPDQQAKMAQMFKEIFGDMLYTPPltssleVLP 129


                   ....*
gi 1622969921  187 TLRQL 191
Cdd:smart00148 130 SPEQL 134
PTZ00268 PTZ00268
glycosylphosphatidylinositol-specific phospholipase C; Provisional
 21-108 9.64e-07

glycosylphosphatidylinositol-specific phospholipase C; Provisional


Pssm-ID: 140294  Cd Length: 380  Bit Score: 49.89  E-value: 9.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  21 EDWMSALCPQLWDVPLHHLSIPGSHDTMTYCLNKKSPISHE------ESRLLQLLNKAFpciTHPVVLKWSVTQALDVTE 94
Cdd:PTZ00268   16 QSWMHDLRSFIGEMAITQVCLVGSHNAASYGIHKDSPFGADapgfllGDSVVASLSRFL---FRGISASWSKCQGMSVRA 92

                          90
                  ....*....|....
gi 1622969921  95 QLDAGVRYLDLRIA 108
Cdd:PTZ00268   93 QLDHGVRYLDLRVA 106
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 84-191 1.31e-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: 38.64  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  84 WSVTQALDVTEQLDAGVRYLDLRIahmLEGSEKNLHFVH-MVYTTAL-VEDTLTEISEWLERHPREVVILacrNFE-GLS 160
Cdd:pfam00388  24 TGESSVEAYIRALLRGCRCVELDC---WDGPDGEPVVYHgYTLTSKIpFRDVLEAIKDYAFVTSPYPVIL---SLEnHCS 97

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622969921 161 EDLHEYLVACIKNIFGDMLCPR------GELPTLRQL 191
Cdd:pfam00388  98 PEQQKKMAEILKEIFGDMLYTPpldddlTELPSPEDL 134
 
Name Accession Description Interval E-value
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 27-317 2.91e-135

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: 385.44  E-value: 2.91e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  27 LCPQLWDVPLHHLSIPGSHDTMTYCLNKKSPISHEESrlLQLLNKAFPCITHPVVLKWSVTQALDVTEQLDAGVRYLDLR 106
Cdd:cd08616     1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQS--VQNLVKVFPCIFKKIVKKWSKTQSLTITEQLEAGIRYFDLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 107 IAHMLEgsEKNLHFVHMVYTTaLVEDTLTEISEWLERHPREVVILACRNFEGLSEDLHEYLVACIKNIFGDMLCPRGEL- 185
Cdd:cd08616    79 IATKPK--DNDLYFVHGLYGI-LVKEILEEINDFLTEHPKEVVILDFNHFYGMTEEDHEKLLKMIKSIFGKKLCPRDPDl 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 186 --PTLRQLWSRGQQVIVSYED-ESSLGRHCELWPGIPYWWGNTAKTEALIRYLETMKSCGRPGGLFVAGTNLTENLQYVL 262
Cdd:cd08616   156 lnVTLEYLWEKGYQVIVFYHDpVAKKPPYLWPSDAIPSPWPNTTDPKKLIQFLETTLKERRPPGFHVSQGILTPDVKTIL 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622969921 263 -AHPSESLEKMTLPNLPRLSAWVREQHPGPGSrCTNVIAGDFVGADSFVGDVIALN 317
Cdd:cd08616   236 rHLTSGLLKTLTLRALPKLLEWLRKQEPGSGQ-GVNIIIADFVDLDEFIDTVIALN 290
PI-PLCXDc_like cd08587
Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and ...
 28-317 1.63e-101

