| pubmed-article:17878204 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17878204 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:17878204 | lifeskim:mentions | umls-concept:C0242209 | lld:lifeskim |
| pubmed-article:17878204 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:17878204 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:17878204 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
| pubmed-article:17878204 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:17878204 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:17878204 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:17878204 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:17878204 | pubmed:dateCreated | 2007-10-31 | lld:pubmed |
| pubmed-article:17878204 | pubmed:abstractText | We expand the functionally uncharacterized DOMON domain superfamily to identify several novel families, including the first prokaryotic representatives. Using several computational tools we show that it is involved in ligand binding--either as heme- or sugar-binding domains. We present evidence that the DOMON domain along with the DM13 domain comprises a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. Other novel versions might function as sugar sensors of histidine kinases of bacterial two component systems. Supplementary information: Supplementary data are available at Bioinformatics online and also at ftp://ftp.ncbi.nih.gov/pub/aravind/domon/. | lld:pubmed |
| pubmed-article:17878204 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17878204 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17878204 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17878204 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17878204 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17878204 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17878204 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17878204 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17878204 | pubmed:issn | 1367-4811 | lld:pubmed |
| pubmed-article:17878204 | pubmed:author | pubmed-author:AravindLL | lld:pubmed |
| pubmed-article:17878204 | pubmed:author | pubmed-author:AnantharamanV... | lld:pubmed |
| pubmed-article:17878204 | pubmed:author | pubmed-author:IyerLakshmina... | lld:pubmed |
| pubmed-article:17878204 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17878204 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:17878204 | pubmed:volume | 23 | lld:pubmed |
| pubmed-article:17878204 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17878204 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17878204 | pubmed:pagination | 2660-4 | lld:pubmed |
| pubmed-article:17878204 | pubmed:dateRevised | 2009-11-4 | lld:pubmed |
| pubmed-article:17878204 | pubmed:meshHeading | pubmed-meshheading:17878204... | lld:pubmed |
| pubmed-article:17878204 | pubmed:meshHeading | pubmed-meshheading:17878204... | lld:pubmed |
| pubmed-article:17878204 | pubmed:meshHeading | pubmed-meshheading:17878204... | lld:pubmed |
| pubmed-article:17878204 | pubmed:meshHeading | pubmed-meshheading:17878204... | lld:pubmed |
| pubmed-article:17878204 | pubmed:meshHeading | pubmed-meshheading:17878204... | lld:pubmed |
| pubmed-article:17878204 | pubmed:meshHeading | pubmed-meshheading:17878204... | lld:pubmed |
| pubmed-article:17878204 | pubmed:meshHeading | pubmed-meshheading:17878204... | lld:pubmed |
| pubmed-article:17878204 | pubmed:meshHeading | pubmed-meshheading:17878204... | lld:pubmed |
| pubmed-article:17878204 | pubmed:meshHeading | pubmed-meshheading:17878204... | lld:pubmed |
| pubmed-article:17878204 | pubmed:meshHeading | pubmed-meshheading:17878204... | lld:pubmed |
| pubmed-article:17878204 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17878204 | pubmed:articleTitle | The DOMON domains are involved in heme and sugar recognition. | lld:pubmed |
| pubmed-article:17878204 | pubmed:affiliation | National Center for Biotechnology Information, National Library of Medicine and National Institute of Health, Bethesda, MD 20894, USA. | lld:pubmed |
| pubmed-article:17878204 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17878204 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
| family:PF10517.4 | family:pubmed | pubmed-article:17878204 | lld:pfam |
| family:PF03351.12 | family:pubmed | pubmed-article:17878204 | lld:pfam |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17878204 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17878204 | lld:pubmed |
