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{
"metadata": {
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"type": "domain",
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"source_database": "cdd",
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"name": {
"name": "Domain II of elongation factor 1-alpha",
"short": "EF1_alpha_II"
},
"description": [
{
"text": "<p>This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression. [[cite:PUB00115982], [cite:PUB00115983], [cite:PUB00115094], [cite:PUB00080181], [cite:PUB00033952], [cite:PUB00027704], [cite:PUB00033961], [cite:PUB00079814], [cite:PUB00007398]]</p>",
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"PUB00033961": {
"PMID": 12102560,
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"volume": "71",
"issue": null,
"year": 2002,
"title": "Mechanisms of EF-Tu, a pioneer GTPase.",
"URL": null,
"raw_pages": "513-51",
"medline_journal": "Prog Nucleic Acid Res Mol Biol",
"ISO_journal": "Prog. Nucleic Acid Res. Mol. Biol.",
"authors": [
"Krab IM",
"Parmeggiani A."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0079-6603(02)71050-7"
},
"PUB00115094": {
"PMID": 10950927,
"ISBN": null,
"volume": "68",
"issue": "1",
"year": 2000,
"title": "The human elongation factor 1 A-2 gene (EEF1A2): complete sequence and characterization of gene structure and promoter activity.",
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"raw_pages": "63-70",
"medline_journal": "Genomics",
"ISO_journal": "Genomics",
"authors": [
"Bischoff C",
"Kahns S",
"Lund A",
"Jorgensen HF",
"Praestegaard M",
"Clark BF",
"Leffers H."
],
"DOI_URL": null
},
"PUB00027704": {
"PMID": 16213500,
"ISBN": null,
"volume": "579",
"issue": "25",
"year": 2005,
"title": "How can elongation factors EF-G and EF-Tu discriminate the functional state of the ribosome using the same binding site?",
"URL": null,
"raw_pages": "5439-42",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Sergiev PV",
"Bogdanov AA",
"Dontsova OA."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.febslet.2005.09.010"
},
"PUB00007398": {
"PMID": 7491491,
"ISBN": null,
"volume": "270",
"issue": "5241",
"year": 1995,
"title": "Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog.",
"URL": null,
"raw_pages": "1464-72",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Nissen P",
"Kjeldgaard M",
"Thirup S",
"Polekhina G",
"Reshetnikova L",
"Clark BF",
"Nyborg J."
],
"DOI_URL": "http://www.sciencemag.org/cgi/content/abstract/270/5241/1464"
},
"PUB00115982": {
"PMID": 16652225,
"ISBN": null,
"volume": "286",
"issue": "1-2",
"year": 2006,
"title": "Identification of elongation factor 1alpha as a potential associated binding partner for Akt2.",
"URL": null,
"raw_pages": "17-22",
"medline_journal": "Mol Cell Biochem",
"ISO_journal": "Mol Cell Biochem",
"authors": [
"Lau J",
"Castelli LA",
"Lin EC",
"Macaulay SL."
],
"DOI_URL": null
},
"PUB00115983": {
"PMID": 11854414,
"ISBN": null,
"volume": "13",
"issue": "2",
"year": 2002,
"title": "Interactions of elongation factor 1alpha with F-actin and beta-actin mRNA: implications for anchoring mRNA in cell protrusions.",
"URL": null,
"raw_pages": "579-92",
"medline_journal": "Mol Biol Cell",
"ISO_journal": "Mol Biol Cell",
"authors": [
"Liu G",
"Grant WM",
"Persky D",
"Latham VM Jr",
"Singer RH",
"Condeelis J."
],
"DOI_URL": null
},
"PUB00033952": {
"PMID": 15922593,
"ISBN": null,
"volume": "15",
"issue": "3",
"year": 2005,
"title": "Elongation factors on the ribosome.",
"URL": null,
"raw_pages": "349-54",
"medline_journal": "Curr Opin Struct Biol",
"ISO_journal": "Curr. Opin. Struct. Biol.",
"authors": [
"Nilsson J",
"Nissen P."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.sbi.2005.05.004"
},
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"PMID": 11909526,
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"volume": "108",
"issue": "4",
"year": 2002,
"title": "Ribosome structure and the mechanism of translation.",
"URL": null,
"raw_pages": "557-72",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Ramakrishnan V."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0092-8674(02)00619-0"
},
"PUB00080181": {
"PMID": 15952884,
"ISBN": null,
"volume": "74",
"issue": null,
"year": 2005,
"title": "Structural insights into translational fidelity.",
"URL": null,
"raw_pages": "129-77",
"medline_journal": "Annu Rev Biochem",
"ISO_journal": "Annu. Rev. Biochem.",
"authors": [
"Ogle JM",
"Ramakrishnan V."
],
"DOI_URL": "http://dx.doi.org/10.1146/annurev.biochem.74.061903.155440"
}
},
"set_info": {
"accession": "cl02787",
"name": "Translation_Factor_II_like"
},
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},
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}