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: 299.64  E-value: 1.63e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  28 CPQLWDVPLHHLSIPGSHDTMTYCLNKKSPISHEESRllqllnkaFPCITHPVVLKWSVTQALDVTEQLDAGVRYLDLRI 107
Cdd:cd08587     1 PSAIGDLPLRDLVIPGSHDSGMYTINGDSPVGPDQPE--------FGKIAKGIVRKWSVTQSLSIYDQLEAGIRYFDLRV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 108 AHMLeGSEKNLHFVHMVYTTALVEDTLTEISEWLERHPREVVILACRNFEGLSE---DLHEYLVACIKNIFGDMLCPRGE 184
Cdd:cd08587    73 AYKP-DSENKLYFVHGLYSGEPVDEVLEDVNDFLDEHPKEVVILDFNHFYGMDDkspEDHEKLVELLEDIFGDKLCPRDS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 185 L---PTLRQLWSRGQQVIVSYEDE-SSLGRHCELWPGIPYWWGNTAKTEALIRYLETMKSCGR-PGGLFVAGTNLTENLQ 259
Cdd:cd08587   152 DlldVTLADLWESGKRVIVFYDDDlASEGPYLWPSPYIPDPWANTDDPQKLIDFLENKLKERRrPDKFFVLQWILTPQAS 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622969921 260 YVLAHP-SESLEKMTLPNLPRLSAWVREQhpGPGSRCTNVIAGDFVGADSFVGDVIALN 317
Cdd:cd08587   232 TIVLGLfSGLLKKLALRANPALLEWLREQ--LPGQDGPNIILNDFVDLGEFIDLAIALN 288
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 29-317 4.84e-66

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: 208.49  E-value: 4.84e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  29 PQLWDVPLHHLSIPGSHDTMTYCLNKKSPIsheesrllqllnkafpcithpvVLKWSVTQALDVTEQLDAGVRYLDLRIA 108
Cdd:cd08557     2 ALLDDLPLSQLSIPGTHNSYAYTIDGNSPI----------------------VSKWSKTQDLSITDQLDAGVRYLDLRVA 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 109 HMleGSEKNLHFVHMVYTTA--LVEDTLTEISEWLERHPREVVILACRNFEGLSEDL-HEYLVACIKNIFGDMLCPR--- 182
Cdd:cd08557    60 YD--PDDGDLYVCHGLFLLNgqTLEDVLNEVKDFLDAHPSEVVILDLEHEYGGDNGEdHDELDALLRDVLGDPLYRPpvr 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 183 -GELPTLRQLWsRGQQVIVSYEDES-SLGRHCELWPGIPYWWGN-TAKTEALIRYLETMKSCGR-PGGLFVAGTNLTENL 258
Cdd:cd08557   138 aGGWPTLGELR-AGKRVLLFYFGGDdSSGGYDWGSLNIQDPYANgTDKLESLKAFLNSALASPRsADFFYVNQASLTPGR 216

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622969921 259 QYVLAHPseSLEKMTLPNLPRLSAWVREQhpGPGSRCTNVIAGDFVGADSFVGDVIALN 317
Cdd:cd08557   217 ITIAVAG--SLYTVATRANPALYEWLKED--GSGASGPNIVATDFVDVGDLIDAVIRLN 271
PI-PLCXDc_CG14945_like cd08622
Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to ...
 28-304 5.68e-34

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: 125.52  E-value: 5.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  28 CPQLWDVPLHHLSIPGSHDTMTYclNKKSPISHeesrllqllnkafpcithPVVLKWSVTQALDVTEQLDAGVRYLDLRI 107
Cdd:cd08622     1 KKSIGNLRIKDLFIPGTHNSAAY--DTNSNANE------------------SLVDKYLLTQDLDIWTQLVHGIRYLDLRV 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 108 AHMlEGSEKNLHFVH-MVYTTALVEdTLTEISEWLERHpREVVILACRNFE---GLSEDLHEYLVACIKNIFGDMLCPRG 183
Cdd:cd08622    61 GYY-PDSPDNFWINHdLVRIVPLLT-VLNDVRNFVQNT-GEIVVLDFHRFPvgfHSHPEVHDELISLLRQELGDLILRRS 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 184 EL----PTLRQLWSRGQQVIVSYEDESSLGRHCELWPGIPYWWGNTAKTEALIRYLET--MKSCGRPGGLFVAGTNLTEN 257
Cdd:cd08622   138 RNygwgPTLSEIWARRKRVIICYDHEYFVRESDWLWPPVQQKWGNVQTLDDLKSYLRKliSQPHRFTNPPVSLMAELTPV 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1622969921 258 LQYVLAHPSESLEKMTLPNLPRLSAWVReqhpGPGSRCTNVIAGDFV 304
Cdd:cd08622   218 PWDIISDRLGNLRKLADIVNRKLTRWYR----DEWGYNANIVATDFF 260
PI-PLCc_BcPLC_like cd08586
Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar ...
 24-317 1.42e-28

