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Conserved domains on  [gi|755512645|ref|XP_011247809|]
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PI-PLC X domain-containing protein 1 isoform X2 [Mus musculus]

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 ...
 11-301 2.37e-121

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: 349.62  E-value: 2.37e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  11 LCPQLWDVPLHHLSIPGSHDTMTYCLNRKSRISRASSWllHLLGRVVPFITGPVVMKWSVTQTLDVTQQLDAGVRYLDLR 90
Cdd:cd08616    1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQSV--QNLVKVFPCIFKKIVKKWSKTQSLTITEQLEAGIRYFDLR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  91 IAHAPEGStrNLCFVHMMYTkALVEDTLTEIAEWLQSHPREVVILACRNFEGMTCELHDYLAGCIVNIFGDMLCP---SG 167
Cdd:cd08616   79 IATKPKDN--DLYFVHGLYG-ILVKEILEEINDFLTEHPKEVVILDFNHFYGMTEEDHEKLLKMIKSIFGKKLCPrdpDL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645 168 EVPTLRQLWAREQQVIVSYEDEATVsRYDQLWP--AIPYWWGNAVKTDVLLRFLETMKGQGRPDGLFVAGINITENLCYI 245
Cdd:cd08616  156 LNVTLEYLWEKGYQVIVFYHDPVAK-KPPYLWPsdAIPSPWPNTTDPKKLIQFLETTLKERRPPGFHVSQGILTPDVKTI 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755512645 246 L-LHPVDSLEEMTRRSLPLMTEWVCAQQPGQSpQCTNIIAGDFVDADGFVSKVISLN 301
Cdd:cd08616  235 LrHLTSGLLKTLTLRALPKLLEWLRKQEPGSG-QGVNIIIADFVDLDEFIDTVIALN 290
 
Name Accession Description Interval E-value
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 11-301 2.37e-121

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: 349.62  E-value: 2.37e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  11 LCPQLWDVPLHHLSIPGSHDTMTYCLNRKSRISRASSWllHLLGRVVPFITGPVVMKWSVTQTLDVTQQLDAGVRYLDLR 90
Cdd:cd08616    1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQSV--QNLVKVFPCIFKKIVKKWSKTQSLTITEQLEAGIRYFDLR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  91 IAHAPEGStrNLCFVHMMYTkALVEDTLTEIAEWLQSHPREVVILACRNFEGMTCELHDYLAGCIVNIFGDMLCP---SG 167
Cdd:cd08616   79 IATKPKDN--DLYFVHGLYG-ILVKEILEEINDFLTEHPKEVVILDFNHFYGMTEEDHEKLLKMIKSIFGKKLCPrdpDL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645 168 EVPTLRQLWAREQQVIVSYEDEATVsRYDQLWP--AIPYWWGNAVKTDVLLRFLETMKGQGRPDGLFVAGINITENLCYI 245
Cdd:cd08616  156 LNVTLEYLWEKGYQVIVFYHDPVAK-KPPYLWPsdAIPSPWPNTTDPKKLIQFLETTLKERRPPGFHVSQGILTPDVKTI 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755512645 246 L-LHPVDSLEEMTRRSLPLMTEWVCAQQPGQSpQCTNIIAGDFVDADGFVSKVISLN 301
Cdd:cd08616  235 LrHLTSGLLKTLTLRALPKLLEWLRKQEPGSG-QGVNIIIADFVDLDEFIDTVIALN 290
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 17-175 1.28e-12

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: 64.22  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645    17 DVPLHHLSIPGSHDTmtyclnrksrisrasswllHLLGRVVpfitgpvvmkWSVTQTLDVTQQLDAGVRYLDLRIAHAPE 96
Cdd:smart00148   2 DKPLSHYFIPSSHNT-------------------YLTGKQL----------WGESSVEGYIQALDAGCRCVELDCWDGPD 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645    97 GSTRnLCFVHMMYTKALVEDTLTEIAEWLQSHPREVVILACRNFEGMtcELHDYLAGCIVNIFGDMLC-----PSGEV-P 170
Cdd:smart00148  53 GEPV-IYHGHTFTLPIKLSEVLEAIKDFAFVTSPYPVILSLENHCSP--DQQAKMAQMFKEIFGDMLYtppltSSLEVlP 129


