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Rrf2 family transcriptional regulator
Several proteins in this family form iron-sulfur clusters enabling iron dependent DNA transcription regulation [1]. The iron binding is mediated by three conserved cysteine residues. Members of this family can also bind O-acetyl-L-serine, [Fe-S] and nitric oxide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). [1]. 23644595. Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity. Rajagopalan S, Teter SJ, Zwart PH, Brennan RG, Phillips KJ, Kiley PJ;. Nat Struct Mol Biol. 2013;20:740-747. (from Pfam)
Rrf2 family transcriptional regulator similar to nitric oxide-responsive regulator NsrR
This HMM represents a superfamily of probable transcriptional regulators. One member, RRF2 of Desulfovibrio vulgaris is an apparent regulatory protein experimentally (MEDLINE:97293189). The N-terminal region appears related to the DNA-binding biotin repressor region of the BirA bifunctional according to results after three rounds of PSI-BLAST with a fairly high stringency.
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