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
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...
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description | 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 Winked 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 aIphaherpesviruses show considerable variation in their genetic content and gene organization. |
doi_str_mv | 10.1016/0042-6822(92)90509-N |
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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 Winked oligosaccharides, and a transmembrane domain near its carboxyl terminus. Several
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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 Winked 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 aIphaherpesviruses show considerable variation in their genetic content and gene organization.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Genes, Viral</subject><subject>Genetics</subject><subject>Glycoproteins - genetics</subject><subject>Herpesviridae - genetics</subject><subject>herpesvirus 1 (equine)</subject><subject>Herpesvirus 1, Equid - genetics</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>nucleotide sequence</subject><subject>Open Reading Frames</subject><subject>predictions</subject><subject>protein kinase</subject><subject>Protein Kinases - genetics</subject><subject>Sequence Alignment</subject><subject>Solubility</subject><subject>Viral Proteins - chemistry</subject><subject>Viral Proteins - genetics</subject><subject>Viral Structural Proteins - genetics</subject><subject>Virology</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkduK1TAUhoso43b0DRRyIaIw1ZyaNDcDMniCYeZGwbuQpqvd0TbpJO2W_Wo-nens7Yg3CoEc1rd-FvmK4inBrwkm4g3GnJaipvSloq8UrrAqr-4VG4KVKDHj5H6xuUMeFo9S-obzXUp8UpwQRoSQbFP8vJ7Aowimdb5HXTQjJATehtu7QVMMMziPvjtvEpyhbRjDEHoUOtQPext-1_uv69OUYGlDNI3LKTsXl3SGjG9zjg87GP5uGc2Efrh5m4_zFtDi3c0CKG1DnFGCfgQ_r5lwszgPaAtxgnSbieb9BIg8Lh50Zkjw5LifFl_ev_t88bG8vP7w6eLtZWk5kXNJoQFoG8lkRxStBW5I1ZpaNaK1iknRVKCarsNCWsaYpdhyJQ2xleCZUTU7LV4ccvPgecI069ElC8NgPIQlaUkVr2uu_gsSQSmmvMogP4A2hpQidHqKbjRxrwnWq1u9itOrOK3yWt3qq9z27Ji_NCO0f5oOMnP9-bFukjVDlumtS3dYxbisFM7Y-QGD_Gk7B1En67JyaF0EO-s2uH_P8QsdY8P4</recordid><startdate>19920601</startdate><enddate>19920601</enddate><creator>Colle, Clarence F.</creator><creator>Clay Flowers, C.</creator><creator>O'Callaghan, Dennis J.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M81</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19920601</creationdate><title>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</title><author>Colle, Clarence F. ; Clay Flowers, C. ; O'Callaghan, Dennis J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-2ebeedb737f192860b15da89b6dc9376b5e9bff067c333c20c497a1c5649b6983</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Genes, Viral</topic><topic>Genetics</topic><topic>Glycoproteins - genetics</topic><topic>Herpesviridae - genetics</topic><topic>herpesvirus 1 (equine)</topic><topic>Herpesvirus 1, Equid - genetics</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>nucleotide sequence</topic><topic>Open Reading Frames</topic><topic>predictions</topic><topic>protein kinase</topic><topic>Protein Kinases - genetics</topic><topic>Sequence Alignment</topic><topic>Solubility</topic><topic>Viral Proteins - chemistry</topic><topic>Viral Proteins - genetics</topic><topic>Viral Structural Proteins - genetics</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Colle, Clarence F.</creatorcontrib><creatorcontrib>Clay Flowers, C.</creatorcontrib><creatorcontrib>O'Callaghan, Dennis J.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Colle, Clarence F.</au><au>Clay Flowers, C.</au><au>O'Callaghan, Dennis J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>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</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>1992-06-01</date><risdate>1992</risdate><volume>188</volume><issue>2</issue><spage>545</spage><epage>557</epage><pages>545-557</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><coden>VIRLAX</coden><abstract>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 Winked 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 aIphaherpesviruses show considerable variation in their genetic content and gene organization.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>1316673</pmid><doi>10.1016/0042-6822(92)90509-N</doi><tpages>13</tpages></addata></record> |
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subjects | Amino Acid Sequence Base Sequence Biological and medical sciences Fundamental and applied biological sciences. Psychology genes Genes, Viral Genetics Glycoproteins - genetics Herpesviridae - genetics herpesvirus 1 (equine) Herpesvirus 1, Equid - genetics Microbiology Molecular Sequence Data nucleotide sequence Open Reading Frames predictions protein kinase Protein Kinases - genetics Sequence Alignment Solubility Viral Proteins - chemistry Viral Proteins - genetics Viral Structural Proteins - genetics Virology |
title | 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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