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http://purl.uniprot.org/citations/8274029http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8274029http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8274029http://www.w3.org/2000/01/rdf-schema#comment"An adenylate kinase gene from a member of the archaebacterial kingdom, the thermoacidophilic archaebacterium (archaeon) Sulfolobus acidocaldarius, has been cloned and sequenced for the first time. Two degenerate oligonucleotide probes, based on the N-terminal amino acid sequence information, led to the amplification of a gene-specific DNA fragment, used to screen subgenomic libraries. Comparing the DNA-derived amino acid sequence of total 194 residues with those of known procaryotic and eucaryotic adenylate kinases revealed only a low degree of similarity, except for a glycine-rich region close to the N-terminus, the so-called P-loop. Using inducible expression systems catalytically active S. acidocaldarius adenylate kinase was produced in large amounts. Although the total length of the protein and the results of alignment procedures suggest a closer relation to eucaryotic than to procaryotic sequences, the archaebacterial enzyme may represent a novel class of adenylate kinases. This is corroborated by the finding that an antiserum against this protein does not cross-react with Escherichia coli nor yeast or rabbit adenylate kinases for example."xsd:string
http://purl.uniprot.org/citations/8274029http://purl.org/dc/terms/identifier"doi:10.1006/abbi.1993.1607"xsd:string
http://purl.uniprot.org/citations/8274029http://purl.org/dc/terms/identifier"doi:10.1006/abbi.1993.1607"xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/author"Schaefer G."xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/author"Schaefer G."xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/author"Schmid R."xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/author"Schmid R."xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/author"Kath T."xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/author"Kath T."xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/pages"405-410"xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/pages"405-410"xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/title"Identification, cloning, and expression of the gene for adenylate kinase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius."xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/title"Identification, cloning, and expression of the gene for adenylate kinase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius."xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/volume"307"xsd:string
http://purl.uniprot.org/citations/8274029http://purl.uniprot.org/core/volume"307"xsd:string
http://purl.uniprot.org/citations/8274029http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8274029
http://purl.uniprot.org/citations/8274029http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8274029
http://purl.uniprot.org/citations/8274029http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8274029
http://purl.uniprot.org/citations/8274029http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8274029