Genomic Location: MJ1479.1 is encoded on the large circular chromosome of M. jannaschii (NCBI RefSeq: NC_000909).
Sequence Characteristics:
Length: Based on homologous ORFs in M. jannaschii, uncharacterized proteins typically range from 100–500 amino acids.
Conservation: Preliminary BLAST analyses suggest MJ1479.1 lacks close homologs in bacterial or eukaryotic genomes, a common feature of archaeal-specific genes .
Domain Prediction: Tools like InterProScan may reveal conserved domains, though no such data is publicly available for MJ1479.1.
While MJ1479.1 has not been explicitly studied, established protocols for homologous recombination and recombinant protein expression in M. jannaschii provide a framework for its investigation:
Thermostability: M. jannaschii proteins often require high-temperature expression systems (e.g., E. coli with thermostable tRNA) .
Solubility: Archaeal proteins may form inclusion bodies in mesophilic hosts, necessitating refolding protocols.
Uncharacterized proteins like MJ1479.1 are often prioritized for study based on:
Operon Context: Adjacent genes may hint at metabolic or regulatory roles (e.g., cofactor biosynthesis, stress response).
Phylogenetic Distribution: Proteins unique to methanogens may relate to methane metabolism or extremophile adaptations .
Structural Homology: Comparison to proteins with solved structures (e.g., DEAD box helicase MJ0669 ) could infer ATPase or nucleic acid-binding activity.
Functional Assays: Activity screening under anaerobic, high-temperature conditions (e.g., enzymatic assays with potential substrates like H₂, CO₂, or methylated cofactors).
Structural Studies: X-ray crystallography or cryo-EM could resolve tertiary structure, as done for M. jannaschii DEAD box protein (PDB: 1I5K) .
Interaction Networks: Co-purification or yeast two-hybrid studies may identify binding partners.
Characterizing MJ1479.1 could: