PROSITE documentation PDOC51750Bro-N domain profile
The baculovirus Bro proteins are encoded by a multigene family. The typical Bro proteins that have been experimentally investigated are BroA, BroC and BroD from Bombyx mori uclear polyhedrosis virus (BmNV). They contain distinct amino- and carboxy-terminal domains (Bro-N and Bro-C, respectively) that are present independently of each other and in distinct contexts in a variety of other viral proteins. The Bro-N domain occurs in a stand-alone form or combined with other domains in proteins from temperate phages that infect Gram-positive bacteria and Myxococcus xanthus, and proteins encoded in the genomes of proteobacteria and Gram positive bacteria. The Bro-N domain appears to define a distinct superfamily of widespread viral DNA-binding domains [1].
Multiple alignment-based secondary-structure prediction of the Bro-N domain reveals a core with two head-to-tail units of a β-hairpin followed by an α-helix. The multiple alignment shows that the Bro-N domains contain two highly conserved aromatic or hydrophobic residues at the end of the second and forth conserved strands [1].
The profile we developed covers the entire Bro-N domain.
Last update:March 2015 / First entry.
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1 | Authors | Iyer L.M. Koonin E.V. Aravind L. |
Title | Extensive domain shuffling in transcription regulators of DNA viruses and implications for the origin of fungal APSES transcription factors. | |
Source | Genome Biol. 3:RESEARCH0012-RESEARCH0012(2002). | |
PubMed ID | 11897024 |
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