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Search results 1001 to 1100 out of 2386 for *

Category restricted to SOTerm (x)

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Categories

Category: SOTerm
Type Details Score
SO Term
Description: An MNV is a multiple nucleotide variant (substitution) in which the inserted sequence is the same length as the replaced sequence.
SO Term
Description: A multiple nucleotide polymorphism with alleles of common length > 1, for example AAA/TTT.
SO Term
Description: An intronic region that has an attribute.
SO Term
Description: A type of non-canonical base pairing, most commonly between G and U, which is important for the secondary structure of RNAs. It has similar thermodynamic stability to the Watson-Crick pairing. Wobble base pairs only have two hydrogen bonds. Other wobble base pair possibilities are I-A, I-U and I-C.
SO Term
Description: A purine-rich sequence in the group I introns which determines the locations of the splice sites in group I intron splicing and has catalytic activity.
SO Term
Description: A sequence variant that falls entirely or partially within a genomic feature.
SO Term
Description: A sequence variant that does not affect protein function. Silent mutations may occur in genic ( CDS, UTR, intron etc) and intergenic regions. Silent mutations may have affects on processes such as splicing and regulation.
SO Term
Description: A sequence_variant is a non exact copy of a sequence_feature or genome exhibiting one or more sequence_alteration.
SO Term
Description: A sequence variant that changes one or more structural features.
SO Term
Description: A binding site that, in the molecule, interacts selectively and non-covalently with antibodies, B cells or T cells.
SO Term
Description: A variation that increases or decreases the copy number of a given region.
SO Term
Description: A chromosomal region that may sustain a double-strand break, resulting in a recombination event.
SO Term
Description: The point within a chromosome where an inversion begins or ends.
SO Term
Description: An allele is one of a set of coexisting sequence variants of a gene.
SO Term
Description: A haplotype is one of a set of coexisting sequence variants of a haplotype block.
SO Term
Description: A sequence variant that is segregating in one or more natural populations of a species.
SO Term
Description: A genotype is a variant genome, complete or incomplete.
SO Term
Description: A diplotype is a pair of haplotypes from a given individual. It is a genotype where the phase is known.
SO Term
Description: DNA belonging to the genome of a mitochondria.
SO Term
Description: DNA belonging to the genome of a chloroplast, a photosynthetic plastid.
SO Term
Description: A de-branched intron which mimics the structure of pre-miRNA and enters the miRNA processing pathway without Drosha mediated cleavage.
SO Term
Description: A small non coding RNA, part of a silencing system that prevents the spreading of selfish genetic elements.
SO Term
Description: A tRNA sequence that has an arginine anticodon, and a 3' arginine binding region.
SO Term
Description: A plasmid sequence that is integrated within the host chromosome.
SO Term
Description: An attachment site located on a conjugative transposon and used for site-specific integration of a conjugative transposon.
SO Term
Description: A nuclear pseudogene of either coding or non-coding mitochondria derived sequence.
SO Term
Description: A MGE region consisting of two fused plasmids resulting from a replicative transposition event.
SO Term
Description: A region located within an inversion site.
SO Term
Description: Component of the inversion site located at the left of a region susceptible to site-specific inversion.
SO Term
Description: Component of the inversion site located at the right of a region susceptible to site-specific inversion.
SO Term
Description: An island that contains genes for integration/excision and the gene and site for the initiation of intercellular transfer by conjugation. It can be complemented for transfer by a conjugative transposon.
SO Term
Description: A repeat that is disrupted by the insertion of another element.
SO Term
Description: A portion of a repeat, interrupted by the insertion of another element.
SO Term
Description: A transposon that is disrupted by the insertion of another element.
SO Term
Description: A portion of a transposon, interrupted by the insertion of another element.
SO Term
Description: The propeptide_cleavage_site is the arginine/lysine boundary on a propeptide where cleavage occurs.
SO Term
Description: A CDS region corresponding to a propeptide of a polypeptide.
SO Term
Description: Active peptides are proteins which are biologically active, released from a precursor molecule.
SO Term
Description: Polypeptide region that is rich in a particular amino acid or homopolymeric and greater than three residues in length.
SO Term
Description: A sequence motif is a short (up to 20 amino acids) region of biological interest. Such motifs, although they are too short to constitute functional domains, share sequence similarities and are conserved in different proteins. They display a common function (protein-binding, subcellular location etc.).
SO Term
Description: A polypeptide_repeat is a single copy of an internal sequence repetition.
SO Term
Description: Arrangement of the polypeptide with respect to the lipid bilayer.
SO Term
Description: Polypeptide region that is localized outside of a lipid bilayer.
SO Term
Description: Polypeptide region that is localized inside the cytoplasm.
SO Term
Description: Polypeptide region that is localized outside of a lipid bilayer and outside of the cytoplasm.
SO Term
Description: Polypeptide region present in the lipid bilayer.