                   ....*
gi 755512645   171 TLRQL 175
Cdd:smart00148 130 SPEQL 134
PTZ00268 PTZ00268
glycosylphosphatidylinositol-specific phospholipase C; Provisional
 7-100 1.38e-08

glycosylphosphatidylinositol-specific phospholipase C; Provisional


Pssm-ID: 140294  Cd Length: 380  Bit Score: 55.28  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645   7 WMSQLCPQLWDVPLHHLSIPGSHDTMTYCLNRKSRISRASSWLLH---LLGRVVPFITGPVVMKWSVTQTLDVTQQLDAG 83
Cdd:PTZ00268  18 WMHDLRSFIGEMAITQVCLVGSHNAASYGIHKDSPFGADAPGFLLgdsVVASLSRFLFRGISASWSKCQGMSVRAQLDHG 97

                         90
                 ....*....|....*..
gi 755512645  84 VRYLDLRIAHAPEGSTR 100
Cdd:PTZ00268  98 VRYLDLRVATNPEDANR 114
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 23-175 1.09e-04

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: 41.34  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645   23 LSIPGSHDTMTYCLNrksrisrasswlLHLLGRVVpfitgpvvmkWSVTQTLDVTQQLDAGVRYLDLRIAHAPEGSTrNL 102
Cdd:pfam00388   1 MSQPLSHYFISSSHN------------TYLTGDQL----------TGESSVEAYIRALLRGCRCVELDCWDGPDGEP-VV 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  103 CFVHMMYTKALVEDTLTEIAEWLQSHPREVVILacrNFEgMTC--ELHDYLAGCIVNIFGDMLCP------SGEVPTLRQ 174
Cdd:pfam00388  58 YHGYTLTSKIPFRDVLEAIKDYAFVTSPYPVIL---SLE-NHCspEQQKKMAEILKEIFGDMLYTppldddLTELPSPED 133


                  .
gi 755512645  175 L 175
Cdd:pfam00388 134 L 134
 
Name Accession Description Interval E-value
PI-PLCXD1c cd08616
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1; This ...
 11-301 2.37e-121

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: 349.62  E-value: 2.37e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  11 LCPQLWDVPLHHLSIPGSHDTMTYCLNRKSRISRASSWllHLLGRVVPFITGPVVMKWSVTQTLDVTQQLDAGVRYLDLR 90
Cdd:cd08616    1 LPEKLKDKPLTNLAIPGSHDSFTYSIDKQSPVSPDQSV--QNLVKVFPCIFKKIVKKWSKTQSLTITEQLEAGIRYFDLR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  91 IAHAPEGStrNLCFVHMMYTkALVEDTLTEIAEWLQSHPREVVILACRNFEGMTCELHDYLAGCIVNIFGDMLCP---SG 167
Cdd:cd08616   79 IATKPKDN--DLYFVHGLYG-ILVKEILEEINDFLTEHPKEVVILDFNHFYGMTEEDHEKLLKMIKSIFGKKLCPrdpDL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645 168 EVPTLRQLWAREQQVIVSYEDEATVsRYDQLWP--AIPYWWGNAVKTDVLLRFLETMKGQGRPDGLFVAGINITENLCYI 245
Cdd:cd08616  156 LNVTLEYLWEKGYQVIVFYHDPVAK-KPPYLWPsdAIPSPWPNTTDPKKLIQFLETTLKERRPPGFHVSQGILTPDVKTI 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755512645 246 L-LHPVDSLEEMTRRSLPLMTEWVCAQQPGQSpQCTNIIAGDFVDADGFVSKVISLN 301
Cdd:cd08616  235 LrHLTSGLLKTLTLRALPKLLEWLRKQEPGSG-QGVNIIIADFVDLDEFIDTVIALN 290
PI-PLCXDc_like cd08587
Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and ...
 12-301 1.27e-93

