1GJI


Conserved Protein Domain Family
RHD-n_c-Rel

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cd07933: RHD-n_c-Rel 
Click on image for an interactive view with Cn3D
N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel
Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the c-Rel family of transcription factors, categorized as a class II member of the NF-kappa B family. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). c-Rel plays an important role in B cell proliferation and survival.
Statistics
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PSSM-Id: 143649
View PSSM: cd07933
Aligned: 4 rows
Threshold Bit Score: 361.5
Threshold Setting Gi: 21465438
Created: 15-Sep-2009
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
DNA binding
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:DNA binding site [nucleic acid binding site]
Evidence:
  • Structure:1GJI_A: Gallus gallus c-Rel monomer binds DNA, contacts at 4A
    View structure with Cn3D
  • Structure:1GJI: Gallus gallus c-Rel dimer binds DNA, contacts at 4A
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                      # ## ##  #                                                        
1GJI_A         1 PYIEIFEQPRQRgMRFRYKCEgRSAGSIPGEHSTDNNKTFPSIQILNYFgKVKIRTTLVTKNEPYKPHPHDLVGKDCRDG 80
gi 37725726   18 PCVQIFEQPKQRgMRFRYKCEgRSAGSIPGERSSDNNRTYPSIQILNVTgKGKVRVTLVTKSEPYKPHPHDLVGKDCKDG 97
gi 213626042   7 PYIEIFEQPRQRgMRYRYKCEgRSAGSILGERSTENNRTYPSIKIMNYTgKGIVRITLVTKNEPHKPHPHDLVGKDCRDG 86
gi 585812      8 PYVEIIEQPRQRgMRFRYKCEgRSAGSIPGERSTDNNRTYPSVQIMNYYgKGKIRITLVTKNDPYKPHPHDLVGKDCRDG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                               ##                                                       
1GJI_A        81 YYEAEFGpERRVLSFQNLGIQCVKKKDLKESISLRISKKINPFNVPEEqlhnidEYDLNVVRLCFQAFLPdehgnytLAL 160
gi 37725726   98 YYEAEFGpERRAIAFQNLGIQCVRRREVKDAIMQRVTRGINPFNVPREqllqteEYDLNVVRLCFQIYLQdesgmysTML 177
gi 213626042  87 YYELEFGsDRTVLCFQNLGIQCVRRREVREAIHARIIRKMNPFGVREEqlltieDYDLNVVRLCLQVFLPdehgnytRAL 166
gi 585812     88 YYEAEFGpERRPLFFQNLGIRCVKKKEVKGAIILRISAGINPFNVGEQqlldieDCDLNVVRCVFMFFLPdedgnftTAL 167
                        170
                 ....*....|..
Feature 1                   #
1GJI_A       161 PPLISNPIYDNR 172
gi 37725726  178 PPIVSNPIYDNR 189
gi 213626042 167 TPVVSNPIYDNR 178
gi 585812    168 PPIVSNPIYDNR 179

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