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: 111.22  E-value: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  24 MSALCPqlwDVPLHHLSIPGSHDTMTYclnkkspisheesrllqllnkafpcitHPVVLKWSVTQALDVTEQLDAGVRYL 103
Cdd:cd08586     1 MSALPD---DTPLSELSIPGTHDSGAL---------------------------HGGLSSSVQCQDWSIAEQLNAGIRFL 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 104 DLRIAHMLEGsekNLHFVH-MVYTTALVEDTLTEISEWLERHPREVVILACRN---FEGLSEDLHEYLVACIKNIFGDML 179
Cdd:cd08586    51 DIRLRLIDNN---DLAIHHgPFYQGLTFGDVLNECYSFLDANPSETIIMSLKQegsGDGNTDSFAEIFKEYLDNYPSYFY 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 180 CPRGELPTLRQLwsRGQQVIVS-YEDESSLGRHCELWPGIPYW--------------------WGNTAKTEALIRYLET- 237
Cdd:cd08586   128 YTESKIPTLGEV--RGKIVLLRrFDGDDEGGGYNNGGPDDTLFtinidngtlyiqdfyevstaEDIEKKWNAIKAHLDKa 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 238 MKSCGRPGGLFVAGTNLTENLQYVLAHPSESLEKMTlpnlPRLSAWVREQHPGpgsRCTNVIAGDFVGADS-FVGDVIAL 316
Cdd:cd08586   206 ASNSSSSNKLYINFTSGSGGGFPLGGGPGKYAEGIN----PLLYNYLKENNGR---GRLGIVIMDFPGADWdLIQLIIGT 278


                  .
gi 1622969921 317 N 317
Cdd:cd08586   279 N 279
PI-PLCc_Rv2075c_like cd08590
Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This ...
 88-236 2.35e-13

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: 68.97  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  88 QALDVTEQLDAGVRYL---------DLRIAHmleGSEKNLHFVHMVYTTaLVEDTLTEISEWLERHPREVVILACRnfEG 158
Cdd:cd08590    43 QELSITDQLDLGARFLeldvhwttgDLRLCH---GGDHGYLGVCSSEDR-LFEDGLNEIADWLNANPDEVVILYLE--DH 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 159 LSEDLHEYLVACIKNIFGDMLCPRGEL---------PTLRQLWSRGQQVIV----SYEDESSLGRHCELWPGIP-----Y 220
Cdd:cd08590   117 GDGGKDDELNALLNDAFGDLLYTPSDCddlqglpnwPTKEDMLNSGKQVVLatggGCSGAQGMYNRKEFADTQPsnfrpY 196

                         170
                  ....*....|....*...
gi 1622969921 221 WWGNTAKTEA--LIRYLE 236
Cdd:cd08590   197 PECAFAMGNNtsLVRVYE 214
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 33-228 3.49e-13

