| pubmed-article:1962437 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:1962437 | lifeskim:mentions | umls-concept:C0206266 | lld:lifeskim |
| pubmed-article:1962437 | lifeskim:mentions | umls-concept:C0598035 | lld:lifeskim |
| pubmed-article:1962437 | lifeskim:mentions | umls-concept:C0029246 | lld:lifeskim |
| pubmed-article:1962437 | lifeskim:mentions | umls-concept:C0441635 | lld:lifeskim |
| pubmed-article:1962437 | lifeskim:mentions | umls-concept:C0004793 | lld:lifeskim |
| pubmed-article:1962437 | lifeskim:mentions | umls-concept:C0017428 | lld:lifeskim |
| pubmed-article:1962437 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1962437 | pubmed:dateCreated | 1992-1-7 | lld:pubmed |
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| pubmed-article:1962437 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1962437 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1962437 | pubmed:abstractText | The complete nucleotide sequences of the RNA-1 segments in broad bean mottle virus (BBMV) and cowpea chlorotic mottle virus (CCMV) were determined. BBMV RNA-1 consists of 3158 nucleotides and CCMV RNA-1 has 3171 nucleotides. Both BBMV and CCMV RNA-1 are capped at the 5' end but, unlike in other tricornaviruses, BBMV RNA-1 initiates with an A residue. Both BBMV and CCMV RNA-1 are monocistronic encoding for highly homologous 1a proteins of 966 and 958 amino acids, respectively. The highest homologies are clustered within two domains: the N-domain that aligns with the nsP1 Sindbis virus protein, a putative methyl transferase, and the C-domain which has a conserved nucleotide binding motif. Previous sequence comparisons suggest that the C-terminal domain may function as an NTP-dependent RNA helicase. In addition, we find that the C-domain has patterns similar to those of the reovirus and vaccinia virus guanylyl transferases. All this implies that 1a protein is a multifunctional polypeptide involved in both RNA capping and RNA polymerization processes. | lld:pubmed |
| pubmed-article:1962437 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1962437 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1962437 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1962437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1962437 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1962437 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:1962437 | pubmed:issn | 0042-6822 | lld:pubmed |
| pubmed-article:1962437 | pubmed:author | pubmed-author:BujarskiJ JJJ | lld:pubmed |
| pubmed-article:1962437 | pubmed:author | pubmed-author:DzianottA MAM | lld:pubmed |
| pubmed-article:1962437 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1962437 | pubmed:volume | 185 | lld:pubmed |
| pubmed-article:1962437 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1962437 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1962437 | pubmed:pagination | 553-62 | lld:pubmed |
| pubmed-article:1962437 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1962437 | pubmed:meshHeading | pubmed-meshheading:1962437-... | lld:pubmed |
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| pubmed-article:1962437 | pubmed:meshHeading | pubmed-meshheading:1962437-... | lld:pubmed |
| pubmed-article:1962437 | pubmed:meshHeading | pubmed-meshheading:1962437-... | lld:pubmed |
| pubmed-article:1962437 | pubmed:meshHeading | pubmed-meshheading:1962437-... | lld:pubmed |
| pubmed-article:1962437 | pubmed:meshHeading | pubmed-meshheading:1962437-... | lld:pubmed |
| pubmed-article:1962437 | pubmed:meshHeading | pubmed-meshheading:1962437-... | lld:pubmed |
| pubmed-article:1962437 | pubmed:meshHeading | pubmed-meshheading:1962437-... | lld:pubmed |
| pubmed-article:1962437 | pubmed:meshHeading | pubmed-meshheading:1962437-... | lld:pubmed |
| pubmed-article:1962437 | pubmed:meshHeading | pubmed-meshheading:1962437-... | lld:pubmed |
| pubmed-article:1962437 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1962437 | pubmed:articleTitle | The nucleotide sequence and genome organization of the RNA-1 segment in two bromoviruses: broad bean mottle virus and cowpea chlorotic mottle virus. | lld:pubmed |
| pubmed-article:1962437 | pubmed:affiliation | Northern Illinois University, Department of Biological Sciences, DeKalb 60115. | lld:pubmed |
| pubmed-article:1962437 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1962437 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:1962437 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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