Gene Details:

  • Gene ID: Aqcoe7G272800.1.p
  • Gene Family: bZIP Family
  • Description: bZIP Family protein
  • Species: Aquilegia coerulea
  • Source: bZIP family gene from PlantTFDB

Protein Features:

Annotation Proteins:

  • Refseq:  XP_010250037.1  — PREDICTED: transcription factor HY5
  • Swissprot:  Q9SM50  — HY5_SOLLC; Transcription factor HY5
  • TrEMBL:  A0A2G5FC48  — A0A2G5FC48_AQUCA; Uncharacterized protein
  • STRING:  Aquca_001_00822.1  — (Aquilegia coerulea)

Gene Ontology:

  • GO:0006355  — Biological Process — regulation of transcription, DNA-templated
  • GO:0009737  — Biological Process — response to abscisic acid
  • GO:0009740  — Biological Process — gibberellic acid mediated signaling pathway
  • GO:0010017  — Biological Process — red or far-red light signaling pathway
  • GO:0010099  — Biological Process — regulation of photomorphogenesis
  • GO:0010114  — Biological Process — response to red light
  • GO:0010218  — Biological Process — response to far red light
  • GO:0010224  — Biological Process — response to UV-B
  • GO:0031539  — Biological Process — positive regulation of anthocyanin metabolic process
  • GO:0042753  — Biological Process — positive regulation of circadian rhythm
  • GO:0080167  — Biological Process — response to karrikin
  • GO:0005634  — Cellular Component — nucleus
  • GO:0003690  — Molecular Function — double-stranded DNA binding
  • GO:0003700  — Molecular Function — transcription factor activity, sequence-specific DNA binding
  • GO:0043565  — Molecular Function — sequence-specific DNA binding

Family Introduction:

  • The bZIP domain consists of two structural features located on a contiguous alpha-helix: first, a basic region of ~ 16 amino acid residues containing a nuclear localization signal followed by an invariant N-x7-R/K motif that contacts the DNA; and, second, a heptad repeat of leucines or other bulky hydrophobic amino acids positioned exactly nine amino acids towards the C-terminus, creating an amphipathic helix. To bind DNA, two subunits adhere via interactions between the hydrophobic sides of their helices, which creates a superimposing coiled-coil structure. The ability to form homo- and heterodimers is influenced by the electrostatic attraction and repulsion of polar residues flanking the hydrophobic interaction surface of the helices.
  • Plant bZIP proteins preferentially bind to DNA sequences with an ACGT core. Binding specificity is regulated by flanking nucleotides. Plant bZIPs preferentially bind to the A-box (TACGTA), C-box (GACGTC) and G-box (CACGTG), but there are also examples of nonpalindromic binding sites.

Literature:

Sequences:

CDS Sequence:
  • >Aqcoe7G272800.1.p|Aquilegia_coerulea|bZIP|Aqcoe7G272800.1.p
    ATGCAAGAACAAGCAGCAAGTTCATTTCCAGCTAATTCTCTTCCTTCAAGTAGTGAGAGATCTTCTAGCTCTGCTCTTCAACTTGAAATCAAAGATGGGATGGAGAGTGATGATGAGATAAGAAGAGTGCCTGAAATGGGGAGTGAAGGAGGAGGAGGAGGAGTTGGTCCATCAACATCAGGTCGAGGAGAAGCGGGTTCAGACCAGGTTCAGGGATCTACAGAAGGTGGAGGAGGAGGAACTACACAGAAAAAAAGAGGTAGAAGTCCAGCTGACAAAGAAAACAAGCGATTGAAAAGGTTGCTGAGGAACAGAGTTTCAGCTCAACAAGCAAGAGAAAGAAAAAAGGCCTACTTGAGTGAGCTGGAGGTCAAAGTTAAGGAATTGGAAAAGAAAAACTCTGAGCTTGAAGAAAGACTCTCCACGTTGCAAAATGAGAATCAGATGCTTAGACATATACTGAAGAATACAACTGCAAGCAGGAGGGAGTAG
Protein Sequence:
  • >Aqcoe7G272800.1.p|Aquilegia_coerulea|bZIP|Aqcoe7G272800.1.p
    MQEQAASSFPANSLPSSSERSSSSALQLEIKDGMESDDEIRRVPEMGSEGGGGGVGPSTSGRGEAGSDQVQGSTEGGGGGTTQKKRGRSPADKENKRLKRLLRNRVSAQQARERKKAYLSELEVKVKELEKKNSELEERLSTLQNENQMLRHILKNTTASRRE*