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: 278.84  E-value: 1.27e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  12 CPQLWDVPLHHLSIPGSHDTMTYCLNRKSRISRASSWLlhllgrvvPFITGPVVMKWSVTQTLDVTQQLDAGVRYLDLRI 91
Cdd:cd08587    1 PSAIGDLPLRDLVIPGSHDSGMYTINGDSPVGPDQPEF--------GKIAKGIVRKWSVTQSLSIYDQLEAGIRYFDLRV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  92 AHAPeGSTRNLCFVHMMYTKALVEDTLTEIAEWLQSHPREVVILACRNFEGMT---CELHDYLAGCIVNIFGDMLCPSGE 168
Cdd:cd08587   73 AYKP-DSENKLYFVHGLYSGEPVDEVLEDVNDFLDEHPKEVVILDFNHFYGMDdksPEDHEKLVELLEDIFGDKLCPRDS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645 169 V---PTLRQLWAREQQVIVSYEDEATVSR-YDQLWPAIPYWWGNAVKTDVLLRFLETMKGQGR-PDGLFVAGINITENLC 243
Cdd:cd08587  152 DlldVTLADLWESGKRVIVFYDDDLASEGpYLWPSPYIPDPWANTDDPQKLIDFLENKLKERRrPDKFFVLQWILTPQAS 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755512645 244 YILLHP-VDSLEEMTRRSLPLMTEWVcaQQPGQSPQCTNIIAGDFVDADGFVSKVISLN 301
Cdd:cd08587  232 TIVLGLfSGLLKKLALRANPALLEWL--REQLPGQDGPNIILNDFVDLGEFIDLAIALN 288
PI-PLCc_bacteria_like cd08557
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar ...
 13-301 9.95e-65

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: 204.63  E-value: 9.95e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  13 PQLWDVPLHHLSIPGSHDTMTYCLNRKSrisrasswllhllgrvvpfitgPVVMKWSVTQTLDVTQQLDAGVRYLDLRIA 92
Cdd:cd08557    2 ALLDDLPLSQLSIPGTHNSYAYTIDGNS----------------------PIVSKWSKTQDLSITDQLDAGVRYLDLRVA 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  93 HAPEGStrNLCFVHMMY--TKALVEDTLTEIAEWLQSHPREVVILACRNFEGM-TCELHDYLAGCIVNIFGDMLCP---- 165
Cdd:cd08557   60 YDPDDG--DLYVCHGLFllNGQTLEDVLNEVKDFLDAHPSEVVILDLEHEYGGdNGEDHDELDALLRDVLGDPLYRppvr 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645 166 SGEVPTLRQLWAReQQVIVSYEDEATVSR-YDQLWPAIPYWWGN-AVKTDVLLRFLETMKGQGR-PDGLFVAGINITENL 242
Cdd:cd08557  138 AGGWPTLGELRAG-KRVLLFYFGGDDSSGgYDWGSLNIQDPYANgTDKLESLKAFLNSALASPRsADFFYVNQASLTPGR 216