SO Term
Description: Polypeptide region localized within the lipid bilayer where both ends traverse the same membrane.
SO Term
Description: Polypeptide region traversing the lipid bilayer.
SO Term
Description: Motif is a three-dimensional structural element within the chain, which appears also in a variety of other molecules. Unlike a domain, a motif does not need to form a stable globular unit.
SO Term
Description: A coiled coil is a structural motif in proteins, in which alpha-helices are coiled together like the strands of a rope.
SO Term
Description: A motif comprising two helices separated by a turn.
SO Term
Description: A helix is a secondary_structure conformation where the peptide backbone forms a coil.
SO Term
Description: Incompatibility in the sequence due to some experimental problem.
SO Term
Description: Indicates that two consecutive residues in a fragment sequence are not consecutive in the full-length protein and that there are a number of unsequenced residues between them.
SO Term
Description: The residue at an extremity of the sequence is not the terminal residue.
SO Term
Description: Different sources report differing sequences.
SO Term
Description: Describes the positions in a sequence where the authors are unsure about the sequence assignment.
SO Term
Description: A region of a peptide that is involved in a biochemical function.
SO Term
Description: A region where a transformation occurs in a protein after it has been synthesized. This which may regulate, stabilize, crosslink or introduce new chemical functionalities in the protein.
SO Term
Description: A region that is involved a contact with another molecule.
SO Term
Description: A binding site that, in the polypeptide molecule, interacts selectively and non-covalently with metal ions.
SO Term
Description: A binding site that, in the molecule, interacts selectively and non-covalently with metal ions.
SO Term
Description: A binding site that, in the protein molecule, interacts selectively and non-covalently with polypeptide residues.
SO Term
Description: A binding site that, in the polypeptide molecule, interacts selectively and non-covalently with calcium ions.
SO Term
Description: A binding site that, in the polypeptide molecule, interacts selectively and non-covalently with cobalt ions.
SO Term
Description: A binding site that, in the polypeptide molecule, interacts selectively and non-covalently with copper ions.
SO Term
Description: A binding site that, in the polypeptide molecule, interacts selectively and non-covalently with iron ions.
SO Term
Description: A binding site that, in the polypeptide molecule, interacts selectively and non-covalently with magnesium ions.
SO Term
Description: A binding site that, in the polypeptide molecule, interacts selectively and non-covalently with manganese ions.
SO Term
Description: A binding site that, in the polypeptide molecule, interacts selectively and non-covalently with molybdenum ions.
SO Term
Description: A binding site that, in the polypeptide molecule, interacts selectively and non-covalently with nickel ions.
SO Term
Description: A binding site that, in the polypeptide molecule, interacts selectively and non-covalently with tungsten ions.
SO Term
Description: A binding site that, in the polypeptide molecule, interacts selectively and non-covalently with zinc ions.
SO Term
Description: A sequence feature that corresponds to a single amino acid residue in a polypeptide.
SO Term
Description: Amino acid involved in the activity of an enzyme.
SO Term
Description: A polypeptide catalytic motif is a short (up to 20 amino acids) polypeptide region that contains one or more active site residues.
SO Term
Description: A binding site that, in the molecule, interacts selectively and non-covalently with a small molecule such as a drug, or hormone.
SO Term
Description: Residues which interact with a ligand.
SO Term
Description: A motif of five consecutive residues and two H-bonds in which: Residue(i) is Aspartate or Asparagine (Asx), side-chain O of residue(i) is H-bonded to the main-chain NH of residue(i+2) or (i+3), main-chain CO of residue(i) is H-bonded to the main-chain NH of residue(i+3) or (i+4).
SO Term
Description: A motif of three residues within a beta-sheet in which the main chains of two consecutive residues are H-bonded to that of the third, and in which the dihedral angles are as follows: Residue(i): -140 degrees < phi(l) -20 degrees , -90 degrees < psi(l) < 40 degrees. Residue (i+1): -180 degrees < phi < -25 degrees or +120 degrees < phi < +180 degrees, +40 degrees < psi < +180 degrees or -180 degrees < psi < -120 degrees.
SO Term
Description: A motif of three residues within a beta-sheet consisting of two H-bonds. Beta bulge loops often occur at the loop ends of beta-hairpins.
SO Term
Description: A motif of three residues within a beta-sheet consisting of two H-bonds in which: the main-chain NH of residue(i) is H-bonded to the main-chain CO of residue(i+4), the main-chain CO of residue i is H-bonded to the main-chain NH of residue(i+3), these loops have an RL nest at residues i+2 and i+3.
SO Term
Description: A motif of three residues within a beta-sheet consisting of two H-bonds in which: the main-chain NH of residue(i) is H-bonded to the main-chain CO of residue(i+5), the main-chain CO of residue i is H-bonded to the main-chain NH of residue(i+4), these loops have an RL nest at residues i+3 and i+4.
