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{
"metadata": {
"accession": "PS51713",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
"member_databases": null,
"integrated": "IPR030388",
"hierarchy": null,
"name": {
"name": "Era-type guanine nucleotide-binding (G) domain profile",
"short": "G_ERA"
},
"description": [
{
"text": "<p>The P-loop guanosine triphosphatases (GTPases) control a\nmultitude of biological processes, ranging from cell division, cell cycling,\nand signal transduction, to ribosome assembly and protein synthesis. GTPases\nexert their control by interchanging between an inactive GDP-bound state and\nan active GTP-bound state, thereby acting as molecular switches. The common\ndenominator of GTPases is the highly conserved guanine nucleotide-binding (G)\ndomain that is responsible for binding and hydrolysis of guanine nucleotides.\n\nEra is a small G-protein widely conserved in eubacteria and eukaryotes. It is\nessential for bacterial cell viability and is required for the maturation of\n16S rRNA and assembly of the 30S ribosomal subunit. Era contains an N-terminal\nGTPase domain and a C-terminal distinct derivative of the type-II RNA-binding\nKH domain [[cite:PUB00013952]][[cite:PUB00072549]][[cite:PUB00055805]][[cite:PUB00055804]].\n\nThe Era-type GTPase domain consists of a central six-stranded beta-sheet\nflanked by five alpha-helices, in which the GTP-binding site is located. Guanine nucleotide molecules interact with highly conserved G\nprotein regions G1-G5 [[cite:PUB00055805]].\n\nThe profile we developed covers the entire Era-type G domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00072549": {
"PMID": 10852878,
"ISBN": null,
"volume": "182",
"issue": "12",
"year": 2000,
"title": "Analysis of guanine nucleotide binding and exchange kinetics of the Escherichia coli GTPase Era.",
"URL": null,
"raw_pages": "3460-6",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Sullivan SM",
"Mishra R",
"Neubig RR",
"Maddock JR."
],
"DOI_URL": "http://dx.doi.org/10.1128/JB.182.12.3460-3466.2000"
},
"PUB00013952": {
"PMID": 11916378,
"ISBN": null,
"volume": "317",
"issue": "1",
"year": 2002,
"title": "Classification and evolution of P-loop GTPases and related ATPases.",
"URL": null,
"raw_pages": "41-72",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Leipe DD",
"Wolf YI",
"Koonin EV",
"Aravind L."
],
"DOI_URL": "http://dx.doi.org/10.1006/jmbi.2001.5378"
},
"PUB00055805": {
"PMID": 19706445,
"ISBN": null,
"volume": "106",
"issue": "35",
"year": 2009,
"title": "Structure of ERA in complex with the 3' end of 16S rRNA: implications for ribosome biogenesis.",
"URL": null,
"raw_pages": "14843-8",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Tu C",
"Zhou X",
"Tropea JE",
"Austin BP",
"Waugh DS",
"Court DL",
"Ji X."
],
"DOI_URL": "http://dx.doi.org/10.1073/pnas.0904032106"
},
"PUB00055804": {
"PMID": 21646538,
"ISBN": null,
"volume": "108",
"issue": "25",
"year": 2011,
"title": "The Era GTPase recognizes the GAUCACCUCC sequence and binds helix 45 near the 3' end of 16S rRNA.",
"URL": null,
"raw_pages": "10156-61",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Tu C",
"Zhou X",
"Tarasov SG",
"Tropea JE",
"Austin BP",
"Waugh DS",
"Court DL",
"Ji X."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 26244,
"pathways": 0,
"proteins": 26244,
"proteomes": 18143,
"sets": 0,
"structural_models": {
"alphafold": 20348,
"bfvd": 0
},
"structures": 12,
"taxa": 31552
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3iev",
"name": "Crystal Structure of ERA in Complex with MgGNP and the 3' End of 16S rRNA"
}
}
}
