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JAB domain-containing protein
A family of proteins present widely across the bacteria. This family was named initially with reference to the E. coli radC102 mutation which suggested that RadC was involved in repair of DNA lesions [1]. However the relevant mutation has subsequently been shown to be in recG, where radC is in fact an allele of recG [2]. In addition, a personal communication from Claverys, J-P, et al, indicates a total failure of all attempts to characterise a radiation-related function for RadC in Streptococcus pneumoniae, suggesting that it is not involved in repair of DNA lesions, in recombination during transformation, in gene conversion, nor in mismatch repair. Computational analysis, however, provides a possible function. The RadC-like family belong to the JAB superfamily of metalloproteins [3]. The domain shows fusions to an N-terminal Helix-hairpin-Helix (HhH) domain in most instances. Other domain combinations include fusions to the anti-restriction module ArdC, the DinG/RAD3-like superfamily II helicases and the DNAG-like primase. In some bacteria, closely related DinG/Rad3- like superfamily II helicases are fused to a 3'-5' exonuclease in the same position as the RadC-like JAB domain. These conserved domain associations lead to the hypothesis that the RadC-like JAB domains might function as a nuclease [3]. [1]. 10224240. Tandem repeat recombination induced by replication fork defects in Escherichia coli requires a novel factor, RadC. Saveson CJ, Lovett ST;. Genetics 1999;152:5-13. [2]. 11053371. radC102 of Escherichia coli is an allele of recG. Lombardo MJ, Rosenberg SM;. J Bacteriol. 2000;182:6287-6291. [3]. 21890906. Evolu. TRUNCATED at 1650 bytes (from Pfam)
RadC family protein
RadC was at one time ascribed a role in determining sensitivity to DNA damaging agents such as UV irradiation. Subsequent work casts doubt on that assertion. Three of four members of this family in Escherichia coli K-12, namely YfjY, YkfG, and YeeS, are found in prophage regions.
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