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{
    "metadata": {
        "accession": "PS51253",
        "entry_id": null,
        "type": "domain",
        "go_terms": null,
        "source_database": "profile",
        "member_databases": null,
        "integrated": "IPR006600",
        "hierarchy": null,
        "name": {
            "name": "CENPB-type HTH domain profile",
            "short": "HTH_CENPB"
        },
        "description": [
            {
                "text": "<p>The CENPB-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of\nabout 70-75 amino acids, present in eukaryotic centromere proteins and\ntransposases. The domain is named after the mammalian major centromere\nautoantigen B or centromere protein B (CENP-B), which is a fundamental\ncentromere component of chromosomes. The N-terminus of CENP-B contains two\nDNA-binding HTH domains, which bind to adjacent major grooves of DNA. The\nN-terminus of CENP-B is formed by a psq-type HTH domain and\nC-terminal to this domain lies the CENPB-type HTH domain. These two HTH\ndomains together bind specifically to a 17-base-pair sequence, the CENP-B box,\nwhich occurs in alpha-satellite DNA in human centromeres [[cite:PUB00035346]].\n\nThe structure of the CENPB-type HTH domain is composed of three alpha-helices. The second and third helices connected via a turn comprise\nthe helix-turn-helix motif. Helix 3 is termed the recognition helix as it\nbinds the DNA major groove, like in other HTHs. In CENP-B this domain\nrecognizes site 3 of the CENP-B box, while the preceding psq-type HTH binds site 1 of the CENP-B box, and a connecting linker loop\nbinds in the minor groove of DNA and recognizes site 2 [[cite:PUB00025705]].\n\nSome proteins known to contain a CENPB-type HTH domain:\n\n - Mammalian centromere protein B (CENP-B), associated with the centromere and\n   specifically binding DNA to the CENP-B box.\n - Mammalian jerky protein, involved in epileptic seizures in mice.\n - Mammalian Pogo transposases.\n - Fission  yeast  ARS-binding  protein  1  (abp1) and CENP-B homolog proteins\n   (CBHP-1 and 2), which are centromere proteins.\n - Candida albicans protein PDC2.\n - Fungal transposases.\n\nThe profile we developed covers the entire CENPB-type HTH domain, including\nthe N-terminal linker loop.</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00035346": {
                "PMID": 16183641,
                "ISBN": null,
                "volume": "280",
                "issue": "50",
                "year": 2005,
                "title": "Human centromere protein B induces translational positioning of nucleosomes on alpha-satellite sequences.",
                "URL": null,
                "raw_pages": "41609-18",
                "medline_journal": "J Biol Chem",
                "ISO_journal": "J. Biol. Chem.",
                "authors": [
                    "Tanaka Y",
                    "Tachiwana H",
                    "Yoda K",
                    "Masumoto H",
                    "Okazaki T",
                    "Kurumizaka H",
                    "Yokoyama S."
                ],
                "DOI_URL": "http://dx.doi.org/10.1074/jbc.M509666200"
            },
            "PUB00025705": {
                "PMID": 11726497,
                "ISBN": null,
                "volume": "20",
                "issue": "23",
                "year": 2001,
                "title": "Crystal structure of the CENP-B protein-DNA complex: the DNA-binding domains of CENP-B induce kinks in the CENP-B box DNA.",
                "URL": null,
                "raw_pages": "6612-8",
                "medline_journal": "EMBO J",
                "ISO_journal": "EMBO J.",
                "authors": [
                    "Tanaka Y",
                    "Nureki O",
                    "Kurumizaka H",
                    "Fukai S",
                    "Kawaguchi S",
                    "Ikuta M",
                    "Iwahara J",
                    "Okazaki T",
                    "Yokoyama S."
                ],
                "DOI_URL": "http://dx.doi.org/10.1093/emboj/20.23.6612"
            }
        },
        "set_info": null,
        "overlaps_with": null,
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 0,
            "interactions": 0,
            "matches": 30844,
            "pathways": 0,
            "proteins": 30463,
            "proteomes": 2562,
            "sets": 0,
            "structural_models": {
                "alphafold": 25959,
                "bfvd": 0
            },
            "structures": 2,
            "taxa": 7471
        },
        "entry_annotations": {},
        "cross_references": {},
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": null
    }
}