Araip.95LB8

Gene Details:

Refseq: XP_016180986.1 — cellulose synthase A catalytic subunit 1 [UDP-forming]-like
Refseq: XP_025682682.1 — cellulose synthase A catalytic subunit 1 [UDP-forming]
TrEMBL: A0A444X3B6 — A0A444X3B6_ARAHY; Uncharacterized protein
STRING: GLYMA18G14750.1 — (Glycine max)

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:0005515 — Molecular Function — protein binding
GO:0008270 — Molecular Function — zinc ion binding
GO:0043565 — Molecular Function — sequence-specific DNA binding

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.

CDS Sequence:

>Araip.95LB8|Arachis_ipaensis|bZIP|Araip.95LB8
ATGGATCAAAGTGGTGGAATTGCGACTGGGCCGCGCGATGTCCTAGGAGTTAGGAACGGTTCCGACATTGGGTGTAAACCCTTGAAGAATTTGAATGGTAAAATCTGTCAGATATGTGGCGATACTGTTGGATTAACAGCCACCGGTGATGTTTTTGTTGCTTGCCAAGAATGTTCCTTCCCACTTTGTCACCGTTGCTATGAATGTGAGTGCGAGAATGGGAACCAATCTTGCCCCCAGTGCAAGACCAGATACAATAGTCACAAAGATAGTTCCCATTTGGAGGGAGATGAGGATGATTATGAAGATGATGATGATGTTGATGATATAGAGAATGAGGTAAATTATGGAGAAGGAAACATTAACACAGCAGGGATGCAATGGGAAGAAGATGCTGACCTCTCTTCTTCGTCGGGACATGATTCTCGGATGCCAAATTCAAATCTCCATATGACAAATAGGCAGCCGCTATCTGGTGAAAAACCGTGTGCTACTCCTGATACAAAATCTGTTCAAGCTACATCTGGTCCTTTGGGTCCTTTGGGTCCATCCAAGGCTCACTCACTTTCCTACACCGATTCAAAGCAGCCAGGTCTTGAGAGTGATGAAGAGGTAAGAAGAGTGCCAGAGATCGGAGGTGAATCTGCTGGACCTTCAGCTTCCCGTCCAGGCGCCGGTCCAACTGGTGGGCAAGAACGTGGTCAGGGGACTGGGGATGGTCAACGGAAGAGAGGCAGAAGCCCGGCAGACAAAGAAAACAAACGGCTAAAGAGGCTACTGAGGAACAGAGTGTCAGCTCAACAAGCAAGGGAGAGGAAAAAGGCATATTTGATCGATTTGGAAACCAGAGTCAAAGACTTGGAGAAGAAGAACTCAGAGCTCAAAGAGAGGCTTTCCACTTTGCAGAATGAGAATCAAATGCTAAGACAAATATTAAAGAATACAACAGCTAGCAGGAGAGGGAGCAACAGTGGTACAAATGCTGAATGA

Protein Sequence:

>Araip.95LB8|Arachis_ipaensis|bZIP|Araip.95LB8
MDQSGGIATGPRDVLGVRNGSDIGCKPLKNLNGKICQICGDTVGLTATGDVFVACQECSFPLCHRCYECECENGNQSCPQCKTRYNSHKDSSHLEGDEDDYEDDDDVDDIENEVNYGEGNINTAGMQWEEDADLSSSSGHDSRMPNSNLHMTNRQPLSGEKPCATPDTKSVQATSGPLGPLGPSKAHSLSYTDSKQPGLESDEEVRRVPEIGGESAGPSASRPGAGPTGGQERGQGTGDGQRKRGRSPADKENKRLKRLLRNRVSAQQARERKKAYLIDLETRVKDLEKKNSELKERLSTLQNENQMLRQILKNTTASRRGSNSGTNAE