| D008969 |
Molecular Sequence Data |
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. |
Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular |
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| D010447 |
Peptide Hydrolases |
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES. |
Peptidase,Peptidases,Peptide Hydrolase,Protease,Proteases,Proteinase,Proteinases,Proteolytic Enzyme,Proteolytic Enzymes,Esteroproteases,Enzyme, Proteolytic,Hydrolase, Peptide |
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| D010940 |
Plant Proteins |
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which PLANT PROTEINS, DIETARY is available. |
Plant Protein,Protein, Plant,Proteins, Plant |
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| D002734 |
Chlorophyll |
Porphyrin derivatives containing magnesium that act to convert light energy in photosynthetic organisms. |
Phyllobilins,Chlorophyll 740 |
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| D000458 |
Cyanobacteria |
A phylum of oxygenic photosynthetic bacteria comprised of unicellular to multicellular bacteria possessing CHLOROPHYLL a and carrying out oxygenic PHOTOSYNTHESIS. Cyanobacteria are the only known organisms capable of fixing both CARBON DIOXIDE (in the presence of light) and NITROGEN. Cell morphology can include nitrogen-fixing heterocysts and/or resting cells called akinetes. Formerly called blue-green algae, cyanobacteria were traditionally treated as ALGAE. |
Algae, Blue-Green,Blue-Green Bacteria,Cyanophyceae,Algae, Blue Green,Bacteria, Blue Green,Bacteria, Blue-Green,Blue Green Algae,Blue Green Bacteria,Blue-Green Algae |
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| D000595 |
Amino Acid Sequence |
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. |
Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein |
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| D012689 |
Sequence Homology, Nucleic Acid |
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function. |
Base Sequence Homology,Homologous Sequences, Nucleic Acid,Homologs, Nucleic Acid Sequence,Homology, Base Sequence,Homology, Nucleic Acid Sequence,Nucleic Acid Sequence Homologs,Nucleic Acid Sequence Homology,Sequence Homology, Base,Base Sequence Homologies,Homologies, Base Sequence,Sequence Homologies, Base |
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| D045322 |
Photosynthetic Reaction Center Complex Proteins |
Protein complexes that take part in the process of PHOTOSYNTHESIS. They are located within the THYLAKOID MEMBRANES of plant CHLOROPLASTS and a variety of structures in more primitive organisms. There are two major complexes involved in the photosynthetic process called PHOTOSYSTEM I and PHOTOSYSTEM II. |
Photosynthetic Complex,Photosynthetic Reaction Center,Photosynthetic Reaction Center Complex Protein,Photosynthetic Complexes,Photosynthetic Reaction Centers,Center, Photosynthetic Reaction,Complex, Photosynthetic,Complexes, Photosynthetic,Reaction Center, Photosynthetic,Reaction Centers, Photosynthetic |
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| D045331 |
Photosystem I Protein Complex |
A large multisubunit protein complex that is found in the THYLAKOID MEMBRANE. It uses light energy derived from LIGHT-HARVESTING PROTEIN COMPLEXES to drive electron transfer reactions that result in either the reduction of NADP to NADPH or the transport of PROTONS across the membrane. |
Photosystem I Reaction Center,Photosystem I |
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| D045342 |
Light-Harvesting Protein Complexes |
Complexes containing CHLOROPHYLL and other photosensitive molecules. They serve to capture energy in the form of PHOTONS and are generally found as components of the PHOTOSYSTEM I PROTEIN COMPLEX or the PHOTOSYSTEM II PROTEIN COMPLEX. |
Antenna Complexes, Light-Harvesting,Light-Harvesting Antenna Complexes,Light-Harvesting Chlorophyll Protein,Light-Harvesting Chlorophyll Protein Complexes,Antenna Complexes, Light Harvesting,Chlorophyll Protein, Light-Harvesting,Complexes, Light-Harvesting Antenna,Complexes, Light-Harvesting Protein,Light Harvesting Antenna Complexes,Light Harvesting Chlorophyll Protein,Light Harvesting Chlorophyll Protein Complexes,Light Harvesting Protein Complexes,Protein Complexes, Light-Harvesting |
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