| 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 |
|
| D011134 |
Polysaccharides |
Long chain polymeric CARBOHYDRATES composed of MONOSACCHARIDES linked by glycosidic bonds. |
Glycan,Glycans,Polysaccharide |
|
| D005656 |
Fungal Proteins |
Proteins found in any species of fungus. |
Fungal Gene Products,Fungal Gene Proteins,Fungal Peptides,Gene Products, Fungal,Yeast Proteins,Gene Proteins, Fungal,Peptides, Fungal,Proteins, Fungal |
|
| D006026 |
Glycoside Hydrolases |
Any member of the class of enzymes that catalyze the cleavage of the glycosidic linkage of glycosides and the addition of water to the resulting molecules. |
Endoglycosidase,Exoglycosidase,Glycohydrolase,Glycosidase,Glycosidases,Glycoside Hydrolase,Endoglycosidases,Exoglycosidases,Glycohydrolases,Hydrolase, Glycoside,Hydrolases, Glycoside |
|
| 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 |
|
| D001203 |
Ascomycota |
A phylum of fungi which have cross-walls or septa in the mycelium. The perfect state is characterized by the formation of a saclike cell (ascus) containing ascospores. Most pathogenic fungi with a known perfect state belong to this phylum. |
Ascomycetes,Cochliobolus,Sclerotinia,Ascomycete,Ascomycotas,Sclerotinias |
|
| D013696 |
Temperature |
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms. |
Temperatures |
|
| D014995 |
Xylosidases |
A group of enzymes that catalyze the hydrolysis of alpha- or beta-xylosidic linkages. EC 3.2.1.8 catalyzes the endo-hydrolysis of 1,4-beta-D-xylosidic linkages; EC 3.2.1.32 catalyzes the endo-hydrolysis of 1,3-beta-D-xylosidic linkages; EC 3.2.1.37 catalyzes the exo-hydrolysis of 1,4-beta-D-linkages from the non-reducing termini of xylans; and EC 3.2.1.72 catalyzes the exo-hydrolysis of 1,3-beta-D-linkages from the non-reducing termini of xylans. Other xylosidases have been identified that catalyze the hydrolysis of alpha-xylosidic bonds. |
Xylobiases,Xylan Hydrolases,Hydrolases, Xylan |
|
| D016415 |
Sequence Alignment |
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms. |
Sequence Homology Determination,Determination, Sequence Homology,Alignment, Sequence,Alignments, Sequence,Determinations, Sequence Homology,Sequence Alignments,Sequence Homology Determinations |
|
| D043325 |
Xylan Endo-1,3-beta-Xylosidase |
A xylosidase that catalyses the random hydrolysis of 1,3-beta-D-xylosidic linkages in 1,3-beta-D-xylans. |
Endo-1,3-beta-Xylanase,Endo 1,3 beta Xylanase,Endo-1,3-beta-Xylosidase, Xylan,Xylan Endo 1,3 beta Xylosidase |
|