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755512645 243 CYILLHPvdSLEEMTRRSLPLMTEWVCAQQPGQSpqCTNIIAGDFVDADGFVSKVISLN 301
Cdd:cd08557  217 ITIAVAG--SLYTVATRANPALYEWLKEDGSGAS--GPNIVATDFVDVGDLIDAVIRLN 271
PI-PLCXDc_CG14945_like cd08622
Catalytic domain of Drosophila melanogaster CG14945-like proteins similar to ...
 12-301 2.44e-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: 126.29  E-value: 2.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  12 CPQLWDVPLHHLSIPGSHDTMTYclnrksrisrasswllhllgRVVPFITGPVVMKWSVTQTLDVTQQLDAGVRYLDLRI 91
Cdd:cd08622    1 KKSIGNLRIKDLFIPGTHNSAAY--------------------DTNSNANESLVDKYLLTQDLDIWTQLVHGIRYLDLRV 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  92 AHAPEgSTRNLCFVH-MMYTKALVEdTLTEIAEWLQSHpREVVILACRNFE---GMTCELHDYLAGCIVNIFGD-MLCPS 166
Cdd:cd08622   61 GYYPD-SPDNFWINHdLVRIVPLLT-VLNDVRNFVQNT-GEIVVLDFHRFPvgfHSHPEVHDELISLLRQELGDlILRRS 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645 167 GEV---PTLRQLWAREQQVIVSYEDEATVSRYDQLWPAIPYWWGNAVKTDVLLRFLETMKGQGR--PDGLFVAGINITEN 241
Cdd:cd08622  138 RNYgwgPTLSEIWARRKRVIICYDHEYFVRESDWLWPPVQQKWGNVQTLDDLKSYLRKLISQPHrfTNPPVSLMAELTPV 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645 242 LCYILLHPVDSLEEMTRRSLPLMTEWVcaQQPGQspQCTNIIAGDFVDADGFVSKVISLN 301
Cdd:cd08622  218 PWDIISDRLGNLRKLADIVNRKLTRWY--RDEWG--YNANIVATDFFLGTNIIDVAIETN 273
PI-PLCc_BcPLC_like cd08586
Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar ...
 17-301 5.84e-22

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: 93.12  E-value: 5.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  17 DVPLHHLSIPGSHDTMTYclnrksrisrasswllhllgrvvpfiTGPVVmKWSVTQTLDVTQQLDAGVRYLDLRIAHAPE 96
Cdd:cd08586    7 DTPLSELSIPGTHDSGAL--------------------------HGGLS-SSVQCQDWSIAEQLNAGIRFLDIRLRLIDN 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  97 GstrNLCFVH-MMYTKALVEDTLTEIAEWLQSHPREVVILACRNfEGMTCELHD----YLAGCIVNIFGDMLCPSGEVPT 171
Cdd:cd08586   60 N---DLAIHHgPFYQGLTFGDVLNECYSFLDANPSETIIMSLKQ-EGSGDGNTDsfaeIFKEYLDNYPSYFYYTESKIPT 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645 172 LRQ------LWAR---------EQQVIVSYEDEATVSRYDQL----------WPAIPYWWgNAVKTdvLLRflETMKGQG 226
Cdd:cd08586  136 LGEvrgkivLLRRfdgddegggYNNGGPDDTLFTINIDNGTLyiqdfyevstAEDIEKKW-NAIKA--HLD--KAASNSS 210

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755512645 227 RPDGLFvagINITeNLCYILLHPVDSLEEMTRRSLPLMTEWVCAQQPGqspQCTNIIAGDFVDAD-GFVSKVISLN 301
Cdd:cd08586  211 SSNKLY---INFT-SGSGGGFPLGGGPGKYAEGINPLLYNYLKENNGR---GRLGIVIMDFPGADwDLIQLIIGTN 279
PI-PLCc cd00137
Catalytic domain of prokaryotic and eukaryotic phosphoinositide-specific phospholipase C; This ...
 17-175 4.44e-14

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: 70.76  E-value: 4.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  17 DVPLHHLSIPGSHDTMTYCLNRksrisrasswllhllgrvvpfitgPVVMKWSVTQTLDVTQQLDAGVRYLDLRiahAPE 96
Cdd:cd00137    5 TQPLAHYSIPGTHDTYLTAGQF------------------------TIKQVWGLTQTEMYRQQLLSGCRCVDIR---CWD 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  97 GSTRNLCFVH-MMYTKALVEDTLTEIAEWLQSHPREVVILACRNFEGMTCELHDYLAGCIVNIFGDMLC-----PSGEVP 170
Cdd:cd00137   58 GKPEEPIIYHgPTFLDIFLKEVIEAIAQFLKKNPPETIIMSLKNEVDSMDSFQAKMAEYCRTIFGDMLLtpplkPTVPLP 137


