http://purl.uniprot.org/keywords/393 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Concept |
http://purl.uniprot.org/keywords/393 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Concept |
http://purl.uniprot.org/keywords/393 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/keywords/9994 |
http://purl.uniprot.org/keywords/393 | http://www.w3.org/2000/01/rdf-schema#comment | "A globular structural motif found in many proteins of the immune system, including immunoglobulins (Igs), T cell receptors (TCRs) and major histocompatibility complex (MHC) molecules. Ig domains are approximately 110 amino acid residues in length, include an internal disulfide bond, and contain two layers of beta-pleated sheets, each layer composed of three to five strands of antiparallel polypeptide chains. Ig domains are classified as V-like or C-like on the basis of closest homology to either Ig V or C domains."xsd:string |
http://purl.uniprot.org/keywords/393 | http://www.w3.org/2004/02/skos/core#prefLabel | "Immunoglobulin domain"xsd:string |
http://purl.uniprot.org/keywords/393 | http://www.w3.org/2004/02/skos/core#altLabel | "Immunoglobulin fold"xsd:string |
http://purl.uniprot.org/keywords/393 | http://purl.uniprot.org/core/category | http://purl.uniprot.org/keywords/9994 |
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http://purl.uniprot.org/uniprot/A0A2K5F3A6 | http://purl.uniprot.org/core/classifiedWith | http://purl.uniprot.org/keywords/393 |
http://purl.uniprot.org/uniprot/A0A0K8W3F0 | http://purl.uniprot.org/core/classifiedWith | http://purl.uniprot.org/keywords/393 |
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http://purl.uniprot.org/uniprot/A0AA35JMQ0 | http://purl.uniprot.org/core/classifiedWith | http://purl.uniprot.org/keywords/393 |
http://purl.uniprot.org/uniprot/A0AA35NSJ5 | http://purl.uniprot.org/core/classifiedWith | http://purl.uniprot.org/keywords/393 |
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