Conserved Protein Domain Family
PB1_aPKC

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cd06404: PB1_aPKC 
Click on image for an interactive view with Cn3D
PB1 domain is an essential modular domain of the atypical protein kinase C (aPKC) which in complex with Par6 and Par3 proteins is crucial for establishment of apical-basal polarity of animal cells. PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The aPKC protein contains a type I/II PB1 domain.
Statistics
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PSSM-Id: 99725
View PSSM: cd06404
Aligned: 12 rows
Threshold Bit Score: 133.625
Threshold Setting Gi: 51701751
Created: 27-Feb-2008
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
PB1 interaction
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1:PB1 interaction surface [polypeptide binding site]
Evidence:
  • Structure:1WMH; Human PKCiota and Par6alpha form an asymmetric heterodimer
    View structure with Cn3D
  • Comment:Par6 contains a type II PB1 domain and aPKC contains a type I/II PB1 domain

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                      # # #        #                    
1WMH_A         7 VRVKAYYrGDIMITHFepsISFEGLCNEVRDMCSFdneqlFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDs-ELLIH 85
gi 148225356  19 VRVKAYFkGDIMITHFepsITFDGLCNEVRDMCSFendqpFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDs-ELLIH 97
gi 54037714   19 VRVKAYYrGDIMITHFepsISYEGLCNEVRDMCSMdndqlFTMKWIDEEGDPCTVSSQLELEEALRLYELNKDs-ELIIH 97
gi 116007694  31 ITVKTAYnGQIIITTInknISYEELCYEIRNICRFpldqpFTIKWVDEENDPCTISTKMELDEAIRLYEMNFDs-QLVIH 109
gi 165905471  15 IPIKAAFnGSILCIRIdpnVTLEDFLQDMRGICNFpekqnFTVKWLDEDGDPCTISSQEELEEAIRLYELNKDs-NINIH 93
gi 68067736   16 VRLKAHYgGDIFITSVdaaTTFEELCEEVRDMCRLhqqhpLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDe-GLIIH 94
gi 118101016  30 FRIRAEFgRDILITNLdayISYDELCDEVREMCNLqqeqpITLKWIDDEGDPCTISSQMELEEAFRLYCQNREe-GLIIH 108
gi 109044366  26 VRVKAYYrGDIMITHFepsISFEGLCNEVRDMCSFdneqlFTMKWIDEEGDSTFLDSTYHVVFAFKLYPLNNSslSLLLH 105
gi 156395204   8 IAVRAAYnGDIMCLSMdphISLDTFTEDMKDIFKFrkeqtFTLKWLDEEGDPCTISSQEELNEAIRLYEINRDs-ELVVH 86
gi 112982924  16 VRVKTVYnGDVMITYInhnITFEEFTHEMVATCRFapdqvFTMKWVDEEGDPCTISTQLELDESLRLYELNRDs-ELTVH 94
gi 51701751   13 IKLKTRFqGQVVVLYArppLILDDFFALLKDACKQhkkqdITVKWIDEDGDPISIDSQMELDEAVRCLNSSQEa-ELNIH 91
gi 76157411    9 LQIKYIHnSIAMVTSCplsANLQAIDQQVRELCRFssdqpFTLKWIDEEQDPIVISSDMELKEAFRLHELNKEw-QLTVL 87

                 ....
Feature 1            
1WMH_A        86 VFPC 89
gi 148225356  98 VFPC 101
gi 54037714   98 VFPC 101
gi 116007694 110 VFPN 113
gi 165905471  94 VFPT 97
gi 68067736   95 VFPS 98
gi 118101016 109 VFPS 112
gi 109044366 106 VFPC 109
gi 156395204  87 LFLG 90
gi 112982924  95 VFPN 98
gi 51701751   92 VFVG 95
gi 76157411   88 VFDG 91

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