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Electronic supplementary material S3. a). A. B. B. C 1. C 2. b). R. W. R. L. N. P. P. T. E. T. G. Q. H. T. P. F. L. C. C. N. N. Zn. T. A. C. C. AAGGANALPTT. GLFLKLHGVVRPLSLKTDVIKKRNRGS. ●. ●. ▲. ■. ●. ●. ●. ■. 697. 751. b 3. b 4. a. loop. b 1. b 2.
E N D
B B C1 C2
b) R W R L N P P T E T G Q H T P F L C C N N Zn T A C C AAGGANALPTT GLFLKLHGVVRPLSLKTDVIKKRNRGS ● ● ▲ ■ ● ● ● ■ 697 751 b3 b4 a loop b1 b2 ■ ● ● ■ ■ ● ● □ ○ Electronic supplementary material S3. Amino acid sequence analysis of the T. borchii deduced major nitrogen regulator polypeptide TBNRE1. a) Alignment of the predicted TBNRE1 polypeptide (TBNRE1) with the homologous polypeptides AreA of Aspergillus nidulans (AnAreA; GenBank XM_676844), NIT-2 of Neurospora crassa (NcNit2; GenBank M33956), AreA of Gibberella fujikuroi (GfAreA; GenBank Y11006), NUT1 of Magnaporthe grisea (MgNut1; GenBank XM_366679) and NRE of Penicillum crysogenum (PcNre; GenBank U02612). The region indicated by A shows a conserved amino-acid sequence placed at the N-terminal domain. The central-zinc finger domain (B), involved in nucleotide binding, is highly conserved. Finally, the regions C1 and C2, placed in the C-terminal domain, show the two highly conserved motives VIPIAAAAPPK and EWEWLTMSL . b) Zinc-finger element of the TBNRE1 protein, the four cysteine residues are shown coordinating a zinc atom with a loop of 17 amino acids residues. The negatively charged region immediately downstream of the zinc finger is shown. Comparison of the TBNRE1 zinc finger and downstream basic region with AnAreA, NcNit2, GfAreA, MgNut1 and PcNre zinc finger domain is also reported. The raised horizontal lines indicate the extents of b-strands 1 to 4, the alpha-helix, and the extended loop. Residues involved in DNA contacts are indicated as follows: major groove, filled symbols; minor groove, open symbols; hydrophobic interactions, circles; electrostatic interactions, squares; hydrogen bonds, triangles; interactions involving backbone amide or alpha protons, diamonds.