The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins and in eukaryotic F-box proteins. The domain is named after the bacterial apaG protein, of which it forms the core. The domain also occurs in the C-terminal part of eukaryotic proteins with an N-terminal F-box domain. The Salmonella typhimurium apaG domain protein corD is involved in Co(2+) resistance and Mg(2+) efflux. Tertiary structures from different apaG proteins show a fold of several beta-sheets. The apaG domain may be involved in protein-protein interactions which could be implicated in substrate-specificity [1,2,3,4]. [1]. 1779764. Magnesium transport in Salmonella typhimurium: the influence of new mutations conferring Co2+ resistance on the CorA Mg2+ transport system. Gibson MM, Bagga DA, Miller CG, Maguire ME;. Mol Microbiol 1991;5:2753-2762. [2]. 10945468. cDNA cloning and expression analysis of new members of the mammalian F-box protein family. Ilyin GP, Rialland M, Pigeon C, Guguen-Guillouzo C;. Genomics. 2000;67:40-47. [3]. 12522211. Identification of a novel protein, PDIP38, that interacts with the p50 subunit of DNA polymerase delta and proliferating cell nuclear antigen. Liu L, Rodriguez-Belmonte EM, Mazloum N, Xie B, Lee MY;. J Biol Chem. 2003;278:10041-10047. [4]. 15213450. 1H, 15N and 13C resonance assignments of the ApaG protein of the phytopathogen Xanthomonas axonopodis pv. citri. Katsuyama AM, Cicero DO, Spisni A, Paci M, Farah CS, Pertinhez TA;. J Biomol NMR. 2004;29:423-424. (from Pfam)
- Date:
- 2024-10-16