Search results for "Phylogenetics"

showing 10 items of 777 documents

Evolutionary relationships of Metazoa within the eukaryotes based on molecular data from Porifera

1999

Recent molecular data provide strong support for the view that all metazoan phyla, including Porifera, are of monophyletic origin. The relationship of Metazoa, including the Porifera, to Plantae, Fungi and unicellular eukaryotes has only rarely been studied by using cDNAs coding for proteins. Sequence data from rDNA suggested a relationship of Porifera to unicellular eukaryotes (choanoflagellates). However, ultrastructural studies of choanocytes did not support these findings. In the present study, we compared amino acid sequences that are found in a variety of metazoans (including sponges) with those of Plantae, Fungi and unicellular eukaryotes, to obtain an answer to this question. We use…

DNA ComplementaryMolecular Sequence DataProtein Serine-Threonine KinasesBiologyGeneral Biochemistry Genetics and Molecular BiologyEvolution MolecularMonophylyCalmodulinTubulinPhylogeneticsAnimalsHSP70 Heat-Shock ProteinsAmino Acid SequenceCloning MolecularPeptide sequencePhylogenyProtein Kinase CDNA PrimersGeneral Environmental ScienceBase SequenceGeneral Immunology and MicrobiologyPhylogenetic treePhylumChoanocytefungiGeneral Medicinebiology.organism_classificationMolecular biologyPoriferaSpongeEukaryotic CellsEvolutionary biologyMolecular phylogeneticsGeneral Agricultural and Biological SciencesResearch ArticleProceedings of the Royal Society of London. Series B: Biological Sciences
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A hemocyanin from the Onychophora and the emergence of respiratory proteins

2002

The velvet worms (Onychophora) are considered living fossils and are closely related to the Euarthropoda. Onychophora possess a tracheal system for respiratory function, but oxygen-transport proteins have been considered unnecessary. Here, we show that the hemolymph of the Epiperipatus sp. (Onychophora: Peripatidae) contains an arthropod-type hemocyanin, demonstrating that such protein exists outside the Euarthropoda. Thus, the evolution of oxygen carriers preceded the divergence of the Onychophora and Euarthropoda and was most likely linked to the evolution of an efficient circulatory system in a low-oxygen environment. The cDNA of the Epiperipatus hemocyanin subunit comprises 2,287 bp an…

DNA ComplementaryMultidisciplinaryBase Sequencebiologymedicine.medical_treatmentMolecular Sequence DataHemocyaninAnatomyBiological Sciencesbiology.organism_classificationEpiperipatusPhylogeneticsEvolutionary biologyHemocyaninsHemolymphmedicineAnimalsRespiratory functionOnychophoraAmino Acid SequenceArthropodPeripatidaeCloning MolecularArthropodsPhylogenyProceedings of the National Academy of Sciences
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Putative phenoloxidases in the tunicate Ciona intestinalis and the origin of the arthropod hemocyanin superfamily.

2003

In addition to the respiratory copper-containing proteins for which it is named, the arthropod hemocyanin superfamily also includes phenoloxidases and various copperless storage proteins (pseudo-hemocyanins, hexamerins and hexamerin receptors). It had long been assumed that these proteins are restricted to the arthropod phylum. However, in their analysis of the predicted genes in the Ciona intestinalis (Urochordata:Tunicata) genome, Dehal et al. (Science 298:2157–2167) proposed that the sea squirt lacks hemoglobin but uses hemocyanin for oxygen transport. While there are, nevertheless, four hemoglobin genes present in Ciona, we have identified and cloned two cDNA sequences from Ciona that i…

DNA ComplementaryPhysiologymedicine.medical_treatmentMolecular Sequence Datachemical and pharmacologic phenomenacomplex mixturesBiochemistryEvolution MolecularEndocrinologyPhylogeneticsmedicineAnimalsCiona intestinalisAmino Acid SequenceArthropodsEcology Evolution Behavior and SystematicsPhylogenybiologyBase SequenceSequence Homology Amino AcidMonophenol MonooxygenaseOxygen transportHemocyaninAnatomybiology.organism_classificationCiona intestinalisCionaEvolutionary biologyHemocyaninsAnimal Science and ZoologyArthropod ProteinsArthropodOxygen bindingJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology
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Identification, molecular cloning, and phylogenetic analysis of a non-respiratory pseudo-hemocyanin of Homarus americanus.