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: 68.44  E-value: 3.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  33 DVPLHHLSIPGSHDTMTYClnkkspisheesrlLQLlnkafpcithPVVLKWSVTQALDVTEQLDAGVRYLDLRiAHMLE 112
Cdd:cd00137     5 TQPLAHYSIPGTHDTYLTA--------------GQF----------TIKQVWGLTQTEMYRQQLLSGCRCVDIR-CWDGK 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 113 GSEKNLHfvH-MVYTTALVEDTLTEISEWLERHPREVVILACRNfEGLSEDLHEYLVA-CIKNIFGDMLC-----PRGEL 185
Cdd:cd00137    60 PEEPIIY--HgPTFLDIFLKEVIEAIAQFLKKNPPETIIMSLKN-EVDSMDSFQAKMAeYCRTIFGDMLLtpplkPTVPL 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622969921 186 PTLRQLwsRGQQVIVSYEDESSLgrhcelwPGI---PYWWGNTAKT 228
Cdd:cd00137   137 PSLEDL--RGKILLLNKKNGFSG-------PTGssnDTGFVSFEFS 173
PI-PLCXDc_like_2 cd08621
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 33-317 7.18e-12

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: 65.09  E-value: 7.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  33 DVPLHHLSIPGSHDT-MtyclnkkSPISHeeSRLLQLLNKAfpcithpvvlkWSVTQALDVTEQLDAGVRYLDLRIAHml 111
Cdd:cd08621     6 DRPLRHIVMPGTHDSgM-------SSLTG--GLWPVDGNDS-----------NTQTQGLSIYDQLRAGARYFDIRPVI-- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 112 eGSEKNLHFVHMVYTTALVE--------DTLTEISEWLERHPREVVILACRNFEGLSEDLHEYLVACIKN-IFGDML--- 179
Cdd:cd08621    64 -THGGELWTGHYNGEDASAQgangesldDILDEVNRFTDENPGELVILNFSHILNTDNGDGRPFSAEEWEkIFDELEgin 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 180 --CP----RGELPTLRQ---LWSRGQQVIVSYEDESSLGRHCELWP--GIPYW--------WGNTAKTEALIRY-LETMK 239
Cdd:cd08621   143 nrCGnideEGDLYTQKLsdfIDASGKACVVFIYDGTISSNQGSTPAkgGIYDGpqftvydsYSNTDDTNYMAEDqLAKLR 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921 240 SCGRPGG----LFVAGTNLTENLQYVLAHPSESLEKMTLPNLPR--LSAWVREQHPgpgsrctNVIAGDFVGADSFV-GD 312
Cdd:cd08621   223 SHRRPSFgddiFFLLSWTLTPQALTVTGSSIKKLAEEANPALFWklVDAMSPWSFP-------NVVYVDYLGNFGEVlAL 295


                  ....*
gi 1622969921 313 VIALN 317
Cdd:cd08621   296 AIGLN 300
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 87-228 4.08e-11

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: 62.35  E-value: 4.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  87 TQALDVTEQLDAGVRYLDLRIaHMLEGSeknLHFVHMV---YTTALVEDTLTEISEWLERHPREVVILACRNFEGLSEDL 163
Cdd:cd08588    36 NQEDDITKQLDDGVRGLMLDI-HDANGG---LRLCHSVcglGDGGPLSDVLREVVDFLDANPNEVVTLFLEDYVSPGPLL 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622969921 164 HEYL--VACIKN-IF--GDMLCPRGELPTLRQLWSRGQQVIV--SYEDESSlgrhCElwPGIPYWWGNTAKT 228
Cdd:cd08588   112 RSKLfrVAGLTDlVYvpDAMPWAGSDWPTLGEMIDANKRLLVftDNEDVST----EP--PGVMYQFDYTVEN 177
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 33-191 8.26e-10

