A homology domain shared between Drosophila optomotor-blind and mouse Brachyury is involved in DNA binding.
The distribution of sequence elements divides the optomotor-blind protein into three regions and is suggestive of a transcriptional regulatory role of this protein. The central region of Omb is homologous to the N-terminal half of the Brachyury protein. The conserved domain of Omb is here shown to possess general DNA binding affinity but has no significant similarity to recognized DNA binding motifs.
Pflugfelder
G O
GO
Theodor-Boveri-Institut, Lehrstuhl für Genetik, Würzburg, Germany.
Roth
H
H
Poeck
B
B
D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D004268:DNA-Binding Proteins / Q000235:genetics*; D004330:Drosophila / Q000235:genetics*; D029721:Drosophila Proteins; D005326:Fetal Proteins / Q000235:genetics*; D051379:Mice; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D020825:T-Box Domain Proteins; D000098908:Brachyury Protein
D004247:DNA; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D005326:Fetal Proteins; D009419:Nerve Tissue Proteins; D020825:T-Box Domain Proteins; D000098908:Brachyury Protein; C072962:bi protein, Drosophila