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{
    "metadata": {
        "accession": "cd03693",
        "entry_id": null,
        "type": "domain",
        "go_terms": null,
        "source_database": "cdd",
        "member_databases": null,
        "integrated": null,
        "hierarchy": null,
        "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>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00033961": {
                "PMID": 12102560,
                "ISBN": null,
                "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.",
                "URL": null,
                "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"
            },
            "PUB00079814": {
                "PMID": 11909526,
                "ISBN": null,
                "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"
        },
        "overlaps_with": null,
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 0,
            "interactions": 0,
            "matches": 57086,
            "pathways": 0,
            "proteins": 57042,
            "proteomes": 3906,
            "sets": 1,
            "structural_models": {
                "alphafold": 48932,
                "bfvd": 0
            },
            "structures": 34,
            "taxa": 56727
        },
        "entry_annotations": {},
        "cross_references": {},
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": null
    }
}