Search results for "Peptide sequence"

showing 10 items of 330 documents

Genetic heterogeneity in the VP7 of group C rotaviruses.

2007

AbstractEvidence for a possible zoonotic role of group C rotaviruses (GCRVs) has been recently provided. To gain information on the genetic relationships between human and animal GCRVs, we sequenced the VP7 gene of 10 porcine strains detected during a large surveillance study from different outbreaks of gastroenteritis in piglets. Four GCRV strains were genetically related to the prototype GCRV porcine Cowden strain. A completely new VP7 genotype included 4 strains (344/04-7-like) that shared 92.5% to 97.0% aa identity to each other, but <83% to human GCRVs and <79% to other porcine and bovine GCRVs. A unique 4-aa insertion (SSSV or SSTI), within a variable region at the carboxy-terminus of…

RotavirusGenotypeSequence analysisSwinevirusesMolecular Sequence DataBiologymedicine.disease_causeEvolution MolecularZoonosisGenetic HeterogeneityPhylogeneticsRotavirusVirologyGenotypemedicineAnimalsHumansAmino Acid SequencePeptide sequenceAntigens ViralPhylogenyGeneticsSequence Homology Amino AcidGenetic heterogeneityStrain (biology)Zoonosisvirus diseasesmedicine.diseaseVirologyEnteritisPigsCapsid ProteinsGroup C rotavirusSequence AnalysisVirology
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Sequence analysis of the VP7 and VP4 genes identifies a novel VP7 gene allele of porcine rotaviruses, sharing a common evolutionary origin with human…

2005

AbstractDuring an epidemiological survey encompassing several porcine herds in Saragoza, Spain, the VP7 and VP4 of a rotavirus-positive sample, 34461-4, could not be predicted by using multiple sets of G- and P-type-specific primers. Sequence analysis of the VP7 gene revealed a low amino acid (aa) identity with those of well-established G serotypes, ranging between 58.33% and 88.88%, with the highest identity being to human G2 rotaviruses. Analysis of the VP4 gene revealed a P[23] VP4 specificity, as its VP8* aa sequence was 95.9% identical to that of the P14[23],G5 porcine strain A34, while analysis of the VP6 indicated a genogroup I, that is predictive of subgroup I specificity. Analysis …

RotavirusSerotypeSwineSequence analysisvirusesMolecular Sequence DataBiologyEvolution MolecularAntigenic Diversityfluids and secretionsPhylogeneticsVirologyAnimalsHumansAmino Acid SequenceAlleleAntigens ViralPeptide sequenceGeneAllelesPhylogenyGeneticsvirus diseasesP-typeVirologyHypervariable regionVP7VP4Capsid ProteinsG-typeSequence AnalysisVirology
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Evolution of DS-1-like human G2P[4] rotaviruses assessed by complete genome analyses

2013

Group A rotaviruses (RVAs) are a leading cause of viral gastroenteritis in children, with G2P[4] RVA being one of the most common human strain worldwide. The complete genome sequences of nine G2P[4] RVA strains, selected from a 26-year archival collection (1985-2011) established in Palermo/Italy, were determined. A strain associated with a peak of G2P[4] RVA activity in 1996 resembled a reassortant strain identified in Kenya in 1982 and completely differed in the genomic make up from more recent strains that circulated during 2004-2011. Conversely, the 2004-2011 G2P[4] RVAs were genetically more similar to contemporary RVA strains circulating globally. Recent G2P[4] strains possessed either…

RotavirusSettore MED/07 - Microbiologia E Microbiologia ClinicaMolecular Sequence DataReassortmentSequence alignmentGenome ViralBiologymedicine.disease_causeGenomeRotavirus InfectionsEvolution MolecularViral ProteinsPhylogeneticsVirologyRotavirusGenotypemedicineHumansAmino Acid SequencePeptide sequencePhylogenyGeneticsRotavirus G2P[4] evolution ItalyStrain (biology)VirologyItalySequence AlignmentJournal of General Virology
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Role of glycine-82 as a pivot point during the transition from the inactive to the active form of the yeast Ras2 protein

1991

AbstractRas proteins bind either GDP or GTP with high affinity. However, only the GTP-bound form of the yeast Ras2 protein is able to stimulate adenylyl cyclase. To identify amino acid residues that play a role in the conversion from the GDP-bound to the GTP-bound state of Ras proteins, we have searched for single amino acid substitutions that selectively affected the binding of one of the two nucleotides. We have found that the replacement of glycine-82 of the Ras2 protein by serine resulted in an increased rate of dissociation of Gpp(NH)p, a nonhydrolysable analog of GTP, while the GDP dissociation rate was not significantly modified. Glycine-82 resides in a region that is highly conserve…