1999

Copper-containing hemocyanins serve to transport oxygen in many arthropod species. Here I describe the identification and cDNA cloning of a structurally closely related non-respiratory pseudo-hemocyanin (PHc) of the American lobster, Homarus americanus. This protein has lost the ability to bind copper and, therefore, oxygen because a histidine residue in copper-binding site A is replaced by tyrosine. Like many arthropod hemocyanins, PHc forms a hexamer. It consists of two different subunit types of 660 and 661 amino acids, respectively, that share a 94.4% sequence identity. Whereas Homarus hemocyanin is produced in the hepatopancreas, PHc is synthesized by the ovaries and the heart tissue. …

DNA ComplementaryProtein subunitmedicine.medical_treatmenteducationMolecular Sequence Datachemical and pharmacologic phenomenaMolecular cloningBiologybehavioral disciplines and activitiesBiochemistryPhylogeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequencePhylogenychemistry.chemical_classificationHomarusBase SequenceSequence Homology Amino AcidEcologyHemocyaninCell BiologyProtein superfamilybiology.organism_classificationAmino acidNephropidaeMicroscopy ElectronBiochemistrychemistryHemocyaninsThe Journal of biological chemistry
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Identification and Expression of the SOS Response, aidB-Like, Gene in the Marine Sponge Geodia cydonium: Implication for the Phylogenetic Relationshi…

1998

Sponges (Porifera) are the phylogenetically oldest metazoan organisms. From one member of the siliceous sponges, Geodia cydonium, the cDNA encoding a putative SOS protein, the AidB-like protein of the Ada system from bacteria, was isolated and characterized. The cDNA, GCaidB, comprises an open reading frame of 446 amino acid (aa) residues encoding a polypeptide with a calculated Mr of 49,335. This molecule shows high similarity to the bacterial AidB proteins from Mycobacterium tuberculosis and Escherichia coli and somewhat lower similarities to acyl-CoA dehydrogenases (ADHs) and acyl-CoA oxidases (AOXs). Northern blot analysis confirmed the presence of the complete transcript. The deduced s…

DNA ComplementarySequence analysisMolecular Sequence DataSequence alignmentBiologymedicine.disease_causeAcyl-CoA DehydrogenaseEvolution MolecularBacterial ProteinsPhylogeneticsComplementary DNAGeneticsmedicineAnimalsAmino Acid SequenceSOS Response GeneticsMolecular BiologyGeneEscherichia coliPeptide sequencePhylogenyEcology Evolution Behavior and SystematicsGeneticsBase SequenceEscherichia coli ProteinsAcyl-CoA Dehydrogenase Long-ChainSequence Analysis DNABlotting NorthernInvertebratesPoriferaOpen reading frameBiochemistryOxidoreductasesSequence AlignmentJournal of Molecular Evolution
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Plant progesterone 5β-reductase is not homologous to the animal enzyme. Molecular evolutionary characterization of P5βR from Digitalis purpurea

2007

Plants of the genus Digitalis produce cardiac glycosides, i.e. digoxin, which are widely used for congestive heart failure. Progesterone 5beta-reductase (P5betaR) is a key enzyme in the biosynthesis of these natural products. Here, we have carried out the purification and partial amino acid sequencing of the native P5betaR from foxglove (Digitalis purpurea), and isolated a cDNA encoding this enzyme. Similarly to other steroid 5beta-reductases, the recombinant P5betaR catalyzes the stereospecific reduction of the Delta(4)-double bond of several steroids with a 3-oxo,Delta(4,5) structure. The gene encoding P5betaR is expressed in all plant organs, and maximally transcribed in leaves and matur…

DNA ComplementarySubfamilyRecombinant Fusion ProteinsMolecular Sequence DataPlant ScienceHorticultureReductaseBiochemistryGas Chromatography-Mass SpectrometryEvolution Molecularchemistry.chemical_compoundPhylogeneticsComplementary DNACardenolideAnimalsAmino Acid SequenceMolecular BiologyGenePhylogenyProgesteronePlant Proteinschemistry.chemical_classificationGeneticsDigitalisBase SequenceMolecular StructureSequence Homology Amino AcidbiologyProgesterone ReductaseReverse Transcriptase Polymerase Chain ReactionGene Expression ProfilingDigitalis purpureaGeneral Medicinebiology.organism_classificationEnzymeModels ChemicalBiochemistrychemistryElectrophoresis Polyacrylamide GelPhytochemistry
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Isolation and characterization of five Fox (Forkhead) genes from the sponge Suberites domuncula.

