{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Natarajan P"],"funding":["Wellcome Trust","NIGMS NIH HHS"],"pagination":["7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4387736"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16"],"pubmed_abstract":["<h4>Background</h4>N-terminal domains of BVU_4064 and BF1687 proteins from Bacteroides vulgatus and Bacteroides fragilis respectively are members of the Pfam family PF12985 (DUF3869). Proteins containing a domain from this family can be found in most Bacteroides species and, in large numbers, in all human gut microbiome samples. Both BVU_4064 and BF1687 proteins have a consensus lipobox motif implying they are anchored to the membrane, but their functions are otherwise unknown. The C-terminal half of BVU_4064 is assigned to protein family PF12986 (DUF3870); the equivalent part of BF1687 was unclassified.<h4>Results</h4>Crystal structures of both BVU_4064 and BF1687 proteins, solved at the JCSG center, show strikingly similar three-dimensional structures. The main difference between the two"],"journal":["BMC bioinformatics"],"pubmed_title":["Structure and sequence analyses of Bacteroides proteins BVU_4064 and BF1687 reveal presence of two novel predominantly-beta domains, predicted to be involved in lipid and cell surface interactions."],"pmcid":["PMC4387736"],"funding_grant_id":["WT077044/Z/05/Z","P41 GM103393","P41GM103393","U54 GM094586"],"pubmed_authors":["Godzik A","Aravind L","Kumar A","Yeh AP","Natarajan P","Punta M"],"additional_accession":[]},"is_claimable":false,"name":"Structure and sequence analyses of Bacteroides proteins BVU_4064 and BF1687 reveal presence of two novel predominantly-beta domains, predicted to be involved in lipid and cell surface interactions.","description":"<h4>Background</h4>N-terminal domains of BVU_4064 and BF1687 proteins from Bacteroides vulgatus and Bacteroides fragilis respectively are members of the Pfam family PF12985 (DUF3869). Proteins containing a domain from this family can be found in most Bacteroides species and, in large numbers, in all human gut microbiome samples. Both BVU_4064 and BF1687 proteins have a consensus lipobox motif implying they are anchored to the membrane, but their functions are otherwise unknown. The C-terminal half of BVU_4064 is assigned to protein family PF12986 (DUF3870); the equivalent part of BF1687 was unclassified.<h4>Results</h4>Crystal structures of both BVU_4064 and BF1687 proteins, solved at the JCSG center, show strikingly similar three-dimensional structures. The main difference between the two","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Jan","modification":"2026-06-16T05:55:39.958Z","creation":"2019-03-27T01:49:31Z"},"accession":"S-EPMC4387736","cross_references":{"pubmed":["25592227"],"doi":["10.1186/s12859-014-0434-7"]}}