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DisCons specifications

Information


Unique identifier OMICS_08564
Name DisCons
Alternative name Disorder Conservation
Software type Package/Module
Interface Command line interface
Restrictions to use None
Operating system Unix/Linux
Programming languages Python
License GNU General Public License version 2.0
Computer skills Advanced
Stability Stable
Maintained Yes

Versioning


No version available

Maintainer


  • person_outline Mihaly Varadi

Information


Unique identifier OMICS_08564
Name DisCons
Alternative name Disorder Conservation
Interface Web user interface
Restrictions to use None
Programming languages Python
Computer skills Basic
Stability Stable
Maintained Yes

Maintainer


  • person_outline Mihaly Varadi

Publication for Disorder Conservation

DisCons citations

 (6)
library_books

Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP

2017
Sci Rep
PMCID: 5498717
PMID: 28680062
DOI: 10.1038/s41598-017-04611-x

[…] tic features of the sequence (Supplementary Fig. ). In general, about half the residues of ID3 fall into potential binding sites predicted by ANCHOR and about half the sequence is highly conserved by DisCons, suggesting the presence of multiple interaction sites within this disordered region of CBP. Several moderately populated helical regions in the N-terminal half appear as potential preformed b […]

library_books

Affinity purification of human m calpain through an intrinsically disordered inhibitor, calpastatin

2017
PLoS One
PMCID: 5358782
PMID: 28319173
DOI: 10.1371/journal.pone.0174125

[…] trieved sequences covered the vertebrate taxonomic groups of mammals, birds and amphibians. We generated a multiple sequence alignment (MSA) with MAFFT and used the MSA as input for the sequence- and disorder conservation analysis carried out with the local version of the DisCons tool[,]. Briefly, DisCons calculates the position-specific sequence- and disorder conservation scores based on a multip […]

library_books

Evolution of the Twist Subfamily Vertebrate Proteins: Discovery of a Signature Motif and Origin of the Twist1 Glycine Rich Motifs in the Amino Terminus Disordered Domain

2016
PLoS One
PMCID: 4996418
PMID: 27556926
DOI: 10.1371/journal.pone.0161029

[…] e Phyre2 Structure Prediction server [] was used to construct a representation of the secondary structure of the Twist1 protein and Pymol [] was used for visualization of the predicted structure. The DisCons web server [] was used for Disorder Conservation analysis using default parameters and a BLOSUM80 similarity matrix. […]

call_split

Intrinsic protein disorder in histone lysine methylation

2016
Biol Direct
PMCID: 4928265
PMID: 27356874
DOI: 10.1186/s13062-016-0129-2
call_split See protocol

[…] extension 1 bit). Each vertebrata multiple alignment file of the proteins contained a broad range of species from primates to the earliest diverged fishes.The calculation of sequence conservation and disorder conservation was carried out by DisCons [], from alignments with default parameters (IUPred long, Jensen-Shannon divergence, window size of 3). As input alignment we used the same vertebrata […]

library_books

Functional Advantages of Conserved Intrinsic Disorder in RNA Binding Proteins

2015
PLoS One
PMCID: 4595337
PMID: 26439842
DOI: 10.1371/journal.pone.0139731

[…] bstitutions[]. Based on the distinct differences in the conservation profiles of de facto binding residues and those that mainly function as flexible linkers, it would seem likely that tools, such as DisCons[]that investigate and quantify the conservation of both the amino acid sequence and the disordered nature of a protein may offer an additional layer of information that can complement and enha […]

library_books

Computational approaches for inferring the functions of intrinsically disordered proteins

2015
Front Mol Biosci
PMCID: 4525029
PMID: 26301226
DOI: 10.3389/fmolb.2015.00045

[…] enhance the performance, for example MoRFpred, which uses order/disorder patterns (Cheng et al., ), ANCHOR, which estimates the interaction of a segment with a general partner (Meszaros et al., ) or DisCons, which takes into consideration the evolutionary conservation of both the amino acid sequence and of the disorder as a feature (Varadi et al., ). […]

Citations

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DisCons institution(s)
VIB Structural Biology Research Center (SBRC), Brussels, Belgium and Vrije Universiteit Brussel, Brussels, Belgium

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