This family includes the DUF34/metal-binding protein/NIF3 proteins, which are widely distributed across superkingdoms. They were previously annotated as GTP cyclohydrolase 1 type 2 [3] and, recently, through a comprehensive literature review and integrative bioinformatic analyses it was revealed that annotations for these members were misleading as they were based on a single set of in vitro results examining the NIF3 homolog of Helicobacter pylori [3]. Actually, they have varied phenotypes with the unifying functional role as metal-binding proteins [4]. This entry contains several NIF3 (NGG1p interacting factor 3) protein homologues. NIF3 interacts with the yeast transcriptional coactivator NGG1p which is part of the ADA complex, the exact function of this interaction is unknown [1,2]. [1]. 8663102. Transcriptional activation by yeast PDR1p is inhibited by its association with NGG1p/ADA3p. Martens JA, Genereaux J, Saleh A, Brandl CJ;. J Biol Chem 1996;271:15884-15890. [2]. 11124544. Isolation and characterization of a novel human gene, NIF3L1, and its mouse ortholog, Nif3l1, highly conserved from bacteria to mammals. Tascou S, Uedelhoven J, Dixkens C, Nayernia K, Engel W, Burfeind P;. Cytogenet Cell Genet 2000;90:330-336. [3]. 23825549. Biochemical Characterization of Hypothetical Proteins from Helicobacter pylori. Choi HP, Juarez S, Ciordia S, Fernandez M, Bargiela R, Albar JP, Mazumdar V, Anton BP, Kasif S, Ferrer M, Steffen M;. PLoS One. 2013;8:e66605. [4]. 34572495. Comparative Genomic Analysis of the DUF34 Protein Family Suggests Role as a Metal Ion Chaperone or Insertase. Reed CJ, Hutinet G, de Crecy-Lagard V;. Bi. TRUNCATED at 1650 bytes (from Pfam)
- Date:
- 2024-10-16