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{
    "metadata": {
        "accession": "PS51295",
        "entry_id": null,
        "type": "domain",
        "go_terms": null,
        "source_database": "profile",
        "member_databases": null,
        "integrated": "IPR001890",
        "hierarchy": null,
        "name": {
            "name": "CRM domain profile",
            "short": "CRM"
        },
        "description": [
            {
                "text": "<p>The CRM domain is an ~100-amino acid RNA-binding domain. The name chloroplast\nRNA splicing and ribosome maturation (CRM) has been suggested to reflect the\nfunctions established for the four characterized members of the family (CRS1,\nCAF1, CAF2 and YhbY). The CRM domain is found in eubacteria, archaea, and\nplants. The CRM domain is represented as a stand-alone protein in archaea and\nbacteria, and in single- and multidomain proteins in plants. It has been\nsuggested that prokaryotic CRM proteins existed as ribosome-associated\nproteins prior to the divergence of archaea and bacteria, and that they were\nco-opted in the plant lineage as RNA binding modules by incorporation into\ndiverse protein contexts. Plant CRM domains are predicted to reside not only\nin the chloroplast, but also in the mitochondrion and the nucleo/cytoplasmic\ncompartment. The diversity of the CRM domain family in plants suggests a\ndiverse set of RNA targets [[cite:PUB00043746]][[cite:PUB00043747]].\n\nThe CRM domain is a compact alpha/beta domain consisting of a four-stranded\nbeta sheet and three alpha helices with an alpha-beta-alpha-beta-alpha-beta-\nbeta topology. The beta sheet face is basic, consistent with\na role in RNA binding. Proximal to the basic beta sheet face is another moiety\nthat could contribute to nucleic acid recognition. Connecting strand beta1 and\nhelix alpha2 is a loop with a six amino acid motif, GxxG flanked by large\naliphatic residues, within which one 'x' is typically a basic residue [[cite:PUB00019352]].\n\nSome proteins known to contain a CRM domain are listed below:\n\n - Maize  CRS1,  CAF1  and  CAF2 proteins. They contain multiple copies of the\n   domain and   are   required  for  the  splicing  of  group  II  introns  in\n   chloroplasts.\n - Escherichia coli protein yhbY. It is bound tightly and specifically to pre-\n   50S ribosomal subunits, suggesting that it facilitates ribosome maturation.\n\nThe profile we developed covers the entire CRM domain.</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00019352": {
                "PMID": 12429100,
                "ISBN": null,
                "volume": "10",
                "issue": "11",
                "year": 2002,
                "title": "Crystal structure of E. coli YhbY: a representative of a novel class of RNA binding proteins.",
                "URL": null,
                "raw_pages": "1593-601",
                "medline_journal": "Structure",
                "ISO_journal": "Structure",
                "authors": [
                    "Ostheimer GJ",
                    "Barkan A",
                    "Matthews BW."
                ],
                "DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(02)00886-9"
            },
            "PUB00043746": {
                "PMID": 12881426,
                "ISBN": null,
                "volume": "22",
                "issue": "15",
                "year": 2003,
                "title": "Group II intron splicing factors derived by diversification of an ancient RNA-binding domain.",
                "URL": null,
                "raw_pages": "3919-29",
                "medline_journal": "EMBO J",
                "ISO_journal": "EMBO J.",
                "authors": [
                    "Ostheimer GJ",
                    "Williams-Carrier R",
                    "Belcher S",
                    "Osborne E",
                    "Gierke J",
                    "Barkan A."
                ],
                "DOI_URL": "http://dx.doi.org/10.1093/emboj/cdg372"
            },
            "PUB00043747": {
                "PMID": 17105995,
                "ISBN": null,
                "volume": "13",
                "issue": "1",
                "year": 2007,
                "title": "The CRM domain: an RNA binding module derived from an ancient ribosome-associated protein.",
                "URL": null,
                "raw_pages": "55-64",
                "medline_journal": "RNA",
                "ISO_journal": "RNA",
                "authors": [
                    "Barkan A",
                    "Klipcan L",
                    "Ostersetzer O",
                    "Kawamura T",
                    "Asakura Y",
                    "Watkins KP."
                ],
                "DOI_URL": "http://dx.doi.org/10.1261/rna.139607"
            }
        },
        "set_info": null,
        "overlaps_with": null,
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 0,
            "interactions": 0,
            "matches": 28153,
            "pathways": 0,
            "proteins": 19931,
            "proteomes": 8215,
            "sets": 0,
            "structural_models": {
                "alphafold": 16313,
                "bfvd": 0
            },
            "structures": 6,
            "taxa": 14551
        },
        "entry_annotations": {},
        "cross_references": {},
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": {
            "accession": "1jo0",
            "name": "Structure of HI1333, a Hypothetical Protein from Haemophilus influenzae with Structural Similarity to RNA-binding Proteins"
        }
    }
}