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DESCRIBE <http://purl.uniprot.org/SHA-384/E49E2A4DE3AA163311EC4F3A84DB7BB8CECD25A307A21508AE26CAFE60AF28551D699FE82DF50ED476041C6B011CD416>
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http://purl.uniprot.org/SHA-384/E49E2A4DE3AA163311EC4F3A84DB7BB8CECD25A307A21508AE26CAFE60AF28551D699FE82DF50ED476041C6B011CD416
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/E49E2A4DE3AA163311EC4F3A84DB7BB8CECD25A307A21508AE26CAFE60AF28551D699FE82DF50ED476041C6B011CD416
http://www.w3.org/2000/01/rdf-schema#comment
"Type I protein arginine methyltransferase (PRMT) activity produces asymmetric dimethylation of the terminal guanidinonitrogen of arginines in substrate proteins particularly glycine and arginine-rich (GAR) segments of proteins"
xsd:string
http://purl.uniprot.org/uniprot/#_FBCD859225426BA873AECF29E390322026780D62A8F855CF835C8D48183D6C78AF359E48D50790DAF3807BE90FBB781A
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/E49E2A4DE3AA163311EC4F3A84DB7BB8CECD25A307A21508AE26CAFE60AF28551D699FE82DF50ED476041C6B011CD416
http://purl.uniprot.org/uniprot/Q9JIF0
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/E49E2A4DE3AA163311EC4F3A84DB7BB8CECD25A307A21508AE26CAFE60AF28551D699FE82DF50ED476041C6B011CD416
http://purl.uniprot.org/uniprot/#_Q9JIF0-mappedCitation-11835310
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/E49E2A4DE3AA163311EC4F3A84DB7BB8CECD25A307A21508AE26CAFE60AF28551D699FE82DF50ED476041C6B011CD416