Summary: Translation initiation factor IF-3, N-terminal domain
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Translation initiation factor IF-3 Edit Wikipedia article
|Translation initiation factor IF-3, N-terminal domain|
translation initiation factor 3 n-terminal domain
|Translation initiation factor IF-3, C-terminal domain|
translation initiation factor 3 c-terminal domain
In molecular biology, translation initiation factor IF-3 (gene infC) is one of the three factors required for the initiation of protein biosynthesis in bacteria. IF-3 is thought to function as a fidelity factor during the assembly of the ternary initiation complex which consists of the 30S ribosomal subunit, the initiator tRNA and the messenger RNA. IF-3 is a basic protein that binds to the 30S ribosomal subunit. The chloroplast initiation factor IF-3(chl) is a protein that enhances the poly(A,U,G)-dependent binding of the initiator tRNA to chloroplast ribosomal 30s subunits in which the central section is evolutionary related to the sequence of bacterial IF-3.
- Liveris D, Schwartz JJ, Geertman R, Schwartz I (September 1993). "Molecular cloning and sequencing of infC, the gene encoding translation initiation factor IF3, from four enterobacterial species". FEMS Microbiol. Lett. 112 (2): 211–6. doi:10.1111/j.1574-6968.1993.tb06450.x. PMID 8405963.
- Lin Q, Ma L, Burkhart W, Spremulli LL (April 1994). "Isolation and characterization of cDNA clones for chloroplast translational initiation factor-3 from Euglena gracilis". J. Biol. Chem. 269 (13): 9436–44. PMID 8144528.
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This tab holds annotation information from the InterPro database.
InterPro entry IPR019814
Initiation factor 3 (IF-3) (gene infC) is one of the three factors required for the initiation of protein biosynthesis in bacteria. IF-3 is thought to function as a fidelity factor during the assembly of the ternary initiation complex which consist of the 30S ribosomal subunit, the initiator tRNA and the messenger RNA. IF-3 is a basic protein that binds to the 30S ribosomal subunit [ PUBMED:8405963 ]. The chloroplast initiation factor IF-3(chl) is a protein that enhances the poly(A,U,G)-dependent binding of the initiator tRNA to chloroplast ribosomal 30s subunits in which the central section is evolutionary related to the sequence of bacterial IF-3 [ PUBMED:8144528 ].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||translation initiation factor activity (GO:0003743)|
|Biological process||translational initiation (GO:0006413)|
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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|Seed source:||Pfam-B_629 (release 2.1)|
|Author:||Bateman A , Finn RD|
|Number in seed:||445|
|Number in full:||8982|
|Average length of the domain:||66.00 aa|
|Average identity of full alignment:||48 %|
|Average coverage of the sequence by the domain:||32.97 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||19|
|Download:||download the raw HMM for this family|
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the IF3_N domain has been found. There are 18 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.