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{
"metadata": {
"accession": "IPR001278",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0004814",
"name": "arginine-tRNA ligase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0005524",
"name": "ATP binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006420",
"name": "arginyl-tRNA aminoacylation",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"hamap": {
"MF_00123": "Arginine--tRNA ligase [argS]"
},
"ncbifam": {
"TIGR00456": "arginine--tRNA ligase"
},
"panther": {
"PTHR11956": "ARGINYL-TRNA SYNTHETASE"
},
"prints": {
"PR01038": "TRNASYNTHARG"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR001278",
"name": "Arginine-tRNA ligase",
"type": "Family",
"children": []
},
"name": {
"name": "Arginine-tRNA ligase",
"short": "Arg-tRNA-ligase"
},
"description": [
{
"text": "<p>Arginine-tRNA ligase ([ec:6.1.1.19]) has been crystallized and preliminary X-ray crystallographic analysis of yeast arginine-tRNA ligase-yeast tRNAArg complexes is available [[cite:PUB00006576]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [[cite:PUB00079872], [cite:PUB00079873]]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [[cite:PUB00007191]].</p>\n\n<p>The 20 aminoacyl-tRNA synthetases are divided into two classes. Class I synthetases contain a characteristic Rossmann fold catalytic domain and are predominantly monomeric [[cite:PUB00006477]]. Class II synthetases feature an antiparallel β-sheet fold flanked by α-helices [[cite:PUB00000386]] and are mostly dimeric or multimeric, with at least three conserved regions [[cite:PUB00000723], [cite:PUB00005365], [cite:PUB00004391]]. Despite these structural differences, both classes share a conserved α-helical structure involved in tRNA binding.</p>\n\n<p>The two classes also differ in their catalytic mechanisms: class I synthetases couple the aminoacyl group to the 2'-hydroxyl of the tRNA, whereas class II synthetases preferentially use the 3'-hydroxyl site.</p>\n\n<p>Class I includes synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic). Class II includes those specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine, and some lysine synthetases (non-archaeal).</p>\n\n<p>Based on their mode of binding to the tRNA acceptor stem, each class has been further subdivided into three subclasses: 1a, 1b, 1c and 2a, 2b, 2c [[cite:PUB00007363]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00004391": {
"PMID": 1852601,
"ISBN": null,
"volume": "19",
"issue": "13",
"year": 1991,
"title": "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"URL": null,
"raw_pages": "3489-98",
"medline_journal": "Nucleic Acids Res",
"ISO_journal": "Nucleic Acids Res.",
"authors": [
"Cusack S",
"Hartlein M",
"Leberman R."
],
"DOI_URL": "http://dx.doi.org/10.1093/nar/19.13.3489"
},
"PUB00000386": {
"PMID": 8364025,
"ISBN": null,
"volume": "32",
"issue": "34",
"year": 1993,
"title": "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"URL": null,
"raw_pages": "8758-71",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Perona JJ",
"Rould MA",
"Steitz TA."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi00085a006"
},
"PUB00079873": {
"PMID": 12458790,
"ISBN": null,
"volume": "8",
"issue": "11",
"year": 2002,
"title": "Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation.",
"URL": null,
"raw_pages": "1363-72",
"medline_journal": "RNA",
"ISO_journal": "RNA",
"authors": [
"Francklyn C",
"Perona JJ",
"Puetz J",
"Hou YM."
],
"DOI_URL": "http://dx.doi.org/10.1017/S1355838202021180"
},
"PUB00079872": {
"PMID": 10704480,
"ISBN": null,
"volume": "64",
"issue": "1",
"year": 2000,
"title": "Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process.",
"URL": null,
"raw_pages": "202-36",
"medline_journal": "Microbiol Mol Biol Rev",
"ISO_journal": "Microbiol. Mol. Biol. Rev.",
"authors": [
"Woese CR",
"Olsen GJ",
"Ibba M",
"Soll D."