Saccharomyces cerevisiae ProteinsGTP'Guanosine diphosphateProtein ConformationRestriction MappingGlycineBiophysicsSaccharomyces cerevisiaeBiochemistryFungal ProteinsGTP-binding protein regulatorsProtein structureGTP-Binding ProteinsStructural BiologyEscherichia coliGeneticsRHO protein GDP dissociation inhibitorAmino Acid SequenceRas2Binding siteMolecular BiologyPeptide sequencechemistry.chemical_classificationGuanylyl ImidodiphosphateBinding SitesPoint mutationChemistryCell BiologyGuanosine triphosphateRecombinant ProteinsAmino acidModels StructuralBiochemistryMutagenesis Site-Directedras ProteinsS. cerevisaePlasmidsRasFEBS Letters
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The ATC1 gene encodes a cell wall-linked acid trehalase required for growth on trehalose in Candida albicans.

2004

After screening a Candida albicans genome data base, the product of an open reading frame (IPF 19760/CA2574) with 41% identity to Saccharomyces cerevisiae vacuolar acid trehalase (Ath1p) was identified and named Atc1p. The deduced amino acid sequence shows that Atc1p contains an N-terminal hydrophobic signal peptide and 20 potential sites for N-glycosylation. C. albicans homozygous mutants that lack acid trehalase activity were constructed by gene disruption at the two ATC chromosomal alleles. Analysis of these null mutants shows that Atc1p is localized in the cell wall and is required for growth on trehalose as a carbon source. An Atc1p endowed with acid trehalase activity was obtained by …

Saccharomyces cerevisiae ProteinsTime FactorsTranscription GeneticMutantBlotting WesternMolecular Sequence DataTrehalase activityBiologyBiochemistrychemistry.chemical_compoundOpen Reading FramesCell WallCandida albicansAmino Acid SequenceRNA MessengerTrehalaseTrehalaseCandida albicansMolecular BiologyPeptide sequenceAlleleschemistry.chemical_classificationCell-Free SystemModels GeneticSequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionStructural geneHomozygoteNuclear ProteinsTrehaloseCell BiologyDNAbiology.organism_classificationPhosphoproteinsTrehaloseCarbonAmino acidProtein Structure TertiaryGlucosechemistryBiochemistryProtein BiosynthesisMutationElectrophoresis Polyacrylamide GelCell DivisionPlasmidsThe Journal of biological chemistry
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Role of Pir1 in the construction of the Candida albicans cell wall

2004

Searches in a Candida albicans database (http://genolist.pasteur.fr/CandidaDB/) identified two Individual Protein Files (IPF 15363 and 19968) whose deduced amino acid sequences showed 42 % and 45 % homology with Saccharomyces cerevisiae Pir4. The two DNA sequences are alleles of the same gene (CaPIR1) but IPF 19968 has a deletion of 117 bases. IPF 19968 encodes a putative polypeptide of 364 aa, which is highly O-glycosylated and has an N-mannosylated chain, four cysteine residues and seven repeats. Both alleles are expressed under different growth conditions and during wall construction by regenerating protoplasts. The heterozygous mutant cells are elongated, form clumps of several cells an…

Saccharomyces cerevisiae Proteinsbeta-GlucansSequence Homology Amino AcidSaccharomyces cerevisiaeNucleic acid sequenceSaccharomyces cerevisiaeBiologybiology.organism_classificationMicrobiologyHomology (biology)EpitopeCorpus albicansFungal ProteinsBiochemistryCell WallCandida albicansAmino Acid SequenceCandida albicansGenePeptide sequenceGlycoproteins
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Cystic Fibrosis Transmembrane Conductance Regulator Interacts with Multiple Immunoglobulin Domains of Filamin A

2010

Mutations of the chloride channel cystic fibrosis transmembrane conductance regulator (CFTR) that impair its apical localization and function cause cystic fibrosis. A previous report has shown that filamin A (FLNa), an actin-cross-linking and -scaffolding protein, interacts directly with the cytoplasmic N terminus of CFTR and that this interaction is necessary for stability and confinement of the channel to apical membranes. Here, we report that the CFTR N terminus has sequence similarity to known FLNa-binding partner-binding sites. FLNa has 24 Ig (IgFLNa) repeats, and a CFTR peptide pulled down repeats 9, 12, 17, 19, 21, and 23, which share sequence similarity yet differ from the other FLN…

Scaffold proteincongenital hereditary and neonatal diseases and abnormalitiesFilaminsMolecular Sequence DataCystic Fibrosis Transmembrane Conductance RegulatorImmunoglobulinsBiologymedicine.disease_causeFilaminBiochemistryContractile ProteinsProtein structureCricetinaemedicineAnimalsHumansFLNAAmino Acid SequenceMolecular BiologyPeptide sequenceMutationSequence Homology Amino AcidCell MembraneMicrofilament ProteinsCell Biologyrespiratory systemMolecular biologyActinsCystic fibrosis transmembrane conductance regulatorProtein Structure Tertiaryrespiratory tract diseasesCell biologySolubilityMutationProtein Structure and FoldingChloride channelbiology.proteinPeptidesDimerizationProtein BindingJournal of Biological Chemistry
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One precursor, three apolipoproteins: The relationship between two crustacean lipoproteins, the large discoidal lipoprotein and the high density lipo…

