EcC054823.150

Gene Details

Gene ID: EcC054823.150
Gene Family: bHLH Family
Description: bHLH Family protein
Species: Eucalyptus camaldulensis
Source: bHLH family gene from PlantTFDB

Functional Annotation

Refseq: XP_010061618.1 — PREDICTED: transcription factor bHLH74
Refseq: XP_010061619.1 — PREDICTED: transcription factor bHLH74
Swissprot: Q6NKN9 — BH074_ARATH; Transcription factor bHLH74
TrEMBL: A0A059BSH8 — A0A059BSH8_EUCGR; Uncharacterized protein
STRING: XP_010061617.1 — (Eucalyptus grandis)

GO:0006355 — Biological Process — regulation of transcription, DNA-templated
GO:0006468 — Biological Process — protein phosphorylation
GO:0006506 — Biological Process — GPI anchor biosynthetic process
GO:0006508 — Biological Process — proteolysis
GO:0006816 — Biological Process — calcium ion transport
GO:0007018 — Biological Process — microtubule-based movement
GO:0015074 — Biological Process — DNA integration
GO:0055114 — Biological Process — oxidation-reduction process
GO:0071805 — Biological Process — potassium ion transmembrane transport
GO:0016021 — Cellular Component — integral component of membrane
GO:0003700 — Molecular Function — transcription factor activity, sequence-specific DNA binding
GO:0003777 — Molecular Function — microtubule motor activity
GO:0004185 — Molecular Function — serine-type carboxypeptidase activity
GO:0004190 — Molecular Function — aspartic-type endopeptidase activity
GO:0004506 — Molecular Function — squalene monooxygenase activity
GO:0004584 — Molecular Function — dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase activity
GO:0004672 — Molecular Function — protein kinase activity
GO:0005388 — Molecular Function — calcium-transporting ATPase activity
GO:0005524 — Molecular Function — ATP binding
GO:0008017 — Molecular Function — microtubule binding
GO:0015079 — Molecular Function — potassium ion transmembrane transporter activity
GO:0043565 — Molecular Function — sequence-specific DNA binding
GO:0046872 — Molecular Function — metal ion binding
GO:0046983 — Molecular Function — protein dimerization activity
GO:0050660 — Molecular Function — flavin adenine dinucleotide binding

Family Introduction

The basic/helix-loop-helix (bHLH) proteins are a superfamily of transcription factors that have been well characterized in nonplant eukaryotes, especially in mammalian systems, in which considerable structural, functional, and phylogenetic analyses have been performed. The data indicate that bHLH proteins are important regulatory components in transcriptional networks in these systems, controlling a diversity of processes from cell proliferation to cell lineage establishment.
This family is defined by the bHLH signature domain, which consists of 60 amino acids with two functionally distinct regions. The basic region, located at the N-terminal end of the domain, is involved in DNA binding and consists of 15 amino acids with a high number of basic residues. The HLH region, at the C-terminal end, functions as a dimerization domain and is constituted mainly of hydrophobic residues that form two amphipathic -helices separated by a loop region of variable sequence and length. Outside of the conserved bHLH domain, these proteins exhibit considerable sequence divergence. Cocrystal structural analysis has shown that the interaction between the HLH regions of two separate polypeptides leads to the formation of homodimers and/or heterodimers and that the basic region of each partner binds to half of the DNA recognition sequence. Some bHLH proteins form homodimers or restrict their heterodimerization activity to closely related members of the family. On the other hand, some can form heterodimers with one or several different partners.
The core DNA sequence motif recognized by the bHLH proteins is a consensus hexanucleotide sequence known as the E-box (5’-CANNTG-3’). There are different types of E-boxes, depending on the identity of the two central bases. One of the most common is the palindromic G-box (5’-CACGTG-3’). Certain conserved amino acids within the basic region of the protein provide recognition of the core consensus site, whereas other residues in the domain dictate specificity for a given type of E-box . In addition, flanking nucleotides outside of the hexanucleotide core have been shown to play a role in binding specificity, and there is evidence that a loop residue in the protein plays a role in DNA binding through elements that lie outside of the core recognition sequence.

Literature and News

Gene Resources

Sequences