],
"DOI_URL": "http://dx.doi.org/10.1128/MMBR.64.1.202-236.2000"
},
"PUB00006576": {
"PMID": 10739930,
"ISBN": null,
"volume": "56",
"issue": "Pt 4",
"year": 2000,
"title": "Crystallization and preliminary X-ray crystallographic analysis of yeast arginyl-tRNA synthetase-yeast tRNAArg complexes.",
"URL": null,
"raw_pages": "492-4",
"medline_journal": "Acta Crystallogr D Biol Crystallogr",
"ISO_journal": "Acta Crystallogr. D Biol. Crystallogr.",
"authors": [
"Delagoutte B",
"Keith G",
"Moras D",
"Cavarelli J."
],
"DOI_URL": "http://dx.doi.org/10.1107/S0907444900001700"
},
"PUB00007363": {
"PMID": 10447505,
"ISBN": null,
"volume": "9",
"issue": "8",
"year": 1999,
"title": "Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events.",
"URL": null,
"raw_pages": "689-710",
"medline_journal": "Genome Res",
"ISO_journal": "Genome Res.",
"authors": [
"Wolf YI",
"Aravind L",
"Grishin NV",
"Koonin EV."
],
"DOI_URL": "http://www.genome.org/cgi/content/abstract/9/8/689"
},
"PUB00006477": {
"PMID": 10673435,
"ISBN": null,
"volume": "8",
"issue": "2",
"year": 2000,
"title": "The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules.",
"URL": null,
"raw_pages": "197-208",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Sugiura I",
"Nureki O",
"Ugaji-Yoshikawa Y",
"Kuwabara S",
"Shimada A",
"Tateno M",
"Lorber B",
"Giege R",
"Moras D",
"Yokoyama S",
"Konno M."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(00)00095-2"
},
"PUB00007191": {
"PMID": 2203971,
"ISBN": null,
"volume": "347",
"issue": "6289",
"year": 1990,
"title": "Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs.",
"URL": null,
"raw_pages": "203-6",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Eriani G",
"Delarue M",
"Poch O",
"Gangloff J",
"Moras D."
],
"DOI_URL": "http://dx.doi.org/10.1038/347203a0"
},
"PUB00005365": {
"PMID": 2053131,
"ISBN": null,
"volume": "16",
"issue": "1",
"year": 1991,
"title": "Classes of aminoacyl-tRNA synthetases and the establishment of the genetic code.",
"URL": null,
"raw_pages": "1-3",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Schimmel P."
],
"DOI_URL": "http://dx.doi.org/10.1016/0968-0004(91)90002-D"
},
"PUB00000723": {
"PMID": 8274143,
"ISBN": null,
"volume": "15",
"issue": "10",
"year": 1993,
"title": "The aminoacyl-tRNA synthetase family: modules at work.",
"URL": null,
"raw_pages": "675-87",
"medline_journal": "Bioessays",
"ISO_journal": "Bioessays",
"authors": [
"Delarue M",
"Moras D."
],
"DOI_URL": "http://dx.doi.org/10.1002/bies.950151007"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR014729",
"name": "Rossmann-like alpha/beta/alpha sandwich fold",
"type": "homologous_superfamily"
},
{
"accession": "IPR036695",
"name": "Arginyl tRNA synthetase N-terminal domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 41669,
"pathways": 8,
"proteins": 41187,
"proteomes": 21236,
"sets": 0,
"structural_models": {
"alphafold": 33082,
"bfvd": 5
},
"structures": 19,
"taxa": 40087
},
"entry_annotations": {},
"cross_references": {
"gp": {
"displayName": "Genome Properties",
"description": "Genome properties is an annotation system whereby functional attributes can be assigned to a genome, based on the presence of a defined set of protein signatures within that genome.",
"rank": 45,
"accessions": [
{
"accession": "GenProp0258",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0258"
}
]
},
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "6.1.1.19",
"url": "https://enzyme.expasy.org/EC/6.1.1.19"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "2zue",
"name": "Crystal structure of Pyrococcus horikoshii arginyl-tRNA synthetase complexed with tRNA(Arg) and an ATP analog (ANP)"
}
}
}
