Conserved Protein Domain Family
PI3Kc_C2_beta

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cd00895: PI3Kc_C2_beta 
Catalytic domain of Class II Phosphoinositide 3-kinase beta
PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. The class II beta isoform, PI3K-C2beta, contributes to the migration and survival of cancer cells. It regulates Rac activity and impacts membrane ruffling, cell motility, and cadherin-mediated cell-cell adhesion. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PtdIns as a substrate to produce PtdIns(3)P, but can also phosphorylate PtdIns(4)P. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a Phox homology (PX) domain, and a second C2 domain at the C-terminus. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.
Statistics
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PSSM-Id: 119421
View PSSM: cd00895
Aligned: 3 rows
Threshold Bit Score: 715.239
Threshold Setting Gi: 326671837
Created: 8-Dec-2000
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
Feature 1:ATP binding site [chemical binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                               # ### #   
O00750        987 REEFNRQCWLVNALAKLAQQVREAAPSARQGILRTGLEEVKQFFAlNGSCRLPLSPSLLVKGIVPRDCSYFNSNAVPLKL 1066 human
XP_417956     981 REEFDRQCLLVNTLARLAQQVRDAAPSARQGILREGLEEVKQFFKaNGSCRLPLSPSLLVKGIVPRDCSYFNSNAVPLKL 1060 chicken
XP_003199535  934 REEFDRQCWLVNVLAKVAQRVREASPSSRQAILREGLDDVKQFFSiNSSCRLPLNPGLLVKGINIQSCSYFNSNAVPLKL 1013 zebrafish
Feature 1                       # #  #                              #           ####    #  #      
O00750       1067 SFQNvdplgenIRVIFKCGDDLRQDMLTLQMIRIMSKIWVQEGLDMRMVIFRCFSTGRGRGMVEMIPNAETLRKIQVEHG 1146 human
XP_417956    1061 SFQNvdplgenIRVIFKCGDDLRQDMLTLQMIRIMNKIWVQEGLDMRMVIFRCFSTGRGRGMVEMIPNAETLRKIQVEHG 1140 chicken
XP_003199535 1014 SFQNqdhlgdnINVIFKAGDDLRQDMLTLQIIRIMNKIWVQEGLDMRMVIFRCFSTGRGRGMVEMIPSAETLRKIQVEHG 1093 zebrafish
Feature 1                                                              # #         ##             
O00750       1147 VTGSFKDRPLADWLQKHNPgedeYEKAVENFIYSCAGCCVATYVLGICDRHNDNIMLKTTGHMFHIDFGRFLGHAQMFGN 1226 human
XP_417956    1141 VTGSFKDRPLADWLQKHNPeedeYEKAVENFIYSCAGCCVATYVLGICDRHNDNIMLKTTGHMFHIDFGRFLGHAQMFGN 1220 chicken
XP_003199535 1094 VTGSFKDRPLADWLQKHNPteeeYEKAVENFIYSCAGCCVATYILGICDRHNDNIMLKTSGHMFHIDFGKFLGHAQMFGN 1173 zebrafish
Feature 1                                                                                         
O00750       1227 IKRDRAPFVFTSDMAYVINGGDKPSSRFHDFVDLCCQAYNLIRKHTHLFLNLLGLMLSCGIPELsdLEDLKYVYDALRPq 1306 human
XP_417956    1221 IKRDRAPFVFTSDMAYVINGGDKPSSRFHDFVDLCCQAYNLIRKHTHLFLNLLGLMLSCGIPELsdLEDLKYVYDALRPq 1300 chicken
XP_003199535 1174 IKRDRAPFVFTSDMAYVINGGDKPSSRFHDFVDLCCEAYNRIRKHAHLFLNLLGLMLSSGIPELsdVDDLKYVYDALRPh 1253 zebrafish
Feature 1                                           
O00750       1307 dtEANATTYFTRLIESSLGSvATKLNFFIHNLAQ 1340 human
XP_417956    1301 dtDADATTYFTRLIESSLGSvATKLNFFIHNLAQ 1334 chicken
XP_003199535 1254 esEADATMHFTRLIESSLGSvATKLNFFIHNLAQ 1287 zebrafish

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