2003

Fox or Forkhead genes constitute a subgroup of the helix-turn-helix class of transcription factors with a characteristic and highly conserved DNA binding domain. To date, around 100 different Fox genes have been reported ranging from yeast to humans; these have been classified into 18 subclasses (A to P). Fox proteins are responsible for a wide range of functions and key roles in early developmental processes, during organogenesis and also for the function of the major organs and tissues in the adult. Here, we report the isolation and phylogenetic characterization of five members of the Fox family from the sponge Suberites domuncula. Four of them (Sd-FoxL2, Sd-FoxP, Sd-FoxD and Sd-FoxF) fal…

DNA ComplementaryTime FactorsSequence analysisMolecular Sequence DataSequence alignmentBiologyFOX proteinsPhylogeneticsparasitic diseasesGeneticsAnimalsCloning MolecularGeneCells CulturedPhylogenyGeneticsSequence Homology Amino AcidGene Expression ProfilingGeneral MedicineDNA-binding domainAnatomySequence Analysis DNAbiology.organism_classificationPoriferaSuberites domunculaSpongeMultigene FamilySequence AlignmentTranscription FactorsGene
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Characterization and phylogenetic analysis of a cDNA encoding the Fes/FER related, non-receptor protein-tyrosine kinase in the marine sponge Sycon ra…

1998

Abstract In search of ancient versions of phylogenetically conserved genes/proteins, which are typical for multicellular animals, we have decided to analyse marine sponges (Porifera), the most ancient and most primitive metazoan organisms. We report here the complete nucleotide sequence of Sycon raphanus cDNA coding for a 879 aa long protein (100 kDa), which displays high overall similarity in primary structure and organization of domains with non-receptor tyrosine kinases (TKs) from the Fes/FER family. The encoded protein, which we named Fes/FER_SR, has a highly conserved, 260 aa long tyrosine kinase domain at the C-terminus. Amino-terminal to the catalytic domain is an 85 aa long SH2 doma…

DNA Complementaryanimal structuresMolecular Sequence DataBiologySH2 domainHomology (biology)PhylogeneticsProto-Oncogene ProteinsComplementary DNAGeneticsAnimalsAmino Acid SequenceSycon raphanusPhylogenyGeneticsSequence Homology Amino AcidProtein primary structureNucleic acid sequenceSequence Analysis DNAGeneral MedicineProtein-Tyrosine Kinasesbiology.organism_classificationPoriferaBiochemistryOncogenes; Signal transduction; SH2 domain; Metazoa; Porifera; PhylogenySequence AlignmentTyrosine kinaseGene
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Immunoglobulin-like domain is present in the extracellular part of the receptor tyrosine kinase from the marine sponge Geodia cydonium.

1994

We have isolated and characterized two cDNAs from the marine sponge Geodia cydonium coding for a new member of a receptor tyrosine kinase of class II. The deduced amino acid sequence shows two characteristic domains: (i) the tyrosine kinase domain; and (ii) and immunoglobulin-like domain. The latter part shows high homology to the vertebrate C2 type immunoglobulin domain. This result demonstrates that immunoglobulin domains are not recent achievements of higher animals but exist also in those animals which have diverged from other organisms about 800 million years ago.

DNA ComplementarybiologySequence Homology Amino AcidMolecular Sequence DatamyrImmunoglobulinsReceptor Protein-Tyrosine KinasesImmunoglobulin domainSH2 domainBiological EvolutionReceptor tyrosine kinasePoriferaProtein Structure TertiaryBiochemistryStructural BiologyPhylogeneticsMultigene FamilyROR1biology.proteinAnimalsAmino Acid SequenceMolecular BiologyPeptide sequenceTyrosine kinaseSequence AlignmentJournal of molecular recognition : JMR
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gcType : a high-quality type strain genome database for microbial phylogenetic and functional research

2020

Abstract Taxonomic and functional research of microorganisms has increasingly relied upon genome-based data and methods. As the depository of the Global Catalogue of Microorganisms (GCM) 10K prokaryotic type strain sequencing project, Global Catalogue of Type Strain (gcType) has published 1049 type strain genomes sequenced by the GCM 10K project which are preserved in global culture collections with a valid published status. Additionally, the information provided through gcType includes >12 000 publicly available type strain genome sequences from GenBank incorporated using quality control criteria and standard data annotation pipelines to form a high-quality reference database. This …

Data AnalysisBACTERIALAcademicSubjects/SCI000100206 medical engineering02 engineering and technologyComputational biologyBiologyGenome03 medical and health sciencesMULTIPLE SEQUENCE ALIGNMENTPhylogeneticsRNA Ribosomal 16SDatabases GeneticGeneticsPROGRAMDatabase IssueALGORITHMPhylogeny030304 developmental biology0303 health sciencesGenomeMultiple sequence alignmentBase SequencePhylogenetic treeResearchGenome databaseBiology and Life SciencesGCM transcription factorsProkaryotic CellsGenBankReference database020602 bioinformatics
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