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. 2005 Apr;25(8):3127–3139. doi: 10.1128/MCB.25.8.3127-3139.2005

FIG. 1.

FIG. 1.

CeBRC-2 possesses a subset of conserved domains present in human BRCA2. A scaled representation of human BRCA2 compared with CeBRC-2 is shown at the top. The various conserved domains, including the BRC repeat region (red), the helical region (yellow), OB folds (green), the tower-like structure (blue), and putative NLSs (black-orange), are indicated. The single BRC motif (residues 9 to 114) in CeBRC-2 is situated at the N terminus of CeBRC-2. Two putative NLSs are located on either side of a single OB fold situated at the C terminus of the protein (residues 263 to 370). aa, amino acids. (A) Protein sequence alignment of the eight BRC motifs of BRCA2 (abbreviated brc1 to brc8) with the single BRC motif of CeBRC-2 (CeBRC-2_brc). Asterisks indicate the critical residues required for the BRC4-Rad51 interaction, as defined structurally (34). (B) Alignment of the OB fold domain of CeBRC-2 (CeBRC-2_OB fold) with the OB fold of RPA1 from six different species (At, A. thaliana; rice; Mus, mouse; Hs, human; Nc, Neurospora crassa; and Ce, C. elegans).