Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC51658Bifunctional nuclease (BFN) domain profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC51658
The bifunctional nuclease (BFN) domain is specific to bacteria and plant organisms. It has both RNase and DNase activities [1].
The dimer of the BFN domain forms a wedge, each monomer being a basic triangular shape. The BFN domain is composed of an eight-stranded, distorted β-sheet consisting of a four-stranded, antiparallel β-sheet (B1, B2, B3, B8), and a four-stranded mixed β-sheet (B4, B5, B6, B7). The sheets are intercalated by three short α-helices (H1, H3, H4), while a longer α-helix (H2) forms the central core of the dimer interface [2].
Some proteins known to contain a BFN domain are listed below:
- Thermotoga maritima TM0160, a conserved hypothetical protein.
- Plant bifunctional nuclease in basal defense response (BBD) proteins, regulators in abscisic acid (ABA)-mediated defense responses.
The profile we developed covers the entire BFN domain.
Last update:October 2012 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | You M.K. Shin H.Y. Kim Y.J. Ok S.H. Cho S.K. Jeung J.U. Yoo S.D. Kim J.K. Shin J.S. |
| Title | Novel bifunctional nucleases, OmBBD and AtBBD1, are involved in abscisic acid-mediated callose deposition in Arabidopsis. | |
| Source | Plant Physiol. 152:1015-1029(2010). | |
| PubMed ID | 20018603 | |
| DOI | 10.1104/pp.109.147645 |
| 2 | Authors | Spraggon G. Pantazatos D. Klock H.E. Wilson I.A. Woods V.L. Jr. Lesley S.A. |
| Title | On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171. | |
| Source | Protein Sci. 13:3187-3199(2004). | |
| PubMed ID | 15557262 | |
| DOI | 10.1110/ps.04939904 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.