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. 2021 Apr 23;9:668309. doi: 10.3389/fcell.2021.668309

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Copyright © 2021 Li and Engebrecht.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Domain structure of BRCA2 proteins. Human BRCA2 encodes an exceptionally large protein with an N-terminal PALB2 binding domain, eight BRC repeats, a DSS1 and DNA binding domain (DBD) composed of one helix-rich domain (HD), three oligonucleotide/oligosaccharide binding (OB) folds and a tower domain, and a C terminal RAD51 binding domain (CTRB). C. elegans BRC-2 represents a simplified version with a single BRC repeat and OB fold. The number of BRC repeats and OB fold domains vary greatly in different organisms (U. maydis Brh2, A. thaliana BRCA2A/B, T. brucei BRCA2 and D. melanogaster BRCA2). Sequence alignment did not identify a putative OB fold/DNA binding domain in Drosophila BRCA2 (Yang et al., 2002).