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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0014665,
umls-concept:C0017968,
umls-concept:C0024779,
umls-concept:C0033640,
umls-concept:C0033840,
umls-concept:C0079941,
umls-concept:C0205314,
umls-concept:C0441635,
umls-concept:C0679058,
umls-concept:C0679622,
umls-concept:C1334043,
umls-concept:C1547699,
umls-concept:C1710548,
umls-concept:C2700640
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pubmed:issue |
2
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pubmed:dateCreated |
1992-6-17
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pubmed:abstractText |
DNA sequence analysis of the unique short (Us) segment of the genome of equine herpesvirus type 1 Kentucky A strain (EHV-1) by our laboratory and strains Kentucky D and AB1 by other workers identifies a total of nine open reading frames (ORF). In this report, we present the DNA sequence of three of these newly identified ORFs, designated EUS 2, EUS 3, and EUS 4. The EUS 2 ORF is 1146 nucleotides (nt) in length and encodes a potential protein of 382 amino acids. Cis-regulatory sequences upstream of the putative ATG start codon include a G/C box 112 nt upstream and two potential TATA-like elements located between 15 and 90 nt before the ATG. The EUS 2 translation product exhibits significant homology to Ser/Thr protein kinases encoded within the Us segments of other herpesviruses, such as herpes simplex virus (26% homology) and pseudorabies virus (PRV), (45% homology), and possesses sequence domains conserved in protein kinases of cellular and viral origin. The EUS 3 ORF begins 127 nt downstream from the EUS 2 stop codon and ends at a stop codon 1119 nt further downstream. A single TATA-like element maps 61 nt upstream of the ORF. This ORF encodes a potential protein of 373 amino acids and is a homolog of glycoprotein gX of PRV, as judged by overall homology of amino acid residues, cysteine displacement, and presence of potential glycosylation sites and signal sequence. Interestingly, the EUS 4 ORF encodes a potential membrane glycoprotein that does not exhibit homology to any reported protein sequence. The EUS 4 ORF encodes a 383 amino acid polypeptide with a sequence indicative of a signal sequence at its amino terminal end, glycosylation sites for N-linked oligosaccharides, and a transmembrane domain near its carboxyl terminus. Several cis-acting regulatory sequences lie upstream of this ORF. These findings support the observation that the short region of alphaherpesviruses show considerable variation in their genetic content and gene organization.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
188
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
545-57
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1316673-Amino Acid Sequence,
pubmed-meshheading:1316673-Base Sequence,
pubmed-meshheading:1316673-Genes, Viral,
pubmed-meshheading:1316673-Glycoproteins,
pubmed-meshheading:1316673-Herpesviridae,
pubmed-meshheading:1316673-Herpesvirus 1, Equid,
pubmed-meshheading:1316673-Molecular Sequence Data,
pubmed-meshheading:1316673-Open Reading Frames,
pubmed-meshheading:1316673-Protein Kinases,
pubmed-meshheading:1316673-Sequence Alignment,
pubmed-meshheading:1316673-Solubility,
pubmed-meshheading:1316673-Viral Proteins,
pubmed-meshheading:1316673-Viral Structural Proteins
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pubmed:year |
1992
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pubmed:articleTitle |
Open reading frames encoding a protein kinase, homolog of glycoprotein gX of pseudorabies virus, and a novel glycoprotein map within the unique short segment of equine herpesvirus type 1.
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pubmed:affiliation |
Department of Microbiology and Immunology, Louisiana State University Medical Center, Shreveport 71130-3932.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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