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http://purl.uniprot.org/citations/24901469http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24901469http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24901469http://www.w3.org/2000/01/rdf-schema#comment"Zinc fingers are a ubiquitous class of protein domain with considerable variation in structure and function. Zf-FCS is a highly diverged group of C2-C2 zinc finger which is present in animals, prokaryotes and viruses, but not in plants. In this study we identified that a plant specific domain of unknown function, DUF581 is a zf-FCS type zinc finger. Based on HMM-HMM comparison and signature motif similarity we named this domain as FCS-Like Zinc finger (FLZ) domain. A genome wide survey identified that FLZ domain containing genes are bryophytic in origin and this gene family is expanded in spermatophytes. Expression analysis of selected FLZ gene family members of A. thaliana identified an overlapping expression pattern suggesting a possible redundancy in their function. Unlike the zf-FCS domain, the FLZ domain found to be highly conserved in sequence and structure. Using a combination of bioinformatic and protein-protein interaction tools, we identified that FLZ domain is involved in protein-protein interaction."xsd:string
http://purl.uniprot.org/citations/24901469http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0099074"xsd:string
http://purl.uniprot.org/citations/24901469http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0099074"xsd:string
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/author"Jamsheer K M."xsd:string
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/author"Jamsheer K M."xsd:string
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/author"Laxmi A."xsd:string
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/author"Laxmi A."xsd:string
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/name"PLoS ONE"xsd:string
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/name"PLoS ONE"xsd:string
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/pages"E99074"xsd:string
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/pages"E99074"xsd:string
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/title"DUF581 is plant specific FCS-like zinc finger involved in protein-protein interaction."xsd:string
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/title"DUF581 is plant specific FCS-like zinc finger involved in protein-protein interaction."xsd:string
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/24901469http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/24901469http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24901469
http://purl.uniprot.org/citations/24901469http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24901469
http://purl.uniprot.org/citations/24901469http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24901469
http://purl.uniprot.org/citations/24901469http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24901469
http://purl.uniprot.org/uniprot/Q8L471http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/24901469
http://purl.uniprot.org/uniprot/Q8VY80http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/24901469