                 ....*
gi 755512645 171 TLRQL 175
Cdd:cd00137  138 SLEDL 142
PLCXc smart00148
Phospholipase C, catalytic domain (part); domain X; Phosphoinositide-specific phospholipases C. ...
 17-175 1.28e-12

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: 64.22  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645    17 DVPLHHLSIPGSHDTmtyclnrksrisrasswllHLLGRVVpfitgpvvmkWSVTQTLDVTQQLDAGVRYLDLRIAHAPE 96
Cdd:smart00148   2 DKPLSHYFIPSSHNT-------------------YLTGKQL----------WGESSVEGYIQALDAGCRCVELDCWDGPD 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645    97 GSTRnLCFVHMMYTKALVEDTLTEIAEWLQSHPREVVILACRNFEGMtcELHDYLAGCIVNIFGDMLC-----PSGEV-P 170
Cdd:smart00148  53 GEPV-IYHGHTFTLPIKLSEVLEAIKDFAFVTSPYPVILSLENHCSP--DQQAKMAQMFKEIFGDMLYtppltSSLEVlP 129


                   ....*
gi 755512645   171 TLRQL 175
Cdd:smart00148 130 SPEQL 134
PI-PLCc_Rv2075c_like cd08590
Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This ...
 17-207 3.01e-12

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: 65.51  E-value: 3.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  17 DVPLHHLSIPGSHDtmtyclnrkSRISRASSWLLHLLGrvvpfitgpvVMKWSVTQTLDVTQQLDAGVRYL--------- 87
Cdd:cd08590    7 NAPLCQAQILGTHN---------SYNSRAYGYGNRYHG----------VRYLDPNQELSITDQLDLGARFLeldvhwttg 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  88 DLRIAHAPEGSTRNLCFVHMMYTkalvEDTLTEIAEWLQSHPREVVILACRnfEGMTCELHDYLAGCIVNIFGDMLCPS- 166
Cdd:cd08590   68 DLRLCHGGDHGYLGVCSSEDRLF----EDGLNEIADWLNANPDEVVILYLE--DHGDGGKDDELNALLNDAFGDLLYTPs 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755512645 167 --------GEVPTLRQLWAREQQVIV--SYEDEATVSRYDQlwpaIPYWWG 207
Cdd:cd08590  142 dcddlqglPNWPTKEDMLNSGKQVVLatGGGCSGAQGMYNR----KEFADT 188
PI-PLCXDc_like_2 cd08621
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 17-135 1.13e-10

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: 61.24  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  17 DVPLHHLSIPGSHDT-MtyclnrksrisrasSWLLHLLgrvvpfITGPVVMKWSVTQTLDVTQQLDAGVRYLDLRIAHAP 95
Cdd:cd08621    6 DRPLRHIVMPGTHDSgM--------------SSLTGGL------WPVDGNDSNTQTQGLSIYDQLRAGARYFDIRPVITH 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 755512645  96 EGstrNLCFVHMMYTKALVE--------DTLTEIAEWLQSHPREVVIL 135
Cdd:cd08621   66 GG---ELWTGHYNGEDASAQgangesldDILDEVNRFTDENPGELVIL 110
PI-PLCc_At5g67130_like cd08588
Catalytic domain of Arabidopsis thaliana PI-PLC X domain-containing protein At5g67130 and its ...
 58-135 1.57e-09

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: 57.73  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  58 PFITGPvvmkwsvTQTLDVTQQLDAGVRYLDLRIAHAPEGstrnLCFVHMM---YTKALVEDTLTEIAEWLQSHPREVVI 134
Cdd:cd08588   30 AFFLAP-------NQEDDITKQLDDGVRGLMLDIHDANGG----LRLCHSVcglGDGGPLSDVLREVVDFLDANPNEVVT 98


