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{
"metadata": {
"accession": "IPR005335",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0051276",
"name": "chromosome organization",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF03592": "Terminase small subunit"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR005335",
"name": "Terminase small subunit",
"type": "Family",
"children": []
},
"name": {
"name": "Terminase small subunit",
"short": "Terminase_ssu"
},
"description": [
{
"text": "<p>Packaging of double-stranded viral DNA concatemers requires interaction of the prohead with virus DNA. This process is mediated by a phage-encoded DNA recognition and terminase protein. The terminase enzymes described so far, which are hetero-oligomers composed of a small and a large subunit, do not have a significant level of sequence homology. The small terminase subunit is thought to form a nucleoprotein structure that helps to position the terminase large subunit at the packaging initiation site [[cite:PUB00008403]]. The small terminase protein is essential for the initial recognition of viral DNA and regulates the motor's ATPase and nuclease activities during DNA translocation [[cite:PUB00057578]] and for switching between viral DNA replication and packaging. DNA packaging in tailed bacteriophages and in evolutionarily related herpesviruses is controlled by a viral-encoded terminase. The terminase complex characterised in Bacillus subtilis bacteriophages SF6 and SPP1 consists of two proteins: G1P and G2P [[cite:PUB00062503], [cite:PUB00067159]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00008403": {
"PMID": 2679356,
"ISBN": null,
"volume": "43",
"issue": null,
"year": 1989,
"title": "DNA packaging in dsDNA bacteriophages.",
"URL": null,
"raw_pages": "267-92",
"medline_journal": "Annu Rev Microbiol",
"ISO_journal": "Annu. Rev. Microbiol.",
"authors": [
"Black LW."
],
"DOI_URL": "http://dx.doi.org/10.1146/annurev.mi.43.100189.001411"
},
"PUB00057578": {
"PMID": 22207627,
"ISBN": null,
"volume": "109",
"issue": "3",
"year": 2012,
"title": "Structural basis for DNA recognition and loading into a viral packaging motor.",
"URL": null,
"raw_pages": "811-6",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Buttner CR",
"Chechik M",
"Ortiz-Lombardia M",
"Smits C",
"Ebong IO",
"Chechik V",
"Jeschke G",
"Dykeman E",
"Benini S",
"Robinson CV",
"Alonso JC",
"Antson AA."
],
"DOI_URL": "http://dx.doi.org/10.1073/pnas.1110270109"
},
"PUB00067159": {
"PMID": 23545641,
"ISBN": null,
"volume": "69",
"issue": "Pt 4",
"year": 2013,
"title": "The 1.58 A resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding.",
"URL": null,
"raw_pages": "376-81",
"medline_journal": "Acta Crystallogr Sect F Struct Biol Cryst Commun",
"ISO_journal": "Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.",
"authors": [
"Benini S",
"Chechik M",
"Ortiz Lombardia M",
"Polier S",
"Leech A",
"Shevtsov MB",
"Alonso JC."
],
"DOI_URL": "http://dx.doi.org/10.1107/S1744309113004399"
},
"PUB00062503": {
"PMID": 22858866,
"ISBN": null,
"volume": "423",
"issue": "3",
"year": 2012,
"title": "Structural and Functional Studies of the Phage Sf6 Terminase Small Subunit Reveal a DNA-Spooling Device Facilitated by Structural Plasticity.",
"URL": null,
"raw_pages": "413-26",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Zhao H",
"Kamau YN",
"Christensen TE",
"Tang L."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.jmb.2012.07.016"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR038713",
"name": "Terminase small subunit, N-terminal DNA-binding domain, HTH motif superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 30,
"interactions": 0,
"matches": 5689,
"pathways": 0,
"proteins": 5685,
"proteomes": 2142,
"sets": 0,
"structural_models": {
"alphafold": 4196,
"bfvd": 26
},
"structures": 7,
"taxa": 5443
},
"entry_annotations": {
"alignment:seed": 27,
"alignment:full": 1476
},
"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": "GenProp0208",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0208"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3zqo",
"name": "Crystal structure of the small terminase oligomerization core domain from a SPP1-like bacteriophage (crystal form 3)"
}
}
}