2014

The novel discoidal lipoprotein (dLp) recently detected in the crayfish, differs from other crustacean lipoproteins in its large size, apoprotein composition and high lipid binding capacity, We identified the dLp sequence by transcriptome analyses of the hepatopancreas and mass spectrometry. Further de novo assembly of the NGS data followed by BLAST searches using the sequence of the high density lipoprotein/1-glucan binding protein (HDL-BGBP) of Astacus leptodactylus as query revealed a putative precursor molecule with an open reading frame of 14.7 kb and a deduced primary structure of 4889 amino acids. The presence of an N-terminal lipid bind- ing domain and a DUF 1943 domain suggests the…

Sequence analysisLipoproteinsBlotting WesternMolecular Sequence DataHepatopancreasSequence alignmentBiologyMass SpectrometryProtein structureCrustaceaHemolymphLectinsAnimalsProtein IsoformsAmino Acid SequenceMolecular BiologyPeptide sequenceFurinBinding proteinProtein primary structureSequence Analysis DNACell BiologyImmunohistochemistryProtein Structure TertiaryApolipoproteinsBiochemistrybiology.proteinlipids (amino acids peptides and proteins)Carrier ProteinsLipoproteins HDLSequence AlignmentPlant lipid transfer proteinsBiochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
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Escherichia coli possesses two homologous anaerobic C4-dicarboxylate membrane transporters (DcuA and DcuB) distinct from the aerobic dicarboxylate tr…

1994

The nucleotide sequences of two Escherichia coli genes, dcuA and dcuB (formerly designated genA and genF), have been shown to encode highly homologous products, M(r) 45,751 and 47,935 (434 and 446 amino acid residues) with 36% sequence identity (63% similarity). These proteins have a high proportion (approximately 61%) of hydrophobic residues and are probably members of a new group of integral inner membrane proteins. The locations of the dcu genes, one upstream of the aspartase gene (dcuA-aspA) and the other downstream of the anaerobic fumarase gene (fumB-dcuB), suggested that they may function in the anaerobic transport of C4-dicarboxylic acids. Growth tests and transport studies with mut…

Sequence analysisMolecular Sequence DataMutantSuccinic AcidBiologymedicine.disease_causeMicrobiologyProtein Structure SecondarySubstrate SpecificityProtein structureBacterial ProteinsFumaratesEscherichia colimedicineAmino Acid SequenceAnaerobiosisMolecular BiologyGeneEscherichia coliPeptide sequenceDicarboxylic Acid Transporterschemistry.chemical_classificationAspartic AcidBase SequenceSequence Homology Amino AcidEscherichia coli ProteinsMembrane ProteinsBiological TransportSuccinatesSequence Analysis DNAAerobiosisAmino acidRepressor ProteinschemistryBiochemistryMembrane proteinGenes BacterialCarrier ProteinsResearch ArticleTranscription FactorsJournal of Bacteriology
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Purification and partial amino acid sequences of the enzyme vinorine synthase involved in a crucial step of ajmaline biosynthesis.

2004

The acetyl-CoA-dependent enzyme vinorine synthase was isolated from hybrid cell suspension cultures of Rauvolfia serpentina and Rhazya stricta. The sarpagan-type alkaloid gardneral was used as a substrate of the enzyme leading to the ajmalan-type 10-methoxyvinorine. An HPLC-based assay was developed to monitor vinorine synthase activity, which allowed establishing a five step purification procedure combining anion exchange, hydrophobic interaction, hydroxyapatite and gel filtration. Purification resulted in a yield of 0.2% and an approximately 991-fold enrichment of the acetyltransfer activity. SDS-PAGE analysis showed a Mr for the enzyme of approximately 50 kDa. The four peptide fragments …

Sequence analysisStereochemistryClinical BiochemistryMolecular Sequence DataPharmaceutical ScienceHybrid CellsBiochemistryRauwolfiaIndole Alkaloidschemistry.chemical_compoundVinorine synthase activityBiosynthesisRauvolfia serpentinaSequence Analysis ProteinDrug DiscoveryAmino Acid SequenceAcetyl-CoA C-AcetyltransferaseMolecular BiologyPeptide sequencechemistry.chemical_classificationAjmalinebiologyATP synthaseMolecular StructureOrganic ChemistrySubstrate (chemistry)biology.organism_classificationApocynaceaeEnzymeBiochemistrychemistrybiology.proteinMolecular MedicineBioorganicmedicinal chemistry
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