SO Term
Description: A beta strand describes a single length of polypeptide chain that forms part of a beta sheet. A single continuous stretch of amino acids adopting an extended conformation of hydrogen bonds between the N-O and the C=O of another part of the peptide. This forms a secondary protein structure in which two or more extended polypeptide regions are hydrogen-bonded to one another in a planar array.
SO Term
Description: A peptide region which hydrogen bonded to another region of peptide running in the oposite direction (one running N-terminal to C-terminal and one running C-terminal to N-terminal). Hydrogen bonding occurs between every other C=O from one strand to every other N-H on the adjacent strand. In this case, if two atoms C-alpha (i) and C-alpha (j) are adjacent in two hydrogen-bonded beta strands, then they form two mutual backbone hydrogen bonds to each other's flanking peptide groups; this is known as a close pair of hydrogen bonds. The peptide backbone dihedral angles (phi, psi) are about (-140 degrees, 135 degrees) in antiparallel sheets.
SO Term
Description: A peptide region which hydrogen bonded to another region of peptide running in the oposite direction (both running N-terminal to C-terminal). This orientation is slightly less stable because it introduces nonplanarity in the inter-strand hydrogen bonding pattern. Hydrogen bonding occurs between every other C=O from one strand to every other N-H on the adjacent strand. In this case, if two atoms C-alpha (i)and C-alpha (j) are adjacent in two hydrogen-bonded beta strands, then they do not hydrogen bond to each other; rather, one residue forms hydrogen bonds to the residues that flank the other (but not vice versa). For example, residue i may form hydrogen bonds to residues j - 1 and j + 1; this is known as a wide pair of hydrogen bonds. By contrast, residue j may hydrogen-bond to different residues altogether, or to none at all. The dihedral angles (phi, psi) are about (-120 degrees, 115 degrees) in parallel sheets.
SO Term
Description: A left handed helix is a region of peptide where the coiled conformation turns in an anticlockwise, left handed screw.
SO Term
Description: A right handed helix is a region of peptide where the coiled conformation turns in a clockwise, right handed screw.
SO Term
Description: The helix has 3.6 residues per turn which corresponds to a translation of 1.5 angstroms (= 0.15 nm) along the helical axis. Every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid four residues earlier.
SO Term
Description: The pi helix has 4.1 residues per turn and a translation of 1.15 (=0.115 nm) along the helical axis. The N-H group of an amino acid forms a hydrogen bond with the C=O group of the amino acid five residues earlier.
SO Term
Description: The 3-10 helix has 3 residues per turn with a translation of 2.0 angstroms (=0.2 nm) along the helical axis. The N-H group of an amino acid forms a hydrogen bond with the C=O group of the amino acid three residues earlier.
SO Term
Description: A motif of two consecutive residues with dihedral angles. Nest should not have Proline as any residue. Nests frequently occur as parts of other motifs such as Schellman loops.
SO Term
Description: A motif of two consecutive residues with dihedral angles: Residue(i): +20 degrees < phi < +140 degrees, -40 degrees < psi < +90 degrees. Residue(i+1): -140 degrees < phi < -20 degrees, -90 degrees < psi < +40 degrees.
SO Term
Description: A motif of two consecutive residues with dihedral angles: Residue(i): -140 degrees < phi < -20 degrees, -90 degrees < psi < +40 degrees. Residue(i+1): +20 degrees < phi < +140 degrees, -40 degrees < psi < +90 degrees.
SO Term
Description: A motif of six or seven consecutive residues that contains two H-bonds.
SO Term
Description: Wild type: A motif of seven consecutive residues that contains two H-bonds in which: the main-chain CO of residue(i) is H-bonded to the main-chain NH of residue(i+6), the main-chain CO of residue(i+1) is H-bonded to the main-chain NH of residue(i+5).
SO Term
Description: Common Type: A motif of six consecutive residues that contains two H-bonds in which: the main-chain CO of residue(i) is H-bonded to the main-chain NH of residue(i+5) the main-chain CO of residue(i+1) is H-bonded to the main-chain NH of residue(i+4).
SO Term
Description: A motif of five consecutive residues and two hydrogen bonds in which: residue(i) is Serine (S) or Threonine (T), the side-chain O of residue(i) is H-bonded to the main-chain NH of residue(i+2) or (i+3) , the main-chain CO group of residue(i) is H-bonded to the main-chain NH of residue(i+3) or (i+4).
SO Term
Description: A motif of four or five consecutive residues and one H-bond in which: residue(i) is Serine (S) or Threonine (T), the side-chain OH of residue(i) is H-bonded to the main-chain CO of residue(i3) or (i4), Phi angles of residues(i1), (i2) and (i3) are negative.
SO Term
Description: Left handed type I (dihedral angles):- Residue(i): -140 degrees < chi (1) -120 degrees < -20 degrees, -90 degrees < psi +120 degrees < +40 degrees. Residue(i+1): -140 degrees < phi < -20 degrees, -90 degrees < psi < +40 degrees.
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