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: 56.52  E-value: 8.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921   33 DVPLHHLSIPGSHDTmtyclnkkspisheesrllQLLNKAFpcithpvvlkWSVTQALDVTEQLDAGVRYLDLRIAHMLE 112
Cdd:smart00148   2 DKPLSHYFIPSSHNT-------------------YLTGKQL----------WGESSVEGYIQALDAGCRCVELDCWDGPD 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  113 GSEKnLHFVHMVYTTALVEDTLTEISEWLERHPREVVILACRNFegLSEDLHEYLVACIKNIFGDMLCPRG------ELP 186
Cdd:smart00148  53 GEPV-IYHGHTFTLPIKLSEVLEAIKDFAFVTSPYPVILSLENH--CSPDQQAKMAQMFKEIFGDMLYTPPltssleVLP 129


                   ....*
gi 1622969921  187 TLRQL 191
Cdd:smart00148 130 SPEQL 134
PI-PLCXDc_plant cd08619
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing ...
 22-154 5.83e-08

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: 53.33  E-value: 5.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  22 DWMSALCPQLWDVPLH--HLSIPGSHDTMTyclNKKSpisheesrllqllnkaFPCITHPVvlkwSVTQALDVTEQLDAG 99
Cdd:cd08619    13 EWMSLSQLKAMDSSLKlrDIVWPGTHDSAT---NKIG----------------IPKVSRPF----ARCQSLSIYNQLCSG 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622969921 100 VRYLDLRIAhmlegseKNLHFVHMVYTTALVEDTLTEISEWLERHPREVVILACR 154
Cdd:cd08619    70 ARVLDIRVQ-------EDRRVCHGCLKTYPVDVVLNDIKRFLSETKSEFVILEIR 117
PTZ00268 PTZ00268
glycosylphosphatidylinositol-specific phospholipase C; Provisional
 21-108 9.64e-07

glycosylphosphatidylinositol-specific phospholipase C; Provisional


Pssm-ID: 140294  Cd Length: 380  Bit Score: 49.89  E-value: 9.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  21 EDWMSALCPQLWDVPLHHLSIPGSHDTMTYCLNKKSPISHE------ESRLLQLLNKAFpciTHPVVLKWSVTQALDVTE 94
Cdd:PTZ00268   16 QSWMHDLRSFIGEMAITQVCLVGSHNAASYGIHKDSPFGADapgfllGDSVVASLSRFL---FRGISASWSKCQGMSVRA 92

                          90
                  ....*....|....
gi 1622969921  95 QLDAGVRYLDLRIA 108
Cdd:PTZ00268   93 QLDHGVRYLDLRVA 106
PI-PLCXDc_like_1 cd08620
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 29-162 4.91e-06

Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins; This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.


Pssm-ID: 176557  Cd Length: 281  Bit Score: 47.39  E-value: 4.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  29 PQLWDVPLHHLSIPGSHDTMTYclnkkspisheesrllqllnkafpcithpVVLKWSVTQALDVTEQLDAGVRYLDLRIA 108
Cdd:cd08620     2 SAPAQQPFNRFVLPGAHDAGMN-----------------------------GMTNLSVTQKDNVSTQLALGARYFDFRPG 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622969921 109 HML-----EGSEKNLHFVHMVYTTALVEDTLTEISEWLERHPREVVILACRNfEGLSED 162
Cdd:cd08620    53 YLWpqtrvLVLLNDLYHQHNMIPGQGFDTFLQDVVTFLKANPTEIVVVHITW-DGFDND 110
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 84-191 1.31e-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: 38.64  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622969921  84 WSVTQALDVTEQLDAGVRYLDLRIahmLEGSEKNLHFVH-MVYTTAL-VEDTLTEISEWLERHPREVVILacrNFE-GLS 160
Cdd:pfam00388  24 TGESSVEAYIRALLRGCRCVELDC---WDGPDGEPVVYHgYTLTSKIpFRDVLEAIKDYAFVTSPYPVIL---SLEnHCS 97

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622969921 161 EDLHEYLVACIKNIFGDMLCPR------GELPTLRQL 191
Cdd:pfam00388  98 PEQQKKMAEILKEIFGDMLYTPpldddlTELPSPEDL 134
 
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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