Summary: Basic region leucine zipper
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This is the Wikipedia entry entitled "BZIP domain". More...
BZIP domain Edit Wikipedia article
Basic Leucine zipper domain (bZIP domain) The bZIP domain is found in many DNA binding eukaryotic proteins. One part of the domain contains a region that mediates sequence specific DNA binding properties and the Leucine zipper that is required for the dimerization of two DNA binding regions. The DNA binding region comprises a number of basic aminoacids such as arginine and lysine
bZIP domain containing proteins
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Basic region leucine zipper Provide feedback
No Pfam abstract.
Literature references
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Jakoby M, Weisshaar B, Droge-Laser W, Vicente-Carbajosa J, Tiedemann J, Kroj T, Parcy F; , Trends Plant Sci 2002;7:106-111.: bZIP transcription factors in Arabidopsis. PUBMED:11906833 EPMC:11906833
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Sinclair AJ; , J Gen Virol 2003;84:1941-1949.: bZIP proteins of human gammaherpesviruses. PUBMED:12867624 EPMC:12867624
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Hurst HC; , Protein Profile 1995;2:101-168.: Transcription factors 1: bZIP proteins. PUBMED:7780801 EPMC:7780801
Internal database links
SCOOP: | ADIP APC_N_CC ASD2 ATG16 bZIP_1 bZIP_Maf CENP-F_leu_zip FlaC_arch GIT_CC HALZ HAP1_N KASH_CCD LMBR1 Macoilin NTP_transf_5 Phlebovirus_NSM SHE3 SR-25 XhlA YabA ZapB |
Similarity to PfamA using HHSearch: | bZIP_1 bZIP_Maf |
External database links
SMART: | SM00338 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR004827
The basic-leucine zipper (bZIP) domain transcription factors [ PUBMED:7780801 ] of eukaryotic are proteins that contain a basic region mediating sequence-specific DNA-binding followed by a leucine zipper region required for dimerisation.
Several structure of bZIP have been solved. The basic region and the leucine zipper form a contiguous alpha helice where the four hydrophobic residues of the leucine zipper are oriented on one side. This conformation allows dimerization in parallel and it bends the helices so that the newly functional dimer forms a flexible fork where the basic domains, at the N-terminal open end, can then interact with DNA. The two leucine zipper are therefore oriented perpendicular to the DNA [ PUBMED:1473154 ].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | DNA-binding transcription factor activity (GO:0003700) |
Biological process | regulation of transcription, DNA-templated (GO:0006355) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
Alignments
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Seed (41) |
Full (10541) |
Representative proteomes | UniProt (17994) |
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RP15 (2173) |
RP35 (4776) |
RP55 (8329) |
RP75 (10931) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (41) |
Full (10541) |
Representative proteomes | UniProt (17994) |
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RP15 (2173) |
RP35 (4776) |
RP55 (8329) |
RP75 (10931) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | PfamB-200; Release 14.0; |
Previous IDs: | none |
Type: | Coiled-coil |
Sequence Ontology: | SO:0001080 |
Author: |
Studholme DJ |
Number in seed: | 41 |
Number in full: | 10541 |
Average length of the domain: | 53.7 aa |
Average identity of full alignment: | 31 % |
Average coverage of the sequence by the domain: | 17.07 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 54 | ||||||||||||
Family (HMM) version: | 18 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the bZIP_2 domain has been found. There are 413 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.