                 .
gi 755512645 135 L 135
Cdd:cd08588   99 L 99
PTZ00268 PTZ00268
glycosylphosphatidylinositol-specific phospholipase C; Provisional
 7-100 1.38e-08

glycosylphosphatidylinositol-specific phospholipase C; Provisional


Pssm-ID: 140294  Cd Length: 380  Bit Score: 55.28  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645   7 WMSQLCPQLWDVPLHHLSIPGSHDTMTYCLNRKSRISRASSWLLH---LLGRVVPFITGPVVMKWSVTQTLDVTQQLDAG 83
Cdd:PTZ00268  18 WMHDLRSFIGEMAITQVCLVGSHNAASYGIHKDSPFGADAPGFLLgdsVVASLSRFLFRGISASWSKCQGMSVRAQLDHG 97

                         90
                 ....*....|....*..
gi 755512645  84 VRYLDLRIAHAPEGSTR 100
Cdd:PTZ00268  98 VRYLDLRVATNPEDANR 114
PI-PLCXDc_plant cd08619
Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing ...
 3-138 1.02e-06

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: 49.09  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645   3 DQADWMSQLCPQLWDVPLH--HLSIPGSHDTMTyclnrkSRISrasswllhllgrvVPFITGPVvmkwSVTQTLDVTQQL 80
Cdd:cd08619   10 DHKEWMSLSQLKAMDSSLKlrDIVWPGTHDSAT------NKIG-------------IPKVSRPF----ARCQSLSIYNQL 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755512645  81 DAGVRYLDLRIAhapegSTRNLCfvHMMYTKALVEDTLTEIAEWLQSHPREVVILACR 138
Cdd:cd08619   67 CSGARVLDIRVQ-----EDRRVC--HGCLKTYPVDVVLNDIKRFLSETKSEFVILEIR 117
PI-PLCXDc_like_1 cd08620
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic ...
 13-225 1.03e-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: 49.32  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  13 PQLWDVPLHHLSIPGSHDTMTYCLNrksrisrasswllhllgrvvpfitgpvvmKWSVTQTLDVTQQLDAGVRYLDLRIA 92
Cdd:cd08620    2 SAPAQQPFNRFVLPGAHDAGMNGMT-----------------------------NLSVTQKDNVSTQLALGARYFDFRPG 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  93 HAP-----EGSTRNLCFVHMMYTKALVEDTLTEIAEWLQSHPREVVILACRNfEGMTCELHDYLAGCIVNIFGDMLCPSG 167
Cdd:cd08620   53 YLWpqtrvLVLLNDLYHQHNMIPGQGFDTFLQDVVTFLKANPTEIVVVHITW-DGFDNDCARPSAQEVVEALAQALASAK 131

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755512645 168 EVP-----------TLRQLWAREQQVIVSYEDeatVSRYDqlwpaiPYWWGNAVKTD---VLLRFLETMKGQ 225
Cdd:cd08620  132 VGYvtsgtvsdlaaSYAQLRQTGKRLIVLFGD---ADKYD------SYSDEDYATSDpqpIIDALNKMLAEG 194
PI-PLC-X pfam00388
Phosphatidylinositol-specific phospholipase C, X domain; This associates with pfam00387 to ...
 23-175 1.09e-04

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: 41.34  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645   23 LSIPGSHDTMTYCLNrksrisrasswlLHLLGRVVpfitgpvvmkWSVTQTLDVTQQLDAGVRYLDLRIAHAPEGSTrNL 102
Cdd:pfam00388   1 MSQPLSHYFISSSHN------------TYLTGDQL----------TGESSVEAYIRALLRGCRCVELDCWDGPDGEP-VV 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512645  103 CFVHMMYTKALVEDTLTEIAEWLQSHPREVVILacrNFEgMTC--ELHDYLAGCIVNIFGDMLCP------SGEVPTLRQ 174
Cdd:pfam00388  58 YHGYTLTSKIPFRDVLEAIKDYAFVTSPYPVIL---SLE-NHCspEQQKKMAEILKEIFGDMLYTppldddLTELPSPED 133


                  .
gi 755512645  175 L 175
Cdd:pfam00388 134 L 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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